ID 104K_THEAN Reviewed; 893 AA. AC Q4U9M9; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 20-FEB-2007, entry version 10. DE 104 kDa microneme-rhoptry antigen precursor (p104). GN ORFNames=TA08425; OS Theileria annulata. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida; OC Theileriidae; Theileria. OX NCBI_TaxID=5874; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ankara; RX PubMed=15994557; DOI=10.1126/science.1110418; RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W., RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., RA Coulson R.M.R., Cronin A., de Villiers E.P., Fraser A., Fosker N., RA Gardner M., Goble A., Griffiths-Jones S., Harris D.E., Katzer F., RA Larke N., Lord A., Maser P., McKellar S., Mooney P., Morton F., RA Nene V., O'Neil S., Price C., Quail M.A., Rabbinowitsch E., RA Rawlings N.D., Rutter S., Saunders D., Seeger K., Shah T., Squares R., RA Squares S., Tivey A., Walker A.R., Woodward J., Dobbelaere D.A.E., RA Langsley G., Rajandream M.A., McKeever D., Shiels B., Tait A., RA Barrell B.G., Hall N.; RT "Genome of the host-cell transforming parasite Theileria annulata RT compared with T. parva."; RL Science 309:131-133(2005). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor CC (Potential). Note=In microneme/rhoptry complexes (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; CR940353; CAI76474.1; -; Genomic_DNA. DR InterPro; IPR007480; DUF529. DR Pfam; PF04385; FAINT; 4. KW Complete proteome; GPI-anchor; Lipoprotein; Membrane; Repeat; Signal; KW Sporozoite. FT SIGNAL 1 19 Potential. FT CHAIN 20 873 104 kDa microneme-rhoptry antigen. FT /FTId=PRO_0000232680. FT PROPEP 874 893 Removed in mature form (Potential). FT /FTId=PRO_0000232681. FT COMPBIAS 215 220 Poly-Leu. FT COMPBIAS 486 683 Lys-rich. FT COMPBIAS 854 859 Poly-Arg. FT LIPID 873 873 GPI-anchor amidated aspartate FT (Potential). SQ SEQUENCE 893 AA; 101921 MW; 2F67CEB3B02E7AC1 CRC64; MKFLVLLFNI LCLFPILGAD ELVMSPIPTT DVQPKVTFDI NSEVSSGPLY LNPVEMAGVK YLQLQRQPGV QVHKVVEGDI VIWENEEMPL YTCAIVTQNE VPYMAYVELL EDPDLIFFLK EGDQWAPIPE DQYLARLQQL RQQIHTESFF SLNLSFQHEN YKYEMVSSFQ HSIKMVVFTP KNGHICKMVY DKNIRIFKAL YNEYVTSVIG FFRGLKLLLL NIFVIDDRGM IGNKYFQLLD DKYAPISVQG YVATIPKLKD FAEPYHPIIL DISDIDYVNF YLGDATYHDP GFKIVPKTPQ CITKVVDGNE VIYESSNPSV ECVYKVTYYD KKNESMLRLD LNHSPPSYTS YYAKREGVWV TSTYIDLEEK IEELQDHRST ELDVMFMSDK DLNVVPLTNG NLEYFMVTPK PHRDIIIVFD GSEVLWYYEG LENHLVCTWI YVTEGAPRLV HLRVKDRIPQ NTDIYMVKFG EYWVRISKTQ YTQEIKKLIK KSKKKLPSIE EEDSDKHGGP PKGPEPPTGP GHSSSESKEH EDSKESKEPK EHGSPKETKE GEVTKKPGPA KEHKPSKIPV YTKRPEFPKK SKSPKRPESP KSPKRPVSPQ RPVSPKSPKR PESLDIPKSP KRPESPKSPK RPVSPQRPVS PRRPESPKSP KSPKSPKSPK VPFDPKFKEK LYDSYLDKAA KTKETVTLPP VLPTDESFTH TPIGEPTAEQ PDDIEPIEES VFIKETGILT EEVKTEDIHS ETGEPEEPKR PDSPTKHSPK PTGTHPSMPK KRRRSDGLAL STTDLESEAG RILRDPTGKI VTMKRSKSFD DLTTVREKEH MGAEIRKIVV DDDGTEADDE DTHPSKEKHL STVRRRRPRP KKSSKSSKPR KPDSAFVPSI IFIFLVSLIV GIL // ID 104K_THEPA Reviewed; 924 AA. AC P15711; Q4N2B5; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 20-FEB-2007, entry version 33. DE 104 kDa microneme-rhoptry antigen precursor (p104). GN OrderedLocusNames=TP04_0437; OS Theileria parva. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida; OC Theileriidae; Theileria. OX NCBI_TaxID=5875; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Muguga; RX MEDLINE=90158697; PubMed=1689460; DOI=10.1016/0166-6851(90)90007-9; RA Iams K.P., Young J.R., Nene V., Desai J., Webster P., Ole-Moiyoi O.K., RA Musoke A.J.; RT "Characterisation of the gene encoding a 104-kilodalton microneme- RT rhoptry protein of Theileria parva."; RL Mol. Biochem. Parasitol. 39:47-60(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Muguga; RX PubMed=15994558; DOI=10.1126/science.1110439; RA Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., RA Hall N., Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., RA Sato S., Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., RA Jiang L., Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., RA Crabtree J., Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., RA Suh B., Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., RA Allen J., Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., RA Fitzhugh H.A., Morzaria S., Venter J.C., Fraser C.M., Nene V.; RT "Genome sequence of Theileria parva, a bovine pathogen that transforms RT lymphocytes."; RL Science 309:134-137(2005). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor CC (Potential). Note=In microneme/rhoptry complexes. CC -!- DEVELOPMENTAL STAGE: Sporozoite antigen. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M29954; AAA18217.1; -; Unassigned_DNA. DR EMBL; AAGK01000004; EAN31789.1; -; Genomic_DNA. DR PIR; A44945; A44945. DR InterPro; IPR007480; DUF529. DR Pfam; PF04385; FAINT; 4. KW Complete proteome; GPI-anchor; Lipoprotein; Membrane; Repeat; Signal; KW Sporozoite. FT SIGNAL 1 19 Potential. FT CHAIN 20 904 104 kDa microneme-rhoptry antigen. FT /FTId=PRO_0000046081. FT PROPEP 905 924 Removed in mature form (Potential). FT /FTId=PRO_0000232679. FT COMPBIAS 508 753 Pro-rich. FT COMPBIAS 880 883 Poly-Arg. FT LIPID 904 904 GPI-anchor amidated aspartate FT (Potential). SQ SEQUENCE 924 AA; 103626 MW; 289B4B554A61870E CRC64; MKFLILLFNI LCLFPVLAAD NHGVGPQGAS GVDPITFDIN SNQTGPAFLT AVEMAGVKYL QVQHGSNVNI HRLVEGNVVI WENASTPLYT GAIVTNNDGP YMAYVEVLGD PNLQFFIKSG DAWVTLSEHE YLAKLQEIRQ AVHIESVFSL NMAFQLENNK YEVETHAKNG ANMVTFIPRN GHICKMVYHK NVRIYKATGN DTVTSVVGFF RGLRLLLINV FSIDDNGMMS NRYFQHVDDK YVPISQKNYE TGIVKLKDYK HAYHPVDLDI KDIDYTMFHL ADATYHEPCF KIIPNTGFCI TKLFDGDQVL YESFNPLIHC INEVHIYDRN NGSIICLHLN YSPPSYKAYL VLKDTGWEAT THPLLEEKIE ELQDQRACEL DVNFISDKDL YVAALTNADL NYTMVTPRPH RDVIRVSDGS EVLWYYEGLD NFLVCAWIYV SDGVASLVHL RIKDRIPANN DIYVLKGDLY WTRITKIQFT QEIKRLVKKS KKKLAPITEE DSDKHDEPPE GPGASGLPPK APGDKEGSEG HKGPSKGSDS SKEGKKPGSG KKPGPAREHK PSKIPTLSKK PSGPKDPKHP RDPKEPRKSK SPRTASPTRR PSPKLPQLSK LPKSTSPRSP PPPTRPSSPE RPEGTKIIKT SKPPSPKPPF DPSFKEKFYD DYSKAASRSK ETKTTVVLDE SFESILKETL PETPGTPFTT PRPVPPKRPR TPESPFEPPK DPDSPSTSPS EFFTPPESKR TRFHETPADT PLPDVTAELF KEPDVTAETK SPDEAMKRPR SPSEYEDTSP GDYPSLPMKR HRLERLRLTT TEMETDPGRM AKDASGKPVK LKRSKSFDDL TTVELAPEPK ASRIVVDDEG TEADDEETHP PEERQKTEVR RRRPPKKPSK SPRPSKPKKP KKPDSAYIPS ILAILVVSLI VGIL // ID 108_SOLLC Reviewed; 102 AA. AC Q43495; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 38. DE Protein 108 precursor. OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. VF36; TISSUE=Anther; RX MEDLINE=94143497; PubMed=8310077; DOI=10.1104/pp.101.4.1413; RA Chen R., Smith A.G.; RT "Nucleotide sequence of a stamen- and tapetum-specific gene from RT Lycopersicon esculentum."; RL Plant Physiol. 101:1413-1413(1993). CC -!- TISSUE SPECIFICITY: Stamen- and tapetum-specific. CC -!- SIMILARITY: Belongs to the A9/FIL1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z14088; CAA78466.1; -; mRNA. DR PIR; S26409; S26409. DR UniGene; Les.3896; -. DR InterPro; IPR013770; LPT_helical. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR SMART; SM00499; AAI; 1. KW Signal. FT SIGNAL 1 30 Potential. FT CHAIN 31 102 Protein 108. FT /FTId=PRO_0000000238. FT DISULFID 41 77 By similarity. FT DISULFID 51 66 By similarity. FT DISULFID 67 92 By similarity. FT DISULFID 79 99 By similarity. SQ SEQUENCE 102 AA; 10576 MW; CFBAA1231C3A5E92 CRC64; MASVKSSSSS SSSSFISLLL LILLVIVLQS QVIECQPQQS CTASLTGLNV CAPFLVPGSP TASTECCNAV QSINHDCMCN TMRIAAQIPA QCNLPPLSCS AN // ID 10KD_VIGUN Reviewed; 75 AA. AC P18646; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 31-OCT-2006, entry version 42. DE 10 kDa protein precursor (Clone PSAS10). OS Vigna unguiculata (Cowpea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Vigna. OX NCBI_TaxID=3917; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cotyledon; RX MEDLINE=91355865; PubMed=2103443; RA Ishibashi N., Yamauchi D., Minamikawa T.; RT "Stored mRNA in cotyledons of Vigna unguiculata seeds: nucleotide RT sequence of cloned cDNA for a stored mRNA and induction of its RT synthesis by precocious germination."; RL Plant Mol. Biol. 15:59-64(1990). CC -!- FUNCTION: This protein is required for germination. CC -!- SIMILARITY: Belongs to the plant defensin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X16877; CAA34760.1; -; mRNA. DR PIR; S11156; S11156. DR HSSP; P81929; 1JKZ. DR InterPro; IPR008176; Gamma-thionin. DR InterPro; IPR003614; Knot1. DR Pfam; PF00304; Gamma-thionin; 1. DR SMART; SM00505; Knot1; 1. DR PROSITE; PS00940; GAMMA_THIONIN; 1. KW Germination; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 75 10 kDa protein. FT /FTId=PRO_0000007058. FT DISULFID 31 75 By similarity. FT DISULFID 42 63 By similarity. FT DISULFID 48 69 By similarity. FT DISULFID 52 71 By similarity. SQ SEQUENCE 75 AA; 8523 MW; 6D72D9D238CF7650 CRC64; MEKKSIAGLC FLFLVLFVAQ EVVVQSEAKT CENLVDTYRG PCFTTGSCDD HCKNKEHLLS GRCRDDVRCW CTRNC // ID 110KD_PLAKN Reviewed; 296 AA. AC P13813; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 20-FEB-2007, entry version 33. DE 110 kDa antigen (PK110) (Fragment). OS Plasmodium knowlesi. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=5850; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88039002; PubMed=2444886; DOI=10.1016/0166-6851(87)90007-7; RA Perler F.B., Moon A.M., Qiang B.Q., Meda M., Dalton M., Card C., RA Schmidt-Ullrich R., Wallach D., Lynch J., Donelson J.E.; RT "Cloning and characterization of an abundant Plasmodium knowlesi RT antigen which cross reacts with Gambian sera."; RL Mol. Biochem. Parasitol. 25:185-193(1987). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M19152; AAA29471.1; -; mRNA. DR PIR; A54527; A54527. DR InterPro; IPR004829; Csurface_antigen. DR ProDom; PD153432; Csurface_antigen; 2. KW Malaria; Repeat. FT CHAIN <1 296 110 kDa antigen. FT /FTId=PRO_0000217176. FT REPEAT 132 143 1; approximate. FT REPEAT 144 155 2; approximate. FT REPEAT 156 167 3. FT REPEAT 168 179 4; approximate. FT REPEAT 180 191 5. FT REPEAT 192 203 6; approximate. FT REPEAT 204 215 7. FT REPEAT 216 227 8. FT REPEAT 228 239 9. FT REPEAT 240 251 10. FT REPEAT 252 263 11. FT REPEAT 264 275 12. FT REPEAT 276 287 13; approximate. FT REPEAT 288 293 14; truncated. FT REGION 132 296 13.5 X 12 AA approximate tandem repeats FT of E-E-T-Q-K-T-V-E-P-E-Q-T. FT NON_TER 1 1 SQ SEQUENCE 296 AA; 34077 MW; B0D7CD175C7A3625 CRC64; FNSNMLRGSV CEEDVSLMTS IDNMIEEIDF YEKEIYKGSH SGGVIKGMDY DLEDDENDED EMTEQMVEEV ADHITQDMID EVAHHVLDNI THDMAHMEEI VHGLSGDVTQ IKEIVQKVNV AVEKVKHIVE TEETQKTVEP EQIEETQNTV EPEQTEETQK TVEPEQTEET QNTVEPEQIE ETQKTVEPEQ TEEAQKTVEP EQTEETQKTV EPEQTEETQK TVEPEQTEET QKTVEPEQTE ETQKTVEPEQ TEETQKTVEP EQTEETQKTV EPEQTEETQN TVEPEPTQET QNTVEP // ID 11S2_SESIN Reviewed; 459 AA. AC Q9XHP0; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 31-OCT-2006, entry version 30. DE 11S globulin seed storage protein 2 precursor (11S globulin seed DE storage protein II) (alpha-globulin) [Contains: 11S globulin seed DE storage protein 2 acidic chain (11S globulin seed storage protein II DE acidic chain); 11S globulin seed storage protein 2 basic chain (11S DE globulin seed storage protein II basic chain)]. OS Sesamum indicum (Oriental sesame) (Gingelly). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Lamiales; Pedaliaceae; Sesamum. OX NCBI_TaxID=4182; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Tainan 1; TISSUE=Seed; RX MEDLINE=20074970; PubMed=10606554; DOI=10.1021/jf990366z; RA Tai S.S.K., Wu L.S.H., Chen E.C.F., Tzen J.T.C.; RT "Molecular cloning of 11S globulin and 2S albumin, the two major seed RT storage proteins in sesame."; RL J. Agric. Food Chem. 47:4932-4938(1999). CC -!- FUNCTION: Seed storage protein. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond (By similarity). CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; AF091842; AAD42944.1; -; mRNA. DR HSSP; P04776; 1FXZ. DR GO; GO:0042735; C:protein body; NAS:UniProtKB. DR GO; GO:0045735; F:nutrient reservoir activity; NAS:UniProtKB. DR GO; GO:0051259; P:protein oligomerization; NAS:UniProtKB. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR006044; Seedstore11s_pln. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 21 Potential. FT CHAIN 22 277 11S globulin seed storage protein 2 FT acidic chain (By similarity). FT /FTId=PRO_0000043209. FT CHAIN 278 459 11S globulin seed storage protein 2 basic FT chain (By similarity). FT /FTId=PRO_0000043210. FT DISULFID 34 67 Potential. FT DISULFID 110 284 Interchain (between acidic and basic FT chains) (By similarity). SQ SEQUENCE 459 AA; 51830 MW; E852F6C47B319200 CRC64; MVAFKFLLAL SLSLLVSAAI AQTREPRLTQ GQQCRFQRIS GAQPSLRIQS EGGTTELWDE RQEQFQCAGI VAMRSTIRPN GLSLPNYHPS PRLVYIERGQ GLISIMVPGC AETYQVHRSQ RTMERTEASE QQDRGSVRDL HQKVHRLRQG DIVAIPSGAA HWCYNDGSED LVAVSINDVN HLSNQLDQKF RAFYLAGGVP RSGEQEQQAR QTFHNIFRAF DAELLSEAFN VPQETIRRMQ SEEEERGLIV MARERMTFVR PDEEEGEQEH RGRQLDNGLE ETFCTMKFRT NVESRREADI FSRQAGRVHV VDRNKLPILK YMDLSAEKGN LYSNALVSPD WSMTGHTIVY VTRGDAQVQV VDHNGQALMN DRVNQGEMFV VPQYYTSTAR AGNNGFEWVA FKTTGSPMRS PLAGYTSVIR AMPLQVITNS YQISPNQAQA LKMNRGSQSF LLSPGGRRS // ID 11S3_HELAN Reviewed; 493 AA. AC P19084; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 31-OCT-2006, entry version 49. DE 11S globulin seed storage protein G3 precursor (Helianthinin G3) DE [Contains: 11S globulin seed storage protein G3 acidic chain; 11S DE globulin seed storage protein G3 basic chain]. GN Name=HAG3; OS Helianthus annuus (Common sunflower). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; OC Heliantheae; Helianthus. OX NCBI_TaxID=4232; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89232734; PubMed=2469623; DOI=10.1016/0378-1119(88)90176-X; RA Vonder Haar R.A., Allen R.D., Cohen E.A., Nessler C.L., Thomas T.L.; RT "Organization of the sunflower 11S storage protein gene family."; RL Gene 74:433-443(1988). CC -!- FUNCTION: This is a seed storage protein. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond. CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; M28832; AAA33374.1; -; Genomic_DNA. DR PIR; JA0089; JA0089. DR HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR006044; Seedstore11s_pln. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 20 FT CHAIN 21 305 11S globulin seed storage protein G3 FT acidic chain. FT /FTId=PRO_0000032025. FT CHAIN 306 493 11S globulin seed storage protein G3 FT basic chain. FT /FTId=PRO_0000032026. FT COMPBIAS 23 35 Gln-rich. FT COMPBIAS 111 127 Gln/Gly-rich. FT COMPBIAS 191 297 Gln-rich. FT DISULFID 103 312 Interchain (between acidic and basic FT chains) (Potential). SQ SEQUENCE 493 AA; 55687 MW; A007B6F99D189AB5 CRC64; MASKATLLLA FTLLFATCIA RHQQRQQQQN QCQLQNIEAL EPIEVIQAEA GVTEIWDAYD QQFQCAWSIL FDTGFNLVAF SCLPTSTPLF WPSSREGVIL PGCRRTYEYS QEQQFSGEGG RRGGGEGTFR TVIRKLENLK EGDVVAIPTG TAHWLHNDGN TELVVVFLDT QNHENQLDEN QRRFFLAGNP QAQAQSQQQQ QRQPRQQSPQ RQRQRQRQGQ GQNAGNIFNG FTPELIAQSF NVDQETAQKL QGQNDQRGHI VNVGQDLQIV RPPQDRRSPR QQQEQATSPR QQQEQQQGRR GGWSNGVEET ICSMKFKVNI DNPSQADFVN PQAGSIANLN SFKFPILEHL RLSVERGELR PNAIQSPHWT INAHNLLYVT EGALRVQIVD NQGNSVFDNE LREGQVVVIP QNFAVIKRAN EQGSRWVSFK TNDNAMIANL AGRVSASAAS PLTLWANRYQ LSREEAQQLK FSQRETVLFA PSFSRGQGIR ASR // ID 11SB_CUCMA Reviewed; 480 AA. AC P13744; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 09-JAN-2007, entry version 55. DE 11S globulin subunit beta precursor [Contains: 11S globulin gamma DE chain (11S globulin acidic chain); 11S globulin delta chain (11S DE globulin basic chain)]. OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3661; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Kurokawa Amakuri Nankin; RX MEDLINE=88166744; PubMed=2450746; RA Hayashi M., Mori H., Nishimura M., Akazawa T., Hara-Nishimura I.; RT "Nucleotide sequence of cloned cDNA coding for pumpkin 11-S globulin RT beta subunit."; RL Eur. J. Biochem. 172:627-632(1988). RN [2] RP PROTEIN SEQUENCE OF 22-30 AND 297-302. RA Ohmiya M., Hara I., Mastubara H.; RT "Pumpkin (Cucurbita sp.) seed globulin IV. Terminal sequences of the RT acidic and basic peptide chains and identification of a pyroglutamyl RT peptide chain."; RL Plant Cell Physiol. 21:157-167(1980). CC -!- FUNCTION: This is a seed storage protein. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond. CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; M36407; AAA33110.1; -; mRNA. DR PDB; 2EVX; X-ray; A=22-480. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR006044; Seedstore11s_pln. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. KW 3D-structure; Direct protein sequencing; Pyrrolidone carboxylic acid; KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 21 FT CHAIN 22 480 11S globulin subunit beta. FT /FTId=PRO_0000032027. FT CHAIN 22 296 11S globulin gamma chain. FT /FTId=PRO_0000032028. FT CHAIN 297 480 11S globulin delta chain. FT /FTId=PRO_0000032029. FT MOD_RES 22 22 Pyrrolidone carboxylic acid. FT DISULFID 124 303 Interchain (between gamma and delta FT chains) (Potential). FT CONFLICT 27 27 S -> E (in Ref. 2). FT CONFLICT 30 30 E -> S (in Ref. 2). SQ SEQUENCE 480 AA; 54626 MW; BCD8A83DD1AED93C CRC64; MARSSLFTFL CLAVFINGCL SQIEQQSPWE FQGSEVWQQH RYQSPRACRL ENLRAQDPVR RAEAEAIFTE VWDQDNDEFQ CAGVNMIRHT IRPKGLLLPG FSNAPKLIFV AQGFGIRGIA IPGCAETYQT DLRRSQSAGS AFKDQHQKIR PFREGDLLVV PAGVSHWMYN RGQSDLVLIV FADTRNVANQ IDPYLRKFYL AGRPEQVERG VEEWERSSRK GSSGEKSGNI FSGFADEFLE EAFQIDGGLV RKLKGEDDER DRIVQVDEDF EVLLPEKDEE ERSRGRYIES ESESENGLEE TICTLRLKQN IGRSVRADVF NPRGGRISTA NYHTLPILRQ VRLSAERGVL YSNAMVAPHY TVNSHSVMYA TRGNARVQVV DNFGQSVFDG EVREGQVLMI PQNFVVIKRA SDRGFEWIAF KTNDNAITNL LAGRVSQMRM LPLGVLSNMY RISREEAQRL KYGQQEMRVL SPGRSQGRRE // ID 128UP_DROME Reviewed; 368 AA. AC P32234; Q9V648; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 23-JAN-2007, entry version 47. DE GTP-binding protein 128up. GN Name=128up; Synonyms=GTP-bp; ORFNames=CG8340; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Oregon-R; RX MEDLINE=94166747; PubMed=8121394; DOI=10.1007/BF00281788; RA Sommer K.A., Petersen G., Bautz E.K.F.; RT "The gene upstream of DmRP128 codes for a novel GTP-binding protein of RT Drosophila melanogaster."; RL Mol. Gen. Genet. 242:391-398(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=8104141; RA Mahaffey J.W., Jones D.F., Hickel J.A., Griswold C.M.; RT "Identification and characterization of a gene activated by the RT deformed homeoprotein."; RL Development 118:203-214(1993). CC -!- FUNCTION: Deformed (Dfd) is required to activate 1.28up in CC maxillary segment cells. CC -!- INTERACTION: CC Q9VGZ4:CG6325; NbExp=1; IntAct=EBI-163407, EBI-111903; CC P25724:nos; NbExp=1; IntAct=EBI-163407, EBI-106556; CC Q9V3H7:Sr-CI; NbExp=1; IntAct=EBI-163407, EBI-125222; CC -!- TISSUE SPECIFICITY: Expressed in posterior-lateral epidermis of CC the maxillary lobe. CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and adults. CC -!- SIMILARITY: Belongs to the GTP1/OBG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X71866; CAA50701.1; -; Genomic_DNA. DR EMBL; AE003823; AAF58591.1; -; Genomic_DNA. DR EMBL; AY069810; AAL39955.1; -; mRNA. DR PIR; S42582; S42582. DR UniGene; Dm.7739; -. DR HSSP; P20964; 1LNZ. DR IntAct; P32234; -. DR Ensembl; CG8340; Drosophila melanogaster. DR KEGG; dme:Dmel_CG8340; -. DR FlyBase; FBgn0010339; 128up. DR GermOnline; CG8340; Drosophila melanogaster. DR GO; GO:0005525; F:GTP binding; IDA:FlyBase. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR006074; GTP1-OBG_dom. DR InterPro; IPR006073; GTP1_OBG. DR InterPro; IPR002917; MMR_HSR1_GTP_bd. DR InterPro; IPR005225; Small_GTP_bd. DR InterPro; IPR004095; TGS. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF02824; TGS; 1. DR PRINTS; PR00326; GTP1OBG. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00905; GTP1_OBG; 1. KW Complete proteome; GTP-binding; Nucleotide-binding. FT CHAIN 1 368 GTP-binding protein 128up. FT /FTId=PRO_0000205430. FT NP_BIND 71 78 GTP (By similarity). FT NP_BIND 117 121 GTP (By similarity). FT NP_BIND 248 251 GTP (By similarity). FT CONFLICT 2 2 S -> I (in Ref. 1). FT CONFLICT 34 35 KL -> NV (in Ref. 1). SQ SEQUENCE 368 AA; 41132 MW; 5B38B09D0C0A92F2 CRC64; MSTILEKISA IESEMARTQK NKATSAHLGL LKAKLAKLRR ELISPKGGGG GTGEAGFEVA KTGDARVGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT TVPGCIKYKG AKIQLLDLPG IIEGAKDGKG RGRQVIAVAR TCNLIFMVLD CLKPLGHKKL LEHELEGFGI RLNKKPPNIY YKRKDKGGIN LNSMVPQSEL DTDLVKTILS EYKIHNADIT LRYDATSDDL IDVIEGNRIY IPCIYLLNKI DQISIEELDV IYKIPHCVPI SAHHHWNFDD LLELMWEYLR LQRIYTKPKG QLPDYNSPVV LHNERTSIED FCNKLHRSIA KEFKYALVWG SSVKHQPQKV GIEHVLNDED VVQIVKKV // ID 12AH_CLOS4 Reviewed; 29 AA. AC P21215; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 31-OCT-2006, entry version 25. DE 12-alpha-hydroxysteroid dehydrogenase (EC 1.1.1.176) (Fragment). OS Clostridium sp. (strain C 48-50). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1507; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=91177018; PubMed=2007406; RA Braun M., Luensdorf H., Bueckmann A.F.; RT "12 alpha-hydroxysteroid dehydrogenase from Clostridium group P, RT strain C 48-50. Production, purification and characterization."; RL Eur. J. Biochem. 196:439-450(1991). CC -!- FUNCTION: Catalyzes the oxidation of the 12-alpha-hydroxyl group CC of bile acids, both in their free and conjugated form. Also acts CC on bile alcohols. CC -!- CATALYTIC ACTIVITY: 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta- CC cholanate + NADP(+) = 3-alpha,7-alpha-dihydroxy-12-oxo-5-beta- CC cholanate + NADPH. CC -!- SUBUNIT: Homotetramer. CC -!- MISCELLANEOUS: The thermostability of the enzyme is greatly CC increased due to NADP binding. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S14099; S14099. DR GO; GO:0047013; F:12-alpha-hydroxysteroid dehydrogenase activity; IEA:EC. KW Bile acid catabolism; Direct protein sequencing; Lipid metabolism; KW NADP; Oxidoreductase; Steroid metabolism. FT CHAIN 1 >29 12-alpha-hydroxysteroid dehydrogenase. FT /FTId=PRO_0000064347. FT NON_TER 29 29 SQ SEQUENCE 29 AA; 2900 MW; A827DB34DB6C8812 CRC64; MIFDGKVAII TGGGKAKSIG YGIAVAYAK // ID 12KD_FRAAN Reviewed; 111 AA. AC Q05349; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 31-OCT-2006, entry version 26. DE Auxin-repressed 12.5 kDa protein. OS Fragaria ananassa (Strawberry). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Rosales; Rosaceae; Rosoideae; Fragaria. OX NCBI_TaxID=3747; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Ozark Beauty; TISSUE=Flower; RX MEDLINE=91329668; PubMed=2101687; RA Reddy A.S.N., Poovaiah B.W.; RT "Molecular cloning and sequencing of a cDNA for an auxin-repressed RT mRNA: correlation between fruit growth and repression of the auxin- RT regulated gene."; RL Plant Mol. Biol. 14:127-136(1990). CC -!- INDUCTION: Repressed by exogenous auxin. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X52429; CAA36676.1; -; mRNA. DR EMBL; L44142; AAA73872.1; -; mRNA. DR PIR; S11850; S11850. DR InterPro; IPR008406; Auxin_repressed. DR Pfam; PF05564; Auxin_repressed; 1. KW Auxin signaling pathway. FT CHAIN 1 111 Auxin-repressed 12.5 kDa protein. FT /FTId=PRO_0000064348. FT COMPBIAS 43 57 Pro/Thr-rich. SQ SEQUENCE 111 AA; 12416 MW; E44CACBADE6F3C51 CRC64; MVLLDKLWDD IVAGPQPERG LGMLRKVPQP LNLKDEGESS KITMPTTPTT PVTPTTPISA RKDNVWRSVF HPGSNLSSKT MGNQVFDSPQ PNSPTVYDWM YSGETRSKHH R // ID 12KD_MYCSM Reviewed; 24 AA. AC P80438; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 31-OCT-2006, entry version 15. DE 12 kDa protein (Fragment). OS Mycobacterium smegmatis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1772; RN [1] RP PROTEIN SEQUENCE. RA Pahl A., Keller U.; RL Submitted (MAR-1995) to Swiss-Prot. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Direct protein sequencing. FT CHAIN 1 >24 12 kDa protein. FT /FTId=PRO_0000064349. FT NON_TER 24 24 SQ SEQUENCE 24 AA; 2766 MW; 0D19F1F488DB3201 CRC64; MFHVLTLTYL CPLDVVXQTR PAHV // ID 12S1_ARATH Reviewed; 472 AA. AC P15455; Q9FFH7; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2002, sequence version 2. DT 31-OCT-2006, entry version 58. DE 12S seed storage protein CRA1 precursor [Contains: 12S seed storage DE protein CRA1 alpha chain (12S seed storage protein CRA1 acidic chain); DE 12S seed storage protein CRA1 beta chain (12S seed storage protein DE CRA1 basic chain)]. GN Name=CRA1; OrderedLocusNames=At5g44120; ORFNames=MLN1.4; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Landsberg erecta; RA Pang P.P., Pruitt R.E., Meyerowitz E.M.; RT "Molecular cloning, genome organization, expression and evolution of RT 12S seed storage protein genes of Arabidopsis thaliana."; RL Plant Mol. Biol. 11:805-820(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=97471969; PubMed=9330910; DOI=10.1093/dnares/4.3.215; RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., RA Miyajima N., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence RT features of the 1.6 Mb regions covered by twenty physically assigned RT P1 clones."; RL DNA Res. 4:215-230(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 420-472. RC STRAIN=cv. Columbia; TISSUE=Green siliques; RX MEDLINE=94108489; PubMed=8281187; RX DOI=10.1046/j.1365-313X.1993.04061051.x; RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., RA Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., RA Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., RA de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., RA Bardet C., Tremousaygue D., Lescure B.; RT "An inventory of 1152 expressed sequence tags obtained by partial RT sequencing of cDNAs from Arabidopsis thaliana."; RL Plant J. 4:1051-1061(1993). CC -!- FUNCTION: This is a seed storage protein. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences; CC Name=1; CC IsoId=P15455-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; M37247; AAA32777.1; -; Genomic_DNA. DR EMBL; X14312; CAA32493.1; -; Genomic_DNA. DR EMBL; AB005239; BAB10979.1; -; Genomic_DNA. DR EMBL; AY070730; AAL50071.1; -; mRNA. DR EMBL; Z17590; CAA79005.1; -; mRNA. DR PIR; S08509; S08509. DR UniGene; At.20540; -. DR HSSP; P04776; 1FXZ. DR GenomeReviews; BA000015_GR; AT5G44120. DR KEGG; ath:At5g44120; -. DR TAIR; At5g44120; -. DR ArrayExpress; P15455; -. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR006044; Seedstore11s_pln. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. KW Alternative splicing; Seed storage protein; Signal; Storage protein. FT SIGNAL 1 24 Potential. FT CHAIN 25 282 12S seed storage protein CRA1 alpha chain FT (By similarity). FT /FTId=PRO_0000031999. FT CHAIN 283 472 12S seed storage protein CRA1 beta chain FT (By similarity). FT /FTId=PRO_0000032000. FT DISULFID 112 289 Interchain (between alpha and beta FT chains) (Potential). FT CONFLICT 167 167 E -> Q (in Ref. 1). FT CONFLICT 356 356 V -> E (in Ref. 1). SQ SEQUENCE 472 AA; 52595 MW; 700B468E4D251994 CRC64; MARVSSLLSF CLTLLILFHG YAAQQGQQGQ QFPNECQLDQ LNALEPSHVL KSEAGRIEVW DHHAPQLRCS GVSFARYIIE SKGLYLPSFF NTAKLSFVAK GRGLMGKVIP GCAETFQDSS EFQPRFEGQG QSQRFRDMHQ KVEHIRSGDT IATTPGVAQW FYNDGQEPLV IVSVFDLASH QNQLDRNPRP FYLAGNNPQG QVWLQGREQQ PQKNIFNGFG PEVIAQALKI DLQTAQQLQN QDDNRGNIVR VQGPFGVIRP PLRGQRPQEE EEEEGRHGRH GNGLEETICS ARCTDNLDDP SRADVYKPQL GYISTLNSYD LPILRFIRLS ALRGSIRQNA MVLPQWNANA NAILYVTDGE AQIQIVNDNG NRVFDGQVSQ GQLIAVPQGF SVVKRATSNR FQWVEFKTNA NAQINTLAGR TSVLRGLPLE VITNGFQISP EEARRVKFNT LETTLTHSSG PASYGRPRVA AA // ID 12S2_ARATH Reviewed; 455 AA. AC P15456; Q9SAW0; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2002, sequence version 2. DT 23-JAN-2007, entry version 62. DE 12S seed storage protein CRB precursor [Contains: 12S seed storage DE protein CRB alpha chain (12S seed storage protein CRB acidic chain); DE 12S seed storage protein CRB beta chain (12S seed storage protein CRB DE basic chain)]. GN Name=CRB; OrderedLocusNames=At1g03880; ORFNames=F21M11.19; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Landsberg erecta; RA Pang P.P., Pruitt R.E., Meyerowitz E.M.; RT "Molecular cloning, genome organization, expression and evolution of RT 12S seed storage protein genes of Arabidopsis thaliana."; RL Plant Mol. Biol. 11:805-820(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 240-360. RC STRAIN=cv. Columbia; TISSUE=Green siliques; RX MEDLINE=94108489; PubMed=8281187; RX DOI=10.1046/j.1365-313X.1993.04061051.x; RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., RA Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., RA Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., RA de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., RA Bardet C., Tremousaygue D., Lescure B.; RT "An inventory of 1152 expressed sequence tags obtained by partial RT sequencing of cDNAs from Arabidopsis thaliana."; RL Plant J. 4:1051-1061(1993). CC -!- FUNCTION: This is a seed storage protein. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond. CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; M37248; AAA32778.1; -; Genomic_DNA. DR EMBL; X14313; CAA32494.1; -; Genomic_DNA. DR EMBL; AC003027; AAD10680.1; -; Genomic_DNA. DR EMBL; AY093005; AAM13004.1; -; mRNA. DR EMBL; BT009682; AAP81800.1; -; mRNA. DR EMBL; Z17654; CAA79024.1; -; mRNA. DR PIR; E86169; E86169. DR PIR; S08510; S08510. DR UniGene; At.20; -. DR HSSP; P04776; 1FXZ. DR GenomeReviews; CT485782_GR; AT1G03880. DR KEGG; ath:At1g03880; -. DR TAIR; At1g03880; -. DR ArrayExpress; P15456; -. DR GermOnline; AT1G03880; Arabidopsis thaliana. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR006044; Seedstore11s_pln. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 24 Potential. FT CHAIN 25 269 12S seed storage protein CRB alpha chain FT (By similarity). FT /FTId=PRO_0000032001. FT CHAIN 270 455 12S seed storage protein CRB beta chain FT (By similarity). FT /FTId=PRO_0000032002. FT DISULFID 106 276 Interchain (between alpha and beta FT chains) (Potential). FT CONFLICT 383 383 A -> R (in Ref. 1). SQ SEQUENCE 455 AA; 50558 MW; BE24BCBD2F69B538 CRC64; MGRVSSIISF SLTLLILFNG YTAQQWPNEC QLDQLNALEP SQIIKSEGGR IEVWDHHAPQ LRCSGFAFER FVIEPQGLFL PTFLNAGKLT FVVHGRGLMG RVIPGCAETF MESPVFGEGQ GQGQSQGFRD MHQKVEHLRC GDTIATPSGV AQWFYNNGNE PLILVAAADL ASNQNQLDRN LRPFLIAGNN PQGQEWLQGR KQQKQNNIFN GFAPEILAQA FKINVETAQQ LQNQQDNRGN IVKVNGPFGV IRPPLRRGEG GQQPHEIANG LEETLCTMRC TENLDDPSDA DVYKPSLGYI STLNSYNLPI LRLLRLSALR GSIRKNAMVL PQWNVNANAA LYVTNGKAHI QMVNDNGERV FDQEISSGQL LVVPQGFSVM KHAIGEQFEW IEFKTNENAQ VNTLAGRTSV MRGLPLEVIT NGYQISPEEA KRVKFSTIET TLTHSSPMSY GRPRA // ID 12S_PROFR Reviewed; 611 AA. AC Q8GBW6; Q05617; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 24. DE Methylmalonyl-CoA carboxyltransferase 12S subunit (EC 2.1.3.1) DE (Transcarboxylase 12S subunit). OS Propionibacterium freudenreichii subsp. shermanii. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1752; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-6; 13-39; RP 56-63; 71-112; 199-213; 252-280; 351-372; 395-405; 500-516; 532-567 RP AND 598-607. RC STRAIN=St33; RX MEDLINE=93374821; PubMed=8366018; RA Thornton C.G., Kumar G.K., Haase F.C., Phillips N.F.B., Woo S.B., RA Park V.M., Magner W.J., Shenoy B.C., Wood H.G., Samols D.; RT "Primary structure of the monomer of the 12S subunit of RT transcarboxylase as deduced from DNA and characterization of the RT product expressed in Escherichia coli."; RL J. Bacteriol. 175:5301-5308(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-525, AND X-RAY CRYSTALLOGRAPHY (1.9 RP ANGSTROMS) OF 1-524. RX PubMed=12743028; DOI=10.1093/emboj/cdg244; RA Hall P.R., Wang Y.-F., Rivera-Hainaj R.E., Zheng X., Pusztai-Carey M., RA Carey P.R., Yee V.C.; RT "Transcarboxylase 12S crystal structure: hexamer assembly and RT substrate binding to a multienzyme core."; RL EMBO J. 22:2334-2347(2003). CC -!- FUNCTION: The 12S subunit specifically catalyzes the transfer of CC the carboxyl group of methylmalonyl CoA to the biotin of the 1.3S CC subunit forming propanoyl-CoA and carboxylated 1.3S-biotin. CC -!- CATALYTIC ACTIVITY: (S)-methylmalonyl-CoA + pyruvate = propanoyl- CC CoA + oxaloacetate. CC -!- SUBUNIT: Homohexamer. Transcarboxylase is composed of three CC subunits: 1.3S, 5S, and 12S. The core of the enzyme is composed of CC six 12S subunits. On each side of the core there are three pairs CC of 5S subunits. Each 5S dimer is attached to the core by two 1.3S CC subunits. Thus the total number of chains is 30 (6 + 12 + 12). CC -!- SIMILARITY: Contains 1 carboxyltransferase domain. CC -!- CAUTION: Ref.1 (AAA25676) sequence differs from that shown due to CC several frameshifts. CC -!- CAUTION: Ref.2 (CAD59919) sequence differs from that shown due to CC a frameshift in position 519. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L04196; AAA25676.1; ALT_FRAME; Genomic_DNA. DR EMBL; AJ535715; CAD59919.1; ALT_FRAME; mRNA. DR PIR; A48665; A48665. DR PDB; 1ON3; X-ray; A/B/C/D/E/F=1-518. DR PDB; 1ON9; X-ray; A/B/C/D/E/F=1-518. DR GO; GO:0047154; F:methylmalonyl-CoA carboxytransferase activity; IEA:EC. DR InterPro; IPR000438; ACoACC_transB. DR InterPro; IPR000022; Carboxyl_trans. DR InterPro; IPR011763; COA_CT_C. DR InterPro; IPR011762; COA_CT_N. DR Pfam; PF01039; Carboxyl_trans; 1. DR PRINTS; PR01070; ACCCTRFRASEB. DR PROSITE; PS50989; COA_CT_CTER; 1. DR PROSITE; PS50980; COA_CT_NTER; 1. KW 3D-structure; Direct protein sequencing; Transferase. FT INIT_MET 1 1 Removed. FT CHAIN 2 611 Methylmalonyl-CoA carboxyltransferase 12S FT subunit. FT /FTId=PRO_0000146817. FT CONFLICT 35 35 R -> L (in Ref. 1). FT CONFLICT 143 143 Missing (in Ref. 1). FT CONFLICT 181 182 GG -> C (in Ref. 1). FT CONFLICT 377 377 Missing (in Ref. 1). FT CONFLICT 390 390 A -> R (in Ref. 1). FT HELIX 13 28 FT TURN 29 31 FT HELIX 33 41 FT TURN 42 43 FT HELIX 47 54 FT TURN 57 58 FT STRAND 61 63 FT TURN 65 66 FT TURN 73 78 FT HELIX 82 85 FT STRAND 86 93 FT TURN 94 95 FT STRAND 96 103 FT TURN 105 107 FT HELIX 108 110 FT HELIX 114 130 FT TURN 131 131 FT STRAND 134 140 FT HELIX 145 148 FT HELIX 149 165 FT TURN 166 168 FT STRAND 171 181 FT HELIX 182 184 FT HELIX 185 189 FT STRAND 190 196 FT TURN 197 198 FT STRAND 200 204 FT HELIX 206 213 FT HELIX 219 223 FT HELIX 225 230 FT TURN 231 232 FT STRAND 236 241 FT HELIX 242 254 FT TURN 255 255 FT TURN 260 261 FT HELIX 277 281 FT TURN 282 282 FT TURN 287 288 FT TURN 293 293 FT HELIX 294 300 FT HELIX 302 304 FT STRAND 306 310 FT TURN 311 312 FT TURN 315 316 FT STRAND 317 324 FT TURN 325 326 FT STRAND 327 334 FT TURN 336 337 FT HELIX 339 341 FT HELIX 345 360 FT TURN 361 362 FT STRAND 365 371 FT HELIX 378 382 FT TURN 383 384 FT HELIX 385 398 FT STRAND 403 412 FT HELIX 413 417 FT TURN 418 420 FT HELIX 422 424 FT TURN 425 425 FT STRAND 427 431 FT TURN 433 434 FT STRAND 436 440 FT HELIX 442 449 FT TURN 450 450 FT HELIX 451 456 FT HELIX 460 475 FT HELIX 478 483 FT TURN 484 485 FT STRAND 486 490 FT HELIX 493 495 FT HELIX 496 506 FT HELIX 507 509 SQ SEQUENCE 611 AA; 65927 MW; 625F1B284107B1FC CRC64; MAENNNLKLA STMEGRVEQL AEQRQVIEAG GGERRVEKQH SQGKQTARER LNNLLDPHSF DEVGAFRKHR TTLFGMDKAV VPADGVVTGR GTILGRPVHA ASQDFTVMGG SAGETQSTKV VETMEQALLT GTPFLFFYDS GGARIQEGID SLSGYGKMFF ANVKLSGVVP QIAIIAGPCA GGASYSPALT DFIIMTKKAH MFITGPQVIK SVTGEDVTAD ELGGAEAHMA ISGNIHFVAE DDDAAELIAK KLLSFLPQNN TEEASFVNPN NDVSPNTELR DIVPIDGKKG YDVRDVIAKI VDWGDYLEVK AGYATNLVTA FARVNGRSVG IVANQPSVMS GCLDINASDK AAEFVNFCDS FNIPLVQLVD VPGFLPGVQQ EYGGIIRHGA KMLYAYSEAT VPKITVVLRK AYGGSYLAMC NRDLGADAVY AWPSAEIAVM GAEGAANVIF RKEIKAADDP DAMRAEKIEE YQNAFNTPYV AAARGQVDDV IDPADTRRKI ASALEMYATK RQTRPAKKPW KLPLLSEEEI MADEEEKDLM IATLNKRVAS LESELGSLQS DTQGVTEDVL TAISAVAAYL GNDGSAEVVH FAPSPNWVRE GRRALQNHSI R // ID 13KDA_SCYCA Reviewed; 14 AA. AC P83011; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 31-OCT-2006, entry version 14. DE 13.2 kDa protein (Fragment). OS Scyliorhinus canicula (Spotted dogfish) (Spotted catshark). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; OC Scyliorhinidae; Scyliorhinus. OX NCBI_TaxID=7830; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Rectal gland; RX MEDLINE=21534268; PubMed=11676495; DOI=10.1006/bbrc.2001.5826; RA Schuurmans Stekhoven F.M.A.H., Flik G., Wendelaar Bonga S.E.; RT "N-terminal sequences of small ion channels in rectal glands of RT sharks: a biochemical hallmark for classification and phylogeny?"; RL Biochem. Biophys. Res. Commun. 288:670-675(2001). CC -!- SUBCELLULAR LOCATION: Microsome. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR GO; GO:0005792; C:microsome; IDA:UniProtKB. KW Direct protein sequencing; Endoplasmic reticulum; Microsome. FT CHAIN 1 >14 13.2 kDa protein. FT /FTId=PRO_0000064350. FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1575 MW; 89B2AE42D9B79D0A CRC64; MIFTAXDRSA IEXV // ID 13KDA_TRISC Reviewed; 13 AA. AC P83010; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 31-OCT-2006, entry version 17. DE 13 kDa protein (Fragment). OS Triakis scyllium (Leopard shark) (Triakis scyllia). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Triakidae; OC Triakis. OX NCBI_TaxID=30494; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Rectal gland; RX MEDLINE=21534268; PubMed=11676495; DOI=10.1006/bbrc.2001.5826; RA Schuurmans Stekhoven F.M.A.H., Flik G., Wendelaar Bonga S.E.; RT "N-terminal sequences of small ion channels in rectal glands of RT sharks: a biochemical hallmark for classification and phylogeny?"; RL Biochem. Biophys. Res. Commun. 288:670-675(2001). CC -!- SUBCELLULAR LOCATION: Microsome. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR GO; GO:0005792; C:microsome; IDA:UniProtKB. DR InterPro; IPR000272; FXYD. KW Direct protein sequencing; Endoplasmic reticulum; Microsome. FT CHAIN 1 >13 13 kDa protein. FT /FTId=PRO_0000064351. FT NON_TER 13 13 SQ SEQUENCE 13 AA; 1497 MW; 1D140C92C1AE1444 CRC64; AGEPANNEDR FNY // ID 13S1_FAGES Reviewed; 565 AA. AC O23878; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 31-OCT-2006, entry version 41. DE 13S globulin seed storage protein 1 precursor (Legumin-like protein 1) DE [Contains: 13S globulin seed storage protein 1 acidic chain; 13S DE globulin seed storage protein 1 basic chain]. GN Name=FA02; OS Fagopyrum esculentum (Common buckwheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Polygonaceae; Fagopyrum. OX NCBI_TaxID=3617; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=cv. Kitayuki; TISSUE=Immature seed; RX MEDLINE=21205935; PubMed=11308332; DOI=10.1021/jf0011485; RA Fujino K., Funatsuki H., Inada M., Shimono Y., Kikuta Y.; RT "Expression, cloning, and immunological analysis of buckwheat RT (Fagopyrum esculentum Moench) seed storage proteins."; RL J. Agric. Food Chem. 49:1825-1829(2001). CC -!- FUNCTION: Seed storage protein. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond (By similarity). CC -!- TISSUE SPECIFICITY: Expressed only in immatures seeds. CC -!- DEVELOPMENTAL STAGE: Expressed between 7 and 28 days after CC pollination. CC -!- MISCELLANEOUS: The sequence of the probable beta chain is highly CC homologous to the N-terminal sequence of BW24KD, a major buckwheat CC allergen. CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; D87980; BAA21758.1; -; mRNA. DR PIR; T10696; T10696. DR HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR006044; Seedstore11s_pln. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 20 Potential. FT CHAIN 21 377 13S globulin seed storage protein 1 FT acidic chain (By similarity). FT /FTId=PRO_0000032003. FT CHAIN 378 565 13S globulin seed storage protein 1 basic FT chain (By similarity). FT /FTId=PRO_0000032004. FT DISULFID 120 384 Interchain (between acidic and basic FT chains) (Potential). SQ SEQUENCE 565 AA; 64518 MW; 2DD7FCC64E3CD4F0 CRC64; MSTKLILSFS LCLMVLSCSA QLLPWRKGQR SRPHRGHQQF HHQCDVQRLT ASEPSRRVRS EAGVTEIWDN DTPEFRCAGF VAVRVVIQPG GLLLPSYSNA PYITFVEQGR GVQGVVVPGC PETFQSESEF EYPQSQRDQR SRQSESEESS RGDQRTRQSE SEEFSRGDQR TRQSESEEFS RGDQRTRQSE SEEFSRGDQR TRQSESEEFS RGDQHQKIFR IRDGDVIPSP AGVVQWTHND GDNDLISITL YDANSFQNQL DGNVRNFFLA GQSKQSREDR RSQRQTREEG SDRQSRESDD DEALLEANIL TGFQDEILQE IFRNVDQETI SKLRGDNDQR GFIVQARDLK LRVPEEYEEE LQRERGDRKR GGSGRSNGLE QAFCNLKFKQ NVNRPSRADV FNPRAGRINT VNSNNLPILE FIQLSAQHVV LYKNAILGPR WNLNAHSALY VTRGEGRVQV VGDEGRSVFD DNVQRGQILV VPQGFAVVLK AGREGLEWVE LKNDDNAITS PIAGKTSVLR AIPVEVLANS YDISTKEAFR LKNGRQEVEV FLPFQSRDEK ERERF // ID 13S2_FAGES Reviewed; 504 AA. AC O23880; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 31-OCT-2006, entry version 41. DE 13S globulin seed storage protein 2 precursor (Legumin-like protein 2) DE [Contains: 13S globulin seed storage protein 2 acidic chain; 13S DE globulin seed storage protein 2 basic chain]. GN Name=FA18; OS Fagopyrum esculentum (Common buckwheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Polygonaceae; Fagopyrum. OX NCBI_TaxID=3617; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Kitayuki; TISSUE=Immature seed; RX MEDLINE=21205935; PubMed=11308332; DOI=10.1021/jf0011485; RA Fujino K., Funatsuki H., Inada M., Shimono Y., Kikuta Y.; RT "Expression, cloning, and immunological analysis of buckwheat RT (Fagopyrum esculentum Moench) seed storage proteins."; RL J. Agric. Food Chem. 49:1825-1829(2001). CC -!- FUNCTION: Seed storage protein. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond (By similarity). CC -!- MISCELLANEOUS: The sequence of the probable beta chain is highly CC homologous to the N-terminal sequence of BW24KD, a major buckwheat CC allergen. CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; D87982; BAA21760.1; -; mRNA. DR PIR; T10698; T10698. DR HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR006044; Seedstore11s_pln. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 20 Potential. FT CHAIN 21 313 13S globulin seed storage protein 2 FT acidic chain (By similarity). FT /FTId=PRO_0000032005. FT CHAIN 314 504 13S globulin seed storage protein 2 basic FT chain (By similarity). FT /FTId=PRO_0000032006. FT DISULFID 122 320 Interchain (between acidic and basic FT chains) (Potential). SQ SEQUENCE 504 AA; 57043 MW; CDCA322394A28194 CRC64; MSTKLILSFS LCLMVLSCSA QLWPWQKGQG SRPHHGRQQH QFQHQCDIQR LTASEPSRRV RSEAGVTEIW DHDTPEFRCT GFVAVRVVIQ PGGLLLPSYS NAPYITFVEQ GRGVQGVVIP GCPETFQSDS EFEYPQSQRG RHSRQSESEE ESSRGDQHQK IFRIREGDVI PSPAGVVQWT HNDGNDDLIS VTLLDANSYH KQLDENVRSF FLAGQSQRET REEGSDRQSR ESDDDEALLG ANILSGFQDE ILHELFRDVD RETISKLRGE NDQRGFIVQA QDLKLRVPQD FEEEYERERG DRRRGQGGSG RSNGVEQGFC NLKFRRNFNT PTNTYVFNPR AGRINTVNSN SLPILEFLQL SAQHVVLYKN AIIGPRWNLN AHSALYVTRG EGRVQVVGDE GKSVFDDKVQ RGQILVVPQG FAVVLKAGRE GLEWVELKNS GNAITSPIGG RTSVLRAIPV EVLANSYDIS TKEAYKLKNG RQEVEVFRPF QSRDEKERER FSIV // ID 13S3_FAGES Reviewed; 538 AA. AC Q9XFM4; Q9M641; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 31-OCT-2006, entry version 39. DE 13S globulin seed storage protein 3 precursor (Legumin-like protein 3) DE (Allergen Fag e 1) [Contains: 13S globulin seed storage protein 3 DE acidic chain; 13S globulin seed storage protein 3 basic chain]. GN Name=FAGAG1; OS Fagopyrum esculentum (Common buckwheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Polygonaceae; Fagopyrum. OX NCBI_TaxID=3617; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Miyazaki zairai; RA Nair A., Ohmoto T., Woo S.H., Adachi T.; RT "A molecular-genetic approach for hypoallergenic buckwheat."; RL Fagopyrum 16:29-36(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 348-538. RX MEDLINE=22690748; PubMed=12806007; DOI=10.1100/tsw.2002.157; RA Nair A., Adachi T.; RT "Screening and selection of hypoallergenic buckwheat species."; RL ScientificWorldJournal 2:818-826(2002). CC -!- FUNCTION: Seed storage protein. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond (By similarity). CC -!- ALLERGEN: Causes an allergic reaction in human. CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; AF152003; AAD32713.1; -; mRNA. DR EMBL; AF216801; AAF34635.1; -; Genomic_DNA. DR HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR006044; Seedstore11s_pln. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. KW Allergen; Seed storage protein; Signal; Storage protein. FT SIGNAL 1 20 Potential. FT CHAIN 21 347 13S globulin seed storage protein 3 FT acidic chain (By similarity). FT /FTId=PRO_0000032007. FT CHAIN 348 538 13S globulin seed storage protein 3 basic FT chain (By similarity). FT /FTId=PRO_0000032008. FT DISULFID 120 354 Interchain (between acidic and basic FT chains) (Potential). SQ SEQUENCE 538 AA; 61164 MW; 41D6BA55220CFDAC CRC64; MSTKLILSFS LCLMVLSCSA QLLPWQKGQR SRPHHGHQQF QHQCDIQRLT ASEPSRRVRS EAGVTEIWDH DTPEFRCAGF VAVRVVIQPG GLLLPSYSNA PYITFVEQGR GVQGVVVPGC PETFQSGSEF EYPRSQRDQR SRQSESGESS RGDQRSRQSE SEESSRGDQR SRQSESEEFS RGDQHQKIFR IRDGDVIPSP AGVVQWTHNN GDNDLISITL YDANSFQNQL DENVRNFFLA GQSKQSREDR RSQRQTREEG SDRQSRESQD DEALLEANIL SGFEDEILQE IFRNVDQETI SKLRGENDQR GFIVQARDLK LRVPEEYEEE LQRERGDRKR GGSGRSNGLE QAFCNLKFRQ NVNRPSRADV FNPRAGRINT VDSNNLPILE FIQLSAQHVV LYKNAILGPR WNLNAHSALY VTRGEGRVQV VGDEGRSVFD DNVQRGQILV VPQGFAVVLK AGREGLEWVE LKNDDNAITS PIAGKTSVLR AIPVEVLANS YDISTKEAFR LKNGRQEVEV FRPFQSRDEK ERERFSIV // ID 13SB_FAGES Reviewed; 194 AA. AC P83004; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 31-OCT-2006, entry version 25. DE 13S globulin basic chain. OS Fagopyrum esculentum (Common buckwheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Polygonaceae; Fagopyrum. OX NCBI_TaxID=3617; RN [1] RP PROTEIN SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=cv. BDS-1354; TISSUE=Endosperm; RX MEDLINE=22545158; PubMed=12657290; DOI=10.1016/S0031-9422(02)00755-0; RA Bharali S., Chrungoo N.K.; RT "Amino acid sequence of the 26 kDa subunit of legumin-type seed RT storage protein of common buckwheat (Fagopyrum esculentum Moench): RT molecular characterization and phylogenetic analysis."; RL Phytochemistry 63:1-5(2003). RN [2] RP PROTEIN SEQUENCE OF 1-17. RX MEDLINE=97357448; PubMed=9214774; DOI=10.1016/S0031-9422(97)00051-4; RA Rout M.K., Chrungoo N.K., Rao K.S.; RT "Amino acid sequence of the basic subunit of 13S globulin of RT buckwheat."; RL Phytochemistry 45:865-867(1997). CC -!- FUNCTION: Seed storage protein with a relatively high level of Lys CC and Met. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond (By similarity). CC -!- TISSUE SPECIFICITY: Cotyledons and endosperm protein bodies. CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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 HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR006044; Seedstore11s_pln. DR Pfam; PF00190; Cupin_1; 1. DR PRINTS; PR00439; 11SGLOBULIN. KW Direct protein sequencing; Seed storage protein; Storage protein. FT CHAIN 1 194 13S globulin basic chain. FT /FTId=PRO_0000152877. FT DISULFID 7 ? Interchain (between basic and acidic FT chains) (Potential). SQ SEQUENCE 194 AA; 21847 MW; 65A6FC49AFC1E9D0 CRC64; GIDENVCTMK LRENIKSPQE ADFYNPKAGR ITTANSQKLP ALRSLQMSAE RGFLYSNGIY APHWNINAHS ALYVTRGNAK VQVVGDEGNK VFDDEVKQGQ LIIVPQYFAV IKKAGNQGFE YVAFKTNDNA MINPLVGRLS AFRAIPEEVL RSSFQISSEE AEELKYGRQE ALLLSEQSQQ GKREVADEKE RERF // ID 140U_DROME Reviewed; 261 AA. AC P81928; Q9VFM8; DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2003, sequence version 2. DT 06-FEB-2007, entry version 38. DE RPII140-upstream gene protein. GN Name=140up; ORFNames=CG9852; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC TISSUE=Embryo; RX MEDLINE=91276237; PubMed=1905256; DOI=10.1016/0378-1119(91)90361-E; RA Sitzler S., Oldenburg I., Petersen G., Bautz E.K.F.; RT "Analysis of the promoter region of the housekeeping gene DmRP140 by RT sequence comparison of Drosophila melanogaster and Drosophila RT virilis."; RL Gene 100:155-162(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: Essential for viability. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein CC (Potential). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M62975; AAD40352.2; -; Genomic_DNA. DR EMBL; AE014297; AAF55023.1; -; Genomic_DNA. DR EMBL; AY058577; AAL13806.1; -; mRNA. DR PIR; JQ1024; JQ1024. DR UniGene; Dm.10056; -. DR Ensembl; CG9852; Drosophila melanogaster. DR KEGG; dme:Dmel_CG9852; -. DR FlyBase; FBgn0010340; 140up. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-011545-MONOMER; -. DR GermOnline; CG9852; Drosophila melanogaster. DR GO; GO:0007275; P:multicellular organismal development; IMP:UniProtKB. DR InterPro; IPR003397; Tim17_Tim22. DR Pfam; PF02466; Tim17; 1. KW Complete proteome; Membrane; Transmembrane. FT CHAIN 1 261 RPII140-upstream gene protein. FT /FTId=PRO_0000064352. FT TRANSMEM 67 87 Potential. FT TRANSMEM 131 151 Potential. FT TRANSMEM 183 203 Potential. FT CONFLICT 64 64 S -> F (in Ref. 1). SQ SEQUENCE 261 AA; 29182 MW; 5DB78CF6CFC4435A CRC64; MNFLWKGRRF LIAGILPTFE GAADEIVDKE NKTYKAFLAS KPPEETGLER LKQMFTIDEF GSISSELNSV YQAGFLGFLI GAIYGGVTQS RVAYMNFMEN NQATAFKSHF DAKKKLQDQF TVNFAKGGFK WGWRVGLFTT SYFGIITCMS VYRGKSSIYE YLAAGSITGS LYKVSLGLRG MAAGGIIGGF LGGVAGVTSL LLMKASGTSM EEVRYWQYKW RLDRDENIQQ AFKKLTEDEN PELFKAHDEK TSEHVSLDTI K // ID 14310_ARATH Reviewed; 254 AA. AC P48347; Q9LME5; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 20-FEB-2007, entry version 55. DE 14-3-3-like protein GF14 epsilon (General regulatory factor 10). GN Name=GRF10; OrderedLocusNames=At1g22300; ORFNames=T16E15.8; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC STRAIN=cv. Columbia; RX MEDLINE=97422888; PubMed=9276953; DOI=10.1104/pp.114.4.1421; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC STRAIN=cv. Columbia; RA Chung H.-J., Shanker S., Ferl R.J.; RT "Sequences of five Arabidopsis general regulatory factor (GRF) genes RT encoding 14-3-3 proteins."; RL (er) Plant Gene Register PGR99-114. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P48347-1; Sequence=Displayed; CC Name=2; CC IsoId=P48347-2; Sequence=VSP_008972; CC -!- SIMILARITY: Belongs to the 14-3-3 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; U36446; AAA79699.1; -; mRNA. DR EMBL; AF145302; AAD51785.1; -; Genomic_DNA. DR EMBL; AC068562; AAF87261.1; -; Genomic_DNA. DR EMBL; AF334382; AAG50088.1; -; mRNA. DR EMBL; AY054505; AAK96696.1; -; mRNA. DR EMBL; AY058834; AAL24222.1; -; mRNA. DR EMBL; AY062838; AAL32916.1; -; mRNA. DR EMBL; AY081674; AAM10236.1; -; mRNA. DR EMBL; AY087580; AAM65122.1; -; mRNA. DR PIR; H86355; H86355. DR UniGene; At.24553; -. DR UniGene; At.67728; -. DR HSSP; P93343; 1O9E. DR SMR; P48347; 4-233. DR GenomeReviews; CT485782_GR; AT1G22300. DR KEGG; ath:At1g22300; -. DR TAIR; At1g22300; -. DR ArrayExpress; P48347; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Alternative splicing. FT CHAIN 1 254 14-3-3-like protein GF14 epsilon. FT /FTId=PRO_0000058672. FT VAR_SEQ 254 254 N -> V (in isoform 2). FT /FTId=VSP_008972. SQ SEQUENCE 254 AA; 28915 MW; 037405C341845C25 CRC64; MENEREKQVY LAKLSEQTER YDEMVEAMKK VAQLDVELTV EERNLVSVGY KNVIGARRAS WRILSSIEQK EESKGNDENV KRLKNYRKRV EDELAKVCND ILSVIDKHLI PSSNAVESTV FFYKMKGDYY RYLAEFSSGA ERKEAADQSL EAYKAAVAAA ENGLAPTHPV RLGLALNFSV FYYEILNSPE SACQLAKQAF DDAIAELDSL NEESYKDSTL IMQLLRDNLT LWTSDLNEEG DERTKGADEP QDEN // ID 14310_SOLLC Reviewed; 252 AA. AC P93207; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 20-FEB-2007, entry version 40. DE 14-3-3 protein 10. GN Name=TFT10; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION TO 45-46 AND 131. RA Roberts M.R.; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-138. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RX MEDLINE=99214454; PubMed=10198082; DOI=10.1104/pp.119.4.1243; RA Roberts M.R., Bowles D.J.; RT "Fusicoccin, 14-3-3 proteins, and defense responses in tomato RT plants."; RL Plant Physiol. 119:1243-1250(1999). CC -!- SUBUNIT: Homodimer (Potential). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X98866; CAA67374.2; -; mRNA. DR UniGene; Les.3391; -. DR HSSP; P93343; 1O9E. DR SMR; P93207; 10-243. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 252 14-3-3 protein 10. FT /FTId=PRO_0000058690. SQ SEQUENCE 252 AA; 28624 MW; 45875AA21ADD0FFA CRC64; MAALIPENLS REQCLYLAKL AEQAERYEEM VQFMDKLVLN STPAGELTVE ERNLLSVAYK NVIGSLRAAW RIVSSIEQKE ESRKNEEHVH LVKEYRGKVE NELSQVCAGI LKLLESNLVP SATTSESKVF YLKMKGDYYR YLAEFKIGDE RKQAAEDTMN SYKAAQEIAL TDLPPTHPIR LGLALNFSVF YFEILNSSDK ACSMAKQAFE EAIAELDTLG EESYKDSTLI MQLLRDNLTL WTSDAQDQLD ES // ID 14311_ARATH Reviewed; 241 AA. AC Q9S9Z8; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 20-FEB-2007, entry version 37. DE 14-3-3-like protein GF14 omicron (General regulatory factor 11). GN Name=GRF11; OrderedLocusNames=At1g34760; ORFNames=F21H2.3; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RA Alsterfjord M., Rosenquist M., Larsson C., Sommarin M.; RT "Novel 14-3-3 isoforms in Arabidopsis thaliana."; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF323920; AAG47840.1; -; mRNA. DR EMBL; AC007894; AAD46005.1; -; Genomic_DNA. DR HSSP; P93343; 1O9E. DR SMR; Q9S9Z8; 4-233. DR KEGG; ath:At1g34760; -. DR TAIR; At1g34760; -. DR ArrayExpress; Q9S9Z8; -. DR GermOnline; AT1G34760; Arabidopsis thaliana. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 241 14-3-3-like protein GF14 omicron. FT /FTId=PRO_0000058673. SQ SEQUENCE 241 AA; 27514 MW; 82376B77F0800B42 CRC64; MENERAKQVY LAKLNEQAER YDEMVEAMKK VAALDVELTI EERNLLSVGY KNVIGARRAS WRILSSIEQK EESKGNEQNA KRIKDYRTKV EEELSKICYD ILAVIDKHLV PFATSGESTV FYYKMKGDYF RYLAEFKSGA DREEAADLSL KAYEAATSSA STELSTTHPI RLGLALNFSV FYYEILNSPE RACHLAKRAF DEAIAELDSL NEDSYKDSTL IMQLLRDNLT LWTSDLEEGG K // ID 14312_ARATH Reviewed; 268 AA. AC Q9C5W6; Q9FZD3; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 23-JAN-2007, entry version 35. DE 14-3-3-like protein GF14 iota (General regulatory factor 12). GN Name=GRF12; OrderedLocusNames=At1g26480; ORFNames=T1K7.15; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RA Alsterfjord M., Rosenquist M., Larsson C., Sommarin M.; RT "Novel 14-3-3 isoforms in Arabidopsis thaliana."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF335544; AAK11271.1; -; mRNA. DR EMBL; AC013427; AAF98570.1; -; Genomic_DNA. DR EMBL; BT006230; AAP12879.1; -; mRNA. DR PIR; F86391; F86391. DR UniGene; At.15965; -. DR HSSP; P93343; 1O9E. DR SMR; Q9C5W6; 9-238. DR GenomeReviews; CT485782_GR; AT1G26480. DR KEGG; ath:At1g26480; -. DR TAIR; At1g26480; -. DR ArrayExpress; Q9C5W6; -. DR GermOnline; AT1G26480; Arabidopsis thaliana. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 268 14-3-3-like protein GF14 iota. FT /FTId=PRO_0000058674. FT CONFLICT 268 268 N -> VVIHFKMRTDQRAWKLNEI (in Ref. 2). SQ SEQUENCE 268 AA; 30545 MW; 914F394CEC07A28C CRC64; MSSSGSDKER ETFVYMAKLS EQAERYDEMV ETMKKVARVN SELTVEERNL LSVGYKNVIG ARRASWRIMS SIEQKEESKG NESNVKQIKG YRQKVEDELA NICQDILTII DQHLIPHATS GEATVFYYKM KGDYYRYLAE FKTEQERKEA AEQSLKGYEA ATQAASTELP STHPIRLGLA LNFSVFYYEI MNSPERACHL AKQAFDEAIA ELDTLSEESY KDSTLIMQLL RDNLTLWTSD LPEDGGEDNI KTEESKQEQA KPADATEN // ID 14331_ARATH Reviewed; 267 AA. AC P42643; Q9M0S7; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 20-FEB-2007, entry version 48. DE 14-3-3-like protein GF14 chi (General regulatory factor 1). GN Name=GRF1; OrderedLocusNames=At4g09000; ORFNames=F23J3.30; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=95062733; PubMed=7972511; DOI=10.1104/pp.105.4.1459; RA Lu G., Rooney M.F., Wu K., Ferl R.J.; RT "Five cDNAs encoding Arabidopsis GF14 proteins."; RL Plant Physiol. 105:1459-1460(1994). RN [2] RP SEQUENCE REVISION TO N-TERMINUS. RA Ferl R.J., Lu G.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=95175611; PubMed=7870824; DOI=10.1104/pp.107.1.283; RA Rooney M.F., Ferl R.J.; RT "Sequences of three Arabidopsis general regulatory factor genes RT encoding GF14 (14-3-3) proteins."; RL Plant Physiol. 107:283-284(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SIMILARITY: Belongs to the 14-3-3 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; L09112; AAA96323.1; -; mRNA. DR EMBL; U09377; AAA96254.1; -; Genomic_DNA. DR EMBL; AL161513; CAB78024.1; -; Genomic_DNA. DR UniGene; At.47549; -. DR HSSP; P29312; 1A38. DR SMR; P42643; 8-241. DR GenomeReviews; CT486007_GR; AT4G09000. DR TAIR; At4g09000; -. DR ArrayExpress; P42643; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 267 14-3-3-like protein GF14 chi. FT /FTId=PRO_0000058663. FT CONFLICT 240 240 A -> T (in Ref. 4). SQ SEQUENCE 267 AA; 29902 MW; 328FA53189EB0290 CRC64; MATPGASSAR DEFVYMAKLA EQAERYEEMV EFMEKVAKAV DKDELTVEER NLLSVAYKNV IGARRASWRI ISSIEQKEES RGNDDHVSLI RDYRSKIETE LSDICDGILK LLDTILVPAA ASGDSKVFYL KMKGDYHRYL AEFKSGQERK DAAEHTLTAY KAAQDIANSE LAPTHPIRLG LALNFSVFYY EILNSPDRAC NLAKQAFDEA IAELDTLGEE SYKDSTLIMQ LLRDNLTLWA SDMQDDVADD IKEAAPAAAK PADEQQS // ID 14331_CAEEL Reviewed; 248 AA. AC P41932; Q21537; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-FEB-2007, entry version 42. DE 14-3-3-like protein 1 (Partitioning defective protein 5). GN Name=par-5; Synonyms=ftt-1; ORFNames=M117.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Bristol N2; RX MEDLINE=95011616; PubMed=7926802; DOI=10.1016/0378-1119(94)90068-X; RA Wang W., Shakes D.C.; RT "Isolation and sequence analysis of a Caenorhabditis elegans cDNA RT which encodes a 14-3-3 homologue."; RL Gene 147:215-218(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DAF-16 AND RP SIR-2.1, AND SUBCELLULAR LOCATION. RX PubMed=16777605; DOI=10.1016/j.cell.2006.04.036; RA Berdichevsky A., Viswanathan M., Horvitz H.R., Guarente L.; RT "C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 RT and extend life span."; RL Cell 125:1165-1177(2006). CC -!- SUBUNIT: Interacts with daf-16 and sir-2.1. CC -!- INTERACTION: CC Q9TYY1:lag-1; NbExp=1; IntAct=EBI-318108, EBI-324482; CC Q9NAE1:Y51H4A.8; NbExp=1; IntAct=EBI-318108, EBI-315053; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U05038; AAA61872.1; -; mRNA. DR EMBL; Z73910; CAA98138.1; -; Genomic_DNA. DR PIR; JC2581; JC2581. DR PIR; T23759; T23759. DR UniGene; Cel.17302; -. DR HSSP; P93343; 1O9E. DR SMR; P41932; 7-232. DR DIP; DIP:27044N; -. DR IntAct; P41932; -. DR Ensembl; M117.2; Caenorhabditis elegans. DR KEGG; cel:M117.2; -. DR WormBase; WBGene00003920; par-5. DR WormPep; M117.2; CE06200. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Complete proteome; Nuclear protein. FT CHAIN 1 248 14-3-3-like protein 1. FT /FTId=PRO_0000058647. FT CONFLICT 118 118 A -> V (in Ref. 2). SQ SEQUENCE 248 AA; 28163 MW; B9350039628341AF CRC64; MSDTVEELVQ RAKLAEQAER YDDMAAAMKK VTEQGQELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TEGSEKKQQL AKEYRVKVEQ ELNDICQDVL KLLDEFLIVK AGAAESKAFY LKMKGDYYRY LAEVASEDRA AVVEKSQKAY QEALDIAKDK MQPTHPIRLG LALNFSVFYY EILNTPEHAC QLAKQAFDDA IAELDTLNED SYKDSTLIMQ LLRDNLTLWT SDVGAEDQEQ EGNQEAGN // ID 14331_ECHGR Reviewed; 244 AA. AC Q9U408; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 28-NOV-2006, entry version 24. DE 14-3-3 protein homolog 1. OS Echinococcus granulosus. OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Taeniidae; Echinococcus. OX NCBI_TaxID=6210; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CW1; RX MEDLINE=21182697; PubMed=11289064; DOI=10.1017/S0031182001007405; RA Siles-Lucas M., Nunes C.P., Zaha A.; RT "Comparative analysis of the 14-3-3 gene and its expression in RT Echinococcus granulosus and Echinococcus multilocularis RT metacestodes."; RL Parasitology 122:281-287(2001). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF207904; AAF19966.1; -; mRNA. DR HSSP; P29312; 1A37. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 244 14-3-3 protein homolog 1. FT /FTId=PRO_0000058652. SQ SEQUENCE 244 AA; 27430 MW; 1FBC366D3054937B CRC64; MSRLAECTIS DTVDELVQRA KLAEQAERYD DMAGACKTMA KMRNELNNEE ANLLSVAYKN VVGARRSSWR IMSSIAKKQA GTPLAHQHDI YLKKVEEELI QICNDVLALP VLPITEKIGA EAKIFYYKMM GDYYRYSAEV QEGEQNDKST EAAEEANQKA TSLAEAELSV THPIRLGLAL NFSVFYYEIK NMPEKACSLA KAAFDAAITE VDSIKDETYK DSTLIMQLLR DNLTLWNSEC ETDS // ID 14331_ECHMU Reviewed; 244 AA. AC Q24902; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 3. DT 28-NOV-2006, entry version 32. DE 14-3-3 protein homolog 1 (Emma14-3-3.1). OS Echinococcus multilocularis. OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Taeniidae; Echinococcus. OX NCBI_TaxID=6211; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98226172; PubMed=9566521; DOI=10.1016/S0166-6851(97)00208-9; RA Siles-Lucas M., Felleisen R.S., Hemphill A., Wilson W., Gottstein B.; RT "Stage-specific expression of the 14-3-3 gene in Echinococcus RT multilocularis."; RL Mol. Biochem. Parasitol. 91:281-293(1998). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U63643; AAC48315.2; -; mRNA. DR HSSP; P29312; 1A37. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 244 14-3-3 protein homolog 1. FT /FTId=PRO_0000058653. SQ SEQUENCE 244 AA; 27368 MW; 593881484ACF4C4C CRC64; MSRLAECTIS DTVDELVQRA KLAEQAERYD DMAGACKTMA EMGNELNNEE RNLLSVAYKN VLGARRSSWR IMSSIAKKQA GTPLADQTDI YLKKVEEELI PICNDVLALP VLPITEKIGA EAKIFYYKMM GDYYRYLAEV QEGEQNDKST EAAEEANQKA TSLAEAELSV THPIRLGLAL NFSVFYYEIK NMPEKACSLA KAAFDAAITE VDSIKDETYK DSTLIMQLLR DNLTLWNSEC ETDS // ID 14331_ENTHI Reviewed; 239 AA. AC P42648; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 28-NOV-2006, entry version 29. DE 14-3-3 protein 1 (14-3-3-1). OS Entamoeba histolytica. OC Eukaryota; Entamoebidae; Entamoeba. OX NCBI_TaxID=5759; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=HM-1:IMSS; RA Samuelson J., Shen P., Meckler G., Descoteaux S., Fu H., Lohia A.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U13418; AAA80185.1; -; Genomic_DNA. DR HSSP; P93343; 1O9E. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 239 14-3-3 protein 1. FT /FTId=PRO_0000058657. SQ SEQUENCE 239 AA; 27338 MW; 6BDE1496C8428FFC CRC64; MASREDCVYT AKLAEQSERY DEMVQCMKQV AEMEAELSIE ERNLLSVAYK NVIGAKRASW RIISSLEQKE QAKGNDKHVE IIKGYRAKIE KELSTCCDDV LKVIQENLLP KASTSESKVF FKKMEGDYYR YFAEFTVDEK RKEVADKSLA AYTEATEISN AELAPTHPIR LGLALNFSVF YFEIMNDADK ACQLAKQAFD DAIAKLDEVP ENMYKDSTLI MQLLRDNLTL WTSDACDEE // ID 14331_MAIZE Reviewed; 261 AA. AC P49106; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 09-JAN-2007, entry version 36. DE 14-3-3-like protein GF14-6. GN Name=GRF1; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95148741; PubMed=7846163; DOI=10.1104/pp.106.4.1593; RA de Vetten N.C., Ferl R.J.; RT "Two genes encoding GF14 (14-3-3) proteins in Zea mays. Structure, RT expression, and potential regulation by the G-box binding complex."; RL Plant Physiol. 106:1593-1604(1994). CC -!- FUNCTION: Is associated with a DNA binding complex to bind to the CC G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SIMILARITY: Belongs to the 14-3-3 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; S77133; AAB33304.1; -; Genomic_DNA. DR PIR; T01752; T01752. DR HSSP; P93343; 1O9E. DR SMR; P49106; 7-239. DR Gramene; P49106; -. DR MaizeGDB; 65832; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 261 14-3-3-like protein GF14-6. FT /FTId=PRO_0000058691. SQ SEQUENCE 261 AA; 29662 MW; 25EC70725A5F6801 CRC64; MASAELSREE NVYMAKLAEQ AERYEEMVEF MEKVAKTVDS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEEGRG NEDRVTLIKD YRGKIETELT KICDGILKLL ETHLVPSSTA PESKVFYLKM KGDYYRYLAE FKTGAERKDA AENTMVAYKA AQDIALAELA PTHPIRLGLA LNFSVFYYEI LNSPDRACSL AKQAFDEAIS ELDTLSEESY KDSTLIMQLL RDNLTLWTSD ISEDPAEEIR EAPKRDSSEG Q // ID 14331_ORYSA Reviewed; 264 AA. AC Q84J55; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 28-NOV-2006, entry version 19. DE 14-3-3-like protein GF14-A (G-box factor 14-3-3 homolog A). GN Name=GF14A; OrderedLocusNames=Os08g0480800, LOC_Os08g37490; GN ORFNames=OJ1113_A10.40, OSJNBb0092C08.10; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=23111120; PubMed=14750518; RX DOI=10.1023/B:PLAN.0000007001.30865.0f; RA Cooper B., Hutchison D., Park S., Guimil S., Luginbuehl P., Ellero C., RA Goff S.A., Glazebrook J.; RT "Identification of rice (Oryza sativa) proteins linked to the cyclin- RT mediated regulation of the cell cycle."; RL Plant Mol. Biol. 53:273-279(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=22584437; PubMed=12684538; DOI=10.1073/pnas.0737574100; RA Cooper B., Clarke J.D., Budworth P., Kreps J., Hutchison D., Park S., RA Guimil S., Dunn M., Luginbuehl P., Ellero C., Goff S.A., RA Glazebrook J.; RT "A network of rice genes associated with stress response and seed RT development."; RL Proc. Natl. Acad. Sci. U.S.A. 100:4945-4950(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RG The international rice genome sequencing project (IRGSP) consortium; RT "Oryza sativa nipponbare chromosome 8 genomic DNA sequence."; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NOMENCLATURE. RX PubMed=16766513; DOI=10.1093/dnares/dsl001; RA Chen F., Li Q., Sun L., He Z.; RT "The rice 14-3-3 gene family and its involvement in responses to RT biotic and abiotic stress."; RL DNA Res. 13:53-63(2006). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AY224524; AAO72644.1; -; mRNA. DR EMBL; AY224434; AAO72553.1; -; mRNA. DR EMBL; AP004643; BAD09765.1; -; Genomic_DNA. DR EMBL; AP005391; BAD10275.1; -; Genomic_DNA. DR UniGene; Os.18498; -. DR HSSP; P93343; 1O9E. DR Gramene; Q84J55; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 264 14-3-3-like protein GF14-A. FT /FTId=PRO_0000246063. SQ SEQUENCE 264 AA; 29001 MW; F4094830FEF61600 CRC64; MAAAAGGGTR EEMVYMAKLA EQAERYEEMV EFMEKVVTAA AAGGGGELTV EERNLLSVAY KNVIGARRAS WRIVSSIEQK EEGRGAAGHA AAARSYRARV EAELSNICAG ILRLLDERLV PAAAAVDAKV FYLKMKGDYH RYLAEFKTGA ERKDAADATL AAYQAAQDIA MKELSPTHPI RLGLALNFSV FYYEILNSPD RACTLAKQAF DEAISELDTL GEESYKDSTL IMQLLRDNLT LWTSDMQDDG GDEMRDATKP EDEH // ID 14331_SCHMA Reviewed; 252 AA. AC Q26540; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 28-NOV-2006, entry version 30. DE 14-3-3 protein homolog 1. OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida; OC Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Puerto Rican; RX MEDLINE=96123403; PubMed=8577340; DOI=10.1016/0166-6851(95)00116-I; RA Schechtman D., Ram D., Tarrab-Hazdai R., Arnon R., Schechter I.; RT "Stage-specific expression of the mRNA encoding a 14-3-3 protein RT during the life cycle of Schistosoma mansoni."; RL Mol. Biochem. Parasitol. 73:275-278(1995). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U24281; AAC46983.1; -; mRNA. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 252 14-3-3 protein homolog 1. FT /FTId=PRO_0000058661. SQ SEQUENCE 252 AA; 28372 MW; 39103EB5B71A2C08 CRC64; MTTSWVLQSK DLSNTDLVHI AKLAEQAERY DDMAAAMKRY TEASGNLGNE ERNLLSVAYK NVVGARRSAW RVIHGSEMKA VNDRTKKQIA EEYRIKMEKE LNTICNQVLA LLEDYLLPNA SPDDSKVFFL KMQGDYYRYL AEVATDDART EVVQKSLDAY TKATTAAENL PTTHPIRLGL ALNFSVFFYE IQNDAAKACE LAKSAFDSAI AELDQLQDDS YKDSTLIMQL LRDNLTLWAS DQTAEGDVEN DS // ID 14331_SOLLC Reviewed; 249 AA. AC P93206; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 28-NOV-2006, entry version 37. DE 14-3-3 protein 1. GN Name=TFT1; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RX MEDLINE=99214454; PubMed=10198082; DOI=10.1104/pp.119.4.1243; RA Roberts M.R., Bowles D.J.; RT "Fusicoccin, 14-3-3 proteins, and defense responses in tomato RT plants."; RL Plant Physiol. 119:1243-1250(1999). RN [2] RP SEQUENCE REVISION TO 17-18 AND 169-170. RA Roberts M.R.; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Homodimer (Potential). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X95900; CAA65145.2; -; Genomic_DNA. DR HSSP; P93343; 1O9E. DR SMR; P93206; 9-240. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 249 14-3-3 protein 1. FT /FTId=PRO_0000058681. SQ SEQUENCE 249 AA; 28219 MW; 12BF2B1926F61021 CRC64; MALPENLTRE QCLYLAKLAE QAERYEEMVK FMDKLVIGSG SSELTVEERN LLSVAYKNVI GSLRAAWRIV SSIEQKEEGR KNDEHVVLVK DYRSKVESEL SDVCAGILKI LDQYLIPSAS AGESKVFYLK MKGDYYRYLA EFKVGNERKE AAEDTMLAYK AAQDIAVAEL APTHPIRLGL ALNFSVFYYE ILNASEKACS MAKQAFEEAI AELDTMGEES YKDSTLIMQL LRDNLTLWTS DMQEQMDEA // ID 14331_SOLTU Reviewed; 259 AA. AC Q41418; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 28-NOV-2006, entry version 28. DE 14-3-3-like protein. OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Desiree; RA Wilczynski G., Szopa J.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. CC -!- TISSUE SPECIFICITY: Leaves specific. CC -!- SIMILARITY: Belongs to the 14-3-3 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; X97724; CAA66309.1; -; mRNA. DR HSSP; P93343; 1O9E. DR SMR; Q41418; 4-236. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 259 14-3-3-like protein. FT /FTId=PRO_0000058698. SQ SEQUENCE 259 AA; 29395 MW; 808C13F2E69498E5 CRC64; MADSREENVY MAKLAEQAER YEEMVEFMEK VAKVDVEELT VEERNLLSVA YKNVIGARRA SWRIISSIEQ KEESRGNEDH VSSIKEYRVK IEAELSKICD GILSLLESHL VPSASTAESK VFYLKMKGDY HRYLAEFKTG ARERKEAAEN TLLAYKSAQD IALAELTPTH PIRLGLALNF SVFYYEILNS PDRACNLAKQ AFDDAIAELD TLGEESYKDS TLIMQLLRDN LTLWTSDTTD DAEDEIREGS KQESGDGQQ // ID 14332_ARATH Reviewed; 259 AA. AC Q01525; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 23-JAN-2007, entry version 55. DE 14-3-3-like protein GF14 omega (General regulatory factor 2). GN Name=GRF2; Synonyms=GF14; OrderedLocusNames=At1g78300; GN ORFNames=F3F9.16; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=93087554; PubMed=1454838; RA Lu G., Delisle A.J., de Vetten N.C., Ferl R.J.; RT "Brain proteins in plants: an Arabidopsis homolog to neurotransmitter RT pathway activators is part of a DNA binding complex."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11490-11494(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=95175611; PubMed=7870824; DOI=10.1104/pp.107.1.283; RA Rooney M.F., Ferl R.J.; RT "Sequences of three Arabidopsis general regulatory factor genes RT encoding GF14 (14-3-3) proteins."; RL Plant Physiol. 107:283-284(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SIMILARITY: Belongs to the 14-3-3 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; M96855; AAA32798.1; -; mRNA. DR EMBL; U09376; AAA96253.1; -; Genomic_DNA. DR EMBL; AC013430; AAF71808.1; -; Genomic_DNA. DR EMBL; AF462807; AAL58901.1; -; mRNA. DR EMBL; AY077667; AAL76145.1; -; mRNA. DR EMBL; AY086467; AAM67316.1; -; mRNA. DR PIR; A47237; A47237. DR UniGene; At.23337; -. DR HSSP; P93343; 1O9E. DR SMR; Q01525; 3-236. DR TRANSFAC; T04365; -. DR GenomeReviews; CT485782_GR; AT1G78300. DR KEGG; ath:At1g78300; -. DR TAIR; At1g78300; -. DR ArrayExpress; Q01525; -. DR GermOnline; AT1G78300; Arabidopsis thaliana. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 259 14-3-3-like protein GF14 omega. FT /FTId=PRO_0000058664. FT CONFLICT 8 8 F -> L (in Ref. 2). SQ SEQUENCE 259 AA; 29162 MW; 9CCE5043A707918A CRC64; MASGREEFVY MAKLAEQAER YEEMVEFMEK VSAAVDGDEL TVEERNLLSV AYKNVIGARR ASWRIISSIE QKEESRGNDD HVTAIREYRS KIETELSGIC DGILKLLDSR LIPAAASGDS KVFYLKMKGD YHRYLAEFKT GQERKDAAEH TLAAYKSAQD IANAELAPTH PIRLGLALNF SVFYYEILNS PDRACNLAKQ AFDEAIAELD TLGEESYKDS TLIMQLLRDN LTLWTSDMQD DAADEIKEAA APKPTEEQQ // ID 14332_CAEEL Reviewed; 248 AA. AC Q20655; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 12-DEC-2006, entry version 34. DE 14-3-3-like protein 2. GN Name=ftt-2; ORFNames=F52D10.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [2] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DAF-16 RP AND SIR-2.1, AND SUBCELLULAR LOCATION. RX PubMed=16777605; DOI=10.1016/j.cell.2006.04.036; RA Berdichevsky A., Viswanathan M., Horvitz H.R., Guarente L.; RT "C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 RT and extend life span."; RL Cell 125:1165-1177(2006). CC -!- FUNCTION: Required for extension of life-span by sir-2.1. CC -!- SUBUNIT: Interacts with daf-16 and sir-2.1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- SIMILARITY: Belongs to the 14-3-3 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; Z66564; CAA91474.1; -; Genomic_DNA. DR PIR; T22500; T22500. DR UniGene; Cel.17467; -. DR HSSP; P93343; 1O9E. DR SMR; Q20655; 5-233. DR DIP; DIP:25505N; -. DR IntAct; Q20655; -. DR Ensembl; F52D10.3; Caenorhabditis elegans. DR KEGG; cel:F52D10.3a; -. DR WormBase; WBGene00001502; ftt-2. DR WormPep; F52D10.3; CE03389. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Complete proteome; Nuclear protein. FT CHAIN 1 248 14-3-3-like protein 2. FT /FTId=PRO_0000058648. SQ SEQUENCE 248 AA; 28067 MW; 566D9CF5DB7A4B96 CRC64; MSDGKEELVN RAKLAEQAER YDDMAASMKK VTELGAELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TEGSEKKQQM AKEYREKVEK ELRDICQDVL NLLDKFLIPK AGAAESKVFY LKMKGDYYRY LAEVASGDDR NSVVEKSQQS YQEAFDIAKD KMQPTHPIRL GLALNFSVFF YEILNAPDKA CQLAKQAFDD AIAELDTLNE DSYKDSTLIM QLLRDNLTLW TSDAATDDTD ANETEGGN // ID 14332_ECHGR Reviewed; 248 AA. AC Q8MUA4; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 28-NOV-2006, entry version 18. DE 14-3-3 protein homolog 2. OS Echinococcus granulosus. OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Taeniidae; Echinococcus. OX NCBI_TaxID=6210; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=15221462; DOI=10.1007/s00436-004-1147-z; RA Nunes C.P., Zaha A., Gottstein B., Muller N., Siles-Lucas M.; RT "14-3-3 gene characterization and description of a second 14-3-3 RT isoform in both Echinococcus granulosus and E. multilocularis."; RL Parasitol. Res. 93:403-409(2004). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF529418; AAM94863.1; -; mRNA. DR HSSP; P29312; 1A37. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 248 14-3-3 protein homolog 2. FT /FTId=PRO_0000058654. SQ SEQUENCE 248 AA; 27751 MW; B2346C649F6C7421 CRC64; MAAITSWITD SGCKDHASLV SIAKLAEQAE RYEDMAVAMK TIAEMGNELN NEERNLLSVA YKNVVGARRS SWRIMSSIAK KQAGTPLADQ TDIYLKKVEE ELTKICNDVL ALLSKNLITE KIGAEAKIFY YKMMGDYYRY LAEVQEGEQN DKSTEAAEEA YQKATSLAEA ELSVTHPIRL GLALNFSVFY YEIKNMPEKA CSLAKAAFDA AITEVDSIKD ETYKDSTLIM QLLRDNLTLW SSECETDS // ID 14332_ECHMU Reviewed; 248 AA. AC Q8MM75; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 28-NOV-2006, entry version 16. DE 14-3-3 protein homolog 2. OS Echinococcus multilocularis. OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Taeniidae; Echinococcus. OX NCBI_TaxID=6211; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RA Nunes C.P., Zaha A., Gottstein B., Siles-Lucas M.; RT "The 14-3-3 in Echinococcus multilocularis."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF529419; AAM94864.1; -; mRNA. DR EMBL; AF529420; AAM94865.1; -; Genomic_DNA. DR HSSP; P29312; 1A37. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 248 14-3-3 protein homolog 2. FT /FTId=PRO_0000058655. SQ SEQUENCE 248 AA; 27778 MW; 2B346C649F6C7430 CRC64; MAAITSWITD SGCKDHASLV SIAKLAEQAE RYEDMAVAMK TIAEMGNELN NEERNLLSVA YKNVVGARRS SWRIMSSIAK KQAGTPLADQ TDIYLKKVEE ELTKICNDVL ALLSKNLITE KIGAEAKIFY YKMMGDYYRY LAEVQEGEQN DKSTEAAEEA YQKATSLAEA ELSVTHPIRL GLALNFSVFY YEIKNMPEKA CSLAKAAFDA AITEVDSIKD ETYKDSTLIM QLLRDNLTLW NSECETDS // ID 14332_ENTHI Reviewed; 238 AA. AC P42649; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 28-NOV-2006, entry version 28. DE 14-3-3 protein 2 (14-3-3-2). OS Entamoeba histolytica. OC Eukaryota; Entamoebidae; Entamoeba. OX NCBI_TaxID=5759; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=HM-1:IMSS; RA Samuelson J., Shen P., Meckler G., Descoteaux S., Fu H., Lohia A.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U13419; AAA80186.1; -; Genomic_DNA. DR HSSP; P29312; 1A4O. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 238 14-3-3 protein 2. FT /FTId=PRO_0000058658. SQ SEQUENCE 238 AA; 27579 MW; 5F2F8EA3C3BE4976 CRC64; MTSREDLVYL SKLAEQSERY EEMVQYMKQV AEMGTELSVE ERNLISVAYK NVVGSRRASW RIISSLEQKE QAKGNTQRVE LIKTYRAKIE QELSQKCDDV LKIITEFLLK NSTSIESKVF FKKMEGDYYR YYAEFTVDEK RKEVADKSLA AYQEATDTAA SLVPTHPIRL GLALNFSVFY YQIMNDADKA CQLAKEAFDE AIQKLDEVPE ESYKESTLIM QLLRDNLTLW TSDMGDDE // ID 14332_MAIZE Reviewed; 261 AA. AC Q01526; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 20-FEB-2007, entry version 41. DE 14-3-3-like protein GF14-12. GN Name=GRF2; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95148741; PubMed=7846163; DOI=10.1104/pp.106.4.1593; RA de Vetten N.C., Ferl R.J.; RT "Two genes encoding GF14 (14-3-3) proteins in Zea mays. Structure, RT expression, and potential regulation by the G-box binding complex."; RL Plant Physiol. 106:1593-1604(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-261. RX MEDLINE=93076113; PubMed=1446170; DOI=10.1105/tpc.4.10.1295; RA de Vetten N.C., Lu G., Ferl R.J.; RT "A maize protein associated with the G-box binding complex has RT homology to brain regulatory proteins."; RL Plant Cell 4:1295-1307(1992). CC -!- FUNCTION: Is associated with a DNA binding complex to bind to the CC G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SIMILARITY: Belongs to the 14-3-3 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; S77135; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M96856; AAA33505.1; -; mRNA. DR PIR; JQ1680; JQ1680. DR UniGene; Zm.20117; -. DR HSSP; P29312; 1A4O. DR SMR; Q01526; 7-239. DR TRANSFAC; T04134; -. DR Gramene; Q01526; -. DR MaizeGDB; 65832; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 261 14-3-3-like protein GF14-12. FT /FTId=PRO_0000058692. SQ SEQUENCE 261 AA; 29636 MW; DE7B707538BA1662 CRC64; MASAELSREE NVYMAKLAEQ AERYEEMVEF MEKVAKTVDS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEEGRG NEDRVTLIKD YRGKIETELT KICDGILKLL ESHLVPSSTA PESKVFYLKM KGDYYRYLAE FKTGAERKDA AENTMVAYKA AQDIALAELA PTHPIRLGLA LNFSVFYYEI LNSPDRACSL AKQAFDEAIS ELDTLSEESY KDSTLIMQLL HDNLTLWTSD ISEDPAEEIR EAPKHDLSEG Q // ID 14332_ORYSA Reviewed; 262 AA. AC Q7XTE8; O24221; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2004, sequence version 2. DT 28-NOV-2006, entry version 18. DE 14-3-3-like protein GF14-B (G-box factor 14-3-3 homolog B). GN Name=GF14B; OrderedLocusNames=Os04g0462500, LOC_Os04g38870; GN ORFNames=B0812A04.1, B1358B12.12, OSJNBa0072F16.20; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=cv. Japonica / Nipponbare; TISSUE=Embryo; RX PubMed=9596641; DOI=10.1105/tpc.10.5.837; RA Schultz T.F., Medina J., Hill A., Quatrano R.S.; RT "14-3-3 proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) RT response complex in the Em promoter and interact with VP1 and EmBP1."; RL Plant Cell 10:837-847(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=22337377; PubMed=12447439; DOI=10.1038/nature01183; RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., RA Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., RA Weng Q., Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., RA Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., RA Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., RA Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y., RA Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W., RA Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W., RA Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y., RA Han B.; RT "Sequence and analysis of rice chromosome 4."; RL Nature 420:316-320(2002). RN [3] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND NOMENCLATURE. RX PubMed=16766513; DOI=10.1093/dnares/dsl001; RA Chen F., Li Q., Sun L., He Z.; RT "The rice 14-3-3 gene family and its involvement in responses to RT biotic and abiotic stress."; RL DNA Res. 13:53-63(2006). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SUBUNIT: May form a complex with the transcriptional activator VP1 CC and the bZIP transcription factor EMBP1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in seedlings and roots. CC -!- INDUCTION: By wounding, drought and salt stresses, CC benzothiadiazole (BTH), ethephon, hydrogen peroxide, abscisic acid CC (ABA) and incompatible and compatible races of rice blast fungus CC (M.grisea) and rice bacterial blight (X.oryzae). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U65956; AAB07456.1; -; mRNA. DR EMBL; AL512547; CAH67631.1; -; Genomic_DNA. DR EMBL; AL606460; CAE01538.2; -; Genomic_DNA. DR EMBL; BX842605; CAE76003.1; -; Genomic_DNA. DR PIR; T04152; T04152. DR UniGene; Os.4837; -. DR HSSP; P93343; 1O9E. DR SMR; Q7XTE8; 8-240. DR TRANSFAC; T04426; -. DR Gramene; Q7XTE8; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Nuclear protein. FT CHAIN 1 262 14-3-3-like protein GF14-B. FT /FTId=PRO_0000246064. SQ SEQUENCE 262 AA; 29864 MW; 739F14BA1BB5E0EA CRC64; MSAQAELSRE ENVYMAKLAE QAERYEEMVE FMEKVAKTVD SEELTVEERN LLSVAYKNVI GARRASWRII SSIEQKEESR GNEDRVTLIK DYRGKIETEL TKICDGILKL LESHLVPSST APESKVFYLK MKGDYYRYLA EFKTGAERKD AAENTMVAYK AAQDIALAEL PPTHPIRLGL ALNFSVFYYE ILNSPDRACN LAKQAFDEAI SELDTLSEES YKDSTLIMQL LRDNLTLWTS DISEDTAEEI REAPKRDSSE GQ // ID 14332_SCHMA Reviewed; 214 AA. AC Q26537; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 28-NOV-2006, entry version 29. DE 14-3-3 protein homolog 2 (14-3-3-2) (Fragment). OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida; OC Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=NMRI; RA Lee K.W., Thakur A., Karim A.M., Loverde P.T.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; L78441; AAB02100.1; -; mRNA. DR HSSP; P93343; 1O9E. DR SMR; Q26537; 4-201. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN <1 214 14-3-3 protein homolog 2. FT /FTId=PRO_0000058662. FT NON_TER 1 1 SQ SEQUENCE 214 AA; 24608 MW; 0B98AEF8CBCC7AD3 CRC64; SNNELTNEER NLLSVAYKNV VGARRSSWRV ISSIEQKTEG SERKQQMAKD YREKIEKELK DICHEVLTLL DKFLIPKATT AESKVFYLKM KGDYYRYLAE VATGDERQKV IEESQRAYND AFDIAKNQMQ PTHPIRLGLA LNFSVFYYEI LNAPDRACHL AKQAFDDAIA ELDTLNEDSY KDSTLIMQLL RDNLTLWTSD TGGDDDANAP DEHQ // ID 14332_SOLLC Reviewed; 254 AA. AC P93208; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 28-NOV-2006, entry version 37. DE 14-3-3 protein 2. GN Name=TFT2; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RX MEDLINE=99214454; PubMed=10198082; DOI=10.1104/pp.119.4.1243; RA Roberts M.R., Bowles D.J.; RT "Fusicoccin, 14-3-3 proteins, and defense responses in tomato RT plants."; RL Plant Physiol. 119:1243-1250(1999). RN [2] RP SEQUENCE REVISION TO 11-12 AND 58-60. RA Roberts M.R.; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Homodimer (Potential). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X95901; CAA65146.2; -; Genomic_DNA. DR HSSP; P93343; 1O9E. DR SMR; P93208; 2-234. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 254 14-3-3 protein 2. FT /FTId=PRO_0000058682. SQ SEQUENCE 254 AA; 28879 MW; 98101E64DFD961C6 CRC64; MAREENVYMA KLAEQAERYE EMVQFMEKVS TSLGSEELTV EERNLLSVAY KNVIGARRAS WRIISSIEQK EESRGNEEHV KCIKEYRSKI ESELSDICDG ILKLLDSNLI PSASNGDSKV FYLKMKGDYH RYLAEFKTGA ERKEAAESTL SAYKAAQDIA NTELAPTHPI RLGLALNFSV FYYEILNSPD RACNLAKQAF DEAIAELDTL GEESYKDSTL IMQLLRDNLT LWTSDMQDDG ADEIKETKND NEQQ // ID 14332_SOLTU Reviewed; 254 AA. AC Q43643; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 28-NOV-2006, entry version 30. DE 14-3-3-like protein RA215. OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Desiree; TISSUE=Root; RA Wilczynski G., Szopa J.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; X87370; CAA60800.1; -; mRNA. DR PIR; S55375; S55375. DR HSSP; P93343; 1O9E. DR SMR; Q43643; 3-235. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 254 14-3-3-like protein RA215. FT /FTId=PRO_0000058699. SQ SEQUENCE 254 AA; 28595 MW; 5C52EC19BE1D742E CRC64; MASPREENVY MANVAARAER YEEMVEFMEK VVAALDTELT VEERNLLSVA YKNVIGARRA SWRIISSIEQ KEESRGNEDH VASIKKYRSQ IENELTSICN GILKLLDSKL IGSAATGDSK VFYLKMKGDY YRYLAEFKTG TERKEAAENT LSAYKSAQDI ANGELAPTHP IRLGLALNFS VFYYEILNSP DRACNLAKQA FDEAIADVDT LGEESYKDST LIMQLLRDNL TLWTSDMQDD GADEIKEPSK ADNE // ID 14333_ARATH Reviewed; 255 AA. AC P42644; Q945L2; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 20-FEB-2007, entry version 47. DE 14-3-3-like protein GF14 psi (General regulatory factor 3) (14-3-3- DE like protein RCI1). GN Name=GRF3; Synonyms=RCI1; OrderedLocusNames=At5g38480; GN ORFNames=MXI10.21; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=95062733; PubMed=7972511; DOI=10.1104/pp.105.4.1459; RA Lu G., Rooney M.F., Wu K., Ferl R.J.; RT "Five cDNAs encoding Arabidopsis GF14 proteins."; RL Plant Physiol. 105:1459-1460(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94339482; PubMed=7520301; RA Jarillo J.A., Capel J., Leyva A., Martinez Zapater J.M., Salinas J.; RT "Two related low-temperature-inducible genes of Arabidopsis encode RT proteins showing high homology to 14-3-3 proteins, a family of RT putative kinase regulators."; RL Plant Mol. Biol. 25:693-704(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=95175611; PubMed=7870824; DOI=10.1104/pp.107.1.283; RA Rooney M.F., Ferl R.J.; RT "Sequences of three Arabidopsis general regulatory factor genes RT encoding GF14 (14-3-3) proteins."; RL Plant Physiol. 107:283-284(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=97471969; PubMed=9330910; DOI=10.1093/dnares/4.3.215; RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., RA Miyajima N., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence RT features of the 1.6 Mb regions covered by twenty physically assigned RT P1 clones."; RL DNA Res. 4:215-230(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- INDUCTION: By cold. CC -!- SIMILARITY: Belongs to the 14-3-3 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; L09110; AAA32799.1; -; mRNA. DR EMBL; X74140; CAA52237.1; -; mRNA. DR EMBL; U09375; AAA96252.1; -; Genomic_DNA. DR EMBL; AB005231; BAB10138.1; -; Genomic_DNA. DR EMBL; AB005248; BAB10138.1; JOINED; Genomic_DNA. DR EMBL; AF412093; AAL06546.1; -; mRNA. DR EMBL; AY093976; AAM16237.1; -; mRNA. DR EMBL; AK226217; BAE98382.1; -; mRNA. DR EMBL; AK228478; BAF00404.1; -; mRNA. DR PIR; S47969; S47969. DR PIR; S57277; S57277. DR UniGene; At.22344; -. DR HSSP; P93343; 1O9E. DR SMR; P42644; 2-235. DR GenomeReviews; BA000015_GR; AT5G38480. DR TAIR; At5g38480; -. DR ArrayExpress; P42644; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 255 14-3-3-like protein GF14 psi. FT /FTId=PRO_0000058665. FT CONFLICT 90 90 K -> E (in Ref. 1 and 3). SQ SEQUENCE 255 AA; 28606 MW; 51E018F146ED2A0F CRC64; MSTREENVYM AKLAEQAERY EEMVEFMEKV AKTVDVEELS VEERNLLSVA YKNVIGARRA SWRIISSIEQ KEESKGNEDH VAIIKDYRGK IESELSKICD GILNVLEAHL IPSASPAESK VFYLKMKGDY HRYLAEFKAG AERKEAAEST LVAYKSASDI ATAELAPTHP IRLGLALNFS VFYYEILNSP DRACSLAKQA FDDAIAELDT LGEESYKDST LIMQLLRDNL TLWTSDMTDE AGDEIKEASK PDGAE // ID 14333_ENTHI Reviewed; 236 AA. AC P42650; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 28-NOV-2006, entry version 29. DE 14-3-3 protein 3 (14-3-3-3) (Fragment). OS Entamoeba histolytica. OC Eukaryota; Entamoebidae; Entamoeba. OX NCBI_TaxID=5759; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=HM-1:IMSS; RA Samuelson J., Shen P., Meckler G., Descoteaux S., Fu H., Lohia A.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U13420; AAA80187.1; -; mRNA. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN <1 236 14-3-3 protein 3. FT /FTId=PRO_0000058659. FT NON_TER 1 1 SQ SEQUENCE 236 AA; 27055 MW; CC7D9958AD1BB46D CRC64; SEDCVFLSKL AEQSERYDEM VQYMKQVAAL NTELSVEERN LLSVAYKNVI GSRRASWRII TSLEQKEQAK GNDKHVEIIK GYRAKIEDEL AKYCDDVLKV IKENLLPNAS TSESKVFYKK MEGDYYRYYA EFTVDEKRQE VADKSLAAYT EATEISNADL APTHPIRLGL ALNFSVFYYE IMNDADKACQ LAKQAFDDSI AKLDEVPESS YKDSTLIMQL LRDNLTLWTS DTADEE // ID 14333_ORYSA Reviewed; 256 AA. AC Q6ZKC0; O24222; Q8W1B7; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-NOV-2006, entry version 14. DE 14-3-3-like protein GF14-C (G-box factor 14-3-3 homolog C). GN Name=GF14C; OrderedLocusNames=Os08g0430500, LOC_Os08g33370; GN ORFNames=OJ1124_B05.7; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=cv. Japonica / Nipponbare; TISSUE=Embryo; RX PubMed=9596641; DOI=10.1105/tpc.10.5.837; RA Schultz T.F., Medina J., Hill A., Quatrano R.S.; RT "14-3-3 proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) RT response complex in the Em promoter and interact with VP1 and EmBP1."; RL Plant Cell 10:837-847(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RG The international rice genome sequencing project (IRGSP) consortium; RT "Oryza sativa nipponbare chromosome 8 genomic DNA sequence."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 83-169. RC STRAIN=cv. Japonica / Stejaree45; RA Lee D.-S., Hur Y.; RT "Expression and regulation of genes involved in carbohydrate RT metabolism in rice."; RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND NOMENCLATURE. RX PubMed=16766513; DOI=10.1093/dnares/dsl001; RA Chen F., Li Q., Sun L., He Z.; RT "The rice 14-3-3 gene family and its involvement in responses to RT biotic and abiotic stress."; RL DNA Res. 13:53-63(2006). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SUBUNIT: May form a complex with the transcriptional activator VP1 CC and the bZIP transcription factor EMBP1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in seedlings, internodes and CC panicles. CC -!- INDUCTION: By wounding, drought and salt stresses, CC benzothiadiazole (BTH), ethephon, methyl jasmonate (MeJa), CC hydrogen peroxide, abscisic acid (ABA) and incompatible and CC compatible races of rice blast fungus (M.grisea) and rice CC bacterial blight (X.oryzae). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U65957; AAB07457.1; -; mRNA. DR EMBL; AP003881; BAD01170.1; -; Genomic_DNA. DR EMBL; AF451190; AAL47850.1; -; mRNA. DR PIR; T04153; T04153. DR UniGene; Os.6323; -. DR HSSP; P93343; 1O9E. DR SMR; Q6ZKC0; 2-234. DR TRANSFAC; T04427; -. DR Gramene; Q6ZKC0; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Nuclear protein. FT CHAIN 1 256 14-3-3-like protein GF14-C. FT /FTId=PRO_0000246065. SQ SEQUENCE 256 AA; 28827 MW; E8B1D9A3ECB4C70D CRC64; MSREENVYMA KLAEQAERYE EMVEYMEKVA KTVDVEELTV EERNLLSVAY KNVIGARRAS WRIVSSIEQK EEGRGNEEHV TLIKEYRGKI EAELSKICDG ILKLLDSHLV PSSTAAESKV FYLKMKGDYH RYLAEFKTGA ERKEAAESTM VAYKAAQDIA LADLAPTHPI RLGLALNFSV FYYEILNSPD KACNLAKQAF DEAISELDTL GEESYKDSTL IMQLLRDNLT LWTSDLTEDG GDEVKEASKG DACEGQ // ID 14333_SOLLC Reviewed; 260 AA. AC P93209; P42651; Q9SCA7; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 20-FEB-2007, entry version 41. DE 14-3-3 protein 3 (PBLT3). GN Name=TFT3; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RX MEDLINE=99214454; PubMed=10198082; DOI=10.1104/pp.119.4.1243; RA Roberts M.R., Bowles D.J.; RT "Fusicoccin, 14-3-3 proteins, and defense responses in tomato RT plants."; RL Plant Physiol. 119:1243-1250(1999). RN [2] RP NUCLEOTIDE SEQUENCE OF 11-240. RC STRAIN=cv. West Virginia 106; TISSUE=Fruit; RA Lemaire-Chamley M., Petit J., Causse M., Raymond P., Chevalier C.; RT "Isolation and characterization of cDNAs expressed during early RT development of tomato fruit by mRNA differential display."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-260. RC STRAIN=cv. Ailsa Craig; TISSUE=Fruit; RX MEDLINE=95359205; PubMed=7632735; DOI=10.1016/0167-4781(95)00092-U; RA Laughner B., Lawrence S.D., Ferl R.J.; RT "Two cDNA clones encoding 14-3-3 homologs from tomato fruit."; RL Biochim. Biophys. Acta 1263:67-70(1995). CC -!- SUBUNIT: Homodimer (Potential). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X95902; CAA65147.1; -; Genomic_DNA. DR EMBL; AJ270959; CAB65693.1; -; mRNA. DR EMBL; L29151; AAA99430.1; ALT_INIT; mRNA. DR PIR; S57271; S57271. DR PIR; T07388; T07388. DR UniGene; Les.10651; -. DR HSSP; P93343; 1O9E. DR SMR; P93209; 6-240. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 260 14-3-3 protein 3. FT /FTId=PRO_0000058683. FT CONFLICT 73 73 I -> V (in Ref. 3). FT CONFLICT 158 158 A -> G (in Ref. 3). SQ SEQUENCE 260 AA; 29305 MW; 2AE0C3E877BBD081 CRC64; MAVVAPTARE ENVYMAKLAD RAESDEEMVE FMEKVSNSLG SEELTVEERN LLSVAYKNVI GARRASWRII SSIEQKEESR GNEEHVNSIR EYRSKIENEL SKICDGILKL LDSKLIPSAT SGDSKVFYLK MKGDYHRYLA EFKTGAERKE AAESTLTAYK AAQDIASAEL APTHPIRLGL ALNFSVFYYE ILNSPDRACN LAKQAFDEAI AELDTLGEES YKDSTLIMQL LRDNLTLWTS DMQDDGADEI KEDPKPEEKN // ID 14334_ARATH Reviewed; 267 AA. AC P46077; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 23-JAN-2007, entry version 46. DE 14-3-3-like protein GF14 phi (General regulatory factor 4). GN Name=GRF4; OrderedLocusNames=At1g35160; ORFNames=T32G9.30; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=95062733; PubMed=7972511; DOI=10.1104/pp.105.4.1459; RA Lu G., Rooney M.F., Wu K., Ferl R.J.; RT "Five cDNAs encoding Arabidopsis GF14 proteins."; RL Plant Physiol. 105:1459-1460(1994). RN [2] RP SEQUENCE REVISION TO 23 AND 245. RA Ferl R.J.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=97422888; PubMed=9276953; DOI=10.1104/pp.114.4.1421; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SIMILARITY: Belongs to the 14-3-3 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; L09111; AAB06231.1; -; mRNA. DR EMBL; AF001414; AAB62224.1; -; Genomic_DNA. DR EMBL; AC079605; AAG50610.1; -; Genomic_DNA. DR EMBL; AY084342; AAM60925.1; -; mRNA. DR PIR; C86472; C86472. DR UniGene; At.22949; -. DR HSSP; P93343; 1O9E. DR SMR; P46077; 9-242. DR GenomeReviews; CT485782_GR; AT1G35160. DR TAIR; At1g35160; -. DR GermOnline; AT1G35160; Arabidopsis thaliana. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 267 14-3-3-like protein GF14 phi. FT /FTId=PRO_0000058666. SQ SEQUENCE 267 AA; 30194 MW; 18FA010F752CC134 CRC64; MAAPPASSSA REEFVYLAKL AEQAERYEEM VEFMEKVAEA VDKDELTVEE RNLLSVAYKN VIGARRASWR IISSIEQKEE SRGNDDHVTT IRDYRSKIES ELSKICDGIL KLLDTRLVPA SANGDSKVFY LKMKGDYHRY LAEFKTGQER KDAAEHTLTA YKAAQDIANA ELAPTHPIRL GLALNFSVFY YEILNSPDRA CNLAKQAFDE AIAELDTLGE ESYKDSTLIM QLLRDNLTLW TSDMQDESPE EIKEAAAPKP AEEQKEI // ID 14334_ORYSA Reviewed; 265 AA. AC Q2R2W2; O24223; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 28-NOV-2006, entry version 13. DE 14-3-3-like protein GF14-D (G-box factor 14-3-3 homolog D). GN Name=GF14D; OrderedLocusNames=Os11g0546900, LOC_Os11g34450; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Japonica / Nipponbare; TISSUE=Embryo; RX PubMed=9596641; DOI=10.1105/tpc.10.5.837; RA Schultz T.F., Medina J., Hill A., Quatrano R.S.; RT "14-3-3 proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) RT response complex in the Em promoter and interact with VP1 and EmBP1."; RL Plant Cell 10:837-847(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RX PubMed=16188032; DOI=10.1186/1741-7007-3-20; RG The rice chromosomes 11 and 12 sequencing consortia; RT "The sequence of rice chromosomes 11 and 12, rich in disease RT resistance genes and recent gene duplications."; RL BMC Biol. 3:20-20(2005). RN [3] RP NOMENCLATURE. RX PubMed=16766513; DOI=10.1093/dnares/dsl001; RA Chen F., Li Q., Sun L., He Z.; RT "The rice 14-3-3 gene family and its involvement in responses to RT biotic and abiotic stress."; RL DNA Res. 13:53-63(2006). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U65958; AAB07458.1; -; mRNA. DR EMBL; DP000010; ABA94230.1; -; Genomic_DNA. DR PIR; T04154; T04154. DR HSSP; P93343; 1O9E. DR SMR; Q2R2W2; 8-243. DR Gramene; Q2R2W2; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 265 14-3-3-like protein GF14-D. FT /FTId=PRO_0000246066. SQ SEQUENCE 265 AA; 29262 MW; 2567FCB5E9177D69 CRC64; MSPAEPTREE SVYKAKLAEQ AERYEEMVEY MERVARAAGG ASGGEELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE EGRGNDAHAA TIRSYRGKIE AELARICDGI LALLDSHLVP SAGAAESKVF YLKMKGDYHR YLAEFKSGDE RKQAAESTMN AYKAAQDIAL ADLAPTHPIR LGLALNFSVF YYEILNSPDR ACNLAKQAFD EAISELDSLG EESYKDSTLI MQLLRDNLTL WTSDANDDGG DEIKEAAAPK EPGDQ // ID 14334_SOLLC Reviewed; 260 AA. AC P42652; Q8L5E2; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-FEB-2007, entry version 41. DE 14-3-3 protein 4 (PBLT4). GN Name=TFT4; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Ailsa Craig; TISSUE=Fruit; RX MEDLINE=95359205; PubMed=7632735; DOI=10.1016/0167-4781(95)00092-U; RA Laughner B., Lawrence S.D., Ferl R.J.; RT "Two cDNA clones encoding 14-3-3 homologs from tomato fruit."; RL Biochim. Biophys. Acta 1263:67-70(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RX MEDLINE=99214454; PubMed=10198082; DOI=10.1104/pp.119.4.1243; RA Roberts M.R., Bowles D.J.; RT "Fusicoccin, 14-3-3 proteins, and defense responses in tomato RT plants."; RL Plant Physiol. 119:1243-1250(1999). CC -!- SUBUNIT: Homodimer (Potential). CC -!- SIMILARITY: Belongs to the 14-3-3 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; L29150; AAA99431.1; -; mRNA. DR EMBL; AJ504807; CAD43308.1; -; mRNA. DR PIR; S57272; S57272. DR UniGene; Les.2473; -. DR HSSP; P93343; 1O9E. DR SMR; P42652; 4-237. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 260 14-3-3 protein 4. FT /FTId=PRO_0000058684. FT CONFLICT 96 96 D -> E (in Ref. 2). FT CONFLICT 125 125 H -> Y (in Ref. 2). SQ SEQUENCE 260 AA; 29299 MW; 955E5BE81765CBB9 CRC64; MADSSREENV YLAKLAEQAE RYEEMIEFME KVAKTADVEE LTVEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVNTIKEYR SKIEADLSKI CDGILSLLES NLIPSASTAE SKVFHLKMKG DYHRYLAEFK TGTERKEAAE NTLLAYKSAQ DIALAELAPT HPIRLGLALN FSVFYYEILN SPDRACNLAK QAFDEAISEL DTLGEESYKD STLIMQLLRD NLTLWTSDNA DDVGDDIKEA SKPESGEGQQ // ID 14335_ARATH Reviewed; 268 AA. AC P42645; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 23-JAN-2007, entry version 50. DE 14-3-3-like protein GF14 upsilon (General regulatory factor 5). GN Name=GRF5; OrderedLocusNames=At5g16050; ORFNames=F1N13_190; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Columbia; RX MEDLINE=95062733; PubMed=7972511; DOI=10.1104/pp.105.4.1459; RA Lu G., Rooney M.F., Wu K., Ferl R.J.; RT "Five cDNAs encoding Arabidopsis GF14 proteins."; RL Plant Physiol. 105:1459-1460(1994). RN [2] RP SEQUENCE REVISION TO 73; 182 AND C-TERMINUS. RA Ferl R.J., Lu G.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=97422888; PubMed=9276953; DOI=10.1104/pp.114.4.1421; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016721; PubMed=11130714; DOI=10.1038/35048507; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SIMILARITY: Belongs to the 14-3-3 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; L09109; AAB06585.1; -; mRNA. DR EMBL; AF001415; AAB62225.1; -; Genomic_DNA. DR EMBL; AL391145; CAC01804.1; -; Genomic_DNA. DR EMBL; AY035170; AAK59674.1; -; mRNA. DR EMBL; AY059115; AAL15221.1; -; mRNA. DR PIR; T51388; T51388. DR UniGene; At.25563; -. DR HSSP; P93343; 1O9E. DR SMR; P42645; 5-238. DR GenomeReviews; BA000015_GR; AT5G16050. DR KEGG; ath:At5g16050; -. DR TAIR; At5g16050; -. DR ArrayExpress; P42645; -. DR GermOnline; AT5G16050; Arabidopsis thaliana. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 268 14-3-3-like protein GF14 upsilon. FT /FTId=PRO_0000058667. SQ SEQUENCE 268 AA; 30182 MW; ECB35B7E53F688FF CRC64; MSSDSSREEN VYLAKLAEQA ERYEEMVEFM EKVAKTVETE ELTVEERNLL SVAYKNVIGA RRASWRIISS IEQKEDSRGN SDHVSIIKDY RGKIETELSK ICDGILNLLE AHLIPAASLA ESKVFYLKMK GDYHRYLAEF KTGAERKEAA ESTLVAYKSA QDIALADLAP THPIRLGLAL NFSVFYYEIL NSSDRACSLA KQAFDEAISE LDTLGEESYK DSTLIMQLLR DNLTLWTSDL NDEAGDDIKE APKEVQKVDE QAQPPPSQ // ID 14335_ORYSA Reviewed; 262 AA. AC Q6EUP4; Q9M3X9; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 20-FEB-2007, entry version 13. DE 14-3-3-like protein GF14-E (G-box factor 14-3-3 homolog E). GN Name=GF14E; OrderedLocusNames=Os02g0580300, LOC_Os02g36974; GN ORFNames=B1267B06.30-1, OJ1115_A05.5-1; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Meristem; RA Fabian T., Huss S., Sauter M.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RG The international rice genome sequencing project (IRGSP) consortium; RT "Oryza sativa nipponbare chromosome 2 genomic DNA sequence."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND NOMENCLATURE. RX PubMed=16766513; DOI=10.1093/dnares/dsl001; RA Chen F., Li Q., Sun L., He Z.; RT "The rice 14-3-3 gene family and its involvement in responses to RT biotic and abiotic stress."; RL DNA Res. 13:53-63(2006). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- INDUCTION: By wounding, drought and salt stresses, CC benzothiadiazole (BTH), ethephon, methyl jasmonate (MeJa), CC hydrogen peroxide, abscisic acid (ABA) and incompatible and CC compatible races of rice blast fungus (M.grisea) and rice CC bacterial blight (X.oryzae). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AJ276594; CAB77673.1; -; mRNA. DR EMBL; AP003999; BAD27625.1; -; Genomic_DNA. DR EMBL; AP006161; BAD29578.1; -; Genomic_DNA. DR UniGene; Os.3440; -. DR HSSP; P93343; 1O9E. DR SMR; Q6EUP4; 8-240. DR Gramene; Q6EUP4; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Nuclear protein. FT CHAIN 1 262 14-3-3-like protein GF14-E. FT /FTId=PRO_0000246067. SQ SEQUENCE 262 AA; 29692 MW; 2026F19B5414CF2A CRC64; MSQPAELSRE ENVYMAKLAE QAERYEEMVE FMEKVAKTVD SEELTVEERN LLSVAYKNVI GARRASWRII SSIEQKEESR GNEDRCTLIK EYRGKIETEL SKICDGILKL LDSHLVPSST APESKVFYLK MKGDYYRYLA EFKTGAERKD AAENTMVAYK AAQDIALAEL PPTHPIRLGL ALNFSVFYYE ILNSPDRACN LAKQAFDEAI SELDTLSEES YKDSTLIMQL LRDNLTLWTS DISEDAAEEI KEAPKGESGD GQ // ID 14335_SOLLC Reviewed; 255 AA. AC P93210; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 28-NOV-2006, entry version 36. DE 14-3-3 protein 5. GN Name=TFT5; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RX MEDLINE=99214454; PubMed=10198082; DOI=10.1104/pp.119.4.1243; RA Roberts M.R., Bowles D.J.; RT "Fusicoccin, 14-3-3 proteins, and defense responses in tomato RT plants."; RL Plant Physiol. 119:1243-1250(1999). CC -!- SUBUNIT: Homodimer (Potential). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X95903; CAA65148.1; -; Genomic_DNA. DR HSSP; P93343; 1O9E. DR SMR; P93210; 3-236. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 255 14-3-3 protein 5. FT /FTId=PRO_0000058685. SQ SEQUENCE 255 AA; 28754 MW; 5E6AA7BEF0B9FE93 CRC64; MASPREENVY MANVADEAER YEEMVEFMEK VVAALNGEEL TVEERNLLSV AYKNVIGARR ASWRIISSIE QKEESRGNED HVASIKKYRS QIENELTSIC NGILKLLDSK LIGSAATGDS KVFYLKMKGD YYRYLAEFKT GTERKEAAEN TLSAYKSAQD IANGELAPTH PIRLGLALNF SVFYYEILNS PDRACNLAKQ AFDEAIAELD TLGEESYKDS TLIMQLLRDN LTLWTSDMQD DGTDEIKEPS KADNE // ID 14335_SOLTU Reviewed; 258 AA. AC P93784; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 28-NOV-2006, entry version 30. DE 14-3-3-like protein 16R. OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Desiree; TISSUE=Root; RA Wilczynski G., Szopa J.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; Y11685; CAA72381.1; -; mRNA. DR HSSP; P93343; 1O9E. DR SMR; P93784; 3-237. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 258 14-3-3-like protein 16R. FT /FTId=PRO_0000058700. SQ SEQUENCE 258 AA; 28936 MW; 1F3B3FD3F3F109D0 CRC64; MASPREENVY MAKLAEQAER YEEMVEFMEK VVAAADGAEE LTVEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVASIKEYR SKIESELTSI CNGILKLLDS KLIGSAATGD SKVFYLKMKG DYHRYLAEFK TGAERKEAAE NTLSAYKAAQ DIANAELAPT HPIRLGLALN FSVFYYEILN SPDRACNLAK QAFDEAIAEL DTLGEESYKD STLIMQLLRD NLTLWTSDMQ DDGTDEIKEA APKPDNNE // ID 14336_ARATH Reviewed; 248 AA. AC P48349; P42647; Q9LX97; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 23-JAN-2007, entry version 54. DE 14-3-3-like protein GF14 lambda (General regulatory factor 6) (14-3-3- DE like protein RCI2) (14-3-3-like protein AFT1). GN Name=GRF6; Synonyms=AFT1, RCI2; OrderedLocusNames=At5g10450; GN ORFNames=F12B17_200; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94339482; PubMed=7520301; RA Jarillo J.A., Capel J., Leyva A., Martinez Zapater J.M., Salinas J.; RT "Two related low-temperature-inducible genes of Arabidopsis encode RT proteins showing high homology to 14-3-3 proteins, a family of RT putative kinase regulators."; RL Plant Mol. Biol. 25:693-704(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; TISSUE=Leaf; RX MEDLINE=95234749; PubMed=7718616; DOI=10.1016/0167-4889(95)00006-E; RA Zhang H., Wang J., Hwang I., Goodman H.M.; RT "Isolation and expression of an Arabidopsis 14-3-3-like protein RT gene."; RL Biochim. Biophys. Acta 1266:113-116(1995). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Columbia; RX MEDLINE=97422888; PubMed=9276953; DOI=10.1104/pp.114.4.1421; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Columbia; RA Chung H.-J., Shanker S., Ferl R.J.; RT "Sequences of five Arabidopsis general regulatory factor (GRF) genes RT encoding 14-3-3 proteins."; RL (er) Plant Gene Register PGR99-114. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016721; PubMed=11130714; DOI=10.1038/35048507; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes (By similarity). CC -!- INDUCTION: By cold. CC -!- SIMILARITY: Belongs to the 14-3-3 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; X74141; CAA52238.1; -; mRNA. DR EMBL; U02565; AAA74737.1; -; mRNA. DR EMBL; U68545; AAB08482.1; -; mRNA. DR EMBL; AF145298; AAD51781.1; -; Genomic_DNA. DR EMBL; AL353995; CAB89398.1; -; Genomic_DNA. DR EMBL; AY052293; AAK96486.1; -; mRNA. DR EMBL; AY061918; AAL31245.1; -; mRNA. DR PIR; S47970; S47970. DR PIR; S53727; S53727. DR PIR; T49994; T49994. DR UniGene; At.24269; -. DR HSSP; P93343; 1O9E. DR SMR; P48349; 6-239. DR GenomeReviews; BA000015_GR; AT5G10450. DR KEGG; ath:At5g10450; -. DR TAIR; At5g10450; -. DR ArrayExpress; P48349; -. DR GermOnline; AT5G10450; Arabidopsis thaliana. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 248 14-3-3-like protein GF14 lambda. FT /FTId=PRO_0000058668. FT CONFLICT 241 248 MQEQMDEA -> YAGADGRGLRI (in Ref. 1). FT CONFLICT 243 248 EQMDEA -> TNQMHHIRDIKEHVKTEITAKPCVLSYYYSM FT (in Ref. 5). SQ SEQUENCE 248 AA; 27976 MW; 4017D23098E74891 CRC64; MAATLGRDQY VYMAKLAEQA ERYEEMVQFM EQLVTGATPA EELTVEERNL LSVAYKNVIG SLRAAWRIVS SIEQKEESRK NDEHVSLVKD YRSKVESELS SVCSGILKLL DSHLIPSAGA SESKVFYLKM KGDYHRYMAE FKSGDERKTA AEDTMLAYKA AQDIAAADMA PTHPIRLGLA LNFSVFYYEI LNSSDKACNM AKQAFEEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD MQEQMDEA // ID 14336_ORYSA Reviewed; 260 AA. AC Q06967; Q53RI8; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 20-FEB-2007, entry version 36. DE 14-3-3-like protein GF14-F (G-box factor 14-3-3 homolog F) (OsGF14a) DE (14-3-3-like protein S94) (Stress-regulated 14-3-3 protein) (SR14-3- DE 3). GN Name=GF14F; OrderedLocusNames=Os03g0710800, LOC_Os03g50290; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94009718; PubMed=8405471; DOI=10.1016/0014-5793(93)80650-J; RA Uchimiya H., Kidou S., Anai T., Umeda M., Aotsuka S., Tsuge T., RA Kato A.; RT "Molecular structure of ras-related small GTP-binding protein genes of RT rice plants and GTPase activities of gene products in Escherichia RT coli."; RL FEBS Lett. 332:282-286(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93144687; PubMed=7678761; RA Kidou S., Umeda M., Kato A., Uchimiya H.; RT "Isolation and characterization of a rice cDNA similar to the bovine RT brain-specific 14-3-3 protein gene."; RL Plant Mol. Biol. 21:191-194(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RX PubMed=16109971; DOI=10.1101/gr.3869505; RG The rice chromosome 3 sequencing consortium; RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., RA Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., RA Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S., RA Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., RA Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., RA de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., RA Kim H.-I., Rambo T., Currie J., Collura K., Kernodle-Thompson S., RA Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., RA Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., RA Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., RA Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., RA Wilson R., Jin W., Lee H.R., Jiang J., Jackson S.; RT "Sequence, annotation, and analysis of synteny between rice chromosome RT 3 and diverged grass species."; RL Genome Res. 15:1284-1291(2005). RN [4] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=9596641; DOI=10.1105/tpc.10.5.837; RA Schultz T.F., Medina J., Hill A., Quatrano R.S.; RT "14-3-3 proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) RT response complex in the Em promoter and interact with VP1 and EmBP1."; RL Plant Cell 10:837-847(1998). RN [5] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND NOMENCLATURE. RX PubMed=16766513; DOI=10.1093/dnares/dsl001; RA Chen F., Li Q., Sun L., He Z.; RT "The rice 14-3-3 gene family and its involvement in responses to RT biotic and abiotic stress."; RL DNA Res. 13:53-63(2006). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SUBUNIT: May form a complex with the transcriptional activator VP1 CC and the bZIP transcription factor EMBP1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots and panicles and CC at lower levels in flag leaves and internodes. CC -!- INDUCTION: By wounding, drought and salt stresses, CC benzothiadiazole (BTH), ethephon, methyl jasmonate (MeJa), CC hydrogen peroxide, abscisic acid (ABA) and incompatible and CC compatible races of rice blast fungus (M.grisea). CC -!- SIMILARITY: Belongs to the 14-3-3 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; D16140; BAA03711.1; -; mRNA. DR EMBL; AC087181; AAX95656.1; -; Genomic_DNA. DR PIR; S30927; S30927. DR UniGene; Os.2673; -. DR HSSP; P93343; 1O9E. DR SMR; Q06967; 7-239. DR Gramene; Q06967; -. DR GO; GO:0004863; F:diacylglycerol-activated phospholipid-depen...; IDA:Gramene. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Nuclear protein. FT CHAIN 1 260 14-3-3-like protein GF14-F. FT /FTId=PRO_0000058696. FT CONFLICT 124 124 K -> N (in Ref. 1; BAA03711). FT CONFLICT 183 183 F -> L (in Ref. 1; BAA03711). SQ SEQUENCE 260 AA; 29178 MW; 483507B10661DF95 CRC64; MSPAEASREE NVYMAKLAEQ AERYEEMVEF MEKVAKTTDV GELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NEAYVASIKE YRSRIETELS KICDGILKLL DSHLVPSATA AESKVFYLKM KGDYHRYLAE FKSGAERKEA AENTLVAYKS AQDIALADLP TTHPIRLGLA LNFSVFYYEI LNSPDRACNL AKQAFDDAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD NAEDGGDEIK EAAKPEGEGH // ID 14336_SOLLC Reviewed; 258 AA. AC P93211; Q947T0; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 20-FEB-2007, entry version 38. DE 14-3-3 protein 6. GN Name=TFT6; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RX MEDLINE=99214454; PubMed=10198082; DOI=10.1104/pp.119.4.1243; RA Roberts M.R., Bowles D.J.; RT "Fusicoccin, 14-3-3 proteins, and defense responses in tomato RT plants."; RL Plant Physiol. 119:1243-1250(1999). RN [2] RP SEQUENCE REVISION TO 3-4; 13-14; 18-20; 47; 57 AND 234. RA Roberts M.R.; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=21624988; PubMed=11752381; DOI=10.1105/tpc.13.12.2687; RA Pnueli L., Gutfinger T., Hareven D., Ben-Naim O., Ron N., Adir N., RA Lifschitz E.; RT "Tomato SP-interacting proteins define a conserved signaling system RT that regulates shoot architecture and flowering."; RL Plant Cell 13:2687-2702(2001). CC -!- SUBUNIT: Homodimer (Potential). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X95904; CAA65149.2; -; Genomic_DNA. DR EMBL; AF079104; AAL04424.1; -; mRNA. DR UniGene; Les.11862; -. DR HSSP; P93343; 1O9E. DR SMR; P93211; 3-237. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 258 14-3-3 protein 6. FT /FTId=PRO_0000058686. SQ SEQUENCE 258 AA; 28967 MW; 5E3B3133F3F109CC CRC64; MASPREENVY MAKLAEQAER YEEMVEFMEK VVAAADGAEE LTVEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVASIKEYR SKIESELTSI CNGILKLLDS KLIGSAATGD SKVFYLKMKG DYHRYLAEFK TGAERKEAAE NTLSAYKAAQ DIANAELAPT HPIRLGLALN FSVFYYEILN SPDRACNLAK QAFDEAIAEL DTLGEESYKD STLIMQLLRD NLTLWTSDMQ DDGTDEIKEA TPKPDDNE // ID 14337_ARATH Reviewed; 265 AA. AC Q96300; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 23-JAN-2007, entry version 46. DE 14-3-3-like protein GF14 nu (General regulatory factor 7). GN Name=GRF7; OrderedLocusNames=At3g02520; ORFNames=F16B3.15; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Columbia; RX MEDLINE=97422888; PubMed=9276953; DOI=10.1104/pp.114.4.1421; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Columbia; RA Chung H.-J., Shanker S., Ferl R.J.; RT "Sequences of five Arabidopsis general regulatory factor (GRF) genes RT encoding 14-3-3 proteins."; RL (er) Plant Gene Register PGR99-114. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U60445; AAB49335.1; -; mRNA. DR EMBL; AF145299; AAD51782.1; -; Genomic_DNA. DR EMBL; AC021640; AAF32459.1; -; Genomic_DNA. DR EMBL; AY065274; AAL38750.1; -; mRNA. DR EMBL; AY096526; AAM20176.1; -; mRNA. DR EMBL; AY087723; AAM65260.1; -; mRNA. DR UniGene; At.21863; -. DR HSSP; P29312; 1A38. DR SMR; Q96300; 3-236. DR GenomeReviews; BA000014_GR; AT3G02520. DR KEGG; ath:At3g02520; -. DR TAIR; At3g02520; -. DR ArrayExpress; Q96300; -. DR GermOnline; AT3G02520; Arabidopsis thaliana. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 265 14-3-3-like protein GF14 nu. FT /FTId=PRO_0000058669. SQ SEQUENCE 265 AA; 29824 MW; BF76ECB7F76E166A CRC64; MSSSREENVY LAKLAEQAER YEEMVEFMEK VAKTVDTDEL TVEERNLLSV AYKNVIGARR ASWRIISSIE QKEESRGNDD HVSIIKDYRG KIETELSKIC DGILNLLDSH LVPTASLAES KVFYLKMKGD YHRYLAEFKT GAERKEAAES TLVAYKSAQD IALADLAPTH PIRLGLALNF SVFYYEILNS PDRACSLAKQ AFDEAISELD TLGEESYKDS TLIMQLLRDN LTLWNSDIND EAGGDEIKEA SKHEPEEGKP AETGQ // ID 14337_ORYSA Reviewed; 257 AA. AC Q5QNB8; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 20-FEB-2007, entry version 11. DE 14-3-3-like protein GF14-G (G-box factor 14-3-3 homolog G). GN Name=GF14G; OrderedLocusNames=Os01g0209200, LOC_Os01g11110; GN ORFNames=OSJNBa0016I09.32; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=22337376; PubMed=12447438; DOI=10.1038/nature01184; RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., RA Okamoto M., Ando T., Aoki H., Arita K., Hamada M., Harada C., RA Hijishita S., Honda M., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., RA Ikeno M., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., RA Karasawa W., Katagiri S., Kikuta A., Kobayashi N., Kono I., RA Machita K., Maehara T., Mizuno H., Mizubayashi T., Mukai Y., RA Nagasaki H., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., RA Namiki N., Negishi M., Ohta I., Ono N., Saji S., Sakai K., Shibata M., RA Shimokawa T., Shomura A., Song J., Takazaki Y., Terasawa K., Tsuji K., RA Waki K., Yamagata H., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., RA Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., Kim H.-I., Eun M.-Y., RA Yano M., Jiang J., Gojobori T.; RT "The genome sequence and structure of rice chromosome 1."; RL Nature 420:312-316(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=22752273; PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). RN [3] RP NOMENCLATURE. RX PubMed=16766513; DOI=10.1093/dnares/dsl001; RA Chen F., Li Q., Sun L., He Z.; RT "The rice 14-3-3 gene family and its involvement in responses to RT biotic and abiotic stress."; RL DNA Res. 13:53-63(2006). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AP003052; BAD73105.1; -; Genomic_DNA. DR EMBL; AK103145; -; NOT_ANNOTATED_CDS; mRNA. DR UniGene; Os.11930; -. DR Gramene; Q5QNB8; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; FALSE_NEG. DR PROSITE; PS00797; 1433_2; FALSE_NEG. FT CHAIN 1 257 14-3-3-like protein GF14-G. FT /FTId=PRO_0000246068. SQ SEQUENCE 257 AA; 28805 MW; BA32650CFB47D095 CRC64; MAPSDDLVYM AKLAEQAERY DEMVEAMNSV AKLDEGLTKE ERNLLSVGYK NLIGAKRAAM RIIGSIELKE ETKGKESHVR QTAEYRRKVE AEMDKICCDV INIIDKYLIP HSSGAESSVF YYKMKGDYYR YLAEFKTGTE KIEVSELSLN AYETASKTAQ TDLTPTDPIR LGLALNISVF YCEIMNSPDK ACQLAKNAFD EAVAELPSLS EENYKDSTLI MQLLRDNLAL WNSDMADDAD DIRERTDTTG AKGDPAA // ID 14337_SOLLC Reviewed; 252 AA. AC P93212; Q947S9; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 20-FEB-2007, entry version 43. DE 14-3-3 protein 7. GN Name=TFT7; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=21624988; PubMed=11752381; DOI=10.1105/tpc.13.12.2687; RA Pnueli L., Gutfinger T., Hareven D., Ben-Naim O., Ron N., Adir N., RA Lifschitz E.; RT "Tomato SP-interacting proteins define a conserved signaling system RT that regulates shoot architecture and flowering."; RL Plant Cell 13:2687-2702(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RX MEDLINE=99214454; PubMed=10198082; DOI=10.1104/pp.119.4.1243; RA Roberts M.R., Bowles D.J.; RT "Fusicoccin, 14-3-3 proteins, and defense responses in tomato RT plants."; RL Plant Physiol. 119:1243-1250(1999). CC -!- SUBUNIT: Homodimer (Potential). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF079450; AAL04425.1; -; mRNA. DR EMBL; X95905; CAA65150.1; -; Genomic_DNA. DR UniGene; Les.143; -. DR HSSP; P93343; 1O9E. DR SMR; P93212; 4-233. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 252 14-3-3 protein 7. FT /FTId=PRO_0000058687. FT CONFLICT 152 152 A -> L (in Ref. 2). SQ SEQUENCE 252 AA; 28814 MW; CAB34DFF9AFCD129 CRC64; MEKEREKQVY LARLAEQAER YDEMVEAMKA IAKMDVELTV EERNLVSVGY KNVIGARRAS WRILSSIEQK EESKGHEQNV KRIKTYRQRV EDELTKICSD ILSVIDEHLV PSSTTGESTV FYYKMKGDYY RYLAEFKAGD DRKEASEQSL KAYEAATATA SSDLAPTHPI RLGLALNFSV FYYEILNSPE RACHLAKQAF DEAIAELDSL SEESYKDSTL IMQLLRDNLT LWTSDLEEGG EHSKGDERQG EN // ID 14338_ARATH Reviewed; 248 AA. AC P48348; Q9SWP7; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 20-FEB-2007, entry version 56. DE 14-3-3-like protein GF14 kappa (General regulatory factor 8). GN Name=GRF8; OrderedLocusNames=At5g65430; ORFNames=MNA5.16; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC STRAIN=cv. Columbia; RX MEDLINE=97422888; PubMed=9276953; DOI=10.1104/pp.114.4.1421; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [2] RP SEQUENCE REVISION TO 53; 72; 121 AND 154. RA Reyes M., Ferl R.J.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC STRAIN=cv. Columbia; RA Chung H.-J., Shanker S., Ferl R.J.; RT "Sequences of five Arabidopsis general regulatory factor (GRF) genes RT encoding 14-3-3 proteins."; RL (er) Plant Gene Register PGR99-114. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=98344145; PubMed=9679202; DOI=10.1093/dnares/5.2.131; RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence RT features of the regions of 1,381,565 bp covered by twenty one RT physically assigned P1 and TAC clones."; RL DNA Res. 5:131-145(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P48348-1; Sequence=Displayed; CC Name=2; CC IsoId=P48348-2; Sequence=VSP_008971; CC Note=Derived from EST data. No experimental confirmation CC available; CC -!- SIMILARITY: Belongs to the 14-3-3 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; U36447; AAA79700.2; -; mRNA. DR EMBL; AF145300; AAD51783.1; -; Genomic_DNA. DR EMBL; AB011479; BAB11565.1; -; Genomic_DNA. DR EMBL; AY050996; AAK93673.1; -; mRNA. DR EMBL; AY079350; AAL85081.1; -; mRNA. DR EMBL; AY085088; AAM61642.1; -; mRNA. DR UniGene; At.10382; -. DR UniGene; At.24133; -. DR HSSP; P93343; 1O9E. DR SMR; P48348; 6-239. DR GenomeReviews; BA000015_GR; AT5G65430. DR KEGG; ath:At5g65430; -. DR TAIR; At5g65430; -. DR ArrayExpress; P48348; -. DR GermOnline; AT5G65430; Arabidopsis thaliana. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Alternative splicing. FT CHAIN 1 248 14-3-3-like protein GF14 kappa. FT /FTId=PRO_0000058670. FT VAR_SEQ 243 244 Missing (in isoform 2). FT /FTId=VSP_008971. FT CONFLICT 103 103 C -> F (in Ref. 1). SQ SEQUENCE 248 AA; 28029 MW; 848897CE6DB6BA37 CRC64; MATTLSRDQY VYMAKLAEQA ERYEEMVQFM EQLVSGATPA GELTVEERNL LSVAYKNVIG SLRAAWRIVS SIEQKEESRK NEEHVSLVKD YRSKVETELS SICSGILRLL DSHLIPSATA SESKVFYLKM KGDYHRYLAE FKSGDERKTA AEDTMIAYKA AQDVAVADLA PTHPIRLGLA LNFSVFYYEI LNSSEKACSM AKQAFEEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD MQEQMDEA // ID 14338_ORYSA Reviewed; 230 AA. AC Q2R1D5; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 28-NOV-2006, entry version 10. DE Putative 14-3-3-like protein GF14-H (G-box factor 14-3-3 homolog H). GN Name=GF14H; OrderedLocusNames=Os11g0609600, LOC_Os11g39540; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RX PubMed=16188032; DOI=10.1186/1741-7007-3-20; RG The rice chromosomes 11 and 12 sequencing consortia; RT "The sequence of rice chromosomes 11 and 12, rich in disease RT resistance genes and recent gene duplications."; RL BMC Biol. 3:20-20(2005). RN [2] RP NOMENCLATURE. RX PubMed=16766513; DOI=10.1093/dnares/dsl001; RA Chen F., Li Q., Sun L., He Z.; RT "The rice 14-3-3 gene family and its involvement in responses to RT biotic and abiotic stress."; RL DNA Res. 13:53-63(2006). CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; DP000010; ABA94733.1; -; Genomic_DNA. DR Gramene; Q2R1D5; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. KW Hypothetical protein. FT CHAIN 1 230 Putative 14-3-3-like protein GF14-H. FT /FTId=PRO_0000246069. SQ SEQUENCE 230 AA; 25854 MW; ED12599F87F8CC31 CRC64; MKEREKVVRL AKLAEQAERY DDMVEFMKTL ARMDVDMSAE ERLLFSVGFK KTIGARRASW RILESLEQKV TAGDQPGVTI NGYKKKVEDE LRAVCNEVLS IIAIHCLPLA NSGENVVFFY KMKGDYYRYL AEFSTGTEKK AATDQSLMAY QAWPCAQLFS LLEIMNSPER ASQVAKQALD EATAEINSAG VEGYKDSMLM MQLLKENLAL WTSELTGGET SKDDDVVMEG // ID 14338_SOLLC Reviewed; 261 AA. AC P93213; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 20-FEB-2007, entry version 43. DE 14-3-3 protein 8. GN Name=TFT8; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION TO 20 AND 76. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RA Roberts M.R.; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-131. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RX MEDLINE=99214454; PubMed=10198082; DOI=10.1104/pp.119.4.1243; RA Roberts M.R., Bowles D.J.; RT "Fusicoccin, 14-3-3 proteins, and defense responses in tomato RT plants."; RL Plant Physiol. 119:1243-1250(1999). CC -!- SUBUNIT: Homodimer (Potential). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X98864; CAA67372.2; -; mRNA. DR UniGene; Les.3678; -. DR HSSP; P29312; 1A4O. DR SMR; P93213; 6-235. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 261 14-3-3 protein 8. FT /FTId=PRO_0000058688. SQ SEQUENCE 261 AA; 29479 MW; 47564EF87AFDBF6D CRC64; MASSKERESL VYIARLAEQA ERYDEMVDAM KNVANLDVEL TVEERNLLSV GYKNVVGSRR ASWRILSSIE QKEDARGNEQ NVKRIQGYRQ KVESELTDIC NNIMTVIDEH LIPSCTAGES TVFYYKMKGD YYRYLAEFKT GDDKKEVSDL SLKAYQTATT TAEAELPITH PIRLGLALNF SVFYYEIMNS PERACQLAKQ VFDEAISELD SLNEDNYKDG TLILQLLRDN LTLWTSDIPE DGEEAPKGDA ANKVGAGEDA E // ID 14339_ARATH Reviewed; 263 AA. AC Q96299; O80367; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 28-NOV-2006, entry version 50. DE 14-3-3-like protein GF14 mu (General regulatory factor 9). GN Name=GRF9; OrderedLocusNames=At2g42590; ORFNames=F14N22.14; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Columbia; RX MEDLINE=97422888; PubMed=9276953; DOI=10.1104/pp.114.4.1421; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [2] RP NUCLEOTIDE SEQUENCE. RA Kuromori T., Yamamoto M.; RT "Members of the Arabidopsis 14-3-3 gene family trans-complement two RT types of defects in fission yeast."; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Columbia; RA Chung H.-J., Shanker S., Ferl R.J.; RT "Sequences of five Arabidopsis general regulatory factor (GRF) genes RT encoding 14-3-3 proteins."; RL (er) Plant Gene Register PGR99-114. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U60444; AAB49334.2; -; mRNA. DR EMBL; AB011545; BAA32735.1; -; mRNA. DR EMBL; AF145301; AAD51784.1; -; Genomic_DNA. DR EMBL; AC007087; AAD23005.1; -; Genomic_DNA. DR EMBL; AY093076; AAM13075.1; -; mRNA. DR EMBL; AY128764; AAM91164.1; -; mRNA. DR EMBL; AY085927; AAM63139.1; -; mRNA. DR PIR; T52037; T52037. DR UniGene; At.21859; -. DR HSSP; P93343; 1O9E. DR SMR; Q96299; 6-235. DR TRANSFAC; T04133; -. DR GenomeReviews; CT485783_GR; AT2G42590. DR KEGG; ath:At2g42590; -. DR TAIR; At2g42590; -. DR ArrayExpress; Q96299; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 263 14-3-3-like protein GF14 mu. FT /FTId=PRO_0000058671. SQ SEQUENCE 263 AA; 29520 MW; B70A45DF64DFD926 CRC64; MGSGKERDTF VYLAKLSEQA ERYEEMVESM KSVAKLNVDL TVEERNLLSV GYKNVIGSRR ASWRIFSSIE QKEAVKGNDV NVKRIKEYME KVELELSNIC IDIMSVLDEH LIPSASEGES TVFFNKMKGD YYRYLAEFKS GNERKEAADQ SLKAYEIATT AAEAKLPPTH PIRLGLALNF SVFYYEIMNA PERACHLAKQ AFDEAISELD TLNEESYKDS TLIMQLLRDN LTLWTSDISE EGGDDAHKTN GSAKPGAGGD DAE // ID 14339_SOLLC Reviewed; 261 AA. AC P93214; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 20-FEB-2007, entry version 43. DE 14-3-3 protein 9. GN Name=TFT9; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Roberts M.R.; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-131. RC STRAIN=cv. Moneymaker; TISSUE=Leaf; RX MEDLINE=99214454; PubMed=10198082; DOI=10.1104/pp.119.4.1243; RA Roberts M.R., Bowles D.J.; RT "Fusicoccin, 14-3-3 proteins, and defense responses in tomato RT plants."; RL Plant Physiol. 119:1243-1250(1999). CC -!- SUBUNIT: Homodimer (Potential). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X98865; CAA67373.2; -; mRNA. DR PIR; T07392; T07392. DR UniGene; Les.1252; -. DR HSSP; P93343; 1O9E. DR SMR; P93214; 6-235. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 261 14-3-3 protein 9. FT /FTId=PRO_0000058689. SQ SEQUENCE 261 AA; 29432 MW; F63081F7DC5553B2 CRC64; MASSKERENF VYVAKLAEQA ERYDEMVEAM KNVANMDVEL TVEERNLLSV GYKNVVGSRR ASWRILSSIE QKEESRGNEQ NVKRIKEYLQ KVESELTNIC NDIMVVIDQH LIPSCSAGES TVFYHKMKGD YYRYLAEFKA GNDKKEVAEL SLKAYQAATT AAEAELAPTH PIRLGLALNF SVFYYEIMNS PERACHLAKQ AFDEAISELD SLNEDSYKDS TLIMQLLRDN LTLWTSDLPE DAEDAQKGDA TNKAGGGEDA E // ID 1433A_HORVU Reviewed; 262 AA. AC P29305; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 28-NOV-2006, entry version 34. DE 14-3-3-like protein A (14-3-3A). OS Hordeum vulgare (Barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Triticeae; Hordeum. OX NCBI_TaxID=4513; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Pallas; TISSUE=Leaf; RX MEDLINE=93258422; PubMed=1302634; RA Brandt J.M., Thordal-Christensen H., Vad K., Gregersen P.L., RA Collinge D.B.; RT "A pathogen-induced gene of barley encodes a protein showing high RT similarity to a protein kinase regulator."; RL Plant J. 2:815-820(1992). CC -!- INDUCTION: In response to penetration attempts of powdery mildew CC fungi. CC -!- SIMILARITY: Belongs to the 14-3-3 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; X62388; CAA44259.1; -; mRNA. DR HSSP; P93343; 1O9E. DR SMR; P29305; 8-239. DR Gramene; P29305; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 262 14-3-3-like protein A. FT /FTId=PRO_0000058678. SQ SEQUENCE 262 AA; 29352 MW; DAE722EA5D416DAA CRC64; MSTAEATREE NVYMAKLAEQ AERYEEMVEF MEKVAKTADV GELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NEAYVASIKE YRTRIETELS KICDGILKLL DSHLVPSATA AESKVFYLKM KGDYHRYLAE FKAGAERKEA AENTLVAYKS AQDIALADLP TTHPIRLGLA LNFSVFYYEI LNSPDRACNL AKQAFDEAIA ELDSLGEESY KDSTLIMQLL RDNLTLWTSD NAEEGGDEIK EAASKPEGEG HS // ID 1433A_SOYBN Reviewed; 257 AA. AC Q96450; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-FEB-2007, entry version 33. DE 14-3-3-like protein A (SGF14A). GN Name=GF14A; OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Williams; RA Ryu G.R., Yoo C.M., Jeong H.J., Hong J.C.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U70533; AAB09580.1; -; mRNA. DR PIR; T08840; T08840. DR UniGene; Gma.1177; -. DR HSSP; P93343; 1O9E. DR SMR; Q96450; 4-237. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 257 14-3-3-like protein A. FT /FTId=PRO_0000058701. SQ SEQUENCE 257 AA; 29049 MW; 76DB93EC9828F430 CRC64; MSDSSREENV YMAKLADEAE RYEEMVEFME KVAKTVEVEE LTVEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVAIIKEYR GKIEAELSKI CDGILNLLES NLIPSAASPE SKVFYLKMKG DYHRYLAEFK TGAERKEAAE STLLAYKSAQ DIALADLAPT HPIRLGLALN FSVFYYEILN SPDRACNLAK QAFDEAISEL DTLGEESYKD STLIMQLLRD NLTLWTSDIT DIAGDEIKET SKQQPGE // ID 1433A_TOBAC Reviewed; 255 AA. AC P93342; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 28-NOV-2006, entry version 30. DE 14-3-3-like protein A. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Bright Yellow 2; RA Shen W.H., Gigot C.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; Y11212; CAA72095.1; -; mRNA. DR PIR; T02050; T02050. DR HSSP; P29312; 1A4O. DR SMR; P93342; 3-235. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 255 14-3-3-like protein A. FT /FTId=PRO_0000058707. SQ SEQUENCE 255 AA; 28660 MW; 29F95F841B418C72 CRC64; MASPREENVY LAKLAEQAER YEEMVEFMEK VVGAGDDELT IEERNLLSVA YKNVIGARRA SWRIISSIEQ KEESRGNEDH VASIKTYRSK IESELTSICN GILKLLDSKL IGTAATGDSK VFYLKMKGDY YRYLAEFKTG AERKEAAENT LSAYKSAQDI ANGELAPTHP IRLGLALNFS VFYYEILNSP DRACNLAKQA FDEAIAELGT LGEESYKDST LIMQLFCDNL TLWTSDMQDD GTDEIKEPSK AEEQQ // ID 1433A_VICFA Reviewed; 261 AA. AC P42653; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 28-NOV-2006, entry version 29. DE 14-3-3-like protein A (VFA-1433A). OS Vicia faba (Broad bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Vicieae; Vicia. OX NCBI_TaxID=3906; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cotyledon; RA Saalbach G., Christov V., Schwerdel M.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; Z48504; CAA88415.1; -; mRNA. DR PIR; S52899; S52899. DR HSSP; P93343; 1O9E. DR SMR; P42653; 5-239. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 261 14-3-3-like protein A. FT /FTId=PRO_0000058713. SQ SEQUENCE 261 AA; 29420 MW; EE41151B7679570F CRC64; MATAPTPREE FVYMAKLAEQ AERYEEMVEF MEKVTAAVES EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NDEHVSVIRD YRSKIETELS NICNGILKLL DSRLIPSAAL GDSKVFYLKM KGDYHRYLAE FKSGAERKDA AESTLTAYKS AQDIANTELP PTHPIRLGLA LNFSVFYYEI LNSPDRACGL AKQAFDEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD MQDDGADEIK EAAPKGNDEP Q // ID 1433B_BOVIN Reviewed; 246 AA. AC P68250; P29358; DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-FEB-2007, entry version 23. DE 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein 1) DE (KCIP-1). GN Name=YWHAB; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP PROTEIN SEQUENCE OF 2-246. RX MEDLINE=91108808; PubMed=1671102; RA Isobe T., Ichimura T., Sunaya T., Okuyama T., Takahashi N., Kuwano R., RA Takahashi Y.; RT "Distinct forms of the protein kinase-dependent activator of tyrosine RT and tryptophan hydroxylases."; RL J. Mol. Biol. 217:125-132(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-146. RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J., RA McConnell D.G.; RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION. RX PubMed=7931346; RA Tanji M., Horwitz R., Rosenfeld G., Waymire J.C.; RT "Activation of protein kinase C by purified bovine brain 14-3-3: RT comparison with tyrosine hydroxylase activation."; RL J. Neurochem. 63:1908-1916(1994). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Interacts with SSH1 (By similarity). Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; CC IsoId=P68250-1; Sequence=Displayed; CC Name=Short; CC IsoId=P68250-2; Sequence=VSP_018631; CC Note=Contains a N-acetylmethionine at position 1 (By CC similarity); CC -!- PTM: Isoform alpha differs from isoform beta in being CC phosphorylated (By similarity). CC -!- PTM: Isoform Short contains a N-acetylmethionine at position 2 (By CC similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF043736; AAC02090.1; -; mRNA. DR UniGene; Bt.5535; -. DR HSSP; P93343; 1O9E. DR SMR; P68250; 3-233. DR KEGG; bta:286863; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Alternative initiation; Direct protein sequencing; KW Phosphorylation. FT INIT_MET 1 1 Removed. FT CHAIN 2 246 14-3-3 protein beta/alpha. FT /FTId=PRO_0000000001. FT MOD_RES 2 2 N-acetylthreonine (By similarity). FT MOD_RES 186 186 Phosphoserine (By similarity). FT VAR_SEQ 1 2 Missing (in isoform Short). FT /FTId=VSP_018631. SQ SEQUENCE 246 AA; 28081 MW; CABA32314D86800D CRC64; MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL QLLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN // ID 1433B_CHICK Reviewed; 244 AA. AC Q5ZLQ6; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 28-NOV-2006, entry version 14. DE 14-3-3 protein beta/alpha. GN Name=YWHAB; ORFNames=RCJMB04_5d11; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., RA Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., RA Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- PTM: Phosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AJ719678; CAG31337.1; -; mRNA. DR UniGene; Gga.4816; -. DR SMR; Q5ZLQ6; 1-231. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Phosphorylation. FT CHAIN 1 244 14-3-3 protein beta/alpha. FT /FTId=PRO_0000058597. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 184 184 Phosphoserine (By similarity). SQ SEQUENCE 244 AA; 27907 MW; 200272F6434A5254 CRC64; MDKSELVQKA KLAEQAERYD DMAAAMKAVT EQGHELSNEE RNLLSVAYKN VVGARRSSWR VISSIEQKTE RNEKKQQMGR EYREKIEAEL QDICNDVLEL LDKYLIVNAT QPESKVFYLK MKGDYYRYLS EVASGDNKQT TVANSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACN LAKTAFDEAI AELDTLNEES YKDSTLIMQL LRDNLTLWTS ENQGDEGDAG EGEN // ID 1433B_HORVU Reviewed; 262 AA. AC Q43470; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 28-NOV-2006, entry version 28. DE 14-3-3-like protein B (14-3-3B). OS Hordeum vulgare (Barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Triticeae; Hordeum. OX NCBI_TaxID=4513; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Pallas; TISSUE=Leaf; RA Thordal-Christensen H., Brandt J.M., Collinge D.B.; RT "A cDNA for a 14-3-3b protein expressed in Barley leaves."; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. CC -!- INDUCTION: In response to penetration attempts of powdery mildew CC fungi. CC -!- SIMILARITY: Belongs to the 14-3-3 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; X93170; CAA63658.1; -; mRNA. DR PIR; T04406; T04406. DR HSSP; P93343; 1O9E. DR SMR; Q43470; 8-240. DR Gramene; Q43470; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 262 14-3-3-like protein B. FT /FTId=PRO_0000058679. SQ SEQUENCE 262 AA; 29691 MW; 00D4A898110EA35F CRC64; MAQPAELSRE ENVYMAKLAE QAERYEEMVE FMEKVAKTVD SEELTVEERN LLSVAYKNVI GARRASWRII SSIEQKEESR GNEDRVTLIK DYRGKIEVEL TKICDGILKL LDSHLVPSST APESKVFYLK MKGDYYRYLA EFKSGTERKD AAENTMVAYK AAQEIALAEL PPTHPIRLGL ALNFSVFYYE ILNSPDRACD LAKQAFDEAI SELDSLSEES YKDSTLIMQL LRDNLTLWTS DISEDAAEEM KDAPKGESGD GQ // ID 1433B_HUMAN Reviewed; 246 AA. AC P31946; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 83. DE 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein 1) DE (KCIP-1) (Protein 1054). GN Name=YWHAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Keratinocyte; RX MEDLINE=93294871; PubMed=8515476; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 3-20. RC TISSUE=Platelet; RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [5] RP INTERACTION WITH SSH1. RX PubMed=15159416; DOI=10.1083/jcb.200401136; RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; RT "A pathway of neuregulin-induced activation of cofilin-phosphatase RT Slingshot and cofilin in lamellipodia."; RL J. Cell Biol. 165:465-471(2004). RN [6] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with SSH1. CC -!- INTERACTION: CC O43521:BCL2L11; NbExp=1; IntAct=EBI-359815, EBI-526406; CC P46527:CDKN1B; NbExp=1; IntAct=EBI-359815, EBI-519280; CC P04049:RAF1; NbExp=4; IntAct=EBI-359815, EBI-365996; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by CC mass spectrometry in melanosome fractions from stage I to stage CC IV. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; CC IsoId=P31946-1; Sequence=Displayed; CC Name=Short; CC IsoId=P31946-2; Sequence=VSP_018632; CC Note=Contains a N-acetylmethionine at position 1 (By CC similarity); CC -!- PTM: Isoform alpha differs from isoform beta in being CC phosphorylated (By similarity). CC -!- PTM: Isoform Short contains a N-acetylmethionine at position 1 (By CC similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X57346; CAA40621.1; -; mRNA. DR EMBL; AL008725; CAA15497.1; -; Genomic_DNA. DR EMBL; BC001359; AAH01359.1; -; mRNA. DR PIR; S34755; S34755. DR UniGene; Hs.651212; -. DR PDB; 2BQ0; X-ray; A/B=1-239. DR PDB; 2C23; X-ray; A=1-239. DR DIP; DIP:743N; -. DR IntAct; P31946; -. DR Cornea-2DPAGE; P31946; HUMAN. DR OGP; P31946; -. DR REPRODUCTION-2DPAGE; P31946; HUMAN. DR Ensembl; ENSG00000166913; Homo sapiens. DR KEGG; hsa:7529; -. DR H-InvDB; HIX0015846; -. DR HGNC; HGNC:12849; YWHAB. DR HPA; CAB003759; -. DR MIM; 601289; gene. DR Reactome; REACT_498.3; Insulin receptor mediated signaling. DR Reactome; REACT_578.1; Apoptosis. DR ArrayExpress; P31946; -. DR GermOnline; ENSG00000166913; Homo sapiens. DR GO; GO:0048471; C:perinuclear region; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW 3D-structure; Acetylation; Alternative initiation; KW Direct protein sequencing; Phosphorylation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 246 14-3-3 protein beta/alpha. FT /FTId=PRO_0000000003. FT MOD_RES 2 2 N-acetylthreonine (By similarity). FT MOD_RES 186 186 Phosphoserine (By similarity). FT VAR_SEQ 1 2 Missing (in isoform Short). FT /FTId=VSP_018632. FT HELIX 5 17 FT TURN 18 19 FT HELIX 21 32 FT TURN 33 34 FT HELIX 40 67 FT TURN 68 69 FT HELIX 75 105 FT TURN 106 106 FT HELIX 107 110 FT HELIX 114 133 FT TURN 134 134 FT TURN 137 137 FT HELIX 138 161 FT TURN 164 165 FT HELIX 167 182 FT TURN 183 183 FT HELIX 187 202 FT HELIX 203 207 FT TURN 210 212 FT HELIX 213 231 SQ SEQUENCE 246 AA; 28082 MW; 6BE1A9BF97468017 CRC64; MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN // ID 1433B_MACFA Reviewed; 246 AA. AC Q4R572; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 18. DE 14-3-3 protein beta/alpha. GN Name=YWHAB; ORFNames=QccE-16215; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer. Interacts with SSH1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; CC IsoId=Q4R572-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q4R572-2; Sequence=VSP_018633; CC Note=No experimental confirmation available. Inferred by CC similarity. Contains a N-acetylmethionine at position 1 (By CC similarity); CC -!- PTM: Isoform alpha differs from isoform beta in being CC phosphorylated (By similarity). CC -!- PTM: Isoform Short contains a N-acetylmethionine at position 1 (By CC similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AB169672; BAE01753.1; -; mRNA. DR SMR; Q4R572; 3-233. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Alternative initiation; Phosphorylation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 246 14-3-3 protein beta/alpha. FT /FTId=PRO_0000042983. FT MOD_RES 2 2 N-acetylthreonine (By similarity). FT MOD_RES 186 186 Phosphoserine (By similarity). FT VAR_SEQ 1 2 Missing (in isoform Short). FT /FTId=VSP_018633. SQ SEQUENCE 246 AA; 28082 MW; 6BE1A9BF97468017 CRC64; MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN // ID 1433B_MOUSE Reviewed; 246 AA. AC Q9CQV8; O70455; Q3TY33; Q3UAN6; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 59. DE 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein 1) DE (KCIP-1). GN Name=Ywhab; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RA Karpitskiy V.V., Shaw A.S.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Bone marrow, Embryo, Kidney, Liver, Thymus, 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 [3] RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-84 AND TYR-106, AND MASS RP SPECTROMETRY. RX PubMed=16800626; DOI=10.1021/bi060474w; RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., RA Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., RA Squier T.C., Bigelow D.J.; RT "Endogenously nitrated proteins in mouse brain: links to RT neurodegenerative disease."; RL Biochemistry 45:8009-8022(2006). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with SSH1 (By similarity). CC -!- INTERACTION: CC O54918:Bcl2l11; NbExp=1; IntAct=EBI-771608, EBI-526067; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; CC IsoId=Q9CQV8-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q9CQV8-2; Sequence=VSP_018634; CC Note=No experimental confirmation available. Contains a CC N-acetylmethionine at position 1 (By similarity); CC -!- PTM: Isoform alpha differs from isoform beta in being CC phosphorylated (By similarity). CC -!- PTM: Isoform Short contains a N-acetylmethionine at position 1 (By CC similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF058797; AAC14343.1; -; mRNA. DR EMBL; AK002632; BAB22246.1; -; mRNA. DR EMBL; AK004872; BAB23631.1; -; mRNA. DR EMBL; AK011389; BAB27587.1; -; mRNA. DR EMBL; AK083367; BAC38886.1; -; mRNA. DR EMBL; AK144061; BAE25678.1; -; mRNA. DR EMBL; AK150414; BAE29538.1; -; mRNA. DR EMBL; AK151294; BAE30278.1; -; mRNA. DR EMBL; AK158932; BAE34730.1; -; mRNA. DR UniGene; Mm.34319; -. DR UniGene; Mm.430961; -. DR HSSP; P93343; 1O9E. DR SMR; Q9CQV8; 3-233. DR IntAct; Q9CQV8; -. DR Ensembl; ENSMUSG00000018326; Mus musculus. DR KEGG; mmu:54401; -. DR MGI; MGI:1891917; Ywhab. DR ArrayExpress; Q9CQV8; -. DR GermOnline; ENSMUSG00000018326; Mus musculus. DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI. DR GO; GO:0006605; P:protein targeting; IDA:MGI. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Alternative initiation; Nitration; Phosphorylation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 246 14-3-3 protein beta/alpha. FT /FTId=PRO_0000000005. FT MOD_RES 2 2 N-acetylthreonine (By similarity). FT MOD_RES 84 84 Nitrated tyrosine. FT MOD_RES 106 106 Nitrated tyrosine. FT MOD_RES 186 186 Phosphoserine (By similarity). FT VAR_SEQ 1 2 Missing (in isoform Short). FT /FTId=VSP_018634. FT CONFLICT 10 10 Q -> H (in Ref. 1). FT CONFLICT 74 74 N -> D (in Ref. 1). FT CONFLICT 126 126 D -> Y (in Ref. 2; BAE29538/BAE30278). SQ SEQUENCE 246 AA; 28086 MW; 51C366ED85B38EED CRC64; MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLILN ATQAESKVFY LKMKGDYFRY LSEVASGENK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN // ID 1433B_RAT Reviewed; 246 AA. AC P35213; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 67. DE 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein 1) DE (KCIP-1) (Prepronerve growth factor RNH-1). GN Name=Ywhab; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Brain; RX MEDLINE=93164855; PubMed=8381897; DOI=10.1016/0169-328X(93)90082-Z; RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H.; RT "Molecular cloning of rat cDNAs for beta and gamma subtypes of 14-3-3 RT protein and developmental changes in expression of their mRNAs in the RT nervous system."; RL Brain Res. Mol. Brain Res. 17:135-146(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=96318520; PubMed=8749325; RA Takai R., Tanaka E., Miyazaki T., Suda M., Tashiro F.; RT "Function of RNH-1/14-3-3 beta gene in cellular differentiation and RT proliferation."; RL J. Biochem. 118:1045-1053(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Interacts with SSH1 (By similarity). Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; CC IsoId=P35213-1; Sequence=Displayed; CC Name=Short; CC IsoId=P35213-2; Sequence=VSP_018635; CC Note=No experimental confirmation available. Contains a CC N-acetylmethionine at position 1 (By similarity); CC -!- PTM: Isoform alpha differs from isoform beta in being CC phosphorylated (By similarity). CC -!- PTM: Isoform Short contains a N-acetylmethionine at position 1 (By CC similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; D17446; BAA04260.1; -; mRNA. DR EMBL; S55223; AAA13843.1; -; mRNA. DR EMBL; S83440; AAB50874.1; -; mRNA. DR EMBL; BC076502; AAH76502.1; -; mRNA. DR PIR; A49023; A49023. DR UniGene; Rn.8653; -. DR HSSP; P93343; 1O9E. DR SMR; P35213; 3-233. DR IntAct; P35213; -. DR Ensembl; ENSRNOG00000010945; Rattus norvegicus. DR KEGG; rno:56011; -. DR RGD; 61998; Ywhab. DR ArrayExpress; P35213; -. DR GermOnline; ENSRNOG00000010945; Rattus norvegicus. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Alternative initiation; Phosphorylation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 246 14-3-3 protein beta/alpha. FT /FTId=PRO_0000000007. FT MOD_RES 2 2 N-acetylthreonine (By similarity). FT MOD_RES 186 186 Phosphoserine (By similarity). FT VAR_SEQ 1 2 Missing (in isoform Short). FT /FTId=VSP_018635. SQ SEQUENCE 246 AA; 28054 MW; B663D1F2182F9C43 CRC64; MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICSDVL ELLDKYLILN ATHAESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN // ID 1433B_SOYBN Reviewed; 247 AA. AC Q96451; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-FEB-2007, entry version 33. DE 14-3-3-like protein B (SGF14B) (Fragment). GN Name=GF14B; OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Williams; RA Ryu G.R., Yoo C.M., Jeong H.J., Hong J.C.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U70534; AAB09581.1; -; mRNA. DR PIR; T08842; T08842. DR UniGene; Gma.1417; -. DR HSSP; P29312; 1A38. DR SMR; Q96451; 6-238. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN <1 247 14-3-3-like protein B. FT /FTId=PRO_0000058702. FT NON_TER 1 1 SQ SEQUENCE 247 AA; 27921 MW; 9EDFBB4B4F61C468 CRC64; AEGLNREQYV YLANVSEQAE RYEEMVEFMQ KVVVGSTPAS ELTVEERNLL SVAYKNVIGS LRAAWRIVSS IEQKEEGRKN DDHVSLVKHY RSKVENELTQ VCATILSLLD SNLVPSASAS ESKVFYLKMK GDYHRYLAEF KVGDERKTAT EDTMLSYKAA QDIASADLPP THPIRLGLAL NFSVFYYEIL NQSDKACAMA KQAFEEAIAE LDTLGEESYK DSTLIMQLLR DNLTLWTSDV QDQLDEP // ID 1433B_TOBAC Reviewed; 255 AA. AC O49995; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 28-NOV-2006, entry version 29. DE 14-3-3-like protein B. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98105599; PubMed=9443388; DOI=10.1007/s004250050238; RA Piotrowski M., Oecking C.; RT "Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for RT the phylogeny of plant 14-3-3 proteins."; RL Planta 204:127-130(1998). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U91723; AAC49891.1; -; mRNA. DR PIR; T04127; T04127. DR HSSP; P93343; 1O9E. DR SMR; O49995; 2-235. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 255 14-3-3-like protein B. FT /FTId=PRO_0000058708. SQ SEQUENCE 255 AA; 28827 MW; 65CE3CD2FD83DF1E CRC64; MAREENVYMA KLAEQAERYE EMVSFMEKVS TSLGTSEELT VEERNLLSVA YKNVIGARRA SWRIISSIEQ KEESRGNEDH VKCIQEYRSK IESELSNICD GILKLLDSCL IPSASAGDSK VFYLKMKGDY HRYLAEFKTG AERKEAAEST LSAYKAAQDI ANAELAPTHP IRLGLALNFS VFYYEILNSP DRACNLAKQA FDEAIAELDT LGEESYKDST LIMQLLRDNL TLWTSDMQDD GADEIKETKT DNEQQ // ID 1433B_VICFA Reviewed; 261 AA. AC P42654; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 28-NOV-2006, entry version 30. DE 14-3-3-like protein B (VFA-1433B). OS Vicia faba (Broad bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Vicieae; Vicia. OX NCBI_TaxID=3906; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cotyledon; RA Saalbach G., Christov V., Schwerdel M.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; Z48505; CAA88416.1; -; mRNA. DR PIR; S52900; S52900. DR HSSP; P93343; 1O9E. DR SMR; P42654; 6-235. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 261 14-3-3-like protein B. FT /FTId=PRO_0000058714. SQ SEQUENCE 261 AA; 29524 MW; 2981BA7AE4C7E314 CRC64; MASTKDRENF VYIAKLAEQA ERYEEMVDSM KNVANLDVEL TIEERNLLSV GYKNVIGARR ASWRILSSIE QKEESKGNDV NAKRIKEYRH KVETELSNIC IDVMRVIDEH LIPSAAAGES TVFYYKMKGD YYRYLAEFKT GNEKKEAGDQ SMKAYESATT AAEAELPPTH PIRLGLALNF SVFYYEILNS PERACHLAKQ AFDEAISELD TLNEESYKDS TLIMQLLRDN LTLWTSDIPE DGEDSQKANG TAKFGGGDDA E // ID 1433B_XENTR Reviewed; 244 AA. AC Q5XGC8; Q28HK2; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 28-NOV-2006, entry version 18. DE 14-3-3 protein beta/alpha. GN Name=ywhab; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG Sanger Xenopus tropicalis EST/cDNA project; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; CR760847; CAJ82973.1; -; mRNA. DR EMBL; BC084514; AAH84514.1; -; mRNA. DR UniGene; Str.8742; -. DR SMR; Q5XGC8; 1-231. DR Ensembl; ENSXETG00000022830; Xenopus tropicalis. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 244 14-3-3 protein beta/alpha. FT /FTId=PRO_0000058600. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 244 AA; 27721 MW; FF766793EA1CA9E5 CRC64; MDKSELVQKA KLSEQAERYD DMAASMKAVT ELGAELSNEE RNLLSVAYKN VVGARRSSWR VISSIEQKTE GNDKRQQMAR EYREKVETEL QDICKDVLGL LDKYLVPNAT PPESKVFYLK MKGDYYRYLS EVASGDSKQE TVTCSQQAYQ EAFEISKSEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKSAFDEAI AELDTLNEES YKDSTLIMQL LRDNLTLWTS ENQGEEADNA EADN // ID 1433C_SOYBN Reviewed; 258 AA. AC Q96452; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-FEB-2007, entry version 34. DE 14-3-3-like protein C (SGF14C). GN Name=GF14C; OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Williams; RA Ryu G.R., Yoo C.M., Jeong H.J., Hong J.C.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U70535; AAB09582.1; -; mRNA. DR PIR; T08843; T08843. DR UniGene; Gma.105; -. DR HSSP; P93343; 1O9E. DR SMR; Q96452; 6-235. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 258 14-3-3-like protein C. FT /FTId=PRO_0000058703. SQ SEQUENCE 258 AA; 29209 MW; 6663BFC6E6992E5F CRC64; MASTKERENF VYVAKLAEQA ERYEEMVEAM KNVANLNVEL TVEERNLLSV GYKNVVGARR ASWRILSSIE QKEEAKGNDV SVKRIKEYRL KVESELSNIC SDIMTVIDEY LIPSSSSGEP SVFFYKMKGD YYRYLAEFKS GDERKEAADH SMKAYQLAST TAEAELASTH PIRLGLALNF SVFYYEILNS PERACHLAKQ AFDEAISELD TLSEESYKDS TLIMQLLRDN LTLWTSDIPE DGEEQKVDSA RADGGDDA // ID 1433C_TOBAC Reviewed; 260 AA. AC P93343; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 28-NOV-2006, entry version 37. DE 14-3-3-like protein C (14-3-3-like protein B). OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Bright Yellow 2; RA Shen W.H., Gigot C.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98105599; PubMed=9443388; DOI=10.1007/s004250050238; RA Piotrowski M., Oecking C.; RT "Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for RT the phylogeny of plant 14-3-3 proteins."; RL Planta 204:127-130(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=12606564; DOI=10.1093/emboj/cdg104; RA Wuertele M., Jelich-Ottmann C., Wittinghofer A., Oecking C.; RT "Structural view of a fungal toxin acting on a 14-3-3 regulatory RT complex."; RL EMBO J. 22:987-994(2003). CC -!- SIMILARITY: Belongs to the 14-3-3 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; Y11211; CAA72094.1; -; mRNA. DR EMBL; U91724; AAC49892.1; -; mRNA. DR PIR; T02051; T02051. DR PDB; 1O9C; X-ray; A=1-260. DR PDB; 1O9D; X-ray; A=1-260. DR PDB; 1O9E; X-ray; A=1-260. DR PDB; 1O9F; X-ray; A=1-260. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW 3D-structure. FT CHAIN 1 260 14-3-3-like protein C. FT /FTId=PRO_0000058709. FT HELIX 7 21 FT TURN 22 22 FT HELIX 24 36 FT TURN 37 37 FT STRAND 39 41 FT HELIX 45 77 FT TURN 78 80 FT HELIX 82 112 FT TURN 113 113 FT HELIX 114 117 FT HELIX 121 141 FT HELIX 145 168 FT TURN 171 172 FT HELIX 174 189 FT TURN 190 190 FT HELIX 194 214 FT TURN 215 215 FT HELIX 223 237 FT TURN 238 238 SQ SEQUENCE 260 AA; 29364 MW; BDCA77561ED45758 CRC64; MAVAPTAREE NVYMAKLAEQ AERYEEMVEF MEKVSNSLGS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NEEHVNSIRE YRSKIENELS KICDGILKLL DAKLIPSAAS GDSKVFYLKM KGDYHRYLAE FKTGAERKEA AESTLTAYKA AQDIATTELA PTHPIRLGLA LNFSVFYYEI LNSPDRACNL AKQAFDEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD MQDDGADEIK EDPKPDEAKN // ID 1433D_SOYBN Reviewed; 261 AA. AC Q96453; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-FEB-2007, entry version 33. DE 14-3-3-like protein D (SGF14D). GN Name=GF14D; OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Williams; RA Ryu G.R., Yoo C.M., Jeong H.J., Hong J.C.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U70536; AAB09583.1; -; mRNA. DR UniGene; Gma.1088; -. DR HSSP; P93343; 1O9E. DR SMR; Q96453; 6-235. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 261 14-3-3-like protein D. FT /FTId=PRO_0000058704. SQ SEQUENCE 261 AA; 29518 MW; F54DF5F5F0E0659B CRC64; MTASKDRENF VYIAKLAEQA ERYEEMVESM KNVANLDVEL TVEERNLLSV GYKNVIGARR ASWRILSSIE QKEETKGNEL NAKRIKEYRQ KVELELSNIC NDVMRVIDEH LIPSAAAGES TVFYYKMKGD YYRYLAEFKS GNEKKEAADQ SMKAYESATA AAEADLPPTH PIRLGLALNF SVFYYEILNS PERACHLAKQ AFDEAISELD TLNEESYKDS TLIMQLLRDN LTLWTSDIPE DGEDAQKVNG TAKLGGGEDA E // ID 1433D_TOBAC Reviewed; 249 AA. AC O49996; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 28-NOV-2006, entry version 29. DE 14-3-3-like protein D. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98105599; PubMed=9443388; DOI=10.1007/s004250050238; RA Piotrowski M., Oecking C.; RT "Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for RT the phylogeny of plant 14-3-3 proteins."; RL Planta 204:127-130(1998). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U91725; AAC49893.1; -; mRNA. DR PIR; T04128; T04128. DR HSSP; P93343; 1O9E. DR SMR; O49996; 9-240. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 249 14-3-3-like protein D. FT /FTId=PRO_0000058710. SQ SEQUENCE 249 AA; 28257 MW; 383ECB97BBF1BBF2 CRC64; MAVPENLTRE QCLYLAKLAE QAERYEEMVK FMDRLVAVSA SSELTVEERN LLSVAYKNVI GSLRAAWRIV SSIEQKEEGR KNEEHVVLVK DYRSKVESEL SDVCAGILKI LDQYLIPSAA AGESKVFYLK MKGDYYRYLA EFKVGNERKE AAEDTMLAYK AAQDIALAEL APTHPIRLGL ALNYSVFYYE ILNASEKACS MAKQAFEEAI AELDTLGEES YKDSTLIMQL LRDNLTLWTS DMQEQMDEA // ID 1433E_BOVIN Reviewed; 255 AA. AC P62261; P29360; P42655; Q3ZC40; Q63631; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 22. DE 14-3-3 protein epsilon (14-3-3E). GN Name=YWHAE; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J., RA McConnell D.G.; RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Thymus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION. RX PubMed=7931346; RA Tanji M., Horwitz R., Rosenfeld G., Waymire J.C.; RT "Activation of protein kinase C by purified bovine brain 14-3-3: RT comparison with tyrosine hydroxylase activation."; RL J. Neurochem. 63:1908-1916(1994). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with NDEL1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By CC similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF043735; AAC61927.1; -; mRNA. DR EMBL; BC102928; AAI02929.1; -; mRNA. DR UniGene; Bt.4035; -. DR HSSP; P93343; 1O9E. DR SMR; P62261; 3-232. DR KEGG; bta:282125; -. DR LinkHub; P62261; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 255 14-3-3 protein epsilon. FT /FTId=PRO_0000058617. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64; MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ // ID 1433E_CHICK Reviewed; 255 AA. AC Q5ZMT0; P84171; DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 28-NOV-2006, entry version 12. DE 14-3-3 protein epsilon (14-3-3E). GN Name=YWHAE; ORFNames=RCJMB04_1e8; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., RA Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., RA Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005). RN [2] RP IDENTIFICATION, AND MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=16287166; DOI=10.1002/pmic.200402056; RA Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., RA Delcan J., Schneider J., Palomar M.A., Linares R.; RT "Proteomic analysis of the Gallus gallus embryo at stage-29 of RT development."; RL Proteomics 5:4946-4957(2005). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- MASS SPECTROMETRY: MW=29440; MW_ERR=2; METHOD=MALDI; RANGE=1-255; CC NOTE=Ref.2. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AJ719304; CAG30963.1; -; mRNA. DR UniGene; Gga.4550; -. DR SMR; Q5ZMT0; 3-232. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 255 14-3-3 protein epsilon. FT /FTId=PRO_0000223506. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64; MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ // ID 1433E_DROME Reviewed; 262 AA. AC P92177; Q8IN87; Q9VEA8; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2003, sequence version 2. DT 20-FEB-2007, entry version 50. DE 14-3-3 protein epsilon (Suppressor of Ras1 3-9). GN Name=14-3-3-epsilon; Synonyms=14-3-3e, SR3-9; ORFNames=CG31196; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM D), AND MUTAGENESIS RP OF GLU-183; PHE-199 AND TYR-214. RX MEDLINE=97302963; PubMed=9159394; RA Chang H.C., Rubin G.M.; RT "14-3-3 epsilon positively regulates Ras-mediated signaling in RT Drosophila."; RL Genes Dev. 11:1132-1139(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: Positively regulates Ras-mediated pathways. Acts CC downstream or parallel to Raf, but upstream of nuclear factors in CC Ras signaling. Three mutants have been isolated, that suppress the CC rough eye phenotype caused by mutated Ras1 (sev-Ras1 v12). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- INTERACTION: CC Q9V3S3:Mst35Ba; NbExp=1; IntAct=EBI-204491, EBI-193363; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms may exist; CC Name=A; CC IsoId=P92177-3; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=B; CC IsoId=P92177-2; Sequence=VSP_008203; CC Note=No experimental confirmation available; CC Name=D; CC IsoId=P92177-1; Sequence=VSP_008204; CC -!- SIMILARITY: Belongs to the 14-3-3 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; U84898; AAC47520.1; -; Genomic_DNA. DR EMBL; U84897; AAC47519.1; -; mRNA. DR EMBL; AE014297; AAF55519.2; -; Genomic_DNA. DR EMBL; AE014297; AAN13764.1; -; Genomic_DNA. DR EMBL; AE014297; AAN13765.1; -; Genomic_DNA. DR UniGene; Dm.2357; -. DR HSSP; P93343; 1O9E. DR SMR; P92177; 3-232. DR IntAct; P92177; -. DR Ensembl; CG31196; Drosophila melanogaster. DR KEGG; dme:Dmel_CG31196; -. DR FlyBase; FBgn0020238; 14-3-3-epsilon. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-012185-MONOMER; -. DR GermOnline; CG31196; Drosophila melanogaster. DR GO; GO:0005694; C:chromosome; IDA:FlyBase. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0045172; C:ring canal (sensu Insecta); IDA:FlyBase. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0000077; P:DNA damage checkpoint; IMP:FlyBase. DR GO; GO:0007444; P:imaginal disc development; TAS:FlyBase. DR GO; GO:0007093; P:mitotic checkpoint; TAS:FlyBase. DR GO; GO:0048129; P:oocyte microtubule cytoskeleton polarizatio...; IMP:FlyBase. DR GO; GO:0009314; P:response to radiation; TAS:FlyBase. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Alternative splicing; Complete proteome. FT CHAIN 1 262 14-3-3 protein epsilon. FT /FTId=PRO_0000058650. FT VAR_SEQ 239 240 Missing (in isoform D). FT /FTId=VSP_008204. FT VAR_SEQ 239 239 Missing (in isoform B). FT /FTId=VSP_008203. FT MUTAGEN 183 183 E->K: Suppressor of sev-Ras1 V12; FT subviable. FT MUTAGEN 199 199 F->Y: Suppressor of sev-Ras1 V12. FT MUTAGEN 214 214 Y->F: Suppressor of sev-Ras1 V12. SQ SEQUENCE 262 AA; 29799 MW; 2C1562208547DA9C CRC64; MTERENNVYK AKLAEQAERY DEMVEAMKKV ASMDVELTVE ERNLLSVAYK NVIGARRASW RIITSIEQKE ENKGAEEKLE MIKTYRGQVE KELRDICSDI LNVLEKHLIP CATSGESKVF YYKMKGDYHR YLAEFATGSD RKDAAENSLI AYKAASDIAM NDLPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQAEEV DPNAGDGEPK EQIQDVEDQD VS // ID 1433E_HUMAN Reviewed; 255 AA. AC P62258; P29360; P42655; Q63631; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 06-FEB-2007, entry version 37. DE 14-3-3 protein epsilon (14-3-3E). GN Name=YWHAE; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95372385; PubMed=7644510; RA Conklin D.S., Galaktionov K., Beach D.; RT "14-3-3 proteins associate with cdc25 phosphatases."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7892-7896(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Heart; RA Luk S.C.W., Lee C.Y., Waye M.M.Y.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96300316; PubMed=8684458; DOI=10.1038/382308a0; RA Jin D.-Y., Lyu M.S., Kozak C.A., Jeang K.-T.; RT "Function of 14-3-3 proteins."; RL Nature 382:308-308(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=97011338; PubMed=8858348; RA Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.; RT "14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on RT chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome RT region."; RL Genome Res. 6:735-741(1996). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Tanigami A., Chong S.S., Ledbetter D.H.; RT "14-3-3 epsilon genomic sequence."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 1-19. RC TISSUE=Platelet; RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP PROTEIN SEQUENCE OF 1-19; 30-50 AND 131-170, ACETYLATION AT MET-1, AND RP MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Unpublished observations (MAY-2005). RN [9] RP INTERACTION WITH HCV CORE PROTEIN. RX MEDLINE=20111292; PubMed=10644344; RX DOI=10.1128/JVI.74.4.1736-1741.2000; RA Aoki H., Hayashi J., Moriyama M., Arakawa Y., Hino O.; RT "Hepatitis C virus core protein interacts with 14-3-3 protein and RT activates the kinase Raf-1."; RL J. Virol. 74:1736-1741(2000). RN [10] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with NDEL1 (By similarity). CC Interacts with HCV core protein. CC -!- INTERACTION: CC P46527:CDKN1B; NbExp=1; IntAct=EBI-356498, EBI-519280; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome. CC Note=Identified by mass spectrometry in melanosome fractions from CC stage I to stage IV. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U20972; AAC50175.1; -; mRNA. DR EMBL; U28936; AAA75301.1; -; mRNA. DR EMBL; U43399; AAC50625.1; -; mRNA. DR EMBL; U43430; AAD00026.1; -; mRNA. DR EMBL; U54778; AAC50710.1; -; mRNA. DR EMBL; AB017103; BAA32538.1; -; Genomic_DNA. DR EMBL; BC000179; AAH00179.1; -; mRNA. DR EMBL; BC001440; AAH01440.1; -; mRNA. DR PIR; I38947; I38947. DR UniGene; Hs.513851; -. DR PDB; 2BR9; X-ray; A=1-233. DR IntAct; P62258; -. DR OGP; P42655; -. DR REPRODUCTION-2DPAGE; P62258; HUMAN. DR KEGG; hsa:7531; -. DR HGNC; HGNC:12851; YWHAE. DR MIM; 605066; gene. DR LinkHub; P62258; -. DR ArrayExpress; P62258; -. DR GermOnline; ENSG00000108953; Homo sapiens. DR RZPD-ProtExp; I0402; -. DR RZPD-ProtExp; RZPDo839G0348; -. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0007242; P:intracellular signaling cascade; TAS:ProtInc. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW 3D-structure; Acetylation; Direct protein sequencing; KW Host-virus interaction. FT CHAIN 1 255 14-3-3 protein epsilon. FT /FTId=PRO_0000058618. FT MOD_RES 1 1 N-acetylmethionine. FT HELIX 4 17 FT TURN 18 18 FT HELIX 20 31 FT TURN 32 33 FT HELIX 39 73 FT TURN 74 74 FT HELIX 76 106 FT TURN 107 107 FT HELIX 108 111 FT HELIX 115 135 FT HELIX 138 162 FT TURN 165 166 FT HELIX 168 183 FT TURN 184 184 FT HELIX 188 204 FT HELIX 205 208 FT TURN 211 213 FT HELIX 214 231 SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64; MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ // ID 1433E_MOUSE Reviewed; 255 AA. AC P62259; P29360; P42655; Q63631; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 35. DE 14-3-3 protein epsilon (14-3-3E). GN Name=Ywhae; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. RC STRAIN=Swiss; TISSUE=Kidney; RX MEDLINE=95269876; PubMed=7750640; DOI=10.1006/dbio.1995.1139; RA McConnell J.E., Armstrong J.F., Bard J.B.; RT "The mouse 14-3-3 epsilon isoform, a kinase regulator whose expression RT pattern is modulated in mesenchyme and neuronal differentiation."; RL Dev. Biol. 169:218-228(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/Sv; RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ILS, and ISS; RX MEDLINE=21363810; 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 [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 INTERACTION WITH NDEL1. RX PubMed=12796778; DOI=10.1038/ng1169; RA Toyo-oka K., Shionoya A., Gambello M.J., Cardoso C., Leventer R., RA Ward H.L., Ayala R., Tsai L.-H., Dobyns W., Ledbetter D., RA Hirotsune S., Wynshaw-Boris A.; RT "14-3-3epsilon is important for neuronal migration by binding to RT NUDEL: a molecular explanation for Miller-Dieker syndrome."; RL Nat. Genet. 34:274-285(2003). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with NDEL1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By CC similarity). CC -!- DEVELOPMENTAL STAGE: In the E8.5 embryo, expressed throughout the CC embryo. Within a day, expression was more marked in mesenchyme CC than elsewhere (e.g., epithelial tissue, where it was generally CC low), although levels in neural tissue rose again by about E12.5. CC This difference was maintained until E15.5 when expression levels CC started to drop in most tissues, with those of the nervous system, CC tooth, and kidney being exceptions. Strongly expressed in early CC mesenchyme. The expression decreased as the mesenchyme CC differentiated. CC -!- SIMILARITY: Belongs to the 14-3-3 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; Z19599; CAA79659.1; -; mRNA. DR EMBL; D87663; BAA13424.1; -; mRNA. DR EMBL; AF483478; AAL90752.1; -; mRNA. DR EMBL; AF483479; AAL90753.1; -; mRNA. DR EMBL; BC058686; AAH58686.1; -; mRNA. DR PIR; I48337; S31975. DR UniGene; Mm.234700; -. DR HSSP; P93343; 1O9E. DR SMR; P62259; 3-232. DR IntAct; P62259; -. DR REPRODUCTION-2DPAGE; P62259; MOUSE. DR Ensembl; ENSMUSG00000020849; Mus musculus. DR KEGG; mmu:22627; -. DR MGI; MGI:894689; Ywhae. DR ArrayExpress; P62259; -. DR GermOnline; ENSMUSG00000020849; Mus musculus. DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI. DR GO; GO:0006605; P:protein targeting; IDA:MGI. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 255 14-3-3 protein epsilon. FT /FTId=PRO_0000058619. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64; MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ // ID 1433E_RAT Reviewed; 255 AA. AC P62260; P29360; P42655; Q63631; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 31. DE 14-3-3 protein epsilon (14-3-3E) (Mitochondrial import stimulation DE factor L subunit) (MSF L). GN Name=Ywhae; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. RC TISSUE=Pineal gland; RX MEDLINE=94296566; PubMed=8024705; RA Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A., RA Moffet J.R., Namboodiri M.A., Klein D.C.; RT "Cloning and characterization of the epsilon and zeta isoforms of the RT 14-3-3 proteins."; RL DNA Cell Biol. 13:629-640(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=95122474; PubMed=7822263; RA Alam R., Hachiya N., Sakaguchi M., Shun-Ichiro K., Iwanaga S., RA Kitajima M., Mihara K., Omura T.; RT "cDNA cloning and characterization of mitochondrial import stimulation RT factor (MSF) purified from rat liver cytosol."; RL J. Biochem. 116:416-425(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=96280718; PubMed=8694795; DOI=10.1006/bbrc.1996.0991; RA Gao L., Gu X.B., Yu D.S., Yu R.K., Zeng G.; RT "Association of a 14-3-3 protein with CMP-NeuAc:GM1 alpha 2,3- RT sialyltransferase."; RL Biochem. Biophys. Res. Commun. 224:103-107(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 119-123; 131-142 AND 197-215. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; RA Lubec G., Diao W., Afjehi-Sadat L.; RL Submitted (NOV-2006) to Swiss-Prot. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with NDEL1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By CC similarity). CC -!- DEVELOPMENTAL STAGE: Present at high levels in the pineal gland CC early in development and decreased steadily thereafter. CC -!- SIMILARITY: Belongs to the 14-3-3 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; M84416; AAC37659.1; -; mRNA. DR EMBL; D30739; BAA06401.1; -; mRNA. DR EMBL; U53882; AAC52676.1; -; mRNA. DR EMBL; BC063163; AAH63163.1; -; mRNA. DR PIR; JX0341; JX0341. DR UniGene; Rn.4225; -. DR HSSP; P93343; 1O9E. DR SMR; P62260; 3-232. DR IntAct; P62260; -. DR Ensembl; ENSRNOG00000005290; Rattus norvegicus. DR KEGG; rno:29753; -. DR RGD; 62000; Ywhae. DR ArrayExpress; P62260; -. DR GermOnline; ENSRNOG00000005290; Rattus norvegicus. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Direct protein sequencing. FT CHAIN 1 255 14-3-3 protein epsilon. FT /FTId=PRO_0000058620. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT CONFLICT 73 73 K -> T (in Ref. 3). FT CONFLICT 120 120 F -> S (in Ref. 3). FT CONFLICT 123 123 K -> Y (in Ref. 3). SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64; MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ // ID 1433E_SHEEP Reviewed; 255 AA. AC P62262; P29360; P42655; Q63631; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 22. DE 14-3-3 protein epsilon (14-3-3E) (Protein kinase C inhibitor protein DE 1) (KCIP-1). GN Name=YWHAE; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pineal gland; RX MEDLINE=94296566; PubMed=8024705; RA Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A., RA Moffet J.R., Namboodiri M.A., Klein D.C.; RT "Cloning and characterization of the epsilon and zeta isoforms of the RT 14-3-3 proteins."; RL DNA Cell Biol. 13:629-640(1994). RN [2] RP PROTEIN SEQUENCE OF 1-152; 165-184 AND 216-255. RC TISSUE=Brain; RX MEDLINE=92283271; PubMed=1317796; RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.; RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) RT from sheep brain. Amino acid sequence of phosphorylated forms."; RL Eur. J. Biochem. 206:453-461(1992). RN [3] RP PROTEIN SEQUENCE OF 1-23 AND 125-140. RC TISSUE=Brain; RX MEDLINE=90345949; PubMed=2143472; RA Toker A., Ellis C.A., Sellers L.A., Aitken A.; RT "Protein kinase C inhibitor proteins. Purification from sheep brain RT and sequence similarity to lipocortins and 14-3-3 protein."; RL Eur. J. Biochem. 191:421-429(1990). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with NDEL1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By CC similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; L07914; AAC37321.1; -; mRNA. DR UniGene; Oar.632; -. DR HSSP; P93343; 1O9E. DR SMR; P62262; 3-232. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Direct protein sequencing. FT CHAIN 1 255 14-3-3 protein epsilon. FT /FTId=PRO_0000058621. FT MOD_RES 1 1 N-acetylmethionine. FT CONFLICT 129 129 H -> Y (in Ref. 3). SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64; MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ // ID 1433E_TOBAC Reviewed; 272 AA. AC O49997; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 28-NOV-2006, entry version 29. DE 14-3-3-like protein E. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98105599; PubMed=9443388; DOI=10.1007/s004250050238; RA Piotrowski M., Oecking C.; RT "Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for RT the phylogeny of plant 14-3-3 proteins."; RL Planta 204:127-130(1998). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U91726; AAC49894.1; -; mRNA. DR PIR; T04129; T04129. DR HSSP; P93343; 1O9E. DR SMR; O49997; 4-237. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 272 14-3-3-like protein E. FT /FTId=PRO_0000058711. SQ SEQUENCE 272 AA; 30570 MW; 6083BA2F40612AD6 CRC64; MAESTREENV YMAKLAEQAE RYEEMVEFME KVAKTVDVEE LTVEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVSSIKEYR GKIEAELSKI CDGILNLLES HLIPVASTAE SKVFYLKMKG DYHRYLAEFK TGAERKEAAE NTLLAYKSAQ DIALAELAPT HPIRLGLALN FSVFYYEILN SSDRACNLAK QAFDDAIAEL DTLGEESYKD STLIMQLLRD NLTLWTSDTT VSLSLSQKYT PTNADAPTNN TVHTSKSFLG SA // ID 1433F_BOVIN Reviewed; 246 AA. AC P68509; P11576; P70198; Q3ZC14; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-FEB-2007, entry version 22. DE 14-3-3 protein eta (Protein kinase C inhibitor protein 1) (KCIP-1). GN Name=YWHAH; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Cerebellum; RX MEDLINE=89017142; PubMed=2902623; RA Ichimura T., Isobe T., Okuyama T., Takahashi N., Araki K., Kuwano R., RA Takahashi Y.; RT "Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a RT protein kinase-dependent activator of tyrosine and tryptophan RT hydroxylases."; RL Proc. Natl. Acad. Sci. U.S.A. 85:7084-7088(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Hypothalamus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP SIMILARITY TO KINASE INHIBITOR. RX MEDLINE=90220866; PubMed=1970123; RA Aitken A., Ellis C.A., Harris A., Sellers L.A., Toker A.; RT "Kinase and neurotransmitters."; RL Nature 344:594-594(1990). RN [4] RP FUNCTION. RX PubMed=7931346; RA Tanji M., Horwitz R., Rosenfeld G., Waymire J.C.; RT "Activation of protein kinase C by purified bovine brain 14-3-3: RT comparison with tyrosine hydroxylase activation."; RL J. Neurochem. 63:1908-1916(1994). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with many nuclear hormone receptors CC and cofactors including AR, ESR1, ESR2, MC2R, NR3C1, NRIP1, PPARBP CC and THRA (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 14-3-3 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; J03868; AAA30347.1; -; mRNA. DR EMBL; BC102982; AAI02983.1; -; mRNA. DR PIR; A40484; A40484. DR UniGene; Bt.76129; -. DR HSSP; P93343; 1O9E. DR SMR; P68509; 2-236. DR KEGG; bta:282126; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Direct protein sequencing; Phosphorylation. FT INIT_MET 1 1 Removed. FT CHAIN 2 246 14-3-3 protein eta. FT /FTId=PRO_0000058622. FT MOD_RES 2 2 N-acetylglycine (By similarity). FT CONFLICT 141 141 E -> Q (in Ref. 2; AAI02983). SQ SEQUENCE 246 AA; 28212 MW; C12F62B4ABA76DA3 CRC64; MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LALLDKFLIK NCNDFQYESK VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEHMQPTHP IRLGLALNFS VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN // ID 1433F_HUMAN Reviewed; 246 AA. AC Q04917; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 06-FEB-2007, entry version 75. DE 14-3-3 protein eta (Protein AS1). GN Name=YWHAH; Synonyms=YWHA1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=94032477; PubMed=8218406; DOI=10.1016/0167-4781(93)90053-G; RA Swanson K.D., Dhar M.S., Joshi J.G.; RT "The human and bovine 14-3-3 eta protein mRNAs are highly conserved in RT both their translated and untranslated regions."; RL Biochim. Biophys. Acta 1216:145-148(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Brain; RX MEDLINE=92251832; PubMed=1578511; RA Ichimura-Ohshima Y., Morii K., Ichimura T., Araki K., Takahashi Y., RA Isobe T., Minoshima S., Fukuyama R., Shimizu N., Kuwano R.; RT "cDNA cloning and chromosome assignment of the gene for human brain RT 14-3-3 protein eta chain."; RL J. Neurosci. Res. 31:600-605(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Leffers H., Tommerup N., Celis J.E.; RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96123461; PubMed=8561965; RA Muratake T., Hayashi S., Ichimura Y., Morii K., Kuwano R., RA Ichikawa T., Kumanishi T., Isobe T., Watanabe M., Kondo H.; RT "The effect on methamphetamine on the mRNA level for 14.3.3 eta chain RT in the human cultured cells."; RL Mol. Neurobiol. 11:223-230(1995). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96411648; PubMed=8812417; DOI=10.1006/geno.1996.0426; RA Muratake T., Hayashi S., Ichikawa T., Kumanishi T., Ichimura Y., RA Kuwano R., Isobe T., Wang Y., Minoshima S., Shimizu N., Takahashi Y.; RT "Structural organization and chromosomal assignment of the human 14-3- RT 3 eta chain gene (YWHAH)."; RL Genomics 36:63-69(1996). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=20057165; PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-225. RC TISSUE=Keratinocyte; RX MEDLINE=93294871; PubMed=8515476; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [10] RP PROTEIN SEQUENCE OF 2-10. RC TISSUE=Platelet; RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [11] RP PROTEIN SEQUENCE OF 2-10; 29-50; 62-69; 126-132; 144-155; 163-172 AND RP 218-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, AND RP MASS SPECTROMETRY. RC TISSUE=Platelet; RA Bienvenut W.V.; RL Unpublished observations (AUG-2005). RN [12] RP INTERACTION WITH AR; ESR1; ESR2; MC2R; NRIP1; NR3C1; PPARBP AND THRA. RX MEDLINE=21168078; PubMed=11266503; DOI=10.1210/me.15.4.501; RA Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., RA Gustafsson J.-A.; RT "Regulation of glucocorticoid receptor activity by 14-3-3-dependent RT intracellular relocalization of the corepressor RIP140."; RL Mol. Endocrinol. 15:501-511(2001). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with many nuclear CC hormone receptors and cofactors including AR, ESR1, ESR2, MC2R, CC NR3C1, NRIP1, PPARBP and THRA. CC -!- INTERACTION: CC O60565:GREM1; NbExp=2; IntAct=EBI-306940, EBI-944395; CC Q14103-4:HNRPD; NbExp=1; IntAct=EBI-306940, EBI-432545; CC Q96L34:MARK4; NbExp=1; IntAct=EBI-306940, EBI-302319; CC Q8TEW0:PARD3; NbExp=1; IntAct=EBI-306940, EBI-81968; CC Q9NPB6:PARD6A; NbExp=1; IntAct=EBI-306940, EBI-81876; CC Q9BYG5:PARD6B; NbExp=1; IntAct=EBI-306940, EBI-295391; CC P41743:PRKCI; NbExp=1; IntAct=EBI-306940, EBI-286199; CC -!- TISSUE SPECIFICITY: Expressed mainly in the brain and present in CC other tissues albeit at lower levels. CC -!- SIMILARITY: Belongs to the 14-3-3 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; L20422; AAA35483.1; -; mRNA. DR EMBL; X80536; CAA56676.1; -; Genomic_DNA. DR EMBL; X78138; CAA55017.1; -; mRNA. DR EMBL; X57345; CAA40620.1; -; mRNA. DR EMBL; D78577; BAA11418.1; -; Genomic_DNA. DR EMBL; S80794; AAB36036.1; -; mRNA. DR EMBL; CR456612; CAG30498.1; -; mRNA. DR EMBL; Z82248; CAB05112.1; -; Genomic_DNA. DR EMBL; BC003047; AAH03047.1; -; mRNA. DR PIR; S34756; S34756. DR PIR; S38509; S38509. DR UniGene; Hs.226755; -. DR PDB; 2C63; X-ray; A/B/C/D=1-246. DR PDB; 2C74; X-ray; A/B=1-246. DR DIP; DIP:27566N; -. DR IntAct; Q04917; -. DR Ensembl; ENSG00000128245; Homo sapiens. DR KEGG; hsa:7533; -. DR H-InvDB; HIX0016401; -. DR HGNC; HGNC:12853; YWHAH. DR MIM; 113508; gene. DR ArrayExpress; Q04917; -. DR GermOnline; ENSG00000128245; Homo sapiens. DR RZPD-ProtExp; IOH4929; -. DR RZPD-ProtExp; W2863; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0003779; F:actin binding; ISS:ProtInc. DR GO; GO:0035259; F:glucocorticoid receptor binding; IPI:UniProtKB. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB. DR GO; GO:0008426; F:protein kinase C inhibitor activity; ISS:UniProtKB. DR GO; GO:0016563; F:transcriptional activator activity; IDA:UniProtKB. DR GO; GO:0007010; P:cytoskeleton organization and biogenesis; ISS:ProtInc. DR GO; GO:0006713; P:glucocorticoid catabolic process; IDA:UniProtKB. DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptosis; ISS:ProtInc. DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISS:UniProtKB. DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB. DR GO; GO:0045941; P:positive regulation of transcription; IDA:UniProtKB. DR GO; GO:0007088; P:regulation of mitosis; ISS:ProtInc. DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:0009966; P:regulation of signal transduction; ISS:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW 3D-structure; Acetylation; Direct protein sequencing; Phosphorylation. FT INIT_MET 1 1 Removed. FT CHAIN 2 246 14-3-3 protein eta. FT /FTId=PRO_0000058623. FT MOD_RES 2 2 N-acetylglycine. FT CONFLICT 144 144 N -> T (in Ref. 9). FT CONFLICT 157 157 A -> G (in Ref. 1). FT CONFLICT 237 237 Q -> L (in Ref. 1). FT HELIX 4 16 FT TURN 17 18 FT HELIX 20 31 FT TURN 32 33 FT HELIX 39 73 FT TURN 74 74 FT HELIX 76 106 FT TURN 107 111 FT TURN 114 115 FT HELIX 117 137 FT HELIX 140 164 FT TURN 167 168 FT HELIX 170 185 FT TURN 186 186 FT HELIX 190 206 FT HELIX 207 210 FT TURN 213 215 FT HELIX 216 234 SQ SEQUENCE 246 AA; 28219 MW; D70FBC100C45D6E5 CRC64; MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LSLLDKFLIK NCNDFQYESK VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEQMQPTHP IRLGLALNFS VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN // ID 1433F_MOUSE Reviewed; 246 AA. AC P68510; P11576; P70198; Q3TGZ9; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 06-FEB-2007, entry version 31. DE 14-3-3 protein eta. GN Name=Ywhah; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PCTK1. RC TISSUE=Brain; RX MEDLINE=97340943; PubMed=9197417; DOI=10.1007/s004380050453; RA Sladeczek F., Camonis J.H., Burnol A.-F., Le Bouffant F.; RT "The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11 RT and 14-3-3 proteins."; RL Mol. Gen. Genet. 254:571-577(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/Sv; RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98411340; PubMed=9738002; DOI=10.1074/jbc.273.39.25356; RA Tang S.J., Seun T.-C., McInnes R.R., Buchwald M.; RT "Association of the TLX-2 homeodomain and 14-3-3eta signaling RT proteins."; RL J. Biol. Chem. 273:25356-25363(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12008017; DOI=10.1016/S0169-328X(02)00129-8; RA Toyooka K., Muratake T., Watanabe H., Hayashi S., Ichikawa T., RA Usui H., Washiyama K., Kumanishi T., Takahashi Y.; RT "Isolation and structure of the mouse 14-3-3 eta chain gene and the RT distribution of 14-3-3 eta mRNA in the mouse brain."; RL Brain Res. Mol. Brain Res. 100:13-20(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Heart, Kidney, 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 [6] 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: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with many nuclear hormone receptors CC and cofactors including AR, ESR1, ESR2, MC2R, NR3C1, NRIP1, PPARBP CC and THRA (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U57311; AAC53256.1; -; mRNA. DR EMBL; D87661; BAA13422.1; -; mRNA. DR EMBL; AF077002; AAC36290.1; -; mRNA. DR EMBL; AB063572; BAB79599.1; -; Genomic_DNA. DR EMBL; AK077596; BAC36887.1; -; mRNA. DR EMBL; AK149224; BAE28768.1; -; mRNA. DR EMBL; AK168520; BAE40399.1; -; mRNA. DR EMBL; AK169035; BAE40826.1; -; mRNA. DR EMBL; AK169189; BAE40965.1; -; mRNA. DR EMBL; BC008187; AAH08187.1; -; mRNA. DR EMBL; BC061497; AAH61497.1; -; mRNA. DR UniGene; Mm.332314; -. DR HSSP; P93343; 1O9E. DR SMR; P68510; 2-236. DR IntAct; P68510; -. DR KEGG; mmu:22629; -. DR MGI; MGI:109194; Ywhah. DR GermOnline; ENSMUSG00000018965; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0003779; F:actin binding; IDA:ProtInc. DR GO; GO:0035259; F:glucocorticoid receptor binding; ISS:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI. DR GO; GO:0016563; F:transcriptional activator activity; ISS:UniProtKB. DR GO; GO:0007010; P:cytoskeleton organization and biogenesis; NAS:ProtInc. DR GO; GO:0006713; P:glucocorticoid catabolic process; ISS:UniProtKB. DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IDA:MGI. DR GO; GO:0043066; P:negative regulation of apoptosis; NAS:ProtInc. DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IDA:MGI. DR GO; GO:0045941; P:positive regulation of transcription; ISS:UniProtKB. DR GO; GO:0007088; P:regulation of mitosis; NAS:ProtInc. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Phosphorylation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 246 14-3-3 protein eta. FT /FTId=PRO_0000058624. FT MOD_RES 2 2 N-acetylglycine (By similarity). FT CONFLICT 15 16 EQ -> DE (in Ref. 2). SQ SEQUENCE 246 AA; 28212 MW; C12F62B4ABA76DA3 CRC64; MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LALLDKFLIK NCNDFQYESK VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEHMQPTHP IRLGLALNFS VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN // ID 1433F_RAT Reviewed; 246 AA. AC P68511; P11576; P70198; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 26. DE 14-3-3 protein eta. GN Name=Ywhah; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91304265; PubMed=1649368; DOI=10.1016/0169-328X(91)90105-7; RA Watanabe M., Isobe T., Okuyama T., Ichimura T., Kuwano R., RA Takahashi Y., Kondo H.; RT "Molecular cloning of cDNA to rat 14-3-3 eta chain polypeptide and the RT neuronal expression of the mRNA in the central nervous system."; RL Brain Res. Mol. Brain Res. 10:151-158(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with many nuclear hormone receptors CC and cofactors including AR, ESR1, ESR2, MC2R, NR3C1, NRIP1, PPARBP CC and THRA (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 14-3-3 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; D17445; BAA04259.1; -; mRNA. DR EMBL; BC081825; AAH81825.1; -; mRNA. DR PIR; A60031; A60031. DR UniGene; Rn.3324; -. DR HSSP; P93343; 1O9E. DR SMR; P68511; 2-236. DR IntAct; P68511; -. DR Ensembl; ENSRNOG00000026119; Rattus norvegicus. DR KEGG; rno:25576; -. DR RGD; 3978; Ywhah. DR ArrayExpress; P68511; -. DR GermOnline; ENSRNOG00000026119; Rattus norvegicus. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Phosphorylation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 246 14-3-3 protein eta. FT /FTId=PRO_0000058625. FT MOD_RES 2 2 N-acetylglycine (By similarity). SQ SEQUENCE 246 AA; 28212 MW; C12F62B4ABA76DA3 CRC64; MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LALLDKFLIK NCNDFQYESK VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEHMQPTHP IRLGLALNFS VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN // ID 1433F_TOBAC Reviewed; 258 AA. AC O49998; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 28-NOV-2006, entry version 29. DE 14-3-3-like protein F. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98105599; PubMed=9443388; DOI=10.1007/s004250050238; RA Piotrowski M., Oecking C.; RT "Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for RT the phylogeny of plant 14-3-3 proteins."; RL Planta 204:127-130(1998). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U91727; AAC49895.1; -; mRNA. DR PIR; T04131; T04131. DR HSSP; P93343; 1O9E. DR SMR; O49998; 3-237. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 258 14-3-3-like protein F. FT /FTId=PRO_0000058712. SQ SEQUENCE 258 AA; 29226 MW; 7A1DF2A7056F94E0 CRC64; MSSSRDEFVY MAKLAEQAER YEEMVDFMEK VVTAADGGEE LTIEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVTSIKTYR SKIESELTSI CNGILKLLDS NLIRAASTGD SKVFYLKMKG DYHRYLAEFK TGAERKEAAE NTLSSYKSAQ DIANAELAPT HPIRLGLALN FSVFYYEILN SPDRACNLAK QAFDEAIAEL DTLGEESYKD STLIMQLLRD NLTLWTSDMQ DEGTEEMKEV AKPDNEEH // ID 1433G_BOVIN Reviewed; 247 AA. AC P68252; P29359; DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 22. DE 14-3-3 protein gamma (Protein kinase C inhibitor protein 1) (KCIP-1). GN Name=YWHAG; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J., RA McConnell D.G.; RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 2-246. RX MEDLINE=91108808; PubMed=1671102; RA Isobe T., Ichimura T., Sunaya T., Okuyama T., Takahashi N., Kuwano R., RA Takahashi Y.; RT "Distinct forms of the protein kinase-dependent activator of tyrosine RT and tryptophan hydroxylases."; RL J. Mol. Biol. 217:125-132(1991). RN [3] RP FUNCTION. RX PubMed=7931346; RA Tanji M., Horwitz R., Rosenfeld G., Waymire J.C.; RT "Activation of protein kinase C by purified bovine brain 14-3-3: RT comparison with tyrosine hydroxylase activation."; RL J. Neurochem. 63:1908-1916(1994). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with RAF1 and SSH1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF043737; AAC02091.1; -; mRNA. DR UniGene; Bt.2814; -. DR HSSP; P93343; 1O9E. DR SMR; P68252; 2-234. DR KEGG; bta:286862; -. DR GO; GO:0005737; C:cytoplasm; ISS:ProtInc. DR GO; GO:0003779; F:actin binding; ISS:ProtInc. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; ISS:AgBase. DR GO; GO:0008426; F:protein kinase C inhibitor activity; ISS:UniProtKB. DR GO; GO:0007010; P:cytoskeleton organization and biogenesis; ISS:ProtInc. DR GO; GO:0043066; P:negative regulation of apoptosis; ISS:ProtInc. DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB. DR GO; GO:0006605; P:protein targeting; ISS:AgBase. DR GO; GO:0007088; P:regulation of mitosis; ISS:ProtInc. DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:0009966; P:regulation of signal transduction; ISS:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Direct protein sequencing; Phosphorylation. FT INIT_MET 1 1 Removed. FT CHAIN 2 247 14-3-3 protein gamma. FT /FTId=PRO_0000058605. FT MOD_RES 2 2 N-acetylvaline. SQ SEQUENCE 247 AA; 28253 MW; A481633DFAF4455D CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQIESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN // ID 1433G_CHICK Reviewed; 247 AA. AC Q5F3W6; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 28-NOV-2006, entry version 13. DE 14-3-3 protein gamma. GN Name=YWHAG; ORFNames=RCJMB04_5e12; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., RA Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., RA Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AJ851534; CAH65168.1; -; mRNA. DR UniGene; Gga.9354; -. DR SMR; Q5F3W6; 2-234. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 247 14-3-3 protein gamma. FT /FTId=PRO_0000058611. SQ SEQUENCE 247 AA; 28231 MW; 86E57A78A1D6455F CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELGAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN // ID 1433G_HUMAN Reviewed; 247 AA. AC P61981; O70457; P35214; Q6FH52; Q9UDP2; Q9UN99; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 06-FEB-2007, entry version 38. DE 14-3-3 protein gamma (Protein kinase C inhibitor protein 1) (KCIP-1). GN Name=YWHAG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, AND INTERACTION WITH RP RAF1. RC TISSUE=Vascular smooth muscle; RX MEDLINE=99360936; PubMed=10433554; DOI=10.1089/104454999315105; RA Autieri M.V., Carbone C.J.; RT "14-3-3gamma interacts with and is phosphorylated by multiple protein RT kinase C isoforms in PDGF-stimulated human vascular smooth muscle RT cells."; RL DNA Cell Biol. 18:555-564(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX MEDLINE=99417686; PubMed=10486217; DOI=10.1006/geno.1999.5887; RA Horie M., Suzuki M., Takahashi E., Tanigami A.; RT "Cloning, expression, and chromosomal mapping of the human 14-3-3gamma RT gene (YWHAG) to 7q11.23."; RL Genomics 60:241-243(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Endometrial 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 PROTEIN SEQUENCE OF 2-12. RC TISSUE=Platelet; RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP PROTEIN SEQUENCE OF 2-10; 13-19; 29-42; 62-69; 133-143 AND 218-227, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND MASS RP SPECTROMETRY. RC TISSUE=Platelet; RA Bienvenut W.V., Claeys D.; RL Unpublished observations (NOV-2005). RN [8] RP INTERACTION WITH SSH1. RX PubMed=15159416; DOI=10.1083/jcb.200401136; RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; RT "A pathway of neuregulin-induced activation of cofilin-phosphatase RT Slingshot and cofilin in lamellipodia."; RL J. Cell Biol. 165:465-471(2004). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with RAF1 and SSH1. CC -!- INTERACTION: CC P46527:CDKN1B; NbExp=1; IntAct=EBI-359832, EBI-519280; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in brain, skeletal muscle, CC and heart. CC -!- PTM: Phosphorylated by various PKC isozymes. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF142498; AAD48408.1; -; mRNA. DR EMBL; AB024334; BAA85184.1; -; mRNA. DR EMBL; CR541904; CAG46702.1; -; mRNA. DR EMBL; CR541925; CAG46723.1; -; mRNA. DR EMBL; AC006388; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC020963; AAH20963.1; -; mRNA. DR UniGene; Hs.520974; -. DR PDB; 2B05; X-ray; A/B/C/D/E/F=1-247. DR IntAct; P61981; -. DR Cornea-2DPAGE; P61981; HUMAN. DR REPRODUCTION-2DPAGE; P61981; HUMAN. DR Ensembl; ENSG00000170027; Homo sapiens. DR KEGG; hsa:7532; -. DR HGNC; HGNC:12852; YWHAG. DR MIM; 605356; gene. DR ArrayExpress; P61981; -. DR GermOnline; ENSG00000170027; Homo sapiens. DR RZPD-ProtExp; IOH11213; -. DR RZPD-ProtExp; RZPDo834F1133; -. DR RZPD-ProtExp; RZPDo834H0133; -. DR RZPD-ProtExp; T4084; -. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:UniProtKB. DR GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB. DR GO; GO:0008426; F:protein kinase C inhibitor activity; NAS:UniProtKB. DR GO; GO:0006469; P:negative regulation of protein kinase activity; NAS:UniProtKB. DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:UniProtKB. DR GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW 3D-structure; Acetylation; Direct protein sequencing; Phosphorylation. FT INIT_MET 1 1 Removed. FT CHAIN 2 247 14-3-3 protein gamma. FT /FTId=PRO_0000058606. FT MOD_RES 2 2 N-acetylvaline. FT CONFLICT 4 4 R -> P (in Ref. 1). FT CONFLICT 19 19 R -> G (in Ref. 1). FT CONFLICT 78 78 Missing (in Ref. 1). FT CONFLICT 89 89 I -> V (in Ref. 1). FT CONFLICT 104 104 L -> V (in Ref. 1). FT CONFLICT 109 109 I -> Y (in Ref. 1). FT CONFLICT 119 122 SKVF -> RKDL (in Ref. 1). FT CONFLICT 144 145 AT -> GD (in Ref. 1). FT CONFLICT 157 158 AH -> R (in Ref. 1). FT CONFLICT 200 202 AFD -> EFE (in Ref. 1). FT CONFLICT 214 214 D -> E (in Ref. 1). FT CONFLICT 240 240 D -> DH (in Ref. 1). FT HELIX 4 16 FT TURN 17 18 FT HELIX 20 31 FT TURN 32 33 FT HELIX 39 73 FT TURN 74 74 FT HELIX 76 106 FT TURN 107 111 FT TURN 114 115 FT HELIX 117 137 FT HELIX 140 164 FT TURN 167 168 FT HELIX 170 185 FT TURN 186 186 FT HELIX 190 206 FT TURN 207 207 FT HELIX 208 210 FT TURN 213 215 FT HELIX 216 233 SQ SEQUENCE 247 AA; 28303 MW; B0D16C6DE1F4455D CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN // ID 1433G_MOUSE Reviewed; 247 AA. AC P61982; O70457; P35214; Q3UFD6; Q4FK44; Q9UDP2; Q9UN99; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 32. DE 14-3-3 protein gamma. GN Name=Ywhag; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RA Karpitskiy V.V., Shaw A.S.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [2] 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 [3] 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 [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: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with RAF1 and SSH1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- PTM: Phosphorylated by various PKC isozymes (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF058799; AAC14345.1; -; mRNA. DR EMBL; CT010208; CAJ18416.1; -; mRNA. DR EMBL; AK088847; BAC40609.1; -; mRNA. DR EMBL; AK148618; BAE28625.1; ALT_INIT; mRNA. DR EMBL; AK153307; BAE31888.1; -; mRNA. DR EMBL; AK164356; BAE37756.1; -; mRNA. DR EMBL; BC008129; AAH08129.1; -; mRNA. DR UniGene; Mm.233813; -. DR HSSP; P93343; 1O9E. DR SMR; P61982; 2-234. DR IntAct; P61982; -. DR Ensembl; ENSMUSG00000051391; Mus musculus. DR KEGG; mmu:22628; -. DR MGI; MGI:108109; Ywhag. DR ArrayExpress; P61982; -. DR GermOnline; ENSMUSG00000051391; Mus musculus. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI. DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB. DR GO; GO:0008426; F:protein kinase C inhibitor activity; ISS:UniProtKB. DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB. DR GO; GO:0006605; P:protein targeting; IDA:MGI. DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:0009966; P:regulation of signal transduction; ISS:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Phosphorylation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 247 14-3-3 protein gamma. FT /FTId=PRO_0000058607. FT MOD_RES 2 2 N-acetylvaline (By similarity). FT CONFLICT 150 150 S -> F (in Ref. 1). SQ SEQUENCE 247 AA; 28303 MW; B0D16C6DE1F4455D CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN // ID 1433G_PONPY Reviewed; 247 AA. AC Q5RC20; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 18. DE 14-3-3 protein gamma. GN Name=YWHAG; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with RAF1 and SSH1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- PTM: Phosphorylated by various PKC isozymes (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; CR858462; CAH90690.1; -; mRNA. DR SMR; Q5RC20; 2-234. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Phosphorylation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 247 14-3-3 protein gamma. FT /FTId=PRO_0000058608. FT MOD_RES 2 2 N-acetylvaline (By similarity). SQ SEQUENCE 247 AA; 28303 MW; B0D16C6DE1F4455D CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN // ID 1433G_RAT Reviewed; 247 AA. AC P61983; O70457; P35214; Q9UDP2; Q9UN99; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 06-FEB-2007, entry version 30. DE 14-3-3 protein gamma. GN Name=Ywhag; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=Brown Norway, and Wistar; TISSUE=Brain; RX MEDLINE=93164855; PubMed=8381897; DOI=10.1016/0169-328X(93)90082-Z; RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H.; RT "Molecular cloning of rat cDNAs for beta and gamma subtypes of 14-3-3 RT protein and developmental changes in expression of their mRNAs in the RT nervous system."; RL Brain Res. Mol. Brain Res. 17:135-146(1993). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with RAF1 and SSH1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Localized in neurons, and axonally transported CC to the nerve terminals. May be also present, at lower levels, in CC various other tissues. CC -!- PTM: Phosphorylated by various PKC isozymes (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; D17447; BAA04261.1; -; mRNA. DR EMBL; S55305; AAA13844.1; -; mRNA. DR PIR; B49023; B49023. DR UniGene; Rn.29936; -. DR HSSP; P93343; 1O9E. DR SMR; P61983; 2-234. DR IntAct; P61983; -. DR Ensembl; ENSRNOG00000001436; Rattus norvegicus. DR KEGG; rno:56010; -. DR RGD; 62002; Ywhag. DR ArrayExpress; P61983; -. DR GermOnline; ENSRNOG00000001436; Rattus norvegicus. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB. DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB. DR GO; GO:0008426; F:protein kinase C inhibitor activity; ISS:UniProtKB. DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB. DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:0009966; P:regulation of signal transduction; ISS:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Phosphorylation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 247 14-3-3 protein gamma. FT /FTId=PRO_0000058609. FT MOD_RES 2 2 N-acetylvaline (By similarity). SQ SEQUENCE 247 AA; 28303 MW; B0D16C6DE1F4455D CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN // ID 1433S_BOVIN Reviewed; 248 AA. AC Q0VC36; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 20-FEB-2007, entry version 6. DE 14-3-3 protein sigma (Stratifin). GN Name=SFN; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal skin; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer. Found in a complex with XPO7, EIF4A1, ARHGAP1, CC VPS26A, VPS29, VPS35 and SFN (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Secreted protein CC (By similarity). Note=May be secreted by a non-classical secretory CC pathway (By similarity). CC -!- MISCELLANEOUS: 14-3-3 proteins have been shown to be PKC CC activators, but this effect could be non-specific and only due to CC the acidic nature of the protein. CC -!- SIMILARITY: Belongs to the 14-3-3 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; BC120373; AAI20374.1; -; mRNA. DR UniGene; Bt.9957; -. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Phosphorylation. FT CHAIN 1 248 14-3-3 protein sigma. FT /FTId=PRO_0000262593. FT MOD_RES 64 64 Phosphoserine (By similarity). FT MOD_RES 216 216 Phosphoserine (By similarity). FT MOD_RES 248 248 Phosphoserine (By similarity). SQ SEQUENCE 248 AA; 27849 MW; F1166FB40B23A9B3 CRC64; MERASLIQKA KLAEQAERYE DMAAFMKSAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EESSEEKGPE VQEYREKVET ELRGVCDTVL GLLDTHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPEEPQS // ID 1433S_HUMAN Reviewed; 248 AA. AC P31947; Q6FH30; Q6FH51; Q96DH0; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 06-FEB-2007, entry version 74. DE 14-3-3 protein sigma (Stratifin) (Epithelial cell marker protein 1). GN Name=SFN; Synonyms=HME1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Keratinocyte; RX MEDLINE=93294871; PubMed=8515476; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX MEDLINE=93002614; PubMed=1390337; RA Prasad G.L., Valverius E.M., McDuffie E., Cooper H.L.; RT "Complementary DNA cloning of a novel epithelial cell marker protein, RT HME1, that may be down-regulated in neoplastic mammary cells."; RL Cell Growth Differ. 3:507-513(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RX MEDLINE=98324083; PubMed=9659898; DOI=10.1016/S1097-2765(00)80002-7; RA Hermeking H., Lengauer C., Polyak K., He T.-C., Zhang L., RA Thiagalingam S., Kinzler K.W., Vogelstein B.; RT "14-3-3 sigma is a p53-regulated inhibitor of G2/M progression."; RL Mol. Cell 1:3-11(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., RA Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Cervix, Lung, and Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 42-49 AND 118-122. RC TISSUE=Keratinocyte; RX MEDLINE=93162043; PubMed=1286667; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [8] RP IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS26A; VPS29 RP AND VPS35. RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338; RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.; RT "Exportin 7 defines a novel general nuclear export pathway."; RL EMBO J. 23:3227-3236(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASS RP SPECTROMETRY. RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=15731107; DOI=10.1074/jbc.M500982200; RA Wilker E.W., Grant R.A., Artim S.C., Yaffe M.B.; RT "A structural basis for 14-3-3sigma functional specificity."; RL J. Biol. Chem. 280:18891-18898(2005). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- FUNCTION: p53-regulated inhibitor of G2/M progression. CC -!- SUBUNIT: Homodimer (By similarity). Found in a complex with XPO7, CC EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. CC -!- INTERACTION: CC P00519:ABL1; NbExp=1; IntAct=EBI-476295, EBI-375543; CC Q14103-3:HNRPD; NbExp=1; IntAct=EBI-476295, EBI-432539; CC Q14103-4:HNRPD; NbExp=3; IntAct=EBI-476295, EBI-432545; CC O00444:PLK4; NbExp=1; IntAct=EBI-476295, EBI-746202; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted protein. Note=May be CC secreted by a non-classical secretory pathway. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P31947-1; Sequence=Displayed; CC Name=2; CC IsoId=P31947-2; Sequence=VSP_021768; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Present mainly in tissues enriched in CC stratified squamous keratinising epithelium. CC -!- SIMILARITY: Belongs to the 14-3-3 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; X57348; CAA40623.1; -; mRNA. DR EMBL; M93010; AAA59546.1; -; mRNA. DR EMBL; AF029081; AAC52029.1; -; Genomic_DNA. DR EMBL; AF029082; AAC52030.1; -; mRNA. DR EMBL; CR541905; CAG46703.1; -; mRNA. DR EMBL; CR541926; CAG46724.1; -; mRNA. DR EMBL; AL034380; CAB92118.1; -; Genomic_DNA. DR EMBL; BC000329; AAH00329.1; -; mRNA. DR EMBL; BC000995; AAH00995.1; -; mRNA. DR EMBL; BC001550; AAH01550.1; -; mRNA. DR EMBL; BC002995; AAH02995.1; -; mRNA. DR EMBL; BC023552; AAH23552.1; -; mRNA. DR PIR; S34753; S34753. DR PIR; S38956; S38956. DR UniGene; Hs.523718; -. DR PDB; 1YWT; X-ray; A/B=1-248. DR PDB; 1YZ5; X-ray; A/B=1-248. DR IntAct; P31947; -. DR SWISS-2DPAGE; P31947; HUMAN. DR Aarhus/Ghent-2DPAGE; 9109; IEF. DR Cornea-2DPAGE; P31947; HUMAN. DR OGP; P31947; -. DR Ensembl; ENSG00000175793; Homo sapiens. DR KEGG; hsa:2810; -. DR H-InvDB; HIX0000327; -. DR HGNC; HGNC:10773; SFN. DR MIM; 601290; gene. DR LinkHub; P31947; -. DR ArrayExpress; P31947; -. DR GermOnline; ENSG00000175793; Homo sapiens. DR RZPD-ProtExp; IOH11681; -. DR RZPD-ProtExp; RZPDo834E0233; -. DR RZPD-ProtExp; RZPDo834H1133; -. DR RZPD-ProtExp; RZPDo839E0691; -. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0008426; F:protein kinase C inhibitor activity; TAS:ProtInc. DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc. DR GO; GO:0006469; P:negative regulation of protein kinase activity; TAS:ProtInc. DR GO; GO:0000074; P:regulation of progression through cell cycle; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Phosphorylation. FT CHAIN 1 248 14-3-3 protein sigma. FT /FTId=PRO_0000058643. FT MOD_RES 64 64 Phosphoserine (By similarity). FT MOD_RES 216 216 Phosphoserine (By similarity). FT MOD_RES 248 248 Phosphoserine. FT VAR_SEQ 85 116 Missing (in isoform 2). FT /FTId=VSP_021768. FT CONFLICT 77 77 K -> M (in Ref. 4; CAG46703). FT CONFLICT 120 120 Y -> H (in Ref. 2). FT CONFLICT 242 242 A -> V (in Ref. 2). FT HELIX 3 15 FT TURN 16 17 FT HELIX 19 31 FT TURN 32 32 FT HELIX 38 66 FT HELIX 67 69 FT HELIX 80 104 FT TURN 105 107 FT STRAND 108 110 FT HELIX 114 133 FT TURN 134 134 FT HELIX 137 161 FT TURN 164 165 FT HELIX 167 182 FT TURN 183 183 FT HELIX 187 202 FT TURN 203 204 FT HELIX 205 207 FT TURN 210 212 FT HELIX 213 229 FT TURN 230 230 SQ SEQUENCE 248 AA; 27774 MW; 7F4B44E3AA59ECE6 CRC64; MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPQEPQS // ID 1433S_MOUSE Reviewed; 248 AA. AC O70456; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 23-JAN-2007, entry version 47. DE 14-3-3 protein sigma (Stratifin). GN Name=Sfn; Synonyms=Mkrn3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=FVB/N; RA Karpitskiy V.V., Shaw A.S.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-216, AND MASS RP SPECTROMETRY. RX PubMed=15648052; DOI=10.1002/pmic.200401066; RA Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., RA Hart G.W., Burlingame A.L.; RT "Quantitative analysis of both protein expression and serine / RT threonine post-translational modifications through stable isotope RT labeling with dithiothreitol."; RL Proteomics 5:388-398(2005). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Found in a complex with XPO7, EIF4A1, ARHGAP1, CC VPS26A, VPS29, VPS35 and SFN (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Secreted protein CC (By similarity). Note=May be secreted by a non-classical secretory CC pathway (By similarity). CC -!- MISCELLANEOUS: 14-3-3 proteins have been shown to be PKC CC activators, but this effect could be non-specific and only due to CC the acidic nature of the protein. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF058798; AAC14344.1; -; mRNA. DR UniGene; Mm.44482; -. DR HSSP; P29312; 1A38. DR SMR; O70456; 1-231. DR Ensembl; ENSMUSG00000047281; Mus musculus. DR KEGG; mmu:55948; -. DR MGI; MGI:1891831; Sfn. DR ArrayExpress; O70456; -. DR GermOnline; ENSMUSG00000047281; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI. DR GO; GO:0000079; P:regulation of cyclin-dependent protein kina...; IDA:MGI. DR GO; GO:0043588; P:skin development; IMP:MGI. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Phosphorylation. FT CHAIN 1 248 14-3-3 protein sigma. FT /FTId=PRO_0000058644. FT MOD_RES 64 64 Phosphoserine. FT MOD_RES 216 216 Phosphoserine. SQ SEQUENCE 248 AA; 27713 MW; D433390433FB3F48 CRC64; MERASLIQKA KLAEQAERYE DMAAFMKSAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VKEYREKVET ELRGVCDTVL GLLDSHLIKG AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADSAGEEGG EAPDDPHI // ID 1433S_SHEEP Reviewed; 248 AA. AC O77642; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 12-DEC-2006, entry version 42. DE 14-3-3 protein sigma (Stratifin). GN Name=SFN; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=New Zealand Wiltshire; TISSUE=Skin; RX MEDLINE=20062954; PubMed=10594723; RX DOI=10.1046/j.1523-1747.1999.00775.x; RA Rufaut N.W., Pearson A.J., Nixon A.J., Wheeler T.T., Wilkins R.J.; RT "Identification of differentially expressed genes during a wool RT follicle growth cycle induced by prolactin."; RL J. Invest. Dermatol. 113:865-872(1999). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Found in a complex with XPO7, EIF4A1, ARHGAP1, CC VPS26A, VPS29, VPS35 and SFN (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Cytoplasmic CC or may be secreted by a non-classical secretory pathway (By CC similarity). CC -!- MISCELLANEOUS: 14-3-3 proteins have been shown to be PKC CC activators, but this effect could be non-specific and only due to CC the acidic nature of the protein. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF071008; AAC24036.1; -; mRNA. DR UniGene; Oar.814; -. DR HSSP; P29312; 1A38. DR SMR; O77642; 1-231. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Phosphorylation. FT CHAIN 1 248 14-3-3 protein sigma. FT /FTId=PRO_0000058645. FT MOD_RES 64 64 Phosphoserine (By similarity). FT MOD_RES 216 216 Phosphoserine (By similarity). FT MOD_RES 248 248 Phosphoserine (By similarity). SQ SEQUENCE 248 AA; 27849 MW; F1166FB40B23A9B3 CRC64; MERASLIQKA KLAEQAERYE DMAAFMKSAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EESSEEKGPE VQEYREKVET ELRGVCDTVL GLLDTHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPEEPQS // ID 1433T_BOVIN Reviewed; 245 AA. AC Q3SZI4; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 20-FEB-2007, entry version 12. DE 14-3-3 protein theta. GN Name=YWHAQ; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer. Interacts with PCTK1 and SSH1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; BC102840; AAI02841.1; -; mRNA. DR UniGene; Bt.44924; -. DR SMR; Q3SZI4; 1-230. DR KEGG; bta:617498; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058635. SQ SEQUENCE 245 AA; 27764 MW; 175534325E9E37C4 CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 1433T_CHICK Reviewed; 245 AA. AC Q5ZMD1; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 28-NOV-2006, entry version 15. DE 14-3-3 protein theta. GN Name=YWHAQ; ORFNames=RCJMB04_2i3; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., RA Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., RA Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AJ719453; CAG31112.1; -; mRNA. DR UniGene; Gga.8471; -. DR SMR; Q5ZMD1; 1-230. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058641. SQ SEQUENCE 245 AA; 27782 MW; 35DF8AC951A252A8 CRC64; MDKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKMQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 1433T_HUMAN Reviewed; 245 AA. AC P27348; Q567U5; Q5TZU8; Q9UP48; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 06-FEB-2007, entry version 73. DE 14-3-3 protein theta (14-3-3 protein tau) (14-3-3 protein T-cell) (HS1 DE protein). GN Name=YWHAQ; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=T-cell; RX MEDLINE=91198149; PubMed=2015305; DOI=10.1016/0167-4781(91)90136-A; RA Nielsen P.J.; RT "Primary structure of a human protein kinase regulator protein."; RL Biochim. Biophys. Acta 1088:425-428(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Keratinocyte; RX MEDLINE=93294871; PubMed=8515476; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye, Skin, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 1-18. RC TISSUE=Platelet; RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [6] RP PROTEIN SEQUENCE OF 42-49; 61-68 AND 159-167, AND MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Unpublished observations (MAR-2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-245. RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP TISSUE SPECIFICITY. RX PubMed=11080204; RA Malaspina A., Kaushik N., de Belleroche J.; RT "A 14-3-3 mRNA is up-regulated in amyotrophic lateral sclerosis spinal RT cord."; RL J. Neurochem. 75:2511-2520(2000). RN [9] RP INTERACTION WITH SSH1. RX PubMed=15159416; DOI=10.1083/jcb.200401136; RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; RT "A pathway of neuregulin-induced activation of cofilin-phosphatase RT Slingshot and cofilin in lamellipodia."; RL J. Cell Biol. 165:465-471(2004). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX MEDLINE=95327195; PubMed=7603573; DOI=10.1038/376188a0; RA Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A., RA Gamblin S.J.; RT "Structure of a 14-3-3 protein and implications for coordination of RT multiple signalling pathways."; RL Nature 376:188-191(1995). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Interacts with PCTK1 (By similarity). Homodimer. CC Interacts with SSH1. CC -!- INTERACTION: CC P23945:FSHR; NbExp=1; IntAct=EBI-359854, EBI-848239; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In neurons, axonally CC transported to the nerve terminals. CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain, heart and CC pancreas, and at lower levels in kidney and placenta. Up-regulated CC in the lumbar spinal cord from patients with sporadic amyotrophic CC lateral sclerosis (ALS) compared with controls, with highest CC levels of expression in individuals with predominant lower motor CC neuron involvement. CC -!- SIMILARITY: Belongs to the 14-3-3 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; X56468; CAA39840.1; -; mRNA. DR EMBL; X57347; CAA40622.1; -; mRNA. DR EMBL; BT020014; AAV38817.1; -; mRNA. DR EMBL; BC001197; AAH01197.1; -; mRNA. DR EMBL; BC050601; AAH50601.1; -; mRNA. DR EMBL; BC056867; AAH56867.1; -; mRNA. DR EMBL; BC093019; AAH93019.1; -; mRNA. DR EMBL; AF070556; AAC28640.1; -; mRNA. DR PIR; S15076; S15076. DR UniGene; Hs.74405; -. DR PDB; 2BTP; X-ray; A/B=1-234. DR DIP; DIP:27584N; -. DR IntAct; P27348; -. DR Cornea-2DPAGE; P27348; HUMAN. DR OGP; P27348; -. DR REPRODUCTION-2DPAGE; P27348; HUMAN. DR Ensembl; ENSG00000134308; Homo sapiens. DR KEGG; hsa:10971; -. DR HGNC; HGNC:12854; YWHAQ. DR MIM; 609009; gene. DR LinkHub; P27348; -. DR ArrayExpress; P27348; -. DR GermOnline; ENSG00000134308; Homo sapiens. DR RZPD-ProtExp; A0338; -. DR RZPD-ProtExp; IOH29111; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW 3D-structure; Direct protein sequencing. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058636. FT CONFLICT 136 136 D -> N (in Ref. 3). FT HELIX 3 15 FT TURN 16 17 FT HELIX 19 31 FT TURN 32 32 FT HELIX 38 68 FT HELIX 75 103 FT TURN 104 108 FT HELIX 112 132 FT HELIX 135 159 FT TURN 162 163 FT HELIX 165 180 FT TURN 181 182 FT HELIX 185 201 FT TURN 202 205 FT HELIX 208 227 FT TURN 228 229 SQ SEQUENCE 245 AA; 27764 MW; 175534325E9E37C4 CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 1433T_MOUSE Reviewed; 245 AA. AC P68254; P35216; Q3TW69; Q3UJN5; Q5SP76; Q5U423; Q66JR6; DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 06-FEB-2007, entry version 26. DE 14-3-3 protein theta (14-3-3 protein tau). GN Name=Ywhaq; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH PCTK1. RC TISSUE=Brain; RX MEDLINE=97340943; PubMed=9197417; DOI=10.1007/s004380050453; RA Sladeczek F., Camonis J.H., Burnol A.-F., Le Bouffant F.; RT "The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11 RT and 14-3-3 proteins."; RL Mol. Gen. Genet. 254:571-577(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX MEDLINE=97355226; PubMed=9211421; RX DOI=10.1002/(SICI)1098-2795(199708)47:4<370::AID-MRD3>3.3.CO;2-W; RA Perego L., Berruti G.; RT "Molecular cloning and tissue-specific expression of the mouse RT homologue of the rat brain 14-3-3 theta protein: characterization of RT its cellular and developmental pattern of expression in the male germ RT line."; RL Mol. Reprod. Dev. 47:370-379(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=129/Sv; RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.; RT "14-3-3 family members play an important role in tumorigenic RT transformation of NIH 3T3 cells and retinoic acid-mediated F9 cell RT differentiation."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Amnion, Blastocyst, Bone marrow, and 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RG The mouse genome sequencing consortium; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6, and FVB/N; RC TISSUE=Brain, 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). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Interacts with SSH1 (By similarity). Homodimer. Interacts CC with PCTK1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P68254-1; Sequence=Displayed; CC Name=2; CC IsoId=P68254-2; Sequence=VSP_016340; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the 14-3-3 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; U57312; AAC53257.1; -; mRNA. DR EMBL; U56243; AAB72023.1; -; mRNA. DR EMBL; D87662; BAA13423.1; -; mRNA. DR EMBL; AK145568; BAE26517.1; -; mRNA. DR EMBL; AK146371; BAE27120.1; -; mRNA. DR EMBL; AK150850; BAE29907.1; -; mRNA. DR EMBL; AK151437; BAE30400.1; -; mRNA. DR EMBL; AK151715; BAE30634.1; -; mRNA. DR EMBL; AK151864; BAE30752.1; -; mRNA. DR EMBL; AK159403; BAE35055.1; -; mRNA. DR EMBL; AK159817; BAE35397.1; -; mRNA. DR EMBL; AK163237; BAE37249.1; -; mRNA. DR EMBL; AK167397; BAE39486.1; -; mRNA. DR EMBL; AL929409; CAI25590.1; -; Genomic_DNA. DR EMBL; BC080802; AAH80802.1; ALT_INIT; mRNA. DR EMBL; BC085299; AAH85299.1; ALT_INIT; mRNA. DR EMBL; BC090838; AAH90838.1; -; mRNA. DR EMBL; BC106164; AAI06165.1; -; mRNA. DR UniGene; Mm.289630; -. DR UniGene; Mm.379344; -. DR HSSP; P93343; 1O9E. DR SMR; P68254; 1-230. DR IntAct; P68254; -. DR Ensembl; ENSMUSG00000066598; Mus musculus. DR MGI; MGI:891963; Ywhaq. DR ArrayExpress; P68254; -. DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI. DR GO; GO:0006605; P:protein targeting; IDA:MGI. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:MGI. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Alternative splicing. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058637. FT VAR_SEQ 227 245 LWTSDSAGEECDAAEGAEN -> FTCVELETVSVCFSLLS FT (in isoform 2). FT /FTId=VSP_016340. FT CONFLICT 26 26 M -> I (in Ref. 4; BAE35397). FT CONFLICT 227 227 L -> S (in Ref. 4; BAE27120). SQ SEQUENCE 245 AA; 27778 MW; E30471260E8B366E CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 1433T_PONPY Reviewed; 245 AA. AC Q5RFJ2; Q5RDK2; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 28-NOV-2006, entry version 15. DE 14-3-3 protein theta. GN Name=YWHAQ; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex, and Kidney; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with PCTK1 and SSH1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; CR857164; CAH89465.1; -; mRNA. DR EMBL; CR857905; CAH90155.1; -; mRNA. DR SMR; Q5RFJ2; 1-230. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058638. FT CONFLICT 119 119 L -> P (in Ref. 1; CAH90155). FT CONFLICT 243 243 A -> V (in Ref. 1; CAH89465). SQ SEQUENCE 245 AA; 27764 MW; 175534325E9E37C4 CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 1433T_RABIT Reviewed; 245 AA. AC Q6Q6X0; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-NOV-2006, entry version 19. DE 14-3-3 protein theta (14-3-3 protein tau). GN Name=YWHAQ; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Qian Z., Barmack N.H.; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with PCTK1 and SSH1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AY555574; AAS72303.1; -; mRNA. DR SMR; Q6Q6X0; 1-230. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058639. SQ SEQUENCE 245 AA; 27778 MW; E30471260E8B366E CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 1433T_RAT Reviewed; 245 AA. AC P68255; P35216; DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 23-JAN-2007, entry version 26. DE 14-3-3 protein theta (14-3-3 protein tau). GN Name=Ywhaq; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Brain; RX MEDLINE=95075231; PubMed=7984035; DOI=10.1016/0169-328X(94)90285-2; RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H., RA Inoue Y.; RT "Molecular cloning of rat cDNAs for the zeta and theta subtypes of 14- RT 3-3 protein and differential distributions of their mRNAs in the RT brain."; RL Brain Res. Mol. Brain Res. 25:113-121(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with PCTK1 and SSH1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 14-3-3 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; D17614; BAA04533.1; -; mRNA. DR EMBL; BC062409; AAH62409.1; -; mRNA. DR PIR; I52647; S59927. DR UniGene; Rn.2502; -. DR HSSP; P93343; 1O9E. DR SMR; P68255; 1-230. DR IntAct; P68255; -. DR Ensembl; ENSRNOG00000008104; Rattus norvegicus. DR KEGG; mmu:22630; -. DR RGD; 3979; Ywhaq. DR ArrayExpress; P68255; -. DR GermOnline; ENSRNOG00000008104; Rattus norvegicus. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058640. SQ SEQUENCE 245 AA; 27778 MW; E30471260E8B366E CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 1433T_XENLA Reviewed; 245 AA. AC Q52M98; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 2. DT 28-NOV-2006, entry version 16. DE 14-3-3 protein theta. GN Name=ywhaq; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; BC090156; AAH90156.1; ALT_INIT; mRNA. DR SMR; Q52M98; 1-230. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058642. SQ SEQUENCE 245 AA; 27778 MW; E30471260E8B366E CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 1433X_MAIZE Reviewed; 61 AA. AC P29306; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 09-JAN-2007, entry version 38. DE 14-3-3-like protein (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. B73; RX MEDLINE=94105294; PubMed=8278499; DOI=10.1104/pp.101.1.329; RA Keith C.S., Hoang D.O., Barrett B.M., Feigelman B., Nelson M.C., RA Thai H., Baysdorfer C.; RT "Partial sequence analysis of 130 randomly selected maize cDNA RT clones."; RL Plant Physiol. 101:329-332(1993). CC -!- SIMILARITY: Belongs to the 14-3-3 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; M95066; AAA18553.2; -; mRNA. DR HSSP; P29312; 1A38. DR SMR; P29306; 1-52. DR Gramene; P29306; -. DR MaizeGDB; 25467; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; PARTIAL. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN <1 >61 14-3-3-like protein. FT /FTId=PRO_0000058693. FT NON_TER 1 1 FT NON_TER 61 61 SQ SEQUENCE 61 AA; 6760 MW; E999A5A3079D6FCA CRC64; ILNSPDRACN LAKQAFDEAI SELDSLGEES YKDSTLIMQL LXDNLTLWTS DTNEDGGDEI K // ID 1433Z_BOVIN Reviewed; 245 AA. AC P63103; P29213; P29312; Q3ZCF9; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 20-FEB-2007, entry version 29. DE 14-3-3 protein zeta/delta (Protein kinase C inhibitor protein 1) DE (KCIP-1) (Factor activating exoenzyme S) (FAS). GN Name=YWHAZ; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Brain; RX MEDLINE=92362864; PubMed=1499718; DOI=10.1016/0014-5793(92)81257-M; RA Isobe T., Hiyane Y., Ichimura T., Okuyama T., Takahashi N., Nakajo S., RA Nakaya K.; RT "Activation of protein kinase C by the 14-3-3 proteins homologous with RT Exo1 protein that stimulates calcium-dependent exocytosis."; RL FEBS Lett. 308:121-124(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 104-115; 140-157 RP AND 194-212. RC TISSUE=Brain; RX MEDLINE=93211953; PubMed=8460141; RA Fu H., Coburn J., Collier R.J.; RT "The eukaryotic host factor that activates exoenzyme S of Pseudomonas RT aeruginosa is a member of the 14-3-3 protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 90:2320-2324(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION. RX PubMed=7931346; RA Tanji M., Horwitz R., Rosenfeld G., Waymire J.C.; RT "Activation of protein kinase C by purified bovine brain 14-3-3: RT comparison with tyrosine hydroxylase activation."; RL J. Neurochem. 63:1908-1916(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX MEDLINE=95327196; PubMed=7603574; DOI=10.1038/376191a0; RA Liu D., Blenkowska J., Petosa C., Collier R.J., Fu H., Liddington R.; RT "Crystal structure of the zeta isoform of the 14-3-3 protein."; RL Nature 376:191-194(1995). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC Activates the ADP-ribosyltransferase (exoS) activity of bacterial CC origin. CC -!- SUBUNIT: Homodimer. Interacts with BSPRY, MLLT7/FOXO4, PCTK1 and CC SSH1. Binds to the C-terminal part of WEE1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome (By similarity). CC -!- PTM: Isoform delta differs from isoform zeta in being CC phosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; L07955; AAA30514.1; -; mRNA. DR EMBL; BC102382; AAI02383.1; -; mRNA. DR PIR; A47389; A47389. DR PIR; S65013; S65013. DR UniGene; Bt.64848; -. DR PDB; 1A37; X-ray; A/B=1-245. DR PDB; 1A38; X-ray; A/B=1-245. DR PDB; 1A4O; X-ray; A/B/C/D=1-245. DR KEGG; bta:287022; -. DR LinkHub; P63103; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW 3D-structure; Acetylation; Direct protein sequencing; Phosphorylation. FT CHAIN 1 245 14-3-3 protein zeta/delta. FT /FTId=PRO_0000058626. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 184 184 Phosphoserine (By similarity). FT MOD_RES 232 232 Phosphothreonine (By similarity). FT CONFLICT 25 25 C -> A (in Ref. 1). FT HELIX 3 14 FT TURN 15 17 FT HELIX 19 30 FT TURN 31 33 FT HELIX 38 66 FT HELIX 74 104 FT TURN 105 105 FT HELIX 106 108 FT HELIX 112 131 FT HELIX 136 157 FT TURN 158 159 FT TURN 162 163 FT TURN 165 166 FT HELIX 167 179 FT TURN 180 182 FT HELIX 185 201 FT HELIX 212 225 FT TURN 226 227 SQ SEQUENCE 245 AA; 27745 MW; D464DF2286BBFE60 CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 1433Z_CHICK Reviewed; 245 AA. AC Q5ZKC9; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 28-NOV-2006, entry version 14. DE 14-3-3 protein zeta. GN Name=YWHAZ; ORFNames=RCJMB04_11l21; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., RA Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., RA Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AJ720155; CAG31814.1; -; mRNA. DR UniGene; Gga.4784; -. DR SMR; Q5ZKC9; 1-232. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Phosphorylation. FT CHAIN 1 245 14-3-3 protein zeta. FT /FTId=PRO_0000058632. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 184 184 Phosphoserine (By similarity). SQ SEQUENCE 245 AA; 27775 MW; F2A813EE4B23B42D CRC64; MDKNELVQKA KLAEQAERYD DMASCMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK MKGDYYRYLA EVAAGDDKKG IVEQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 1433Z_DROME Reviewed; 248 AA. AC P29310; O01665; Q0E9D5; Q0E9D6; Q0E9D7; Q8IGB9; Q8MKV5; Q9V5G6; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 20-FEB-2007, entry version 64. DE 14-3-3-like protein (Leonardo protein) (14-3-3 protein zeta). GN Name=14-3-3-zeta; Synonyms=14-3-3, 14-3-3EZ, leo, THAP; GN ORFNames=CG17870; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VI). RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=92241667; PubMed=1349290; DOI=10.1016/0378-1119(92)90394-5; RA Swanson K.D., Ganguly R.; RT "Characterization of a Drosophila melanogaster gene similar to the RT mammalian genes encoding the tyrosine/tryptophan hydroxylase activator RT and protein kinase C inhibitor proteins."; RL Gene 113:183-190(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS RP VI AND VI'). RC STRAIN=Oregon-R; RX MEDLINE=97302964; PubMed=9159395; RA Kockel L., Vorbrueggen G., Jaeckle H., Mlodzik M., Bohmann D.; RT "Requirement for Drosophila 14-3-3 zeta in Raf-dependent photoreceptor RT development."; RL Genes Dev. 11:1140-1147(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP FUNCTION, AND INTERACTION WITH SLOB. RX PubMed=10230800; DOI=10.1016/S0896-6273(00)80739-4; RA Zhou Y., Schopperle W.M., Murrey H., Jaramillo A., Dagan D., RA Griffith L.C., Levitan I.B.; RT "A dynamically regulated 14-3-3, Slob, and Slowpoke potassium channel RT complex in Drosophila presynaptic nerve terminals."; RL Neuron 22:809-818(1999). RN [7] RP HOMODIMERIZATION, AND MUTAGENESIS OF ARG-59 AND ARG-63. RX PubMed=12529354; DOI=10.1074/jbc.M211907200; RA Zhou Y., Reddy S., Murrey H., Fei H., Levitan I.B.; RT "Monomeric 14-3-3 protein is sufficient to modulate the activity of RT the Drosophila slowpoke calcium-dependent potassium channel."; RL J. Biol. Chem. 278:10073-10080(2003). CC -!- FUNCTION: Required in Raf-dependent cell proliferation and CC photoreceptor differentiation during eye development. Acts CC upstream of Raf and downstream of Ras, and is essential for CC viability. Acts as a negative regulator by decreasing its voltage CC sensitivity. CC -!- SUBUNIT: Homodimer; homodimerization is not essential for CC modulating the activity of Slo. Interacts with phosphorylated CC Slob; the interaction with Slob mediates an indirect interaction CC with Slo. CC -!- INTERACTION: CC Q9VKK3:CG16854; NbExp=1; IntAct=EBI-198120, EBI-160025; CC Q9VYF3:HDAC4; NbExp=1; IntAct=EBI-198120, EBI-149766; CC Q9VS36:mei-P22; NbExp=1; IntAct=EBI-198120, EBI-102811; CC Q9V721:phyl; NbExp=1; IntAct=EBI-198120, EBI-77033; CC Q8IPH9:Slob; NbExp=1; IntAct=EBI-198100, EBI-142379; CC Q9V3M9:Tektin-A; NbExp=1; IntAct=EBI-198120, EBI-116269; CC Q9VUR1:Tfb2; NbExp=1; IntAct=EBI-198120, EBI-132746; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=VI; Synonyms=D, E; CC IsoId=P29310-1; Sequence=Displayed; CC Name=VI'; Synonyms=A, B; CC IsoId=P29310-2; Sequence=VSP_000001; CC Name=C; Synonyms=F; CC IsoId=P29310-3; Sequence=VSP_010303, VSP_010304; CC Note=No experimental confirmation available. Ref.5 (AAN71617) CC sequence is in conflict in position: 149:K->E; CC -!- TISSUE SPECIFICITY: Predominantly expressed in the ventral nerve CC cord of the embryo, and in the neural tissues of the head. Also CC found in the region posterior to the morphogenetic furrow of the CC eye imaginal disk where cells differentiate as photoreceptors. CC -!- DEVELOPMENTAL STAGE: Expressed throughout all stages of embryonic CC and larval development. CC -!- SIMILARITY: Belongs to the 14-3-3 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; M77518; AAA28324.1; -; mRNA. DR EMBL; Y12573; CAA73152.1; -; Genomic_DNA. DR EMBL; Y12573; CAA73153.1; -; Genomic_DNA. DR EMBL; AE013599; AAF58843.3; -; Genomic_DNA. DR EMBL; AE013599; AAM71060.1; -; Genomic_DNA. DR EMBL; AE013599; AAM71063.2; -; Genomic_DNA. DR EMBL; BT001855; AAN71617.1; -; mRNA. DR PIR; JC1122; JC1122. DR UniGene; Dm.4705; -. DR HSSP; P93343; 1O9E. DR SMR; P29310; 4-235. DR DIP; DIP:17371N; -. DR IntAct; P29310; -. DR Ensembl; CG17870; Drosophila melanogaster. DR KEGG; dme:Dmel_CG17870; -. DR FlyBase; FBgn0004907; 14-3-3-zeta. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-003789-MONOMER; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-003790-MONOMER; -. DR GermOnline; CG17870; Drosophila melanogaster. DR GO; GO:0005634; C:nucleus; NAS:FlyBase. DR GO; GO:0045172; C:ring canal (sensu Insecta); IDA:FlyBase. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008426; F:protein kinase C inhibitor activity; NAS:FlyBase. DR GO; GO:0007059; P:chromosome segregation; IMP:FlyBase. DR GO; GO:0045448; P:mitotic cell cycle, embryonic; IMP:FlyBase. DR GO; GO:0008355; P:olfactory learning; NAS:FlyBase. DR GO; GO:0048129; P:oocyte microtubule cytoskeleton polarizatio...; IGI:FlyBase. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Alternative splicing; Complete proteome; Developmental protein; KW Differentiation; Neurogenesis. FT CHAIN 1 248 14-3-3-like protein. FT /FTId=PRO_0000058651. FT VAR_SEQ 146 161 DDSQTAYQDAFDISKG -> EDSKKAYQEAFDIAKT (in FT isoform C). FT /FTId=VSP_010303. FT VAR_SEQ 149 161 QTAYQDAFDISKG -> KNAYQEAFDIAKT (in FT isoform VI'). FT /FTId=VSP_000001. FT VAR_SEQ 185 193 LNSPDKACQ -> INSPARACH (in isoform C). FT /FTId=VSP_010304. FT MUTAGEN 59 59 R->A: Abolishes homodimerization but not FT regulatory function on Slo; when FT associated with A-63. FT MUTAGEN 63 63 R->A: Abolishes homodimerization but not FT regulatory function on Slo; when FT associated with A-59. SQ SEQUENCE 248 AA; 28228 MW; C645CF3B10C6701A CRC64; MSTVDKEELV QKAKLAEQSE RYDDMAQAMK SVTETGVELS NEERNLLSVA YKNVVGARRS SWRVISSIEQ KTEASARKQQ LAREYRERVE KELREICYEV LGLLDKYLIP KASNPESKVF YLKMKGDYYR YLAEVATGDA RNTVVDDSQT AYQDAFDISK GKMQPTHPIR LGLALNFSVF YYEILNSPDK ACQLAKQAFD DAIAELDTLN EDSYKDSTLI MQLLRDNLTL WTSDTQGDEA EPQEGGDN // ID 1433Z_HUMAN Reviewed; 245 AA. AC P63104; P29213; P29312; Q32P43; Q5XJ08; Q6GPI2; Q6IN74; Q6NUR9; AC Q6P3U9; Q86V33; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 20-FEB-2007, entry version 39. DE 14-3-3 protein zeta/delta (Protein kinase C inhibitor protein 1) DE (KCIP-1). GN Name=YWHAZ; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX MEDLINE=92250445; PubMed=1577711; RA Zupan L.A., Steffens D.L., Berry C.A., Landt M.L., Gross R.W.; RT "Cloning and expression of a human 14-3-3 protein mediating RT phospholipolysis. Identification of an arachidonoyl-enzyme RT intermediate during catalysis."; RL J. Biol. Chem. 267:8707-8710(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Bone marrow; RX MEDLINE=98173806; PubMed=9512661; DOI=10.1016/S0167-4781(97)00171-1; RA Seluja G.A., Pietromonaco S.F., Elias L.; RT "Two unique 5' untranslated regions in mRNAs encoding human 14-3-3 RT zeta: differential expression in hemopoietic cells."; RL Biochim. Biophys. Acta 1395:281-287(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Colon, Eye, Melanoma, PNS, Skin, Testis, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 1-18. RC TISSUE=Platelet; RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [5] RP PROTEIN SEQUENCE OF 1-9; 12-18; 28-49; 61-68; 86-91; 128-158 AND RP 213-222, ACETYLATION AT MET-1, AND MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma, and Platelet; RA Bienvenut W.V., Potts A., Barblan J., Claeys D., Quadroni M.; RL Unpublished observations (NOV-2005). RN [6] RP INTERACTION WITH SSH1. RX PubMed=15159416; DOI=10.1083/jcb.200401136; RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; RT "A pathway of neuregulin-induced activation of cofilin-phosphatase RT Slingshot and cofilin in lamellipodia."; RL J. Cell Biol. 165:465-471(2004). RN [7] RP INTERACTION WITH MLLT7. RX PubMed=16114898; DOI=10.1021/bi050618r; RA Obsilova V., Vecer J., Herman P., Pabianova A., Sulc M., Teisinger J., RA Boura E., Obsil T.; RT "14-3-3 protein interacts with nuclear localization sequence of RT forkhead transcription factor FoxO4."; RL Biochemistry 44:11608-11617(2005). RN [8] RP INTERACTION WITH SSH1. RX PubMed=15660133; DOI=10.1038/sj.emboj.7600543; RA Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., RA Sarcevic B., Sampath R., Bamburg J.R., Bernard O.; RT "Interplay between components of a novel LIM kinase-slingshot RT phosphatase complex regulates cofilin."; RL EMBO J. 24:473-486(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, AND MASS RP SPECTROMETRY. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [10] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=99417955; PubMed=10488331; DOI=10.1016/S1097-2765(00)80363-9; RA Rittinger K., Budman J., Xu J., Volinia S., Cantley L.C., RA Smerdon S.J., Gamblin S.J., Yaffe M.B.; RT "Structural analysis of 14-3-3 phosphopeptide complexes identifies a RT dual role for the nuclear export signal of 14-3-3 in ligand binding."; RL Mol. Cell 4:153-166(1999). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AANAT. RX PubMed=11336675; DOI=10.1016/S0092-8674(01)00316-6; RA Obsil T., Ghirlando R., Klein D.C., Ganguly S., Dyda F.; RT "Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase RT complex. a role for scaffolding in enzyme regulation."; RL Cell 105:257-267(2001). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HISTONE H3 RP PHOSPHOPEPTIDE. RX PubMed=16246723; DOI=10.1016/j.molcel.2005.08.032; RA Macdonald N., Welburn J.P.I., Noble M.E.M., Nguyen A., Yaffe M.B., RA Clynes D., Moggs J.G., Orphanides G., Thomson S., Edmunds J.W., RA Clayton A.L., Endicott J.A., Mahadevan L.C.; RT "Molecular basis for the recognition of phosphorylated and RT phosphoacetylated histone h3 by 14-3-3."; RL Mol. Cell 20:199-211(2005). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with PCTK1. Binds to the C-terminal CC part of WEE1. Interacts with BSPRY (By similarity). Interacts with CC MLLT7/FOXO4 and SSH1. CC -!- INTERACTION: CC P00519:ABL1; NbExp=1; IntAct=EBI-347088, EBI-375543; CC P23528:CFL1; NbExp=1; IntAct=EBI-347088, EBI-352733; CC Q9NRI5:DISC1; NbExp=2; IntAct=EBI-347088, EBI-529989; CC P00533:EGFR; NbExp=1; IntAct=EBI-347088, EBI-297353; CC Q9Y2K2:KIAA0999; NbExp=2; IntAct=EBI-347088, EBI-1181460; CC Q75MU3:LIMK1; NbExp=1; IntAct=EBI-347088, EBI-445580; CC Q99683:MAP3K5; NbExp=1; IntAct=EBI-347088, EBI-476263; CC Q7KZI7:MARK2; NbExp=1; IntAct=EBI-347088, EBI-516560; CC Q96L34:MARK4; NbExp=1; IntAct=EBI-347088, EBI-302319; CC Q8TEW0:PARD3; NbExp=1; IntAct=EBI-347088, EBI-81968; CC Q9NPB6:PARD6A; NbExp=1; IntAct=EBI-347088, EBI-81876; CC Q9BYG5:PARD6B; NbExp=1; IntAct=EBI-347088, EBI-295391; CC P41743:PRKCI; NbExp=1; IntAct=EBI-347088, EBI-286199; CC P04049:RAF1; NbExp=2; IntAct=EBI-347088, EBI-365996; CC P57059:SNF1LK; NbExp=1; IntAct=EBI-347088, EBI-1181640; CC P84198:VIM (xeno); NbExp=5; IntAct=EBI-347088, EBI-457639; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by CC mass spectrometry in melanosome fractions from stage I to stage CC IV. CC -!- PTM: Isoform delta differs from isoform zeta in being CC phosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC -!- CAUTION: Was originally (Ref.1) thought to have phospholipase A2 CC 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; M86400; AAA36446.1; -; mRNA. DR EMBL; U28964; AAC52052.1; -; mRNA. DR EMBL; BC003623; AAH03623.3; -; mRNA. DR EMBL; BC051814; AAH51814.1; ALT_INIT; mRNA. DR EMBL; BC063824; AAH63824.2; -; mRNA. DR EMBL; BC068456; AAH68456.2; -; mRNA. DR EMBL; BC072426; AAH72426.2; -; mRNA. DR EMBL; BC073141; AAH73141.1; ALT_INIT; mRNA. DR EMBL; BC083508; AAH83508.2; -; mRNA. DR EMBL; BC099904; AAH99904.1; -; mRNA. DR EMBL; BC101483; AAI01484.1; -; mRNA. DR EMBL; BC108281; AAI08282.1; -; mRNA. DR EMBL; BC111951; AAI11952.1; -; mRNA. DR PIR; A38246; PSHUAM. DR UniGene; Hs.492407; -. DR PDB; 1IB1; X-ray; A/B/C/D=1-245. DR PDB; 1QJA; X-ray; A/B=1-245. DR PDB; 1QJB; X-ray; A/B=1-245. DR PDB; 2C1J; X-ray; A=1-245, B=-. DR PDB; 2C1N; X-ray; A/B=1-245. DR IntAct; P63104; -. DR Cornea-2DPAGE; P29312; HUMAN. DR DOSAC-COBS-2DPAGE; P63104; HUMAN. DR OGP; P63104; -. DR REPRODUCTION-2DPAGE; P63104; HUMAN. DR Ensembl; ENSG00000164924; Homo sapiens. DR KEGG; hsa:7534; -. DR HGNC; HGNC:12855; YWHAZ. DR MIM; 601288; gene. DR LinkHub; P63104; -. DR ArrayExpress; P63104; -. DR GermOnline; ENSG00000164924; Homo sapiens. DR RZPD-ProtExp; C0032; -. DR RZPD-ProtExp; IOH3874; -. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0006916; P:anti-apoptosis; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW 3D-structure; Acetylation; Direct protein sequencing; Phosphorylation. FT CHAIN 1 245 14-3-3 protein zeta/delta. FT /FTId=PRO_0000058627. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 184 184 Phosphoserine (By similarity). FT MOD_RES 232 232 Phosphothreonine. FT CONFLICT 22 22 M -> V (in Ref. 3; AAH68456). FT HELIX 3 15 FT TURN 16 17 FT HELIX 19 31 FT TURN 32 32 FT HELIX 38 65 FT HELIX 78 103 FT TURN 104 104 FT HELIX 105 108 FT HELIX 112 131 FT TURN 132 132 FT HELIX 138 159 FT TURN 162 163 FT HELIX 165 180 FT TURN 181 181 FT HELIX 185 201 FT HELIX 203 205 FT TURN 208 210 FT HELIX 211 229 SQ SEQUENCE 245 AA; 27745 MW; D464DF2286BBFE60 CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 1433Z_MOUSE Reviewed; 245 AA. AC P63101; P35215; P70197; P97286; Q3TSF1; Q5EBQ1; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 20-FEB-2007, entry version 35. DE 14-3-3 protein zeta/delta (Protein kinase C inhibitor protein 1) DE (KCIP-1) (SEZ-2). GN Name=Ywhaz; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX MEDLINE=96216731; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/Sv; RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.; RT "14-3-3 family members play an important role in tumorigenic RT transformation of NIH 3T3 cells and retinoic acid-mediated F9 cell RT differentiation."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PCTK1. RX MEDLINE=97340943; PubMed=9197417; DOI=10.1007/s004380050453; RA Sladeczek F., Camonis J.H., Burnol A.-F., Le Bouffant F.; RT "The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11 RT and 14-3-3 proteins."; RL Mol. Gen. Genet. 254:571-577(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH WEE1. RX MEDLINE=97168955; PubMed=9016762; DOI=10.1006/bbrc.1996.5933; RA Honda R., Ohba Y., Yasuda H.; RT "14-3-3 zeta protein binds to the carboxyl half of mouse wee1 RT kinase."; RL Biochem. Biophys. Res. Commun. 230:262-265(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Blastocyst, Bone marrow macrophage, Egg, Embryonic kidney, and RC 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/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: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Interacts with BSPRY, MLLT7/FOXO4 and SSH1 (By CC similarity). Homodimer. Interacts with PCTK1. Binds to the C- CC terminal part of WEE1. CC -!- INTERACTION: CC Q9QWV4:Mlf1; NbExp=1; IntAct=EBI-354751, EBI-354765; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome (By similarity). CC -!- PTM: Isoform delta differs from isoform zeta in being CC phosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; D78647; BAA11464.1; -; mRNA. DR EMBL; D87660; BAA13421.1; -; mRNA. DR EMBL; U79231; AAC53254.1; -; mRNA. DR EMBL; D83037; BAA11751.1; -; mRNA. DR EMBL; AK083368; BAC38887.1; -; mRNA. DR EMBL; AK145657; BAE26570.1; -; mRNA. DR EMBL; AK146800; BAE27442.1; -; mRNA. DR EMBL; AK150381; BAE29512.1; -; mRNA. DR EMBL; AK151900; BAE30783.1; -; mRNA. DR EMBL; AK162099; BAE36724.1; -; mRNA. DR EMBL; AK167128; BAE39275.1; -; mRNA. DR EMBL; BC050891; AAH50891.1; -; mRNA. DR EMBL; BC089334; AAH89334.1; -; mRNA. DR UniGene; Mm.266215; -. DR UniGene; Mm.3360; -. DR UniGene; Mm.433390; -. DR HSSP; P29312; 1QJB. DR SMR; P63101; 1-232. DR IntAct; P63101; -. DR PMMA-2DPAGE; P63101; -. DR Ensembl; ENSMUSG00000022285; Mus musculus. DR MGI; MGI:109484; Ywhaz. DR ArrayExpress; P63101; -. DR GermOnline; ENSMUSG00000022285; Mus musculus. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0019904; F:protein domain specific binding; IDA:UniProtKB. DR GO; GO:0006605; P:protein targeting; IDA:MGI. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Phosphorylation. FT CHAIN 1 245 14-3-3 protein zeta/delta. FT /FTId=PRO_0000058628. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 184 184 Phosphoserine (By similarity). FT MOD_RES 232 232 Phosphothreonine (By similarity). FT CONFLICT 78 78 M -> V (in Ref. 4). FT CONFLICT 139 139 K -> R (in Ref. 5; BAE36724). FT CONFLICT 218 219 MQ -> IE (in Ref. 2). FT CONFLICT 236 236 E -> D (in Ref. 4). SQ SEQUENCE 245 AA; 27771 MW; 2164DF3793B45B7A CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QPESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 1433Z_PONPY Reviewed; 245 AA. AC Q5R651; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 20-FEB-2007, entry version 18. DE 14-3-3 protein zeta/delta. GN Name=YWHAZ; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with BSPRY, MLLT7/FOXO4, PCTK1 and CC SSH1. Binds to the C-terminal part of WEE1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By CC similarity). CC -!- PTM: Isoform delta differs from isoform zeta in being CC phosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; CR860645; CAH92765.1; -; mRNA. DR SMR; Q5R651; 1-232. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Phosphorylation. FT CHAIN 1 245 14-3-3 protein zeta/delta. FT /FTId=PRO_0000058629. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 184 184 Phosphoserine (By similarity). FT MOD_RES 232 232 Phosphothreonine (By similarity). SQ SEQUENCE 245 AA; 27745 MW; D464DF2286BBFE60 CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 1433Z_RAT Reviewed; 245 AA. AC P63102; P35215; P70197; P97286; Q52KK1; Q6IRF4; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 20-FEB-2007, entry version 33. DE 14-3-3 protein zeta/delta (Protein kinase C inhibitor protein 1) DE (KCIP-1) (Mitochondrial import stimulation factor S1 subunit). GN Name=Ywhaz; Synonyms=Msfs1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Brain; RX MEDLINE=95075231; PubMed=7984035; DOI=10.1016/0169-328X(94)90285-2; RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H., RA Inoue Y.; RT "Molecular cloning of rat cDNAs for the zeta and theta subtypes of 14- RT 3-3 protein and differential distributions of their mRNAs in the RT brain."; RL Brain Res. Mol. Brain Res. 25:113-121(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus; RX MEDLINE=97128314; PubMed=8972907; DOI=10.1016/S0378-1119(96)00368-X; RA Murakami K., Situ S.Y., Eshete F.; RT "A gene variation of 14-3-3 zeta isoform in rat hippocampus."; RL Gene 179:245-249(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=95122474; PubMed=7822263; RA Alam R., Hachiya N., Sakaguchi M., Shun-Ichiro K., Iwanaga S., RA Kitajima M., Mihara K., Omura T.; RT "cDNA cloning and characterization of mitochondrial import stimulation RT factor (MSF) purified from rat liver cytosol."; RL J. Biochem. 116:416-425(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 1-9; 12-18; 42-49; 61-68 AND 128-139, ACETYLATION RP AT MET-1, AND MASS SPECTROMETRY. RC TISSUE=Pheochromocytoma; RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.; RL Unpublished observations (AUG-2006). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-245. RC STRAIN=Sprague-Dawley; TISSUE=Pineal gland; RX MEDLINE=94296566; PubMed=8024705; RA Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A., RA Moffet J.R., Namboodiri M.A., Klein D.C.; RT "Cloning and characterization of the epsilon and zeta isoforms of the RT 14-3-3 proteins."; RL DNA Cell Biol. 13:629-640(1994). RN [7] RP PROTEIN SEQUENCE OF 92-115 AND 140-157. RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord; RA Lubec G., Chen W.-Q., Afjehi-Sadat L.; RL Submitted (NOV-2006) to Swiss-Prot. RN [8] RP TISSUE SPECIFICITY, AND INTERACTION WITH BSPRY. RX MEDLINE=22501915; PubMed=12615066; DOI=10.1016/S0006-291X(03)00182-7; RA Birkenfeld J., Kartmann B., Anliker B., Ono K., Schloetcke B., RA Betz H., Roth D.; RT "Characterization of zetin 1/rBSPRY, a novel binding partner of 14-3-3 RT proteins."; RL Biochem. Biophys. Res. Commun. 302:526-533(2003). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with MLLT7/FOXO4, PCTK1 and SSH1. CC Binds to the C-terminal part of WEE1 (By similarity). Interacts CC with BSPRY. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in brain (at protein level). CC -!- PTM: Isoform delta differs from isoform zeta in being CC phosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; D17615; BAA04534.1; -; mRNA. DR EMBL; U37252; AAA80544.1; -; mRNA. DR EMBL; D30740; BAA06402.1; -; mRNA. DR EMBL; BC070941; AAH70941.2; -; mRNA. DR EMBL; BC094305; AAH94305.1; -; mRNA. DR EMBL; L07913; AAC37660.1; -; mRNA. DR PIR; JC2502; JC2502. DR PIR; JC5232; JC5232. DR PIR; S59915; S59915. DR UniGene; Rn.1292; -. DR HSSP; P29312; 1QJB. DR SMR; P63102; 1-232. DR IntAct; P63102; -. DR Ensembl; ENSRNOG00000008195; Rattus norvegicus. DR KEGG; mmu:22631; -. DR RGD; 3980; Ywhaz. DR ArrayExpress; P63102; -. DR GermOnline; ENSRNOG00000008195; Rattus norvegicus. DR GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Direct protein sequencing; Phosphorylation. FT CHAIN 1 245 14-3-3 protein zeta/delta. FT /FTId=PRO_0000058630. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 184 184 Phosphoserine (By similarity). FT MOD_RES 232 232 Phosphothreonine (By similarity). FT CONFLICT 88 88 T -> M (in Ref. 2; AAA80544). FT CONFLICT 109 109 A -> R (in Ref. 6; AAC37660). SQ SEQUENCE 245 AA; 27771 MW; 2164DF3793B45B7A CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QPESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 1433Z_SHEEP Reviewed; 245 AA. AC P29361; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 20-FEB-2007, entry version 52. DE 14-3-3 protein zeta/delta (Protein kinase C inhibitor protein 1) DE (KCIP-1). GN Name=YWHAZ; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Brain; RX MEDLINE=92283271; PubMed=1317796; RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.; RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) RT from sheep brain. Amino acid sequence of phosphorylated forms."; RL Eur. J. Biochem. 206:453-461(1992). RN [2] RP PROTEIN SEQUENCE OF 1-22 AND 122-137. RC TISSUE=Brain; RX MEDLINE=90345949; PubMed=2143472; RA Toker A., Ellis C.A., Sellers L.A., Aitken A.; RT "Protein kinase C inhibitor proteins. Purification from sheep brain RT and sequence similarity to lipocortins and 14-3-3 protein."; RL Eur. J. Biochem. 191:421-429(1990). RN [3] RP PHOSPHORYLATION. RX MEDLINE=95197587; PubMed=7890696; DOI=10.1074/jbc.270.11.5706; RA Aitken A., Howell S., Jones D., Madrazo J., Patel Y.; RT "14-3-3 alpha and delta are the phosphorylated forms of raf-activating RT 14-3-3 beta and zeta. In vivo stoichiometric phosphorylation in brain RT at a Ser-Pro-Glu-Lys motif."; RL J. Biol. Chem. 270:5706-5709(1995). RN [4] RP POST-TRANSLATIONAL MODIFICATIONS. RA Aitken A., Patel Y., Martin H., Jones D., Robinson K., Madrazo J., RA Howell S.; RT "Electrospray mass spectroscopy analysis with online trapping of RT posttranslationally modified mammalian and avian brain 14-3-3 RT isoforms."; RL J. Protein Chem. 13:463-465(1994). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with BSPRY, MLLT7/FOXO4, PCTK1 and CC SSH1. Binds to the C-terminal part of WEE1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome (By similarity). CC -!- PTM: Isoform delta differs from isoform zeta in being CC phosphorylated. CC -!- SIMILARITY: Belongs to the 14-3-3 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 PIR; S23304; S23304. DR HSSP; P29312; 1QJA. DR SMR; P29361; 1-232. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation; Direct protein sequencing; Phosphorylation. FT CHAIN 1 245 14-3-3 protein zeta/delta. FT /FTId=PRO_0000058631. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 184 184 Phosphoserine. FT MOD_RES 232 232 Phosphothreonine (By similarity). SQ SEQUENCE 245 AA; 27856 MW; 292158A893B44CE5 CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNRS QPESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 1433Z_XENLA Reviewed; 245 AA. AC Q91896; O57469; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 2. DT 28-NOV-2006, entry version 37. DE 14-3-3 protein zeta. GN Name=ywhaz; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97341071; PubMed=9197545; DOI=10.1016/S0378-1119(97)00013-9; RA Kousteni S., Tura F., Sweeney G.E., Ramji D.P.; RT "Sequence and expression analysis of a Xenopus laevis cDNA which RT encodes a homologue of mammalian 14-3-3 zeta protein."; RL Gene 190:279-285(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98119747; PubMed=9450960; RA Kumagai A., Yakowec P.S., Dunphy W.G.; RT "14-3-3 proteins act as negative regulators of the mitotic inducer RT Cdc25 in Xenopus egg extracts."; RL Mol. Biol. Cell 9:345-354(1998). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Present in all adult tissues examined with the CC highest levels in the brain. CC -!- SIMILARITY: Belongs to the 14-3-3 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; X95519; CAA64773.1; -; mRNA. DR EMBL; AF033312; AAC41252.1; -; mRNA. DR HSSP; P93343; 1O9E. DR SMR; Q91896; 1-232. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 245 14-3-3 protein zeta. FT /FTId=PRO_0000058633. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT CONFLICT 173 185 NFSVFYYEILNCP -> KLLCVLTNEESSTVQ (in Ref. FT 1). SQ SEQUENCE 245 AA; 27729 MW; 8ACF62C58E68C630 CRC64; MDKNELVQKA KLAEQAERYD DMAACMKRVT EEGGELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQEMSR EYREKIEAEL REICNDVLNL LDKFLIANAT QPESKVFYLK MKGDYYRYLA EVAAGNAKTE IVGQSQKAYQ DAFDISKTEM QPTHPIRLGL ALNFSVFYYE ILNCPDKACA LAKAAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEQG EGGEN // ID 1433Z_XENTR Reviewed; 245 AA. AC Q6P4Z5; Q28CE4; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 21. DE 14-3-3 protein zeta. GN Name=ywhaz; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG Sanger Xenopus tropicalis EST/cDNA project; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 14-3-3 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; CR926430; CAJ82916.1; -; mRNA. DR EMBL; BC063188; AAH63188.1; -; mRNA. DR UniGene; Str.51905; -. DR SMR; Q6P4Z5; 1-232. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 245 14-3-3 protein zeta. FT /FTId=PRO_0000058634. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 245 AA; 27732 MW; 8828727CE522D2FE CRC64; MDKNELVQKA KLAEQAERYD DMAACMKRVT EEGGELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQEMSR EYREKIEAEL REICNDVLNL LDKFLIANAS QPESKVFYLK MKGDYYRYLA EVASGDAKAD IVAQSQKAYQ DAFDISKTEM QPTHPIRLGL ALNFSVFYYE ILNCPEKACS LAKAAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEQG EGGEN // ID 1433_CANAL Reviewed; 264 AA. AC O42766; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 19-DEC-2001, sequence version 2. DT 28-NOV-2006, entry version 30. DE 14-3-3 protein homolog. GN Name=BMH1; Synonyms=BMH; OS Candida albicans (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5476; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=SC5314; RX MEDLINE=21626410; PubMed=11754483; DOI=10.1002/yea.804; RA Cognetti D., Davis D., Sturtevant J.; RT "The Candida albicans 14-3-3 gene, BMH1, is essential for growth."; RL Yeast 19:55-67(2002). CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF038154; AAB96910.2; -; Genomic_DNA. DR HSSP; P93343; 1O9E. DR SMR; O42766; 5-233. DR COMPLUYEAST-2DPAGE; O42766; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 264 14-3-3 protein homolog. FT /FTId=PRO_0000058719. SQ SEQUENCE 264 AA; 29480 MW; 192EC2FFEFD52BB6 CRC64; MPASREDSVY LAKLAEQAER YEEMVENMKA VASSGQELSV EERNLLSVAY KNVIGARRAS WRIVSSIEQK EEAKGNESQV ALIRDYRAKI EAELSKICED ILSVLSDHLI TSAQTGESKV FYYKMKGDYH RYLAEFAIAE KRKEAADLSL EAYKAASDVA VTELPPTHPI RLGLALNFSV FYYEILNSPD RACHLAKQAF DDAVADLETL SEDSYKDSTL IMQLLRDNLT LWTDLSEAPA ATEEQQQSSQ APAAQPTEGK ADQE // ID 1433_CHLRE Reviewed; 259 AA. AC P52908; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 28-NOV-2006, entry version 31. DE 14-3-3-like protein. OS Chlamydomonas reinhardtii. OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cw15; RX MEDLINE=95359208; PubMed=7632738; DOI=10.1016/0167-4781(95)00097-Z; RA Lieblich I., Voigt J.; RT "A Chlamydomonas homologue to the 14-3-3 proteins: cDNA and deduced RT amino acid sequence."; RL Biochim. Biophys. Acta 1263:79-85(1995). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=20461845; PubMed=11004511; DOI=10.1016/S0167-4781(00)00124-X; RA Voigt J., Liebich I., Woestemeyer J., Adam K.H., Marquardt O.; RT "Nucleotide sequence, genomic organization and cell-cycle-dependent RT expression of a Chlamydomonas 14-3-3 gene."; RL Biochim. Biophys. Acta 1492:395-405(2000). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X79445; CAA55964.1; -; mRNA. DR EMBL; Y19105; CAC03467.1; -; Genomic_DNA. DR PIR; S57283; S57283. DR HSSP; P93343; 1O9E. DR SMR; P52908; 4-235. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 259 14-3-3-like protein. FT /FTId=PRO_0000058675. SQ SEQUENCE 259 AA; 29514 MW; 2FE3D203FC8B27A1 CRC64; MAVDREECVY MAKLAEQAER YDEMVEEMKK VAKLVHDQEL SVEERNLLSV AYKNVIGARR ASWRIISSIE QKEEAKGNEE HVQRIRKYRT VVEEELSKIC ASILQLLDDH LIPTASTGES KVFYLKMKGD YHRYLAEFKT GADRKEAAEH TLLAYKAAQD IALVDLPPTH PIRLGLALNF SVFYYEILNS PERACHLAKQ AFDEAIAELD SLGEESYKDS TLIMQLLRDN LTLWTSDMQD PAAGDDREGA DMKVEDAEP // ID 1433_DICDI Reviewed; 252 AA. AC P54632; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 28-NOV-2006, entry version 29. DE 14-3-3-like protein. GN Name=fttB; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Knetsch M.L.W., Ennis H.L., van Heusden P., Snaar-Jagalska B.E.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; X95568; CAA64814.1; -; mRNA. DR HSSP; P93343; 1O9E. DR SMR; P54632; 3-231. DR DictyBase; DDB0001672; fttB. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 252 14-3-3-like protein. FT /FTId=PRO_0000058649. SQ SEQUENCE 252 AA; 28734 MW; 8A5A966E363E3A9A CRC64; MTREENVYMA KLAEQAERYE EMVETMKKVA ELDVELTVEE RNLLSVAYKN VIGARRASWR IISSIEQKEE SKGNENHVKK IKEYKCKVEK ELTDICNDIL EVLESHLIVS SASGESKVFY YKMKGDYFRY LAEFATGNPR KTSAESSLIA YKAASDIAVT ELPPTHPIRL GLALNFSVFY YEILNSPDRA CNLAKTAFDD AIAELDTLSE DSYKDSTLIM QLLRDNLTLW TSDVHNMEKN QDGDDDQNEP GM // ID 1433_EIMTE Reviewed; 277 AA. AC O96436; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 20-FEB-2007, entry version 24. DE 14-3-3 protein. OS Eimeria tenella. OC Eukaryota; Alveolata; Apicomplexa; Coccidia; Eucoccidiorida; OC Eimeriorina; Eimeriidae; Eimeria. OX NCBI_TaxID=5802; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=LS18; RA Myers R.W., Liberator P.A., Allocco J.J., Anderson J.W., Sardana M.K., RA Wood T.L., Griffin P.R., Fujioka H., Schmatz D.M.; RT "14-3-3 protein regulation of protozoan mannitol metabolism via RT inhibition of mannitol-1-phosphate dehydrogenase."; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF055715; AAD02687.1; -; mRNA. DR HSSP; P93343; 1O9E. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 277 14-3-3 protein. FT /FTId=PRO_0000058656. SQ SEQUENCE 277 AA; 31660 MW; 749A6D6A0726E7D5 CRC64; MIEDIKTLRE EHVYRAKLAE QAERYDEMAE AMKNLVENCL DQNNSPPGAK GDELTVEERN LLSVAYKNAV GARRASWRII SSVEQKEANR NHMANKALAA SYRQKVENEL NKICQEILTL LTDKLLPRTT DSESRVFYFK MKGDYYRYIS EFSNEEGKKA SAEQAEESYK RATDTAEAEL PSTHPIRLGL ALNYSVFYYE ILNQPQKACE MAKLAFDDAI TEFDSVSEDS YKDSTLIMQL LRDNLTLWTS DLQTQEQQQQ PVGEGAEAPK VEATEQQ // ID 1433_FUCVE Reviewed; 251 AA. AC Q39757; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 28-NOV-2006, entry version 27. DE 14-3-3-like protein. OS Fucus vesiculosus (Bladder wrack). OC Eukaryota; stramenopiles; Phaeophyceae; Fucales; Fucaceae; Fucus. OX NCBI_TaxID=49266; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Frond tip; RA Nicolaus B.H.H.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; X98886; CAA67389.1; -; mRNA. DR HSSP; P93343; 1O9E. DR SMR; Q39757; 4-230. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; FALSE_NEG. FT CHAIN 1 251 14-3-3-like protein. FT /FTId=PRO_0000058676. SQ SEQUENCE 251 AA; 28170 MW; 749042151B2684B8 CRC64; MASRDDLVYM AKLAEQAERF DEMVDHMKAV AQQPKELSVE ERNLLSVAYK NVIGSRRASW RVISSIEGKD TVSDQLPLIR DYKSKIETEL TDICADILKI IEAELIPNST SEEGKVFYYK MKGDYHRYLA EFQSADERKT SASDALDAYQ LASDHANQDL PPTHPIRLGL ALNFSVFYYE ILNSPDRACG LAKAAFDDAI AELDTLSEES YKDSTLIIMQ LLRDNLTLWT SDQGEAEEAP GNADGTVVED L // ID 1433_HELAN Reviewed; 259 AA. AC O65352; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 28-NOV-2006, entry version 29. DE 14-3-3-like protein. OS Helianthus annuus (Common sunflower). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; OC Heliantheae; Helianthus. OX NCBI_TaxID=4232; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. HA300; TISSUE=Pollen; RA Eliasson A., Hammann P., Steinmetz A.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF066076; AAC17447.1; -; mRNA. DR PIR; T12951; T12951. DR HSSP; P93343; 1O9E. DR SMR; O65352; 6-240. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 259 14-3-3-like protein. FT /FTId=PRO_0000058677. SQ SEQUENCE 259 AA; 28947 MW; B027B91EE9BE3313 CRC64; MAAASSPREE NVYLAKLAEQ AERYEEMVEF MEKVVAAADG GEELTIEERN LLSVAYKNVI GARRASWRII SSIEQKEESR GNEGHVSTIR DYRSKIESEL SSICDGILKV LDSKLIGSAS GGDSKVFYLK MKGDYYRYLA EFKTGDERKL AAENTLSAYK AAQDIANAEL APTHPIRLGL ALNFSVFYYE ILNSPDRACN LAKQAFDEAI AELDTLGEDS YKDSTLIMQL LRDNLTLWTS DMQDDTAEEV KEAPKPDDQ // ID 1433_LILLO Reviewed; 259 AA. AC Q9SP07; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 28-NOV-2006, entry version 23. DE 14-3-3-like protein. OS Lilium longiflorum (Trumpet lily). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Liliales; Liliaceae; Lilium. OX NCBI_TaxID=4690; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pollen; RA Pertl H., Himly M., Gehwolf R., Kriechbaumer R., Strasser D., RA Michalke W., Richter K., Ferreira F., Obermeyer G.; RT "A 14-3-3 protein may be involved in regulation of the plasma membrane RT H+ ATPase during pollen grain germination and tube growth of lily RT pollen."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AF191746; AAF05737.1; -; mRNA. DR HSSP; P93343; 1O9E. DR SMR; Q9SP07; 7-239. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 259 14-3-3-like protein. FT /FTId=PRO_0000058680. SQ SEQUENCE 259 AA; 29253 MW; 392E38B1430B446B CRC64; MSPAEPSREE NVYMAKLAEQ AERYEEMVEF MEKVARTVDT EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NEDHVALIKD YRGKIEAELS KICDGILKLL DSHLVPSSTA PESKVFYLKM KGDYHRYLAE FKSGAERKEA AESTLLAYKS AQDIALAELA PTHPIRLGLA LNFSVFYYEI LNSPDRACNL AKQAFDEAIS ELDTLGEESY KDSTLIMQLL RDNLTLWTSD INEEAGDEIK EASKAVEGQ // ID 1433_MESCR Reviewed; 264 AA. AC P93259; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 28-NOV-2006, entry version 30. DE 14-3-3-like protein (G-box-binding factor). GN Name=GBF; OS Mesembryanthemum crystallinum (Common ice plant). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Aizoaceae; Mesembryanthemum. OX NCBI_TaxID=3544; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Michalowski C.B., Quigley-Landreau F., Bohnert H.J.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is associated with a DNA binding complex that binds to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plant genes. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U80070; AAB40395.1; -; mRNA. DR PIR; T12572; T12572. DR HSSP; P93343; 1O9E. DR SMR; P93259; 5-238. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 264 14-3-3-like protein. FT /FTId=PRO_0000058694. SQ SEQUENCE 264 AA; 29912 MW; E8F2EE8D617435D6 CRC64; MSSESSREEN VYMAKLAEQA ERYEEMVEFM EKVAKMTDTE ELSVEERNLL SVAYKNVIGA RRASWRIISS IEQKEESRGN EDHVSTIKEY RGKIETELSK ICDGILNLLE SHLIPSASTA ESKVFYLKMK GDYHRYLAEF KTGAERKEAA ENTLLAYKSA QDIALAELAP THPIRLGLAL NFSVFYYEIL NSPDRACNLA KQAFDEAISE LDTLGEESYK DSTLIMQLLR DNLTLWTSDN AEEGGDEIKE AAAKRESGEE KPQQ // ID 1433_NEOCA Reviewed; 266 AA. AC Q25538; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 27. DE 14-3-3 protein homolog. OS Neospora caninum. OC Eukaryota; Alveolata; Apicomplexa; Coccidia; Eucoccidiorida; OC Eimeriorina; Sarcocystidae; Neospora. OX NCBI_TaxID=29176; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Nc-1; RX MEDLINE=96258557; PubMed=8992315; DOI=10.1016/0166-6851(95)02530-8; RA Lally N.C., Jenkins M.C., Dubey J.P.; RT "Development of a polymerase chain reaction assay for the diagnosis of RT neosporosis using the Neospora caninum 14-3-3 gene."; RL Mol. Biochem. Parasitol. 75:169-178(1996). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U31542; AAC47012.1; -; mRNA. DR HSSP; P93343; 1O9E. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 266 14-3-3 protein homolog. FT /FTId=PRO_0000058660. FT COMPBIAS 251 254 Poly-Gln. SQ SEQUENCE 266 AA; 30650 MW; 6DA471FE7ECC7C04 CRC64; MAEEIKNLRD EYVYKAKLAE QAERYDEMAE AMKNLVENCL DEQQPKDELS VEERNLLSVA YKNAVGARRA SWRIISSVEQ KELSKQHMQN KALAAEYRQK VEEELNKICH DILQLLTDKL IPKTSDSESK VFYYKMKGDY YRYISEFSGE EGKKQAADQA QESYQKATET AEGHSPATHP IRLGLALNYS VFFYEILNLP QQACEMAKRA FDDAITEFDN VSEDSYKDST LIMQLLRDNL TLWTSDLQAD QQQQEGGEKP AEQADQ // ID 1433_OENHO Reviewed; 260 AA. AC P29307; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 28-NOV-2006, entry version 29. DE 14-3-3-like protein. OS Oenothera hookeri (Hooker's evening primrose). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; Myrtales; Onagraceae; Oenothera. OX NCBI_TaxID=85636; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92128551; PubMed=1733782; DOI=10.1016/0014-5793(92)80384-S; RA Hirsch S., Aitken A., Bertsch U., Soll J.; RT "A plant homologue to mammalian brain 14-3-3 protein and protein RT kinase C inhibitor."; RL FEBS Lett. 296:222-224(1992). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X62838; CAA44642.1; -; mRNA. DR PIR; S20580; S20580. DR HSSP; P93343; 1O9E. DR SMR; P29307; 5-239. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 260 14-3-3-like protein. FT /FTId=PRO_0000058695. SQ SEQUENCE 260 AA; 29256 MW; A333C405F8416291 CRC64; MATAPSPREE NVYLAKLAEQ AERYEEMVEF MEKVCAAADS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NDDHVSTIRD YRSKIETELS NICGGILKLL DSRLIPSAAS GDSKVFYLKM KGDYHRYLAE FKTGAERKEA AESTLSAYKA AQDIANAELA PTHPIRLGLA LNFSVFYYEI LNSPDRACNL ANEAFDEAIA ELDTLEEESY KDSTLIMQLL RDNLTLWTSD MQDDGGDEIK EAAPKPDEQY // ID 1433_PEA Reviewed; 260 AA. AC P46266; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 28-NOV-2006, entry version 31. DE 14-3-3-like protein. OS Pisum sativum (Garden pea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Vicieae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Alaska; RX MEDLINE=95288384; PubMed=7770545; DOI=10.1104/pp.107.4.1481; RA Stankovic B., Garic-Stankovic A., Smith C.M., Davies E.; RT "Isolation, sequencing, and analysis of a 14-3-3 brain protein homolog RT from pea (Pisum sativum L.)."; RL Plant Physiol. 107:1481-1482(1995). CC -!- SIMILARITY: Belongs to the 14-3-3 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; U15036; AAA85817.1; -; mRNA. DR HSSP; P93343; 1O9E. DR SMR; P46266; 6-239. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 260 14-3-3-like protein. FT /FTId=PRO_0000058697. SQ SEQUENCE 260 AA; 29331 MW; 9A5D103E0F87C13A CRC64; MAAAHTPREE NVYMAKLAEQ AERYEEMVEF MEKVSANADS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NEDHVAVIRD YRSKIESELS NICDGILKLL DTRLIPSASS GDSKVFYLKM KGDYHRYLAE FKTGAERKEA AESTLTGYKS AQDIANAELP PTHPIRLGLA LNFSVFYYEI LNSPDRACNL AKQAFDEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD MQDDGADEIK EAAPKADEQQ // ID 1433_SPIOL Reviewed; 220 AA. AC P29308; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 28-NOV-2006, entry version 28. DE 14-3-3-like protein (Fragment). OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Amaranthaceae; Spinacia. OX NCBI_TaxID=3562; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92128551; PubMed=1733782; DOI=10.1016/0014-5793(92)80384-S; RA Hirsch S., Aitken A., Bertsch U., Soll J.; RT "A plant homologue to mammalian brain 14-3-3 protein and protein RT kinase C inhibitor."; RL FEBS Lett. 296:222-224(1992). CC -!- SIMILARITY: Belongs to the 14-3-3 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; X62837; CAA44641.1; -; mRNA. DR PIR; S20581; S20581. DR HSSP; P29312; 1A38. DR SMR; P29308; 1-192. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN <1 220 14-3-3-like protein. FT /FTId=PRO_0000058705. FT NON_TER 1 1 SQ SEQUENCE 220 AA; 24731 MW; E6D91ABC807944DA CRC64; RNLLSVAYKN VVGARRASWR IISSIEQKEE SRGNEDHVSV IRDYRSRIEK ELSDNCDGIL KLLDTKLVPA ASSGDSKVFY LKMKGDYHRY LAEFKTGAQR KEAAESTLTA YKAAQDIANA ELAPTHPIRL GLALNFSVFY YEILNSPDRA CNLAKQAFVE AIAELDTLGE DSYKDSTLIM QLLRDNLTLW TSDMQDEAAD EITEEAAKQQ KAVNNNKIAY // ID 1433_TOBAC Reviewed; 251 AA. AC Q41246; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 28-NOV-2006, entry version 30. DE 14-3-3-like protein. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Wisconsin 38; RX MEDLINE=95093475; PubMed=8000427; RA Chen Z., Fu H., Liu D., Chang P.F., Narasimhan M., Ferl R., RA Hasegawa P.M., Bressan R.A.; RT "A NaCl-regulated plant gene encoding a brain protein homology that RT activates ADP ribosyltransferase and inhibits protein kinase C."; RL Plant J. 6:729-740(1994). CC -!- TISSUE SPECIFICITY: Most abundant in roots and flowers. CC -!- SIMILARITY: Belongs to the 14-3-3 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; S76737; AAB32832.1; -; mRNA. DR PIR; T04101; T04101. DR HSSP; P29312; 1A4O. DR SMR; Q41246; 4-232. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 251 14-3-3-like protein. FT /FTId=PRO_0000058706. SQ SEQUENCE 251 AA; 28667 MW; FC010F3FF8674740 CRC64; MDKEREKQVY LARLAEQAER YDEMVEAMKT VAKMDVELTV EERNLVSVGY KNVIGARRAS WRILSSIEQK EESKGHDQNV KRIKTYQQRV EDELTKYALT LSVIDEHVVP SSTSGESTVF YYKMKGDYYR YLAEFKSGDD RKEAADQSLK AYEAATATAS ADLAPTHPIR LGLALNFSVF YYEILNSPER ACHLAKQAFD EAIAELDSLS EESYKDSTLI MQLLRDNFTL WTSDLEEGGE HSKGDERQGE N // ID 1433_TRIHA Reviewed; 262 AA. AC Q99002; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 28-NOV-2006, entry version 32. DE 14-3-3 protein homolog (Th1433). OS Trichoderma harzianum (Hypocrea lixii). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea. OX NCBI_TaxID=5544; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=P1; RX MEDLINE=96257206; PubMed=8675020; DOI=10.1016/0378-1119(96)00031-5; RA Klemsdal S.S., Hayes C.K., Hjeljord L., Lorito M., Harman G.E., RA Tronsmo A.; RT "Isolation and characterization of a cDNA from Trichoderma harzianum RT P1 encoding a 14-3-3 protein homolog."; RL Gene 171:123-127(1996). CC -!- DEVELOPMENTAL STAGE: Highest expression during the active growth CC period 10-12 hours after germination. CC -!- SIMILARITY: Belongs to the 14-3-3 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; U24158; AAB17101.1; -; mRNA. DR HSSP; P93343; 1O9E. DR SMR; Q99002; 4-231. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 262 14-3-3 protein homolog. FT /FTId=PRO_0000058720. SQ SEQUENCE 262 AA; 29998 MW; 377D1B15E06A2103 CRC64; MGHEDAVYLA KLAEQAERYE EMVENMKIVA SEDRDLTVEE RNLLSVAYKN VIGARRASWR IVTSIEQKEE SKGNSSQVTL IKEYRQKIEN ELAKICDDIL EVLDQHLIPS AKSGESKVFY HKIKGDYHRY LAEFAIGDRR KDSADKSLEA YKAATEVAQT ELPPTHPIRL GLALNFSVFY YEILNAPDQA CHLAKQAFDD AIAELDTLSE ESYKDSTLIM QLLRDNLTLW TSSEAETPAR LMPLLRRRPL LRLPSRRRRA QG // ID 1433_XENLA Reviewed; 235 AA. AC P29309; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 20-FEB-2007, entry version 31. DE 14-3-3-like protein (Fragment). OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92272745; PubMed=1375463; RA Martens G.J., Piosik P.A., Danen E.H.J.; RT "Evolutionary conservation of the 14-3-3 protein."; RL Biochem. Biophys. Res. Commun. 184:1456-1459(1992). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SIMILARITY: Belongs to the 14-3-3 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; M86928; AAA49698.1; -; mRNA. DR PIR; A56757; A56757. DR UniGene; Xl.37147; -. DR HSSP; P29312; 1A38. DR SMR; P29309; 1-222. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN <1 235 14-3-3-like protein. FT /FTId=PRO_0000058646. FT NON_TER 1 1 SQ SEQUENCE 235 AA; 26785 MW; 09928B15D86A3E7A CRC64; AKLSEQAERY DDMAASMKAV TELGAELSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT EGNDKRQQMA REYREKVETE LQDICKDVLD LLDRFLVPNA TPPESKVFYL KMKGDYYRYL SEVASGDSKQ ETVASSQQAY QEAFEISKSE MQPTHPIRLG LALNFSVFYY EILNSPEKAC SLAKSAFDEA IRELDTLNEE SYKDSTLIMQ LLRDNLTLWT SENQGEEADN VEGDN // ID 143B1_BRARE Reviewed; 244 AA. AC Q5PRD0; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 2. DT 20-FEB-2007, entry version 25. DE 14-3-3 protein beta/alpha-1. GN Name=ywhab1; Synonyms=ywhabb; ORFNames=wu:fb80c08; OS Brachydanio rerio (Zebrafish) (Danio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; BC086710; AAH86710.1; ALT_INIT; mRNA. DR UniGene; Dr.105206; -. DR SMR; Q5PRD0; 1-231. DR Ensembl; ENSDARG00000013078; Danio rerio. DR ZFIN; ZDB-GENE-030131-6583; ywhab1. DR ArrayExpress; Q5PRD0; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 244 14-3-3 protein beta/alpha-1. FT /FTId=PRO_0000058602. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 244 AA; 27647 MW; D8421934B4BF17EA CRC64; MDKSDLVQKA KLAEQAERYD DMAASMKAVT EGGVELSNEE RNLLSVAYKN VVGARRSSWR VISSIEQKTE GNEKKQQMAR EYREKIEAEL QEICNDVLGL LEKYLIPNAS QAESKVFYLK MKGDYYRYLS EVASGDSKRT TVENSQKAYQ DAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNTPEQACS LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS ENQGDEGDAG EGEN // ID 143B1_ONCMY Reviewed; 244 AA. AC Q6UFZ9; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-NOV-2006, entry version 14. DE 14-3-3 protein beta/alpha-1 (Protein 14-3-3B1). OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; OC Protacanthopterygii; Salmoniformes; Salmonidae; Oncorhynchus. OX NCBI_TaxID=8022; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, RP AND INDUCTION. RX PubMed=15326212; DOI=10.1242/jeb.01165; RA Koskinen H., Krasnov A., Rexroad C., Gorodilov Y., Afanasyev S., RA Moelsae H.; RT "The 14-3-3 proteins in the teleost fish rainbow trout (Oncorhynchus RT mykiss)."; RL J. Exp. Biol. 207:3361-3368(2004). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in brain, gill, heart, intestine, CC kidney, liver, ovary, skin, spleen and testis. CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Expressed CC in the neural crest, eyes, yolk syncytium, tail bud and caudal CC somites of somitic embryos. Expressed in the neural crest, gill CC covers and gill arches, and the pectoral fins of post-somitic CC embryos. CC -!- INDUCTION: Repressed under stress conditions such as netting. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AY370879; AAQ72487.1; -; mRNA. DR SMR; Q6UFZ9; 1-231. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 244 14-3-3 protein beta/alpha-1. FT /FTId=PRO_0000058603. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 244 AA; 27575 MW; 5D92FAA5E242B092 CRC64; MDKNDLVQKA KLAEQAERYD DMAAAMKAVT EQGGELSNEE RNLLSVAYKN VVGARRSSWR VISSIEQKTE GNEKKQQMAR EYREKIEAEL QDICKDVLAL LDNYLIANAT QAESKVFYLK MKGDYYRYLS EVASGDSKKT TVENSQQAYQ EAFDISKKDM QPTHPIRLGL ALNFSVFYYE ILNSPEQACS LAKAAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS ENQGDEGDAG EGEN // ID 143B2_BRARE Reviewed; 242 AA. AC Q7T356; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 09-JAN-2007, entry version 23. DE 14-3-3 protein beta/alpha-2. GN Name=ywhab2; Synonyms=ywhab, ywhaba; ORFNames=zgc:64092; OS Brachydanio rerio (Zebrafish) (Danio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; BC053247; AAH53247.1; -; mRNA. DR UniGene; Dr.5301; -. DR SMR; Q7T356; 1-231. DR Ensembl; ENSDARG00000015382; Danio rerio. DR ZFIN; ZDB-GENE-040426-2160; ywhab2. DR ArrayExpress; Q7T356; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 242 14-3-3 protein beta/alpha-2. FT /FTId=PRO_0000058601. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 242 AA; 27393 MW; 5F9F0AAA69636022 CRC64; MDKSDLVQKA KLAEQAERYD DMAAAMKAVT EGGVELSNEE RNLLSVAYKN VVGARRSSWR VISSIEQKTE GNEKKQQMAR EYREKIETEL QDICSDVLGL LEKYLIANAS QAESKVFYLK MKGDYYRYLS EVASGDSKAT TVENSQKAYQ DAFDISKKDM QPTHPIRLGL ALNFSVFYYE ILNSPENACQ LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS ENQGEEAGEN EN // ID 143B2_ONCMY Reviewed; 244 AA. AC Q6UFZ8; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-NOV-2006, entry version 14. DE 14-3-3 protein beta/alpha-2 (Protein 14-3-3B2). OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; OC Protacanthopterygii; Salmoniformes; Salmonidae; Oncorhynchus. OX NCBI_TaxID=8022; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, RP AND INDUCTION. RX PubMed=15326212; DOI=10.1242/jeb.01165; RA Koskinen H., Krasnov A., Rexroad C., Gorodilov Y., Afanasyev S., RA Moelsae H.; RT "The 14-3-3 proteins in the teleost fish rainbow trout (Oncorhynchus RT mykiss)."; RL J. Exp. Biol. 207:3361-3368(2004). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in brain, gill, heart, intestine, CC kidney, liver, ovary, skeletal muscle, spleen and testis. CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. CC -!- INDUCTION: Repressed under stress conditions such as netting. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AY370880; AAQ72488.1; -; mRNA. DR SMR; Q6UFZ8; 1-231. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. KW Acetylation. FT CHAIN 1 244 14-3-3 protein beta/alpha-2. FT /FTId=PRO_0000058604. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 244 AA; 27441 MW; 69D32DFFA9DA1F09 CRC64; MDKNDLVQKA KLAEQAERYD DMAGAMKSVT EQGGELSNEE RNLLSVAYKN VVGARRSSWR VISSIEQKTE GNEKKQAMAK EYREKIETEL QDICNDVLGL LDKYLIANAT AAESKVFYLK MKGDYYRYLS EVAAGDAKKT TVDNSQQAYQ DAFDISKKEM QPTHPIRLGL ALNFSVFFYE ILNNPEKACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LKGHLTLWTS ENQGDEGETG EGEN // ID 143BA_XENLA Reviewed; 244 AA. AC Q5XHK2; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 28-NOV-2006, entry version 14. DE 14-3-3 protein beta/alpha-A. GN Name=ywhab-A; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; BC084055; AAH84055.1; -; mRNA. DR SMR; Q5XHK2; 1-231. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 244 14-3-3 protein beta/alpha-A. FT /FTId=PRO_0000058598. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 244 AA; 27759 MW; 99F128ADFA185A77 CRC64; MDKSELVQKA KLSEQAERYD DMAASMKAVT ELGAELSNEE RNLLSVAYKN VVGARRSSWR VISSIEQKTE GNDKRQQMAR EYREKVETEL QDICKDVLDL LDRFLVPNAT PPESKVFYLK MKGDYYRYLS EVASGDSKQE TVASSQQAYQ EAFEISKSEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKSAFDEAI AELDTLNEES YKDSTLIMQL LRDNLTLWTS ENQGEEADNV EGDN // ID 143BB_XENLA Reviewed; 244 AA. AC Q8AVQ3; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 20-FEB-2007, entry version 24. DE 14-3-3 protein beta/alpha-B. GN Name=ywhab-B; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; BC041526; AAH41526.1; -; mRNA. DR UniGene; Xl.3969; -. DR HSSP; P93343; 1O9E. DR SMR; Q8AVQ3; 1-231. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Acetylation. FT CHAIN 1 244 14-3-3 protein beta/alpha-B. FT /FTId=PRO_0000058599. FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 244 AA; 27759 MW; 9153B815F615BB99 CRC64; MDKSELVQKA KLSEQAERYD DMAASMKAVT ELGAELSNEE RNLLSVAYKN VVGARRSSWR VISSIEQKTE GNDKRQQMAR EYREKVETEL QDICKDVLDL LDRFLVPNAT PPESKVFYLK MKGDYYRYLS EVASGDSKQE TVANSQQAYQ EAFEISKSEM QPTHPIRLGL ALNFSVFYYE ILNSPDKACS LAKSAFDEAI AELDTLNEES YKDSTLIMQL LRDNLTLWTS ETQGEEADNV EGDN // ID 143G1_BRARE Reviewed; 247 AA. AC Q6PC29; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 23. DE 14-3-3 protein gamma-1. GN Name=ywhag1; Synonyms=ywhag; ORFNames=zgc:73131; OS Brachydanio rerio (Zebrafish) (Danio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Retina; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; BC059494; AAH59494.1; -; mRNA. DR UniGene; Dr.107091; -. DR SMR; Q6PC29; 2-234. DR Ensembl; ENSDARG00000041067; Danio rerio. DR ZFIN; ZDB-GENE-011115-1; ywhag1. DR ArrayExpress; Q6PC29; -. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 247 14-3-3 protein gamma-1. FT /FTId=PRO_0000058614. SQ SEQUENCE 247 AA; 28235 MW; E572D924CA8DA6A6 CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKSV TELNEALSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELETVCQDV LNLLDNFLIK NCGETQHESK VFYLKMKGDY YRYLAEVATG EKRAAVVESS EKSYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD EGGEGNN // ID 143G1_ONCMY Reviewed; 247 AA. AC Q6UFZ3; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-NOV-2006, entry version 14. DE 14-3-3 protein gamma-1 (Protein 14-3-3G1). OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; OC Protacanthopterygii; Salmoniformes; Salmonidae; Oncorhynchus. OX NCBI_TaxID=8022; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, RP AND INDUCTION. RX PubMed=15326212; DOI=10.1242/jeb.01165; RA Koskinen H., Krasnov A., Rexroad C., Gorodilov Y., Afanasyev S., RA Moelsae H.; RT "The 14-3-3 proteins in the teleost fish rainbow trout (Oncorhynchus RT mykiss)."; RL J. Exp. Biol. 207:3361-3368(2004). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in brain, gill, heart, intestine, CC kidney, liver, ovary, skeletal muscle, spleen and testis. CC -!- DEVELOPMENTAL STAGE: Expressed from late gastrula onwards. CC -!- INDUCTION: Repressed under stress conditions such as netting. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AY370885; AAQ72493.1; -; mRNA. DR SMR; Q6UFZ3; 2-234. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 247 14-3-3 protein gamma-1. FT /FTId=PRO_0000058615. SQ SEQUENCE 247 AA; 28396 MW; D905A7A4ED49C7FE CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKSV TELNEALSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKME MVRAYREKIE KELETVCRDV LNLLDNFLIK NCNETQHESK VFYLKMKGDY YRYLAEVATG EKRVGVVESS EKSYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQZDD EGGETNN // ID 143G2_ONCMY Reviewed; 248 AA. AC Q6UFZ2; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-NOV-2006, entry version 15. DE 14-3-3 protein gamma-2 (Protein 14-3-3G2). OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; OC Protacanthopterygii; Salmoniformes; Salmonidae; Oncorhynchus. OX NCBI_TaxID=8022; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, RP AND INDUCTION. RX PubMed=15326212; DOI=10.1242/jeb.01165; RA Koskinen H., Krasnov A., Rexroad C., Gorodilov Y., Afanasyev S., RA Moelsae H.; RT "The 14-3-3 proteins in the teleost fish rainbow trout (Oncorhynchus RT mykiss)."; RL J. Exp. Biol. 207:3361-3368(2004). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in brain, gill, heart, intestine, CC kidney, liver, ovary, skeletal muscle, spleen and testis. CC -!- DEVELOPMENTAL STAGE: Expressed from the 34 somite stage. CC -!- INDUCTION: Repressed under stress conditions such as netting. CC -!- SIMILARITY: Belongs to the 14-3-3 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; AY370886; AAQ72494.1; -; mRNA. DR SMR; Q6UFZ2; 2-234. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. FT CHAIN 1 248 14-3-3 protein gamma-2. FT /FTId=PRO_0000058616. SQ SEQUENCE 248 AA; 28462 MW; 10E5951473BA38F7 CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKSV TELNEALSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LNLLDNYLIK NCNETQHESK VFYLKMKGDY YRYLAEVATG EKRATVIESS EKAYNEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYQDST LIMQLLRDNL TLWTSDQQDD EGGEGNKD // ID 143GA_XENLA Reviewed; 247 AA. AC Q6PCG0; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 21. DE 14-3-3 protein gamma-A. GN Name=ywhag-A; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; BC059340; AAH59340.1; -; mRNA. DR UniGene; Xl.31784; -. DR SMR; Q6PCG0; 2-234. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 247 14-3-3 protein gamma-A. FT /FTId=PRO_0000058612. SQ SEQUENCE 247 AA; 28274 MW; DB8C6F4673A4F959 CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKAV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELETVCQDV LSLLDNFLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN // ID 143GB_XENLA Reviewed; 247 AA. AC Q6NRY9; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 21. DE 14-3-3 protein gamma-B. GN Name=ywhag-B; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathway. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 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; BC070566; AAH70566.1; -; mRNA. DR UniGene; Xl.47144; -. DR SMR; Q6NRY9; 2-234. DR InterPro; IPR000308; 14-3-3. DR Gene3D; G3DSA:1.20.190.20; 14-3-3; 1. DR PANTHER; PTHR18860; 14-3-3; 1. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT CHAIN 1 247 14-3-3 protein gamma-B. FT /FTId=PRO_0000058613. SQ SEQUENCE 247 AA; 28245 MW; 42CE4F928C85F071 CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKAV TELNEALSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LNLLDNFLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN // ID 14KD_DAUCA Reviewed; 137 AA. AC P14009; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 31-OCT-2006, entry version 42. DE 14 kDa proline-rich protein DC2.15 precursor. OS Daucus carota (Carrot). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; OC Daucinae; Daucus. OX NCBI_TaxID=4039; RN [1] RP NUCLEOTIDE SEQUENCE. RA Aleith F., Richter G.; RT "Gene expression during induction of somatic embryogenesis in carrot RT cell suspensions."; RL Planta 183:17-24(1990). RN [2] RP NUCLEOTIDE SEQUENCE OF 1-8. RA Kaldenhoff R., Holk A., Richter G.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May be connected with the initiation of embryogenesis or CC with the metabolic changes produced by the removal of auxins. CC -!- DEVELOPMENTAL STAGE: Transiently expressed during early CC embryogenesis. CC -!- INDUCTION: By the removal of auxins. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X15436; CAA33476.1; -; mRNA. DR EMBL; X75806; CAA53441.1; -; Genomic_DNA. DR EMBL; X75807; CAA53442.1; -; Genomic_DNA. DR EMBL; X75808; CAA53443.1; -; Genomic_DNA. DR EMBL; X75809; CAA53444.1; -; Genomic_DNA. DR EMBL; X75810; CAA53445.1; -; Genomic_DNA. DR PIR; S35714; S35714. DR HSSP; P24337; 1HYP. DR InterPro; IPR013770; LPT_helical. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR SMART; SM00499; AAI; 1. KW Membrane; Signal; Transmembrane. FT SIGNAL 1 25 Potential. FT CHAIN 26 137 14 kDa proline-rich protein DC2.15. FT /FTId=PRO_0000020572. FT TRANSMEM 88 104 Potential. FT COMPBIAS 30 49 Pro-rich. SQ SEQUENCE 137 AA; 14392 MW; CAED1BDB3949F890 CRC64; MGSKNSASVA LFFTLNILFF ALVSSTEKCP DPYKPKPKPT PKPTPTPYPS AGKCPRDALK LGVCADVLNL VHNVVIGSPP TLPCCSLLEG LVNLEAAVCL CTAIKANILG KNLNLPIALS LVLNNCGKQV PNGFECT // ID 14KD_MYCBO Reviewed; 144 AA. AC P0A5B8; P30223; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 13. DE 14 kDa antigen (16 kDa antigen) (HSP 16.3). GN Name=hspX; OrderedLocusNames=Mb2057c; OS Mycobacterium bovis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1765; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX MEDLINE=22709107; PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., RA Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., RA Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., RA Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). CC -!- SUBCELLULAR LOCATION: Cell wall (By similarity). Note=Probably the CC external side of the cell wall (By similarity). CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) 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; BX248341; CAD96910.1; -; Genomic_DNA. DR GenomeReviews; BX248333_GR; Mb2057c. DR KEGG; mbo:Mb2057c; -. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Complete proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 144 14 kDa antigen. FT /FTId=PRO_0000126010. SQ SEQUENCE 144 AA; 16227 MW; A0C96872035CDDF8 CRC64; MATTLPVQRH PRSLFPEFSE LFAAFPSFAG LRPTFDTRLM RLEDEMKEGR YEVRAELPGV DPDKDVDIMV RDGQLTIKAE RTEQKDFDGR SEFAYGSFVR TVSLPVGADE DDIKATYDKG ILTVSVAVSE GKPTEKHIQI RSTN // ID 14KD_MYCTU Reviewed; 144 AA. AC P0A5B7; P30223; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 15. DE 14 kDa antigen (16 kDa antigen) (HSP 16.3). GN Name=hspX; OrderedLocusNames=Rv2031c, MT2090; ORFNames=MTV018.18c; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv, and ATCC 35801 / TMC 107 / Erdman; RX MEDLINE=92138631; PubMed=1370952; RA Verbon A., Hartskeerl R.A., Schuitema A., Kolk A.H.J., Young D.B., RA Lathigra R.; RT "The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is RT related to the alpha-crystallin family of low-molecular-weight heat RT shock proteins."; RL J. Bacteriol. 174:1352-1359(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). RN [4] RP PROTEIN SEQUENCE OF 2-144, CHARACTERIZATION, AND MASS SPECTROMETRY. RC STRAIN=ATCC 35801 / TMC 107 / Erdman; RX MEDLINE=92225631; PubMed=1563797; RA Lee B.-Y., Hefta S.A., Brennan P.J.; RT "Characterization of the major membrane protein of virulent RT Mycobacterium tuberculosis."; RL Infect. Immun. 60:2066-2074(1992). CC -!- SUBCELLULAR LOCATION: Cell wall. Note=Probably the external side CC of the cell wall. CC -!- MASS SPECTROMETRY: MW=16100; METHOD=Electrospray; RANGE=2-144; CC NOTE=Ref.4. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) 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; S79751; AAB21317.1; -; Genomic_DNA. DR EMBL; M76712; AAA25342.1; -; Genomic_DNA. DR EMBL; BX842578; CAA17245.1; -; Genomic_DNA. DR EMBL; AE000516; AAK46369.1; -; Genomic_DNA. DR PIR; F70942; F70942. DR GenomeReviews; AE000516_GR; MT2090. DR GenomeReviews; AL123456_GR; Rv2031c. DR KEGG; mtc:MT2090; -. DR KEGG; mtu:Rv2031c; -. DR TIGR; MT2090; -. DR TubercuList; Rv2031c; -. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Complete proteome; Direct protein sequencing. FT INIT_MET 1 1 Removed. FT CHAIN 2 144 14 kDa antigen. FT /FTId=PRO_0000126011. SQ SEQUENCE 144 AA; 16227 MW; A0C96872035CDDF8 CRC64; MATTLPVQRH PRSLFPEFSE LFAAFPSFAG LRPTFDTRLM RLEDEMKEGR YEVRAELPGV DPDKDVDIMV RDGQLTIKAE RTEQKDFDGR SEFAYGSFVR TVSLPVGADE DDIKATYDKG ILTVSVAVSE GKPTEKHIQI RSTN // ID 14KD_RHOSH Reviewed; 124 AA. AC P16536; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 31-OCT-2006, entry version 35. DE 14 kDa peptide of ubiquinol-cytochrome c2 oxidoreductase complex. OS Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=1063; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91340695; PubMed=1651916; RA Usui S., Yu L.; RT "Subunit IV (Mr = 14,384) of the cytochrome b-c1 complex from RT Rhodobacter sphaeroides. Cloning, DNA sequencing, and ubiquinone RT binding domain."; RL J. Biol. Chem. 266:15644-15649(1991). RN [2] RP PROTEIN SEQUENCE OF 61-108. RX MEDLINE=90110107; PubMed=2153104; RA Purvis D.J., Theiler R., Niederman R.A.; RT "Chromatographic and protein chemical analysis of the ubiquinol- RT cytochrome c2 oxidoreductase isolated from Rhodobacter sphaeroides."; RL J. Biol. Chem. 265:1208-1215(1990). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M68939; AAA26107.1; -; Genomic_DNA. DR PIR; A40794; A40794. KW Direct protein sequencing; Electron transport; Inner membrane; KW Membrane; Oxidoreductase; Respiratory chain; Transmembrane; Transport. FT CHAIN 1 124 14 kDa peptide of ubiquinol-cytochrome c2 FT oxidoreductase complex. FT /FTId=PRO_0000064353. FT TRANSMEM 85 102 Potential. SQ SEQUENCE 124 AA; 14393 MW; E390C856C1D752F3 CRC64; MFSFIDDIPS FEQIKARVRD DLRKHGWEKR WNDSRLVQKS RELLNDEELK IDPATWIWKR MPSREEVAAR RQRDFETVWK YRYRLGGFAS GALLALALAG IFSTGNFGGS SDAGNRPSVV YPIE // ID 15E2_HUMAN Reviewed; 136 AA. AC O43716; Q3KNR8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 20-FEB-2007, entry version 33. DE Putative protein 15E1.2. GN Name=15E1.2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). 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 -!- SIMILARITY: Belongs to the gatC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL021546; CAA16496.1; -; Genomic_DNA. DR EMBL; BC107145; AAI07146.1; -; mRNA. DR PIR; T09477; T09477. DR UniGene; Hs.369624; -. DR Ensembl; ENSG00000111780; Homo sapiens. DR KEGG; hsa:283459; -. DR LinkHub; O43716; -. DR ArrayExpress; O43716; -. DR GermOnline; ENSG00000111780; Homo sapiens. DR RZPD-ProtExp; F0484; -. DR RZPD-ProtExp; IOH41184; -. DR InterPro; IPR003837; Glu-tRNAGlntrans. DR Pfam; PF02686; Glu-tRNAGln; 1. DR TIGRFAMs; TIGR00135; gatC; 1. KW Hypothetical protein. FT CHAIN 1 136 Putative protein 15E1.2. FT /FTId=PRO_0000105365. SQ SEQUENCE 136 AA; 15086 MW; 113118E9507234E4 CRC64; MWSRLVWLGL RAPLGGRQGF TSKADPQGSG RITAAVIEHL ERLALVDFGS REAVARLEKA IAFADRLRAV DTDGVEPMES VLEDRCLYLR SDNVVEGNCA DELLQNSHRV VEEYFVAPPG NISLPKLDEQ EPFPHS // ID 170K_TRVPS Reviewed; 179 AA. AC P05079; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 20-FEB-2007, entry version 27. DE Putative 170 kDa protein (Fragment). OS Tobacco rattle virus (strain PSG). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Tobravirus. OX NCBI_TaxID=12297; OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet). OH NCBI_TaxID=4072; Capsicum annuum (Bell pepper). OH NCBI_TaxID=82024; Hyacinthus. OH NCBI_TaxID=39639; Narcissus pseudonarcissus (Daffodil). OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco). OH NCBI_TaxID=4113; Solanum tuberosum (Potato). OH NCBI_TaxID=3562; Spinacia oleracea (Spinach). OH NCBI_TaxID=13274; Stellaria media (Common chickweed). OH NCBI_TaxID=13305; Tulipa. OH NCBI_TaxID=97415; Viola arvensis (European field pansy) (Field violet). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX MEDLINE=86176720; PubMed=3960718; DOI=10.1093/nar/14.5.2157; RA Cornelissen B.J.C., Linthorst H.J.M., Brederode F.T., Bol J.F.; RT "Analysis of the genome structure of tobacco rattle virus strain RT PSG."; RL Nucleic Acids Res. 14:2157-2169(1986). CC -!- MISCELLANEOUS: Residues 8 to 173 are identical to residues 86 to CC 251 in strain SYM 194 kDa protein. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X03685; CAA27319.1; -; Genomic_RNA. DR PIR; A05248; A05248. DR InterPro; IPR001788; RNA_dep_RNApol2. DR Pfam; PF00978; RdRP_2; 1. FT CHAIN <1 179 Putative 170 kDa protein. FT /FTId=PRO_0000222513. FT NON_TER 1 1 SQ SEQUENCE 179 AA; 19950 MW; A321512687CA92D4 CRC64; GAHLVPTKSG DADTYNANSD RTLCALLSEL PLEKAVMVTY GGDDSLIAFP RGTQFVDPCP KLATKWNFEC KIFKYDVPMF CGKFLLKTSS CYEFVPDPVK VLTKLGKKSI KDVQHLAEIY ISLNDSNRAL GNYMVVSKLS ESVSDRYLYK GDSVHALCAL WKHIKSFTAL CTLLPRRKG // ID 17KD_RICAM Reviewed; 154 AA. AC P50927; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 29. DE 17 kDa surface antigen precursor (Fragment). GN Name=omp; OS Rickettsia amblyommii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=33989; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MO 85-1084; RA Stothard D.R., Ralph D.A., Clark J.B., Fuerst P.A., Pretzman C.; RT "Rickettsia amblyommii, sp. nov., isolated from the Lone Star tick, RT Amblyomma americanum (Ixodidae)."; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; U11013; AAB07704.1; -; Genomic_DNA. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Lipoprotein; Membrane; Outer membrane; Palmitate; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 >154 17 kDa surface antigen. FT /FTId=PRO_0000018014. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). FT NON_TER 154 154 SQ SEQUENCE 154 AA; 15879 MW; E4FBE4C29D943581 CRC64; MKLLSKIMII ALAASTLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ VGAGMDEQDR RIAELTSQKA LETAPNGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGQ // ID 17KD_RICAU Reviewed; 154 AA. AC P50928; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 29. DE 17 kDa surface antigen precursor (Fragment). GN Name=omp; OS Rickettsia australis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=787; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Baird R.W., Ross B., Dwyer B.; RT "Characterization and comparison of the 17 kilodalton protein of RT Rickettsia australis."; RL Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; M74042; AAA26394.1; -; Genomic_DNA. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Lipoprotein; Membrane; Outer membrane; Palmitate; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 >154 17 kDa surface antigen. FT /FTId=PRO_0000018015. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). FT NON_TER 154 154 SQ SEQUENCE 154 AA; 15967 MW; E3AA833346FAC320 CRC64; MKLLSKIMII ALAASMLQAC NSPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSNGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGQ // ID 17KD_RICBE Reviewed; 159 AA. AC Q84I68; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 20-FEB-2007, entry version 12. DE 17 kDa surface antigen precursor. GN Name=omp; OS Rickettsia bellii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=33990; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=G2D42; RA Stothard D.R., Pretzman C.I., Fuerst P.A., Feng H.-M., Walker D.H., RA Bouyer D.H.; RT "Classification of Rickettsia amblyommii sp. nov. isolated from the RT Lone Star Tick, Amblyomma americanum (Acari:Ixodidae), based upon 17, RT 120 and 130 kilodalton antigen gene phylogenies."; RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; AF445380; AAO38433.1; -; Genomic_DNA. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Lipoprotein; Membrane; Outer membrane; Palmitate; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 159 17 kDa surface antigen. FT /FTId=PRO_0000277890. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 159 AA; 16331 MW; 86BB5171CF09DBE7 CRC64; MKIISKIIVI LLAASMLQAC QGPGGMNKQG SGTLIGGTAG ALLGSQFGGG TGRLAAVGAG ALLGAILGNQ IGAGMDEQDR KLAELTSQRA LEAAPSGSSV QWRNPDNGNY GTVTPSKAYK NNTGQYCREY TQTVVVGGKQ QKAYGTACRQ PDGQWQVVN // ID 17KD_RICBR Reviewed; 159 AA. AC Q1RGK9; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 20-FEB-2007, entry version 8. DE 17 kDa surface antigen precursor. GN Name=omp; OrderedLocusNames=RBE_1424; OS Rickettsia bellii (strain RML369-C). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=336407; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076; RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., RA Fournier P.-E., Claverie J.-M., Raoult D.; RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae RT in gene exchanges between intracellular pathogens."; RL PLoS Genet. 2:E76-E76(2006). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; CP000087; ABE05505.1; -; Genomic_DNA. DR GenomeReviews; CP000087_GR; RBE_1424. DR KEGG; rbe:RBE_1424; -. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Complete proteome; Lipoprotein; Membrane; Outer membrane; Palmitate; KW Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 159 17 kDa surface antigen. FT /FTId=PRO_0000277888. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 159 AA; 16331 MW; 86BB5171CF09DBE7 CRC64; MKIISKIIVI LLAASMLQAC QGPGGMNKQG SGTLIGGTAG ALLGSQFGGG TGRLAAVGAG ALLGAILGNQ IGAGMDEQDR KLAELTSQRA LEAAPSGSSV QWRNPDNGNY GTVTPSKAYK NNTGQYCREY TQTVVVGGKQ QKAYGTACRQ PDGQWQVVN // ID 17KD_RICCA Reviewed; 80 AA. AC P29697; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 30. DE 17 kDa surface antigen (Fragment). GN Name=omp; OS Rickettsia canada. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=788; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92108069; PubMed=1729713; RA Azad A.F., Sacci J.B. Jr., Nelson W.M., Dasch G.A., Schmidtmann E.T., RA Carl M.; RT "Genetic characterization and transovarial transmission of a typhus- RT like rickettsia found in cat fleas."; RL Proc. Natl. Acad. Sci. U.S.A. 89:43-46(1992). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; M82879; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; PARTIAL. KW Lipoprotein; Membrane; Outer membrane. FT CHAIN <1 >80 17 kDa surface antigen. FT /FTId=PRO_0000096159. FT NON_TER 1 1 FT NON_TER 80 80 SQ SEQUENCE 80 AA; 8372 MW; AD289A48EAB19E0E CRC64; GSQFGKGKGQ LIGVGAGALL GAILGNQIGA GMDEQDRRLA ELTSQRALET TPSGTSIEWR NPDNGNYGYV TPSKTYKNST // ID 17KD_RICCN Reviewed; 159 AA. AC P0A3N4; P05372; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-FEB-2007, entry version 13. DE 17 kDa surface antigen precursor. GN Name=omp; OrderedLocusNames=RC1287; OS Rickettsia conorii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=781; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89359171; PubMed=2768201; RA Anderson B.E., Tzianabos T.; RT "Comparative sequence analysis of a genus-common rickettsial antigen RT gene."; RL J. Bacteriol. 171:5199-5201(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX MEDLINE=21442074; PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., RA Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; M28480; AAA26376.1; -; Genomic_DNA. DR EMBL; AE008675; AAL03825.1; -; Genomic_DNA. DR PIR; A33971; A33971. DR PIR; G97860; G97860. DR GenomeReviews; AE006914_GR; RC1287. DR KEGG; rco:RC1287; -. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Complete proteome; Lipoprotein; Membrane; Outer membrane; Palmitate; KW Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 159 17 kDa surface antigen. FT /FTId=PRO_0000018021. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 159 AA; 16581 MW; 206A2BBF74FCE169 CRC64; MKLLSKIMII ALATSMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGQWQVVN // ID 17KD_RICFE Reviewed; 159 AA. AC Q9F9F2; Q4UJW7; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 20-FEB-2007, entry version 21. DE 17 kDa surface antigen precursor. GN Name=omp; OrderedLocusNames=RF_1321; OS Rickettsia felis (Rickettsia azadi). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=42862; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=21217364; PubMed=11321078; RA Bouyer D.H., Stenos J., Crocquet-Valdes P., Moron C.G., Popov V.L., RA Zavala-Velazquez J.E., Foil L.D., Stothard D.R., Azad A.F., RA Walker D.H.; RT "Rickettsia felis: molecular characterization of a new member of the RT spotted fever group."; RL Int. J. Syst. Evol. Microbiol. 51:339-347(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:E248-E248(2005). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; AF195118; AAG28452.1; -; Genomic_DNA. DR EMBL; CP000053; AAY62172.1; -; Genomic_DNA. DR GenomeReviews; CP000053_GR; RF_1321. DR KEGG; rfe:RF_1321; -. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Complete proteome; Lipoprotein; Membrane; Outer membrane; Palmitate; KW Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 159 17 kDa surface antigen. FT /FTId=PRO_0000277889. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 159 AA; 16497 MW; 34C5B020AF470A1F CRC64; MKLLSKIMII ALAASMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LEATPSGTSV EWRNPDNGNH GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGLWQVVN // ID 17KD_RICJA Reviewed; 159 AA. AC Q52764; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 29. DE 17 kDa surface antigen precursor. GN Name=omp; OS Rickettsia japonica. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=35790; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=YH; RX MEDLINE=95229950; PubMed=7714214; RA Furuya Y., Katayama T., Yoshida Y., Kaiho I.; RT "Specific amplification of Rickettsia japonica DNA from clinical RT specimens by PCR."; RL J. Clin. Microbiol. 33:487-489(1995). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; D16515; BAA03965.1; -; Genomic_DNA. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Lipoprotein; Membrane; Outer membrane; Palmitate; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 159 17 kDa surface antigen. FT /FTId=PRO_0000018016. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 159 AA; 16554 MW; CDDCE7CEBDCD6B41 CRC64; MKLLSKIMII ALATSMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG TGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGQWQVVN // ID 17KD_RICMO Reviewed; 154 AA. AC P50929; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 30. DE 17 kDa surface antigen precursor (Fragment). GN Name=omp; OS Rickettsia montana. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=33991; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Ohio 83-441; RA Stothard D.R., Ralph D.A., Clark J.B., Fuerst P.A., Pretzman C.; RT "Rickettsia amblyommii, sp. nov., isolated from the Lone Star tick, RT Amblyomma americanum (Ixodidae)."; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; U11017; AAB07705.1; -; Genomic_DNA. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Lipoprotein; Membrane; Outer membrane; Palmitate; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 >154 17 kDa surface antigen. FT /FTId=PRO_0000018017. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). FT NON_TER 154 154 SQ SEQUENCE 154 AA; 15881 MW; A09C53B8769E31DA CRC64; MKLLSKIMII ALAASMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGQG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACLQ PDGQ // ID 17KD_RICPA Reviewed; 154 AA. AC P50930; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 30. DE 17 kDa surface antigen precursor (Fragment). GN Name=omp; OS Rickettsia parkeri. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=35792; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Maculatum; RA Pretzman C.I., Stothard D.R., Ralph D., Clark J.B., Fuerst P.A.; RT "Rickettsia amblyommii, sp. nov., isolated from the Lone Star tick, RT Amblyomma americanum (Ixodidae)."; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; U17008; AAA82040.1; -; Genomic_DNA. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Lipoprotein; Membrane; Outer membrane; Palmitate; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 >154 17 kDa surface antigen. FT /FTId=PRO_0000018018. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). FT NON_TER 154 154 SQ SEQUENCE 154 AA; 15897 MW; 5D06F45F9DBD5EEC CRC64; MKLLSKIMVI ALATSMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACLQ PDGQ // ID 17KD_RICPR Reviewed; 159 AA. AC P16624; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 2. DT 20-FEB-2007, entry version 44. DE 17 kDa surface antigen precursor. GN Name=omp; OrderedLocusNames=RP833; OS Rickettsia prowazekii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=782; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Madrid E; RX MEDLINE=89359171; PubMed=2768201; RA Anderson B.E., Tzianabos T.; RT "Comparative sequence analysis of a genus-common rickettsial antigen RT gene."; RL J. Bacteriol. 171:5199-5201(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX MEDLINE=99039499; PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., RA Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., RA Eriksson A.-S., Winkler H.H., Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; M28482; AAA26378.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ235273; CAA15258.1; -; Genomic_DNA. DR PIR; D33971; D33971. DR GenomeReviews; AJ235269_GR; RP833. DR KEGG; rpr:RP833; -. DR BioCyc; RPRO782:RP833-MONOMER; -. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Complete proteome; Lipoprotein; Membrane; Outer membrane; Palmitate; KW Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 159 17 kDa surface antigen. FT /FTId=PRO_0000018019. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 159 AA; 16672 MW; A33D404B65EEB071 CRC64; MKLLSKIMII ALAASMLQAC NGQSGMNKQG TGTLLGGAGG ALLGSQFGQG KGQLVGVGVG ALLGAVLGGQ IGASMDEQDR RLLELTSQRA LESAPSGSNI EWRNPDNGNH GYVTPNKTYR NSAGQYCREY TQTVIIGGKQ QKTYGNACRQ PDGQWQVVN // ID 17KD_RICRH Reviewed; 154 AA. AC P50931; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 29. DE 17 kDa surface antigen precursor (Fragment). GN Name=omp; OS Rickettsia rhipicephali. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=33992; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Stothard D.R., Ralph D.A., Clark J.B., Fuerst P.A., Pretzman C.; RT "Rickettsia amblyommii, sp. nov., isolated from the Lone Star tick, RT Amblyomma americanum (Ixodidae)."; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; U11020; AAB07706.1; -; Genomic_DNA. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Lipoprotein; Membrane; Outer membrane; Palmitate; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 >154 17 kDa surface antigen. FT /FTId=PRO_0000018020. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). FT NON_TER 154 154 SQ SEQUENCE 154 AA; 15895 MW; 0CF85AD5D96DFEFB CRC64; MKLLSKIMII ALAASMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYITPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACLQ PDGQ // ID 17KD_RICRI Reviewed; 159 AA. AC P0A3N5; P05372; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-FEB-2007, entry version 11. DE 17 kDa surface antigen precursor. GN Name=omp; OS Rickettsia rickettsii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=783; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87222152; PubMed=3108232; RA Anderson B.E., Regnery R.L., Carlone G.M., Tzianabos T., McDade J.E., RA Fu Z.Y., Bellini W.J.; RT "Sequence analysis of the 17-kilodalton-antigen gene from Rickettsia RT rickettsii."; RL J. Bacteriol. 169:2385-2390(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89359171; PubMed=2768201; RA Anderson B.E., Tzianabos T.; RT "Comparative sequence analysis of a genus-common rickettsial antigen RT gene."; RL J. Bacteriol. 171:5199-5201(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30. RX MEDLINE=89008059; PubMed=3139629; RA Anderson B.E., Baumstark B.R., Bellini W.J.; RT "Expression of the gene encoding the 17-kilodalton antigen from RT Rickettsia rickettsii: transcription and posttranslational RT modification."; RL J. Bacteriol. 170:4493-4500(1988). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; M16486; AAA26381.1; -; Genomic_DNA. DR EMBL; M28479; AAA26379.1; -; Genomic_DNA. DR EMBL; J03371; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A25972; A25972. DR PIR; A31836; A31836. DR PIR; B33971; B33971. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Lipoprotein; Membrane; Outer membrane; Palmitate; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 159 17 kDa surface antigen. FT /FTId=PRO_0000018022. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). FT CONFLICT 146 146 N -> D (in Ref. 2). FT CONFLICT 153 153 G -> E (in Ref. 2). SQ SEQUENCE 159 AA; 16581 MW; 206A2BBF74FCE169 CRC64; MKLLSKIMII ALATSMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGQWQVVN // ID 17KD_RICSI Reviewed; 159 AA. AC Q7PA29; Q84I65; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 20-FEB-2007, entry version 11. DE 17 kDa surface antigen precursor. GN Name=omp; ORFNames=rsib_orf.806; OS Rickettsia sibirica. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group; OC Rickettsia sibirica subgroup. OX NCBI_TaxID=35793; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-151 / 246; RA Malek J.A., Eremeeva M.E., Dasch G.A.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156. RC STRAIN=ATCC VR-151 / 246; RA Stothard D.R., Pretzman C.I., Fuerst P.A., Feng H.-M., Walker D.H., RA Bouyer D.H.; RT "Classification of Rickettsia amblyommii sp. nov. isolated from the RT Lone Star Tick, Amblyomma americanum (Acari:Ixodidae), based upon 17, RT 120 and 130 kilodalton antigen gene phylogenies."; RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; AABW01000001; EAA26008.1; -; Genomic_DNA. DR EMBL; AF445384; AAO38436.1; -; Genomic_DNA. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Lipoprotein; Membrane; Outer membrane; Palmitate; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 159 17 kDa surface antigen. FT /FTId=PRO_0000277891. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 159 AA; 16581 MW; 206A2BBF74FCE169 CRC64; MKLLSKIMII ALATSMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGQWQVVN // ID 17KD_RICTY Reviewed; 159 AA. AC P22882; Q68Y14; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 09-NOV-2004, sequence version 2. DT 20-FEB-2007, entry version 41. DE 17 kDa surface antigen precursor. GN Name=omp; OrderedLocusNames=RT0821; OS Rickettsia typhi. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=785; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89359171; PubMed=2768201; RA Anderson B.E., Tzianabos T.; RT "Comparative sequence analysis of a genus-common rickettsial antigen RT gene."; RL J. Bacteriol. 171:5199-5201(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-144 / Wilmington; RX PubMed=15317790; DOI=10.1128/JB.186.17.5842-5855.2004; RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., RA Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., RA Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., RA Gibbs R.A., Hong C., Yu X.-J., Walker D.H., Weinstock G.M.; RT "Complete genome sequence of Rickettsia typhi and comparison with RT sequences of other Rickettsiae."; RL J. Bacteriol. 186:5842-5855(2004). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rickettsiale 17 kDa surface antigen 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; M28481; AAA26377.1; -; Genomic_DNA. DR EMBL; AE017197; AAU04276.1; -; Genomic_DNA. DR PIR; C33971; C33971. DR GenomeReviews; AE017197_GR; RT0821. DR KEGG; rty:RT0821; -. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Complete proteome; Lipoprotein; Membrane; Outer membrane; Palmitate; KW Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 159 17 kDa surface antigen. FT /FTId=PRO_0000018023. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). FT CONFLICT 75 75 M -> L (in Ref. 1). FT CONFLICT 158 158 A -> V (in Ref. 1). SQ SEQUENCE 159 AA; 16539 MW; A9893F26492727A9 CRC64; MKLLSKVMIL ALAASMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGHG KGQLVGVGVG ALLGAVLGGQ IGASMDEQDR KLLELTSQRA LESAPSGSNI EWRNPDNGNH GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QTTYGNACRQ PDGQWQVAN // ID 18C_DROME Reviewed; 215 AA. AC P16909; Q9VPA8; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 20-FEB-2007, entry version 51. DE Histone-like protein 18C. GN Name=Mst77F; Synonyms=18c, ANON-77F; ORFNames=CG3354; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Canton-S; RX MEDLINE=89107990; PubMed=3215511; RA Kalderon D., Rubin G.M.; RT "Isolation and characterization of Drosophila cAMP-dependent protein RT kinase genes."; RL Genes Dev. 2:1539-1556(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: Not known. Encoded in the intron of cAMP-dependent CC protein kinase regulatory chain type I. CC -!- DEVELOPMENTAL STAGE: In pupae and in adults. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X16962; CAA34836.1; -; Genomic_DNA. DR EMBL; AE014296; AAF51647.1; -; Genomic_DNA. DR UniGene; Dm.2510; -. DR Ensembl; CG3354; Drosophila melanogaster. DR KEGG; dme:Dmel_CG3354; -. DR FlyBase; FBgn0000093; Mst77F. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-017620-MONOMER; -. DR GermOnline; CG3354; Drosophila melanogaster. DR InterPro; IPR009071; HMG-box. KW Complete proteome. FT CHAIN 1 215 Histone-like protein 18C. FT /FTId=PRO_0000064354. SQ SEQUENCE 215 AA; 24472 MW; 8199C152FA39ACEF CRC64; MSNLKQKDSK PEVAVTKSVK TYKKSIEYVN SDASDIEEDI NRAEDEYASS SGFVNFLRDF KKRYGEYYSN NEIRRAAETR WNEMSFRHRC QYSAEPLDTF HVEPNSVSSL QRSSEGEHRM HSEISGCADT FFGAGGSNSC TPRKENKCSK PRVRKSCPKP RAKTSKQRRS CGKPKPKGAR PRKACPRPRK KMECGKAKAK PRCLKPKSSK PKCSM // ID 18K1_MYCAV Reviewed; 147 AA. AC P46729; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 31-OCT-2006, entry version 29. DE 18 kDa antigen 1 (Clone MAVC124). OS Mycobacterium avium. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=1764; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Serovar 2; RX MEDLINE=93202760; PubMed=8454357; RA Booth R.J., Williams D.L., Moudgil K.D., Noonan L.C., Grandison P.M., RA McKee J.J., Prestidge R.L., Watson J.D.; RT "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium RT tuberculosis 19-kilodalton antigens in other mycobacteria."; RL Infect. Immun. 61:1509-1515(1993). CC -!- FUNCTION: Not known. This protein is one of the major immune CC reactive proteins in mycobacteria. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) 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; L12236; AAA25341.1; -; Genomic_DNA. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. FT CHAIN 1 147 18 kDa antigen 1. FT /FTId=PRO_0000126012. SQ SEQUENCE 147 AA; 16544 MW; 4EFCBD131AB53999 CRC64; MLMRSDPFRE LDRLTNQVLG TPTRPAVMPM DAWRVGRRLV VEFDLPGIDA ESLDIDIERN VLTVRAERPA LDPNREMLAT ERPRGVFSRE LVLGDNLDTD KIEASYRDGV LSLHIPVDEK ARPRKIAVGA ARHPEPSPKT AREVVNA // ID 18K1_MYCIT Reviewed; 149 AA. AC P46730; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 31-OCT-2006, entry version 31. DE 18 kDa antigen 1 (18 kDa antigen clone MINTC73). OS Mycobacterium intracellulare. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=1767; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 35772 / TMC 1469 / Darden / Serovar 19; RX MEDLINE=93202760; PubMed=8454357; RA Booth R.J., Williams D.L., Moudgil K.D., Noonan L.C., Grandison P.M., RA McKee J.J., Prestidge R.L., Watson J.D.; RT "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium RT tuberculosis 19-kilodalton antigens in other mycobacteria."; RL Infect. Immun. 61:1509-1515(1993). CC -!- FUNCTION: Not known. This protein is one of the major immune CC reactive proteins in mycobacteria. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) 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; L12240; AAA25348.1; -; Genomic_DNA. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. FT CHAIN 1 149 18 kDa antigen 1. FT /FTId=PRO_0000126014. SQ SEQUENCE 149 AA; 16509 MW; 7101A31AC98964D4 CRC64; MLMRSDPFRE LDRFAHQVLG TAARPAVMPM DAWRQGEEFV VEFDLPGIDA DSLDIDIERN VVTVRAERPA LDPNREMLAT ERPRGVFSRQ LVLGENLDTD KIQASYSEGV LSLHIPVAEK AKPRKIAVGR GDGHHAVAEG AAQREVINA // ID 18K2_MYCAV Reviewed; 138 AA. AC P46731; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 31-OCT-2006, entry version 29. DE 18 kDa antigen 2 (Clone MAVC83). OS Mycobacterium avium. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=1764; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Serovar 2; RX MEDLINE=93202760; PubMed=8454357; RA Booth R.J., Williams D.L., Moudgil K.D., Noonan L.C., Grandison P.M., RA McKee J.J., Prestidge R.L., Watson J.D.; RT "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium RT tuberculosis 19-kilodalton antigens in other mycobacteria."; RL Infect. Immun. 61:1509-1515(1993). CC -!- FUNCTION: Not known. This protein is one of the major immune CC reactive proteins in mycobacteria. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) 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; L12237; AAA25349.1; -; Genomic_DNA. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. FT CHAIN 1 138 18 kDa antigen 2. FT /FTId=PRO_0000126013. SQ SEQUENCE 138 AA; 15949 MW; 568CCB098A67E769 CRC64; MVLMRTDPFR DLDRWTQQVL GTRRPAVMPM DAWRDGDQFV VEFDLPGVNA DSLDLDVERN VLTVRAERPD LDQNREMVSA ERPRGVFSRQ LFLGDNLDTD KIEANYHDGV LRLTIPVAEK AKPRRIEINH NHRTAINA // ID 18K2_MYCIT Reviewed; 140 AA. AC P46732; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 31-OCT-2006, entry version 31. DE 18 kDa antigen 2 (18 kDa antigen clone MINTC541). OS Mycobacterium intracellulare. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=1767; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 35772 / TMC 1469 / Darden / Serovar 19; RX MEDLINE=93202760; PubMed=8454357; RA Booth R.J., Williams D.L., Moudgil K.D., Noonan L.C., Grandison P.M., RA McKee J.J., Prestidge R.L., Watson J.D.; RT "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium RT tuberculosis 19-kilodalton antigens in other mycobacteria."; RL Infect. Immun. 61:1509-1515(1993). CC -!- FUNCTION: Not known. This protein is one of the major immune CC reactive proteins in mycobacteria. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) 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; L12239; AAA25347.1; -; Genomic_DNA. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. FT CHAIN 1 140 18 kDa antigen 2. FT /FTId=PRO_0000126015. SQ SEQUENCE 140 AA; 15749 MW; 4CCCB07BE235600E CRC64; MLVRSDPFRD LDRFTQQLSG TAARPAAMPM DAWRDGEQFV VEFDLPGIDE QSLDLDIERN VVTVRAERPD VDPSREMLAT ERARGVFSRQ LVLGDNLDTE HIDACYDAGV LRLRIPVAEK AKPRKIAVNR GDRQQTAISA // ID 18KD_MYCLE Reviewed; 148 AA. AC P12809; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 31-OCT-2006, entry version 46. DE 18 kDa antigen (HSP 16.7). GN Name=hsp18; OrderedLocusNames=ML1795; OS Mycobacterium leprae. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1769; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89053927; PubMed=3056923; RA Nerland A.H., Mustafa A.S., Sweetser D., Godal T., Young R.A.; RT "A protein antigen of Mycobacterium leprae is related to a family of RT small heat shock proteins."; RL J. Bacteriol. 170:5919-5921(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88088878; PubMed=2447183; RA Booth R.J., Harris D.P., Love J.M., Watson J.D.; RT "Antigenic proteins of Mycobacterium leprae. Complete sequence of the RT gene for the 18-kDa protein."; RL J. Immunol. 140:597-601(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN; RX MEDLINE=21128732; PubMed=11234002; DOI=10.1038/35059006; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). CC -!- FUNCTION: Not known. This protein is one of the major immune CC reactive proteins in mycobacteria. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) 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; M22587; AAA25343.1; -; Genomic_DNA. DR EMBL; M19058; AAA88229.1; -; Genomic_DNA. DR EMBL; AL583923; CAC30748.1; -; Genomic_DNA. DR PIR; A27586; A27586. DR GenomeReviews; AL450380_GR; ML1795. DR KEGG; mle:ML1795; -. DR Leproma; ML1795; -. DR BioCyc; MLEP1769:ML1795-MONOMER; -. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Complete proteome. FT CHAIN 1 148 18 kDa antigen. FT /FTId=PRO_0000126016. FT CONFLICT 13 20 RFAEQVLG -> LRRASVS (in Ref. 1). FT CONFLICT 100 100 E -> Q (in Ref. 1). SQ SEQUENCE 148 AA; 16707 MW; 82B11CC40845C391 CRC64; MLMRTDPFRE LDRFAEQVLG TSARPAVMPM DAWREGEEFV VEFDLPGIKA DSLDIDIERN VVTVRAERPG VDPDREMLAA ERPRGVFNRQ LVLGENLDTE RILASYQEGV LKLSIPVAER AKPRKISVDR GNNGHQTINK TAHEIIDA // ID 194K_TRVSY Reviewed; 1707 AA. AC P05080; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 2. DT 31-OCT-2006, entry version 40. DE Putative 194 kDa protein (Putative replicase) [Contains: 134 kDa DE protein]. OS Tobacco rattle virus (strain SYM). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Tobravirus. OX NCBI_TaxID=12298; OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet). OH NCBI_TaxID=4072; Capsicum annuum (Bell pepper). OH NCBI_TaxID=82024; Hyacinthus. OH NCBI_TaxID=39639; Narcissus pseudonarcissus (Daffodil). OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco). OH NCBI_TaxID=4113; Solanum tuberosum (Potato). OH NCBI_TaxID=3562; Spinacia oleracea (Spinach). OH NCBI_TaxID=13274; Stellaria media (Common chickweed). OH NCBI_TaxID=13305; Tulipa. OH NCBI_TaxID=97415; Viola arvensis (European field pansy) (Field violet). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX MEDLINE=88034943; PubMed=3668507; RA Hamilton W.D.O., Boccara M., Robinson D.J., Baulcombe D.C.; RT "The complete nucleotide sequence of tobacco rattle virus RNA-1."; RL J. Gen. Virol. 68:2563-2575(1987). RN [2] RP PARTIAL NUCLEOTIDE SEQUENCE. RA Boccara M., Hamilton W.D.O., Baulcombe D.C.; RT "The organisation and interviral homologies of genes at the 3' end of RT tobacco rattle virus RNA1."; RL EMBO J. 5:223-229(1986). CC -!- SIMILARITY: Contains 1 RdRp catalytic 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; X06172; CAA29537.1; -; Genomic_RNA. DR EMBL; D00155; BAA00110.1; -; Genomic_RNA. DR PIR; S01865; S01865. DR InterPro; IPR001788; RNA_dep_RNApol2. DR InterPro; IPR007094; RNA_pol_PSvir. DR InterPro; IPR002588; V_methyltrans. DR InterPro; IPR000606; Viral_helicase1. DR Pfam; PF00978; RdRP_2; 1. DR Pfam; PF01443; Viral_helicase1; 1. DR Pfam; PF01660; Vmethyltransf; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. KW Nucleotide-binding; Nucleotidyltransferase; RNA replication; KW RNA-directed RNA polymerase; Transferase. FT CHAIN 1 1707 Putative 194 kDa protein. FT /FTId=PRO_0000040215. FT CHAIN 1 1187 134 kDa protein. FT /FTId=PRO_0000040216. FT DOMAIN 1449 1562 RdRp catalytic. SQ SEQUENCE 1707 AA; 194330 MW; F4DABDB6C7F51F04 CRC64; MANGNFKLSQ LLNVDEMSAE QRSHFFDLML TKPDCEIGQM MQRVVVDKVD DMIRERKTKD PVIVHEVLSQ KEQNKLMEIY PEFNIVFKDD KNMVHGFAAA ERKLQALLLL DRVPALQEVD DIGGQWSFWV TRGEKRIHSC CPNLDIRDDQ REISRQIFLT AIGDQARSGK RQMSENELWM YDQFRKNIAA PNAVRCNNTY QGCTCRGFSD GKKKGAQYAI ALHSLYDFKL KDLMATMVEK KTKVVHAAML FAPESMLVDE GPLPSVDGYY MKKNGKIYFG FEKDPSFSYI HDWEEYKKYL LGKPVSYQGN VFYFEPWQVR GDTMLFSIYR IAGVPRRSLS SQEYYRRIYI SRWENMVVVP IFDLVESTRE LVKKDLFVEK QFMDKCLDYI ARLSDQQLTI SNVKSYLSSN NWVLFINGAA VKNKQSVDSR DLQLLAQTLL VKEQVARPVM RELREAILTE TKPITSLTDV LGLISRKLWK QFANKIAVGG FVGMVGTLIG FYPKKVLTWA KDTPNGPELC YENSHKTKVI VFLSVVYAIG GITLMRRDIR DGLVKKLCDM FDIKRGAHVL DVENPCRYYE INDFFSSLYS ASESGETVLP DLSEVKAKSD KLLQQKKEIA DEFLSAKFSN YSGSSVRTSP PSVVGSSRSG LGLLLEDSNV LTQARVGVSR KVDDEEIMEQ FLSGLIDTEA EIDEVVSAFS AECERGETSG TKVLCKPLTP PGFENVLPAV KPLVSKGKTV KRVDYFQVMG GERLPKRPVV SGDNSVDARR EFLYYLDAER VAQNDEIMSL YRDYSRGVIR TGGQNYPHGL GVWDVEMKNW CIRPVVTEHA YVFQPDKRMD DWSGYLEVAV WERGMLVNDF AVERMSDYVI VCDQTYLCNN RLILDNLSAL DLGPVNCSFE LVDGVPGCGK STMIVNSANP CVDVVLSTGR AATDDLIERF ASKGFPCKLK RRVKTVDSFL MHCVDGSLTG DVLHFDEALM AHAGMVYFCA QIAGAKRCIC QGDQNQISFK PRVSQVDLRF SSLVGKFDIV TEKRETYRSP ADVAAVLNKY YTGDVRTHNA TANSMTVRKI VSKEQVSLKP GAQYITFLQS EKKELVNLLA LRKVAAKVST VHESQGETFK DVVLVRTKPT DDSIARGREY LIVALSRHTQ SLVYETVKED DVSKEIRESA ALTKAALARF FVTETVLXRF RSRFDVFRHH EGPCAVPDSG TITDLEMWYD ALFPGNSLRD SSLDGYLVAT TDCNLRLDNV TIKSGNWKDK FAEKETFLKP VIRTAMPDKR KTTQLESLLA LQKRNQAAPD LQENVHATVL IEETMKKLKS VVYDVGKIRA DPIVNRAQME RWWRNQSTAV QAKVVADVRE LHEIDYSSYM YMIKSDVKPK TDLTPQFEYS ALQTVVYHEK LINSLFGPIF KEINERKLDA MQPHFVFNTR MTSSDLNDRV KFLNTEAAYD FVEIDMSKFD KSANRFHLQL QLEIYRLFGL DEWAAFLWEV SHTQTTVRDI QNGMMAHIWY QQKSGDADTY NANSDRTLCA LLSELPLEKA VMVTYGGDDS LIAFPRGTQF VDPCPKLATK WNFECKIFKY DVPMFCGKFL LKTSSCYEFV PDPVKVLTKL GKKSIKDVQH LAEIYISLND SNRALGNYMV VSKLSESVSD RYLYKGDSVH ALCALWKHIK SFTALCTLFR DENDKELNPA KVDWKKAQRA VSNFYDW // ID 1A01_GORGO Reviewed; 365 AA. AC P30375; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 48. DE Class I histocompatibility antigen, GOGO-A0101 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60258; CAA42810.1; -; mRNA. DR PIR; JH0534; JH0534. DR HSSP; P10315; 1HSB. DR SMR; P30375; 25-299. DR InterPro; IPR013151; Ig. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 365 Class I histocompatibility antigen, GOGO- FT A0101 alpha chain. FT /FTId=PRO_0000018897. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40830 MW; FB1B14BCD4DF63A8 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAHSQTDRV DLGTLRGYYN QSEDGSHTIQ RMYGCDVGSD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAEITKRK WEAAHFAEQL RAYLEGTCVE WLRRHLENGK ETLQRTDAPK THMTHHAVSD HEAILRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A01_HUMAN Reviewed; 365 AA. AC P30443; O77964; O78171; Q9MYA3; Q9TP25; Q9TQP5; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 64. DE HLA class I histocompatibility antigen, A-1 alpha chain precursor (MHC DE class I antigen A*1). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*0101). RX MEDLINE=88234547; PubMed=3375250; RA Parham P., Lomen C.E., Lawlor D.A., Ways J.P., Holmes N., Coppin H.L., RA Salter R.D., Wan A.M., Ennis P.D.; RT "Nature of polymorphism in HLA-A, -B, and -C molecules."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4005-4009(1988). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*0101). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE A*0101). RA Warren E.; RL Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*0101). RX MEDLINE=91067475; PubMed=2251137; DOI=10.1093/nar/18.22.6701; RA Girdlestone J.; RT "Nucleotide sequence of an HLA-A1 gene."; RL Nucleic Acids Res. 18:6701-6701(1990). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*0101). RX MEDLINE=98007773; PubMed=9349617; RA Laforet M., Froelich N., Parissiadis A., Pfeiffer B., Schell A., RA Faller B., Woehl-Jaegle M.L., Cazenave J.P., Tongio M.M.; RT "A nucleotide insertion in exon 4 is responsible for the absence of RT expression of an HLA-A*01 allele."; RL Tissue Antigens 50:347-350(1997). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE A*0101). RA Waller M.J., Robinson J., Marsh S.G.E.; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE A*0101). 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*0102). RX MEDLINE=95282145; PubMed=7761977; RA Browning M.J., Madrigal J.A., Krausa P., Kowalski H., Allsopp C.E., RA Little A.-M., Turner S., Adams E.J., Arnett K.L., Bodmer W.F., RA Parham P.; RT "The HLA-A,B,C genotype of the class I negative cell line Daudi RT reveals novel HLA-A and -B alleles."; RL Tissue Antigens 45:177-187(1995). RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*0103). RX MEDLINE=98101100; PubMed=9438203; DOI=10.1016/S0198-8859(97)00204-8; RA Sitha S., Scheltinga S.A., Johnston-Dow L.A., White C.B., RA der van Zwan A.W., Bakema J.E., Rozemuller E.H., van der Tweel J.G., RA Kronink M.N., Tilanus M.G.J.; RT "A generic sequencing based typing approach for the identification of RT HLA-A diversity."; RL Hum. Immunol. 57:120-128(1997). RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*0103). RC TISSUE=Blood; RX MEDLINE=21100775; PubMed=11182232; DOI=10.1016/S0198-8859(00)00238-X; RA Poland G.A., Sohni Y., Domanico M., Kroning C.M., DeGoey S.R., RA Jimale M., Jacobson R.M., Moore S.B.; RT "High frequency of HLA-A*0103 allele in a Somali population."; RL Hum. Immunol. 62:197-200(2001). RN [11] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*0106). RX MEDLINE=20309230; PubMed=10852390; RX DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [12] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*0107). RA Tamouza R., Fortier C., Mahfoudh N., Schaeffer V., Poirier J.C., RA Marzais F., Gautreau C., Charron D.; RT "A new HLA-A*01 allele."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [13] RP SULFATION. RX MEDLINE=88088800; PubMed=3121736; RA Sant A.J., Zacheis M., Rumbarger T., Giacoletto K.S., Schwartz B.D.; RT "Human Ia alpha- and beta-chains are sulfated."; RL J. Immunol. 140:155-160(1988). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Sulfated. Polyubiquitinated in a post ER compartment through CC interaction with human herpesvirus 8 MIR1 protein. This targets CC the protein for rapid degradation via the ubiquitin system (By CC similarity). CC -!- POLYMORPHISM: The following alleles of A-1 are known: A*0101, CC A*0102, A*0103, A*0106 and A*0107. The sequence shown is that of CC A*0101. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24043; AAA59652.1; -; Genomic_DNA. DR EMBL; X55710; CAA39243.1; -; Genomic_DNA. DR EMBL; Z93949; CAB07989.1; -; Genomic_DNA. DR EMBL; AJ278305; CAB93537.1; -; Genomic_DNA. DR EMBL; BC003069; AAH03069.1; -; mRNA. DR EMBL; U07161; AAA80569.1; -; mRNA. DR EMBL; Y12469; CAA73072.1; -; Genomic_DNA. DR EMBL; Y12470; CAA73073.1; -; Genomic_DNA. DR EMBL; AF214112; AAF19525.1; -; Genomic_DNA. DR EMBL; AF214111; AAF19525.1; JOINED; Genomic_DNA. DR EMBL; AF143232; AAD33894.1; -; Genomic_DNA. DR EMBL; AF143231; AAD33894.1; JOINED; Genomic_DNA. DR EMBL; AF219633; AAF73862.1; -; Genomic_DNA. DR EMBL; AF219632; AAF73862.1; JOINED; Genomic_DNA. DR PIR; I38518; I38518. DR PIR; I61856; I61856. DR UniGene; Hs.181244; -. DR PDB; 1W72; X-ray; A/D=25-298. DR Ensembl; ENSG00000197499; Homo sapiens. DR H-InvDB; HIX0005684; -. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR LinkHub; P30443; -. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Immunoglobulin domain; Membrane; MHC I; Polymorphism; Signal; KW Sulfation; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-1 alpha chain. FT /FTId=PRO_0000018813. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT MOD_RES 83 83 Sulfotyrosine (Potential). FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 33 33 F -> S (in allele A*0102). FT /FTId=VAR_004332. FT VARIANT 41 41 R -> S (in allele A*0102). FT /FTId=VAR_004333. FT VARIANT 80 80 G -> R (in allele A*0107). FT /FTId=VAR_016719. FT VARIANT 91 91 M -> V (in allele A*0107). FT /FTId=VAR_016720. FT VARIANT 100 100 A -> E (in allele A*0107). FT /FTId=VAR_016721. FT VARIANT 114 114 D -> A (in allele A*0107). FT /FTId=VAR_016722. FT VARIANT 121 121 I -> M (in allele A*0103). FT /FTId=VAR_016723. FT VARIANT 180 180 R -> L (in allele A*0106). FT /FTId=VAR_016724. FT VARIANT 182 182 V -> A (in allele A*0106). FT /FTId=VAR_016725. FT STRAND 27 38 FT TURN 39 41 FT STRAND 42 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 70 73 FT HELIX 74 78 FT HELIX 81 108 FT TURN 109 110 FT STRAND 113 115 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT TURN 244 245 FT STRAND 250 254 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 294 297 SQ SEQUENCE 365 AA; 40846 MW; 8667AFF3F06C4932 CRC64; MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQKME PRAPWIEQEG PEYWDQETRN MKAHSQTDRA NLGTLRGYYN QSEDGSHTIQ IMYGCDVGPD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAVHAAEQR RVYLEGRCVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A01_PANTR Reviewed; 365 AA. AC P16209; Q549C1; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 31-OCT-2006, entry version 50. DE CHLA class I histocompatibility antigen, A-2 alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90201944; PubMed=1690682; RA Lawlor D.A., Warren E., Ward F.E., Parham P.; RT "Comparison of class I MHC alleles in humans and apes."; RL Immunol. Rev. 113:147-185(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RX MEDLINE=20322475; PubMed=10866106; DOI=10.1007/s002510050638; RA de Groot N.G., Otting N., Arguello R., Watkins D.I., Doxiadis G.G., RA Madrigal J.A., Bontrop R.E.; RT "Major histocompatibility complex class I diversity in a West African RT chimpanzee population: implications for HIV research."; RL Immunogenetics 51:398-409(2000). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M30678; AAA87970.1; -; mRNA. DR EMBL; AF168394; AAF72775.1; -; mRNA. DR PIR; I36961; I36961. DR HSSP; P10315; 1HSB. DR SMR; P16209; 25-299. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 FT CHAIN 25 365 CHLA class I histocompatibility antigen, FT A-2 alpha chain. FT /FTId=PRO_0000018910. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40849 MW; FC452786BD038D3E CRC64; MAVMPPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDEETRS AKAHSQTDRV DLGTLRGYYN QSEDGSHTIQ IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAAHAAEQR RAYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A01_PONPY Reviewed; 365 AA. AC P16211; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 31-OCT-2006, entry version 49. DE Class I histocompatibility antigen, A-1 alpha chain precursor. OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90201944; PubMed=1690682; RA Lawlor D.A., Warren E., Ward F.E., Parham P.; RT "Comparison of class I MHC alleles in humans and apes."; RL Immunol. Rev. 113:147-185(1990). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M30680; AAA88835.1; -; mRNA. DR PIR; I84432; I84432. DR HSSP; P10315; 1HSB. DR SMR; P16211; 25-299. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 FT CHAIN 25 365 Class I histocompatibility antigen, A-1 FT alpha chain. FT /FTId=PRO_0000018918. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40658 MW; 11A5BC183009CF70 CRC64; MAIMAPRTLL LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRTPWMEQEG PEYWDRETRS VKAHAQTNRV DLGTLRGYYN QSDGGSHTIQ RMFGCDVGPD GRFLRGYEQH AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAAGAAEQD RAYLEGLCVE SLRRYLENGK ETLQRTDAPK THMTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGKEQR YTCHVQHEGL PEPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRRNSDRK GGSYSQAASN DSAQGSDVSL TACKV // ID 1A01_SAGOE Reviewed; 365 AA. AC P30515; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 45. DE Class I histocompatibility antigen, A alpha chain precursor. OS Saguinus oedipus (Cotton-top tamarin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Saguinus. OX NCBI_TaxID=9490; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90111120; PubMed=2104912; RA Watkins D.I., Letvin N.L., Hughes A.L., Tedder T.F.; RT "Molecular cloning of cDNA that encode MHC class I molecules from a RT New World primate (Saguinus oedipus). Natural selection acts at RT positions that may affect peptide presentation to T cells."; RL J. Immunol. 144:1136-1143(1990). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M33475; AAA36951.1; -; mRNA. DR PIR; I56053; I56053. DR HSSP; Q29961; 1HSA. DR SMR; P30515; 25-299. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 365 Class I histocompatibility antigen, A FT alpha chain. FT /FTId=PRO_0000018920. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40973 MW; B34B24FB6848E373 CRC64; MTVMAPRTLL LLLSGALVLT ETWAGSHSMR YFETSVSRPG RGEPRYISVG YVDDTQFVRF DSDAASPRME PRAPWMEQEG PEYWEEETRK GKADAQTFRV DLQTLLGYYN QSEAGSHTIQ WMYGCDLGPD GRLLRGYDQH AYDGKDYIAL NEDLRSWTAT DVAAQITQRK WEAANEAERT RAYLEGTCVE WLHRYLENGK ETLQRAEPPK THVTHHPVSD HEATLRCWAL GFYPAEITVT WQRDGEDQTQ DMELVETRPA GDGTFQKWAA VVVLSGEEQR YTCHVQHEGL PEPLTLRWEP PSQPTIPIMG IVAILAILGV VVTGAVVAAV MWRKKSSDKK GGSYSQAARS DSAQGSDVSL TACKV // ID 1A02_GORGO Reviewed; 365 AA. AC P30376; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 46. DE Class I histocompatibility antigen, GOGO-A0201 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60259; CAA42811.1; -; mRNA. DR PIR; JH0535; JH0535. DR HSSP; P10315; 1HSB. DR SMR; P30376; 25-300. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 365 Class I histocompatibility antigen, GOGO- FT A0201 alpha chain. FT /FTId=PRO_0000018898. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40896 MW; 09E0E5FCD8E58507 CRC64; MAVMAPRTLL LLLLGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEE PEYWDGETRK VKAHSQTDRV NLGTLRGYYN QSEAGSHTIQ KMYGCDVGSD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAEITKRK WEAAHFAEQL RAYLEGECVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEAILRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHESL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVIAAV RWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A02_HUMAN Reviewed; 365 AA. AC P01892; O19619; P06338; P10313; P30444; P30445; P30446; P30514; AC Q29680; Q29837; Q29899; Q95352; Q95380; Q9TPX8; Q9TPX9; Q9TPY0; AC Q9TQH5; Q9TQI3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 20-FEB-2007, entry version 85. DE HLA class I histocompatibility antigen, A-2 alpha chain precursor (MHC DE class I antigen A*2). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*0201). RX MEDLINE=85132727; PubMed=2982951; RA Koller B.H., Orr H.T.; RT "Cloning and complete sequence of an HLA-A2 gene: analysis of two HLA- RT A alleles at the nucleotide level."; RL J. Immunol. 134:2727-2733(1985). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*0201). RX MEDLINE=89122144; PubMed=2914713; RA Cianetti L., Testa U., Scotto L., la Valle R., Simeone A., Boccoli G., RA Giannella G., Peschle C., Boncinelli E.; RT "Three new class I HLA alleles: structure of mRNAs and alternative RT mechanisms of processing."; RL Immunogenetics 29:80-91(1989). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE A*0201). RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 91-365. RX MEDLINE=86033791; PubMed=3863816; RA Davidson W.F., Kress M., Khoury G., Jay G.; RT "Comparison of HLA class I gene sequences. Derivation of locus- RT specific oligonucleotide probes specific for HLA-A, HLA-B, and HLA-C RT genes."; RL J. Biol. Chem. 260:13414-13423(1985). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELES A*0201; A*0211 AND A*0212). RX MEDLINE=92269955; PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-365 (ALLELE A*0201). RX MEDLINE=85230571; PubMed=3874058; RA Krangel M.S.; RT "Unusual RNA splicing generates a secreted form of HLA-A2 in a RT mutagenized B lymphoblastoid cell line."; RL EMBO J. 4:1205-1210(1985). RN [7] RP PROTEIN SEQUENCE OF 25-295 (A*0201). RX MEDLINE=80056745; PubMed=92029; RA Orr H.T., Lopez de Castro J.A., Parham P., Ploegh H.L., RA Strominger J.L.; RT "Comparison of amino acid sequences of two human histocompatibility RT antigens, HLA-A2 and HLA-B7: location of putative alloantigenic RT sites."; RL Proc. Natl. Acad. Sci. U.S.A. 76:4395-4399(1979). RN [8] RP SEQUENCE REVISION (A*0201). RX MEDLINE=82247941; PubMed=6179086; RA Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.; RT "Structure of crossreactive human histocompatibility antigens HLA-A28 RT and HLA-A2: possible implications for the generation of HLA RT polymorphism."; RL Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*0201). RC TISSUE=Blood; RX MEDLINE=95137784; PubMed=7836067; DOI=10.1016/0198-8859(94)90087-6; RA Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.; RT "HLA class I allele (HLA-A2) expression defect associated with a RT mutation in its enhancer B inverted CAT box in two families."; RL Hum. Immunol. 41:69-73(1994). RN [10] RP SEQUENCE REVISION. RA Balas A.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE (ALLELE A*0201). RA Cox S.T.; RT "Confirmation of HLA-A*0201."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELES A*0202 AND RP A*0203). RX MEDLINE=87306734; PubMed=3497874; RA Mattson D.H., Handy D.E., Bradley D.A., Coligan J.E., Cowan E.P., RA Biddison W.E.; RT "DNA sequences of the genes that encode the CTL-defined HLA-A2 RT variants M7 and DK1."; RL Immunogenetics 26:190-192(1987). RN [13] RP NUCLEOTIDE SEQUENCE (ALLELES A*0203 AND A*0205). RX MEDLINE=87252273; PubMed=3496393; RA Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.; RT "Multiple genetic mechanisms have contributed to the generation of the RT HLA-A2/A28 family of class I MHC molecules."; RL J. Immunol. 139:936-941(1987). RN [14] RP NUCLEOTIDE SEQUENCE (ALLELES A*0203 AND A*0205). RA Domena J.D.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*0204). RX MEDLINE=92039809; PubMed=1937577; DOI=10.1007/BF00211991; RA Castano A.R., Lopez de Castro J.A.; RT "Structure of the HLA-A*0204 antigen, found in South American Indians. RT Spatial clustering of HLA-A2 subtype polymorphism."; RL Immunogenetics 34:281-285(1991). RN [16] RP NUCLEOTIDE SEQUENCE OF 9-365 (ALLELE A*0204). RX MEDLINE=92269956; PubMed=1589035; DOI=10.1038/357329a0; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). RN [17] RP NUCLEOTIDE SEQUENCE (ALLELE A*0206). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [18] RP PARTIAL PROTEIN SEQUENCE (A*0206). RX MEDLINE=86305811; PubMed=3489037; RA Ezquerra A., Domenech N., van der Poel J., Strominger J.L., Vega M.A., RA Lopez de Castro J.A.; RT "Molecular analysis of an HLA-A2 functional variant CLA defined by RT cytolytic T lymphocytes."; RL J. Immunol. 137:1642-1649(1986). RN [19] RP PARTIAL PROTEIN SEQUENCE (A*0207). RX MEDLINE=88113844; PubMed=2448239; RA Domenech N., Ezquerra A., Castano R., Lopez de Castro J.A.; RT "Structural analysis of HLA-A2.4 functional variant KNE. Implications RT for the mapping of HLA-A2-specific T-cell epitopes."; RL Immunogenetics 27:196-202(1988). RN [20] RP PARTIAL PROTEIN SEQUENCE (A*0208). RX MEDLINE=88314183; PubMed=2457548; RA Domenech N., Castano R., Goulmy E., Lopez de Castro J.A.; RT "Molecular analysis of HLA-A2.4 functional variant KLO: close RT structural and evolutionary relatedness to the HLA-A2.2 subtype."; RL Immunogenetics 28:143-152(1988). RN [21] RP PARTIAL PROTEIN SEQUENCE (A*0209). RX MEDLINE=88186100; PubMed=3258580; RA Castano R., Ezquerra A., Domenech N., Lopez de Castro J.A.; RT "An HLA-A2 population variant with structural polymorphism in the RT alpha 3 region."; RL Immunogenetics 27:345-355(1988). RN [22] RP NUCLEOTIDE SEQUENCE (ALLELE A*0210). RX MEDLINE=89122133; PubMed=2783680; RA Epstein H., Kennedy L., Holmes N.; RT "An Oriental HLA-A2 subtype is closely related to a subset of RT Caucasoid HLA-A2 alleles."; RL Immunogenetics 29:112-116(1989). RN [23] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*0211). RX MEDLINE=92218010; PubMed=1559719; DOI=10.1007/BF00189898; RA Castano A.R., Lopez de Castro J.A.; RT "Structure of the HLA-A*0211 (A2.5) subtype: further evidence for RT selection-driven diversification of HLA-A2 antigens."; RL Immunogenetics 35:344-346(1992). RN [24] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*0213). RX MEDLINE=94222455; PubMed=8168863; DOI=10.1007/BF00189243; RA Barber D.F., Fernandez J.M., Lopez de Castro J.A.; RT "Primary structure of a new HLA-A2 subtype: HLA-A*0213."; RL Immunogenetics 39:378-378(1994). RN [25] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*0216). RX MEDLINE=95278976; PubMed=7759139; RA Barouch D., Krausa P., Bodmer J., Browning M.J., McMichael A.J.; RT "Identification of a novel HLA-A2 subtype, HLA-A*0216."; RL Immunogenetics 41:388-388(1995). RN [26] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*0217). RC TISSUE=Blood; RX MEDLINE=95381236; PubMed=7652742; RA Selvakumar A., Granja C.B., Salazar M., Alosco S.M., Yunis E.J., RA Dupont B.; RT "A novel subtype of A2 (A*0217) isolated from the South American RT Indian B-cell line AMALA."; RL Tissue Antigens 45:343-347(1995). RN [27] RP NUCLEOTIDE SEQUENCE (ALLELE A*0218). RC TISSUE=Blood; RA Kashiwase K., Tokunaga K., Ishikawa Y., Oohashi H., Hashimoto M., RA Akaza T., Tadokoro K., Juji T.; RT "A new A2 sequence HLA-A2K from Japanese."; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [28] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*0220). RC TISSUE=Blood; RX MEDLINE=97161038; PubMed=9008310; RA Fleischhauer K., Zino E., Mazzi B., Severini G.M., Benazzi E., RA Bordignon C.; RT "HLA-A*02 subtype distribution in Caucasians from northern Italy: RT identification of A*0220."; RL Tissue Antigens 48:673-679(1996). RN [29] RP NUCLEOTIDE SEQUENCE (ALLELE A*0221). RC TISSUE=Blood; RA Szmania S., Baxter-Lowe L.A.; RT "Nucleotide sequence of a novel HLA-A2 gene."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [30] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*0231). RX MEDLINE=20156437; PubMed=10689125; DOI=10.1016/S0198-8859(99)00155-X; RA Ellis J.M., Henson V., Slack R., Ng J., Hartzman R.J., RA Katovich Hurley C.; RT "Frequencies of HLA-A2 alleles in five U.S. population groups. RT Predominance Of A*02011 and identification of HLA-A*0231."; RL Hum. Immunol. 61:334-340(2000). RN [31] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELE A*0234). RX MEDLINE=20208581; PubMed=10746792; RX DOI=10.1034/j.1399-0039.2000.550212.x; RA Moses J.H., Greville W.D., Downes J., McClenahan W., Kennedy A., RA Dunckley H.; RT "A new HLA-A*02 allele, A*0234, detected by polymerase chain reaction RT using sequence-specific primers (PCR-SSP)."; RL Tissue Antigens 55:175-177(2000). RN [32] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*0235; A*0236 AND A*0237). RX MEDLINE=20309230; PubMed=10852390; RX DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [33] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF A*0201. RX MEDLINE=88014204; PubMed=3309677; DOI=10.1038/329506a0; RA Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L., RA Wiley D.C.; RT "Structure of the human class I histocompatibility antigen, HLA-A2."; RL Nature 329:506-512(1987). RN [34] RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I. RX PubMed=11390610; DOI=10.1128/JVI.75.13.6086-6094.2001; RA Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L., RA Mulloy J.C., Jacobson S., Franchini G.; RT "Free major histocompatibility complex class I heavy chain is RT preferentially targeted for degradation by human T-cell RT leukemia/lymphotropic virus type 1 p12(I) protein."; RL J. Virol. 75:6086-6094(2001). RN [35] RP INTERACTION WITH HUMAN HERPESVIRUS 8 MIR1 PROTEIN. RX PubMed=12006494; DOI=10.1093/emboj/21.10.2418; RA Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G., RA Lehner P.J.; RT "Ubiquitylation of MHC class I by the K3 viral protein signals RT internalization and TSG101-dependent degradation."; RL EMBO J. 21:2418-2429(2002). RN [36] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF A*0201. RX MEDLINE=91245570; PubMed=2038058; RA Saper M.A., Bjorkman P.J., Wiley D.C.; RT "Refined structure of the human histocompatibility antigen HLA-A2 at RT 2.6-A resolution."; RL J. Mol. Biol. 219:277-319(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein. CC Interacts with HTLV-1 accessory protein p12I. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment through CC interaction with human herpesvirus 8 MIR1 protein. This targets CC the protein for rapid degradation via the ubiquitin system. CC -!- POLYMORPHISM: The following alleles of A-2 are known: A*0201, CC A*0202, A*0203, A*0204, A*0205, A*0206 (A2.4A), A*0207, A*0208, CC A*0209, A*0210, A*0211 (A2.5), A*0212, A*0213 (A*02SLU), A*0216, CC A*0217, A*0218 (A2K), A*0219, A*0220, A*0221, A*0231, A*0234 CC (A*AAT), A*0235, A*0236 and A*0237. The sequence shown is that of CC A*0201. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC -!- CAUTION: Ref.6 and Ref.7 sequences differ from that shown CC extensively. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K02883; AAA98727.1; -; Genomic_DNA. DR EMBL; M84379; AAA59606.1; -; mRNA. DR EMBL; X02457; CAA26297.1; -; mRNA. DR EMBL; M11887; AAA52656.1; -; mRNA. DR EMBL; M19670; AAA03683.2; -; Genomic_DNA. DR EMBL; M17690; AAB02120.1; -; Genomic_DNA. DR EMBL; U03863; AAA03604.1; -; Unassigned_DNA. DR EMBL; M86404; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; X57954; CAA41022.1; ALT_SEQ; mRNA. DR EMBL; U02935; AAA76608.2; -; Genomic_DNA. DR EMBL; AJ555412; CAD87771.1; -; Genomic_DNA. DR EMBL; U03862; AAA03603.1; -; Unassigned_DNA. DR EMBL; M24042; AAA59653.1; -; mRNA. DR EMBL; Z23071; CAA80612.1; -; mRNA. DR EMBL; M84377; AAA59603.1; -; mRNA. DR EMBL; X60764; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M84378; AAA59604.1; -; mRNA. DR EMBL; Z27120; CAA81644.1; -; mRNA. DR EMBL; Z46633; CAA86602.1; -; mRNA. DR EMBL; U18930; AAA87076.1; -; mRNA. DR EMBL; D83515; BAA11935.1; -; mRNA. DR EMBL; X96724; CAA65501.1; -; mRNA. DR EMBL; U56825; AAB17465.1; -; mRNA. DR EMBL; AF113924; AAD23437.1; -; Genomic_DNA. DR EMBL; AF113923; AAD23437.1; JOINED; Genomic_DNA. DR EMBL; AF129431; AAD30272.1; -; Genomic_DNA. DR EMBL; AF129429; AAD30272.1; JOINED; Genomic_DNA. DR EMBL; AF129430; AAD30272.1; JOINED; Genomic_DNA. DR EMBL; AF157311; AAD45690.1; -; Genomic_DNA. DR EMBL; AF157310; AAD45690.1; JOINED; Genomic_DNA. DR EMBL; AF157309; AAD45689.1; -; Genomic_DNA. DR EMBL; AF157308; AAD45689.1; JOINED; Genomic_DNA. DR EMBL; AF157564; AAD45324.1; -; Genomic_DNA. DR EMBL; AF157563; AAD45324.1; JOINED; Genomic_DNA. DR PIR; B24512; HLHU10. DR PIR; I38418; I38418. DR PIR; I38442; I38442. DR PIR; I61857; I61857. DR UniGene; Hs.181244; -. DR PDB; 1AKJ; X-ray; A=25-300. DR PDB; 1AO7; X-ray; A=25-299. DR PDB; 1AQD; X-ray; C/F/I/L=127-141. DR PDB; 1B0G; X-ray; A/D=25-299. DR PDB; 1B0R; X-ray; A=25-299. DR PDB; 1BD2; X-ray; A=25-299. DR PDB; 1DUY; X-ray; A/D=25-299. DR PDB; 1DUZ; X-ray; A/D=25-299. DR PDB; 1EEY; X-ray; A/D=25-299. DR PDB; 1EEZ; X-ray; A/D=25-299. DR PDB; 1HHG; X-ray; A/D=25-299. DR PDB; 1HHH; X-ray; A=25-299. DR PDB; 1HHI; X-ray; A/D=25-299. DR PDB; 1HHJ; X-ray; A/D=25-299. DR PDB; 1HHK; X-ray; A/D=25-299. DR PDB; 1HLA; X-ray; A=25-294. DR PDB; 1I1F; X-ray; A/D=25-299. DR PDB; 1I1Y; X-ray; A/D=25-299. DR PDB; 1I4F; X-ray; A=25-299. DR PDB; 1I7R; X-ray; A/D=25-299. DR PDB; 1I7T; X-ray; A/D=25-299. DR PDB; 1I7U; X-ray; A/D=25-299. DR PDB; 1IM3; X-ray; A/E/I/M=25-299. DR PDB; 1JF1; X-ray; A=25-299. DR PDB; 1JHT; X-ray; A=25-299. DR PDB; 1LP9; X-ray; A/H=25-299. DR PDB; 1OGA; X-ray; A=25-300. DR PDB; 1P7Q; X-ray; A=25-300. DR PDB; 1QEW; X-ray; A=25-299. DR PDB; 1QR1; X-ray; A/D=25-299. DR PDB; 1QRN; X-ray; A=25-298. DR PDB; 1QSE; X-ray; A=25-298. DR PDB; 1QSF; X-ray; A=25-298. DR PDB; 1S9W; X-ray; A=25-298. DR PDB; 1S9X; X-ray; A=25-298. DR PDB; 1S9Y; X-ray; A=25-298. DR PDB; 1TVB; X-ray; A/D=25-299. DR PDB; 1TVH; X-ray; A/D=25-299. DR PDB; 1UR7; Model; A=25-299. DR PDB; 2AV1; X-ray; A/D=25-299. DR PDB; 2AV7; X-ray; A/D=25-299. DR PDB; 2BNQ; X-ray; A=25-300. DR PDB; 2BNR; X-ray; A=25-300. DR PDB; 2BSU; X-ray; A/D=25-300. DR PDB; 2BSV; X-ray; A/D=25-300. DR PDB; 2C7U; X-ray; A/D=25-300. DR PDB; 2CLR; X-ray; A/D=25-299. DR PDB; 2F53; X-ray; A=25-299. DR PDB; 2F54; X-ray; A/F=25-298. DR PDB; 3HLA; X-ray; A=25-294. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR LinkHub; P01892; -. DR ArrayExpress; P01892; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Direct protein sequencing; Glycoprotein; KW Host-virus interaction; Immune response; Membrane; MHC I; KW Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-2 alpha chain. FT /FTId=PRO_0000018814. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 33 33 F -> Y (in allele A*0205, allele A*0206, FT allele A*0208, allele A*0210 and allele FT A*0221). FT /FTId=VAR_004334. FT VARIANT 54 54 D -> N (in allele A*0221). FT /FTId=VAR_004335. FT VARIANT 65 65 A -> G (in allele A*0231). FT /FTId=VAR_016726. FT VARIANT 67 67 Q -> R (in allele A*0202, allele A*0205 FT and allele A*0208). FT /FTId=VAR_004336. FT VARIANT 90 90 K -> N (in allele A*0208 and allele FT A*0220). FT /FTId=VAR_004337. FT VARIANT 94 94 H -> Q (in allele A*0234 and allele FT A*0235). FT /FTId=VAR_016727. FT VARIANT 97 97 T -> I (in allele A*0211). FT /FTId=VAR_004338. FT VARIANT 98 98 H -> D (in allele A*0211 and allele FT A*0235). FT /FTId=VAR_016728. FT VARIANT 119 119 V -> L (in allele A*0202, allele A*0205, FT allele A*0208 and allele A*0217). FT /FTId=VAR_004339. FT VARIANT 121 121 R -> M (in allele A*0204 and allele FT A*0217). FT /FTId=VAR_004340. FT VARIANT 123 123 Y -> C (in allele A*0207 and allele FT A*0218). FT /FTId=VAR_004341. FT VARIANT 123 123 Y -> F (in allele A*0210 and allele FT A*0217). FT /FTId=VAR_004342. FT VARIANT 131 131 W -> G (in allele A*0210). FT /FTId=VAR_004343. FT VARIANT 162 162 M -> K (in allele A*0218). FT /FTId=VAR_004344. FT VARIANT 173 173 A -> T (in allele A*0203). FT /FTId=VAR_004345. FT VARIANT 176 176 V -> E (in allele A*0203 and allele FT A*0213). FT /FTId=VAR_004346. FT VARIANT 180 180 L -> Q (in allele A*0212, allele A*0213 FT and allele A*0237). FT /FTId=VAR_004348. FT VARIANT 180 180 L -> W (in allele A*0202, allele A*0203, FT allele A*0205 and allele A*0208). FT /FTId=VAR_004347. FT VARIANT 187 187 T -> E (in allele A*0216; requires 2 FT nucleotide substitutions). FT /FTId=VAR_004349. FT VARIANT 190 190 E -> D (in allele A*0236 and allele FT A*0237). FT /FTId=VAR_016729. FT VARIANT 191 191 W -> G (in allele A*0236 and allele FT A*0237). FT /FTId=VAR_016730. FT VARIANT 260 260 A -> E (in allele A*0209). FT /FTId=VAR_004350. FT CONFLICT 115 115 G -> V (in Ref. 4). FT CONFLICT 140 140 Y -> V (in Ref. 4). FT CONFLICT 277 277 Q -> E (in Ref. 4). FT CONFLICT 318 318 F -> L (in Ref. 4). FT STRAND 27 36 FT TURN 39 40 FT STRAND 41 43 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT STRAND 113 115 FT STRAND 118 127 FT TURN 129 130 FT STRAND 131 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 154 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 184 FT TURN 185 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 235 FT STRAND 238 243 FT TURN 244 245 FT STRAND 246 248 FT TURN 250 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 294 297 SQ SEQUENCE 365 AA; 40922 MW; B54A97B24B337C08 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDGETRK VKAHSQTHRV DLGTLRGYYN QSEAGSHTVQ RMYGCDVGSD WRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A02_PANTR Reviewed; 362 AA. AC P16210; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 31-OCT-2006, entry version 49. DE CHLA class I histocompatibility antigen, A-5 alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90201944; PubMed=1690682; RA Lawlor D.A., Warren E., Ward F.E., Parham P.; RT "Comparison of class I MHC alleles in humans and apes."; RL Immunol. Rev. 113:147-185(1990). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M30679; AAA87971.1; -; mRNA. DR PIR; I36962; I36962. DR HSSP; P30474; 1A9E. DR SMR; P16210; 25-300. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 FT CHAIN 25 362 CHLA class I histocompatibility antigen, FT A-5 alpha chain. FT /FTId=PRO_0000018911. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 362 AA; 40487 MW; 9B5A674445037056 CRC64; MQVTAPRTVL LLLSAALALT ETWAGSHSMK YFYTAVSRPG RGEPRFISVG YVDDTQFVWF DSDAASPREE PRAPWIEQEG PEYWDRETQI SKTNAQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDMGPD GRLLRGYEQY AYDGKDYIAL NQDLSSWTAA DTAAQITQRK WEAARWAEQL RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1A03_GORGO Reviewed; 365 AA. AC P30377; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 47. DE Class I histocompatibility antigen, GOGO-A0401 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60257; CAA42809.1; -; mRNA. DR PIR; JH0536; JH0536. DR HSSP; P10315; 1HSB. DR SMR; P30377; 25-299. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 365 Class I histocompatibility antigen, GOGO- FT A0401 alpha chain. FT /FTId=PRO_0000018899. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40934 MW; 9207ABBDF9B406C9 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEE PEYWDGETRN MKARSQTDRV DLGTLRGYYN QSEDGSHTIQ RMYGCDVGSD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAAHEAEQL RAYLEGTCVE WLRRYLENGK ETLQLTDAPK THMTHHPVSD HEAILRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A03_HUMAN Reviewed; 365 AA. AC P04439; O19546; O19756; Q65A82; Q9GJE6; Q9GJE7; Q9GJE8; Q9MYG4; AC Q9TPR8; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 20-FEB-2007, entry version 68. DE HLA class I histocompatibility antigen, A-3 alpha chain precursor (MHC DE class I antigen A*3). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*0301). RX MEDLINE=84207948; PubMed=6609814; RA Strachan T., Sodoyer R., Damotte M., Jordan B.R.; RT "Complete nucleotide sequence of a functional class I HLA gene, HLA- RT A3: implications for the evolution of HLA genes."; RL EMBO J. 3:887-894(1984). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*0301). RA Ellexson M.E., Hildebrand W.H.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE A*0301). RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE A*0302). RX MEDLINE=85290871; PubMed=2993417; RA Cowan E.P., Jordan B.E., Coligan J.E.; RT "Molecular cloning and DNA sequence analysis of genes encoding RT cytotoxic T lymphocyte-defined HLA-A3 subtypes: the E1 subtype."; RL J. Immunol. 135:2835-2841(1985). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELE A*0302). RA Bettinotti M.P., Hadzikadic L., Adams S., Marincola F.M.; RT "Complete coding sequence of HLA-A*0302."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Mayor N.P.; RT "Full length sequence of an HLA-A*0301 intron 2 variant."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-341 (ALLELE A*0304). RX MEDLINE=99180630; PubMed=10079303; DOI=10.1007/s002510050506; RA Santos S., Balas A., Garcia-Sanchez F., Lillo R., Merino J.L., RA Vicario J.L.; RT "Complete cDNA coding sequence of a new HLA-A3 subtype (A*0304) with a RT new HLA polymorphism at exon 3."; RL Immunogenetics 49:360-361(1999). RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*0305). RA Becher M.P., Wu J., Williams T.; RT "Novel human HLA-A alleles identified in potential bone marrow RT donors."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE OF 26-298 (ALLELE A*0305). RC TISSUE=Blood; RA Poli F., Frison S., Crespiatico L., Longhi E.; RT "Identification of a HLA-A*03 new variant."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-3 are known: A*0301 (A- CC 3.1), A*0302, A*0304 and A*0305. The sequence shown is that of CC A*0301. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X00492; CAA25162.1; ALT_SEQ; Genomic_DNA. DR EMBL; U32184; AAB63980.1; -; mRNA. DR EMBL; BA000025; BAB63400.1; -; Genomic_DNA. DR EMBL; AF217561; AAF28734.1; -; mRNA. DR EMBL; AF015930; AAB66582.1; -; mRNA. DR EMBL; AF190719; AAF03243.1; -; Genomic_DNA. DR EMBL; AF190718; AAF03243.1; JOINED; Genomic_DNA. DR EMBL; AJ401085; CAC06086.1; -; Genomic_DNA. DR EMBL; AJ401086; CAC06087.1; -; Genomic_DNA. DR EMBL; AJ401087; CAC06088.1; -; Genomic_DNA. DR EMBL; AJ748743; CAG38621.1; -; Genomic_DNA. DR EMBL; AL671277; CAI18372.1; -; Genomic_DNA. DR PIR; A02192; HLHUA3. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P04439; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR KEGG; hsa:3105; -. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P04439; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-3 alpha chain. FT /FTId=PRO_0000018815. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 176 176 E -> V (in allele A*0302). FT /FTId=VAR_004351. FT VARIANT 180 180 L -> Q (in allele A*0302). FT /FTId=VAR_004352. FT VARIANT 185 185 D -> E (in allele A*0305). FT /FTId=VAR_016604. FT VARIANT 199 199 G -> R (in allele A*0304). FT /FTId=VAR_016605. FT CONFLICT 319 319 G -> A (in Ref. 8). SQ SEQUENCE 365 AA; 40841 MW; DEDFCEC4450E0580 CRC64; MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAAHEAEQL RAYLDGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A03_PANTR Reviewed; 365 AA. AC P13748; Q547D5; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 28-NOV-2006, entry version 52. DE CHLA class I histocompatibility antigen, A-108 alpha chain precursor DE (MHC class I antigen Patr-A*0301). GN Name=Patr-A; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89030641; PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=22016141; PubMed=12021342; RX DOI=10.1128/JVI.76.12.6093-6103.2002; RA Mizukoshi E., Nascimbeni M., Blaustein J.B., Mihalik K., Rice C.M., RA Liang T.J., Feinstone S.M., Rehermann B.; RT "Molecular and immunological significance of chimpanzee major RT histocompatibility complex haplotypes for hepatitis C virus immune RT response and vaccination studies."; RL J. Virol. 76:6093-6103(2002). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X13113; CAA31505.1; ALT_INIT; mRNA. DR EMBL; AF500288; AAM49754.1; -; mRNA. DR PIR; S03535; S03535. DR HSSP; P10315; 1HSB. DR SMR; P13748; 25-299. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 FT CHAIN 25 365 CHLA class I histocompatibility antigen, FT A-108 alpha chain. FT /FTId=PRO_0000018912. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40823 MW; 48CC757055221FC3 CRC64; MAVMPPRTLL LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN MKASAQTDRV DLGTLRGYYN QSEDGSHTIQ IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA AMAAQITKRK WEAAHAAEQL RAYLEGRCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAVITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A04_GORGO Reviewed; 365 AA. AC P30378; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 48. DE Class I histocompatibility antigen, GOGO-A0501 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60256; CAA42808.1; -; mRNA. DR PIR; JH0537; JH0537. DR HSSP; P10315; 1HSB. DR SMR; P30378; 25-302. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 365 Class I histocompatibility antigen, GOGO- FT A0501 alpha chain. FT /FTId=PRO_0000018900. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40896 MW; 340DAD21F9B3B8AB CRC64; MAVVAPRTLL LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWMEQEE PEYWDRQTQI SKTNAQIELE SLRIALRYYN QSEDGSHTIQ RMYGCDVGSD GRFLRGYQQD AYDGKDYIAS NEDLRSWTAA DMAAEITKRK WEAAHFAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THTTHQAVSD HEATLKCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A04_PANTR Reviewed; 365 AA. AC P13749; Q7JJU4; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 31-OCT-2006, entry version 51. DE CHLA class I histocompatibility antigen, A-126 alpha chain precursor DE (MHC class I antigen Patr-A*0401). GN Name=Patr-A; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89030641; PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RX MEDLINE=20322475; PubMed=10866106; DOI=10.1007/s002510050638; RA de Groot N.G., Otting N., Arguello R., Watkins D.I., Doxiadis G.G., RA Madrigal J.A., Bontrop R.E.; RT "Major histocompatibility complex class I diversity in a West African RT chimpanzee population: implications for HIV research."; RL Immunogenetics 51:398-409(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22709134; PubMed=12799463; DOI=10.1073/pnas.1230533100; RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A., RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y., RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., RA Meyer A., Ikeo K., Gojobori T., Bahram S., Inoko H.; RT "Comparative sequencing of human and chimpanzee MHC class I regions RT unveils insertions/deletions as the major path to genomic RT divergence."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X13114; CAA31506.1; -; mRNA. DR EMBL; AF168401; AAF72782.1; -; mRNA. DR EMBL; BA000041; BAC78189.1; -; Genomic_DNA. DR PIR; S01171; S01171. DR HSSP; P10315; 1HSB. DR SMR; P13749; 25-299. DR KEGG; ptr:450151; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 FT CHAIN 25 365 CHLA class I histocompatibility antigen, FT A-126 alpha chain. FT /FTId=PRO_0000018913. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40656 MW; D3C9A810B22A768F CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDEETRS VKASAQTDRV DLGTLRGYYN QSEDGSHTIQ LMFGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAAHAAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD REATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A110_ARATH Reviewed; 557 AA. AC Q9LQ10; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 23-JAN-2007, entry version 30. DE Probable aminotransferase ACS10 (EC 2.6.1.-). GN Name=ACS10; OrderedLocusNames=At1g62960; ORFNames=F16P17.11; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP LACK OF ACS ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). CC -!- FUNCTION: Probable aminotransferase. Does not have 1- CC aminocyclopropane-1-carboxylate synthase (ACS) activity, CC suggesting that it is not involved in ethylene biosynthesis. CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in roots. CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC -!- CAUTION: Contains a Gln instead of a Glu in position 176 and a Phe CC residue instead of a Tyr in position 209; theses residues being CC essential in substrate recognition by ACS enzymes. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC011000; AAF75807.1; -; Genomic_DNA. DR EMBL; AF348575; AAK15546.1; -; mRNA. DR EMBL; AY054691; AAK96882.1; -; mRNA. DR EMBL; BT008906; AAP68345.1; -; mRNA. DR PIR; D96654; D96654. DR UniGene; At.14857; -. DR HSSP; P18485; 1IAX. DR GenomeReviews; CT485782_GR; AT1G62960. DR KEGG; ath:At1g62960; -. DR TAIR; At1g62960; -. DR ArrayExpress; Q9LQ10; -. DR GermOnline; AT1G62960; Arabidopsis thaliana. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; FALSE_NEG. KW Aminotransferase; Pyridoxal phosphate; Transferase. FT CHAIN 1 557 Probable aminotransferase ACS10. FT /FTId=PRO_0000123904. FT BINDING 394 394 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 557 AA; 61016 MW; 78850961F7DB5236 CRC64; MTRTEPNRSR SSNSDSDKNS GNVGGGRTTG MRVIVPLQGV VQGRGGLFLG SVIPCAFFYF LQFYLKRNRK NDESDNSGEQ NSSASSSSSP NSGLPDPTRS QSAGHLTELT GLPRSLSRIL LSPRNSGGAV SVSGRVNCVL KGGDSSPYYV GQKRVEDDPY DELGNPDGVI QLGLAQNNKL SLDDWVLENP KEAISDGLSI SGIASYEPSD GLLELKMAVA GFMTEATKNS VTFDPSQLVL TSGASSAIEI LSFCLADSGN AFLVPTPCSP GYDRDVKWRT GVDIIHVPCR SADNFNMSMV VLDRAFYQAK KRGVRIRGII ISNPSNPMGS LLSRENLYAL LDFARERNIH IISNEIFAGS VHGEEGEFVS MAEIVDTEEN IDRERVHIVY DLSKDLSFRG LRSAAIYSFN ESVLSASRKL TTLSPVSSPT QHLLISAISN PKNVQRFVKT NRQRLQSIYT ELVEGLKELG IECTRSNGGF YCWADMRGLI SSYSEKGEIE LWNKLLNIGK INVIPGSCCH CIEPGWFRIC FSNLSERDVP VVMNRIRKVC ETCKSQN // ID 1A111_ARATH Reviewed; 460 AA. AC Q9S9U6; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 23-JAN-2007, entry version 33. DE 1-aminocyclopropane-1-carboxylate synthase 11 (EC 4.4.1.14) (ACC DE synthase 11) (S-adenosyl-L-methionine methylthioadenosine-lyase 11). GN Name=ACS11; OrderedLocusNames=At4g08040; ORFNames=T17A2.2; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND PUTATIVE RP PROCESSING. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of CC ethylene. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=25 uM for AdoMet; CC Vmax=25.20 uM/h/mg enzyme; CC pH dependence: CC Optimum pH is 8; CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of CC heterodimerization with other ACS enzymes is however unsure (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed in roots. CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). CC -!- PTM: May be processed at its C-terminus. CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation CC of such stability, play a central role in ethylene biosynthesis. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF160183; AAD48074.1; -; Genomic_DNA. DR EMBL; AL161509; CAB81141.1; -; Genomic_DNA. DR EMBL; AF332405; AAG48768.1; -; mRNA. DR PIR; B85079; B85079. DR UniGene; At.4151; -. DR HSSP; P37821; 1B8G. DR SMR; Q9S9U6; 10-423. DR GenomeReviews; CT486007_GR; AT4G08040. DR KEGG; ath:At4g08040; -. DR TAIR; At4g08040; -. DR ArrayExpress; Q9S9U6; -. DR GermOnline; AT4G08040; Arabidopsis thaliana. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 460 1-aminocyclopropane-1-carboxylate FT synthase 11. FT /FTId=PRO_0000123905. FT BINDING 45 45 Substrate (By similarity). FT BINDING 83 83 Substrate (By similarity). FT BINDING 267 267 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 460 AA; 51799 MW; 1A056347680E7E2F CRC64; MLSSKVVGDS HGQDSSYFLG WQEYEKNPFH ESFNTSGIVQ MGLAENQLSF DLIEKWLEEH PEVLGLKKND ESVFRQLALF QDYHGLPAFK DAMAKFMGKI RENKVKFDTN KMVLTAGSTS ANETLMFCLA NPGDAFLIPA PYYPGFDRDL KWRTGVEIVP IHCVSSNGYK ITEDALEDAY ERALKHNLNV KGVLITNPSN PLGTSTTREE LDLLLTFTST KKIHMVSDEI YSGTVFDSPE FTSVLEVAKD KNMGLDGKIH VVYSLSKDLG LPGFRVGLIY SNNEKVVSAA TKMSSFGLIS SQTQHLLANL LSDERFTTNY LEENKKRLRE RKDRLVSGLK EAGISCLKSN AGLFCWVDLR HLLKSNTFEA EHSLWTKIVC EVGLNISPGS SCHCDEPGWF RVCFANMSDQ TMEVAMDRVK GFVDNNNGGK QKRTMWDTRR RSLINKWVSK LSSVTCESER // ID 1A112_ARATH Reviewed; 495 AA. AC Q8GYY0; Q9C5W4; Q9FLJ0; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 2. DT 20-FEB-2007, entry version 26. DE Probable aminotransferase ACS12 (EC 2.6.1.-). GN Name=ACS12; OrderedLocusNames=At5g51690; ORFNames=K10D11.3, MIO24.18; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=98290546; PubMed=9628582; DOI=10.1093/dnares/5.1.41; RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. RT Sequence features of the regions of 1,456,315 bp covered by nineteen RT physically assigned P1 and TAC clones."; RL DNA Res. 5:41-54(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 290-495. RC STRAIN=cv. Columbia; RX MEDLINE=21932900; PubMed=11910074; DOI=10.1126/science.1071006; RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., RA Shibata K., Shinagawa A., Shinozaki K.; RT "Functional annotation of a full-length Arabidopsis cDNA collection."; RL Science 296:141-145(2002). RN [4] RP LACK OF ACS ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). CC -!- FUNCTION: Probable aminotransferase. Does not have 1- CC aminocyclopropane-1-carboxylate synthase (ACS) activity, CC suggesting that it is not involved in ethylene biosynthesis. CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in roots. Expressed at low level in CC leaves, stems, flowers and siliques. CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC -!- CAUTION: Contains a Phe residue instead of a Tyr in position 151, CC the Tyr residue being essential in substrate recognition by ACS CC enzymes. CC -!- CAUTION: Ref.1 sequence differs from that shown due to erroneous CC 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; AB010074; BAB11238.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF336920; AAG54001.1; -; mRNA. DR EMBL; BT000463; AAN17440.1; -; mRNA. DR EMBL; BT002111; AAN72122.1; -; mRNA. DR EMBL; AK117323; BAC41994.1; ALT_INIT; mRNA. DR UniGene; At.18827; -. DR UniGene; At.68524; -. DR PDB; 2GEA; Model; A=1-495. DR GenomeReviews; BA000015_GR; AT5G51690. DR KEGG; ath:At5g51690; -. DR TAIR; At5g51690; -. DR ArrayExpress; Q8GYY0; -. DR GermOnline; AT5G51690; Arabidopsis thaliana. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Transferase. FT CHAIN 1 495 Probable aminotransferase ACS12. FT /FTId=PRO_0000123906. FT BINDING 334 334 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 495 AA; 55214 MW; 66C89DF8501044A2 CRC64; MRLIVPLRGV IQGRGGLFVG SLIPCCLFYF LQLYLKRRRP PPSDPTDLPR TFSRTNLFSR GNSIGRVRVS SRAVPVAKPS DSPYYIGLER VKTDPYDRIT NTDGIIQLGL AESTLCFDLL QRWMSENLME SMMQSDDGEF DISSIAMYKP FEGLLELRVA FADFMSRIMG GNVSFDPSNM VITAGGTPAI EVLAFCLADH GNAFLIPTPY YPGFDRDIKF RTGVELIPVH CRSSDNFTVT VSALEQALNQ ARKRGSKVSG ILFSNPSNPV GNILSRETLC DILRFAQEKN IHVISDEIFA GSVYGDKEFV SMAEIAGSGE FDKTRVHIIY GLSKDLSIPG FRAGVIYSFH EDVVNAAKKL MRFSSVPVLV QRILISLLSD VRFIEGYMAA HRQRIRDKHI RFVEGLKQLG IPCAESGGGL YCWVDMSSLL TSYSEKGELE LFEKLLTVAK INATPGTACY CIEPGWFRCC FTALADEDIP VIMERIRQLA ESFRS // ID 1A11_ARATH Reviewed; 488 AA. AC Q06429; Q43368; Q9S9C6; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 2. DT 23-JAN-2007, entry version 43. DE 1-aminocyclopropane-1-carboxylate synthase-like protein 1. GN Name=ACS1; Synonyms=ACC2; OrderedLocusNames=At3g61510; GN ORFNames=F2A19.110; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ABSENCE OF ENZYME ACTIVITY, RP AND MUTAGENESIS OF SER-205. RC STRAIN=cv. Columbia; RX MEDLINE=96144243; PubMed=8566772; DOI=10.1016/0378-1119(95)00694-X; RA Liang X.-W., Oono Y., Shen N.F., Koehler C., Li K., Scolnik P.A., RA Theologis A.; RT "Characterization of two members (ACS1 and ACS3) of the 1- RT aminocyclopropane-1-carboxylate synthase gene family of Arabidopsis RT thaliana."; RL Gene 167:17-24(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE OF 57-88. RX MEDLINE=93066381; PubMed=1438312; RA Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.; RT "The 1-aminocyclopropane-1-carboxylate synthase gene family of RT Arabidopsis thaliana."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-152. RC STRAIN=cv. C24; TISSUE=Flower; RX MEDLINE=93028584; PubMed=1357670; RA van der Straeten D., Rodrigues-Pousada R.A., Villarroel R., Hanley S., RA Goodman H.M., Van Montagu M.; RT "Cloning, genetic mapping, and expression analysis of an Arabidopsis RT thaliana gene that encodes 1-aminocyclopropane-1-carboxylate RT synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:9969-9973(1992). RN [6] RP TISSUE SPECIFICITY. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). CC -!- FUNCTION: Unknown. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in young leaves and flowers. Not CC expressed in roots. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC -!- CAUTION: Lacks the conserved tripeptide Ser/Thr-Asn-Pro in CC position 205 necessary for the ACS 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; U26542; AAA96006.1; -; Genomic_DNA. DR EMBL; U26543; AAB60312.1; -; mRNA. DR EMBL; AL132962; CAB71081.1; -; Genomic_DNA. DR EMBL; AY133715; AAM91649.1; -; mRNA. DR EMBL; Z12615; CAA78261.1; -; mRNA. DR PIR; B47199; B47199. DR PIR; T47943; T47943. DR UniGene; At.945; -. DR HSSP; P18485; 1IAX. DR SMR; Q06429; 15-429. DR GenomeReviews; BA000014_GR; AT3G61510. DR KEGG; ath:At3g61510; -. DR GeneFarm; 4048; -. DR TAIR; At3g61510; -. DR ArrayExpress; Q06429; -. DR GermOnline; AT3G61510; Arabidopsis thaliana. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Pyridoxal phosphate. FT CHAIN 1 488 1-aminocyclopropane-1-carboxylate FT synthase-like protein 1. FT /FTId=PRO_0000123896. FT BINDING 273 273 Pyridoxal phosphate (covalent) (By FT similarity). FT MUTAGEN 205 205 S->TNPS: Restores ACS activity; when FT expressed in E.coli. SQ SEQUENCE 488 AA; 55003 MW; 411E049B993DEEE1 CRC64; MSQGACENQL LSKLALSDKH GEASPYFHGW KAYDNNPFHP THNPQGVIQM GLAENQLCSD LIKEWIKENP QASICTAEGI DSFSDIAVFQ DYHGLKQFRQ AIATFMERAR GGRVRFEAER VVMSGGATGA NETIMFCLAD PGDAFLVPTP YYAAFDRDLR WRTGVRIIPV ECSSSNNFQI TKQALESAYL KAQETGIKIK GLIISNPLGT SLDRETLESL VSFINDKQIH LVCDEIYAAT VFAEPGFISV AEIIQEMYYV NRDLIHIVYS LSKDMGLPGF RVGVVYSYND VVVSCARRMS SFGLVSSQTQ SFLAAMLSDQ SFVDNFLVEV SKRVAKRHHM FTEGLEEMGI SCLRSNAGLF VLMDLRHMLK DQTFDSEMAL WRVIINKVKI NVSPGSSFHC SEPGWFRVCF ANMDEDTLQI ALERIKDFVV GDRANKNKNC NCICNNKREN KKRKSFQKNL KLSLSSMRYE EHVRSPKLMS PHSPLLRA // ID 1A11_CUCMA Reviewed; 493 AA. AC P23599; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 31-OCT-2006, entry version 46. DE 1-aminocyclopropane-1-carboxylate synthase CMW33 (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN Name=ACS1; Synonyms=ACCW; OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3661; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Nakajima N., Mori H., Yamazaki K., Imaseki H.; RT "Molecular cloning and sequence of a complementary DNA encoding 1- RT aminocyclopropane-1-carboxylate synthase induced by tissue wounding."; RL Plant Cell Physiol. 31:1021-1029(1990). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- INDUCTION: By tissue wounding. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D01032; BAA00838.1; -; mRNA. DR PIR; JQ0926; JQ0926. DR HSSP; P18485; 1IAX. DR SMR; P23599; 18-435. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 493 1-aminocyclopropane-1-carboxylate FT synthase CMW33. FT /FTId=PRO_0000123907. FT BINDING 279 279 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 493 AA; 55896 MW; F39234AC99CBEF6B CRC64; MEFHQIDERN QALLSKIAVD DGHGENSPYF DGWKAYDNDP FHPEDNPLGV IQMGLAENQL SFDMIVDWIR KHPEASICTP KGLERFKSIA NFQDYHGLPE FRNGIASFMG KVRGGRVQFD PSRIVMGGGA TGASETVIFC LADPGDAFLV PSPYYAAFDR DLKWRTRAQI IRVHCNSSNN FQVTKAALEI AYKKAQEANI KVKGVIITNP SNPLGTTYDR DTLKTLVTFV NQHDIHLICD EIYSATVFKA PTFISIAQIV EEMEHCKKEL IHILYSLSKD MGLPGFRVGI IYSYNDVVVR RARQMSSFGL VSSQTQHLLA AMLSDEDFVD KFLAENSKRL AERHARFTKE LDKMGITCLN SNAGVFVWMD LRRLLKDQTF KAEMELWRVI INEVKLNVSP GSSFHVTEPG WFRVCFANMD DNTVDVALNR IHSFVENIDK KEDNTVAMPS KTRRRENKLR LSFSFSGRRY DEGNVLNSPH TMSPHSPLVI AKN // ID 1A11_CUCPE Reviewed; 493 AA. AC P23279; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 31-OCT-2006, entry version 50. DE 1-aminocyclopropane-1-carboxylate synthase 1 (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN Name=ACC1A; OS Cucurbita pepo (Vegetable marrow) (Summer squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3663; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91139670; PubMed=1995630; RA Sato T., Oeller P.W., Theologis A.; RT "The 1-aminocyclopropane-1-carboxylate synthase of Cucurbita. RT Purification, properties, expression in Escherichia coli, and primary RT structure determination by DNA sequence analysis."; RL J. Biol. Chem. 266:3752-3759(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91334397; PubMed=1871117; RA Huang P.-L., Parks J.E., Rottman W.H., Theologis A.; RT "Two genes encoding 1-aminocyclopropane-1-carboxylate synthase in RT zucchini (Cucurbita pepo) are clustered and similar but differentially RT regulated."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7021-7025(1991). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- INDUCTION: By wounding in fruit and etiolated hypocotyls. By CC indoleacetic acid (IAA)/benzyladenine/LiCl only in fruit tissue. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M58323; AAA33113.1; -; mRNA. DR EMBL; M61195; AAA33111.1; -; Genomic_DNA. DR PIR; A41141; A41141. DR HSSP; P18485; 1IAX. DR SMR; P23279; 18-435. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 493 1-aminocyclopropane-1-carboxylate FT synthase 1. FT /FTId=PRO_0000123909. FT BINDING 279 279 Pyridoxal phosphate (covalent). FT CONFLICT 177 177 G -> R (in Ref. 2). SQ SEQUENCE 493 AA; 55780 MW; 921DC3DFB17A8769 CRC64; MGFHQIDERN QALLSKIALD DGHGENSPYF DGWKAYDNDP FHPENNPLGV IQMGLAENQL SFDMIVDWIR KHPEASICTP EGLERFKSIA NFQDYHGLPE FRNAIANFMG KVRGGRVKFD PSRIVMGGGA TGASETVIFC LADPGDAFLV PSPYYAGFDR DLKWRTRAQI IRVHCNGSNN FQVTKAALEI AYKKAQEANM KVKGVIITNP SNPLGTTYDR DTLKTLVTFV NQHDIHLICD EIYSATVFKA PTFTSIAEIV EQMEHCKKEL IHILYSLSKD MGLPGFRVGI IYSYNDVVVR RARQMSSFGL VSSQTQHLLA AMLSDEDFVD KFLAENSKRV GERHARFTKE LDKMGITCLN SNAGVFVWMD LRRLLKDQTF KAEMELWRVI INEVKLNVSP GSSFHVTEPG WFRVCFANMD DNTVDVALNR IHSFVENIDK KEDNTVAMPS KTRHRDNKLR LSFSFSGRRY DEGNVLNSPH TMSPHSPLVI AKN // ID 1A11_HUMAN Reviewed; 365 AA. AC P13746; O19605; O19606; Q29747; Q29835; Q9BCN0; Q9MYI5; Q9TQE9; AC Q9TQP6; Q9TQP7; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 20-FEB-2007, entry version 69. DE HLA class I histocompatibility antigen, A-11 alpha chain precursor DE (MHC class I antigen A*11). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*1101 AND A*1102). RX MEDLINE=89030641; PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*1101 AND A*1102). RX MEDLINE=94287401; PubMed=8016845; RA Lin L., Tokunaga K., Ishikawa Y., Bannai M., Kashiwase K., Kuwata S., RA Akaza T., Tadokoro K., Shibata Y., Juji T.; RT "Sequence analysis of serological HLA-A11 split antigens, A11.1 and RT A11.2."; RL Tissue Antigens 43:78-82(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-365 (ALLELE A*1101). RX MEDLINE=87192928; PubMed=2437024; DOI=10.1007/BF00404694; RA Cowan E.P., Jelachich M.L., Biddison W.E., Coligan J.E.; RT "DNA sequence of HLA-A11: remarkable homology with HLA-A3 allows RT identification of residues involved in epitopes recognized by RT antibodies and T cells."; RL Immunogenetics 25:241-250(1987). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*1103). RC TISSUE=Blood; RX MEDLINE=20166353; PubMed=10703613; RX DOI=10.1034/j.1399-0039.2000.550113.x; RA Tijssen H.J., Sistermans E.A., van den Beucken M.J.G., Krausa P., RA Joosten I.; RT "Complete sequence analysis of the A*1103 allele."; RL Tissue Antigens 55:68-70(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) (A*1103). RC TISSUE=Blood; RX MEDLINE=20340071; PubMed=10885562; RX DOI=10.1034/j.1399-0039.2000.550504.x; RA Tijssen H.J., Sistermans E.A., Joosten I.; RT "A unique second donor splice site in the intron 5 sequence of the RT HLA-A*11 alleles results in a class I transcript encoding a molecule RT with an elongated cytoplasmic domain."; RL Tissue Antigens 55:422-428(2000). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE A*1104). RA Bettinotti M.P.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*1104). RA Chandanayingyong D., Sirikong M., Luangtrakool K., Srinak D., RA Rungroung E., Bejchandra S.; RT "A11 alleles (A*11O4)."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE (ALLELE A*1105). RX MEDLINE=99321035; PubMed=10395112; RX DOI=10.1034/j.1399-0039.1999.530612.x; RA Morrell G., Whalley J., Stewart A., Day S., Lewis L., Makar Y., RA Ross J., Dunn P.P.; RT "Identification of an HLA-A11 serological variant and its RT characterization by sequencing based typing."; RL Tissue Antigens 53:591-594(1999). RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*1105). RX MEDLINE=20309230; PubMed=10852390; RX DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*1107). RX MEDLINE=21561663; PubMed=11703829; RX DOI=10.1034/j.1399-0039.2001.580309.x; RA Pyo C.W., Choi H.B., Han H., Hong Y.S., Kim T.G.; RT "Identification of HLA-A*11 variant (A*1107) in the Korean RT population."; RL Tissue Antigens 58:190-192(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P13746-1; Sequence=Displayed; CC Name=2; Synonyms=Long; CC IsoId=P13746-2; Sequence=VSP_008099; CC Note=Only produced by allele A*1103; CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-11 are known: A*1101 (A- CC 11E), A*1102 (A-11K), A*1103, A*1104, A*1105 and A*1107. The CC sequence shown is that of A*1101. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X13111; CAA31503.1; -; mRNA. DR EMBL; X13112; CAA31504.1; -; mRNA. DR EMBL; D16841; BAA04117.1; -; mRNA. DR EMBL; D16842; BAA04118.1; -; mRNA. DR EMBL; M16010; AAA65449.1; -; Genomic_DNA. DR EMBL; M16007; AAA65449.1; JOINED; Genomic_DNA. DR EMBL; M16008; AAA65449.1; JOINED; Genomic_DNA. DR EMBL; M16009; AAA65449.1; JOINED; Genomic_DNA. DR EMBL; Y17224; CAB38056.1; -; mRNA. DR EMBL; Y17224; CAB38057.1; -; mRNA. DR EMBL; X91399; CAA62745.1; -; mRNA. DR EMBL; U50574; AAB60406.1; -; mRNA. DR EMBL; AF030910; AAB87052.1; -; Genomic_DNA. DR EMBL; AF030909; AAB87052.1; JOINED; Genomic_DNA. DR EMBL; AF030908; AAB87051.1; -; Genomic_DNA. DR EMBL; AF030907; AAB87051.1; JOINED; Genomic_DNA. DR EMBL; AJ306733; CAC37336.1; -; Genomic_DNA. DR EMBL; AF147455; AAD33991.1; -; Genomic_DNA. DR EMBL; AF147454; AAD33991.1; JOINED; Genomic_DNA. DR EMBL; AF165065; AAF25781.1; -; mRNA. DR PIR; I83063; I83063. DR PIR; S03536; A47636. DR UniGene; Hs.181244; -. DR PDB; 1Q94; X-ray; A/D=25-299. DR PDB; 1QVO; X-ray; A/D=25-299. DR PDB; 1X7Q; X-ray; A=25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P13746; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Alternative splicing; Glycoprotein; KW Host-virus interaction; Immune response; Membrane; MHC I; KW Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-11 alpha chain. FT /FTId=PRO_0000018816. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VAR_SEQ 337 337 S -> SGGEGVK (in isoform 2). FT /FTId=VSP_008099. FT VARIANT 43 43 E -> K (in allele A*1102). FT /FTId=VAR_004353. FT VARIANT 133 133 F -> L (in allele A*1107). FT /FTId=VAR_016731. FT VARIANT 168 168 K -> E (in allele A*1105). FT /FTId=VAR_016732. FT VARIANT 175 175 H -> R (in allele A*1103). FT /FTId=VAR_016733. FT VARIANT 176 176 A -> E (in allele A*1103). FT /FTId=VAR_016734. FT VARIANT 187 187 R -> T (in allele A*1104). FT /FTId=VAR_016735. FT VARIANT 345 345 T -> S (in allele A*1105). FT /FTId=VAR_016736. FT STRAND 27 36 FT TURN 39 40 FT STRAND 41 43 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT STRAND 113 115 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 159 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT TURN 244 245 FT TURN 250 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 294 297 SQ SEQUENCE 365 AA; 40937 MW; FE449CE2D4BF6CC5 CRC64; MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEDGSHTIQ IMYGCDVGPD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAAHAAEQQ RAYLEGRCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A11_ORYSA Reviewed; 487 AA. AC Q07215; Q6ATI2; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 20-FEB-2007, entry version 47. DE 1-aminocyclopropane-1-carboxylate synthase 1 (EC 4.4.1.14) (ACC DE synthase 1) (S-adenosyl-L-methionine methylthioadenosine-lyase 1). GN Name=ACC1; OrderedLocusNames=Os03g0727600, LOC_Os03g51740; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INDUCTION. RC STRAIN=cv. Indica / IR36; RX MEDLINE=93283732; PubMed=8389618; RA Zarembinski T.I., Theologis A.; RT "Anaerobiosis and plant growth hormones induce two genes encoding 1- RT aminocyclopropane-1-carboxylate synthase in rice (Oryza sativa L.)."; RL Mol. Biol. Cell 4:363-373(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RX PubMed=16109971; DOI=10.1101/gr.3869505; RG The rice chromosome 3 sequencing consortium; RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., RA Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., RA Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S., RA Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., RA Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., RA de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., RA Kim H.-I., Rambo T., Currie J., Collura K., Kernodle-Thompson S., RA Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., RA Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., RA Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., RA Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., RA Wilson R., Jin W., Lee H.R., Jiang J., Jackson S.; RT "Sequence, annotation, and analysis of synteny between rice chromosome RT 3 and diverged grass species."; RL Genome Res. 15:1284-1291(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-99. RX MEDLINE=93066381; PubMed=1438312; RA Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.; RT "The 1-aminocyclopropane-1-carboxylate synthase gene family of RT Arabidopsis thaliana."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- INDUCTION: By anaerobiosis and indoleacetic acid (IAA) + CC benzyladenine (BA) + LiCl treatment. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M96672; AAA33887.1; -; mRNA. DR EMBL; M96673; AAA33888.1; -; Genomic_DNA. DR EMBL; AC135956; AAT77071.1; -; Genomic_DNA. DR PIR; A47729; A47729. DR PIR; B46376; B46376. DR UniGene; Os.53146; -. DR HSSP; P37821; 1B8G. DR Gramene; Q07215; -. DR GO; GO:0005737; C:cytoplasm; IEP:Gramene. DR GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase ...; IEP:Gramene. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 487 1-aminocyclopropane-1-carboxylate FT synthase 1. FT /FTId=PRO_0000123916. FT BINDING 286 286 Pyridoxal phosphate (covalent) (By FT similarity). FT CONFLICT 129 129 T -> N (in Ref. 1; AAA33887). FT CONFLICT 151 151 L -> F (in Ref. 1; AAA33887). FT CONFLICT 188 188 P -> A (in Ref. 1). FT CONFLICT 273 273 D -> G (in Ref. 1; AAA33887). SQ SEQUENCE 487 AA; 53139 MW; 561D262125D7759E CRC64; MVSQVVAEEK PQLLSKKAGC NSHGQDSSYF LGWQEYEKNP FDPVSNPSGI IQMGLAENQL SFDLLEEWLE KNPHALGLRR EGGGASVFRE LALFQDYHGL PAFKNALARF MSEQRGYKVV FDPSNIVLTA GATSANEALM FCLADHGDAF LIPTPYYPGF DRDLKWRTGA EIVPVHCASA NGFRVTRPAL DDAYRRAQKR RLRVKGVLIT NPSNPLGTAS PRADLETIVD FVAAKGIHLI SDEIYAGTAF AEPPAGFVSA LEVVAGRDGG GADVSDRVHV VYSLSKDLGL PGFRVGAIYS ANAAVVSAAT KMSSFGLVSS QTQYLLAALL GDRDFTRSYV AENKRRIKER HDQLVDGLRE IGIGCLPSNA GLFCWVDMSH LMRSRSFAGE MELWKKVVFE VGLNISPGSS CHCREPGWFR VCFANMSAKT LDVAMQRLRS FVDSATGGGD NAALRRAAVP VRSVSCPLAI KWALRLTPSI ADRKAER // ID 1A11_PRUMU Reviewed; 492 AA. AC Q9MB95; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 31-OCT-2006, entry version 36. DE 1-aminocyclopropane-1-carboxylate synthase 1 (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN Name=ACS1; OS Prunus mume (Japanese flowering apricot). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Rosales; Rosaceae; Amygdaloideae; Prunus. OX NCBI_TaxID=102107; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Mita S., Kirita C., Kato M., Hyodo H.; RT "Expression of ACC synthase is enhanced earlier than that of ACC RT oxidase during fruit ripening of mume (Prunus mume)."; RL Physiol. Plantarum 107:319-328(1999). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB031026; BAA90549.1; -; mRNA. DR HSSP; P18485; 1IAX. DR SMR; Q9MB95; 17-433. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 492 1-aminocyclopropane-1-carboxylate FT synthase 1. FT /FTId=PRO_0000123918. FT BINDING 277 277 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 492 AA; 55066 MW; 2002047AF2B43D89 CRC64; MGSSSATANR FLLSKIATSE GHGENSPYFD GWKAYDRNPF HPTKNPEGVI QMGLAENQLS FDSIEDWIKK NPKASICTPE GVEEFKNVAI FQDYHGFPEF RKAVAMFMSK ARGGRVTFDP NRVVMSGGAT GANELVMFCL ADPGDAFLVP SPYYPAFFRD LGWRTGVQIV PVDCDSSNNF KITKEALEAA YEKAQKNNIN VKGLIITNPS NPLGTTLDRN TLESLVEFIN QKNIHLVCDE IYAATVFSSP TFTCISEVIQ NMNCNPNLIH IVYSLSKDMG LPGLRVGIVY SYNDDVVNIG RKMSSFGLVS SQTQHMLPSM LLDEEFVARF LETSPKRLAK RHGVFTKGLE EVGINCLKSN AGLFCWMDLR RLLEDQTFDG EMVLWRVIVN EVGPNVSPGS SFKCVEPGWF RVCFANMDDE TLEVALKRIR TFVRQGKKAQ DQVVQVKSPK RWKSNLRLSF SSSSTRRFDQ ESVNVLSPHM MSPHSPLVRA KT // ID 1A12_ARATH Reviewed; 496 AA. AC Q06402; Q941E7; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 23-JAN-2007, entry version 61. DE 1-aminocyclopropane-1-carboxylate synthase 2 (EC 4.4.1.14) (ACC DE synthase 2) (S-adenosyl-L-methionine methylthioadenosine-lyase 2). GN Name=ACS2; Synonyms=ACC1; OrderedLocusNames=At1g01480; GN ORFNames=F22L4.4; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1), RP AND VARIANT ILE-136. RC STRAIN=cv. Columbia; RX MEDLINE=93028584; PubMed=1357670; RA van der Straeten D., Rodrigues-Pousada R.A., Villarroel R., Hanley S., RA Goodman H.M., Van Montagu M.; RT "Cloning, genetic mapping, and expression analysis of an Arabidopsis RT thaliana gene that encodes 1-aminocyclopropane-1-carboxylate RT synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:9969-9973(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX MEDLINE=93066381; PubMed=1438312; RA Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.; RT "The 1-aminocyclopropane-1-carboxylate synthase gene family of RT Arabidopsis thaliana."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM RP 1). RC STRAIN=cv. Columbia; RX MEDLINE=98332714; PubMed=9666060; DOI=10.1016/S0378-1119(98)00286-8; RA Terryn N., Gielen J., De Keyser A., Van Den Daele H., Ardiles W., RA Neyt P., De Clercq R., Coppieters J., Dehais P., Villarroel R., RA Rouze P., Van Montagu M.; RT "Sequence analysis of a 40-kb Arabidopsis thaliana genomic region RT located at the top of chromosome 1."; RL Gene 215:11-17(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP MUTAGENESIS OF 206-THR--PRO-208. RC STRAIN=cv. Columbia; RX MEDLINE=96144243; PubMed=8566772; DOI=10.1016/0378-1119(95)00694-X; RA Liang X.-W., Oono Y., Shen N.F., Koehler C., Li K., Scolnik P.A., RA Theologis A.; RT "Characterization of two members (ACS1 and ACS3) of the 1- RT aminocyclopropane-1-carboxylate synthase gene family of Arabidopsis RT thaliana."; RL Gene 167:17-24(1995). RN [7] RP ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND PUTATIVE RP PROCESSING. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). RN [8] RP PHOSPHORYLATION AT SER-483; SER-488 AND SER-491. RX PubMed=15539472; DOI=10.1105/tpc.104.026609; RA Liu Y., Zhang S.; RT "Phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase by RT MPK6, a stress-responsive mitogen-activated protein kinase, induces RT ethylene biosynthesis in Arabidopsis."; RL Plant Cell 16:3386-3399(2004). CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of CC ethylene. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=45 uM for AdoMet; CC Vmax=32 uM/h/mg enzyme; CC pH dependence: CC Optimum pH is 8.2; CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of CC heterodimerization with other ACS enzymes is however unsure (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q06402-1; Sequence=Displayed; CC Name=2; CC IsoId=Q06402-2; Sequence=VSP_009111; CC -!- TISSUE SPECIFICITY: High in developing leaves and in flowers. CC Expressed in roots and siliques. CC -!- INDUCTION: By ethylene. By indole-3-acetic acid (IAA) and CC cycloheximide (CHX). CC -!- PTM: Phosphorylated on serine residue by MAP kinase (MPK6). CC -!- PTM: May be processed at its C-terminus. CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation CC of such stability, play a central role in ethylene biosynthesis. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z12614; CAA78260.1; -; Genomic_DNA. DR EMBL; M95594; AAA97516.1; -; Genomic_DNA. DR EMBL; M95595; AAB59298.1; -; mRNA. DR EMBL; Y12776; CAA73310.1; -; Genomic_DNA. DR EMBL; AC061957; AAF81308.1; -; Genomic_DNA. DR EMBL; AF334719; AAG50097.1; -; mRNA. DR EMBL; AY052207; AAK97678.1; -; mRNA. DR EMBL; AY143877; AAN28816.1; -; mRNA. DR PIR; A47199; A47199. DR UniGene; At.164; -. DR HSSP; P18485; 1IAX. DR GenomeReviews; CT485782_GR; AT1G01480. DR KEGG; ath:At1g01480; -. DR GeneFarm; 4049; -. DR TAIR; At1g01480; -. DR ArrayExpress; Q06402; -. DR GermOnline; AT1G01480; Arabidopsis thaliana. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Alternative splicing; Ethylene biosynthesis; Fruit ripening; Lyase; KW Phosphorylation; Polymorphism; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 496 1-aminocyclopropane-1-carboxylate FT synthase 2. FT /FTId=PRO_0000123897. FT BINDING 55 55 Substrate (By similarity). FT BINDING 93 93 Substrate (By similarity). FT BINDING 279 279 Pyridoxal phosphate (covalent) (By FT similarity). FT MOD_RES 483 483 Phosphoserine. FT MOD_RES 488 488 Phosphoserine. FT MOD_RES 491 491 Phosphoserine. FT VAR_SEQ 1 106 Missing (in isoform 2). FT /FTId=VSP_009111. FT VARIANT 136 136 M -> I. FT MUTAGEN 206 208 Missing: Abolishes 1-aminocyclopropane-1- FT carboxylate synthase function. SQ SEQUENCE 496 AA; 55532 MW; 766318AE9B5F1566 CRC64; MGLPGKNKGA VLSKIATNNQ HGENSEYFDG WKAYDKDPFH LSRNPHGIIQ MGLAENQLCL DLIKDWVKEN PEASICTLEG IHQFSDIANF QDYHGLKKFR QAIAHFMGKA RGGRVTFDPE RVVMSGGATG ANETIMFCLA DPGDVFLIPS PYYAAFDRDL RWRTGVEIIP VPCSSSDNFK LTVDAAEWAY KKAQESNKKV KGLILTNPSN PLGTMLDKDT LTNLVRFVTR KNIHLVVDEI YAATVFAGGD FVSVAEVVND VDISEVNVDL IHIVYSLSKD MGLPGFRVGI VYSFNDSVVS CARKMSSFGL VSSQTQLMLA SMLSDDQFVD NFLMESSRRL GIRHKVFTTG IKKADIACLT SNAGLFAWMD LRHLLRDRNS FESEIELWHI IIDRVKLNVS PGSSFRCTEP GWFRICFANM DDDTLHVALG RIQDFVSKNK NKIVEKASEN DQVIQNKSAK KLKWTQTNLR LSFRRLYEDG LSSPGIMSPH SPLLRA // ID 1A12_CUCMA Reviewed; 475 AA. AC Q00257; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 31-OCT-2006, entry version 48. DE 1-aminocyclopropane-1-carboxylate synthase CMA101 (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN Name=ACS2; Synonyms=PCVV4A; OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3661; RN [1] RP NUCLEOTIDE SEQUENCE. RA Nakagawa N., Mori H., Yamazaki K., Imaseki H.; RT "Cloning of a complementary DNA for auxin-induced 1-aminocyclopropane- RT 1-carboxylate synthase and differential expression of the gene by RT auxin and wounding."; RL Plant Cell Physiol. 32:1153-1163(1991). RN [2] RP NUCLEOTIDE SEQUENCE. RA Nakagawa N., Kamiya Y., Imaseki H.; RT "Nucleotide sequence of an auxin-regulated 1-aminocyclopropane-1- RT carboxylic acid synthase gene from Cucurbita maxima Duch."; RL (er) Plant Gene Register PGR95-110. CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- INDUCTION: By tissue wounding and auxin. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U37774; AAA91152.1; -; Genomic_DNA. DR EMBL; D01033; BAA00839.1; -; mRNA. DR PIR; JQ2214; JQ2214. DR HSSP; P37821; 1M7Y. DR SMR; Q00257; 10-430. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 475 1-aminocyclopropane-1-carboxylate FT synthase CMA101. FT /FTId=PRO_0000123908. FT BINDING 272 272 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 475 AA; 53481 MW; D02A666E137F44A0 CRC64; MKMLSTKATC NSHGQDSSYF LGWEAYENNP FHHTSNPNGI IQMGLAENQL SFDLLESWLS KNPDAASFKR DGKSIFRELA LFQDYHGLPA FKKALVEFMA EIRGNKVSFE ANNIVLTAGA TSANETLMFC LAEAGDAFLL PTPYYPGFDR DLKWRTGVEI VPIHCTSSNG FQITQSALEQ AYKDAQTRNL RVKGVLVTNP SNPLGTTMNR DELNLVFDFI TSKGIHLISD EIYSGTVFGS PGFVSAMEVL KERSSEDEEV WKRVHIVYSL SKDLGLPGFR VGAIYSNDDM VVAAATKMSS FGLVSSQTQY LLSAMLSDKK FTISYISENQ KRLKQRQKML VSGLQKAGIN CLDSNAGLFC WVDMRHLLES DKFESELELW KKIVYEVGLN ISPGSSCHCT EPGWFRVCFA NMSESTLKLA VRRLKSFVTE LRSTTTSNHR NHDNKICKNI KKNIFTKWVF RQSAQEANRK MQAER // ID 1A12_CUCPE Reviewed; 494 AA. AC Q00379; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 46. DE 1-aminocyclopropane-1-carboxylate synthase 2 (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN Name=ACS2; Synonyms=ACC1B; OS Cucurbita pepo (Vegetable marrow) (Summer squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3663; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91334397; PubMed=1871117; RA Huang P.-L., Parks J.E., Rottman W.H., Theologis A.; RT "Two genes encoding 1-aminocyclopropane-1-carboxylate synthase in RT zucchini (Cucurbita pepo) are clustered and similar but differentially RT regulated."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7021-7025(1991). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- INDUCTION: Hormones, such as auxin, environmental factors, such as CC mechanical wounding and a number of chemicals. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M61195; AAA33112.1; -; Genomic_DNA. DR PIR; B41141; B41141. DR HSSP; P18485; 1IAX. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 494 1-aminocyclopropane-1-carboxylate FT synthase 2. FT /FTId=PRO_0000123910. FT BINDING 279 279 Pyridoxal phosphate (covalent) (By FT similarity). FT CONFLICT 345 345 A -> AS (in Ref. 1; AAA33112). SQ SEQUENCE 494 AA; 55923 MW; 02AE029AA4912C36 CRC64; MGFHQIDERN QALLSKIAID DGHGENSAYF DGWKAYDNNP FHPENNPLGV IQMGLAENQL SFGMIVDWIR KHPEASICTP EGLEKFKSIA NFQDYHGLQE FRKAMASFMG KVRGGRVKFD PSRIVMGGGA TGASETVIFC LADPGDAFLV PSPYYAAFDR DLKWRTRAQI IPVHCNSSNN FQVTEAALEI AYKKAQEANM KVKGVIITNP SNPLGTTYDR DTLKTLVTFV NQHDIHLICD EIYSATVFKA PTFTSIAEIV EQMEHCKKEL IHILYSLSKD MGLPGFRVGI IYSYNDVVVR RARQMSSFGL VSSQTQHLLA AMLSDEDFVD KFLAENSKRL GERHARFTKE LDKMGITCLN SNAGVFVWMD LRRLLKDQTF KAEMELWRVI INEVKLNVSP GSSFHVTEPG WFRVCFANMD DNTVDVALNR IHSFVENIDK KEDNTVAMPS KTRHRDNKLR LSFSFSGRRY DKGNVLNSPH TMSPHSPLVR ARTY // ID 1A12_SOLLC Reviewed; 485 AA. AC P18485; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 2. DT 31-OCT-2006, entry version 69. DE 1-aminocyclopropane-1-carboxylate synthase 2 (EC 4.4.1.14) (ACC DE synthase 2) (S-adenosyl-L-methionine methylthioadenosine-lyase 2) DE (ACS-2) (Le-ACS2). GN Name=ACS2; Synonyms=ACC2, PCVV4A; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC TISSUE=Etiolated hypocotyl; RX MEDLINE=92106351; PubMed=1762159; RA Rottmann W.H., Peter G.F., Oeller P.W., Keller J.A., Shen N.F., RA Nagy B.P., Taylor L.P., Campbell A.D., Theologis A.; RT "1-aminocyclopropane-1-carboxylate synthase in tomato is encoded by a RT multigene family whose transcription is induced during fruit and RT floral senescence."; RL J. Mol. Biol. 222:937-961(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=cv. Orlando; TISSUE=Fruit; RX MEDLINE=90280476; PubMed=2191304; RA van der Straeten D., van Wiemeersch L., Goodman H.M., van Montagu M.; RT "Cloning and sequence of two different cDNAs encoding 1- RT aminocyclopropane-1-carboxylate synthase in tomato."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4859-4863(1990). RN [3] RP HOMODIMERIZATION, AND MUTAGENESIS OF TYR-92 AND LYS-278. RX MEDLINE=98241624; PubMed=9575209; DOI=10.1074/jbc.273.20.12509; RA Tarun A.S., Theologis A.; RT "Complementation analysis of mutants of 1-aminocyclopropane-1- RT carboxylate synthase reveals the enzyme is a dimer with shared active RT sites."; RL J. Biol. Chem. 273:12509-12514(1998). RN [4] RP MUTAGENESIS OF ARG-286. RX MEDLINE=20027433; PubMed=10557240; DOI=10.1104/pp.121.3.913; RA Zhou H., Wang H.W., Zhu K., Sui S.F., Xu P., Yang S.F., Li N.; RT "The multiple roles of conserved arginine 286 of 1-aminocyclopropane- RT 1-carboxylate synthase. Coenzyme binding, substrate binding, and RT beyond."; RL Plant Physiol. 121:913-919(1999). RN [5] RP PHOSPHORYLATION AT SER-460. RX MEDLINE=21359418; PubMed=11375393; DOI=10.1074/jbc.M101543200; RA Tatsuki M., Mori H.; RT "Phosphorylation of tomato 1-aminocyclopropane-1-carboxylic acid RT synthase, LE-ACS2, at the C-terminal region."; RL J. Biol. Chem. 276:28051-28057(2001). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-438. RX MEDLINE=21474282; PubMed=11431475; DOI=10.1074/jbc.M103840200; RA Huai Q., Xia Y., Chen Y., Callahan B., Li N., Ke H.; RT "Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) RT synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'- RT phosphate provide new insight into catalytic mechanisms."; RL J. Biol. Chem. 276:38210-38216(2001). CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of CC ethylene. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of CC heterodimerization with other ACS enzymes is however unsure. CC -!- INDUCTION: Hormones, such as auxin, environmental factors, such as CC mechanical wounding and a number of chemicals. CC -!- PTM: Phosphorylated on Ser 460; phosphorylation may regulate its CC turnover. CC -!- PTM: May be processed at its C-terminus. CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation CC of such stability, play a central role in ethylene biosynthesis. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X59139; CAA41855.1; -; Genomic_DNA. DR EMBL; X59145; CAA41856.1; -; mRNA. DR EMBL; M34289; AAA81580.1; -; mRNA. DR PIR; S19677; S19677. DR PDB; 1IAX; X-ray; A/B=11-438. DR PDB; 1IAY; X-ray; A=11-438. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW 3D-structure; Direct protein sequencing; Ethylene biosynthesis; KW Fruit ripening; Lyase; Phosphorylation; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 485 1-aminocyclopropane-1-carboxylate FT synthase 2. FT /FTId=PRO_0000123912. FT BINDING 55 55 Substrate. FT BINDING 92 92 Substrate. FT BINDING 278 278 Pyridoxal phosphate (covalent). FT MOD_RES 460 460 Phosphoserine. FT MUTAGEN 92 92 Y->F: Loss of function; when expressed FT alone in E.Coli. Partially complemented; FT when coexpressed with another ACS2 FT protein mutated on K-278. FT MUTAGEN 278 278 K->A: Loss of function; when expressed FT alone in E.Coli. Partially complemented; FT when coexpressed with another ACS2 FT protein mutated on Y-72. FT MUTAGEN 286 286 R->L: Loss of function; due to a strong FT reduction in both substrate and pyridoxal FT phosphate binding. FT MUTAGEN 460 460 S->G: Abolishes phosphoryaltion. FT MUTAGEN 462 462 S->G: No effect. FT CONFLICT 124 124 A -> V (in Ref. 1; CAA41856). FT CONFLICT 322 322 L -> P (in Ref. 2). FT CONFLICT 399 399 P -> L (in Ref. 2). FT HELIX 14 17 FT TURN 27 28 FT HELIX 29 36 FT TURN 41 43 FT TURN 45 46 FT STRAND 47 50 FT TURN 58 59 FT HELIX 60 66 FT TURN 67 68 FT STRAND 69 71 FT HELIX 83 88 FT TURN 92 93 FT HELIX 96 109 FT TURN 110 113 FT HELIX 118 120 FT STRAND 122 125 FT HELIX 126 138 FT TURN 141 142 FT STRAND 144 150 FT TURN 153 154 FT HELIX 155 158 FT TURN 159 163 FT STRAND 166 170 FT HELIX 174 176 FT TURN 177 178 FT HELIX 182 194 FT TURN 195 196 FT STRAND 199 207 FT TURN 209 211 FT HELIX 217 228 FT TURN 229 231 FT STRAND 233 237 FT TURN 239 240 FT HELIX 241 243 FT STRAND 246 248 FT HELIX 253 256 FT TURN 257 258 FT HELIX 260 262 FT TURN 263 264 FT HELIX 267 269 FT STRAND 270 281 FT HELIX 283 285 FT STRAND 287 293 FT HELIX 295 304 FT HELIX 305 308 FT HELIX 312 322 FT TURN 323 323 FT HELIX 325 352 FT TURN 353 354 FT STRAND 361 369 FT HELIX 371 373 FT STRAND 375 378 FT HELIX 379 391 FT TURN 392 392 FT HELIX 400 403 FT TURN 404 404 FT TURN 408 409 FT STRAND 410 414 FT STRAND 416 418 FT HELIX 420 435 FT TURN 436 437 SQ SEQUENCE 485 AA; 54663 MW; 40B3F55B5EF0D9C7 CRC64; MGFEIAKTNS ILSKLATNEE HGENSPYFDG WKAYDSDPFH PLKNPNGVIQ MGLAENQLCL DLIEDWIKRN PKGSICSEGI KSFKAIANFQ DYHGLPEFRK AIAKFMEKTR GGRVRFDPER VVMAGGATGA NETIIFCLAD PGDAFLVPSP YYPAFNRDLR WRTGVQLIPI HCESSNNFKI TSKAVKEAYE NAQKSNIKVK GLILTNPSNP LGTTLDKDTL KSVLSFTNQH NIHLVCDEIY AATVFDTPQF VSIAEILDEQ EMTYCNKDLV HIVYSLSKDM GLPGFRVGII YSFNDDVVNC ARKMSSFGLV STQTQYFLAA MLSDEKFVDN FLRESAMRLG KRHKHFTNGL EVVGIKCLKN NAGLFCWMDL RPLLRESTFD SEMSLWRVII NDVKLNVSPG SSFECQEPGW FRVCFANMDD GTVDIALARI RRFVGVEKSG DKSSSMEKKQ QWKKNNLRLS FSKRMYDESV LSPLSSPIPP SPLVR // ID 1A13_SOLLC Reviewed; 469 AA. AC Q42881; Q96571; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 41. DE 1-aminocyclopropane-1-carboxylate synthase 3 (EC 4.4.1.14) (ACC DE synthase 3) (S-adenosyl-L-methionine methylthioadenosine-lyase 3) DE (ACS-3) (Le-ACS3). GN Name=ACS3; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. VFN8; TISSUE=Leaf, and Root; RX MEDLINE=95294010; PubMed=7775465; DOI=10.1074/jbc.270.23.14056; RA Olson D.C., Oetiker J.H., Yang S.F.; RT "Analysis of LE-ACS3, a 1-aminocyclopropane-1-carboxylic acid synthase RT gene expressed during flooding in the roots of tomato plants."; RL J. Biol. Chem. 270:14056-14061(1995). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Rutgers; RA Kawakita K., Hennig L., Rottmann W.R., Yu G.X., Zarembinski T.I., RA Taylor L.D., Theologis A.; RT "The tomato 1-aminocyclopropane-1-carboxylate (ACC) synthase multigene RT family is encoded by at least eight members."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP PARTIAL PROTEIN SEQUENCE. RX MEDLINE=91045911; PubMed=2122449; RA Yip W.K., Dong J.G., Kenny J.W., Thompson G.A., Yang S.F.; RT "Characterization and sequencing of the active site of 1- RT aminocyclopropane-1-carboxylate synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 87:7930-7934(1990). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- INDUCTION: By flooding. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L34171; AAA78789.1; -; Genomic_DNA. DR EMBL; U18055; AAB48946.1; -; Genomic_DNA. DR EMBL; U17972; AAB48945.1; -; mRNA. DR PIR; A57540; A57540. DR UniGene; Les.3642; -. DR HSSP; P37821; 1M7Y. DR SMR; Q42881; 12-428. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Direct protein sequencing; Ethylene biosynthesis; Fruit ripening; KW Lyase; Pyridoxal phosphate; S-adenosyl-L-methionine. FT CHAIN 1 469 1-aminocyclopropane-1-carboxylate FT synthase 3. FT /FTId=PRO_0000123913. FT BINDING 272 272 Pyridoxal phosphate (covalent). FT CONFLICT 243 243 F -> L (in Ref. 2). FT CONFLICT 335 335 K -> R (in Ref. 2). SQ SEQUENCE 469 AA; 53094 MW; FA5ADCCE3F54F5BC CRC64; MKLLSEKATC NSHGQDSSYF LGWQEYEKNP YDEIQNPKGI IQMGLAENQL SFDLLESWLA QNPDAAGFKR NGESIFRELA LFQDYHGLPA FKNAMTKFMS EIRGNRVSFD SNNLVLTAGA TSANETLMFC LANQGDAFLL PTPYYPGFDR DLKWRTGAEI VPIHCSSSNG FRITESALEE AYLDAKKRNL KVKGVLVTNP SNPLGTTLNR NELELLLTFI DEKGIHLISD EIYSGTVFNS PGFVSVMEVL IEKNYMKTRV WERVHIVYSL SKDLGLPGFR IGAIYSNDEM VVSAATKMSS FGLVSSQTQY LLSCMLSDKK FTKKYISENQ KRLKKRHAML VKGLKSAGIN CLESNAGLFC WVDMRHLLSS NNFDAEMDLW KKIVYDVGLN ISPGSSCHCT EPGWFRVCFA NMSEDTLDLA MRRIKDFVES TAPNATNHQN QQQSNANSKK KSFSKWVFRL SFNDRQRER // ID 1A14_ARATH Reviewed; 474 AA. AC Q43309; Q9S9C4; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 44. DE 1-aminocyclopropane-1-carboxylate synthase 4 (EC 4.4.1.14) (ACC DE synthase 4) (S-adenosyl-L-methionine methylthioadenosine-lyase 4). GN Name=ACS4; Synonyms=ACC4; OrderedLocusNames=At2g22810; GN ORFNames=T20K9.2; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND RP INDUCTION. RC STRAIN=cv. Columbia; RX MEDLINE=95370228; PubMed=7642574; DOI=10.1074/jbc.270.32.19093; RA Abel S., Nguyen M.D., Chow W., Theologis A.; RT "ACS4, a primary indoleacetic acid-responsive gene encoding 1- RT aminocyclopropane-1-carboxylate synthase in Arabidopsis thaliana. RT Structural characterization, expression in Escherichia coli, and RT expression characteristics in response to auxin."; RL J. Biol. Chem. 270:19093-19099(1995). RN [2] RP ERRATUM. RA Abel S., Nguyen M.D., Chow W., Theologis A.; RL J. Biol. Chem. 270:26020-26020(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE OF 50-81. RX MEDLINE=93066381; PubMed=1438312; RA Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.; RT "The 1-aminocyclopropane-1-carboxylate synthase gene family of RT Arabidopsis thaliana."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992). RN [6] RP ENZYME ACTIVITY, AND INDUCTION. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of CC ethylene. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=15 uM for AdoMet; CC Vmax=31.20 uM/h/mg enzyme; CC pH dependence: CC Optimum pH is 7.8; CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of CC heterodimerization with other ACS enzymes is however unsure (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers. CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). CC By auxin. CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation CC of such stability, play a central role in ethylene biosynthesis. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U23481; AAC49037.1; -; mRNA. DR EMBL; U23482; AAA85039.1; -; Genomic_DNA. DR EMBL; AC004786; AAC32428.1; -; Genomic_DNA. DR EMBL; AC005617; AAM15065.1; -; Genomic_DNA. DR EMBL; AF332404; AAG48767.1; -; mRNA. DR PIR; B84617; B84617. DR PIR; G46376; G46376. DR UniGene; At.1549; -. DR HSSP; P37821; 1B8G. DR SMR; Q43309; 10-431. DR GenomeReviews; CT485783_GR; AT2G22810. DR KEGG; ath:At2g22810; -. DR GeneFarm; 4050; -. DR TAIR; At2g22810; -. DR ArrayExpress; Q43309; -. DR GermOnline; AT2G22810; Arabidopsis thaliana. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 474 1-aminocyclopropane-1-carboxylate FT synthase 4. FT /FTId=PRO_0000123898. FT BINDING 47 47 Substrate (By similarity). FT BINDING 85 85 Substrate (By similarity). FT BINDING 273 273 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 474 AA; 53795 MW; 98FD27622EAF3C21 CRC64; MVQLSRKATC NSHGQVSSYF LGWEEYEKNP YDVTKNPQGI IQMGLAENQL CFDLLESWLA QNTDAACFKR DGQSVFRELA LFQDYHGLSS FKNAFADFMS ENRGNRVSFD SNNLVLTAGA TSANETLMFC LADPGDAFLL PTPYYPGFDR DLKWRTGVEI VPIQSSSTNG FRITKLALEE AYEQAKKLDL NVKGILITNP SNPLGTTTTQ TELNILFDFI TKNKNIHLVS DEIYSGTVFN SSEFISVMEI LKNNQLENTD VLNRVHIVCS LSKDLGLPGF RVGAIYSNDK DVISAATKMS SFGLVSSQTQ YLLSSLLSDK KFTKNYLREN QKRLKNRQRK LVLGLEAIGI KCLKSNAGLF CWVDMRPLLR SKTFEAEMDL WKKIVYEVKL NISPGSSCHC EEPGWFRVCF ANMIDETLKL ALKRLKMLVD DENSSRRCQK SKSERLNGSR KKTMSNVSNW VFRLSFHDRE AEER // ID 1A14_SOLLC Reviewed; 476 AA. AC P29535; Q42894; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 55. DE 1-aminocyclopropane-1-carboxylate synthase 4 (EC 4.4.1.14) (ACC DE synthase 4) (S-adenosyl-L-methionine methylthioadenosine-lyase 4) DE (ACS-4) (Le-ACS4). GN Name=ACS4; Synonyms=ACC4, BTAS4, PCVV4B; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Caruso; TISSUE=Etiolated hypocotyl; RX MEDLINE=93374928; PubMed=8366090; RA Lincoln J.E., Campbell A.D., Oetiker J., Rottmann W.H., Oeller P.W., RA Shen N.F., Theologis A.; RT "LE-ACS4, a fruit ripening and wound-induced 1-aminocyclopropane-1- RT carboxylate synthase gene of tomato (Lycopersicon esculentum). RT Expression in Escherichia coli, structural characterization, RT expression characteristics, and phylogenetic analysis."; RL J. Biol. Chem. 268:19422-19430(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Etiolated hypocotyl; RX MEDLINE=92106351; PubMed=1762159; RA Rottmann W.H., Peter G.F., Oeller P.W., Keller J.A., Shen N.F., RA Nagy B.P., Taylor L.P., Campbell A.D., Theologis A.; RT "1-aminocyclopropane-1-carboxylate synthase in tomato is encoded by a RT multigene family whose transcription is induced during fruit and RT floral senescence."; RL J. Mol. Biol. 222:937-961(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91271385; PubMed=1711229; RA Olson D.C., White J.A., Edelman L., Harkins R.N., Kende H.; RT "Differential expression of two genes for 1-aminocyclopropane-1- RT carboxylate synthase in tomato fruits."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5340-5344(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-159. RC STRAIN=cv. Orlando; TISSUE=Fruit; RX MEDLINE=90280476; PubMed=2191304; RA van der Straeten D., van Wiemeersch L., Goodman H.M., van Montagu M.; RT "Cloning and sequence of two different cDNAs encoding 1- RT aminocyclopropane-1-carboxylate synthase in tomato."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4859-4863(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 235-307, AND INDUCTION. RC TISSUE=Pericarp; RX MEDLINE=92196141; PubMed=1549612; RA Yip W.K., Moore T., Yang S.F.; RT "Differential accumulation of transcripts for four tomato 1- RT aminocyclopropane-1-carboxylate synthase homologs under various RT conditions."; RL Proc. Natl. Acad. Sci. U.S.A. 89:2475-2479(1992). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- INDUCTION: Associated with fruit ripening, but unresponsive to CC auxin treatment in vegetative tissue. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M88487; AAA03164.1; -; Unassigned_DNA. DR EMBL; X59146; CAA41857.1; -; mRNA. DR EMBL; M63490; AAA34131.1; -; mRNA. DR EMBL; M38705; AAA81581.1; -; mRNA. DR EMBL; M83329; AAA68623.1; -; mRNA. DR PIR; S19679; S19679. DR UniGene; Les.3661; -. DR HSSP; P18485; 1IAX. DR SMR; P29535; 21-438. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 476 1-aminocyclopropane-1-carboxylate FT synthase 4. FT /FTId=PRO_0000123914. FT BINDING 282 282 Pyridoxal phosphate (covalent) (By FT similarity). FT CONFLICT 15 15 V -> A (in Ref. 2). FT CONFLICT 82 82 T -> A (in Ref. 4). FT CONFLICT 253 253 S -> P (in Ref. 2 and 5). SQ SEQUENCE 476 AA; 53537 MW; 9BC7D97BD64CB044 CRC64; MDLETSEISN YKSSVVLSKL ASNEQHGENS PYFDGWKAYD NDPFHLVNNL NGVIQMGLAE NQLSVDLIEE WIKRNPKASI CTNDGIESFR RIANFQDYHG LPEFTNAIAK FMEKTRGGKV KFDAKRVVMA GGATGANETL ILCLADPGDA FLVPTPYYPG FNRDLRWRSG VQLLPISCKS CNNFKITIEA IEEAYEKGQQ ANVKIKGLIL TNPCNPLGTI LDRDTLKKIS TFTNEHNIHL VCDEIYAATV FNSPKFVSIA EIINEDNCIN KDLVHIVSSL SKDLGFPGFR VGIVYSFNDD VVNCARKMSS FGLVSTQTQH LLAFMLSDDE FVEEFLIESA KRLRERYEKF TRGLEEIGIK CLESNAGVYC WMDLRSLLKE ATLDAEMSLW KLIINEVKLN VSPGSSFNCS EVGWFRVCFA NIDDQTMEIA LARIRMFMDA YNNVNKNGVM KNKHNGRGTT YDLTPQMGST MKMLLA // ID 1A15_ARATH Reviewed; 470 AA. AC Q37001; O49537; Q9S9C3; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 44. DE 1-aminocyclopropane-1-carboxylate synthase 5 (EC 4.4.1.14) (ACC DE synthase 5) (S-adenosyl-L-methionine methylthioadenosine-lyase 5) DE (Ethylene-overproduction protein 2). GN Name=ACS5; Synonyms=ACC5, ETO2; OrderedLocusNames=At5g65800; GN ORFNames=MPA24.15, F6H11.90; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=cv. Columbia; TISSUE=Seedling; RX PubMed=9011084; RA Liang X.-W., Shen N.F., Theologis A.; RT "Li(+)-regulated 1-aminocyclopropane-1-carboxylate synthase gene RT expression in Arabidopsis thaliana."; RL Plant J. 10:1027-1036(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=98290546; PubMed=9628582; DOI=10.1093/dnares/5.1.41; RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. RT Sequence features of the regions of 1,456,315 bp covered by nineteen RT physically assigned P1 and TAC clones."; RL DNA Res. 5:41-54(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016721; PubMed=11130714; DOI=10.1038/35048507; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE OF 50-81. RX MEDLINE=93066381; PubMed=1438312; RA Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.; RT "The 1-aminocyclopropane-1-carboxylate synthase gene family of RT Arabidopsis thaliana."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992). RN [6] RP MUTANT ETO2. RX PubMed=12566591; DOI=10.1105/tpc.006882; RA Chae H.S., Faure F., Kieber J.J.; RT "The eto1, eto2, and eto3 mutations and cytokinin treatment increase RT ethylene biosynthesis in Arabidopsis by increasing the stability of RT ACS protein."; RL Plant Cell 15:545-559(2003). RN [7] RP ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND PUTATIVE RP PROCESSING. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). RN [8] RP DEGRADATION, AND INTERACTION WITH ETO1; EOL1 AND EOL2. RX PubMed=15118728; DOI=10.1038/nature02516; RA Wang K.L.-C., Yoshida H., Lurin C., Ecker J.R.; RT "Regulation of ethylene gas biosynthesis by the Arabidopsis ETO1 RT protein."; RL Nature 428:945-950(2004). CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of CC ethylene. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=37 uM for S-adenosyl-L-methionine; CC Vmax=81.70 uM/h/mg enzyme; CC pH dependence: CC Optimum pH is 7.8; CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of CC heterodimerization with other ACS enzymes is however unsure (By CC similarity). Interacts with ETO1, EOL1 and EOL2 via its C-terminal CC region. CC -!- INTERACTION: CC O65020:ETO1; NbExp=2; IntAct=EBI-593450, EBI-593440; CC -!- TISSUE SPECIFICITY: Expressed in roots and siliques. CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). CC In response to low dose of cytokinin. CC -!- PTM: May be processed at its C-terminus. CC -!- PTM: Ubiquitinated (Probable). The interaction with ETO1 (and CC possibly EOL1 and EOL2) mediate its proteasome-dependent CC degradation. Its stability and degradation plays a central role in CC ethylene biosynthesis. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L29261; AAA87292.1; -; mRNA. DR EMBL; L29260; AAA87291.1; -; Genomic_DNA. DR EMBL; AB010075; BAB10687.1; -; Genomic_DNA. DR EMBL; AB020743; BAB10687.1; JOINED; Genomic_DNA. DR EMBL; AL021684; CAA16680.1; -; Genomic_DNA. DR EMBL; AF334720; AAG50098.1; -; mRNA. DR PIR; S71174; S71174. DR UniGene; At.1918; -. DR HSSP; P37821; 1B8G. DR SMR; Q37001; 17-428. DR IntAct; Q37001; -. DR GenomeReviews; BA000015_GR; AT5G65800. DR KEGG; ath:At5g65800; -. DR TAIR; At5g65800; -. DR ArrayExpress; Q37001; -. DR GermOnline; AT5G65800; Arabidopsis thaliana. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine; Ubl conjugation. FT CHAIN 1 470 1-aminocyclopropane-1-carboxylate FT synthase 5. FT /FTId=PRO_0000123899. FT BINDING 47 47 Substrate (By similarity). FT BINDING 85 85 Substrate (By similarity). FT BINDING 272 272 Pyridoxal phosphate (covalent) (By FT similarity). FT MUTAGEN 201 201 S->F: In cin5-3; defective in cytokinin FT induced ethylene. FT MUTAGEN 269 269 S->N: In cin5-2; defective in cytokinin FT induced ethylene. FT MUTAGEN 459 470 RVSWTDRVPDER->PGFMDRSCT: In eto2; FT increases its stability leading to FT ethylene overproduction. SQ SEQUENCE 470 AA; 53313 MW; 8B2527C9B52AE19A CRC64; MKQLSTKVTS NGHGQDSSYF LGWEEYEKNP YDEIKNPNGM IQMGLAENQL CFDLIESWLT KNPDAASLKR NGQSIFRELA LFQDYHGMPE FKKAMAEFME EIRGNRVTFD PKKIVLAAGS TSANETLMFC LAEPGDAFLL PTPYYPGFDR DLKWRTGAEI VPIHCSSSNG FQITESALQQ AYQQAQKLDL KVKGVLVTNP SNPLGTALTR RELNLLVDFI TSKNIHLISD EIYSGTMFGF EQFISVMDVL KDKKLEDTEV SKRVHVVYSL SKDLGLPGFR VGAIYSNDEM IVSAATKMSS FGLVSSQTQY LLSALLSDKK FTSQYLEENQ KRLKSRQRRL VSGLESAGIT CLRSNAGLFC WVDMRHLLDT NTFEAELDLW KKIVYNVKLN ISPGSSCHCT EPGWFRVCFA NMSEDTLDLA LKRLKTFVES TDCGRMISRS SHERLKSLRK KTVSNWVFRV SWTDRVPDER // ID 1A16_ARATH Reviewed; 495 AA. AC Q9SAR0; O82719; Q9SUT3; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 2. DT 23-JAN-2007, entry version 35. DE 1-aminocyclopropane-1-carboxylate synthase 6 (EC 4.4.1.14) (ACC DE synthase 6) (S-adenosyl-L-methionine methylthioadenosine-lyase 6). GN Name=ACS6; Synonyms=ACC6; OrderedLocusNames=At4g11280; GN ORFNames=F8L21.70; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-495, AND INDUCTION. RC STRAIN=cv. Columbia; RX MEDLINE=99178774; PubMed=10080689; DOI=10.1023/A:1006177902093; RA Arteca J.M., Arteca R.N.; RT "A multi-responsive gene encoding 1-aminocyclopropane-1-carboxylate RT synthase (ACS6) in mature Arabidopsis leaves."; RL Plant Mol. Biol. 39:209-219(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-418, AND INDUCTION. RA Vahala J., Schlagnhaufer C.D., Pell E.J.; RT "Induction of an ACC synthase cDNA by ozone in light-grown Arabidopsis RT thaliana leaves."; RL Physiol. Plantarum 103:45-50(1998). RN [5] RP ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND PUTATIVE RP PROCESSING. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). RN [6] RP FUNCTION, PHOSPHORYLATION AT SER-480; SER-483 AND SER-488, AND RP MUTAGENESIS OF SER-480; SER-483 AND SER-488. RX PubMed=15539472; DOI=10.1105/tpc.104.026609; RA Liu Y., Zhang S.; RT "Phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase by RT MPK6, a stress-responsive mitogen-activated protein kinase, induces RT ethylene biosynthesis in Arabidopsis."; RL Plant Cell 16:3386-3399(2004). CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of CC ethylene. Involved in bacterial flagellin-induced ethylene CC production. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=23 uM for AdoMet; CC Vmax=120.60 uM/h/mg enzyme; CC pH dependence: CC Optimum pH is 7.3; CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of CC heterodimerization with other ACS enzymes is however unsure (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers. CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). CC By auxin. By treatment with ozone. CC -!- PTM: Phosphorylated on serine residue by MAP kinase (MPK6). CC -!- PTM: May be processed at its C-terminus. CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation CC of such stability, play a central role in ethylene biosynthesis. CC The phosphorylation of serine residues on the C-terminus increases CC protein stability. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL096882; CAB51412.1; -; Genomic_DNA. DR EMBL; AL161531; CAB81229.1; -; Genomic_DNA. DR EMBL; AF361097; AAK27237.1; -; mRNA. DR EMBL; AF428292; AAL16124.1; -; mRNA. DR EMBL; BT000487; AAN18056.1; -; mRNA. DR EMBL; U73786; AAC63850.1; -; mRNA. DR EMBL; U79524; AAC32251.1; -; mRNA. DR PIR; T13019; T13019. DR UniGene; At.3654; -. DR HSSP; P18485; 1IAX. DR GenomeReviews; CT486007_GR; AT4G11280. DR KEGG; ath:At4g11280; -. DR TAIR; At4g11280; -. DR ArrayExpress; Q9SAR0; -. DR GermOnline; AT4G11280; Arabidopsis thaliana. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Phosphorylation; KW Plant defense; Pyridoxal phosphate; S-adenosyl-L-methionine. FT CHAIN 1 495 1-aminocyclopropane-1-carboxylate FT synthase 6. FT /FTId=PRO_0000123900. FT BINDING 58 58 Substrate (By similarity). FT BINDING 96 96 Substrate (By similarity). FT BINDING 280 280 Pyridoxal phosphate (covalent) (By FT similarity). FT MOD_RES 480 480 Phosphoserine. FT MOD_RES 483 483 Phosphoserine. FT MOD_RES 488 488 Phosphoserine. FT MUTAGEN 480 480 S->D: 40-fold increase in ethylene FT production; when associated with D-483 FT and D-488. FT MUTAGEN 483 483 S->D: 40-fold increase in ethylene FT production; when associated with D-480 FT and D-488. FT MUTAGEN 488 488 S->D: 40-fold increase in ethylene FT production; when associated with D-480 FT and D-483. FT CONFLICT 56 56 L -> F (in Ref. 4). FT CONFLICT 433 433 R -> K (in Ref. 3). SQ SEQUENCE 495 AA; 55524 MW; 7FA94D3EABBCB4AB CRC64; MVAFATEKKQ DLNLLSKIAS GDGHGENSSY FDGWKAYEEN PFHPIDRPDG VIQMGLAENQ LCGDLMRKWV LKHPEASICT SEGVNQFSDI AIFQDYHGLP EFRQAVAKFM EKTRNNKVKF DPDRIVMSGG ATGAHETVAF CLANPGDGFL VPTPYYPGFD RDLRWRTGVN LVPVTCHSSN GFKITVEALE AAYENARKSN IPVKGLLVTN PSNPLGTTLD RECLKSLVNF TNDKGIHLIA DEIYAATTFG QSEFISVAEV IEEIEDCNRD LIHIVYSLSK DMGLPGLRVG IVYSYNDRVV QIARKMSSFG LVSSQTQHLI AKMLSDEEFV DEFIRESKLR LAARHAEITT GLDGLGIGWL KAKAGLFLWM DLRNLLKTAT FDSETELWRV IVHQVKLNVS PGGSFHCHEP GWFRVCFANM DHKTMETALE RIRVFTSQLE EETKPMAATT MMAKKKKKCW QSNLRLSFSD TRRFDDGFFS PHSPVPPSPL VRAQT // ID 1A17_ARATH Reviewed; 447 AA. AC Q9STR4; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 23-JAN-2007, entry version 33. DE 1-aminocyclopropane-1-carboxylate synthase 7 (EC 4.4.1.14) (ACC DE synthase 7) (S-adenosyl-L-methionine methylthioadenosine-lyase 7). GN Name=ACS7; OrderedLocusNames=At4g26200; ORFNames=T25K17.10; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP ENZYME ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of CC ethylene. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=8.3 uM for AdoMet; CC Vmax=13.5 uM/h/mg enzyme; CC pH dependence: CC Optimum pH is 8; CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of CC heterodimerization with other ACS enzymes is however unsure (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed in roots. CC -!- INDUCTION: By cycloheximide (CHX). CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation CC of such stability, play a central role in ethylene biosynthesis. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL049171; CAB38949.1; -; Genomic_DNA. DR EMBL; AL161564; CAB79475.1; -; Genomic_DNA. DR EMBL; AF332390; AAG48754.1; -; mRNA. DR PIR; T06004; T06004. DR UniGene; At.20362; -. DR HSSP; P18485; 1IAX. DR GenomeReviews; CT486007_GR; AT4G26200. DR KEGG; ath:At4g26200; -. DR TAIR; At4g26200; -. DR ArrayExpress; Q9STR4; -. DR GermOnline; AT4G26200; Arabidopsis thaliana. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 447 1-aminocyclopropane-1-carboxylate FT synthase 7. FT /FTId=PRO_0000123901. FT BINDING 61 61 Substrate (By similarity). FT BINDING 100 100 Substrate (By similarity). FT BINDING 285 285 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 447 AA; 50666 MW; E78CC1FC834FD4A9 CRC64; MGLPLMMERS SNNNNVELSR VAVSDTHGED SPYFAGWKAY DENPYDESHN PSGVIQMGLA ENQVSFDLLE TYLEKKNPEG SMWGSKGAPG FRENALFQDY HGLKTFRQAM ASFMEQIRGG KARFDPDRIV LTAGATAANE LLTFILADPN DALLVPTPYY PGFDRDLRWR TGVKIVPIHC DSSNHFQITP EALESAYQTA RDANIRVRGV LITNPSNPLG ATVQKKVLED LLDFCVRKNI HLVSDEIYSG SVFHASEFTS VAEIVENIDD VSVKERVHIV YSLSKDLGLP GFRVGTIYSY NDNVVRTARR MSSFTLVSSQ TQHMLASMLS DEEFTEKYIR INRERLRRRY DTIVEGLKKA GIECLKGNAG LFCWMNLGFL LEKKTKDGEL QLWDVILKEL NLNISPGSSC HCSEVGWFRV CFANMSENTL EIALKRIHEF MDRRRRF // ID 1A18_ARATH Reviewed; 469 AA. AC Q9T065; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 23-JAN-2007, entry version 35. DE 1-aminocyclopropane-1-carboxylate synthase 8 (EC 4.4.1.14) (ACC DE synthase 8) (S-adenosyl-L-methionine methylthioadenosine-lyase 8). GN Name=ACS8; OrderedLocusNames=At4g37770; ORFNames=T28I19.50; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND PUTATIVE RP PROCESSING. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of CC ethylene. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=15 uM for AdoMet; CC Vmax=143 uM/h/mg enzyme; CC pH dependence: CC Optimum pH is 8.2; CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of CC heterodimerization with other ACS enzymes is however unsure (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed in roots. Expressed at low level in CC flowers and siliques. CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). CC -!- PTM: May be processed at its C-terminus. CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation CC of such stability, play a central role in ethylene biosynthesis. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL035709; CAB38925.1; -; Genomic_DNA. DR EMBL; AL161592; CAB80442.1; -; Genomic_DNA. DR EMBL; AF334712; AAG50090.1; -; mRNA. DR PIR; T06024; T06024. DR UniGene; At.2875; -. DR HSSP; P37821; 1M7Y. DR SMR; Q9T065; 10-428. DR GenomeReviews; CT486007_GR; AT4G37770. DR KEGG; ath:At4g37770; -. DR TAIR; At4g37770; -. DR ArrayExpress; Q9T065; -. DR GermOnline; AT4G37770; Arabidopsis thaliana. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 469 1-aminocyclopropane-1-carboxylate FT synthase 8. FT /FTId=PRO_0000123902. FT BINDING 47 47 Substrate (By similarity). FT BINDING 85 85 Substrate (By similarity). FT BINDING 272 272 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 469 AA; 53371 MW; 7BB3CE13E87BDDCE CRC64; MGLLSKKASC NTHGQDSSYF WGWEEYEKNP YDEIKNPDGI IQMGLAENQL SFDLIESWLA KNPDAANFQR EGQSIFRELA LFQDYHGLPS FKNAMADFMS ENRGNRVSFN PNKLVLTAGA TPANETLMFC LADPGDAFLL PTPYYPGFDR DLKWRTGAEI VPIQCKSANG FRITKVALEE AYEQAQKLNL KVKGVLITNP SNPLGTTTTR TELNHLLDFI SRKKIHLISD EIYSGTVFTN PGFISVMEVL KDRKLENTDV FDRVHIVYSL SKDLGLPGFR VGVIYSNDDF VVSAATKMSS FGLISSQTQY LLSALLSDKT FTKNYLEENQ IRLKNRHKKL VSGLEAAGIE CLKSNAGLFC WVDMRHLLKS NTFEAEIELW KKIVYEVKLN ISPGSSCHCN EPGWFRVCFA NLSEETLKVA LDRLKRFVDG PSPTRRSQSE HQRLKNLRKM KVSNWVFRLS FHDREPEER // ID 1A19_ARATH Reviewed; 470 AA. AC Q9M2Y8; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 23-JAN-2007, entry version 33. DE 1-aminocyclopropane-1-carboxylate synthase 9 (EC 4.4.1.14) (ACC DE synthase 9) (S-adenosyl-L-methionine methylthioadenosine-lyase 9) DE (Ethylene-overproduction protein 3). GN Name=ACS9; Synonyms=ETO3; OrderedLocusNames=At3g49700; GN ORFNames=T16K5.50; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP MUTANT ETO3. RX PubMed=12566591; DOI=10.1105/tpc.006882; RA Chae H.S., Faure F., Kieber J.J.; RT "The eto1, eto2, and eto3 mutations and cytokinin treatment increase RT ethylene biosynthesis in Arabidopsis by increasing the stability of RT ACS protein."; RL Plant Cell 15:545-559(2003). RN [4] RP ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND PUTATIVE RP PROCESSING. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of CC ethylene. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=40 uM for AdoMet; CC Vmax=324.5 uM/h/mg enzyme; CC pH dependence: CC Optimum pH is 8; CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of CC heterodimerization with other ACS enzymes is however unsure (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed in roots and siliques. CC -!- INDUCTION: By cycloheximide (CHX). CC -!- PTM: May be processed at its C-terminus. CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation CC of such stability, play a central role in ethylene biosynthesis. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL132965; CAB66908.1; -; Genomic_DNA. DR EMBL; AF332391; AAG48755.1; -; mRNA. DR PIR; T46036; T46036. DR UniGene; At.743; -. DR HSSP; P37821; 1M7Y. DR SMR; Q9M2Y8; 10-428. DR GenomeReviews; BA000014_GR; AT3G49700. DR KEGG; ath:At3g49700; -. DR TAIR; At3g49700; -. DR ArrayExpress; Q9M2Y8; -. DR GermOnline; AT3G49700; Arabidopsis thaliana. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 470 1-aminocyclopropane-1-carboxylate FT synthase 9. FT /FTId=PRO_0000123903. FT BINDING 47 47 Substrate (By similarity). FT BINDING 85 85 Substrate (By similarity). FT BINDING 272 272 Pyridoxal phosphate (covalent) (By FT similarity). FT MUTAGEN 457 457 V->D: In eto3; increases its stability FT heading to ethylene overproduction. SQ SEQUENCE 470 AA; 53170 MW; 2110331C76ACED4E CRC64; MKQLSRKVTS NAHGQDSSYF LGWEEYEKNP YDEIKNPNGI IQMGLAENQL CFDLIETWLA KNPDAAGLKK DGQSIFKELA LFQDYHGLPE FKKALAEFME EIRGNRVTFD PSKIVLAAGS TSANETLMFC LAEPGDAFLL PTPYYPGFDR DLKWRTGAEI VPIHCSSSNG FQITESALQQ AYQQAQKLDL KVKGVLVTNP SNPLGTMLTR RELNLLVDFI TSKNIHLISD EIYSGTVFGF EQFVSVMDVL KDKNLENSEV SKRVHIVYSL SKDLGLPGFR VGAIYSNDEM VVSAATKMSS FGLVSSQTQY LLSALLSDKK FTSTYLDENQ KRLKIRQKKL VSGLEAAGIT CLKSNAGLFC WVDMRHLLDT NTFEAELELW KKIVYDVKLN ISPGSSCHCT EPGWFRVCFA NMSEDTLDLA MKRLKEYVES TDSRRVISKS SHDRIKSLRK RTVSNWVFRV SWTDRVPDER // ID 1A1C_DIACA Reviewed; 517 AA. AC P27486; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 31-OCT-2006, entry version 46. DE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN Name=ACS2; Synonyms=CARACC; OS Dianthus caryophyllus (Carnation) (Clove pink). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Caryophyllaceae; Dianthus. OX NCBI_TaxID=3570; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Petal; RX MEDLINE=92119258; PubMed=1731995; RA Park K.Y., Drory A., Woodson W.R.; RT "Molecular cloning of an 1-aminocyclopropane-1-carboxylate synthase RT from senescing carnation flower petals."; RL Plant Mol. Biol. 18:377-386(1992). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M66619; AAA33275.1; -; mRNA. DR PIR; S19252; S19252. DR HSSP; P18485; 1IAX. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 517 1-aminocyclopropane-1-carboxylate FT synthase. FT /FTId=PRO_0000123911. FT COMPBIAS 453 470 Poly-Thr. FT BINDING 277 277 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 517 AA; 58057 MW; C31BA10732E940AE CRC64; MGSYKGVYDR EILSKIATND GHGENLEYFD GWKAYDRDPY HSTKNSNGVI QMGLAENQLC FDLVTEWLLK NPQASICTNE GVNKFMDIAI FQDYHGLPEF RSAVAKFMGK ARDEKVIFNP DRIVMSGGAS ASETLLFCLA NPGDAFLIPS PYYPAFNRDL RWRTGVNLIP FTCSSSNNFK ITKEALQSAY EDALKKNIKV KGIIVTNPSN PLGTVLDKDT LKMLLTFVNA KNIHLVCDEI YATTVFNSPS FISVAEVIKD MPHVNQDLVH ILYSLSKDMG MPGFRVGIIY SYNDRVVSTA RRMSSFGLVS SQTQFMIAAL LSDDDFVRRF LVESRDRLFR RHQHFTSELA KIGIGCLQGN AALFVWMDLR HLLDEATVER ELKLWRVIIN EVKINVSPGS SFLCSEPGWF RVCFANMDNA TLDVALNRIR SFVTRGRVDN STMTTTSARA AATTTTTTTT TTTTTTTTTT IKKKRGQMEL RLSFNNRRFE DGLMSPHSIL LSPHSPMPQS PLVKART // ID 1A1C_MALDO Reviewed; 473 AA. AC P37821; O04993; Q40278; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 31-OCT-2006, entry version 50. DE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN Name=ACS-1; OS Malus domestica (Apple) (Malus sylvestris). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Rosales; Rosaceae; Maloideae; Malus. OX NCBI_TaxID=3750; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Golden Delicious; TISSUE=Fruit cortical tissue; RX MEDLINE=95232185; PubMed=7716231; DOI=10.1104/pp.107.3.1017; RA Lay-Yee M., Knighton M.L.; RT "A full-length cDNA encoding 1-aminocyclopropane-1-carboxylate RT synthase from apple."; RL Plant Physiol. 107:1017-1018(1995). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Golden Delicious; RA Harada T., Sunako T., Sakuraba W., Goto S., Senda M., Akada S., RA Ishikawa R., Niizeki M.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE OF 10-473. RC STRAIN=cv. Golden Delicious; TISSUE=Fruit; RA Dong J.G., Kim W.T., Yip W.K., Thompson G.A., Li L., Bennett A.B., RA Yang S.F.; RT "Cloning of a cDNA encoding 1-aminocyclopropane-1-carboxylate synthase RT and expression of its mRNA in ripening apple fruit."; RL Planta 185:38-45(1991). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS). RX MEDLINE=20079531; PubMed=10610793; DOI=10.1006/jmbi.1999.3255; RA Capitani G., Hohenester E., Feng L., Storici P., Kirsch J.F., RA Jansonius J.N.; RT "Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme RT in the biosynthesis of the plant hormone ethylene."; RL J. Mol. Biol. 294:745-756(1999). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L31347; AAA73941.1; -; mRNA. DR EMBL; U89156; AAB68617.1; -; Genomic_DNA. DR EMBL; U03294; AAA03472.1; -; mRNA. DR PIR; T16999; T16999. DR PDB; 1B8G; X-ray; A/B=3-431. DR PDB; 1M4N; X-ray; A=1-435. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW 3D-structure; Ethylene biosynthesis; Fruit ripening; Lyase; KW Pyridoxal phosphate; S-adenosyl-L-methionine. FT CHAIN 1 473 1-aminocyclopropane-1-carboxylate FT synthase. FT /FTId=PRO_0000123915. FT BINDING 273 273 Pyridoxal phosphate (covalent). FT CONFLICT 15 15 Q -> E (in Ref. 3). FT CONFLICT 101 101 E -> K (in Ref. 3). FT TURN 7 8 FT TURN 20 20 FT HELIX 21 28 FT TURN 33 35 FT TURN 37 38 FT STRAND 39 42 FT HELIX 52 61 FT TURN 63 64 FT HELIX 65 67 FT TURN 68 68 FT TURN 71 72 FT HELIX 76 81 FT TURN 85 86 FT HELIX 89 102 FT TURN 103 105 FT HELIX 111 113 FT STRAND 114 118 FT HELIX 119 131 FT TURN 134 135 FT STRAND 136 143 FT TURN 146 147 FT HELIX 148 151 FT TURN 152 156 FT STRAND 159 163 FT HELIX 167 169 FT TURN 170 171 FT HELIX 175 187 FT TURN 188 189 FT STRAND 191 200 FT TURN 202 204 FT HELIX 210 223 FT TURN 224 224 FT STRAND 226 230 FT TURN 232 233 FT HELIX 234 236 FT STRAND 239 241 FT HELIX 246 252 FT TURN 253 254 FT TURN 257 258 FT HELIX 261 263 FT STRAND 264 271 FT TURN 272 274 FT HELIX 278 280 FT STRAND 282 288 FT HELIX 290 299 FT HELIX 300 303 FT HELIX 307 317 FT TURN 318 318 FT HELIX 320 346 FT TURN 347 349 FT STRAND 357 364 FT HELIX 366 368 FT STRAND 370 373 FT HELIX 374 386 FT TURN 387 387 FT HELIX 395 398 FT TURN 399 399 FT TURN 403 404 FT STRAND 405 409 FT TURN 411 412 FT HELIX 415 428 FT TURN 429 429 SQ SEQUENCE 473 AA; 53251 MW; 6ACA20759615E75D CRC64; MRMLSRNATF NSHGQDSSYF LGWQEYEKNP YHEVHNTNGI IQMGLAENQL CFDLLESWLA KNPEAAAFKK NGESIFAELA LFQDYHGLPA FKKAMVDFMA EIRGNKVTFD PNHLVLTAGA TSANETFIFC LADPGEAVLI PTPYYPGFDR DLKWRTGVEI VPIHCTSSNG FQITETALEE AYQEAEKRNL RVKGVLVTNP SNPLGTTMTR NELYLLLSFV EDKGIHLISD EIYSGTAFSS PSFISVMEVL KDRNCDENSE VWQRVHVVYS LSKDLGLPGF RVGAIYSNDD MVVAAATKMS SFGLVSSQTQ HLLSAMLSDK KLTKNYIAEN HKRLKQRQKK LVSGLQKSGI SCLNGNAGLF CWVDMRHLLR SNTFEAEMEL WKKIVYEVHL NISPGSSCHC TEPGWFRVCF ANLPERTLDL AMQRLKAFVG EYYNVPEVNG GSQSSHLSHS RRQSLTKWVS RLSFDDRGPI PGR // ID 1A1C_PHAAU Reviewed; 368 AA. AC Q01912; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 31-OCT-2006, entry version 45. DE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase) DE (Fragment). GN Name=ACS5; OS Phaseolus aureus (Mung bean) (Vigna radiata). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Vigna. OX NCBI_TaxID=3916; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Berken / Rwilcz; TISSUE=Hypocotyl; RX MEDLINE=93043033; PubMed=1421146; RA Botella J.R., Arteca J.M., Schlagnhaufer C.D., Arteca R.N., RA Phillips A.T.; RT "Identification and characterization of a full-length cDNA encoding RT for an auxin-induced 1-aminocyclopropane-1-carboxylate synthase from RT etiolated mung bean hypocotyl segments and expression of its mRNA in RT response to indole-3-acetic acid."; RL Plant Mol. Biol. 20:425-436(1992). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- INDUCTION: Hormones, such as auxin, environmental factors, such as CC mechanical wounding and a number of chemicals. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11562; CAA77655.1; -; mRNA. DR HSSP; P18485; 1IAX. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN <1 >368 1-aminocyclopropane-1-carboxylate FT synthase. FT /FTId=PRO_0000123917. FT BINDING 230 230 Pyridoxal phosphate (covalent) (By FT similarity). FT NON_TER 1 1 FT NON_TER 368 368 SQ SEQUENCE 368 AA; 41477 MW; 31BA61D5FC2D4CB8 CRC64; QMGLAENQLT SDLVEDWILN NPEASICTPE GINDFRAIAN FQDYHGLAEF RNAVAKFMAR TRGNRITFDP DRIVMSGGAT GAHEVTAFCL ADPGEAFLVP IPYYPGFDRD LRWRTGVKLV PVMCDSSNNF VLTKEALEDA YEKAREDNIR VKGLLITNPS NPLGTIMDRK TLRTVVSFIN EKRIHLVCDE IYAATVFSQP GFISIAEILE DETDIECDRN LVHIVYSLSK DMGFPGFRVG IIYSYNDAVV NCARKMSSFG LVSTQTQYLL ASMLNDDEFV ERFLAESAKR LAQRFRVFTG GLAKVGIKCL QSNAGLFVWM DLRQLLKKPT FDSETELWKV IIHEVKINVS PGYSFHCTEP GWFRVCFA // ID 1A1C_SOYBN Reviewed; 484 AA. AC P31531; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 20-FEB-2007, entry version 45. DE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN Name=ACS1; OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Century; TISSUE=Leaf; RA Liu D., Li N., Mattoo A.K.; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X67100; CAA47474.1; -; mRNA. DR PIR; S25002; S25002. DR UniGene; Gma.28781; -. DR HSSP; P18485; 1IAX. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 484 1-aminocyclopropane-1-carboxylate FT synthase. FT /FTId=PRO_0000123919. FT BINDING 279 279 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 484 AA; 54731 MW; 152F7AD12B992987 CRC64; MGLMDVDQTQ LLSKMVIGDG HGEASPYFDG WKAYDENPFH PKENPNGVIQ MGLAENQLTS DLVEDWILNN PEASICTPEG INDFRAIANF QDYHGLPEFR NAVAKFMGRT RGNRVTFDPD RIVMSGGATG AHEVTTFCLA DPGDAFLVPI PYYPGFDRDL RWRTGIKLVP VMCDSSNNFK LTKQALEDAY EKAKEDNIRV KGLLITNPSN PLGTVMDRNT LRTVMSFINE KRIHLVSDEI YSATVFSHPS FISIAEILEE DTDIECDRNL VHIVYSLSKD MGFPGFRVGI IYSYNDAVVH CARKMSSFGL VSTQTQYLLA SMLNDDEFVE SFLVESAKRL AQRHRVFTGG LAKVGIKCLQ SNAGLFVWMD LRQLLKKPTL DSEMELWRVI IDEVKINVSP GSSFHCTEPG WFRVCYANMD DMAVQIALQR IRNFVLQNKE IMVPNKKHCW HSNLRLSLKT RRFDDIMMSP HSPIPQSPLV KATI // ID 1A1C_TOBAC Reviewed; 491 AA. AC Q07262; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 31-OCT-2006, entry version 42. DE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN Name=ACS1; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Xanthi; RA Bailey B.A., Avni A., Li N., Matoo A.K., Anderson J.D.; RT "Nucleotide sequence of the Nicotiana tabacum cv Xanthi gene encoding RT 1-aminocyclopropane-1-carboxylate synthase."; RL Plant Physiol. 100:1615-1616(1992). CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1- CC carboxylate, a direct precursor of ethylene in higher plants. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Ethylene biosynthesis; first (rate-limiting) step. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X65982; CAA46797.1; -; mRNA. DR PIR; T03978; T03978. DR HSSP; P18485; 1IAX. DR SMR; Q07262; 16-438. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHtransf_1_BS. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate; KW S-adenosyl-L-methionine. FT CHAIN 1 491 1-aminocyclopropane-1-carboxylate FT synthase. FT /FTId=PRO_0000123920. FT BINDING 278 278 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 491 AA; 55291 MW; 57B9FF4306686DFD CRC64; MGFENEKNSS ILSKLATNEE LGENSPYFDG WKAYDNDPFH PLKNPNGVIQ MGLAENQLCF DLIEEWIKRN PNASICTTEG IKSFRAIANF QDYHGLPEFR SAIAKFMEKT RGGRVTFDPE RVVMAGGATG ANETIIFCLA DTGDAFLVPS PYYPAFNRDL RWRTGVQLIP IPCDSSNNFQ ITTKAVREAY ENAQKSNIKV KGLILTNPSN PLGTTLDRDT LKNLLTFTNQ HNIHLVCDEI YAATVFNTPQ FVSIAEILDD ETSHCNKDLV HIVYSLSKDM GLPGFRVGIV YSFNDAVVNC ARKMSSFGLV STQTQYLLAE MLSDERFVSN FLTESSKRLA KRHKHFTNGL EEVGIKCLRS NAGLFCWMDL RPLLKESTFD SEMSLWRVII NDVKLNVSPG SSFDCQEPGF FRVCFANMDD ETVDIALARI RSFVGVKKSG DESTPILMEK KQQWKKNNLR LSFSKRMYDE SVNLSPLSSP IPHSPLVRAR T // ID 1A1D_AGRTU Reviewed; 337 AA. AC Q9AHF0; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 06-FEB-2007, entry version 21. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OS Agrobacterium tumefaciens. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=358; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=d3; RX MEDLINE=21322708; PubMed=11429459; RA Trott S., Bauer R., Knackmuss H.J., Stolz A.; RT "Genetic and biochemical characterization of an enantioselective RT amidase from Agrobacterium tumefaciens strain d3."; RL Microbiology 147:1815-1824(2001). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AF315580; AAK28496.1; ALT_INIT; Genomic_DNA. DR HSSP; O57809; 1J0A. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Hydrolase; Pyridoxal phosphate. FT CHAIN 1 337 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184496. FT ACT_SITE 77 77 Nucleophile (By similarity). FT BINDING 50 50 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 337 AA; 36676 MW; FF5CCED8FE6FB09B CRC64; MLEKFERYPL TFGATAIEYL PRLTEALGGD VEIWAKREDC NSGLAMGGNK LRKLEYIVPD AIASNADTLV SIGGVQSNHT RMVAAVAAKL GMKCRLVQES WVPHEDAVYD RVGNILMTRL MGADSRIVDD GFDIGIRQSW EDAIQSVIDE GGKPYAIPAG ASVHKYGGLG YVAFAEEVAR QEADLGFKFD YIIVCVVTGS TQAGMIVGFA AQDRADRVIG IDASGTPEQT RSQVRQIVDN TAELVELGRP VREDEIVILN DYAYPAYGVP SNETNEAIRL AARTEAMITD PVYEGKSMQG MIDLTRKGFF PKGSKVLYAH LGGAPALNGY SYTYRNG // ID 1A1D_BRAJA Reviewed; 337 AA. AC Q89XR6; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 06-FEB-2007, entry version 19. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OrderedLocusNames=blr0241; OS Bradyrhizobium japonicum. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=375; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USDA 110; RX MEDLINE=22484998; PubMed=12597275; DOI=10.1093/dnares/9.6.189; RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., RA Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., RA Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., RA Tabata S.; RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium RT Bradyrhizobium japonicum USDA110."; RL DNA Res. 9:189-197(2002). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; BA000040; BAC45506.1; -; Genomic_DNA. DR HSSP; O57809; 1J0A. DR SMR; Q89XR6; 2-337. DR GenomeReviews; BA000040_GR; blr0241. DR KEGG; bja:blr0241; -. DR BioCyc; BJAP224911:BLR0241-MONOMER; -. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Complete proteome; Hydrolase; Pyridoxal phosphate. FT CHAIN 1 337 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184497. FT ACT_SITE 77 77 Nucleophile (By similarity). FT BINDING 50 50 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 337 AA; 36432 MW; AD4C73D2E1CC893B CRC64; MLEKFARYPL TFGPTPIEKL ERLSKHLGGN VEIYAKREDC NSGLAYGGNK LRKLEYIIPD AIASNADTLV SIGGVQSNHT RMIAAVAAKI GMKCRLVQEA WVPHEDAVYD RVGNIMLSRI MGADVRLVDD GFDIGIRKSW EQAIEEVKAA GGKPYAIPAG ASVHKYGGLG YVGFAEEVRK QEAELGFKFD YIVVCTVTGS THAGMLVGFA ADGRARKVIG IDGSFTPAQT KAQVLSIAQN TAKLVELGKD IVADDVVLIE DYAYPAYGVP SEETKEAIRL TARLEAMITD PVYEGKSMQG LIDLTQKGYF EKGAKVLYAH LGGAPALNGY GYAFRNG // ID 1A1D_BURMA Reviewed; 338 AA. AC Q62CE3; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 06-FEB-2007, entry version 14. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OrderedLocusNames=BMAA0952; OS Burkholderia mallei (Pseudomonas mallei). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=13373; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23344; RX PubMed=15377793; DOI=10.1073/pnas.0403306101; RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., RA Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., RA Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., RA Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M., RA Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y., RA Zafar N., Zhou L., Fraser C.M.; RT "Structural flexibility in the Burkholderia mallei genome."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; CP000011; AAU46138.1; -; Genomic_DNA. DR SMR; Q62CE3; 1-338. DR GenomeReviews; CP000011_GR; BMAA0952. DR KEGG; bma:BMAA0952; -. DR TIGR; BMAA0952; -. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Complete proteome; Hydrolase; Pyridoxal phosphate. FT CHAIN 1 338 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184498. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 338 AA; 36481 MW; 64927D39E112B86F CRC64; MNLQKFSRYP LTFGPTPIQP LKRLSAHLGG KVELYAKRDD CNSGLAFGGN KTRKLEYLIP DALAQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYHDAVY DRVGNIQMSR MMGADVRLVP DGFDIGFRKS WEDALADVRA RGGKPYAIPA GCSDHPLGGL GFVGFAEEVR AQEAELGFQF DYVVVCSVTG STQAGMVVGF AADGRADRVI GVDASAKPAQ TREQILRIAK HTADRVELGR DITSADVVLD ERFGGPEYGL PNEGTLEAIR LCAKLEGVLT DPVYEGKSMH GMIEKVRLGE FPAGSKVLYA HLGGVPALNA YSFLFRDG // ID 1A1D_BURPS Reviewed; 338 AA. AC Q63KN7; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 06-FEB-2007, entry version 15. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OrderedLocusNames=BPSS1324; OS Burkholderia pseudomallei (Pseudomonas pseudomallei). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=28450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., RA Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A., RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, RT Burkholderia pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; BX571966; CAH38795.1; -; Genomic_DNA. DR SMR; Q63KN7; 1-338. DR GenomeReviews; BX571966_GR; BPSS1324. DR KEGG; bps:BPSS1324; -. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Complete proteome; Hydrolase; Pyridoxal phosphate. FT CHAIN 1 338 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184499. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 338 AA; 36481 MW; 64927D39E112B86F CRC64; MNLQKFSRYP LTFGPTPIQP LKRLSAHLGG KVELYAKRDD CNSGLAFGGN KTRKLEYLIP DALAQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYHDAVY DRVGNIQMSR MMGADVRLVP DGFDIGFRKS WEDALADVRA RGGKPYAIPA GCSDHPLGGL GFVGFAEEVR AQEAELGFQF DYVVVCSVTG STQAGMVVGF AADGRADRVI GVDASAKPAQ TREQILRIAK HTADRVELGR DITSADVVLD ERFGGPEYGL PNEGTLEAIR LCAKLEGVLT DPVYEGKSMH GMIEKVRLGE FPAGSKVLYA HLGGVPALNA YSFLFRDG // ID 1A1D_CRYNE Reviewed; 345 AA. AC Q5KMX3; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 23-JAN-2007, entry version 12. DE Probable 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) DE (ACC deaminase) (ACCD). GN OrderedLocusNames=CNB00190; OS Cryptococcus neoformans (Filobasidiella neoformans). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Heterobasidiomycetes; OC Tremellomycetidae; Tremellales; Tremellaceae; Filobasidiella. OX NCBI_TaxID=5207; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JEC21; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., RA D'Souza C.A., Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., RA Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., RA Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., RA Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., RA Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., RA Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., RA Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., RA Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen RT Cryptococcus neoformans."; RL Science 307:1321-1324(2005). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AE017342; AAW41453.1; -; Genomic_DNA. DR UniGene; Fne.2533; -. DR GenomeReviews; AE017342_GR; CNB00190. DR KEGG; cne:CNB00190; -. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Complete proteome; Hydrolase; Pyridoxal phosphate. FT CHAIN 1 345 Probable 1-aminocyclopropane-1- FT carboxylate deaminase. FT /FTId=PRO_0000184510. FT ACT_SITE 85 85 Nucleophile (By similarity). FT BINDING 58 58 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 345 AA; 37050 MW; 82A7CAC10E8F3D39 CRC64; MSTPAYLTKL ESIPKEKFLF GPSPISYLPN LTAVLGGKVK LYAKREDCNS GLAYGGNKVR KLEYLVADAK AKGCNTLVSV GGVQSNHTRA VTAVAVASGL KAVTVQEKWV PIDPPLYSET GNILLSRLMG GDVRLNQETF DIRHKKATED AFKDVEAKGG KPYYIPAGAS DHPLGGLGFT NWVVELAKQE KELGVFFDVV IVCSVTGSSH AGTVVGAVAE GRKRKIIGID ASGKPEATRN QVLKIARNTA ALLDERLEIK EEDVILDDRF HAGIYGIPDD ETIAAMKLAA QTDAFITDPV YEGKSMAGMI RLVKEGAIKE GSNVLYIHLG GQPALNAYSS YFPHA // ID 1A1D_ENTCL Reviewed; 338 AA. AC Q9ZHW3; Q9ZHW4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 06-FEB-2007, entry version 33. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OS Enterobacter cloacae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=550; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CAL2; RX MEDLINE=99068011; PubMed=9851025; DOI=10.1139/cjm-44-9-833; RA Shah S., Li J., Moffatt B.A., Glick B.R.; RT "Isolation and characterization of ACC deaminase genes from two RT different plant growth-promoting rhizobacteria."; RL Can. J. Microbiol. 44:833-843(1998). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source. CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate. CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AF047840; AAD05070.1; -; Genomic_DNA. DR HSSP; O57809; 1J0A. DR SMR; Q9ZHW3; 1-338. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Hydrolase; Pyridoxal phosphate. FT CHAIN 1 338 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184500. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 338 AA; 36871 MW; 0B94C8C887772AF8 CRC64; MNLNRFERYP LTFGPSPITP LKRLSQHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLIP EAIEQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIEMSR IMGADVRLDA AGFDIGIRPS WEKAMSDVVE QGGKPFPIPA GCSEHPYGGL GFVGFAKKLR QQEKELGFKF NYIVVCSVTG STQAGMVVGF AADGRSKNVI GVDASAKPEQ TKAQILRIAR HTAELVELGR EITEEDVVLD TRFAYPEYGL PNEGTLEAIR LCGSLEGVLT DPVYEGKSMH GMIEMVRRGE FPEGSKVLYA HLGGAPALNA YSFLFRDG // ID 1A1D_PSEFL Reviewed; 338 AA. AC Q51813; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 06-FEB-2007, entry version 33. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OS Pseudomonas fluorescens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=294; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=17; RX MEDLINE=96242319; PubMed=9026447; DOI=10.1016/0378-1097(96)00108-5; RA Campbell B.G., Thompson J.A.; RT "1-aminocyclopropane-1-carboxylate deaminase genes from Pseudomonas RT strains."; RL FEMS Microbiol. Lett. 138:207-210(1996). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source. CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate. CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; U37103; AAC44163.1; -; Genomic_DNA. DR HSSP; O57809; 1J0A. DR SMR; Q51813; 1-338. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Hydrolase; Pyridoxal phosphate. FT CHAIN 1 338 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184501. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 338 AA; 36855 MW; E6E98B3EB6FE6144 CRC64; MNLNRFKRYP LTFGPSPITP LKRLSEHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLIP EALEQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIEMSR IMGADVRLDA AGFDIGIRPS WEKAMNDVVE RGGKPFPIPA GCSEHPYGGL GFVGFAEEVR EQEKQLGFKF DYIVVCSVTG STQAGMVVGF AADGRSKNVI GIDASAKPEK TKAQILRIAR HTAELVELGR EITEDDVVLD TPFAYPEYGL PNEGTLEAIR LCGSLEGVLT DPVYEGKSMH GMIEMVRRGE FPEGSKVLYA HLGGAPALNA YSFLFRNG // ID 1A1D_PSEPU Reviewed; 338 AA. AC Q5PWZ8; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 06-FEB-2007, entry version 12. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OS Pseudomonas putida. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=UW4; RX MEDLINE=99068011; PubMed=9851025; DOI=10.1139/cjm-44-9-833; RA Shah S., Li J., Moffatt B.A., Glick B.R.; RT "Isolation and characterization of ACC deaminase genes from two RT different plant growth-promoting rhizobacteria."; RL Can. J. Microbiol. 44:833-843(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND MUTAGENESIS RP OF GLY-44. RC STRAIN=UW4; RX PubMed=15588698; DOI=10.1016/j.bbapap.2004.09.015; RA Hontzeas N., Zoidakis J., Glick B.R., Abu-Omar M.M.; RT "Expression and characterization of 1-aminocyclopropane-1-carboxylate RT deaminase from the rhizobacterium Pseudomonas putida UW4: a key enzyme RT in bacterial plant growth promotion."; RL Biochim. Biophys. Acta 1703:11-19(2004). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.4 mM for 1-aminocyclopropane-1-carboxylate; CC pH dependence: CC Optimum pH is 8.0; CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AF047710; AAD05069.1; -; Genomic_DNA. DR EMBL; AY823987; AAV73804.1; -; Genomic_DNA. DR SMR; Q5PWZ8; 1-338. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Hydrolase; Pyridoxal phosphate. FT CHAIN 1 338 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184502. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent) (By FT similarity). FT MUTAGEN 44 44 G->D: Loss of activity. FT CONFLICT 177 179 EEV -> KEL (in Ref. 1). FT CONFLICT 185 185 E -> D (in Ref. 1). SQ SEQUENCE 338 AA; 36874 MW; B4827E8BEF82C2AE CRC64; MNLNRFERYP LTFGPSPITP LKRLSEHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLIP EAIEQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIEMSR IMGADVRLDA AGFDIGIRPS WEKAMSDVVE RGGKPFPIPA GCSEHPYGGL GFVGFAEEVR QQEKELGFKF DYIVVCSVTG STQAGMVVGF AADGRSKNVI GVDASAKPEQ TKAQILRIAR HTAELVELGR EITEEDVVLD TRFAYPEYGL PNEGTLEAIR LCGSLEGVLT DPVYEGKSMH GMIEMVRRGE FPDGSKVLYA HLGGAPALNA YSFLFRNG // ID 1A1D_PSES0 Reviewed; 338 AA. AC P30297; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 06-FEB-2007, entry version 36. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OS Pseudomonas sp. (strain 6G5). OC Bacteria; Proteobacteria. OX NCBI_TaxID=29439; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92338840; PubMed=1821764; DOI=10.1105/tpc.3.11.1187; RA Klee H.J., Hayford M.B., Kretzmer K.A., Barry G.F., Kishore G.M.; RT "Control of ethylene synthesis by expression of a bacterial enzyme in RT transgenic tomato plants."; RL Plant Cell 3:1187-1193(1991). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source. CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate. CC -!- SUBUNIT: Homotrimer. CC -!- BIOTECHNOLOGY: Introduced by genetic manipulation and expressed in CC improved ripening tomato by Monsanto. ACC is the immediate CC precursor of the phytohormone ethylene which is involved in the CC control of ripening. ACC deaminase reduces ethylene biosynthesis CC and thus extends the shelf life of fruits and vegetables. CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; M80882; AAA73153.1; -; Genomic_DNA. DR PIR; JQ1330; JQ1330. DR HSSP; O57809; 1J0A. DR SMR; P30297; 1-338. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Genetically modified food; Hydrolase; Pyridoxal phosphate. FT CHAIN 1 338 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184503. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 338 AA; 36873 MW; F496374E7C12B6AD CRC64; MNLNRFERYP LTFGPSPITP LKRLSQHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLIP EAIEQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIEMSR IMGADVRLDA AGFDIGIRPS WEKAMSDVVE QGGKPFPIPA GCSEHPYGGL GFVGFAEEVR QQEKELGFKF DYIVVCSVTG STQAGMVVGF AADGRSKNVI GIDASAKPEQ TKAQILRIAR HTAELVELGR EITEEDVVLD TRFAYPEYGL PNEGTLEAIR LCGSLEGVLT DPVYEGKSMH GMIEMVRRGE FPEGSKVLYA HLGGAPALNA YSFLFRNG // ID 1A1D_PSESM Reviewed; 338 AA. AC Q87YW7; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 06-FEB-2007, entry version 21. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OrderedLocusNames=PSPTO_3675; OS Pseudomonas syringae pv. tomato. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=323; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DC3000; RX MEDLINE=22834015; PubMed=12928499; DOI=10.1073/pnas.1731982100; RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., RA Madupu R., Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., RA Nelson W.C., Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., RA Khouri H.M., Fedorova N.B., Tran B., Russell D., Berry K.J., RA Utterback T.R., Van Aken S.E., Feldblyum T.V., D'Ascenzo M., RA Deng W.-L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K., RA Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X., RA Bender C.L., White O., Fraser C.M., Collmer A.; RT "The complete genome sequence of the Arabidopsis and tomato pathogen RT Pseudomonas syringae pv. tomato DC3000."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AE016853; AAO57144.1; -; Genomic_DNA. DR HSSP; O57809; 1J0A. DR SMR; Q87YW7; 1-338. DR GenomeReviews; AE016853_GR; PSPTO_3675. DR KEGG; pst:PSPTO_3675; -. DR TIGR; PSPTO_3675; -. DR BioCyc; PSYR223283:PSPTO3675-MONOMER; -. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Complete proteome; Hydrolase; Pyridoxal phosphate. FT CHAIN 1 338 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184504. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 338 AA; 36851 MW; AE1AFA70223B0B97 CRC64; MNLSKFKRYP LTFGPSPITP LKRLSEHLGG KVDLYAKRED CNSGLAFGGN KTRKLEYLVP EAIEGGYDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDALY DRVGNIEMSR IMGADVRLDS AGFDIGIRPS WEKAMADVVE SGGKPFPIPA GCSEHPYGGL GFVRFADEVR QQEEELGFKF DYIVVCSVTG STHAGMLVGF AADGRAQRVI GIDASAKPDK TREQVLRIAQ NTAKLVDLGR EITAEDVVLD TRYAYPEYGL PNDGTLEAIR LCARLEGVLT DPVYEGKSMH GMIDMVRNGE FPEGSKVLYA HLGGVPALNA YSFLFKDG // ID 1A1D_PSEUD Reviewed; 338 AA. AC Q00740; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 06-FEB-2007, entry version 38. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OS Pseudomonas sp. (strain ACP). OC Bacteria; Proteobacteria. OX NCBI_TaxID=74568; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE. RX MEDLINE=91358299; PubMed=1885510; RA Sheehy R.E., Honma M., Yamada M., Sasaki T., Martineau B., Hiatt W.R.; RT "Isolation, sequence, and expression in Escherichia coli of the RT Pseudomonas sp. strain ACP gene encoding 1-aminocyclopropane-1- RT carboxylate deaminase."; RL J. Bacteriol. 173:5260-5265(1991). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source. CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate. CC -!- SUBUNIT: Homotrimer. CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; M73488; AAA25689.1; -; Genomic_DNA. DR PDB; 1RQX; X-ray; A/B/C/D=1-338. DR PDB; 1TYZ; X-ray; A/B/C/D=1-338. DR PDB; 1TZ2; X-ray; A/B/C/D=1-338. DR PDB; 1TZJ; X-ray; A/B/C/D=1-338. DR PDB; 1TZK; X-ray; A/B/C/D=1-338. DR PDB; 1TZM; X-ray; A/B/C/D=1-338. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW 3D-structure; Direct protein sequencing; Hydrolase; KW Pyridoxal phosphate. FT CHAIN 1 338 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184505. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent). FT HELIX 3 5 FT STRAND 12 15 FT STRAND 18 20 FT HELIX 22 27 FT TURN 28 29 FT STRAND 30 38 FT HELIX 39 41 FT TURN 46 47 FT HELIX 50 64 FT TURN 65 66 FT STRAND 69 75 FT TURN 76 77 FT HELIX 79 91 FT TURN 92 92 FT STRAND 94 100 FT TURN 108 112 FT HELIX 114 121 FT TURN 122 123 FT STRAND 125 127 FT HELIX 140 150 FT TURN 151 152 FT STRAND 155 158 FT HELIX 160 162 FT TURN 163 163 FT TURN 166 169 FT HELIX 171 186 FT TURN 187 187 FT STRAND 191 200 FT HELIX 201 211 FT TURN 212 214 FT HELIX 216 218 FT STRAND 219 223 FT HELIX 228 246 FT TURN 247 247 FT HELIX 254 256 FT STRAND 258 260 FT TURN 262 263 FT TURN 268 269 FT HELIX 273 286 FT TURN 292 294 FT HELIX 295 307 FT TURN 308 309 FT TURN 313 314 FT STRAND 316 321 FT HELIX 325 331 FT TURN 332 332 FT HELIX 333 335 FT TURN 336 337 SQ SEQUENCE 338 AA; 36672 MW; 01FC286177012FDF CRC64; MNLQRFPRYP LTFGPTPIQP LARLSKHLGG KVHLYAKRED CNSGLAFGGN KTRKLEYLIP EALAQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIQMSR ILGADVRLVP DGFDIGFRRS WEDALESVRA AGGKPYAIPA GCSDHPLGGL GFVGFAEEVR AQEAELGFKF DYVVVCSVTG STQAGMVVGF AADGRADRVI GVDASAKPAQ TREQITRIAR QTAEKVGLER DIMRADVVLD ERFAGPEYGL PNEGTLEAIR LCARTEGMLT DPVYEGKSMH GMIEMVRNGE FPEGSRVLYA HLGGVPALNG YSFIFRDG // ID 1A1D_PYRAB Reviewed; 330 AA. AC Q9V2L2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 31-OCT-2006, entry version 34. DE Putative 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) DE (ACC deaminase). GN OrderedLocusNames=PYRAB00630; ORFNames=PAB2303; OS Pyrococcus abyssi. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=29292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GE5 / Orsay; RX MEDLINE=22511545; PubMed=12622808; RX DOI=10.1046/j.1365-2958.2003.03381.x; RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., RA Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.; RT "An integrated analysis of the genome of the hyperthermophilic RT archaeon Pyrococcus abyssi."; RL Mol. Microbiol. 47:1495-1512(2003). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AJ248283; CAB48986.1; -; Genomic_DNA. DR PIR; C75192; C75192. DR HSSP; O57809; 1J0A. DR GenomeReviews; AL096836_GR; PYRAB00630. DR KEGG; pab:PAB2303; -. DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase...; IEA:EC. DR InterPro; IPR001926; B6_enzyme_beta. DR InterPro; IPR005966; PyridoxP_deam. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01275; ACC_deam_rel; 1. KW Complete proteome; Hydrolase; Hypothetical protein; KW Pyridoxal phosphate. FT CHAIN 1 330 Putative 1-aminocyclopropane-1- FT carboxylate deaminase. FT /FTId=PRO_0000184521. FT BINDING 54 54 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 330 AA; 35755 MW; CC8699923C0B11CD CRC64; MHPKVDALLS RFPRITLIPW ETPIQYLPRI SRELGVDVYV KRDDLTGLGI GGNKIRKLEF LLGDALSRGC DTVITIGAVH SNHAFVTALA AKKLGLGAVL ILRGEEVLKG NYLLDKLMGI ETRIYEADNS WELMKVAEEV AEELKGEGKK PYIIPPGGAS PVGTLGYIRG VGELYTQVKK LGLRIDTVVD AVGSGGTYAG LLLGSAIVNA EWSVVGIDVS SATEKAKERV KNLVEKTKEL LGINVKVQEP RIYDYGFGAY GKIVKEVAKL IKSVGTMEGL LLDPVYTGKA FYGLMDLAKK GDLGESVLFI HTGGLPGIFH YGEEMLELLV // ID 1A1D_PYRFU Reviewed; 329 AA. AC Q8U4R3; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 15-NOV-2002, sequence version 2. DT 31-OCT-2006, entry version 23. DE Putative 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) DE (ACC deaminase). GN OrderedLocusNames=PF0010; OS Pyrococcus furiosus. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=2261; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RA Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.; RT "The complete sequence of the Pyrococcus furiosus genome."; RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AE010126; AAL80134.1; ALT_INIT; Genomic_DNA. DR HSSP; O57809; 1J0A. DR SMR; Q8U4R3; 1-329. DR GenomeReviews; AE009950_GR; PF0010. DR KEGG; pfu:PF0010; -. DR BioCyc; PFUR186497:PF0010-MONOMER; -. DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase...; IEA:EC. DR InterPro; IPR001926; B6_enzyme_beta. DR InterPro; IPR005966; PyridoxP_deam. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01275; ACC_deam_rel; 1. KW Complete proteome; Hydrolase; Hypothetical protein; KW Pyridoxal phosphate. FT CHAIN 1 329 Putative 1-aminocyclopropane-1- FT carboxylate deaminase. FT /FTId=PRO_0000184522. FT BINDING 54 54 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 329 AA; 35795 MW; 627852CFD0A450F8 CRC64; MHPKVQSLLS KFPRVELIPW ETPIQYLPNI SKLVGADIYV KRDDLTGLGI GGNKIRKLEY LLGDAIIRKA DVIITVGAVH SNHAFVTGLA AKKLGFDVVL VLRGKEELRG NYLLDKIMGI ETRVYEAKDS FELMKYAEEV AKELEEKGRK PYIIPVGGAS PVGTLGYVRA SGEIAEQGNR IGVNFDSIVV ATGSGGTLAG LSVGLAILRK ETRAIGMAVG KFGETMVNKV EELAKATGEF IGVKNLKLKI ELYDYSFGEY GKITREVAET IRLVGTKEGV ILDPVYTGKA FYGLLDLAKK GELGEKILFI HTGGISGTFH YGDKILSFL // ID 1A1D_PYRHO Reviewed; 325 AA. AC O57809; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 31-OCT-2006, entry version 38. DE Putative 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) DE (ACC deaminase). GN OrderedLocusNames=PH0054; ORFNames=PHBE027; OS Pyrococcus horikoshii. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=53953; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OT3; RX MEDLINE=98344137; PubMed=9679194; DOI=10.1093/dnares/5.2.55; RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., RA Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., RA Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., RA Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., RA Masuchi Y., Shizuya H., Kikuchi H.; RT "Complete sequence and gene organization of the genome of a hyper- RT thermophilic archaebacterium, Pyrococcus horikoshii OT3."; RL DNA Res. 5:55-76(1998). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; BA000001; BAA29122.1; ALT_INIT; Genomic_DNA. DR PDB; 1J0A; X-ray; A/B/C=1-325. DR PDB; 1J0B; X-ray; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q=1-325. DR GenomeReviews; BA000001_GR; PH0054. DR KEGG; pho:PH0054; -. DR BioCyc; PHOR53953:PH0054-MONOMER; -. DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase...; IEA:EC. DR InterPro; IPR001926; B6_enzyme_beta. DR InterPro; IPR005966; PyridoxP_deam. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01275; ACC_deam_rel; 1. KW 3D-structure; Complete proteome; Hydrolase; Hypothetical protein; KW Pyridoxal phosphate. FT CHAIN 1 325 Putative 1-aminocyclopropane-1- FT carboxylate deaminase. FT /FTId=PRO_0000184523. FT BINDING 54 54 Pyridoxal phosphate (covalent) (By FT similarity). FT HELIX 3 9 FT TURN 10 11 FT STRAND 24 26 FT HELIX 28 34 FT TURN 35 35 FT STRAND 36 42 FT HELIX 43 45 FT TURN 49 50 FT TURN 53 53 FT HELIX 54 67 FT TURN 68 69 FT STRAND 71 76 FT TURN 79 80 FT HELIX 82 93 FT TURN 94 95 FT STRAND 97 104 FT HELIX 110 117 FT TURN 118 119 FT STRAND 121 126 FT TURN 130 132 FT HELIX 133 144 FT TURN 145 146 FT STRAND 151 154 FT HELIX 156 158 FT HELIX 161 164 FT TURN 165 165 FT HELIX 166 177 FT STRAND 183 192 FT HELIX 193 204 FT TURN 205 206 FT STRAND 210 215 FT STRAND 220 222 FT HELIX 223 237 FT TURN 238 239 FT STRAND 247 250 FT TURN 253 254 FT TURN 256 257 FT HELIX 261 274 FT TURN 280 282 FT HELIX 283 295 FT TURN 296 297 FT STRAND 301 307 FT HELIX 311 316 FT TURN 317 317 FT HELIX 318 322 FT TURN 323 324 SQ SEQUENCE 325 AA; 35188 MW; 60AE1B7A37CDF231 CRC64; MHPKIFALLA KFPRVELIPW ETPIQYLPNI SREIGADVYI KRDDLTGLGI GGNKIRKLEY LLGDALSKGA DVVITVGAVH SNHAFVTGLA AKKLGLDAIL VLRGKEELKG NYLLDKIMGI ETRVYDAKDS FELMKYAEEI AEELKREGRK PYVIPPGGAS PIGTLGYVRA VGEIATQSEV KFDSIVVAAG SGGTLAGLSL GLSILNEDIR PVGIAVGRFG EVMTSKLDNL IKEAAELLGV KVEVRPELYD YSFGEYGKIT GEVAQIIRKV GTREGIILDP VYTGKAFYGL VDLARKGELG EKILFIHTGG ISGTFHYGDK LLSLL // ID 1A1D_RALSO Reviewed; 338 AA. AC Q8XS35; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 06-FEB-2007, entry version 23. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OrderedLocusNames=RSp0646; ORFNames=RS05576; OS Ralstonia solanacearum (Pseudomonas solanacearum). OG Plasmid megaplasmid Rsp. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=305; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GMI1000; RX MEDLINE=21681879; PubMed=11823852; DOI=10.1038/415497a; RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., RA Arlat M., Billault A., Brottier P., Camus J.C., Cattolico L., RA Chandler M., Choisne N., Claudel-Renard C., Cunnac S., Demange N., RA Gaspin C., Lavie M., Moisan A., Robert C., Saurin W., Schiex T., RA Siguier P., Thebault P., Whalen M., Wincker P., Levy M., RA Weissenbach J., Boucher C.A.; RT "Genome sequence of the plant pathogen Ralstonia solanacearum."; RL Nature 415:497-502(2002). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AL646080; CAD17797.1; -; Genomic_DNA. DR HSSP; O57809; 1J0A. DR SMR; Q8XS35; 1-338. DR GenomeReviews; AL646053_GR; RSp0646. DR KEGG; rso:RS05576; -. DR BioCyc; RSOL305:RSP0646-MONOMER; -. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Complete proteome; Hydrolase; Plasmid; Pyridoxal phosphate. FT CHAIN 1 338 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184506. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 338 AA; 36702 MW; 04A22A282744E95A CRC64; MNLNKHPRHP LTFGPTPIQP LKRLSAHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLVP EVLAGGYDTL VSIGGIQSNQ TRQVAAVAAH LGLKCVLVQE NWVNYADAVY DRVGNIELSR ILGADVRLDA AGFDIGIRPS WEQAMEDVRR AGGKPFPIPA GCSEHPLGGL GFVGFAEEVR QQEAEFGFRF DYIVVCSVTG STQAGMVVGF AADGRADRVI GIDASAKPEQ TREQILRIAR DTAKLVELGR DITEDDVVLD TRYGGPEYGL PNEGTLEAIR LCARQEGMLT DPVYEGKSMH GMIDRVRGGE FPEGSRVLYA HLGGVPALNA YSFLFRNG // ID 1A1D_RHILO Reviewed; 337 AA. AC Q98AM7; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 06-FEB-2007, entry version 21. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OrderedLocusNames=mlr5932; OS Rhizobium loti (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=381; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF303099; RX MEDLINE=21082930; PubMed=11214968; DOI=10.1093/dnares/7.6.331; RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium RT Mesorhizobium loti."; RL DNA Res. 7:331-338(2000). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; BA000012; BAB52295.1; -; Genomic_DNA. DR HSSP; O57809; 1J0A. DR GenomeReviews; BA000012_GR; mlr5932. DR KEGG; mlo:mlr5932; -. DR BioCyc; MLOT381:MLR5932-MONOMER; -. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Complete proteome; Hydrolase; Pyridoxal phosphate. FT CHAIN 1 337 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184508. FT BINDING 50 50 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 337 AA; 36602 MW; 3C5C52F995C49646 CRC64; MLEKFERYPL TFGLTPIEKL DRLGKHLGGK VEIYAKREDC NSGLAFGGNK LRKLEYVIPD AIASDADTLV TVGGVQSNHT RMVAAVAAKI GMKCLLVHES WVPHEDVVYD RVGNILLSRI LGAEVRLVDD GFDIGIRRSW EKALYEVKAR GGRPYAIPAG ASVHPNGGLG YVGFAEEVRA QEEQLGFAFD YMVVCTVTGS THAGMLVGFA KDGRQRNVIG IDASATPAKT KAQVLSIARH TATLVELGSE LAEDDVVLLE DYAHPRYGIP SEETKEAIRL CARLEGMITD PVYEGKSMQG MIDLVQKGFF PAGSRILYAH LGGAPAINGY GYTFRNG // ID 1A1D_RHILV Reviewed; 339 AA. AC Q93AG0; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 06-FEB-2007, entry version 20. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OS Rhizobium leguminosarum bv. viciae. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=387; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=128c53; RX MEDLINE=22783811; PubMed=12902221; RX DOI=10.1128/AEM.69.8.4396-4402.2003; RA Ma W., Guinel F.C., Glick B.R.; RT "Rhizobium leguminosarum biovar viciae 1-aminocyclopropane-1- RT carboxylate deaminase promotes nodulation of pea plants."; RL Appl. Environ. Microbiol. 69:4396-4402(2003). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source. CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AF421376; AAL16088.1; -; Genomic_DNA. DR HSSP; O57809; 1J0A. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Hydrolase; Pyridoxal phosphate. FT CHAIN 1 339 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184507. FT ACT_SITE 79 79 Nucleophile (By similarity). FT BINDING 52 52 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 339 AA; 36607 MW; B736AB026D982A6B CRC64; MSLLEKFERY PLTFGPTPIE HLPRLTAALG GKVDIYAKRD DCNSGLAMGG NKLRKLEYIV PDAIASGADT LVSIGGVQSN HTRMVAATAA KIGMKCVVIQ EKWVPHYDAV YDRVGNILMT KLMGADSRLV EDGFDIGIRK SWEDAIQSVE DAGGKPYAIP AGASVHKFGG LGYVGFAEEV AAQEKDLGFI FDYIIVCVVT GSTQGGMIVG FAALDRADRV IGIDASGTLQ QTRDQVRKIV DATSELVNLG RSVREDEIVI NPDYAYPAYG VPSEETNEAI RLAARTEAMI TDPVYEGKSM QGMIDLARKG FFPEGSKVLY AHLGGAPALN GYSYYYKDG // ID 1A1D_SCHPO Reviewed; 338 AA. AC Q9URX3; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 31-OCT-2006, entry version 27. DE Probable 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) DE (ACC deaminase) (ACCD). GN ORFNames=SPAC922.03; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AL133522; CAB63550.1; -; Genomic_DNA. DR PIR; T50268; T50268. DR HSSP; O57809; 1J0A. DR GeneDB_Spombe; SPAC922.03; -. DR ArrayExpress; Q9URX3; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Complete proteome; Hydrolase; Pyridoxal phosphate. FT CHAIN 1 338 Probable 1-aminocyclopropane-1- FT carboxylate deaminase. FT /FTId=PRO_0000184511. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 338 AA; 36687 MW; AE480741BD708BF3 CRC64; MGLEQFKKYP LTFGPTPITS MKRLSKTLGG KVEIFAKRED CNSGLAFGGN KIRKLEYLIP EAIDGGYDTL VSIGGIQSNQ TRQVAAVAAH LGLDCVLIQE DWVDYKDTMY DRVGNIELSR IVNADVRLDS SKFDIGIRPS FKNALEELTK KGKKPFPIPA GCSEHPYGGL GFVGCVEEIY EQEKQLGFKF DKIVVCTVTG SSFAGIIVGM ALTGRQKDVI GIDASATPEK TKAQVLRIAQ NTAKLIGLEK ELTESDVNID TRFAHPAYGI PNEGTIEAIK LCGATEGVLT DPVYEGKSMQ GLIHLVRNNE IAEGSKVLYI HLGGAPALSA YSAYFKNT // ID 1A1D_THEMA Reviewed; 312 AA. AC Q9WY68; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 20-FEB-2007, entry version 37. DE Putative 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) DE (ACC deaminase). GN OrderedLocusNames=TM_0225; OS Thermotoga maritima. OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=2336; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX MEDLINE=99287316; PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AE000512; AAD35317.1; -; Genomic_DNA. DR PIR; D72401; D72401. DR HSSP; O57809; 1J0A. DR GenomeReviews; AE000512_GR; TM0225. DR KEGG; tma:TM0225; -. DR TIGR; TM_0225; -. DR BioCyc; TMAR2336:TM0225-MONOMER; -. DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase...; IEA:EC. DR InterPro; IPR001926; B6_enzyme_beta. DR InterPro; IPR005966; PyridoxP_deam. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01275; ACC_deam_rel; 1. KW Complete proteome; Hydrolase; Hypothetical protein; KW Pyridoxal phosphate. FT CHAIN 1 312 Putative 1-aminocyclopropane-1- FT carboxylate deaminase. FT /FTId=PRO_0000184520. FT BINDING 42 42 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 312 AA; 34756 MW; 6BE2A4A0BFC1E15F CRC64; MRIDLSLKPT PVQFLKRLSE KYGFNIYVKR DDLTELVGSG NKIRKLEYLL WEALKKGATT VFTCGGLQSN HARATAYVSR RYGLKPVLFL RKGEKVLNGN LLLDILLGAE IVEVSPEEYE RIDEIFDVHK KMREKKGEKV YVIPEGGSNS LGAFGYFNAV LEMKDQLNLE SFDAIVCAVG SGGTIAGLSA GISFLEYHVP VVGVNVTTKN SDYFVGKVKR IISGMEEYGL RVNETVFEVV DDYRGPGYAI PSSEDVEILK EVASIEGIIL DPVYTAKAFR GMIEMFRNSE KNVLFIHTGG IFGLFAQSRR LV // ID 1A1D_VARPD Reviewed; 338 AA. AC Q6J256; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 2. DT 06-FEB-2007, entry version 13. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). GN Name=acdS; OS Variovorax paradoxus. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=34073; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=5C2; RA Hontzeas N., Belimov A., Safronova V., Glick B.R.; RT "Rapid molecular screening of soil bacteria for 1-aminocyclopropane-1- RT carboxylate (ACC) deaminase genes."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. Allows growth on ACC as a CC nitrogen source (By similarity). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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; AY604531; AAT35829.2; -; Genomic_DNA. DR SMR; Q6J256; 1-338. DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic...; IEA:HAMAP. DR HAMAP; MF_00807; -; 1. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW Hydrolase; Pyridoxal phosphate. FT CHAIN 1 338 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184509. FT ACT_SITE 78 78 Nucleophile (By similarity). FT BINDING 51 51 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 338 AA; 36592 MW; C0BFF113A31A17AD CRC64; MNLKKFPRHV LTFGPTPIQP LKRLSAHLGG KVDLYAKRED CNSGLAFGGN KTRKLEYLIP EALEGGYDTL VSIGGIQSNQ TRQVAAVAAH LGLKCVLVQE NWVNYSDAVY DRVGNIEMSR IMGADVRLDA AGFDIGIRQS WEQAMADVRA AGGKPFPIPA GCSEHPRGGL GSVGFAEEVR QQEAELGFKF DYLVVCSVTG STQAGMVVGF AADGRADRVI GIDASAKPQQ TFEQILRIAK NTAELVELGR DITEKDVVLD RRFGGPEYGL PNEGTLEAIR LSARFEGMLT DPVYEGKSMH GMIEKVRLGE FPAGSKVLYA HLGGVPALNA YSFLFRNG // ID 1A1D_WILSA Reviewed; 341 AA. AC Q7M523; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 31-OCT-2006, entry version 19. DE 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (ACC DE deaminase) (ACCD). OS Williopsis saturnus (Yeast) (Hansenula saturnus). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Williopsis. OX NCBI_TaxID=4906; RN [1] RP NUCLEOTIDE SEQUENCE, CHARACTERIZATION, AND ACETYLATION AT SER-1. RX MEDLINE=98269041; PubMed=9604000; RA Minami R., Uchiyama K., Murakami T., Kawai J., Mikami K., Yamada T., RA Yokoi D., Ito H., Matsui H., Honma M.; RT "Properties, sequence, and synthesis in Escherichia coli of 1- RT aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus."; RL J. Biochem. 123:1112-1118(1998). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=10938279; DOI=10.1074/jbc.M004681200; RA Yao M., Ose T., Sugimoto H., Horiuchi A., Nakagawa A., Wakatsuki S., RA Yokoi D., Murakami T., Honma M., Tanaka I.; RT "Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from RT Hansenula saturnus."; RL J. Biol. Chem. 275:34557-34565(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS). RX PubMed=12882962; DOI=10.1074/jbc.M305865200; RA Ose T., Fujino A., Yao M., Watanabe N., Honma M., Tanaka I.; RT "Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate RT deaminase: insight into PLP-dependent cyclopropane ring-opening RT reaction."; RL J. Biol. Chem. 278:41069-41076(2003). CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) CC to ammonia and alpha-ketobutyrate. CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: Pyridoxal phosphate. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase 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 PIR; PW0041; PW0041. DR PDB; 1F2D; X-ray; A/B/C/D=2-341. DR PDB; 1J0C; X-ray; A/B/C/D=2-341. DR PDB; 1J0D; X-ray; A/B/C/D=2-341. DR PDB; 1J0E; X-ray; A/B/C/D=2-341. DR InterPro; IPR005965; Amcycprop_deam. DR InterPro; IPR001926; B6_enzyme_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01274; ACC_deam; 1. KW 3D-structure; Acetylation; Hydrolase; Pyridoxal phosphate. FT CHAIN 1 341 1-aminocyclopropane-1-carboxylate FT deaminase. FT /FTId=PRO_0000184512. FT ACT_SITE 78 78 Nucleophile. FT BINDING 51 51 Pyridoxal phosphate (covalent). FT MOD_RES 1 1 N-acetylserine. FT TURN 3 4 FT STRAND 12 15 FT STRAND 18 20 FT HELIX 22 27 FT TURN 28 30 FT STRAND 32 38 FT HELIX 39 41 FT TURN 46 47 FT HELIX 50 55 FT TURN 56 58 FT HELIX 59 64 FT STRAND 68 75 FT TURN 76 77 FT HELIX 79 91 FT TURN 92 92 FT STRAND 94 100 FT HELIX 107 109 FT TURN 110 115 FT HELIX 117 124 FT TURN 125 126 FT STRAND 128 131 FT HELIX 142 153 FT TURN 154 155 FT STRAND 158 161 FT HELIX 163 165 FT TURN 166 167 FT TURN 169 173 FT HELIX 174 189 FT TURN 190 190 FT STRAND 194 203 FT HELIX 204 213 FT HELIX 214 216 FT TURN 217 217 FT HELIX 219 221 FT STRAND 222 226 FT HELIX 231 249 FT TURN 250 250 FT TURN 263 264 FT TURN 266 267 FT TURN 269 270 FT HELIX 274 287 FT TURN 293 295 FT HELIX 296 308 FT TURN 309 310 FT TURN 314 315 FT STRAND 317 322 FT HELIX 326 335 SQ SEQUENCE 341 AA; 37061 MW; 64904CDD7AA2C5FA CRC64; SGVAKFAKYP LTFGPSPISN LNRLSQHLGS KVNVYAKRED CNSGLAFGGN KLRKLEYIVP DIVEGDYTHL VSIGGRQSNQ TRMVAALAAK LGKKCVLIQE DWVPIPEAEK DVYNRVGNIE LSRIMGADVR VIEDGFDIGM RKSFANALQE LEDAGHKPYP IPAGCSEHKY GGLGFVGFAD EVINQEVELG IKFDKIVVCC VTGSTTAGIL AGMAQYGRQD DVIAIDASFT SEKTKEQTLR IANNTAKLIG VEHEFKDFTL DTRFAYPCYG VPNEGTIEAI RTCAEQEGVL TDPVYEGKSM QGLIALIKED YFKPGANVLY VHLGGAPALS AYSSFFPTKT A // ID 1A23_HUMAN Reviewed; 365 AA. AC P30447; Q9TQF1; Q9TQF8; Q9TQG5; Q9TQM6; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 23-JAN-2007, entry version 57. DE HLA class I histocompatibility antigen, A-23 alpha chain precursor DE (MHC class I antigen A*23) (A-9). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*2301). RX MEDLINE=92104637; PubMed=1729171; DOI=10.1007/BF00216625; RA Little A.-M., Madrigal J.A., Parham P.; RT "Molecular definition of an elusive third HLA-A9 molecule: HLA-A9.3."; RL Immunogenetics 35:41-45(1992). RN [2] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*2302 AND A*2303). RX MEDLINE=20309230; PubMed=10852390; RX DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [3] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*2304 AND A*2305). RX MEDLINE=21068830; PubMed=11169246; RX DOI=10.1034/j.1399-0039.2000.560610.x; RA Steiner N.K., Edson S.M., Mitton W., Ng J., Hartzman R.J., RA Hurley C.K.; RT "Seven novel HLA-A alleles carry previously observed polymorphisms."; RL Tissue Antigens 56:551-552(2000). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-23 are known: A*2301, CC A*2302, A*2303, A*2304 and A*2305. The sequence shown is that of CC A*2301. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M64742; AAA03662.1; -; Unassigned_RNA. DR EMBL; AF137080; AAD33736.1; -; Genomic_DNA. DR EMBL; AF137079; AAD33736.1; JOINED; Genomic_DNA. DR EMBL; AF102572; AAD28171.1; -; Genomic_DNA. DR EMBL; AF102571; AAD28171.1; JOINED; Genomic_DNA. DR EMBL; AF135549; AAD22272.1; -; Genomic_DNA. DR EMBL; AF135548; AAD22272.1; JOINED; Genomic_DNA. DR EMBL; AF140860; AAD31878.1; -; Genomic_DNA. DR EMBL; AF140859; AAD31878.1; JOINED; Genomic_DNA. DR HSSP; Q29961; 1HSA. DR SMR; P30447; 25-302. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P30447; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-23 alpha chain. FT /FTId=PRO_0000018817. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 31 31 Y -> C (in allele A*2305). FT /FTId=VAR_016606. FT VARIANT 151 151 K -> N (in allele A*2303). FT /FTId=VAR_016607. FT VARIANT 180 180 L -> W (in allele A*2302). FT /FTId=VAR_016608. FT VARIANT 190 191 DG -> EW (in allele A*2304). FT /FTId=VAR_016609. SQ SEQUENCE 365 AA; 40733 MW; C372DE503BF393D0 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDEETGK VKAHSQTDRE NLRIALRYYN QSEAGSHTLQ MMFGCDVGSD GRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTVHIVG IIAGLVLLGA VITGAVVAAV MWRRNSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A24_HUMAN Reviewed; 365 AA. AC P05534; P30448; P30449; Q29908; Q29909; Q29910; Q95355; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2003, sequence version 2. DT 20-FEB-2007, entry version 79. DE HLA class I histocompatibility antigen, A-24 alpha chain precursor DE (MHC class I antigen A*24) (Aw-24) (A-9). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*2401). RX MEDLINE=85206128; PubMed=2987115; RA N'Guyen C., Sodoyer R., Trucy J., Strachan T., Jordan B.R.; RT "The HLA-AW24 gene: sequence, surroundings and comparison with the RT HLA-A2 and HLA-A3 genes."; RL Immunogenetics 21:479-489(1985). RN [2] RP SEQUENCE REVISION. RA Jordan B.R.; RL Submitted (JUL-1988) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELES A*2402 AND A*2403). RX MEDLINE=92104637; PubMed=1729171; DOI=10.1007/BF00216625; RA Little A.-M., Madrigal J.A., Parham P.; RT "Molecular definition of an elusive third HLA-A9 molecule: HLA-A9.3."; RL Immunogenetics 35:41-45(1992). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE A*2402). RX MEDLINE=92269955; PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*2402). RX MEDLINE=98007772; PubMed=9349616; RA Laforet M., Froelich N., Parissiadis A., Bausinger H., Pfeiffer B., RA Tongio M.M.; RT "An intronic mutation responsible for a low level of expression of an RT HLA-A*24 allele."; RL Tissue Antigens 50:340-346(1997). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE A*2408). RC TISSUE=Blood; RA Kashiwase K., Tokunaga K., Ishikawa Y., Qiu L., Furuya M., RA Sawanaka K., Akaza T., Tadokoro K., Juji T.; RT "Sequence analysis of a serological subtype, HLA-A9HH, observed in RT Japanese and the confirmatory sequence of A*2408."; RL MHC 3:9-14(1996). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE A*2410). RC TISSUE=Blood; RX MEDLINE=97161044; PubMed=9008316; RA Gao X., Matheson B.; RT "A novel HLA-A*24 (A*2410) identified in a Javanese population."; RL Tissue Antigens 48:711-713(1996). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES A*2406; A*2413 RP AND A*2414). RC TISSUE=Blood; RX MEDLINE=97417771; PubMed=9271829; RA Gao X., Lester S., Matheson B., Boettcher B., McCluskey J.; RT "Three newly identified A*24 alleles: A*2406, A*2413 and A*2414."; RL Tissue Antigens 50:192-196(1997). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-24 are known: A*2401, CC A*2402, A*2403, A*2406, A*2408 (A9HH), A*2410 (A*24JV), A*2413 CC (A*24YM) and A*2414 (A*24SA). Allele A*2402 is represented in all CC major racial groups. Allele A*2406 and allele A*2413 are found in CC the Australian Aborigenal population. Allele A*2414 is found in CC individuals of South American descent. The sequence shown is that CC of A*2402. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M15497; AAA59611.1; -; Genomic_DNA. DR EMBL; M64740; AAA59600.1; -; mRNA. DR EMBL; M64741; AAA59601.1; -; Genomic_DNA. DR EMBL; Z72422; CAA96532.1; -; Genomic_DNA. DR EMBL; D83516; BAA11936.1; -; mRNA. DR EMBL; U37111; AAA83264.1; -; Genomic_DNA. DR EMBL; U37110; AAA83264.1; JOINED; Genomic_DNA. DR EMBL; U37113; AAA83265.1; -; Genomic_DNA. DR EMBL; U37112; AAA83265.1; JOINED; Genomic_DNA. DR EMBL; U37115; AAB40048.1; -; Genomic_DNA. DR EMBL; U37114; AAB40048.1; JOINED; Genomic_DNA. DR EMBL; U19733; AAB60651.1; -; Genomic_DNA. DR EMBL; U18987; AAB60651.1; JOINED; Genomic_DNA. DR PIR; I54416; I54416. DR UniGene; Hs.181244; -. DR PDB; 2BCK; X-ray; A/D=25-302. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P05534; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-24 alpha chain. FT /FTId=PRO_0000018818. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 5 5 A -> G (in allele A*2401). FT /FTId=VAR_004354. FT VARIANT 27 27 H -> Q (in allele A*2408). FT /FTId=VAR_004355. FT VARIANT 86 86 E -> G (in allele A*2408). FT /FTId=VAR_004356. FT VARIANT 89 89 G -> R (in allele A*2408). FT /FTId=VAR_004357. FT VARIANT 119 119 L -> V (in allele A*2414). FT /FTId=VAR_015765. FT VARIANT 121 121 M -> R (in allele A*2414). FT /FTId=VAR_015766. FT VARIANT 123 123 F -> Y (in allele A*2414). FT /FTId=VAR_015767. FT VARIANT 131 131 G -> W (in allele A*2414). FT /FTId=VAR_015768. FT VARIANT 180 180 Q -> L (in allele A*2413). FT /FTId=VAR_015769. FT VARIANT 180 180 Q -> W (in allele A*2406; requires 2 FT nucleotide substitutions). FT /FTId=VAR_004358. FT VARIANT 187 187 T -> R (in allele A*2410). FT /FTId=VAR_015770. FT VARIANT 190 191 DG -> EW (in allele A*2403 and allele FT A*2410). FT /FTId=VAR_004359. FT VARIANT 206 206 T -> A (in allele A*2401). FT /FTId=VAR_004360. FT STRAND 27 36 FT TURN 39 40 FT STRAND 41 43 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 76 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 159 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 197 FT TURN 198 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 212 217 FT STRAND 219 235 FT STRAND 238 243 FT TURN 244 245 FT HELIX 249 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 290 292 FT STRAND 294 296 FT STRAND 298 302 SQ SEQUENCE 365 AA; 40689 MW; D33684D126F98EC3 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDEETGK VKAHSQTDRE NLRIALRYYN QSEAGSHTLQ MMFGCDVGSD GRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQITKRK WEAAHVAEQQ RAYLEGTCVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTVPIVG IIAGLVLLGA VITGAVVAAV MWRRNSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A25_HUMAN Reviewed; 365 AA. AC P18462; Q95362; Q9TQE8; Q9TQG0; Q9UQU3; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 20-FEB-2007, entry version 68. DE HLA class I histocompatibility antigen, A-25 alpha chain precursor DE (MHC class I antigen A*25) (A-10). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*2501). RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE A*2501). 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] (ALLELE A*2502). RC TISSUE=Hematopoietic; RX MEDLINE=97045042; PubMed=8881046; DOI=10.1007/s002510050175; RA Krausa P., Young D.M., Gotch F.; RT "Identification of a new HLA-A allele (A*2502) by PCR-SSP."; RL Immunogenetics 45:84-85(1996). RN [4] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*2502). RA Guttridge M.G.; RT "Sequence confirmation of HLA-A*2502."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*2503). RX MEDLINE=20309230; PubMed=10852390; RX DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-25 are known: A*2501 CC A*2502 and A*2503. The sequence shown is that of A*2501. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M32321; AAA36234.1; -; mRNA. DR EMBL; BC008611; AAH08611.1; -; mRNA. DR EMBL; X97802; CAA66389.1; -; mRNA. DR EMBL; AJ238524; CAB41888.1; -; Genomic_DNA. DR EMBL; AF137076; AAD33737.1; -; Genomic_DNA. DR EMBL; AF137075; AAD33737.1; JOINED; Genomic_DNA. DR EMBL; AF148898; AAD34010.1; -; Genomic_DNA. DR EMBL; AF148897; AAD34010.1; JOINED; Genomic_DNA. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P18462; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P18462; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-25 alpha chain. FT /FTId=PRO_0000018819. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 33 33 Y -> F (in allele A*2503). FT /FTId=VAR_016737. FT VARIANT 94 94 H -> Q (in allele A*2502). FT /FTId=VAR_004361. SQ SEQUENCE 365 AA; 41218 MW; 00F71BD2F97C3620 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAHSQTDRE SLRIALRYYN QSEDGSHTIQ RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW RAYLEGRCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A26_HUMAN Reviewed; 365 AA. AC P30450; O02963; O78073; P79563; Q30208; Q31623; Q95377; Q9BD15; AC Q9BD19; Q9MW42; Q9TQK5; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 20-FEB-2007, entry version 64. DE HLA class I histocompatibility antigen, A-26 alpha chain precursor DE (MHC class I antigen A*26). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELES A*2601 AND A*2602). RX MEDLINE=93235211; PubMed=8475492; RA Madrigal J.A., Hildebrand W.H., Belich M.P., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA du Toit E.D., Parham P.; RT "Structural diversity in the HLA-A10 family of alleles: correlations RT with serology."; RL Tissue Antigens 41:72-80(1993). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*2601). RX MEDLINE=90256559; PubMed=1692821; DOI=10.1016/0198-8859(90)90047-S; RA Zinzsner H., Masset M., Bourge J.-F., Colombani J., Cohen D., RA Degos L., Paul P.; RT "Nucleotide sequence of the HLA-A26 class I gene: identification of RT specific residues and molecular mapping of public HLA class I RT epitopes."; RL Hum. Immunol. 27:155-166(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*2601; A*2602; A*2603 AND RP A*2604). RC TISSUE=Blood; RX MEDLINE=94299439; PubMed=8026990; DOI=10.1016/0198-8859(94)90263-1; RA Ishikawa Y., Tokunaga K., Lin L., Imanishi T., Saitou S., RA Kashiwase K., Akaza T., Tadokoro K., Juji T.; RT "Sequences of four splits of HLA-A10 group. Implications for serologic RT cross-reactivities and their evolution."; RL Hum. Immunol. 39:220-224(1994). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE A*2601). RC TISSUE=Lymphocyte; RA Miyashita H., Fujiyoshi T., Yashiki S., Kuwayama M., Fujiyama C., RA Sonoda S.; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*2603). RC TISSUE=Lymphocyte; RX MEDLINE=96435465; PubMed=8838351; RA Miyashita H., Fujiyoshi T., Yashiki S., Kuwayama M., Fujiyama C., RA Sonoda S.; RT "Cloning of HLA-A26 cDNA from Japanese donors possessing 'ATL- RT associated HLA haplotypes'."; RL Tissue Antigens 46:398-400(1995). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE A*2605). RC TISSUE=Blood; RA Maruya E., Ishikawa Y., Lin L., Tokunaga K., Kimura A., Saitou S., RA Nita H., Juji T., Saji H.; RT "A novel A26 sequence found in Japanese, and identification of four RT major HLA-A26 subtypes."; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*2607). RX MEDLINE=96387673; PubMed=8795143; RA Arnett K.L., Moses J.H., Williams F., Marsh S.G.E., Bodmer J.G., RA Parham P., Middleton D.; RT "HLA-A *2607: sequence of a novel A*26 subtype predicted by DNA typing RT which shares the MA2.1 epitope with A*02, B*57 and B*58."; RL Tissue Antigens 47:422-425(1996). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*2608). RX MEDLINE=97051455; PubMed=8896181; RA Szmania S., Baxter-Lowe L.A.; RT "Nucleotide sequence for HLA-A*2608 which encodes glutamine at codon RT 156."; RL Tissue Antigens 48:210-212(1996). RN [9] RP NUCLEOTIDE SEQUENCE (ALLELE A*2608). RA Ellexson M.E., Hildebrand W.H.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*2612). RX MEDLINE=20548605; PubMed=11098929; RX DOI=10.1034/j.1399-0039.2000.560401.x; RA Ellis J.M., Mack S.J., Leke R.F.G., Quakyi I., Johnson A.H., RA Hurley C.K.; RT "Diversity is demonstrated in class I HLA-A and HLA-B alleles in RT Cameroon, Africa: description of HLA-A*03012, *2612, *3006 and HLA- RT B*1403, *4016, *4703."; RL Tissue Antigens 56:291-302(2000). RN [11] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*2612). RX MEDLINE=21160440; PubMed=11260503; RX DOI=10.1034/j.1399-0039.2001.057002095.x; RA Hickman H.D., Cavett J.W., Ellexson-Turner M.E., Sparkman J.N., RA Bennett T.T., Turner S., Sidebottom D.A., Trachtenberg E.A., RA Confer D.L., Hildebrand W.H.; RT "Non-conservative substitutions distinguish previously uncharacterized RT HLA-A molecules."; RL Tissue Antigens 57:95-102(2001). RN [12] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*2615). RA Voorter C.E., Gervais T., van den Berg-Loonene E.M.; RT "New HLA-A alleles detected by sequence-based typing."; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE OF 26-298 (ALLELE A*2607). RA Moine A.; RT "A new variant form of a HLA A*2607 allele."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-365 (ALLELE A*2601). RX MEDLINE=89122144; PubMed=2914713; RA Cianetti L., Testa U., Scotto L., la Valle R., Simeone A., Boccoli G., RA Giannella G., Peschle C., Boncinelli E.; RT "Three new class I HLA alleles: structure of mRNAs and alternative RT mechanisms of processing."; RL Immunogenetics 29:80-91(1989). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-26 are known: A*2601, CC A*2602, A*2603, A*2604 (A-10SA), A*2605, A*2607, A*2608, A*2612 CC and A*2615. The sequence shown is that of A*2601. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; U03697; AAA03720.1; -; mRNA. DR EMBL; M98453; AAA35991.1; -; mRNA. DR EMBL; D14350; BAA03279.1; -; mRNA. DR EMBL; D14351; BAA03280.1; -; mRNA. DR EMBL; D14354; BAA03282.1; -; mRNA. DR EMBL; D16843; BAA04119.1; -; mRNA. DR EMBL; D32130; BAA06856.1; -; mRNA. DR EMBL; D32131; BAA06857.1; -; mRNA. DR EMBL; D32129; BAA06855.1; -; mRNA. DR EMBL; D50068; BAA08783.1; -; mRNA. DR EMBL; L48341; AAF25960.1; -; Genomic_DNA. DR EMBL; U52429; AAB08574.1; -; mRNA. DR EMBL; U45480; AAB38491.1; -; mRNA. DR EMBL; AF065487; AAC17438.1; -; Genomic_DNA. DR EMBL; AF065486; AAC17438.1; JOINED; Genomic_DNA. DR EMBL; AF042187; AAD02210.1; -; Genomic_DNA. DR EMBL; AF042186; AAD02210.1; JOINED; Genomic_DNA. DR EMBL; AJ291695; CAC27239.1; -; Genomic_DNA. DR EMBL; AJ291696; CAC27239.1; JOINED; Genomic_DNA. DR EMBL; AJ290394; CAC27416.2; -; mRNA. DR EMBL; M24095; AAA59655.1; -; mRNA. DR PIR; I38436; I38436. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P30450; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P30450; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-26 alpha chain. FT /FTId=PRO_0000018820. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 60 60 F -> L (in allele A*2615). FT /FTId=VAR_016341. FT VARIANT 86 87 RN -> GE (in allele A*2607). FT /FTId=VAR_016342. FT VARIANT 90 90 N -> K (in allele A*2607). FT /FTId=VAR_016343. FT VARIANT 98 101 DRAN -> HRVD (in allele A*2603). FT /FTId=VAR_004362. FT VARIANT 100 100 A -> E (in allele A*2605). FT /FTId=VAR_016344. FT VARIANT 140 140 D -> N (in allele A*2602). FT /FTId=VAR_004364. FT VARIANT 176 176 E -> V (in allele A*2612). FT /FTId=VAR_016345. FT VARIANT 180 180 W -> Q (in allele A*2608; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016346. FT VARIANT 187 187 R -> L (in allele A*2604). FT /FTId=VAR_004363. FT VARIANT 306 306 I -> V (in dbSNP:rs1136949). FT /FTId=VAR_014603. FT CONFLICT 153 153 D -> H (in Ref. 14). FT CONFLICT 160 160 A -> G (in Ref. 14). SQ SEQUENCE 365 AA; 41062 MW; 44B54DD363B46EDA CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAHSQTDRA NLGTLRGYYN QSEDGSHTIQ RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW RAYLEGRCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A29_HUMAN Reviewed; 365 AA. AC P30512; O02955; O19687; O98011; P30451; P79562; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 20-FEB-2007, entry version 65. DE HLA class I histocompatibility antigen, A-29 alpha chain precursor DE (MHC class I antigen A*29) (Aw-19). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*2901). RX MEDLINE=89065816; PubMed=2461903; RA Trapani J.A., Mizuno S., Kang S.H., Yang S.Y., Dupont B.; RT "Molecular mapping of a new public HLA class I epitope shared by all RT HLA-B and HLA-C antigens and defined by a monoclonal antibody."; RL Immunogenetics 29:25-32(1989). RN [2] RP SEQUENCE REVISION TO 345. RA Yang S.Y.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE A*2901). RA Szmania S., Baxter-Lowe L.A.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*2902). RX MEDLINE=92145462; PubMed=1782566; RA Tabary T., Prochnicka-Chalufour A., Cornillet P., Lehoang P., RA Betuel H., Cohen H.M.; RT "HLA-A29 sub-types and 'Birdshot' choroido-retinopathy susceptibility: RT a possible 'resistance motif' in the HLA-A29.1 molecule."; RL C. R. Acad. Sci. III, Sci. Vie 313:599-605(1991). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELE A*2903). RX MEDLINE=98119601; PubMed=9459513; RA Prokupek B., Dunn P., Ross J., Jordan F., Holman R., Madrigal J.A., RA Little A.-M.; RT "HLA-A*2903 expresses an epitope shared with HLA-A*8001."; RL Tissue Antigens 51:115-118(1998). RN [6] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*2904). RX MEDLINE=21160440; PubMed=11260503; RX DOI=10.1034/j.1399-0039.2001.057002095.x; RA Hickman H.D., Cavett J.W., Ellexson-Turner M.E., Sparkman J.N., RA Bennett T.T., Turner S., Sidebottom D.A., Trachtenberg E.A., RA Confer D.L., Hildebrand W.H.; RT "Non-conservative substitutions distinguish previously uncharacterized RT HLA-A molecules."; RL Tissue Antigens 57:95-102(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-29 are known: A*2901 CC (A29.1), A*2902 (A29.2), A*2903 and A*2904. The sequence shown is CC that of A*2901. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M23739; AAB47873.1; -; mRNA. DR EMBL; U83415; AAB53373.1; -; mRNA. DR EMBL; X60108; CAA42702.1; -; mRNA. DR EMBL; AJ000661; CAA04209.1; -; mRNA. DR EMBL; Y09218; CAA70419.1; -; Genomic_DNA. DR EMBL; AF042189; AAD02224.1; -; Genomic_DNA. DR EMBL; AF042188; AAD02224.1; JOINED; Genomic_DNA. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P30512; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P30512; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-29 alpha chain. FT /FTId=PRO_0000018821. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 90 90 N -> H (in allele A*2904). FT /FTId=VAR_016347. FT VARIANT 126 126 H -> D (in allele A*2902, allele A*2903 FT and allele A*2904). FT /FTId=VAR_004365. FT VARIANT 190 191 EW -> DG (in allele A*2903). FT /FTId=VAR_010372. SQ SEQUENCE 365 AA; 40863 MW; 56E4B9039B3C783C CRC64; MAVMAPRTLL LLLLGALALT QTWAGSHSMR YFTTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDLQTRN VKAQSQTDRA NLGTLRGYYN QSEAGSHTIQ MMYGCHVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VFAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A30_HUMAN Reviewed; 365 AA. AC P16188; O19598; O62921; P30452; Q9UIP7; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 20-FEB-2007, entry version 65. DE HLA class I histocompatibility antigen, A-30 alpha chain precursor DE (MHC class I antigen A*30). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*3001). RX MEDLINE=90038496; PubMed=2478623; RA Kato K., Trapani J.A., Allopenna J., Dupont B., Yang S.Y.; RT "Molecular analysis of the serologically defined HLA-Aw19 antigens. A RT genetically distinct family of HLA-A antigens comprising A29, A31, RT A32, and Aw33, but probably not A30."; RL J. Immunol. 143:3371-3378(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*3001). RX MEDLINE=95176329; PubMed=7871528; RA Olerup O., Daniels T.J., Baxter-Lowe L.; RT "Correct sequence of the A*3001 allele obtained by PCR-SSP typing and RT automated nucleotide sequencing."; RL Tissue Antigens 44:265-267(1994). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE A*3002). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-279 (ALLELE A*3003). RX MEDLINE=93209813; PubMed=8458735; DOI=10.1016/0198-8859(93)90004-K; RA Choo S.Y., Starling G.C., Anasetti C., Hansen J.A.; RT "Selection of an unrelated donor for marrow transplantation RT facilitated by the molecular characterization of a novel HLA-A RT allele."; RL Hum. Immunol. 36:20-26(1993). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*3004). RX MEDLINE=96058597; PubMed=8522453; DOI=10.1016/0198-8859(95)00046-7; RA Krausa P., Carcassi C., Orru S., Bodmer J.G., Browning M.J., Contu L.; RT "Defining the allelic variants of HLA-A30 in the Sardinian population RT using amplification refractory mutation system -- polymerase chain RT reaction."; RL Hum. Immunol. 44:35-42(1995). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 26-206 (ALLELE A*3004). RX MEDLINE=96435464; PubMed=8838350; RA Lienert K., Russ G., Bennett G., Gao X., McCluskey J.; RT "HLA-A*3004: a new A30 allele identified in an Australian Caucasoid RT population."; RL Tissue Antigens 46:394-397(1995). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-205 (ALLELE A*3004). RX MEDLINE=96124443; PubMed=8560452; RA Blasczyk R., Wehling J., Paessler M., Hahn U., Huhn D., Salama A.; RT "A novel HLA-A30 allele (A*3004) identified by single-strand RT conformation polymorphism analysis and confirmed by solid-phase RT sequencing."; RL Tissue Antigens 46:322-326(1995). RN [8] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3006). RX MEDLINE=20548605; PubMed=11098929; RX DOI=10.1034/j.1399-0039.2000.560401.x; RA Ellis J.M., Mack S.J., Leke R.F.G., Quakyi I., Johnson A.H., RA Hurley C.K.; RT "Diversity is demonstrated in class I HLA-A and HLA-B alleles in RT Cameroon, Africa: description of HLA-A*03012, *2612, *3006 and HLA- RT B*1403, *4016, *4703."; RL Tissue Antigens 56:291-302(2000). RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3007). RX MEDLINE=20309230; PubMed=10852390; RX DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [10] RP NUCLEOTIDE SEQUENCE (ALLELE A*3008). RX MEDLINE=21108617; PubMed=11169261; RX DOI=10.1034/j.1399-0039.2001.057001070.x; RA Cox S.T., Mcwhinnie A.J., Koester R.P., Heine U., Holman R., RA Madrigal A.J., Little A.-M.; RT "Further diversity at HLA-A and -B loci identified in Afro-Caribbean RT potential bone marrow donors."; RL Tissue Antigens 57:70-72(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-30 are known: A*3001 CC (A30.3), A*3002, A*3003, A*3004 (A30W7), A*3006, A*3007 and CC A*3008. The sequence shown is that of A*3001. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M30576; AAA59612.1; -; Genomic_DNA. DR EMBL; U07234; AAA70162.1; -; mRNA. DR EMBL; X61702; CAA43871.1; -; mRNA. DR EMBL; M93657; AAA58650.1; -; Genomic_DNA. DR EMBL; Z34921; CAA84401.1; -; Genomic_DNA. DR EMBL; U19734; AAB53658.1; -; Genomic_DNA. DR EMBL; U18988; AAB53658.1; JOINED; Genomic_DNA. DR EMBL; U24261; AAB50434.1; -; mRNA. DR EMBL; X83770; CAA58723.1; -; Genomic_DNA. DR EMBL; X83771; CAA58724.1; -; Genomic_DNA. DR EMBL; AF028714; AAC14191.1; -; Genomic_DNA. DR EMBL; AF028713; AAC14191.1; JOINED; Genomic_DNA. DR EMBL; AF065643; AAC18600.1; -; Genomic_DNA. DR EMBL; AF065642; AAC18600.1; JOINED; Genomic_DNA. DR EMBL; AJ249308; CAB57306.1; -; Genomic_DNA. DR EMBL; AJ249309; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249310; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249311; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249312; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249313; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249314; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249315; CAB57306.1; JOINED; Genomic_DNA. DR PIR; I38519; I38519. DR PIR; I56039; I56039. DR HSSP; P10315; 1HSB. DR SMR; P16188; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P16188; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-30 alpha chain. FT /FTId=PRO_0000018822. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 21 21 H -> Q (in allele A*3002, allele A*3004 FT and allele A*3008). FT /FTId=VAR_004366. FT VARIANT 33 33 S -> Y (in allele A*3008). FT /FTId=VAR_010284. FT VARIANT 55 55 T -> A (in allele A*3006). FT /FTId=VAR_016653. FT VARIANT 80 80 R -> G (in allele A*3003). FT /FTId=VAR_004367. FT VARIANT 86 86 Q -> E (in allele A*3007). FT /FTId=VAR_016738. FT VARIANT 89 90 RN -> GK (in allele A*3007). FT /FTId=VAR_016739. FT VARIANT 94 94 Q -> H (in allele A*3002, allele A*3003, FT allele A*3004, allele A*3006 and allele FT A*3007). FT /FTId=VAR_004368. FT VARIANT 100 101 VD -> EN (in allele A*3002, allele FT A*3003, allele A*3004, allele A*3006 and FT allele A*3007). FT /FTId=VAR_004369. FT VARIANT 175 176 RW -> HV (in allele A*3004 and allele FT A*3006). FT /FTId=VAR_004370. FT VARIANT 176 176 W -> R (in allele A*3002, allele A*3003 FT and allele A*3007). FT /FTId=VAR_004371. FT VARIANT 180 180 L -> W (in allele A*3004 and allele FT A*3006). FT /FTId=VAR_004372. FT CONFLICT 33 33 S -> F (in Ref. 1). SQ SEQUENCE 365 AA; 40905 MW; 521166D95FB1DC28 CRC64; MAVMAPRTLL LLLSGALALT HTWAGSHSMR YFSTSVSRPG SGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQER PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ IMYGCDVGSD GRFLRGYEQH AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARWAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A31_HUMAN Reviewed; 365 AA. AC P16189; O62924; O98009; O98137; Q8MHM1; Q9TPQ3; Q9TQ24; Q9UQU6; AC Q9UQU7; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 20-FEB-2007, entry version 65. DE HLA class I histocompatibility antigen, A-31 alpha chain precursor DE (MHC class I antigen A*31). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*3101). RX MEDLINE=90038496; PubMed=2478623; RA Kato K., Trapani J.A., Allopenna J., Dupont B., Yang S.Y.; RT "Molecular analysis of the serologically defined HLA-Aw19 antigens. A RT genetically distinct family of HLA-A antigens comprising A29, A31, RT A32, and Aw33, but probably not A30."; RL J. Immunol. 143:3371-3378(1989). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*3101). RX MEDLINE=92269955; PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE A*3101). RX MEDLINE=96387675; PubMed=8795145; RA Arnett K.L., Adams E.J., Parham P.; RT "On the sequence of A*3101."; RL Tissue Antigens 47:428-430(1996). RN [4] RP NUCLEOTIDE SEQUENCE OF 9-365 (ALLELE A*3101). RX MEDLINE=92269956; PubMed=1589035; DOI=10.1038/357329a0; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELE A*3104). RA Bettinotti M.P., Dhillon G., Hackett J., Simonis T.B., Marincola F.M.; RT "A new HLA-A*31 allele."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3103). RA Bunce M., Dunn P., Ross J.; RT "Characterization of two new HLA-A alleles identified by PCR-SSP."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3104). RA Mitsuishi Y.; RT "New HLA-A31 allele identified in African American population."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3102). RA Dunn P.P.; RT "Characterization of an HLA-A*31 variant."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3105). RA Juji T., Akesaka T., Kashiwase K., Ishikawa Y.; RT "HLA-A31012V1."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3102). RX MEDLINE=21160440; PubMed=11260503; RX DOI=10.1034/j.1399-0039.2001.057002095.x; RA Hickman H.D., Cavett J.W., Ellexson-Turner M.E., Sparkman J.N., RA Bennett T.T., Turner S., Sidebottom D.A., Trachtenberg E.A., RA Confer D.L., Hildebrand W.H.; RT "Non-conservative substitutions distinguish previously uncharacterized RT HLA-A molecules."; RL Tissue Antigens 57:95-102(2001). RN [11] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3106). RC TISSUE=Blood; RA Anholts J.D.H.; RT "Four new HLA alleles found, and confirmation of DRB1*0322, DRB1*1433 RT and A*3106."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-31 are known: A*3101, CC A*3102, A*3103, A*3104, A*3105 (A3101v1) and A*3106. The sequence CC shown is that of A*3101. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M30578; AAA59613.1; -; Genomic_DNA. DR EMBL; M84375; AAA59599.1; -; mRNA. DR EMBL; L78918; AAB05976.1; -; Genomic_DNA. DR EMBL; AF148863; AAD39981.1; -; Genomic_DNA. DR EMBL; AF067439; AAC18859.1; -; Genomic_DNA. DR EMBL; AF067438; AAC18859.1; JOINED; Genomic_DNA. DR EMBL; AF105028; AAC79721.1; -; Genomic_DNA. DR EMBL; AF105027; AAC79721.1; JOINED; Genomic_DNA. DR EMBL; AJ239045; CAB43109.1; -; Genomic_DNA. DR EMBL; AJ239046; CAB43110.1; -; Genomic_DNA. DR EMBL; AB032597; BAA84645.1; -; Genomic_DNA. DR EMBL; AF041370; AAD02207.1; -; Genomic_DNA. DR EMBL; AF041369; AAD02207.1; JOINED; Genomic_DNA. DR EMBL; AJ506789; CAD44950.1; -; Genomic_DNA. DR EMBL; AJ506790; CAD44950.1; JOINED; Genomic_DNA. DR PIR; I72170; I72170. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P16189; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P16189; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-31 alpha chain. FT /FTId=PRO_0000018823. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 90 90 N -> K (in allele A*3102). FT /FTId=VAR_016348. FT VARIANT 114 114 A -> D (in allele A*3103). FT /FTId=VAR_016349. FT VARIANT 121 121 M -> I (in allele A*3103 and allele FT A*3104). FT /FTId=VAR_010373. FT VARIANT 138 138 Q -> R (in allele A*3103, allele A*3104 FT and allele A*3106). FT /FTId=VAR_010374. FT VARIANT 190 191 EW -> DG (in allele A*3105). FT /FTId=VAR_016350. SQ SEQUENCE 365 AA; 41004 MW; 4E760C821A3C553B CRC64; MAVMAPRTLL LLLLGALALT QTWAGSHSMR YFTTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQER PEYWDQETRN VKAHSQIDRV DLGTLRGYYN QSEAGSHTIQ MMYGCDVGSD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VFAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A32_HUMAN Reviewed; 365 AA. AC P10314; O77937; Q29838; Q8MHN9; Q9MYE9; Q9MYG5; Q9TQF5; Q9TQF9; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 20-FEB-2007, entry version 66. DE HLA class I histocompatibility antigen, A-32 alpha chain precursor DE (MHC class I antigen A*32). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*3201). RA Domena J.D.; RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE OF 25-298 (ALLELE A*3201). RX MEDLINE=87058961; PubMed=2431040; RA Wan A.M., Ennis P., Parham P., Holmes N.; RT "The primary structure of HLA-A32 suggests a region involved in RT formation of the Bw4/Bw6 epitopes."; RL J. Immunol. 137:3671-3674(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*3202). RC TISSUE=Blood; RX MEDLINE=97045038; PubMed=8881042; DOI=10.1007/s002510050171; RA Zino E., Severini G.M., Mazzi B., Bordignon C., Benazzi E., RA Fleischhauer K.; RT "Sequencing of a new HLA-A*32 subtype (A*3202)."; RL Immunogenetics 45:76-77(1996). RN [4] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*3203 AND A*3204). RX MEDLINE=20309230; PubMed=10852390; RX DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [5] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3203). RA Kanaan C., Hepner J., Thornton A.; RT "Confirmatory exon 2 and 3 sequence for HLA-A*3203."; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE A*3205). RA Bettinotti M.P., Hadzikadic L., Adams S., Marincola F.M.; RT "A new HLA A-32 allele."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3206). RA Jones P.F., Hurley C.K.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-32 are known: A*3201, CC A*3202, A*3203, A*3204, A*3205 and A*3206. The sequence shown is CC that of A*3201. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; U03907; AAA03605.1; -; mRNA. DR EMBL; X97120; CAA65786.1; -; mRNA. DR EMBL; AF072762; AAC26020.1; -; Genomic_DNA. DR EMBL; AF072761; AAC26020.1; JOINED; Genomic_DNA. DR EMBL; AF137078; AAD33738.1; -; Genomic_DNA. DR EMBL; AF137077; AAD33738.1; JOINED; Genomic_DNA. DR EMBL; AF139892; AAD33849.1; -; Genomic_DNA. DR EMBL; AF139891; AAD33849.1; JOINED; Genomic_DNA. DR EMBL; AF517562; AAM78538.1; -; Genomic_DNA. DR EMBL; AF517561; AAM78538.1; JOINED; Genomic_DNA. DR EMBL; AF217560; AAF28733.1; -; mRNA. DR EMBL; AF226837; AAF29554.1; -; Genomic_DNA. DR EMBL; AF226836; AAF29554.1; JOINED; Genomic_DNA. DR PIR; A26088; HLHU32. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P10314; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P10314; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-32 alpha chain. FT /FTId=PRO_0000018824. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 89 90 RN -> GK (in allele A*3205). FT /FTId=VAR_016656. FT VARIANT 101 101 S -> N (in allele A*3203). FT /FTId=VAR_016657. FT VARIANT 121 121 M -> I (in allele A*3204). FT /FTId=VAR_016831. FT VARIANT 129 129 P -> S (in allele A*3204). FT /FTId=VAR_016832. FT VARIANT 133 133 L -> F (in allele A*3204). FT /FTId=VAR_016833. FT VARIANT 138 138 Q -> R (in allele A*3204). FT /FTId=VAR_016834. FT VARIANT 168 168 Q -> K (in allele A*3204). FT /FTId=VAR_016835. FT VARIANT 175 175 R -> H (in allele A*3202, allele A*3204 FT and allele A*3206). FT /FTId=VAR_004373. FT VARIANT 176 176 V -> E (in allele A*3204). FT /FTId=VAR_016836. FT VARIANT 180 180 L -> Q (in allele A*3202). FT /FTId=VAR_004374. FT VARIANT 185 185 E -> D (in allele A*3204). FT /FTId=VAR_016837. SQ SEQUENCE 365 AA; 41048 MW; BF7AF225329E0319 CRC64; MAVMAPRTLL LLLLGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAHSQTDRE SLRIALRYYN QSEAGSHTIQ MMYGCDVGPD GRLLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA MFAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A33_HUMAN Reviewed; 365 AA. AC P16190; O02939; O02954; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 3. DT 23-JAN-2007, entry version 66. DE HLA class I histocompatibility antigen, A-33 alpha chain precursor DE (MHC class I antigen A*33) (Aw-33) (Aw-19). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*3301). RX MEDLINE=90038496; PubMed=2478623; RA Kato K., Trapani J.A., Allopenna J., Dupont B., Yang S.Y.; RT "Molecular analysis of the serologically defined HLA-Aw19 antigens. A RT genetically distinct family of HLA-A antigens comprising A29, A31, RT A32, and Aw33, but probably not A30."; RL J. Immunol. 143:3371-3378(1989). RN [2] RP SEQUENCE REVISION TO 178-179; 210 AND 345. RA Yang S.Y.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE A*3301). RA Szmania S., Baxter-Lowe L.A.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*3302). RX MEDLINE=93369838; PubMed=8362415; RA Kato N., Kikuchi A., Kano K., Egawa K., Takiguchi M.; RT "Molecular analysis of a novel HLA-A33 subtype associated with HLA- RT B44."; RL Tissue Antigens 41:211-213(1993). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*3303). RX MEDLINE=95242316; PubMed=7725315; RA Balas A., Garcia-Sanchez F., Vicario J.L.; RT "Molecular characterization of a novel HLA-A33 allele (A*3303)."; RL Tissue Antigens 45:73-76(1995). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-99 AND 122-205 (ALLELES A*3301 RP AND A*3303). RX MEDLINE=95381237; PubMed=7652743; RA Blasczyk R., Wehling J., Hahn U., Schwella N., Huhn D., Salama A.; RT "Identification of a novel HLA-A33 subtype (A*3303) and correction of RT the A*3301 sequence."; RL Tissue Antigens 45:348-352(1995). RN [7] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*3301 AND A*3303). RA Gao X., Jakobsen I., Serjeantson S.W.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-33 are known: A*3301 (Aw- CC 33.1), A*3302 and A*3303. The sequence shown is that of A*3301. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M30580; AAB47870.1; -; Genomic_DNA. DR EMBL; U83416; AAB53374.1; -; mRNA. DR EMBL; L06440; AAA71914.1; -; mRNA. DR EMBL; U09740; AAA79865.1; -; mRNA. DR EMBL; X83004; CAA58125.1; -; Genomic_DNA. DR EMBL; X83005; CAA58126.1; -; Genomic_DNA. DR EMBL; X83002; CAA58123.1; -; Genomic_DNA. DR EMBL; X83003; CAA58124.1; -; Genomic_DNA. DR EMBL; U19735; AAB60652.1; -; Genomic_DNA. DR EMBL; U19736; AAB60653.1; -; Genomic_DNA. DR PIR; I38610; I38610. DR PIR; S51099; S51099. DR PIR; S51100; S51100. DR HSSP; P10315; 1HSB. DR SMR; P16190; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P16190; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-33 alpha chain. FT /FTId=PRO_0000018825. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 41 41 R -> S (in allele A*3302). FT /FTId=VAR_004375. FT VARIANT 195 195 H -> Y (in allele A*3302 and allele FT A*3303). FT /FTId=VAR_004376. FT VARIANT 217 218 AV -> PI (in allele A*3302). FT /FTId=VAR_004377. FT VARIANT 358 358 M -> V (in allele A*3302). FT /FTId=VAR_004378. FT CONFLICT 210 210 K -> R (in Ref. 3). SQ SEQUENCE 365 AA; 40892 MW; 060AE508EADEB328 CRC64; MAVMAPRTLL LLLLGALALT QTWAGSHSMR YFTTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAHSQIDRV DLGTLRGYYN QSEAGSHTIQ MMYGCDVGSD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRHLENGK ETLQRTDPPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VFAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A34_HUMAN Reviewed; 365 AA. AC P30453; P30454; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 59. DE HLA class I histocompatibility antigen, A-34 alpha chain precursor DE (MHC class I antigen A*34) (Aw-34) (A-10). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*3401 AND A*3402). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*3401 AND A*3402). RX MEDLINE=93235211; PubMed=8475492; RA Madrigal J.A., Hildebrand W.H., Belich M.P., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA du Toit E.D., Parham P.; RT "Structural diversity in the HLA-A10 family of alleles: correlations RT with serology."; RL Tissue Antigens 41:72-80(1993). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-34 are known: A*3401 (Aw- CC 34.1) and A*3402 (Aw-34.2). The sequence shown is that of A*3401. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X61704; CAA43873.1; -; mRNA. DR EMBL; X61705; CAA43874.1; -; mRNA. DR PIR; I37477; I37477. DR PIR; I37483; I37483. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P30453; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P30453; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-34 alpha chain. FT /FTId=PRO_0000018826. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 3 3 I -> V (in allele A*3402). FT /FTId=VAR_004379. FT VARIANT 90 90 K -> N (in allele A*3402). FT /FTId=VAR_004380. FT VARIANT 121 121 R -> I (in allele A*3402). FT /FTId=VAR_004381. FT VARIANT 129 129 P -> S (in allele A*3402). FT /FTId=VAR_004382. FT VARIANT 138 138 Q -> R (in allele A*3402). FT /FTId=VAR_004383. FT VARIANT 180 180 W -> L (in allele A*3402). FT /FTId=VAR_004384. FT VARIANT 312 312 L -> I (in allele A*3402). FT /FTId=VAR_004385. SQ SEQUENCE 365 AA; 41055 MW; 063BF63E6E6E01F6 CRC64; MAIMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRK VKAQSQTDRV DLGTLRGYYN QSEDGSHTIQ RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG ILAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A36_HUMAN Reviewed; 365 AA. AC P30455; Q9MY89; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 57. DE HLA class I histocompatibility antigen, A-36 alpha chain precursor DE (MHC class I antigen A*36) (Aw-36). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*3601). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*3602). RA Rizzuto G.A., Hurley C.K.; RT "Novel HLA-A Allele."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-36 are known: A*3601 and CC A*3602. The sequence shown is that of A*3601. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X61700; CAA43869.1; -; mRNA. DR EMBL; AF274505; AAF78082.1; -; Genomic_DNA. DR EMBL; AF274504; AAF78082.1; JOINED; Genomic_DNA. DR PIR; I37478; I37478. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P30455; 25-298. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-36 alpha chain. FT /FTId=PRO_0000018827. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 182 182 V -> A (in allele A*3602). FT /FTId=VAR_016610. FT VARIANT 185 185 E -> D (in allele A*3602). FT /FTId=VAR_016611. SQ SEQUENCE 365 AA; 40934 MW; BA00A0085989CD3E CRC64; MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQKME PRAPWIEQEG PEYWDQETRN MKAHSQTDRA NLGTLRGYYN QSEDGSHTIQ IMYGCDVGPD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAVHAAEQR RVYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A43_HUMAN Reviewed; 365 AA. AC P30456; O19509; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 59. DE HLA class I histocompatibility antigen, A-43 alpha chain precursor DE (MHC class I antigen A*43) (Aw-43). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*4301). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*4301). RX MEDLINE=93235211; PubMed=8475492; RA Madrigal J.A., Hildebrand W.H., Belich M.P., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA du Toit E.D., Parham P.; RT "Structural diversity in the HLA-A10 family of alleles: correlations RT with serology."; RL Tissue Antigens 41:72-80(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE A*4301). RX MEDLINE=99446859; PubMed=10519370; RX DOI=10.1034/j.1399-0039.1999.540314.x; RA Bei M., Ng J., Slack R., Ellis J., Hartzman R.J., Hurley C.K.; RT "The relative frequencies of HLA-A*10 alleles in five major United RT States ethnic populations."; RL Tissue Antigens 54:295-299(1999). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The only allele of A-43 known is A*4301 which is CC shown here. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X61703; CAA43872.1; -; mRNA. DR EMBL; AF008306; AAB65408.1; -; Genomic_DNA. DR EMBL; AF008305; AAB65408.1; JOINED; Genomic_DNA. DR PIR; I72171; I72171. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P30456; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P30456; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-43 alpha chain. FT /FTId=PRO_0000018828. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 41033 MW; 213FC69745FB4B0B CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDLQTRN VKAHSQTDRA NLGTLRGYYN QSEDGSHTIQ RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW RAYLEGRCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A66_HUMAN Reviewed; 365 AA. AC P30457; P30458; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 61. DE HLA class I histocompatibility antigen, A-66 alpha chain precursor DE (MHC class I antigen A*66) (Aw-66) (A-10). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*6601 AND A*6602). RX MEDLINE=92044300; PubMed=1940790; DOI=10.1084/jem.174.5.1085; RA Madrigal J., Belich M.P., Benjamin R.J., Little A.-M., RA Hildebrand W.H., Mann D.L., Parham P.; RT "Molecular definition of a polymorphic antigen (LA45) of free HLA-A RT and -B heavy chains found on the surfaces of activated B and T RT cells."; RL J. Exp. Med. 174:1085-1095(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*6602). RX MEDLINE=90237739; PubMed=2139695; DOI=10.1084/jem.171.5.1431; RA Schnabl E., Stockinger H., Majdic O., Gaugitsch H., Lindley I.J.D., RA Maurer D., Hajek-Rosenmayr A., Knapp W.; RT "Activated human T lymphocytes express MHC class I heavy chains not RT associated with beta 2-microglobulin."; RL J. Exp. Med. 171:1431-1442(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-322 (ALLELE A*6601). RA Hurley C., Bei M.; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-66 are known: A*6601 and CC A*6602 (Aw67). The sequence shown is that of A*6601. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X61711; CAA43880.1; -; mRNA. DR EMBL; X61712; CAA43881.1; -; mRNA. DR EMBL; X51745; CAA36034.1; -; mRNA. DR EMBL; U17571; AAA56781.1; -; mRNA. DR PIR; JL0135; JL0135. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P30457; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P30457; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-66 alpha chain. FT /FTId=PRO_0000018829. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 28 28 S -> W (in allele A*6602). FT /FTId=VAR_004386. FT VARIANT 114 114 D -> A (in allele A*6602). FT /FTId=VAR_004387. FT VARIANT 187 187 R -> E (in allele A*6602; requires 2 FT nucleotide substitutions). FT /FTId=VAR_004388. SQ SEQUENCE 365 AA; 41082 MW; A3272DBE4008328D CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAQSQTDRV DLGTLRGYYN QSEDGSHTIQ RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW RAYLEGRCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A68_HUMAN Reviewed; 365 AA. AC P01891; O19673; O19695; O19794; O19795; O43907; O77938; O98010; AC P10315; P79505; Q9MYA5; Q9MYC4; Q9TQG7; Q9TQN5; Q9UIN2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 4. DT 20-FEB-2007, entry version 80. DE HLA class I histocompatibility antigen, A-68 alpha chain precursor DE (MHC class I antigen A*68) (Aw-68) (A-28). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*6802). RX MEDLINE=87252273; PubMed=3496393; RA Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.; RT "Multiple genetic mechanisms have contributed to the generation of the RT HLA-A2/A28 family of class I MHC molecules."; RL J. Immunol. 139:936-941(1987). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*6802). RA Domena J.D.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*6803). RX MEDLINE=97045039; PubMed=8881043; DOI=10.1007/s002510050172; RA Ellexson M., Lau M., Terasaki P., Hildebrand W.H.; RT "Molecular characterization of HLA-A*6803."; RL Immunogenetics 45:78-79(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*6808). RX MEDLINE=99321037; PubMed=10395114; RX DOI=10.1034/j.1399-0039.1999.530614.x; RA Cox S.T., Arguello J.R., Marsh S.G.E., Boham E., Lau M., Kwan P.L., RA Madrigal J.A., Little A.-M.; RT "Sequence of HLA-A*6808."; RL Tissue Antigens 53:597-600(1999). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELE A*68011). RC TISSUE=Blood; RA Cox S.T.; RT "Confirmation of HLA-A*68011."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*6817). RX MEDLINE=20340076; PubMed=10885567; RX DOI=10.1034/j.1399-0039.2000.550509.x; RA Ramon D., Scott I., Cox S.T., Pesoa S., Vullo C., Little A.M., RA Madrigal J.A.; RT "HLA-A*6817, identified in the Kolla Amerindians of north-west RT Argentina possesses a novel nucleotide substitution."; RL Tissue Antigens 55:453-454(2000). RN [7] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*6806). RA Bei M., Hurley C.K.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE A*6803). RC TISSUE=Blood; RX MEDLINE=97419180; PubMed=9271640; DOI=10.1007/s002510050304; RA Vargas-Alarcon G., Martinez-Laso J., Gomez-Casado E., Perez-Blas M., RA Granados J., Alegre R., Alvarez M., Zuniga J., Arnaiz-Villena A.; RT "Description of HLA-A*6803 and A*68N in Mazatecan Indians from RT Mexico."; RL Immunogenetics 46:446-447(1997). RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*6803). RC TISSUE=Blood; RA Blasczyk R.; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*6802). RA Edson S.M., Hurley C.K.; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*6809 AND A*6810). RX MEDLINE=20309230; PubMed=10852390; RX DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-206 (ALLELE A*6816). RX MEDLINE=20260982; PubMed=10803837; DOI=10.1007/s002510050618; RA Gomez-Casado E., Martinez-Laso J., Gonzalez-Hevilla M., Longas J., RA Rubio I., Silvera-Redondo C., Garcia-Gomez A., Lowy E., RA Arnaiz-Villena A.; RT "A novel HLA-A*6816 allele possible generated by a point mutation in a RT Chilean from Punta Arenas (Magellan Strait)."; RL Immunogenetics 51:257-260(2000). RN [13] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*6807 AND A*6817). RX MEDLINE=21160440; PubMed=11260503; RX DOI=10.1034/j.1399-0039.2001.057002095.x; RA Hickman H.D., Cavett J.W., Ellexson-Turner M.E., Sparkman J.N., RA Bennett T.T., Turner S., Sidebottom D.A., Trachtenberg E.A., RA Confer D.L., Hildebrand W.H.; RT "Non-conservative substitutions distinguish previously uncharacterized RT HLA-A molecules."; RL Tissue Antigens 57:95-102(2001). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-297 (ALLELE A*6801). RX MEDLINE=86055720; PubMed=3877632; RA Holmes N., Parham P.; RT "Exon shuffling in vivo can generate novel HLA class I molecules."; RL EMBO J. 4:2849-2854(1985). RN [15] RP PARTIAL PROTEIN SEQUENCE OF 25-294 (A*6801). RX MEDLINE=82247941; PubMed=6179086; RA Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.; RT "Structure of crossreactive human histocompatibility antigens HLA-A28 RT and HLA-A2: possible implications for the generation of HLA RT polymorphism."; RL Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (A*6801). RX MEDLINE=93078854; PubMed=1448153; DOI=10.1038/360364a0; RA Guo H.-C., Jardetzky T.S., Garrett T.P.J., Lane W.S., Strominger J.L., RA Wiley D.C.; RT "Different length peptides bind to HLA-Aw68 similarly at their ends RT but bulge out in the middle."; RL Nature 360:364-366(1992). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (A*6801). RX MEDLINE=93078855; PubMed=1448154; DOI=10.1038/360367a0; RA Silver M.L., Guo H.-C., Strominger J.L., Wiley D.C.; RT "Atomic structure of a human MHC molecule presenting an influenza RT virus peptide."; RL Nature 360:367-369(1992). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-199 (A*6801). RX MEDLINE=95166800; PubMed=7862664; RA Collins E.J., Garboczi D.N., Karpusas M.N., Wiley D.C.; RT "The three-dimensional structure of a class I major histocompatibility RT complex molecule missing the alpha 3 domain of the heavy chain."; RL Proc. Natl. Acad. Sci. U.S.A. 92:1218-1221(1995). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-68 are known: A*6801 CC (Aw68.1), A*6802, A*6803. A*6804, A*6805, A*6806, A*6807, A*6808, CC A*6809, A*6810, A*6816 and A*6817. The sequence shown is that of CC A*6801. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; U03861; AAA03602.1; -; Unassigned_DNA. DR EMBL; X03070; CAB56605.1; -; Genomic_DNA. DR EMBL; X03071; CAB56606.1; -; Genomic_DNA. DR EMBL; U41057; AAB41292.1; -; mRNA. DR EMBL; AJ315642; CAC44382.1; -; Genomic_DNA. DR EMBL; AF144013; AAF74211.1; -; Genomic_DNA. DR EMBL; AJ245567; CAB59722.1; -; Genomic_DNA. DR EMBL; U91628; AAB50567.1; -; Genomic_DNA. DR EMBL; U91627; AAB50567.1; JOINED; Genomic_DNA. DR EMBL; U89946; AAB82079.1; -; Genomic_DNA. DR EMBL; U89947; AAB82080.1; -; Genomic_DNA. DR EMBL; AJ001274; CAA04647.1; -; mRNA. DR EMBL; AF072770; AAC25782.1; -; Genomic_DNA. DR EMBL; AF072769; AAC25782.1; JOINED; Genomic_DNA. DR EMBL; AF135545; AAD22270.1; -; Genomic_DNA. DR EMBL; AF135544; AAD22270.1; JOINED; Genomic_DNA. DR EMBL; AF108431; AAD27539.1; -; Genomic_DNA. DR EMBL; AF108430; AAD27539.1; JOINED; Genomic_DNA. DR EMBL; AJ223972; CAA11708.1; -; Genomic_DNA. DR EMBL; AF041372; AAD02208.1; -; Genomic_DNA. DR EMBL; AF041371; AAD02208.1; JOINED; Genomic_DNA. DR EMBL; AF268398; AAF73477.1; -; Genomic_DNA. DR EMBL; AF268397; AAF73477.1; JOINED; Genomic_DNA. DR UniGene; Hs.181244; -. DR PDB; 1HSB; X-ray; A=25-294. DR PDB; 1TMC; X-ray; A=25-199. DR PDB; 2HLA; X-ray; A=25-294. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR LinkHub; P01891; -. DR ArrayExpress; P01891; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Direct protein sequencing; Glycoprotein; KW Host-virus interaction; Immune response; Membrane; MHC I; KW Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-68 alpha chain. FT /FTId=PRO_0000018830. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 36 36 V -> M (in allele A*6802). FT /FTId=VAR_004389. FT VARIANT 86 87 RN -> EE (in allele A*6810). FT /FTId=VAR_010362. FT VARIANT 94 94 Q -> H (in allele A*6803, allele A*6804 FT and allele A*6805). FT /FTId=VAR_010363. FT VARIANT 97 97 T -> I (in allele A*6804). FT /FTId=VAR_010364. FT VARIANT 98 98 D -> H (in allele A*6805). FT /FTId=VAR_010365. FT VARIANT 121 121 M -> R (in allele A*6802). FT /FTId=VAR_004390. FT VARIANT 129 129 S -> P (in allele A*6802). FT /FTId=VAR_004391. FT VARIANT 138 138 R -> E (in allele A*6806; requires 2 FT nucleotide substitutions). FT /FTId=VAR_010366. FT VARIANT 138 138 R -> H (in allele A*6802). FT /FTId=VAR_004392. FT VARIANT 140 140 D -> H (in allele A*6806 and allele FT A*6807). FT /FTId=VAR_010367. FT VARIANT 140 140 D -> V (in allele A*6817). FT /FTId=VAR_010368. FT VARIANT 140 140 D -> Y (in allele A*6802). FT /FTId=VAR_004393. FT VARIANT 175 175 H -> L (in allele A*6816). FT /FTId=VAR_010369. FT VARIANT 180 180 W -> L (in allele A*6808). FT /FTId=VAR_010370. FT VARIANT 180 180 W -> Q (in allele A*6809; requires 2 FT nucleotide substitutions). FT /FTId=VAR_010371. FT CONFLICT 206 206 T -> A (in Ref. 12). FT CONFLICT 231 231 S -> G (in Ref. 15). FT STRAND 27 36 FT TURN 39 40 FT STRAND 41 43 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 235 FT STRAND 238 243 FT TURN 244 245 FT STRAND 246 248 FT TURN 250 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 290 292 SQ SEQUENCE 365 AA; 40909 MW; 78539C59DB8B1DFC CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ MMYGCDVGSD GRFLRGYRQD AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQW RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWVA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A69_HUMAN Reviewed; 365 AA. AC P10316; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 2. DT 20-FEB-2007, entry version 66. DE HLA class I histocompatibility antigen, A-69 alpha chain (MHC class I DE antigen A*69) (Aw-69) (A-28). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELE A*6901). RX MEDLINE=86055720; PubMed=3877632; RA Holmes N., Parham P.; RT "Exon shuffling in vivo can generate novel HLA class I molecules."; RL EMBO J. 4:2849-2854(1985). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The only allele of A-69 known is A*6901 which is CC shown here. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X03158; CAB56607.1; -; Genomic_DNA. DR EMBL; X03159; CAB56608.1; -; Genomic_DNA. DR PIR; B24671; HLHU69. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; P10316; 1-273. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P10316; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Gene3D; G3DSA:3.30.500.10; G3DSA:3.30.500.10; 1. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; MHC I; KW Ubl conjugation. FT CHAIN 1 365 HLA class I histocompatibility antigen, FT A-69 alpha chain. FT /FTId=PRO_0000080740. FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1 (By similarity). FT REGION 115 206 Alpha-2 (By similarity). FT REGION 207 298 Alpha-3 (By similarity). FT REGION 299 308 Connecting peptide (By similarity). FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40977 MW; 050F1B01157EFDF6 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTVQ RMYGCDVGSD WRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A74_HUMAN Reviewed; 365 AA. AC P30459; O19647; O43906; O46874; Q95IZ5; Q9UIN1; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 23-JAN-2007, entry version 60. DE HLA class I histocompatibility antigen, A-74 alpha chain precursor DE (MHC class I antigen A*74) (Aw-74) (Aw-19). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*7401). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*7401). RA Hurley C.; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-206 (ALLELES A*7402 AND A*7403). RC TISSUE=Blood; RX MEDLINE=97051454; PubMed=8896180; RA Blasczyk R., Wehling J., Onaldi-Mohr D., Rebmann V., RA Chandanayingyong D., Grosse-Wilde H.; RT "Structural definition of the A*74 group: implications for matching in RT bone marrow transplantation with alternative donors."; RL Tissue Antigens 48:205-209(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-206 (ALLELE A*7404). RX MEDLINE=21108617; PubMed=11169261; RX DOI=10.1034/j.1399-0039.2001.057001070.x; RA Cox S.T., Mcwhinnie A.J., Koester R.P., Heine U., Holman R., RA Madrigal A.J., Little A.-M.; RT "Further diversity at HLA-A and -B loci identified in Afro-Caribbean RT potential bone marrow donors."; RL Tissue Antigens 57:70-72(2001). RN [5] RP NUCLEOTIDE SEQUENCE OF 25-206 (ALLELE A*7405). RX MEDLINE=21160440; PubMed=11260503; RX DOI=10.1034/j.1399-0039.2001.057002095.x; RA Hickman H.D., Cavett J.W., Ellexson-Turner M.E., Sparkman J.N., RA Bennett T.T., Turner S., Sidebottom D.A., Trachtenberg E.A., RA Confer D.L., Hildebrand W.H.; RT "Non-conservative substitutions distinguish previously uncharacterized RT HLA-A molecules."; RL Tissue Antigens 57:95-102(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-74 are known: A*7401 CC A*7402, A*7403, A*7404 and A*7405. The sequence shown is that of CC A*7401. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X61701; CAA43870.1; -; mRNA. DR EMBL; U17569; AAA56779.1; -; mRNA. DR EMBL; U17570; AAA56780.1; -; mRNA. DR EMBL; AJ223060; CAA11063.1; -; mRNA. DR EMBL; AJ002678; CAA05681.1; -; mRNA. DR EMBL; AJ249370; CAB58124.1; -; Genomic_DNA. DR EMBL; AF255721; AAK49188.1; -; Genomic_DNA. DR EMBL; AF255720; AAK49188.1; JOINED; Genomic_DNA. DR PIR; I37482; I37482. DR HSSP; P10315; 1HSB. DR SMR; P30459; 25-299. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; P30459; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-74 alpha chain. FT /FTId=PRO_0000018831. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 23 23 R -> W (in allele A*7402). FT /FTId=VAR_010375. FT VARIANT 86 86 Q -> G (in allele A*7404; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016612. FT VARIANT 90 90 N -> K (in allele A*7404). FT /FTId=VAR_016613. FT VARIANT 97 97 T -> A (in allele A*7405). FT /FTId=VAR_016614. FT VARIANT 103 103 G -> A (in allele A*7403). FT /FTId=VAR_016615. SQ SEQUENCE 365 AA; 40891 MW; C94BF2569A852371 CRC64; MAVMAPRTLL LLLLGALALT QTRAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAHSQTDRV DLGTLRGYYN QSEAGSHTIQ MMYGCDVGPD GRLLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA MFAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A80_HUMAN Reviewed; 365 AA. AC Q09160; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-FEB-2007, entry version 56. DE HLA class I histocompatibility antigen, A-80 alpha chain precursor DE (MHC class I antigen A*80) (Aw-80) (A-1). GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*8001). RX MEDLINE=94245293; PubMed=8188325; DOI=10.1007/BF00176169; RA Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.; RT "Characterization of a new and highly distinguishable HLA-A allele in RT a Spanish family."; RL Immunogenetics 39:452-452(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*8001). RX PubMed=8284791; RA Domena J.D., Hildebrand W.H., Bias W.B., Parham P.; RT "A sixth family of HLA-A alleles defined by HLA-A*8001."; RL Tissue Antigens 42:156-159(1993). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The only allele of A-80 known is A*8001 which is CC shown here. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; U03754; AAC04322.1; -; mRNA. DR EMBL; L18898; AAA17012.1; -; mRNA. DR PIR; I59638; I38439. DR UniGene; Hs.181244; -. DR HSSP; P10315; 1HSB. DR SMR; Q09160; 25-298. DR Ensembl; ENSG00000197499; Homo sapiens. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR ArrayExpress; Q09160; -. DR GermOnline; ENSG00000204632; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-80 alpha chain. FT /FTId=PRO_0000018832. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40792 MW; CE1BC1CD60CA8FA8 CRC64; MAVMPPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDSQFVQF DSDAASQRME PRAPWIEQEE PEYWDEETRN VKAHSQTNRA NLGTLRGYYN QSEDGSHTIQ IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAARRAEQL RAYLEGECVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGKEKR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IIAGLVLLGA VIAGAVVAAV MWRKKSSVRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1B01_GORGO Reviewed; 362 AA. AC P30379; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 44. DE Class I histocompatibility antigen, GOGO-B0101 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60255; CAA42807.1; -; mRNA. DR PIR; JH0539; JH0539. DR HSSP; Q29961; 1HSA. DR SMR; P30379; 25-300. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 362 Class I histocompatibility antigen, GOGO- FT B0101 alpha chain. FT /FTId=PRO_0000018901. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 362 AA; 40171 MW; 419EEE29817165A4 CRC64; MRVTAPRTLL LLLSAALALT ETWAGSHSMR YFDTAVSRPG RGEPRFITVG YVDDTQFVRF DSDAASPRME PRAPWIEQEG PEYWDRETQT SKAQAQTDRE NLRIALRYYN QSEAGSHTIQ RMFGCDVGPD GRLLRGYSQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRYLENGR ETLQRADTPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEER YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVTAV ICRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B01_PANTR Reviewed; 359 AA. AC P13750; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 31-OCT-2006, entry version 50. DE CHLA class I histocompatibility antigen, B-1 alpha chain precursor DE (Fragment). OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89030641; PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). RN [2] RP SEQUENCE REVISION. RA Mayer W.; RL Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X13115; CAA31507.1; -; mRNA. DR HSSP; Q29961; 1HSA. DR SMR; P13750; 21-294. DR KEGG; ptr:450150; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL <1 20 FT CHAIN 21 359 CHLA class I histocompatibility antigen, FT B-1 alpha chain. FT /FTId=PRO_0000018916. FT TOPO_DOM 21 305 Extracellular (Potential). FT TRANSMEM 306 329 Potential. FT TOPO_DOM 330 359 Cytoplasmic (Potential). FT DOMAIN 205 291 Ig-like C1-type. FT REGION 21 110 Alpha-1. FT REGION 111 202 Alpha-2. FT REGION 203 294 Alpha-3. FT REGION 295 305 Connecting peptide. FT CARBOHYD 106 106 N-linked (GlcNAc...) (By similarity). FT DISULFID 121 184 By similarity. FT DISULFID 223 279 By similarity. FT NON_TER 1 1 SQ SEQUENCE 359 AA; 40174 MW; 858ACBAF74D6829D CRC64; APRTVLLLLS AALALTETWA GSHSMRYFYT SVSRPGRGEP RFITVGYVDD TQFVRFDSDA ASPRMEPRAP WIEQEGPEYW DRETRNMKAS AQTDRENLRI ALRYYNQSEA GSHTWQTMYG CDMGPDGRLL RGYGQYAYDG KDYIALNEDL SSWTAADTAA QITQRKWEAA REAEQRRAYL EGTCVEWLRR YLENGKETLQ RADPPKTHVT HHPISDHEAT LRCWALGFYP AEITLTWQRD GEDQTQDTEL VETRPEGDRT FQKWAAVVVP SGEEQRYTCH VQHEGLPKPL TLRWEPSSQS TIPIVGIVAG LAVLVVTVAV VAVVAAVMCR RKSSGGKGGS YSQAASSDSA QGSDVSLTA // ID 1B01_SAGOE Reviewed; 365 AA. AC P30516; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 46. DE Class I histocompatibility antigen, B alpha chain precursor. OS Saguinus oedipus (Cotton-top tamarin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Saguinus. OX NCBI_TaxID=9490; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90111120; PubMed=2104912; RA Watkins D.I., Letvin N.L., Hughes A.L., Tedder T.F.; RT "Molecular cloning of cDNA that encode MHC class I molecules from a RT New World primate (Saguinus oedipus). Natural selection acts at RT positions that may affect peptide presentation to T cells."; RL J. Immunol. 144:1136-1143(1990). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M33476; AAA36952.1; ALT_INIT; mRNA. DR PIR; I72217; I72217. DR HSSP; P30504; 1IM9. DR SMR; P30516; 25-298. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 365 Class I histocompatibility antigen, B FT alpha chain. FT /FTId=PRO_0000018921. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40999 MW; B79A9E1FE54C5634 CRC64; MTVMAPRTLL LLLSGALVLT ETWAGSHSMR YFSTAVSRPG REEPRYIEVG YVDDTQFVRF DSDAASPRME PRAQWVEKEG REYWEEETQR AKAFAQTFRV NLQTALGYYN QSEAGSHTIQ MMSGCDLGPD GRLLRGYDQH AYDGKDYISL NEDLRSWTAA DVAAQITQRK WEAANEAERT RAYLEGTCVE WLHRYLENGK ETLQRAEPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DMELVETRPT GNGTFQKWAA VVVLSGEEHR YTCHVQHEGL PEPLTLRWEP PSQPTIPIMG IVAILAILGA VVTGAVVTAV MWRKKSSDKK GGSYSQAARS DSAQGSDVSL TACKV // ID 1B02_GORGO Reviewed; 362 AA. AC P30380; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 44. DE Class I histocompatibility antigen, GOGO-B0102 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60693; CAA43101.1; -; mRNA. DR PIR; JH0540; JH0540. DR HSSP; Q29961; 1HSA. DR SMR; P30380; 25-300. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 362 Class I histocompatibility antigen, GOGO- FT B0102 alpha chain. FT /FTId=PRO_0000018902. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 362 AA; 40205 MW; E19EEE2B7CC7BECD CRC64; MRVTAPRTLL LLLSAALALT ETWAGSHSMR YFDTAVSRPG RGEPRFITVG YVDDTQFVRF DSDAASPRME PRAPWIEQEG PEYWDRETQT SKAQAQTDRE NLRIALRYYN QSEAGSHTFQ RMFGCDVGPD GRLLRGYSQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRYLENGR ETLQRADTPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEER YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVTAV ICRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B02_PANTR Reviewed; 362 AA. AC P13751; Q9MXK0; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 31-OCT-2006, entry version 51. DE CHLA class I histocompatibility antigen, B-2 alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89030641; PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). RN [2] RP SEQUENCE REVISION. RA Mayer W.; RL Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RX MEDLINE=20322475; PubMed=10866106; DOI=10.1007/s002510050638; RA de Groot N.G., Otting N., Arguello R., Watkins D.I., Doxiadis G.G., RA Madrigal J.A., Bontrop R.E.; RT "Major histocompatibility complex class I diversity in a West African RT chimpanzee population: implications for HIV research."; RL Immunogenetics 51:398-409(2000). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X13116; CAA31508.1; -; mRNA. DR EMBL; AF168411; AAF72792.2; -; mRNA. DR PIR; S03538; S03538. DR HSSP; P30474; 1A9E. DR SMR; P13751; 25-300. DR KEGG; ptr:450202; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 FT CHAIN 25 362 CHLA class I histocompatibility antigen, FT B-2 alpha chain. FT /FTId=PRO_0000018917. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 362 AA; 40488 MW; FFDB2991044DAA83 CRC64; MQVTAPRTVL LLLSAALALT ETWAGSHSMK YFYTAVSRPG RGEPRFISVG YVDDTQFVWF DSDAASPREE PRAPWIEQEG PEYWDRETQI SKTNAQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDMGPD GRLLRGYEQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARWAEQL RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B03_GORGO Reviewed; 362 AA. AC P30381; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 44. DE Class I histocompatibility antigen, GOGO-B0103 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60254; CAA42806.1; -; mRNA. DR PIR; JH0541; JH0541. DR HSSP; Q29961; 1HSA. DR SMR; P30381; 25-300. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 362 Class I histocompatibility antigen, GOGO- FT B0103 alpha chain. FT /FTId=PRO_0000018903. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 362 AA; 40249 MW; 3DEE82572BD81469 CRC64; MRVTAPRTLL LLLSAALALT ETWAGSHSMR YFDTAVSRPG RGEPRFITVG YVDDTQFVRF DSDAASPRME PRAPWIEQEG PEYWDRETQT SKAQAQTDRE NLRIALRYYN QSEAGSHTIQ WMYGCDMGPD GRLLRGYSQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRYLENGR ETLQRADTPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEER YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVTAV ICRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B04_GORGO Reviewed; 363 AA. AC P30382; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 46. DE Class I histocompatibility antigen, GOGO-B0201 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60253; CAA42805.1; -; mRNA. DR PIR; JH0542; JH0542. DR HSSP; P30474; 1A9E. DR SMR; P30382; 25-300. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 363 Class I histocompatibility antigen, GOGO- FT B0201 alpha chain. FT /FTId=PRO_0000018904. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 363 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 363 AA; 40439 MW; A8CA366ED9A2B264 CRC64; MQVTAPRTLL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTQFVWF DSDAASPRKE PRTPWIEQEG PEYWDRETQI SKTNTQTYRV GLGTLRGYYN QSEDGSHTIQ RMYGCDMGPD GRLLRGYSQL AYDGKDYLAL NEDLSSWTAA DTAAQITQRK WEAARAAEQE RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCRVQHEGL PEPLTLRWEP SSQSTIPIVG IVAGLAVLVV TVAVVAVVAA VMCRRKSSGG KGGSYSQAAS SDSAQGSDVS LTA // ID 1B07_HUMAN Reviewed; 362 AA. AC P01889; Q29638; Q29681; Q29854; Q29861; Q31613; Q9GIX1; Q9TP95; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 3. DT 20-FEB-2007, entry version 76. DE HLA class I histocompatibility antigen, B-7 alpha chain precursor (MHC DE class I antigen B*7). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*0702). RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*0702). RX MEDLINE=90315860; PubMed=2700944; RA Parham P., Benjamin R.J., Chen B.P., Clayberger C., Ennis P.D., RA Krensky A.M., Lawlor D.A., Littman D.R., Norment A.M., Orr H.T., RA Salter R.D., Zemmour J.; RT "Diversity of class I HLA molecules: functional and evolutionary RT interactions with T cells."; RL Cold Spring Harb. Symp. Quant. Biol. 54:529-543(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*0702). RX MEDLINE=85287366; PubMed=2993161; RA Sood A.K., Pan J., Biro P.A., Pereira D., Srivastava R., Reddy V.B., RA Duceman B.W., Weissman S.M.; RT "Structure and polymorphism of class I MHC antigen mRNA."; RL Immunogenetics 22:101-121(1985). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*0702). RA Ellexson M.E., Zhang L., Hildebrand W.H.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*0703). RX MEDLINE=94148707; PubMed=8106270; DOI=10.1016/0198-8859(93)90533-7; RA Bergmans A., Tijssen H., Lardy J., Reekers P.; RT "Complete nucleotide sequence of HLA-B*0703, a B7-variant (BPOT)."; RL Hum. Immunol. 38:159-162(1993). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*0704). RX MEDLINE=95381233; PubMed=7652739; RA Kubens B.S., Arnett K.L., Adams E.J., Parham P., Grosse-Wilde H.; RT "Definition of a new HLA-B7 subtype (B*0704) by isoelectric focusing, RT family studies and DNA sequence analysis."; RL Tissue Antigens 45:322-327(1995). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*0705). RX MEDLINE=95184211; PubMed=7878658; RA Arnett K.L., Adams E.J., Domena J.D., Parham P.; RT "Structure of a novel subtype of B7 (B*0705) isolated from a Chinese RT individual."; RL Tissue Antigens 44:318-321(1994). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*0703 AND B*0705). RX MEDLINE=96128250; PubMed=8537119; RA Smith K.D., Epperson D.F., Lutz C.T.; RT "Alloreactive cytotoxic T-lymphocyte-defined HLA-B7 subtypes differ in RT peptide antigen presentation."; RL Immunogenetics 43:27-37(1996). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*0706). RX MEDLINE=96369317; PubMed=8773323; RA Sanz L., Vilches C., de Pablo R., Bunce M., Moreno M.E., Kreisler M.; RT "Haplotypic association of two new HLA class I alleles: Cw*15052 and RT B*0706: evolutionary relationships of HLA-Cw*15 alleles."; RL Tissue Antigens 47:329-332(1996). RN [10] RP NUCLEOTIDE SEQUENCE (ALLELE B*0718). RA Bettinotti M.P., Hadzikadic L., Dhillon G., Barracchini K., RA Marincola F.M.; RT "A new HLA-B allele."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE (ALLELE B*0702). RA Marsh S.G.E.; RT "Intron sequences of HLA class I."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE (ALLELE B*0702). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*0724). RC TISSUE=Peripheral blood; RX MEDLINE=21442086; PubMed=11556973; RX DOI=10.1034/j.1399-0039.2001.057005471.x; RA Middleton D., Curran M.D., Anholts J.D., Reilly E.R., Schreuder G.M.; RT "Characterisation of a new HLA-B allele, HLA-B*0724."; RL Tissue Antigens 57:471-473(2001). RN [14] RP PROTEIN SEQUENCE OF 25-295 (B*0702). RX MEDLINE=80088278; PubMed=518865; DOI=10.1021/bi00592a030; RA Orr H.T., Lopez de Castro J.A., Lancet D., Strominger J.L.; RT "Complete amino acid sequence of a papain-solubilized human RT histocompatibility antigen, HLA-B7. 2. Sequence determination and RT search for homologies."; RL Biochemistry 18:5711-5720(1979). RN [15] RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I. RX PubMed=11390610; DOI=10.1128/JVI.75.13.6086-6094.2001; RA Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L., RA Mulloy J.C., Jacobson S., Franchini G.; RT "Free major histocompatibility complex class I heavy chain is RT preferentially targeted for degradation by human T-cell RT leukemia/lymphotropic virus type 1 p12(I) protein."; RL J. Virol. 75:6086-6094(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). Interacts with HTLV-1 accessory protein p12I. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-7 are known: B*0702 CC (B7.2), B*0703 (BPOT), B*0704, B*0705, B*0706 (B7_L79), B*0718 and CC B*0724. The sequence shown is B*0702. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M32317; AAA36230.1; -; mRNA. DR EMBL; M16102; AAA59622.1; ALT_SEQ; mRNA. DR EMBL; U29057; AAA91229.1; -; mRNA. DR EMBL; X64454; CAA45785.1; -; mRNA. DR EMBL; U04245; AAA87398.1; -; mRNA. DR EMBL; L33922; AAA65639.1; -; mRNA. DR EMBL; U21052; AAA92563.1; -; mRNA. DR EMBL; U21053; AAA92564.1; -; mRNA. DR EMBL; X91749; CAA62864.1; -; mRNA. DR EMBL; AF189017; AAF01052.1; -; mRNA. DR EMBL; AJ309047; CAC35468.1; -; Genomic_DNA. DR EMBL; AJ292075; CAC33440.1; -; Genomic_DNA. DR EMBL; AJ401222; CAC10402.1; -; Genomic_DNA. DR PIR; B35997; HLHUB7. DR PIR; I59651; I59651. DR PIR; S60601; S60601. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; Q29961; 1HSA. DR SMR; P01889; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR KEGG; hsa:3106; -. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR LinkHub; P01889; -. DR ArrayExpress; P01889; -. DR GermOnline; ENSG00000204523; Homo sapiens. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Direct protein sequencing; Glycoprotein; Host-virus interaction; KW Immune response; Membrane; MHC I; Polymorphism; Signal; Transmembrane; KW Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-7 alpha chain. FT /FTId=PRO_0000018833. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 93 95 AQA -> TNT (in allele B*0703). FT /FTId=VAR_016351. FT VARIANT 118 119 TL -> II (in allele B*0718). FT /FTId=VAR_016352. FT VARIANT 121 121 S -> R (in allele B*0718). FT /FTId=VAR_016353. FT VARIANT 138 138 D -> N (in allele B*0705 and allele FT B*0706). FT /FTId=VAR_016354. FT VARIANT 180 180 R -> D (in allele B*0704; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016355. FT VARIANT 187 187 E -> L (in allele B*0724; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016616. FT VARIANT 306 306 V -> I (in allele B*0705). FT /FTId=VAR_016356. FT CONFLICT 15 18 AALA -> GPW (in Ref. 3). FT CONFLICT 266 266 Q -> E (in Ref. 14). FT CONFLICT 268 268 W -> S (in Ref. 3). FT CONFLICT 297 297 R -> G (in Ref. 3). FT CONFLICT 314 315 GL -> RP (in Ref. 3). SQ SEQUENCE 362 AA; 40460 MW; 5E5A7BDE031403D6 CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHDQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQR RAYLEGECVE WLRRYLENGK DKLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B08_HUMAN Reviewed; 362 AA. AC P30460; O62901; O95730; O98140; P79542; Q95369; Q95J00; Q9GJ20; AC Q9MY78; Q9MYF4; Q9TQH6; Q9TQM2; Q9UQT0; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 69. DE HLA class I histocompatibility antigen, B-8 alpha chain precursor (MHC DE class I antigen B*8). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*0801). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*0801). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE B*0801). RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*0804). RX MEDLINE=97473039; PubMed=9331954; RA Hoyer R.J., Bratlie A., Schreuder G.M., Hurley C.K.; RT "Characterization of a novel HLA-B allele, B*0804, in a Norwegian RT family."; RL Tissue Antigens 50:308-310(1997). RN [5] RP NUCLEOTIDE SEQUENCE OF 33-257 (ALLELE B*0804). RA Eberle M., Lorentzen D., Iwanaga K.K., Watkins D.I.; RT "Identification of a new HLA-B*08 variant, B*08NEW."; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*0806). RA Marcos C.Y., Lazaro A.M., Noreen H., Stastny P.; RT "New HLA-B locus allele."; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES B*0807 AND RP B*0809). RX MEDLINE=20236861; PubMed=10777103; RX DOI=10.1034/j.1399-0039.2000.550311.x; RA Kennedy C.T., Dodd R., Le T., Wallace R., Ng G., Greville W.D., RA Kennedy A., Taverniti A., Moses J.H., Clow N., Watson N., Dunckley H.; RT "Routine HLA-B genotyping with PCR-sequence-specific oligonucleotides RT (PCR-SSO) detects eight new alleles: B*0807, B*0809, B*1551, B*3529, RT B*3532, B*4025, B*5304 and B*5508."; RL Tissue Antigens 55:266-270(2000). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-206 (ALLELE B*0809). RX MEDLINE=20166355; PubMed=10703615; RX DOI=10.1034/j.1399-0039.2000.550115.x; RA Elsner H.A., Blasczyk R.; RT "Identification of the novel allele HLA-B*0809 in a Caucasian RT individual: estimation of allogeneic potential between B*08 RT variants."; RL Tissue Antigens 55:74-77(2000). RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES B*0809; B*0812; B*0813 AND RP B*0814). RX MEDLINE=21276061; PubMed=11380951; RX DOI=10.1034/j.1399-0039.2001.057004373.x; RA Steiner N.K., Gans C.P., Kosman C., Baldassarre L.A., Edson S., RA Jones P.F., Rizzuto G., Pimtanothai N., Koester R., Mitton W., Ng J., RA Hartzman R.J., Hurley C.K.; RT "Novel HLA-B alleles associated with antigens in the 8C CREG."; RL Tissue Antigens 57:373-375(2001). RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*0810). RA Day S.; RT "A new B*08 variant allele."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [11] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-300. RX MEDLINE=97130420; PubMed=8976183; DOI=10.1084/jem.184.6.2279; RA Reid S.W., McAdam S., Smith K.J., Klenerman P., O'Callaghan C.A., RA Harlos K., Jakobsen B.K., McMichael A.J., Bell J.I., Stuart D.I., RA Jones E.Y.; RT "Antagonist HIV-1 Gag peptides induce structural changes in HLA B8."; RL J. Exp. Med. 184:2279-2286(1996). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-8 are known: B*0801, CC B*0804, B*0806, B*0807 (B*NV), B*0809 (B*HM; B*08HO), B*0810, CC B*0812, B*0813 and B*0814. The sequence shown is B*0801. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24036; AAA52662.1; -; Genomic_DNA. DR EMBL; AJ295294; CAC18876.1; -; Genomic_DNA. DR EMBL; BA000025; BAB63309.1; -; Genomic_DNA. DR EMBL; U67331; AAB07726.1; -; Genomic_DNA. DR EMBL; U67330; AAB07726.1; JOINED; Genomic_DNA. DR EMBL; U74386; AAB41720.1; -; mRNA. DR EMBL; AF056484; AAC14124.1; -; Genomic_DNA. DR EMBL; AF056483; AAC14124.1; JOINED; Genomic_DNA. DR EMBL; AF105226; AAD05244.1; -; Genomic_DNA. DR EMBL; AF127248; AAD31431.1; -; Genomic_DNA. DR EMBL; AF127247; AAD31431.1; JOINED; Genomic_DNA. DR EMBL; AJ131853; CAA10522.1; -; Genomic_DNA. DR EMBL; AF102560; AAD28165.1; -; Genomic_DNA. DR EMBL; AF102559; AAD28165.1; JOINED; Genomic_DNA. DR EMBL; AF226151; AAF36681.1; -; Genomic_DNA. DR EMBL; AF226150; AAF36681.1; JOINED; Genomic_DNA. DR EMBL; AF279675; AAF81604.1; -; Genomic_DNA. DR EMBL; AF279674; AAF81604.1; JOINED; Genomic_DNA. DR EMBL; AF310145; AAG27470.1; -; Genomic_DNA. DR EMBL; AF310144; AAG27470.1; JOINED; Genomic_DNA. DR EMBL; AY016212; AAK38401.1; -; Genomic_DNA. DR EMBL; AY016211; AAK38401.1; JOINED; Genomic_DNA. DR EMBL; AJ133101; CAB38945.1; -; Genomic_DNA. DR EMBL; AJ133102; CAB38945.1; JOINED; Genomic_DNA. DR PIR; I84431; I84431. DR UniGene; Hs.549053; -. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR PDB; 1AGB; X-ray; A=25-300. DR PDB; 1AGC; X-ray; A=25-300. DR PDB; 1AGD; X-ray; A=25-300. DR PDB; 1AGE; X-ray; A=25-300. DR PDB; 1AGF; X-ray; A=25-300. DR PDB; 1M05; X-ray; A/C=25-301. DR PDB; 1MI5; X-ray; A=25-301. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR LinkHub; P30460; -. DR RZPD-ProtExp; IOH11225; -. DR RZPD-ProtExp; IOH42052; -. DR RZPD-ProtExp; T1025; -. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-8 alpha chain. FT /FTId=PRO_0000018834. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 87 87 N -> D (in allele B*0810). FT /FTId=VAR_016502. FT VARIANT 91 91 F -> S (in allele B*0804). FT /FTId=VAR_016503. FT VARIANT 101 101 S -> N (in allele B*0806). FT /FTId=VAR_016504. FT VARIANT 119 119 L -> W (in allele B*0809). FT /FTId=VAR_016505. FT VARIANT 121 121 S -> R (in allele B*0812). FT /FTId=VAR_016506. FT VARIANT 121 121 S -> T (in allele B*0809). FT /FTId=VAR_016507. FT VARIANT 137 138 HN -> YH (in allele B*0814). FT /FTId=VAR_016519. FT VARIANT 138 138 N -> D (in allele B*0807). FT /FTId=VAR_016508. FT VARIANT 140 140 Y -> D (in allele B*0814). FT /FTId=VAR_016520. FT VARIANT 176 176 V -> E (in allele B*0806). FT /FTId=VAR_016509. FT VARIANT 180 180 D -> L (in allele B*0813; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016510. FT VARIANT 180 180 D -> R (in allele B*0806; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016511. FT STRAND 27 36 FT TURN 39 40 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT STRAND 70 73 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 174 FT TURN 175 175 FT HELIX 177 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT TURN 244 245 FT HELIX 249 251 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40331 MW; 9B2A9760021680DF CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFDTAMSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI FKTNTQTDRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQD RAYLEGTCVE WLRRYLENGK DTLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B13_HUMAN Reviewed; 362 AA. AC P30461; O02956; O78180; Q29661; Q29933; Q9GIY5; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 58. DE HLA class I histocompatibility antigen, B-13 alpha chain precursor DE (MHC class I antigen B*13). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*1302). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*1302). RX MEDLINE=88152906; PubMed=3257938; RA Zemmour J., Ennis P.D., Parham P., Dupont B.; RT "Comparison of the structure of HLA-Bw47 to HLA-B13 and its RT relationship to 21-hydroxylase deficiency."; RL Immunogenetics 27:281-287(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*1301). RX MEDLINE=89122134; PubMed=2914710; RA Kato K., Dupont B., Yang S.Y.; RT "Localization of nucleotide sequence which determines Mongoloid RT subtype of HLA-B13."; RL Immunogenetics 29:117-120(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*1301 AND B*1302). RC TISSUE=Blood; RX MEDLINE=96053518; PubMed=7558929; DOI=10.1016/0198-8859(94)00120-F; RA Lin L., Tokunaga K., Nakajima F., Ishikawa Y., Kashiwase K., RA Tanaka H., Kuwata S., Sideltseva E., Akaza T., Tadokoro K., RA Shibata Y., Chandanayingyong D., Juji T.; RT "Both HLA-B*1301 and B*1302 exist in Asian populations and are RT associated with different haplotypes."; RL Hum. Immunol. 43:51-56(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*1303). RC TISSUE=Blood; RX MEDLINE=96232969; PubMed=8655357; DOI=10.1016/0198-8859(95)00143-3; RA Balas A., Garcia-Sanchez F., Vicario J.L.; RT "HLA-B*1303: a new example of poor correlation between serology and RT structure."; RL Hum. Immunol. 45:32-36(1996). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*1304). RX MEDLINE=97469330; PubMed=9328792; DOI=10.1016/S0198-8859(97)00055-4; RA Ellexson M., Lai-Kwan P., Lau M., Muto K., Terasaki P., Cole J., RA Thompson C., Hildebrand W.H.; RT "Polymorphism at codons 114, 116, 145, and 163 muddle the typing of RT HLA-B1304."; RL Hum. Immunol. 55:66-73(1997). RN [7] RP NUCLEOTIDE SEQUENCE (ALLELE B*1308). RA Carter V., Dunn P.P.; RT "Identification of a HLA-B*13 null allele."; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-13 are known: B*1301 CC (B13.1), B*1302 (B13.2), B*1304 and B*1308. The sequence shown is CC that of B*1302. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24041; AAA59660.1; -; Genomic_DNA. DR EMBL; M19757; AAA52657.1; -; Genomic_DNA. DR EMBL; M24075; AAA59627.1; -; Genomic_DNA. DR EMBL; D50290; BAA08821.1; -; mRNA. DR EMBL; D50291; BAA08822.1; -; mRNA. DR EMBL; U14943; AAB06829.1; -; mRNA. DR EMBL; U75533; AAC31793.1; -; mRNA. DR EMBL; AJ295279; CAC17137.1; -; Genomic_DNA. DR PIR; A45850; A45850. DR PIR; I54442; I54442. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P18464; 1E27. DR SMR; P30461; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-13 alpha chain. FT /FTId=PRO_0000018835. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 118 119 TW -> II (in allele B*1301). FT /FTId=VAR_016357. FT VARIANT 121 121 T -> R (in allele B*1301). FT /FTId=VAR_016358. FT VARIANT 138 138 N -> D (in allele B*1304). FT /FTId=VAR_016360. FT VARIANT 140 140 L -> S (in allele B*1304). FT /FTId=VAR_016361. FT VARIANT 169 169 L -> R (in allele B*1303 and allele FT B*1304; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016362. FT VARIANT 183 183 Y -> C (in allele B*1308). FT /FTId=VAR_016359. FT VARIANT 187 187 E -> L (in allele B*1303 and allele FT B*1304). FT /FTId=VAR_016363. SQ SEQUENCE 362 AA; 40474 MW; 28FF66B20961C75C CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFITVG YVDDTQFVRF DSDATSPRMA PRAPWIEQEG PEYWDRETQI SKTNTQTYRE NLRTALRYYN QSEAGSHTWQ TMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQLK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B14_HUMAN Reviewed; 362 AA. AC P30462; O02862; P30463; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 57. DE HLA class I histocompatibility antigen, B-14 alpha chain precursor DE (MHC class I antigen B*14). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES B*1401 AND B*1402). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*1402). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*1403). RX MEDLINE=20548605; PubMed=11098929; RX DOI=10.1034/j.1399-0039.2000.560401.x; RA Ellis J.M., Mack S.J., Leke R.F.G., Quakyi I., Johnson A.H., RA Hurley C.K.; RT "Diversity is demonstrated in class I HLA-A and HLA-B alleles in RT Cameroon, Africa: description of HLA-A*03012, *2612, *3006 and HLA- RT B*1403, *4016, *4703."; RL Tissue Antigens 56:291-302(2000). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-14 are known: B*1401 (Bw- CC 64; B-64), B*1402 (Bw-65, B-65) and B*1403. The sequence shown is CC that of B*1401. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24040; AAA59661.1; -; Genomic_DNA. DR EMBL; M24032; AAA59664.1; -; Genomic_DNA. DR EMBL; AJ301657; CAC20461.1; -; Genomic_DNA. DR EMBL; U91331; AAB61335.1; -; Genomic_DNA. DR EMBL; U91330; AAB61335.1; JOINED; Genomic_DNA. DR PIR; I61859; I61859. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P30474; 1A9E. DR SMR; P30462; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; IOH11225; -. DR RZPD-ProtExp; IOH42052; -. DR RZPD-ProtExp; T1025; -. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-14 alpha chain. FT /FTId=PRO_0000018836. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 35 35 S -> A (in allele B*1402 and allele FT B*1403). FT /FTId=VAR_016364. FT VARIANT 180 180 L -> R (in allele B*1403). FT /FTId=VAR_016654. SQ SEQUENCE 362 AA; 40358 MW; 9039122CC400337F CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI CKTNTQTDRE SLRNLRGYYN QSEAGSHTLQ WMYGCDVGPD GRLLRGYNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRHLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B15_HUMAN Reviewed; 362 AA. AC P30464; P30465; P30513; Q29633; Q29636; Q29829; Q29953; Q29982; AC Q95343; Q95344; Q9BD06; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 20-FEB-2007, entry version 63. DE HLA class I histocompatibility antigen, B-15 alpha chain precursor DE (MHC class I antigen B*15). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*1502). RX MEDLINE=92196792; PubMed=1801311; RA Little A.-M., Parham P.; RT "The HLA-Bw75 subtype of B15: molecular characterization and RT comparison with crossreacting antigens."; RL Tissue Antigens 38:186-190(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*1501; B*1511 AND B*1519). RX MEDLINE=94367483; PubMed=7521976; RA Hildebrand W.H., Domena J.D., Shen S.Y., Lau M., Terasaki P.I., RA Bunce M., Marsh S.G.E., Guttridge M.G., Bias W.B., Parham P.; RT "HLA-B15: a widespread and diverse family of HLA-B alleles."; RL Tissue Antigens 43:209-218(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*1501; B*1502 AND B*1511). RC TISSUE=Blood; RX MEDLINE=96369309; PubMed=8773315; RA Lin L., Tokunaga K., Tanaka H., Nakajima F., Imanishi T., RA Kashiwase K., Bannai M., Mizuno S., Akaza T., Tadokoro K., Shibata Y., RA Juji T.; RT "Further molecular diversity in the HLA-B15 group."; RL Tissue Antigens 47:265-274(1996). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*1503). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELE B*1504). RX MEDLINE=92269956; PubMed=1589035; DOI=10.1038/357329a0; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE B*1504). RC TISSUE=Blood; RA Ramos M., Barber D.F., Layrisse Z., de Castro J.A.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE (ALLELE B*1501). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [8] RP NUCLEOTIDE SEQUENCE (ALLELE B*1566). RX MEDLINE=22140958; PubMed=12144628; RX DOI=10.1034/j.1399-0039.2002.590511.x; RA Cox S.T., Prokupek B., Baker F., Holman R., Leung V.T., Wong A.S., RA Madrigal J.A., Little A.-M.; RT "Identification of HLA-B*1566."; RL Tissue Antigens 59:424-425(2002). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-362 (ALLELE B*1501). RX MEDLINE=89233295; PubMed=2714852; RA Pohla H., Kuon W., Tabaczewski P., Doerner C., Weiss E.H.; RT "Allelic variation in HLA-B and HLA-C sequences and the evolution of RT the HLA-B alleles."; RL Immunogenetics 29:297-307(1989). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-362 (ALLELE B*1501). RX MEDLINE=93138717; PubMed=8423049; RA Choo S.Y., Fan L.A., Hansen J.A.; RT "Allelic variations clustered in the antigen binding sites of HLA-Bw62 RT molecules."; RL Immunogenetics 37:108-113(1993). RN [11] RP ASSOCIATION OF ALLELE B*1502 WITH STEVENS-JOHNSON SYNDROME. RX PubMed=15057820; DOI=10.1038/428486a; RA Chung W.-H., Hung S.-I., Hong H.-S., Hsih M.-S., Yang L.-C., Ho H.-C., RA Wu J.-Y., Chen Y.-T.; RT "Medical genetics: a marker for Stevens-Johnson syndrome."; RL Nature 428:486-486(2004). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-15 are known: B*1501 (Bw- CC 62; B-62), B*1502 (Bw-75, B-75), B*1503 (Bw-72; B-72; B-70) CC B*1504, B*1511, B*1519 and B*1566. Allele B*1502 is associated CC with susceptibility to Stevens-Johnson syndrome. The sequence CC shown is that of B*1501. CC -!- DISEASE: Involved in susceptibility to Stevens-Johnson syndrome CC [MIM:608579]. This is a life-threatening reaction of the skin to CC particular types of medication. It is characterized by high fever, CC malaise and blistering exanthema. The more severe form of the CC disease is referred to as toxic epidermal necrolysis. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M75138; AAA59630.1; -; mRNA. DR EMBL; U03859; AAA03601.1; -; mRNA. DR EMBL; U03027; AAA18902.1; -; mRNA. DR EMBL; L11604; AAA56836.1; -; mRNA. DR EMBL; D50292; BAA08823.1; -; mRNA. DR EMBL; D50293; BAA08824.1; -; mRNA. DR EMBL; D50294; BAA08825.1; -; mRNA. DR EMBL; X61709; CAA43878.1; -; mRNA. DR EMBL; M84382; AAA59632.1; -; mRNA. DR EMBL; U70528; AAB16918.1; -; mRNA. DR EMBL; AJ295140; CAC17462.1; -; Genomic_DNA. DR EMBL; AJ308399; CAC33441.1; -; Genomic_DNA. DR EMBL; M28203; AAA53258.1; -; mRNA. DR EMBL; M83193; AAA58628.1; -; mRNA. DR PIR; G01230; G01230. DR PIR; I38421; I38421. DR PIR; I62042; I62042. DR PIR; S16789; S16789. DR PIR; S77966; S77966. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR PDB; 1XR8; X-ray; A=25-300. DR PDB; 1XR9; X-ray; A=25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR MIM; 608579; phenotype. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-15 alpha chain. FT /FTId=PRO_0000018837. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 48 48 A -> S (in allele B*1503). FT /FTId=VAR_016365. FT VARIANT 69 70 MA -> EE (in allele B*1503). FT /FTId=VAR_016366. FT VARIANT 87 87 E -> N (in allele B*1502 and allele FT B*1511; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016367. FT VARIANT 91 91 S -> C (in allele B*1566). FT /FTId=VAR_016368. FT VARIANT 91 91 S -> Y (in allele B*1511). FT /FTId=VAR_016369. FT VARIANT 118 119 TL -> II (in allele B*1502). FT /FTId=VAR_016370. FT VARIANT 119 119 L -> W (in allele B*1504). FT /FTId=VAR_016371. FT VARIANT 121 121 R -> T (in allele B*1504). FT /FTId=VAR_016372. FT VARIANT 137 137 H -> Y (in allele B*1502). FT /FTId=VAR_016373. FT VARIANT 180 180 W -> L (in allele B*1502 and allele FT B*1503). FT /FTId=VAR_016374. FT VARIANT 190 191 EW -> DG (in allele B*1519). FT /FTId=VAR_016375. FT VARIANT 274 274 P -> L (in allele B*1519). FT /FTId=VAR_016376. FT STRAND 27 36 FT TURN 39 40 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 77 FT TURN 78 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 219 FT TURN 220 221 FT STRAND 222 235 FT STRAND 238 243 FT TURN 244 245 FT HELIX 249 251 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40388 MW; 86E938087372EBE0 CRC64; MRVTAPRTVL LLLSGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRMA PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQW RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B18_HUMAN Reviewed; 362 AA. AC P30466; O62897; Q29845; Q9BCM6; Q9GJ23; Q9MY84; Q9MYC7; Q9TP37; AC Q9TQH7; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 58. DE HLA class I histocompatibility antigen, B-18 alpha chain precursor DE (MHC class I antigen B*18). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*1801). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*1802). RC TISSUE=Blood; RX MEDLINE=95270437; PubMed=7751157; DOI=10.1016/0198-8859(94)00073-Y; RA Lin L., Tokunaga K., Ishikawa Y., Kashiwase K., Nakajima F., RA Nishimura M., Kuwata S., Akaza T., Tadokoro K., Shibata Y., Juji T.; RT "A new B18 sequence (B*1802) from Asian individuals."; RL Hum. Immunol. 42:23-26(1995). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE B*1801). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*1803). RA Dunn P.P.J.; RT "Complete nucleotide sequencing of HLA class I genes."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*1807). RA Kennedy C.T., Dodd R., Le T., Wallace R., Ng G., Hersee J., RA Taverniti A., Kennedy A., Moses J., Trejaut J., Dunckley H.; RT "HLA-B typing with sequence specific oligonucleotides reveals a new RT allele, B*MF."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES B*1807; B*1810; RP B*1811; B*1812 AND B*1813). RX MEDLINE=21442089; PubMed=11556976; RX DOI=10.1034/j.1399-0039.2001.057005481.x; RA Steiner N.K., Kosman C., Jones P.F., Gans C.P., Rodriguez-Marino S.G., RA Rizzuto G., Baldassarre L.A., Edson S., Koester R., Sese D., RA Mitton W., Ng J., Hartzman R.J., Hurley C.K.; RT "Twenty-nine new HLA-B alleles associated with antigens in the 5C RT CREG."; RL Tissue Antigens 57:481-485(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-18 are known: B*1801 CC B*1802, B*1803, B*1807 (B*MF), B*1810, B*1811, B*1812 and B*1813. CC The sequence shown is that of B*1801. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24039; AAA59662.1; -; Genomic_DNA. DR EMBL; D25275; BAA04965.1; -; mRNA. DR EMBL; AJ310507; CAC34572.1; -; Genomic_DNA. DR EMBL; AJ309979; CAC34305.1; -; Genomic_DNA. DR EMBL; AF117775; AAD13298.1; -; Genomic_DNA. DR EMBL; AF117774; AAD13298.1; JOINED; Genomic_DNA. DR EMBL; AF054010; AAC32821.1; -; Genomic_DNA. DR EMBL; AF054009; AAC32821.1; JOINED; Genomic_DNA. DR EMBL; AF198651; AAF20813.1; -; Genomic_DNA. DR EMBL; AF198650; AAF20813.1; JOINED; Genomic_DNA. DR EMBL; AF266526; AAF73066.1; -; Genomic_DNA. DR EMBL; AF266525; AAF73066.1; JOINED; Genomic_DNA. DR EMBL; AF275717; AAF85974.1; -; Genomic_DNA. DR EMBL; AF275716; AAF85974.1; JOINED; Genomic_DNA. DR EMBL; AF310139; AAG27466.1; -; Genomic_DNA. DR EMBL; AF310138; AAG27466.1; JOINED; Genomic_DNA. DR PIR; I61860; I61860. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P30474; 1A9E. DR SMR; P30466; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-18 alpha chain. FT /FTId=PRO_0000018838. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 87 87 N -> E (in allele B*1812; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016661. FT VARIANT 91 91 S -> F (in allele B*1807). FT /FTId=VAR_016662. FT VARIANT 98 98 Y -> D (in allele B*1803). FT /FTId=VAR_016377. FT VARIANT 121 121 R -> N (in allele B*1802; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016378. FT VARIANT 180 180 L -> R (in allele B*1813). FT /FTId=VAR_016663. FT VARIANT 187 187 T -> E (in allele B*1810; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016664. FT VARIANT 195 195 H -> Y (in allele B*1810 and allele FT B*1811). FT /FTId=VAR_016665. SQ SEQUENCE 362 AA; 40275 MW; 106552F4A0F28E17 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFISVG YVDGTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRHLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B27_HUMAN Reviewed; 362 AA. AC P03989; O19692; P10317; P10318; P19373; P30467; Q08136; Q29693; AC Q29846; Q29961; DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 2. DT 20-FEB-2007, entry version 79. DE HLA class I histocompatibility antigen, B-27 alpha chain precursor DE (MHC class I antigen B*27). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*2701). RX MEDLINE=86138405; PubMed=3912316; RA Weiss E.H., Kuon W., Doerner C., Lang M., Riethmueller G.; RT "Organization, sequence and expression of the HLA-B27 gene: a RT molecular approach to analyze HLA and disease associations."; RL Immunobiology 170:367-380(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-361 (ALLELE B*2701). RX MEDLINE=86149317; PubMed=3485286; RA Szoets H., Riethmueller G., Weiss E., Meo T.; RT "Complete sequence of HLA-B27 cDNA identified through the RT characterization of structural markers unique to the HLA-A, -B, and -C RT allelic series."; RL Proc. Natl. Acad. Sci. U.S.A. 83:1428-1432(1986). RN [3] RP PROTEIN SEQUENCE OF 25-295 (B*2701). RX MEDLINE=85226361; PubMed=2408663; DOI=10.1021/bi00328a025; RA Ezquerra A., Bragado R., Vega M.A., Strominger J.L., Woody J., RA Lopez de Castro J.A.; RT "Primary structure of papain-solubilized human histocompatibility RT antigen HLA-B27."; RL Biochemistry 24:1733-1741(1985). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES B*2701 AND B*2702). RX MEDLINE=86220133; PubMed=3011411; RA Seemann G.H.A., Rein R.S., Brown C.S., Ploegh H.L.; RT "Gene conversion-like mechanisms may generate polymorphism in human RT class I genes."; RL EMBO J. 5:547-552(1986). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*2702). RX MEDLINE=96086486; PubMed=7482496; RA Moses J.H., Marsh S.G.E., Arnett K.L., Adams E.J., Bodmer J.G., RA Parham P.; RT "On the nucleotide sequences of B*2702 and B*2705."; RL Tissue Antigens 46:50-53(1995). RN [6] RP PROTEIN SEQUENCE OF 86-107 AND 171-181 (B*2702). RX MEDLINE=86042671; PubMed=2414775; RA Vega M.A., Ezquerra A., Rojo S., Aparicio P., Bragado R., RA Lopez de Castro J.A.; RT "Structural analysis of an HLA-B27 functional variant: identification RT of residues that contribute to the specificity of recognition by RT cytolytic T lymphocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 82:7394-7398(1985). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*2703). RX MEDLINE=88227491; PubMed=3286582; DOI=10.1016/0198-8859(88)90072-9; RA Choo S.Y., St John T., Orr H.T., Hansen J.A.; RT "Molecular analysis of the variant alloantigen HLA-B27d (HLA-B*2703) RT identifies a unique single amino acid substitution."; RL Hum. Immunol. 21:209-219(1988). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*2704 AND B*2706). RX MEDLINE=96134006; PubMed=8550101; DOI=10.1007/BF00176678; RA Rudwaleit M., Bowness P., Wordsworth P.; RT "The nucleotide sequence of HLA-B*2704 reveals a new amino acid RT substitution in exon 4 which is also present in HLA-B*2706."; RL Immunogenetics 43:160-162(1996). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*2705). RX PubMed=3489755; RA Coppin H.L., McDevitt H.O.; RT "Absence of polymorphism between HLA-B27 genomic exon sequences RT isolated from normal donors and ankylosing spondylitis patients."; RL J. Immunol. 137:2168-2172(1986). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*2706). RX MEDLINE=94102824; PubMed=8276469; DOI=10.1007/BF00241265; RA Vilches C., de Pablo R., Kreisler M.; RT "Nucleotide sequence of HLA-B*2706."; RL Immunogenetics 39:219-219(1994). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*2707). RX MEDLINE=91268545; PubMed=1711072; RA Choo Y.S., Fan L.A., Hansen J.A.; RT "A novel HLA-B27 allele maps B27 allospecificity to the region around RT position 70 in the alpha 1 domain."; RL J. Immunol. 147:174-180(1991). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*2708). RX MEDLINE=95064789; PubMed=7974468; RA Hildebrand W.H., Domena J.D., Shen S.Y., Marsh S.G.E., Bunce M., RA Guttridge M.G., Darke C., Parham P.; RT "The HLA-B7Qui antigen is encoded by a new subtype of HLA-B27 RT (B*2708)."; RL Tissue Antigens 44:47-51(1994). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*2709). RC TISSUE=Blood; RX MEDLINE=94375872; PubMed=8089488; RA Del Porto P., D'Amato M., Fiorillo M.T., Tuosto L., Piccolella E., RA Sorrentino R.; RT "Identification of a novel HLA-B27 subtype by restriction analysis of RT a cytotoxic gamma/delta T cell clone."; RL J. Immunol. 153:3093-3100(1994). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-300. RX MEDLINE=92405152; PubMed=1525820; DOI=10.1016/0092-8674(92)90252-8; RA Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.; RT "The three-dimensional structure of HLA-B27 at 2.1-A resolution RT suggests a general mechanism for tight peptide binding to MHC."; RL Cell 70:1035-1048(1992). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-300. RX MEDLINE=92018187; PubMed=1922337; DOI=10.1038/353321a0; RA Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.; RT "The structure of HLA-B27 reveals nonamer self-peptides bound in an RT extended conformation."; RL Nature 353:321-325(1991). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-300. RX MEDLINE=22344622; PubMed=12244049; DOI=10.1074/jbc.M206392200; RA Hulsmeyer M., Hillig R.C., Volz A., Ruhl M., Schroder W., Saenger W., RA Ziegler A., Uchanska-Ziegler B.; RT "HLA-B27 subtypes differentially associated with disease exhibit RT subtle structural alterations."; RL J. Biol. Chem. 277:47844-47853(2002). RN [17] RP 3D-STRUCTURE MODELING OF 115-206. RX MEDLINE=95148615; PubMed=7846047; RA Rognan D., Scapozza L., Folkers G., Daser A.; RT "Rational design of nonnatural peptides as high-affinity ligands for RT the HLA-B*2705 human leukocyte antigen."; RL Proc. Natl. Acad. Sci. U.S.A. 92:753-757(1995). RN [18] RP DISEASE, AND POSSIBLE PROTECTIVE ROLE OF ALLELE B*2707. RX PubMed=15603872; DOI=10.1016/j.humimm.2004.08.177; RA Varnavidou-Nicolaidou A., Karpasitou K., Georgiou D., Stylianou G., RA Kokkofitou A., Michalis C., Constantina C., Gregoriadou C., RA Kyriakides G.; RT "HLA-B27 in the Greek Cypriot population: distribution of subtypes in RT patients with ankylosing spondylitis and other HLA-B27-related RT diseases. The possible protective role of B*2707."; RL Hum. Immunol. 65:1451-1454(2004). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-27 are known: CC B*2701=B*2705, B*2702 (B27.2; B-27k; B27e), B*2703 (B27d), B*2704, CC B*2706, B*2707, B*2708 (B7Qui) and B*2709 (B27-ci). The sequence CC shown is that of B*2701. CC -!- DISEASE: HLA-B27 is associated with the development of ankylosing CC spondylitis (AS) [MIM:106300]. AS is a chronic inflammatory CC rheumatic disease that mainly affects the axial skeleton and is CC considered the prototype of seronegative spondyloarthropathies CC (SNSA), which include reactive arthritis (e.g., Reiter's CC syndrome), psoritic spondylitis, and other spondyloarthropathies CC (SpA). In the Greek Cypriot population, a restricted number of CC HLA-B27 subtypes are associated with AS and other B27-related CC diseases and an elevated frequency of the B*2702 allele in the AS CC patients is identified. The allele B*2707 seems to have a CC protective role in this population because it was found only in CC the healthy controls. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X03945; CAA27578.1; ALT_SEQ; Genomic_DNA. DR EMBL; X03664; CAA27301.1; -; Genomic_DNA. DR EMBL; X03667; CAA27301.1; JOINED; Genomic_DNA. DR EMBL; L38504; AAA69724.1; -; mRNA. DR EMBL; M54883; AAA59616.1; -; Genomic_DNA. DR EMBL; X03665; CAA27302.1; -; Genomic_DNA. DR EMBL; X03666; CAA27302.1; JOINED; Genomic_DNA. DR EMBL; M12967; AAA36221.1; -; Genomic_DNA. DR EMBL; U27608; AAC50444.1; -; mRNA. DR EMBL; U35734; AAC50447.1; -; mRNA. DR EMBL; M14013; AAA59643.1; -; Genomic_DNA. DR EMBL; X73578; CAA51980.1; -; mRNA. DR EMBL; M62852; AAA59647.1; -; mRNA. DR EMBL; L19923; AAA59658.1; -; mRNA. DR EMBL; Z33453; CAA83876.1; -; mRNA. DR PIR; I37515; I37515. DR PIR; I56116; I56116. DR PIR; S07441; HLHUB2. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR PDB; 1HSA; X-ray; A/D=25-300. DR PDB; 1JGD; X-ray; A=25-300. DR PDB; 1JGE; X-ray; A=25-300. DR PDB; 1K5N; X-ray; A=25-300. DR PDB; 1OF2; X-ray; A=25-300. DR PDB; 1OGT; X-ray; A=25-300. DR PDB; 1ROG; Model; A=25-206. DR PDB; 1ROH; Model; A=25-206. DR PDB; 1ROI; Model; A=25-206. DR PDB; 1ROJ; Model; A=25-206. DR PDB; 1ROK; Model; A=25-206. DR PDB; 1ROL; Model; A=25-206. DR PDB; 1UXS; X-ray; A=25-300. DR PDB; 1UXW; X-ray; A=25-300. DR PDB; 1W0V; X-ray; A=25-300. DR PDB; 1W0W; X-ray; A=25-300. DR PDB; 2A83; X-ray; A=25-300. DR PDB; 2BSR; X-ray; A=25-300. DR PDB; 2BSS; X-ray; A=25-300. DR PDB; 2BST; X-ray; A=25-300. DR DIP; DIP:6188N; -. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 106300; phenotype. DR MIM; 142830; gene. DR LinkHub; P03989; -. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR GO; GO:0005624; C:membrane fraction; TAS:UniProtKB. DR GO; GO:0006952; P:defense response; TAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Direct protein sequencing; Glycoprotein; KW Host-virus interaction; Immune response; Membrane; MHC I; KW Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-27 alpha chain. FT /FTId=PRO_0000018839. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 83 83 Y -> H (in allele B*2703). FT /FTId=VAR_016379. FT VARIANT 101 101 D -> N (in allele B*2702). FT /FTId=VAR_016380. FT VARIANT 101 101 D -> S (in allele B*2704, allele B*2706 FT and allele B*2708; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016381. FT VARIANT 104 105 TL -> IA (in allele B*2702). FT /FTId=VAR_016382. FT VARIANT 104 104 T -> N (in allele B*2708). FT /FTId=VAR_016383. FT VARIANT 106 107 LR -> RG (in allele B*2708). FT /FTId=VAR_016384. FT VARIANT 121 121 N -> S (in allele B*2707). FT /FTId=VAR_016385. FT VARIANT 137 138 YH -> HN (in allele B*2707). FT /FTId=VAR_016386. FT VARIANT 138 138 H -> D (in allele B*2706). FT /FTId=VAR_016387. FT VARIANT 140 140 D -> H (in allele B*2709). FT /FTId=VAR_016388. FT VARIANT 140 140 D -> Y (in allele B*2706 and allele FT B*2707). FT /FTId=VAR_016389. FT VARIANT 155 155 S -> R (in allele B*2707). FT /FTId=VAR_016390. FT VARIANT 176 176 V -> E (in allele B*2704 and allele FT B*2706). FT /FTId=VAR_016391. FT VARIANT 235 235 A -> G (in allele B*2704 and allele FT B*2706). FT /FTId=VAR_016392. FT CONFLICT 206 206 A -> V (in Ref. 2). FT CONFLICT 266 266 Q -> E (in Ref. 3). FT STRAND 27 36 FT TURN 39 40 FT STRAND 41 43 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT STRAND 113 115 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 204 FT STRAND 210 219 FT TURN 220 221 FT STRAND 222 235 FT STRAND 238 243 FT TURN 244 245 FT HELIX 249 251 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40428 MW; C8D2F154E3292031 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI CKAKAQTDRE DLRTLLRYYN QSEAGSHTLQ NMYGCDVGPD GRLLRGYHQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B35_HUMAN Reviewed; 362 AA. AC P30685; O62919; P30468; P30469; P30470; P30471; P30472; P30473; AC P30474; Q9GJM7; Q9TPV2; Q9TQH3; Q9TQH9; Q9TQN4; Q9TQN6; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 70. DE HLA class I histocompatibility antigen, B-35 alpha chain precursor DE (MHC class I antigen B*35). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*3501). RX MEDLINE=89339610; PubMed=2788131; RA Ooba T., Hayashi H., Karaki S., Tanabe M., Kano K., Takiguchi M.; RT "The structure of HLA-B35 suggests that it is derived from HLA-Bw58 by RT two genetic mechanisms."; RL Immunogenetics 30:76-80(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*3502). RX MEDLINE=91365651; PubMed=1890016; DOI=10.1016/0198-8859(91)90020-A; RA Chertkoff L.P., Herrera M., Fainboim L., Satz M.L.; RT "Complete nucleotide sequence of a genomic clone encoding HLA-B35 RT isolated from a Caucasian individual of Hispanic origin. RT Identification of a new variant of HLA-B35."; RL Hum. Immunol. 31:153-158(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*3503). RX MEDLINE=92176661; PubMed=1541831; RA Zemmour J., Little A.-M., Schendel D.J., Parham P.; RT "The HLA-A,B 'negative' mutant cell line C1R expresses a novel HLA-B35 RT allele, which also has a point mutation in the translation initiation RT codon."; RL J. Immunol. 148:1941-1948(1992). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*3503). RC TISSUE=Blood; RX MEDLINE=95279930; PubMed=7759996; DOI=10.1084/jem.181.6.2037; RA Beck Y., Satz L., Takamiya Y., Nakayama S., Ling L., Ishikawa Y., RA Nagao T., Uchida H., Tokunaga K., Mueller C., Juji T., Takiguchi M.; RT "Polymorphism of human minor histocompatibility antigens: T cell RT recognition of human minor histocompatibility peptides presented by RT HLA-B35 subtype molecules."; RL J. Exp. Med. 181:2037-2048(1995). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELES B*3505 AND B*3506). RX MEDLINE=92269955; PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*3507 AND B*3508). RX MEDLINE=93303752; PubMed=8316945; RA Theiler G., Pando M., Delfino J.M., Takiguchi M., Satz M.L.; RT "Isolation and characterization of two new functional subtypes of HLA- RT B35."; RL Tissue Antigens 41:143-147(1993). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*3508). RX MEDLINE=94186367; PubMed=8138421; DOI=10.1016/0198-8859(93)90553-D; RA Steinle A., Reinhardt C., Noessner E., Uchanska-Ziegler B., RA Ziegler A., Schendel D.J.; RT "Microheterogeneity in HLA-B35 alleles influences peptide-dependent RT allorecognition by cytotoxic T cells but not binding of a peptide- RT restricted monoclonal antibody."; RL Hum. Immunol. 38:261-269(1993). RN [8] RP NUCLEOTIDE SEQUENCE OF 9-362 (ALLELE B*3504). RX MEDLINE=92269956; PubMed=1589035; DOI=10.1038/357329a0; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES B*3529 AND RP B*3532). RX MEDLINE=20236861; PubMed=10777103; RX DOI=10.1034/j.1399-0039.2000.550311.x; RA Kennedy C.T., Dodd R., Le T., Wallace R., Ng G., Greville W.D., RA Kennedy A., Taverniti A., Moses J.H., Clow N., Watson N., Dunckley H.; RT "Routine HLA-B genotyping with PCR-sequence-specific oligonucleotides RT (PCR-SSO) detects eight new alleles: B*0807, B*0809, B*1551, B*3529, RT B*3532, B*4025, B*5304 and B*5508."; RL Tissue Antigens 55:266-270(2000). RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES B*3525; B*3528; B*3529; B*3530 RP AND B*3536). RX MEDLINE=21442089; PubMed=11556976; RX DOI=10.1034/j.1399-0039.2001.057005481.x; RA Steiner N.K., Kosman C., Jones P.F., Gans C.P., Rodriguez-Marino S.G., RA Rizzuto G., Baldassarre L.A., Edson S., Koester R., Sese D., RA Mitton W., Ng J., Hartzman R.J., Hurley C.K.; RT "Twenty-nine new HLA-B alleles associated with antigens in the 5C RT CREG."; RL Tissue Antigens 57:481-485(2001). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-300. RX MEDLINE=96209671; PubMed=8624811; DOI=10.1016/S1074-7613(00)80429-X; RA Smith K.J., Reid S.W., Stuart D.I., McMichael A.J., Jones E.Y., RA Bell J.I.; RT "An altered position of the alpha 2 helix of MHC class I is revealed RT by the crystal structure of HLA-B*3501."; RL Immunity 4:203-214(1996). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=99096952; PubMed=9878435; DOI=10.1006/jmbi.1998.2363; RA Menssen R., Orth P., Ziegler A., Saenger W.; RT "Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due RT to non-standard positioning of the C-terminus."; RL J. Mol. Biol. 285:645-653(1999). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-35 are known: B*3501, CC B*3502, B*3503, B*3504, B*3505 (B35-G), B*3506 (B35-K), B*3507, CC B*3508, B*3525, B*3528, B*3529 (B*KG), B*3530, B*3532 (B*TMUL) and CC B*3536. The sequence shown is that of B*3501. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M28115; AAA59617.1; -; Genomic_DNA. DR EMBL; M28109; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M28110; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M28111; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M28112; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M28113; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M28114; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M63454; AAA59682.1; -; Genomic_DNA. DR EMBL; M81798; AAA59684.1; -; mRNA. DR EMBL; D50299; BAA08828.1; -; mRNA. DR EMBL; M84385; AAA59635.1; -; mRNA. DR EMBL; M84381; AAA59631.1; -; mRNA. DR EMBL; L04695; AAA59694.1; -; mRNA. DR EMBL; L04696; AAA52674.1; -; mRNA. DR EMBL; Z22651; CAA80366.1; -; mRNA. DR EMBL; M86403; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF117771; AAD23460.1; -; Genomic_DNA. DR EMBL; AF117770; AAD23460.1; JOINED; Genomic_DNA. DR EMBL; AF134867; AAD30277.1; -; Genomic_DNA. DR EMBL; AF134866; AAD30277.1; JOINED; Genomic_DNA. DR EMBL; AF061864; AAC32570.1; -; Genomic_DNA. DR EMBL; AF061863; AAC32570.1; JOINED; Genomic_DNA. DR EMBL; AF108429; AAD27538.1; -; Genomic_DNA. DR EMBL; AF108428; AAD27538.1; JOINED; Genomic_DNA. DR EMBL; AF176078; AAD51745.1; -; Genomic_DNA. DR EMBL; AF176077; AAD51745.1; JOINED; Genomic_DNA. DR EMBL; AF110505; AAD26151.1; -; Genomic_DNA. DR EMBL; AF110504; AAD26151.1; JOINED; Genomic_DNA. DR EMBL; AF282766; AAG01819.1; -; Genomic_DNA. DR EMBL; AF282765; AAG01819.1; JOINED; Genomic_DNA. DR PIR; A45880; A45880. DR PIR; I54298; I54298. DR PIR; I56133; I56133. DR PIR; I61904; I61904. DR PIR; I61907; I61907. DR PIR; I81233; I81233. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR PDB; 1A1N; X-ray; A=25-300. DR PDB; 1A9B; X-ray; A/D=25-301. DR PDB; 1A9E; X-ray; A=25-301. DR PDB; 1XH3; X-ray; A=25-300. DR PDB; 1ZHK; X-ray; A=25-300. DR PDB; 1ZHL; X-ray; A=25-300. DR PDB; 1ZSD; X-ray; A=25-300. DR PDB; 2AK4; X-ray; A/F/K/Q=25-300. DR PDB; 2AXF; X-ray; A=25-300. DR PDB; 2AXG; X-ray; A=25-300. DR PDB; 2CIK; X-ray; A=25-300. DR DIP; DIP:6056N; -. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR LinkHub; P30685; -. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-35 alpha chain. FT /FTId=PRO_0000018840. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 40 40 G -> V (in allele B*3507). FT /FTId=VAR_016393. FT VARIANT 48 48 A -> S (in allele B*3525). FT /FTId=VAR_016394. FT VARIANT 69 69 T -> E (in allele B*3525; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016395. FT VARIANT 87 87 N -> E (in allele B*3528; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016396. FT VARIANT 91 91 F -> S (in allele B*3528). FT /FTId=VAR_016397. FT VARIANT 98 98 Y -> D (in allele B*3529). FT /FTId=VAR_016398. FT VARIANT 107 107 G -> D (in allele B*3536). FT /FTId=VAR_016399. FT VARIANT 118 119 II -> TL (in allele B*3505 and allele FT B*3532). FT /FTId=VAR_016400. FT VARIANT 121 121 R -> S (in allele B*3505 and allele FT B*3530). FT /FTId=VAR_016401. FT VARIANT 127 127 L -> V (in allele B*3532). FT /FTId=VAR_016402. FT VARIANT 133 133 L -> F (in allele B*3502). FT /FTId=VAR_016403. FT VARIANT 138 138 D -> N (in allele B*3502, allele B*3504 FT and allele B*3506). FT /FTId=VAR_016404. FT VARIANT 140 140 S -> F (in allele B*3506 and allele FT B*3536). FT /FTId=VAR_016405. FT VARIANT 140 140 S -> Y (in allele B*3502, allele B*3503 FT and allele B*3504). FT /FTId=VAR_016406. FT VARIANT 180 180 L -> R (in allele B*3508). FT /FTId=VAR_016407. FT STRAND 27 36 FT TURN 39 40 FT STRAND 41 43 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT TURN 244 245 FT HELIX 249 251 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40455 MW; 52906854FC43E7A6 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B37_HUMAN Reviewed; 362 AA. AC P18463; O19627; Q95HA3; Q95HA8; Q95HM9; Q9GJ31; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 20-FEB-2007, entry version 60. DE HLA class I histocompatibility antigen, B-37 alpha chain precursor DE (MHC class I antigen B*37). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*3701). RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*3704). RC TISSUE=Peripheral blood; RX MEDLINE=22025782; PubMed=12028544; RX DOI=10.1034/j.1399-0039.2002.590213.x; RA Estefania E., Gomez-Lozano N., de Pablo R., Moreno M.E., Vilches C.; RT "Complementary DNA sequence of the novel HLA-B*3704 allele."; RL Tissue Antigens 59:142-144(2002). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*3705). RX MEDLINE=22131942; PubMed=12135437; RX DOI=10.1034/j.1399-0039.2002.590416.x; RA Pyo C.-W., Han H., Kim T.G.; RT "Identification of a new HLA-B allele, B*3705 containing a Bw6 RT sequence motif."; RL Tissue Antigens 59:335-337(2002). RN [4] RP NUCLEOTIDE SEQUENCE OF 1-322 (ALLELE B*3701). RA Hurley C.K., Bei M., Rodriguez S., Johnson A.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*3704). RA Gans C.P., Hurley C.K.; RT "Novel HLA-B allele."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-37 are known: B*3701, CC B*3704 and B*3705. The sequence shown is that of B*3701. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M32320; AAA36233.1; -; mRNA. DR EMBL; AF389378; AAL26324.1; -; mRNA. DR EMBL; AF418978; AAL07502.1; -; mRNA. DR EMBL; AF284828; AAK82990.1; -; Genomic_DNA. DR EMBL; AF284826; AAK82990.1; JOINED; Genomic_DNA. DR EMBL; AF284827; AAK82990.1; JOINED; Genomic_DNA. DR EMBL; U11267; AAA19927.1; -; mRNA. DR EMBL; AF303102; AAG21400.1; -; Genomic_DNA. DR EMBL; AF303101; AAG21400.1; JOINED; Genomic_DNA. DR PIR; C35997; C35997. DR UniGene; Hs.5737; -. DR UniGene; Hs.618326; -. DR UniGene; Hs.620192; -. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; Q29961; 1HSA. DR SMR; P18463; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR LinkHub; P18463; -. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-37 alpha chain. FT /FTId=PRO_0000018841. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 104 104 T -> N (in allele B*3705). FT /FTId=VAR_016408. FT VARIANT 106 107 LR -> RG (in allele B*3705). FT /FTId=VAR_016409. FT VARIANT 195 195 Y -> H (in allele B*3704). FT /FTId=VAR_016410. SQ SEQUENCE 362 AA; 40456 MW; FAB4375F05474725 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE DLRTLLRYYN QSEAGSHTIQ RMSGCDVGPD GRLLRGYNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQD RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B38_HUMAN Reviewed; 362 AA. AC Q95365; O19779; O77959; O78160; Q29935; Q29936; Q95IB8; Q95IH5; AC Q9BCM8; Q9MY92; Q9MYG1; Q9TPT2; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-FEB-2007, entry version 52. DE HLA class I histocompatibility antigen, B-38 alpha chain precursor DE (MHC class I antigen B*38) (Bw-4). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*3801). RX MEDLINE=95242308; PubMed=7725307; RA Adams E.J., Martinez-Naves E., Arnett K.L., Little A.-M., Tyan D.B., RA Parham P.; RT "HLA-B16 antigens: sequence of the ST-16 antigen, further definition RT of two B38 subtypes and evidence for convergent evolution of B*3902."; RL Tissue Antigens 45:18-26(1995). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*3801). RA Morlighem G.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE B*3802). RA Little A.-M., Domena J.D., Hildebrand W.H., Parham P.; RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*3802). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [5] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*3802). RX MEDLINE=98116675; PubMed=9455497; DOI=10.1016/S0198-8859(97)00112-2; RA Steiner N.K., Ng J., Bush J., Hartzman R.J., Johnston-Dow L., RA Hurley C.K.; RT "HLA-B alleles associated with the B15 serologically defined RT antigens."; RL Hum. Immunol. 56:84-93(1997). RN [6] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*3802). RA Guttridge M.G., Hammond L., Darke C.; RT "Confirmatory sequence and serology of HLA-B*38021."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 26-206 (ALLELE B*3803). RX MEDLINE=99254921; PubMed=10323342; RX DOI=10.1034/j.1399-0039.1999.530408.x; RA Balas A., Santos S., Garcia-Sanchez F., Lillo R., Merino J.L., RA Vicario J.L.; RT "Characterization of a new HLA-B*38 allele (B*3803) in a Spanish RT Caucasian individual which is closely related to the Oriental B*38021 RT and B*39021 alleles."; RL Tissue Antigens 53:374-377(1999). RN [8] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES B*3804 AND B*3806). RX MEDLINE=21276061; PubMed=11380951; RX DOI=10.1034/j.1399-0039.2001.057004373.x; RA Steiner N.K., Gans C.P., Kosman C., Baldassarre L.A., Edson S., RA Jones P.F., Rizzuto G., Pimtanothai N., Koester R., Mitton W., Ng J., RA Hartzman R.J., Hurley C.K.; RT "Novel HLA-B alleles associated with antigens in the 8C CREG."; RL Tissue Antigens 57:373-375(2001). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELE B*3805). RX MEDLINE=21970277; PubMed=11972879; RX DOI=10.1034/j.1399-0039.2002.590109.x; RA Garcia-Sanchez F., Fernandez-De-Velasco J., Lillo R., RA Alvarez-Doval A., Rodriguez M.A., Aviles M.J., Balas A., Vicario J.L.; RT "Two new HLA class I alleles recognised by PCR sequence-specific RT primer and sequencing based typing: B*3805 and Cw*0408."; RL Tissue Antigens 59:47-48(2002). RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*3807). RA Cavett J.W., Hildebrand W.H., Bennett T.T., Sparkman J.N.; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*3808). RA Chapman G., Dodd R., Greville W.D., Dunckley H.; RT "Novel HLA-B allele Identified by PCR SSO."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*3801). RX MEDLINE=89379286; PubMed=2777338; RA Mueller C.A., Engler-Blum G., Gekeler V., Steiert I., Weiss E., RA Schmidt H.; RT "Genetic and serological heterogeneity of the supertypic HLA-B locus RT specificities Bw4 and Bw6."; RL Immunogenetics 30:200-207(1989). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-38 are known: B*3801, CC B*3802, B*3803, B*3804, B*3805, B*3806, B*3807 and B*3808. The CC sequence shown is that of B*3801. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; L36591; AAA73509.1; -; mRNA. DR EMBL; U40498; AAD00010.1; -; mRNA. DR EMBL; L22028; AAA59618.1; -; mRNA. DR EMBL; AJ297317; CAC29063.1; -; Genomic_DNA. DR EMBL; U90241; AAB82305.1; -; Genomic_DNA. DR EMBL; U90240; AAB82305.1; JOINED; Genomic_DNA. DR EMBL; AJ308991; CAC34965.1; -; Genomic_DNA. DR EMBL; AJ308992; CAC34965.1; JOINED; Genomic_DNA. DR EMBL; AF081275; AAC32198.1; -; mRNA. DR EMBL; AF081276; AAC32199.1; -; Genomic_DNA. DR EMBL; AF181858; AAD56222.1; -; Genomic_DNA. DR EMBL; AF181857; AAD56222.1; JOINED; Genomic_DNA. DR EMBL; AF262961; AAF78055.1; -; Genomic_DNA. DR EMBL; AF262960; AAF78055.1; JOINED; Genomic_DNA. DR EMBL; AF218804; AAF67340.1; -; Genomic_DNA. DR EMBL; AF218802; AAF67340.1; JOINED; Genomic_DNA. DR EMBL; AF218803; AAF67340.1; JOINED; Genomic_DNA. DR EMBL; AF281054; AAK69506.1; -; Genomic_DNA. DR EMBL; AF281053; AAK69506.1; JOINED; Genomic_DNA. DR EMBL; AF402321; AAL04500.1; -; Genomic_DNA. DR EMBL; AF402320; AAL04500.1; JOINED; Genomic_DNA. DR EMBL; M29864; AAA36222.1; -; Genomic_DNA. DR PIR; A59028; A59028. DR PIR; I54463; I54463. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P18464; 1E27. DR SMR; Q95365; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; IOH11225; -. DR RZPD-ProtExp; IOH42052; -. DR RZPD-ProtExp; T1025; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-38 alpha chain. FT /FTId=PRO_0000018842. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 35 35 S -> A (in allele B*3805). FT /FTId=VAR_016411. FT VARIANT 69 69 E -> T (in allele B*3806 and allele FT B*3807; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016412. FT VARIANT 82 82 E -> G (in allele B*3807). FT /FTId=VAR_016413. FT VARIANT 87 87 N -> E (in allele B*3803 and allele FT B*3804; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016414. FT VARIANT 91 91 C -> F (in allele B*3806 and allele FT B*3807). FT /FTId=VAR_016415. FT VARIANT 91 91 C -> S (in allele B*3803). FT /FTId=VAR_016416. FT VARIANT 98 98 Y -> D (in allele B*3803). FT /FTId=VAR_016417. FT VARIANT 101 101 N -> S (in allele B*3803). FT /FTId=VAR_016418. FT VARIANT 104 104 I -> T (in allele B*3802, allele B*3803, FT allele B*3804 and allele B*3808). FT /FTId=VAR_016419. FT VARIANT 187 187 T -> M (in allele B*3808). FT /FTId=VAR_016420. FT CONFLICT 130 131 DG -> ER (in Ref. 12). FT CONFLICT 191 192 WL -> CV (in Ref. 12). SQ SEQUENCE 362 AA; 40416 MW; 41F49A1A19DF21C7 CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI CKTNTQTYRE NLRIALRYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RTYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B39_HUMAN Reviewed; 362 AA. AC P30475; O02960; O78217; P30476; P79504; Q29665; Q29697; Q29749; AC Q29847; Q29852; Q29858; Q8HWF0; Q9TPQ7; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 61. DE HLA class I histocompatibility antigen, B-39 alpha chain precursor DE (MHC class I antigen B*39). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES B*3901 AND B*3902). RX MEDLINE=93131294; PubMed=8420828; DOI=10.1007/BF00191887; RA Kato N., Karaki S., Kashiwase K., Mueller C., Akaza T., Juji T., RA Kano K., Takiguchi M.; RT "Molecular analysis of HLA-B39 subtypes."; RL Immunogenetics 37:212-216(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*3902 AND B*3905). RX MEDLINE=95242308; PubMed=7725307; RA Adams E.J., Martinez-Naves E., Arnett K.L., Little A.-M., Tyan D.B., RA Parham P.; RT "HLA-B16 antigens: sequence of the ST-16 antigen, further definition RT of two B38 subtypes and evidence for convergent evolution of B*3902."; RL Tissue Antigens 45:18-26(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*3904). RC TISSUE=Peripheral blood; RX MEDLINE=95189597; PubMed=7533753; DOI=10.1016/0198-8859(94)90042-6; RA Ogawa A., Tokunaga K., Nakajima F., Kikuchi A., Karaki S., RA Kashiwase K., Ge J., Hannestad K., Juji T., Takiguchi M.; RT "Identification of the gene encoding a novel HLA-B39 subtype. Two RT amino acid substitutions on the beta-sheet out of the peptide-binding RT floor form a novel serological epitope."; RL Hum. Immunol. 41:241-247(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*3909). RC TISSUE=Blood; RX MEDLINE=96435466; PubMed=8838352; RA Ramos M., Postigo J.M., Vilches C., Layrisse Z., Lopez de Castro J.A.; RT "Primary structure of a novel HLA-B39 allele (B*3909) from the Warao RT Indians of Venezuela. Further evidence for local HLA-B diversification RT in South America."; RL Tissue Antigens 46:401-404(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*3906). RX MEDLINE=96387677; PubMed=8795147; RA Zhao W., Fernandez-Vina M.A., Lazaro A.M., Araujo H.A., Miller S., RA Stastny P.; RT "Full cDNA of a novel HLA-B39 subtype, B*39061."; RL Tissue Antigens 47:435-437(1996). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE B*3906). RA Zhang L., Ellexson M.E., Hildebrand W.H.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*3910). RX MEDLINE=97142356; PubMed=8988545; RA Wells R.S., Parham P.; RT "A novel recombinant HLA-B*39 allele (B*3910) in a South African RT Zulu."; RL Tissue Antigens 48:595-597(1996). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*3910). RX MEDLINE=97378891; PubMed=9234488; RA Vilches C., Bunce M., de Pablo R., Moreno M.E., Puente S., Sanz L., RA Kreisler M.; RT "The novel HLA-Cw*1802 allele is associated with B*5703 in the Bubi RT population from Equatorial Guinea."; RL Tissue Antigens 49:644-648(1997). RN [9] RP NUCLEOTIDE SEQUENCE (ALLELE B*3901). RA Kashiwase K.; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*3924). RC TISSUE=Peripheral blood; RX MEDLINE=22447027; PubMed=12558815; RX DOI=10.1046/j.1365-2370.2003.00362.x; RA Estefania E., Gomez-Lozano N., de Pablo R., Moreno M.E., Vilches C.; RT "Complementary DNA sequence of the HLA-B*3924 allele."; RL Eur. J. Immunogenet. 30:11-12(2003). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-362 (ALLELE B*3908). RX MEDLINE=96435470; PubMed=8838356; RA Adams E.J., Little A.-M., Arnett K.L., McAuley J.E., Williams R.C., RA Parham P.; RT "Three new HLA-B alleles found in Mexican-Americans."; RL Tissue Antigens 46:414-416(1995). RN [12] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*3912). RX MEDLINE=99299758; PubMed=10372543; RX DOI=10.1034/j.1399-0039.1999.530504.x; RA Marcos C.Y., Fernandez-Vina M.A., Lazaro A.M., Moraes M.E., RA Moraes J.R., Stastny P.; RT "Novel HLA-A and HLA-B alleles in South American Indians."; RL Tissue Antigens 53:476-485(1999). RN [13] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*3912). RX MEDLINE=20066996; PubMed=10600013; DOI=10.1016/S0198-8859(99)00092-0; RA Lazaro A.M., Moraes M.E., Marcos C.Y., Moraes J.R., RA Fernandez-Vina M.A., Stastny P.; RT "Evolution of HLA-class I compared to HLA-class II polymorphism in RT Terena, a South-American Indian tribe."; RL Hum. Immunol. 60:1138-1149(1999). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*3923). RX MEDLINE=21160452; PubMed=11260515; RX DOI=10.1034/j.1399-0039.2001.057002169.x; RA Akesaka T., Kashiwase K., Ishikawa Y., Tanaka H., Shimizu M., RA Kawai S., Akaza T., Takahashi T., Juji T.; RT "Allele frequency of HLA-B39 in the Japanese population and RT identification of a novel B39 allele, B*3923."; RL Tissue Antigens 57:169-172(2001). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-196 (ALLELE B*3907). RX MEDLINE=95317819; PubMed=7797264; RA Garber T.L., Butler L.M., Trachtenberg E.A., Erlich H.A., Rickards O., RA De Stefano G., Watkins D.I.; RT "HLA-B alleles of the Cayapa of Ecuador: new B39 and B15 alleles."; RL Immunogenetics 42:19-27(1995). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-39 are known: B*3901 CC (B39.1), B*3902 (B9.2), B*3903, B*3904 (B39N), B*3905 (ST-16), CC B*3906 (B39G), B*3907 (B39uw3), B*3909, B*3910, B*3912 (B3901v), CC B*3923 (B39022v1) and B*3924. The sequence shown is that of CC B*3901. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M94052; AAA52658.1; -; Genomic_DNA. DR EMBL; M94051; AAA52660.1; -; Genomic_DNA. DR EMBL; M94053; AAA52659.1; -; Genomic_DNA. DR EMBL; U04243; AAA87396.1; -; mRNA. DR EMBL; L36318; AAA73942.1; -; mRNA. DR EMBL; L22649; AAA69861.1; -; Genomic_DNA. DR EMBL; U29480; AAC50392.1; -; mRNA. DR EMBL; L42024; AAB59484.1; -; mRNA. DR EMBL; U29083; AAC32741.1; -; mRNA. DR EMBL; U56246; AAB01985.1; -; Genomic_DNA. DR EMBL; Y09058; CAA70261.1; -; mRNA. DR EMBL; AB091216; BAC11810.1; -; Genomic_DNA. DR EMBL; AB091218; BAC11811.1; -; Genomic_DNA. DR EMBL; AF428252; AAN63555.1; -; mRNA. DR EMBL; L42280; AAB51452.1; -; Genomic_DNA. DR EMBL; U76395; AAB39108.1; -; Genomic_DNA. DR EMBL; U76394; AAB39108.1; JOINED; Genomic_DNA. DR EMBL; AB032097; BAA84116.1; -; Genomic_DNA. DR EMBL; U15640; AAA74047.1; -; Genomic_DNA. DR PIR; I38876; I38876. DR PIR; I54314; I54314. DR PIR; I54505; I54505. DR PIR; I68850; I68850. DR PIR; I84488; I84488. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P30474; 1A9E. DR SMR; P30475; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; IOH11225; -. DR RZPD-ProtExp; IOH42052; -. DR RZPD-ProtExp; T1025; -. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-39 alpha chain. FT /FTId=PRO_0000018843. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 33 33 Y -> D (in allele B*3912). FT /FTId=VAR_016659. FT VARIANT 35 35 S -> A (in allele B*3904 and allele FT B*3912). FT /FTId=VAR_016421. FT VARIANT 36 36 V -> M (in allele B*3904). FT /FTId=VAR_016660. FT VARIANT 87 87 N -> E (in allele B*3902, allele B*3908 FT and allele B*3923; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016422. FT VARIANT 91 91 C -> S (in allele B*3902, allele B*3908 FT and allele B*3923). FT /FTId=VAR_016423. FT VARIANT 91 91 C -> Y (in allele B*3910). FT /FTId=VAR_016424. FT VARIANT 98 98 D -> Y (in allele B*3905, allele B*3907 FT and allele B*3908). FT /FTId=VAR_016425. FT VARIANT 119 119 L -> W (in allele B*3906). FT /FTId=VAR_016426. FT VARIANT 121 121 R -> S (in allele B*3903 and allele FT B*3924). FT /FTId=VAR_016427. FT VARIANT 121 121 R -> T (in allele B*3906). FT /FTId=VAR_016428. FT VARIANT 122 122 M -> T (in allele B*3924). FT /FTId=VAR_016429. FT VARIANT 123 123 Y -> S (in allele B*3909). FT /FTId=VAR_016430. FT VARIANT 138 138 N -> D (in allele B*3907). FT /FTId=VAR_016431. FT VARIANT 140 140 F -> S (in allele B*3907). FT /FTId=VAR_016432. FT VARIANT 168 168 Q -> R (in allele B*3923). FT /FTId=VAR_016433. FT VARIANT 180 180 L -> R (in allele B*3908). FT /FTId=VAR_016434. SQ SEQUENCE 362 AA; 40328 MW; 422698063DEAB039 CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI CKTNTQTDRE SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RTYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B40_HUMAN Reviewed; 362 AA. AC Q04826; O19556; O19651; P01890; P30477; P30478; Q29762; Q29842; AC Q29855; Q30173; Q31603; Q9TPT6; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 20-FEB-2007, entry version 61. DE HLA class I histocompatibility antigen, B-40 alpha chain precursor DE (MHC class I antigen B*40) (Bw-60). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*4001). RX MEDLINE=87192942; PubMed=2437025; DOI=10.1007/BF00404425; RA Ways J.W., Lawlor D.A., Wan A.M., Parham P.; RT "A transposable epitope of HLA-B7, B40 molecules."; RL Immunogenetics 25:323-328(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*4001). RX MEDLINE=94294981; PubMed=7517584; RA Little A.-M., Domena J.D., Hildebrand W.H., Shen S.Y., Barber L.D., RA Marsh S.G.E., Bias W.B., Parham P.; RT "HLA-B67: a member of the HLA-B16 family that expresses the ME1 RT epitope."; RL Tissue Antigens 43:38-43(1994). RN [3] RP PROTEIN SEQUENCE OF 25-295 (B*4001). RX MEDLINE=84000412; PubMed=6193808; DOI=10.1021/bi00285a036; RA Lopez de Castro J.A., Bragado R., Strong D.M., Strominger J.L.; RT "Primary structure of papain-solubilized human histocompatibility RT antigen HLA-B40 (-Bw60). An outline of alloantigenic determinants."; RL Biochemistry 22:3961-3969(1983). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*4002). RX MEDLINE=93127148; PubMed=1362296; RA Domena J.D., Johnston-Dow L., Parham P.; RT "The B*4002 allele encodes the B61 antigen: B40* is identical to RT B61."; RL Tissue Antigens 40:254-256(1992). RN [5] RP NUCLEOTIDE SEQUENCE OF 13-318 (ALLELE B*4002). RC TISSUE=Blood; RX MEDLINE=93127149; PubMed=1481202; RA Lin L., Watanabe Y., Tokunaga K., Kuwata S., Kohsaka T., Akaza T.; RT "A common Japanese haplotype HLA-A26-Cw3-B61-DR9-DQ3 carries HLA- RT B*4002."; RL Tissue Antigens 40:257-260(1992). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELES B*4003 AND B*4004). RX MEDLINE=92269955; PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [7] RP NUCLEOTIDE SEQUENCE (ALLELE B*4005). RX MEDLINE=93056529; PubMed=1385528; RA Hildebrand W.H., Madrigal J.A., Belich M.P., Zemmour J., Ward F.E., RA Williams R.C., Parham P.; RT "Serologic cross-reactivities poorly reflect allelic relationships in RT the HLA-B12 and HLA-B21 groups. Dominant epitopes of the alpha 2 RT helix."; RL J. Immunol. 149:3563-3568(1992). RN [8] RP NUCLEOTIDE SEQUENCE (ALLELE B*4006). RA Herrero M.J.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE (ALLELE B*4006). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*4008). RX MEDLINE=96097410; PubMed=8525480; RA Adams E.J., Little A.-M., Arnett K.L., Leushner J., Parham P.; RT "Identification of a novel HLA-B40 allele (B*4008) in a patient with RT leukemia."; RL Tissue Antigens 46:204-205(1995). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-206 (ALLELE B*4009). RX MEDLINE=99299758; PubMed=10372543; RX DOI=10.1034/j.1399-0039.1999.530504.x; RA Marcos C.Y., Fernandez-Vina M.A., Lazaro A.M., Moraes M.E., RA Moraes J.R., Stastny P.; RT "Novel HLA-A and HLA-B alleles in South American Indians."; RL Tissue Antigens 53:476-485(1999). RN [12] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*4016). RX MEDLINE=20548605; PubMed=11098929; RX DOI=10.1034/j.1399-0039.2000.560401.x; RA Ellis J.M., Mack S.J., Leke R.F.G., Quakyi I., Johnson A.H., RA Hurley C.K.; RT "Diversity is demonstrated in class I HLA-A and HLA-B alleles in RT Cameroon, Africa: description of HLA-A*03012, *2612, *3006 and HLA- RT B*1403, *4016, *4703."; RL Tissue Antigens 56:291-302(2000). RN [13] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*4027). RA Pimtanothai N., Hurley C.K.; RT "Novel HLA-B allele."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-40 are known: B*4001, CC B*4002, B*4003 (B40-G1), B*4004 (B40-G2), B*4005 (BN21), B*4006, CC B*4008, B*4009, B*4016 and B*4027. The sequence shown is that of CC B*4002. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; U03698; AAA03719.1; -; mRNA. DR EMBL; L41628; AAA65040.1; -; Genomic_DNA. DR EMBL; L09736; AAA36224.1; -; mRNA. DR EMBL; D14343; BAA03277.1; -; mRNA. DR EMBL; M84383; AAA59633.1; -; mRNA. DR EMBL; M84384; AAA59634.1; -; mRNA. DR EMBL; M84694; AAA03661.1; -; mRNA. DR EMBL; X84725; CAA59215.1; -; mRNA. DR EMBL; AJ300180; CAC15501.1; -; Genomic_DNA. DR EMBL; AJ292253; CAC29021.1; -; Genomic_DNA. DR EMBL; L41353; AAC41923.1; -; Genomic_DNA. DR EMBL; L76934; AAA96270.1; -; mRNA. DR EMBL; AF017023; AAB70252.1; -; Genomic_DNA. DR EMBL; AF017022; AAB70252.1; JOINED; Genomic_DNA. DR EMBL; AF181472; AAD56943.1; -; Genomic_DNA. DR EMBL; AF181471; AAD56943.1; JOINED; Genomic_DNA. DR PIR; I38437; HLHU40. DR PIR; I56149; I56149. DR PIR; I59655; I59655. DR PIR; I61905; I61905. DR PIR; I61906; I61906. DR PIR; S52486; S52486. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P30474; 1A9E. DR SMR; Q04826; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Direct protein sequencing; Glycoprotein; Host-virus interaction; KW Immune response; Membrane; MHC I; Polymorphism; Signal; Transmembrane; KW Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-40 alpha chain. FT /FTId=PRO_0000018844. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 9 9 L -> V (in allele B*4001). FT /FTId=VAR_016435. FT VARIANT 14 15 WG -> SA (in allele B*4001). FT /FTId=VAR_016436. FT VARIANT 17 17 V -> L (in allele B*4001). FT /FTId=VAR_016437. FT VARIANT 35 36 SV -> AM (in allele B*4001 and allele FT B*4016). FT /FTId=VAR_016438. FT VARIANT 87 87 E -> N (in allele B*4008; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016439. FT VARIANT 91 91 S -> F (in allele B*4008). FT /FTId=VAR_016440. FT VARIANT 118 119 TL -> II (in allele B*4003). FT /FTId=VAR_016441. FT VARIANT 119 119 L -> W (in allele B*4006). FT /FTId=VAR_016442. FT VARIANT 121 121 S -> R (in allele B*4001 and allele FT B*4003). FT /FTId=VAR_016443. FT VARIANT 121 121 S -> T (in allele B*4006). FT /FTId=VAR_016444. FT VARIANT 127 127 V -> L (in allele B*4003). FT /FTId=VAR_016445. FT VARIANT 137 137 H -> Y (in allele B*4009). FT /FTId=VAR_016658. FT VARIANT 138 138 N -> D (in allele B*4004 and allele FT B*4009). FT /FTId=VAR_016446. FT VARIANT 140 140 Y -> N (in allele B*4027). FT /FTId=VAR_016447. FT VARIANT 140 140 Y -> S (in allele B*4004). FT /FTId=VAR_016448. FT VARIANT 167 167 T -> S (in allele B*4001). FT /FTId=VAR_016449. FT VARIANT 171 171 W -> L (in allele B*4001). FT /FTId=VAR_016450. FT VARIANT 176 176 V -> E (in allele B*4005 and allele FT B*4016). FT /FTId=VAR_016451. FT VARIANT 180 180 L -> R (in allele B*4016). FT /FTId=VAR_016655. FT VARIANT 187 187 E -> L (in allele B*4005; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016452. FT VARIANT 201 202 ET -> DK (in allele B*4001 and allele FT B*4016). FT /FTId=VAR_016453. FT VARIANT 204 204 Q -> E (in allele B*4001 and allele FT B*4016). FT /FTId=VAR_016454. FT CONFLICT 167 167 Missing (in Ref. 3). SQ SEQUENCE 362 AA; 40505 MW; 7D66503ACD865152 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B41_HUMAN Reviewed; 362 AA. AC P30479; O19595; Q29848; Q9MY79; Q9MY94; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 57. DE HLA class I histocompatibility antigen, B-41 alpha chain precursor DE (MHC class I antigen B*41) (Bw-41). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*4101). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*4102). RX MEDLINE=95237906; PubMed=7721359; DOI=10.1007/BF00172162; RA Rufer N., Roosnek E., Kressig R., Jeannet M., Tiercy J.-M.; RT "Sequencing of a new HLA-B41 subtype (B*4102) that occurs with a high RT frequency in the Caucasoid population."; RL Immunogenetics 41:333-333(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*4103). RX MEDLINE=98378282; PubMed=9714480; RA Hurley C.K., Steiner N.K., Kosman C., Mitton W., Koester R., Bei M., RA Bush J., McCormack J., Hahn A., Henson V., Hoyer R., Wade J.A., RA Hartzman R.J., Ng J.; RT "Novel HLA-A and HLA-B alleles."; RL Tissue Antigens 52:84-87(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*4104). RX MEDLINE=21108621; PubMed=11169265; RX DOI=10.1034/j.1399-0039.2001.057001083.x; RA Turner D.M., Vlachos G., Cavanna S.L., Brown J., Brown C., RA Navarrete C.V.; RT "A novel HLA allele, B*4104, identified in a cord blood donor."; RL Tissue Antigens 57:83-84(2001). RN [5] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*4105). RA Gans C.P., Hurley C.K.; RT "Novel HLA-B allele."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-41 are known: B*4101, CC B*4102 (B41.2), B*4103, B*4104 and B*4105. The sequence shown is CC that of B*4101. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24035; AAA59666.1; -; Genomic_DNA. DR EMBL; X81363; CAA57128.1; -; mRNA. DR EMBL; AF028596; AAC33187.1; -; Genomic_DNA. DR EMBL; AF028595; AAC33187.1; JOINED; Genomic_DNA. DR EMBL; AF258782; AAF76144.1; -; Genomic_DNA. DR EMBL; AF279118; AAF81603.1; -; Genomic_DNA. DR EMBL; AF279117; AAF81603.1; JOINED; Genomic_DNA. DR PIR; I37492; I37492. DR PIR; I61864; I61864. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P30474; 1A9E. DR SMR; P30479; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; IOH11225; -. DR RZPD-ProtExp; IOH42052; -. DR RZPD-ProtExp; T1025; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-41 alpha chain. FT /FTId=PRO_0000018845. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 104 104 N -> K (in allele B*4105). FT /FTId=VAR_016459. FT VARIANT 119 119 W -> L (in allele B*4102, allele B*4103 FT and allele B*4104). FT /FTId=VAR_016455. FT VARIANT 121 121 R -> S (in allele B*4102 and allele FT B*4104). FT /FTId=VAR_016456. FT VARIANT 127 127 V -> L (in allele B*4104). FT /FTId=VAR_016457. FT VARIANT 138 138 N -> D (in allele B*4104). FT /FTId=VAR_016458. SQ SEQUENCE 362 AA; 40539 MW; 7443DC40CF7A38F5 CRC64; MRVTAPRTVL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTWQ RMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQD RAYLEGTCVE WLRRYLENGK DTLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B42_HUMAN Reviewed; 362 AA. AC P30480; P79555; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 59. DE HLA class I histocompatibility antigen, B-42 alpha chain precursor DE (MHC class I antigen B*42). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*4201). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*4202). RX MEDLINE=97387746; PubMed=9243763; RA Lardy N.M., Otting N., van de Weerd M.J., van de Horst A.R., RA Waal L.P., Bontrop R.E.; RT "Full-length cDNA nucleotide sequence of the HLA-B*4202 allele."; RL Tissue Antigens 50:83-84(1997). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE B*4201). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-42 are known: B*4201 (Bw- CC 42) and B*4202. The sequence shown is that of B*4201. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24034; AAA59667.1; -; Genomic_DNA. DR EMBL; U88407; AAC16437.1; -; mRNA. DR EMBL; AJ309194; CAC38393.1; -; Genomic_DNA. DR PIR; I61865; I61865. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; Q29961; 1HSA. DR SMR; P30480; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR ArrayExpress; P30480; -. DR GermOnline; ENSG00000204523; Homo sapiens. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-42 alpha chain. FT /FTId=PRO_0000018846. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 33 33 Y -> H (in allele B*4202). FT /FTId=VAR_016460. SQ SEQUENCE 362 AA; 40333 MW; C9155AB015DEA1BE CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQD RAYLEGTCVE WLRRYLENGK DTLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B44_HUMAN Reviewed; 362 AA. AC P30481; P10320; P30482; P79524; Q29850; Q860I4; Q861B5; Q9BCM7; AC Q9MYC3; Q9UQS8; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 58. DE HLA class I histocompatibility antigen, B-44 alpha chain precursor DE (MHC class I antigen B*44) (Bw-44). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*4402). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*4403). RX MEDLINE=91335451; PubMed=1871765; RA Fleischhauer K., Kernan N.A., Dupont B., Yang S.Y.; RT "The two major subtypes of HLA-B44 differ for a single amino acid in RT codon 156."; RL Tissue Antigens 37:133-137(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*4403). RX MEDLINE=96435470; PubMed=8838356; RA Adams E.J., Little A.-M., Arnett K.L., McAuley J.E., Williams R.C., RA Parham P.; RT "Three new HLA-B alleles found in Mexican-Americans."; RL Tissue Antigens 46:414-416(1995). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*4407). RX MEDLINE=97004417; PubMed=8851728; RA Vilches C., Sanz L., de Pablo R., Moreno M.E., Puente S., Kreisler M.; RT "Molecular characterization of the new alleles HLA-B*8101 and RT B*4407."; RL Tissue Antigens 47:139-142(1996). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*4408). RX MEDLINE=97387735; PubMed=9243752; RA Darke C., Street J., Fussell H., Thomas M., Guttridge M., RA Goldberg T.E., Arnett K.L., Parham P.; RT "A new HLA-B44 variant (B44BO [B*4408]) identified by serology."; RL Tissue Antigens 50:32-37(1997). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE B*4412). RA Cox S.T., McWhinnie A.J., Prokupek B., Madrigal A., Little A.-M.; RT "Further diversity within the HLA-B44 group: two novel alleles RT identified in UK Caucasoid potential bone marrow donors."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*4413). RX MEDLINE=20208584; PubMed=10746795; RX DOI=10.1034/j.1399-0039.2000.550215.x; RA Cox S.T., McWhinnie A.J., Prokupek B., Madrigal A., Little A.-M.; RT "HLA-B*4413 identified in a UK Caucasoid potential bone marrow RT donor."; RL Tissue Antigens 55:185-187(2000). RN [8] RP NUCLEOTIDE SEQUENCE (ALLELES B*4402 AND B*4409). RA Dunn P.P.J.; RT "Complete nucleotide sequencing of HLA class I genes."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE (ALLELE B*4405). RA Vilches C., Sepulveda S.; RT "Complete cDNA sequence of HLA-B*4405."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE (ALLELE B*4404). RC TISSUE=Blood; RA Cox S.T.; RT "Confirmation of HLA-B*4404."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-362 (ALLELE B*4402). RX MEDLINE=86249389; PubMed=3459708; RA Kottmann A.H., Seemann G.H.A., Guessow H.D., Roos M.H.; RT "DNA sequence of the coding region of the HLA-B44 gene."; RL Immunogenetics 23:396-400(1986). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-44 are known: B*4402 (B- CC 12; B44.2), B*4404, B*4405, B*4407, B*4408 (B44BO), B*4409, B*4412 CC and B*4413. The sequence shown is that of B*4402. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24038; AAA59663.1; -; Genomic_DNA. DR EMBL; X64366; CAA45718.1; -; mRNA. DR EMBL; L42282; AAB51454.1; -; Genomic_DNA. DR EMBL; L42283; AAB51455.1; -; Genomic_DNA. DR EMBL; X90391; CAA62036.1; -; mRNA. DR EMBL; U64801; AAB40632.1; -; mRNA. DR EMBL; AJ133267; CAB38071.2; -; Genomic_DNA. DR EMBL; AJ131118; CAB37868.1; -; mRNA. DR EMBL; AJ309936; CAC33891.1; -; Genomic_DNA. DR EMBL; AJ309937; CAC33892.1; -; Genomic_DNA. DR EMBL; AJ535113; CAD59381.1; -; mRNA. DR EMBL; AJ550735; CAD79566.1; -; Genomic_DNA. DR EMBL; M15470; AAA59619.1; -; mRNA. DR PIR; A25295; HLHUB4. DR PIR; I61861; I61861. DR PIR; S25415; S25415. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR PDB; 1M6O; X-ray; A=25-300. DR PDB; 1SYS; X-ray; A=25-300. DR PDB; 1SYV; X-ray; A=25-300. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-44 alpha chain. FT /FTId=PRO_0000018847. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 65 65 T -> A (in allele B*4407 and allele FT B*4408). FT /FTId=VAR_016461. FT VARIANT 69 70 KE -> MA (in allele B*4408). FT /FTId=VAR_016462. FT VARIANT 85 85 D -> E (in allele B*4413). FT /FTId=VAR_016463. FT VARIANT 87 87 E -> N (in allele B*4412; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016464. FT VARIANT 101 101 N -> S (in allele B*4409). FT /FTId=VAR_016465. FT VARIANT 104 107 TALR -> NLRG (in allele B*4409). FT /FTId=VAR_016466. FT VARIANT 140 140 D -> Y (in allele B*4405). FT /FTId=VAR_016467. FT VARIANT 180 180 D -> L (in allele B*4403, allele B*4407 FT and allele B*4413; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016468. FT VARIANT 180 180 D -> R (in allele B*4404; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016469. FT VARIANT 187 187 L -> T (in allele B*4404; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016470. FT CONFLICT 106 106 L -> A (in Ref. 11). FT CONFLICT 223 223 V -> A (in Ref. 11). FT CONFLICT 229 229 A -> S (in Ref. 11). FT STRAND 27 36 FT TURN 39 40 FT STRAND 41 43 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 219 FT TURN 220 221 FT STRAND 222 235 FT STRAND 238 243 FT TURN 244 245 FT HELIX 249 251 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40481 MW; E45C71FDEFC628AD CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE NLRTALRYYN QSEAGSHIIQ RMYGCDVGPD GRLLRGYDQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQD RAYLEGLCVE SLRRYLENGK ETLQRADPPK THVTHHPISD HEVTLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B45_HUMAN Reviewed; 362 AA. AC P30483; Q9GIZ0; Q9MX21; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 28-NOV-2006, entry version 55. DE HLA class I histocompatibility antigen, B-45 alpha chain precursor DE (MHC class I antigen B*45) (Bw-45). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*4501). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*4504). RA Carey K., Green A., Dunn P.P.; RT "The complete nucleotide sequence of a variant HLA-B*4501 allele."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE B*4501). RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*4503). RX MEDLINE=21108617; PubMed=11169261; RX DOI=10.1034/j.1399-0039.2001.057001070.x; RA Cox S.T., Mcwhinnie A.J., Koester R.P., Heine U., Holman R., RA Madrigal A.J., Little A.-M.; RT "Further diversity at HLA-A and -B loci identified in Afro-Caribbean RT potential bone marrow donors."; RL Tissue Antigens 57:70-72(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-45 are known: B*4501 (B- CC 12), B*4503 and B*4504. The sequence shown is that of B*4501. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X61710; CAA43879.1; -; mRNA. DR EMBL; AJ278944; CAC07211.1; -; Genomic_DNA. DR EMBL; AJ458992; CAD30340.1; -; Genomic_DNA. DR EMBL; AJ275937; CAB83041.1; -; Genomic_DNA. DR PIR; I37519; I37519. DR HSSP; P30474; 1A9E. DR SMR; P30483; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-45 alpha chain. FT /FTId=PRO_0000018848. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 139 139 Q -> R (in allele B*4503). FT /FTId=VAR_016471. FT VARIANT 191 191 S -> W (in allele B*4504). FT /FTId=VAR_016472. SQ SEQUENCE 362 AA; 40414 MW; A6C843121D613695 CRC64; MRVTAPRTVL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTWQ RMYGCDLGPD GRLLRGYNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQD RAYLEGLCVE SLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B46_HUMAN Reviewed; 362 AA. AC P30484; Q9TPR2; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 58. DE HLA class I histocompatibility antigen, B-46 alpha chain precursor DE (MHC class I antigen B*46) (Bw-46). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*4601). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*4601). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*4602). RX MEDLINE=20340078; PubMed=10885569; RX DOI=10.1034/j.1399-0039.2000.550511.x; RA Akesaka T., Kashiwase K., Shimamura M., Ishikawa Y., Tanaka H., RA Fujii M., Akaza T., Honda K., Yuasa S., Takahashi T., Juji T.; RT "Identification of a novel HLA-B46 allele, B*4602, in Japanese."; RL Tissue Antigens 55:460-462(2000). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-46 are known: B*4601 and CC B*4602. The sequence shown is that of B*4601. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24033; AAA59665.1; -; mRNA. DR EMBL; AJ310508; CAC34573.1; -; Genomic_DNA. DR EMBL; AB032091; BAA84111.1; -; Genomic_DNA. DR PIR; I61863; I61863. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P30474; 1A9E. DR SMR; P30484; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR ArrayExpress; P30484; -. DR GermOnline; ENSG00000204523; Homo sapiens. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-46 alpha chain. FT /FTId=PRO_0000018849. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 98 98 D -> G (in allele B*4602). FT /FTId=VAR_016473. SQ SEQUENCE 362 AA; 40440 MW; 481B4C6876CB0E85 CRC64; MRVTAPRTVL LLLSGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRMA PRAPWIEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQW RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B47_HUMAN Reviewed; 362 AA. AC P30485; O19555; O77933; Q95392; Q9GIL3; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 28-NOV-2006, entry version 54. DE HLA class I histocompatibility antigen, B-47 alpha chain precursor DE (MHC class I antigen B*47) (Bw-47). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*4701). RX MEDLINE=88152906; PubMed=3257938; RA Zemmour J., Ennis P.D., Parham P., Dupont B.; RT "Comparison of the structure of HLA-Bw47 to HLA-B13 and its RT relationship to 21-hydroxylase deficiency."; RL Immunogenetics 27:281-287(1988). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*4701). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-302 (ALLELE B*4702). RC TISSUE=Peripheral blood; RX MEDLINE=97316881; PubMed=9174155; RA Fischer G.F., Broer E., Fae I., Leitner D., Mayr W.R.; RT "Nucleotide sequence analysis of an HLA-B47 variant (HLA-B*4702)."; RL Tissue Antigens 49:540-542(1997). RN [4] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*4703). RX MEDLINE=20548605; PubMed=11098929; RX DOI=10.1034/j.1399-0039.2000.560401.x; RA Ellis J.M., Mack S.J., Leke R.F.G., Quakyi I., Johnson A.H., RA Hurley C.K.; RT "Diversity is demonstrated in class I HLA-A and HLA-B alleles in RT Cameroon, Africa: description of HLA-A*03012, *2612, *3006 and HLA- RT B*1403, *4016, *4703."; RL Tissue Antigens 56:291-302(2000). RN [5] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*4703). RA Kosman C.A., Hurley C.K.; RT "Novel HLA class I B locus alleles."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-47 are known: B*4701, CC B*4702 and B*4703. The sequence shown is that of B*4701. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M19756; AAA52664.1; -; Genomic_DNA. DR EMBL; AJ308398; CAC33087.2; -; Genomic_DNA. DR EMBL; AJ295141; CAC17463.2; -; Genomic_DNA. DR EMBL; Y09118; CAA70335.1; -; mRNA. DR EMBL; AF016843; AAB70513.1; -; Genomic_DNA. DR EMBL; AF016842; AAB70513.1; JOINED; Genomic_DNA. DR EMBL; AF071764; AAC23752.1; -; Genomic_DNA. DR EMBL; AF071763; AAC23752.1; JOINED; Genomic_DNA. DR PIR; I68724; I68724. DR HSSP; Q29961; 1HSA. DR SMR; P30485; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-47 alpha chain. FT /FTId=PRO_0000018850. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 101 101 D -> S (in allele B*4702 and allele FT B*4703; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016474. FT VARIANT 104 104 T -> N (in allele B*4702 and allele FT B*4703). FT /FTId=VAR_016475. FT VARIANT 106 107 LR -> RG (in allele B*4702). FT /FTId=VAR_016476. SQ SEQUENCE 362 AA; 40571 MW; E3D3E4CBF8C15EAE CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE DLRTLLRYYN QSEAGSHTLQ RMFGCDVGPD GRLLRGYHQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV VCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B48_HUMAN Reviewed; 362 AA. AC P30486; Q29764; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 23-JAN-2007, entry version 58. DE HLA class I histocompatibility antigen, B-48 alpha chain precursor DE (MHC class I antigen B*48) (Bw-48). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*4801). RX MEDLINE=92269955; PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*4801). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-206 (ALLELE B*4803). RX MEDLINE=99299758; PubMed=10372543; RX DOI=10.1034/j.1399-0039.1999.530504.x; RA Marcos C.Y., Fernandez-Vina M.A., Lazaro A.M., Moraes M.E., RA Moraes J.R., Stastny P.; RT "Novel HLA-A and HLA-B alleles in South American Indians."; RL Tissue Antigens 53:476-485(1999). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-48 are known: B*4801 and CC B*4803. The sequence shown is that of B*4801. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M84380; AAA59629.1; -; mRNA. DR EMBL; AJ309139; CAC38066.1; -; Genomic_DNA. DR EMBL; L76931; AAB59617.1; -; mRNA. DR PIR; I61903; I61903. DR HSSP; P30474; 1A9E. DR SMR; P30486; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR ArrayExpress; P30486; -. DR GermOnline; ENSG00000204523; Homo sapiens. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-48 alpha chain. FT /FTId=PRO_0000018851. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 121 121 S -> R (in allele B*4803). FT /FTId=VAR_016477. SQ SEQUENCE 362 AA; 40362 MW; 8FADC7B64EBD5C8D CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQISQRK LEAARVAEQL RAYLEGECVE WLRRYLENGK DKLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWTA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B49_HUMAN Reviewed; 362 AA. AC P30487; O19625; Q9MY37; Q9MY93; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 20-FEB-2007, entry version 55. DE HLA class I histocompatibility antigen, B-49 alpha chain precursor DE (MHC class I antigen B*49) (B-21). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*4901). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP SEQUENCE REVISION TO 78. RX MEDLINE=93056529; PubMed=1385528; RA Hildebrand W.H., Madrigal J.A., Belich M.P., Zemmour J., Ward F.E., RA Williams R.C., Parham P.; RT "Serologic cross-reactivities poorly reflect allelic relationships in RT the HLA-B12 and HLA-B21 groups. Dominant epitopes of the alpha 2 RT helix."; RL J. Immunol. 149:3563-3568(1992). RN [3] RP NUCLEOTIDE SEQUENCE OF 1-322 (ALLELE B*4901). RA Hurley C.K., Bei M., Rodriguez S., Johnson A.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*4902). RA Gans C.P., Hurley C.K.; RT "Novel HLA-B Allele."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*4903). RX MEDLINE=21442088; PubMed=11556975; RX DOI=10.1034/j.1399-0039.2001.057005478.x; RA Darke C., Street J., Guttridge M.G.; RT "Sequence, genetics and serology of a new HLA-B allele: B*4903."; RL Tissue Antigens 57:478-480(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-49 are known: B*4901, CC B*4902 and B*4903 (B*RA). The sequence shown is that of B*4901. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24037; AAA02950.1; -; Unassigned_DNA. DR EMBL; U11263; AAA19923.1; -; mRNA. DR EMBL; AF262959; AAF78054.1; -; Genomic_DNA. DR EMBL; AF262958; AAF78054.1; JOINED; Genomic_DNA. DR EMBL; AJ288980; CAB88084.1; -; Genomic_DNA. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P18464; 1E27. DR SMR; P30487; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-49 alpha chain. FT /FTId=PRO_0000018852. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 48 48 T -> A (in allele B*04903). FT /FTId=VAR_016512. FT VARIANT 56 56 L -> Q (in allele B*04903). FT /FTId=VAR_016513. FT VARIANT 65 65 T -> A (in allele B*04903). FT /FTId=VAR_016514. FT VARIANT 69 69 K -> T (in allele B*04903). FT /FTId=VAR_016515. FT VARIANT 104 104 I -> T (in allele B*04902). FT /FTId=VAR_016516. SQ SEQUENCE 362 AA; 40581 MW; 77B1C82AD3DAEB4A CRC64; MRVTAPRTVL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE NLRIALRYYN QSEAGSHTWQ RMYGCDLGPD GRLLRGYNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B50_HUMAN Reviewed; 362 AA. AC P30488; O19615; O19624; O19641; O19783; O46702; O78172; Q9TQG1; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 28-NOV-2006, entry version 54. DE HLA class I histocompatibility antigen, B-50 alpha chain precursor DE (MHC class I antigen B*50) (Bw-50) (B-21). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*5001). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP NUCLEOTIDE SEQUENCE OF 1-322 (ALLELE B*5001). RA Hurley C.K., Bei M., Rodriguez S., Johnson A.; RT "HLA-B71."; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5001). RA Ando H., Mizuki N., Ohno S., Inoko H.; RT "Identification of new HLA-B alleles among Greek population."; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5002). RX MEDLINE=97387736; PubMed=9243753; RA Vilches C., Bunce M., de Pablo R., Murray A.K., McIntyre C.A., RA Kreisler M.; RT "Complete coding regions of two novel HLA-B alleles detected by RT phototyping (PCR-SSP) in the British Caucasoid population: B*5108 and RT B*5002."; RL Tissue Antigens 50:38-41(1997). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELE B*5002). RA Balas A., Santos S., Vicario J.L.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*5002). RC TISSUE=Blood; RX MEDLINE=98357735; PubMed=9694362; RA Darke C., Guttridge M.G., Thompson J., Street J., Thomas M.; RT "Molecular, serological and population studies on a novel HLA-B allele RT -- HLA-B*5002."; RL Tissue Antigens 51:666-670(1998). RN [7] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5002). RC TISSUE=Blood; RA Gao X., Matheson B.; RT "A novel hla-b50 variant found in an Australian Caucasoid donor."; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5002). RA Steiner N.K., Hurley C.K.; RT "Novel HLA-B alleles."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5004). RX MEDLINE=21442089; PubMed=11556976; RX DOI=10.1034/j.1399-0039.2001.057005481.x; RA Steiner N.K., Kosman C., Jones P.F., Gans C.P., Rodriguez-Marino S.G., RA Rizzuto G., Baldassarre L.A., Edson S., Koester R., Sese D., RA Mitton W., Ng J., Hartzman R.J., Hurley C.K.; RT "Twenty-nine new HLA-B alleles associated with antigens in the 5C RT CREG."; RL Tissue Antigens 57:481-485(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-50 are known: B*5001, CC B*5002 (B*45ZJ; B50IM) and B*5004. The sequence shown is that of CC B*5001. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X61706; CAA43875.1; -; mRNA. DR EMBL; U11261; AAA19921.1; -; mRNA. DR EMBL; D50693; BAA23588.1; -; Genomic_DNA. DR EMBL; Y08995; CAA70199.1; -; mRNA. DR EMBL; AF006634; AAD01274.1; -; mRNA. DR EMBL; Y14205; CAA74596.1; -; Genomic_DNA. DR EMBL; U58318; AAB87724.1; -; Genomic_DNA. DR EMBL; U58317; AAB87724.1; JOINED; Genomic_DNA. DR EMBL; AF008927; AAB63511.1; -; Genomic_DNA. DR EMBL; AF008926; AAB63511.1; JOINED; Genomic_DNA. DR EMBL; AF136398; AAD34474.1; -; Genomic_DNA. DR EMBL; AF136397; AAD34474.1; JOINED; Genomic_DNA. DR PIR; I37520; I37520. DR HSSP; P30474; 1A9E. DR SMR; P30488; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-50 alpha chain. FT /FTId=PRO_0000018853. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Potential. FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 127 127 L -> V (in allele B*5004). FT /FTId=VAR_016517. FT VARIANT 191 191 W -> S (in allele B*5002). FT /FTId=VAR_016518. SQ SEQUENCE 362 AA; 40541 MW; 729B0736F81C4AB4 CRC64; MRVTAPRTVL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTWQ RMYGCDLGPD GRLLRGYNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B51_HUMAN Reviewed; 362 AA. AC P18464; O19675; O78173; P30489; Q29851; Q29857; Q96IT9; Q9MY43; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 20-FEB-2007, entry version 67. DE HLA class I histocompatibility antigen, B-51 alpha chain precursor DE (MHC class I antigen B*51). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5101). RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*5101). RX MEDLINE=89080265; PubMed=2909619; RA Hayashi H., Ennis P.D., Ariga H., Salter R.D., Parham P., Kano K., RA Takiguchi M.; RT "HLA-B51 and HLA-Bw52 differ by only two amino acids which are in the RT helical region of the alpha 1 domain."; RL J. Immunol. 142:306-311(1989). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE B*5101). RX MEDLINE=89233295; PubMed=2714852; RA Pohla H., Kuon W., Tabaczewski P., Doerner C., Weiss E.H.; RT "Allelic variation in HLA-B and HLA-C sequences and the evolution of RT the HLA-B alleles."; RL Immunogenetics 29:297-307(1989). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*5104). RX MEDLINE=92269955; PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*5103). RC TISSUE=Peripheral blood; RX MEDLINE=94069479; PubMed=8248893; RA Kawaguchi G., Nakayama S., Nagao T., Takiguchi M.; RT "A single amino acid substitution at residue 167 forms a novel HLA-B51 RT subtype."; RL Tissue Antigens 42:39-41(1993). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5102). RX MEDLINE=97083138; PubMed=8929712; RA Prilliman K., Steiner N.K., Ellexson M., Stewart D., Lau M., RA Terasaki P., Hurley C., Hildebrand W.H.; RT "Novel alleles HLA-B*7802 and B*51022: evidence for convergency in the RT HLA-B5 family."; RL Tissue Antigens 47:49-57(1996). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5108). RX MEDLINE=97387736; PubMed=9243753; RA Vilches C., Bunce M., de Pablo R., Murray A.K., McIntyre C.A., RA Kreisler M.; RT "Complete coding regions of two novel HLA-B alleles detected by RT phototyping (PCR-SSP) in the British Caucasoid population: B*5108 and RT B*5002."; RL Tissue Antigens 50:38-41(1997). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*5101). RX MEDLINE=21553639; PubMed=11696219; RX DOI=10.1034/j.1399-0039.2001.580202.x; RA Sano K., Yabuki K., Imagawa Y., Shiina T., Mizuki N., Ohno S., RA Kulski J.K., Inoko H.; RT "The absence of disease-specific polymorphisms within the HLA-B51 gene RT that is the susceptible locus for Behcet's disease."; RL Tissue Antigens 58:77-82(2001). RN [9] RP NUCLEOTIDE SEQUENCE (ALLELE B*5101). RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-206 (ALLELE B*5101). RX MEDLINE=95176330; PubMed=7871529; RA Steinle A., Schendel D.J.; RT "HLA class I alleles of LCL 721 and 174 x CEM.T2 (T2)."; RL Tissue Antigens 44:268-270(1994). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-362 (ALLELE B*5101). RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*5124). RC TISSUE=Peripheral blood; RX MEDLINE=21466687; PubMed=11580855; RX DOI=10.1034/j.1399-0039.2001.580107.x; RA Anholts J.D.H., Kemps-Mols B., Verduijn W., Oudshoorn M., RA Schreuder G.M.T.; RT "Three newly identified HLA-B alleles: B*5124, B*5306, B*5307 and RT confirmation of B*0809 and B*5606."; RL Tissue Antigens 58:38-41(2001). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-300 (B*5101). RX MEDLINE=20432310; PubMed=10975842; RA Maenaka K., Maenaka T., Tomiyama H., Takiguchi M., Stuart D.I., RA Jones E.Y.; RT "Nonstandard peptide binding revealed by crystal structures of HLA- RT B*5101 complexed with HIV immunodominant epitopes."; RL J. Immunol. 165:3260-3267(2000). RN [14] RP INVOLVEMENT IN BEHCET DISEASE. RX PubMed=15063364; DOI=10.1016/j.coph.2003.10.009; RA Arayssi T., Hamdan A.; RT "New insights into the pathogenesis and therapy of Behcet's disease."; RL Curr. Opin. Pharmacol. 4:183-188(2004). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-51 are known: B*5101, CC B*5103, B*5104, B*5108 and B*5124. The sequence shown is that of CC B*5101. CC -!- DISEASE: HLA-B51 is associated with Behcet disease but it is not CC certain whether HLA-B51 itself or a closely linked gene is CC responsible for susceptibility. About 20% of healthy individuals CC of various ethnic origin carries the HLA-B 51 locus, compared with CC 50 to 80% of patients. Behcet disease is a systemic disorder of CC recurrent acute inflammation characterized by 4 major symptoms: CC oral aphthous ulcers, skin lesions, ocular symptoms and genital CC ulcerations. Occasionally, inflammation in tissues and organs CC throughout the body can occur, including the gastrointestinal CC tract, central nervous system, vascular system, lungs, and CC kidneys. The etiology of Behcet disease is unclear. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M32319; AAA36232.1; -; mRNA. DR EMBL; M22792; AAA59620.1; ALT_SEQ; Genomic_DNA. DR EMBL; M22786; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; M22787; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; M22788; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; M22789; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; M22790; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; M22791; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; L41087; AAA64513.1; -; Genomic_DNA. DR EMBL; L41086; AAA64513.1; JOINED; Genomic_DNA. DR EMBL; Z15143; CAA78849.1; -; mRNA. DR EMBL; M80670; AAA52661.1; -; Genomic_DNA. DR EMBL; L41925; AAC41979.1; -; mRNA. DR EMBL; Y08994; CAA70198.1; -; mRNA. DR EMBL; AB056860; BAB64902.1; -; Genomic_DNA. DR EMBL; AB056862; BAB64904.1; -; Genomic_DNA. DR EMBL; AB056863; BAB64905.1; -; Genomic_DNA. DR EMBL; AB056864; BAB64906.1; -; Genomic_DNA. DR EMBL; AB056865; BAB64907.1; -; Genomic_DNA. DR EMBL; AJ278903; CAC05371.1; -; Genomic_DNA. DR EMBL; BC007243; AAH07243.1; -; mRNA. DR EMBL; AJ276995; CAB86196.1; -; Genomic_DNA. DR EMBL; Z46808; CAA86838.1; -; mRNA. DR PIR; A30345; A30345. DR PIR; I37120; I37120. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR PDB; 1E27; X-ray; A=25-300. DR PDB; 1E28; X-ray; A=25-300. DR DIP; DIP:6150N; -. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-51 alpha chain. FT /FTId=PRO_0000018854. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 118 121 TWQT -> IIQR (in allele B*5104). FT /FTId=VAR_016478. FT VARIANT 155 155 S -> R (in allele B*5124). FT /FTId=VAR_017442. FT VARIANT 176 176 E -> V (in allele B*5108). FT /FTId=VAR_016479. FT VARIANT 180 180 L -> D (in allele B*5108; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016480. FT VARIANT 191 191 W -> G (in allele B*5103). FT /FTId=VAR_016481. FT VARIANT 195 195 H -> Y (in allele B*5102). FT /FTId=VAR_016482. FT STRAND 27 36 FT TURN 39 40 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT TURN 244 245 FT HELIX 249 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40566 MW; D104163B4CC71F92 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE NLRIALRYYN QSEAGSHTWQ TMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRHLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B52_HUMAN Reviewed; 362 AA. AC P30490; Q9MY75; Q9TPT4; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 55. DE HLA class I histocompatibility antigen, B-52 alpha chain precursor DE (MHC class I antigen B*52) (Bw-52) (B-5). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*5201). RX MEDLINE=89080265; PubMed=2909619; RA Hayashi H., Ennis P.D., Ariga H., Salter R.D., Parham P., Kano K., RA Takiguchi M.; RT "HLA-B51 and HLA-Bw52 differ by only two amino acids which are in the RT helical region of the alpha 1 domain."; RL J. Immunol. 142:306-311(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*5202). RA Jones P.F., Hurley C.K.; RT "Novel HLA-B allele."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*5203). RA Gans C.P., Hurley C.K.; RT "Novel HLA-B allele."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-52 are known: B*5201, CC B*5202 (B*52012V) and B*5203. The sequence shown is that of CC B*5201. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M22799; AAA59645.1; ALT_SEQ; Genomic_DNA. DR EMBL; M22793; AAA59645.1; JOINED; Genomic_DNA. DR EMBL; M22794; AAA59645.1; JOINED; Genomic_DNA. DR EMBL; M22795; AAA59645.1; JOINED; Genomic_DNA. DR EMBL; M22796; AAA59645.1; JOINED; Genomic_DNA. DR EMBL; M22797; AAA59645.1; JOINED; Genomic_DNA. DR EMBL; M22798; AAA59645.1; JOINED; Genomic_DNA. DR EMBL; AF181845; AAF00933.1; -; Genomic_DNA. DR EMBL; AF181844; AAF00933.1; JOINED; Genomic_DNA. DR EMBL; AF281153; AAF81610.1; -; Genomic_DNA. DR EMBL; AF281152; AAF81610.1; JOINED; Genomic_DNA. DR PIR; B30345; B30345. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P18464; 1E27. DR SMR; P30490; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-52 alpha chain. FT /FTId=PRO_0000018855. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 69 70 TE -> MA (in allele B*5202). FT /FTId=VAR_016521. FT VARIANT 176 176 E -> V (in allele B*5203). FT /FTId=VAR_016522. FT VARIANT 195 195 H -> Y (in allele B*5203). FT /FTId=VAR_016523. SQ SEQUENCE 362 AA; 40521 MW; A32E36370FD84F91 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE NLRIALRYYN QSEAGSHTWQ TMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRHLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B53_HUMAN Reviewed; 362 AA. AC P30491; O78053; O78138; Q30198; Q9BD43; Q9GJF0; Q9MY42; Q9TP36; AC Q9TQH8; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 64. DE HLA class I histocompatibility antigen, B-53 alpha chain precursor DE (MHC class I antigen B*53) (Bw-53). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*5301). RX MEDLINE=91033941; PubMed=1699887; RA Hayashi H., Ooba T., Nakayama S., Sekimata M., Kano K., Takiguchi M.; RT "Allospecificities between HLA-Bw53 and HLA-B35 are generated by RT substitution of the residues associated with HLA-Bw4/Bw6 public RT epitopes."; RL Immunogenetics 32:195-199(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-206 (ALLELE B*5301). RC TISSUE=Blood; RX MEDLINE=98025078; PubMed=9321426; DOI=10.1007/s002510050307; RA Gomez-Casado E., Vargas-Alarcon G., Martinez-Laso J., Perez-Blas M., RA Granados J., Layrisse Z., Montoya F., Varela P., Arnaiz-Villena A.; RT "Generation of the HLA-B35, -B5, -B16, and B15 groups of alleles RT studied by intron 1 and 2 sequence analysis."; RL Immunogenetics 46:469-476(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*5302). RA Hurley C.K., Hoyer R.J.; RT "Human MHC class I antigen HLA-B*5302."; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES B*5303 AND RP B*5305). RX MEDLINE=21442089; PubMed=11556976; RX DOI=10.1034/j.1399-0039.2001.057005481.x; RA Steiner N.K., Kosman C., Jones P.F., Gans C.P., Rodriguez-Marino S.G., RA Rizzuto G., Baldassarre L.A., Edson S., Koester R., Sese D., RA Mitton W., Ng J., Hartzman R.J., Hurley C.K.; RT "Twenty-nine new HLA-B alleles associated with antigens in the 5C RT CREG."; RL Tissue Antigens 57:481-485(2001). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*5304). RX MEDLINE=20236861; PubMed=10777103; RX DOI=10.1034/j.1399-0039.2000.550311.x; RA Kennedy C.T., Dodd R., Le T., Wallace R., Ng G., Greville W.D., RA Kennedy A., Taverniti A., Moses J.H., Clow N., Watson N., Dunckley H.; RT "Routine HLA-B genotyping with PCR-sequence-specific oligonucleotides RT (PCR-SSO) detects eight new alleles: B*0807, B*0809, B*1551, B*3529, RT B*3532, B*4025, B*5304 and B*5508."; RL Tissue Antigens 55:266-270(2000). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*5305). RA Tait B., Holdsworth R., Cantwell L., Boyle A., Diviney M.; RT "Confirmatory B*5305 sequence."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES B*5306 AND RP B*5307). RC TISSUE=Peripheral blood; RX MEDLINE=21466687; PubMed=11580855; RX DOI=10.1034/j.1399-0039.2001.580107.x; RA Anholts J.D.H., Kemps-Mols B., Verduijn W., Oudshoorn M., RA Schreuder G.M.T.; RT "Three newly identified HLA-B alleles: B*5124, B*5306, B*5307 and RT confirmation of B*0809 and B*5606."; RL Tissue Antigens 58:38-41(2001). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-302. RX MEDLINE=96209672; PubMed=8624812; DOI=10.1016/S1074-7613(00)80430-6; RA Smith K.J., Reid S.W., Harlos K., McMichael A.J., Stuart D.I., RA Bell J.I., Jones E.Y.; RT "Bound water structure and polymorphic amino acids act together to RT allow the binding of different peptides to MHC class I HLA-B53."; RL Immunity 4:215-228(1996). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-53 are known: B*5301, CC B*5302, B*5303, B*5304, B*5305, B*5306 and B*5307. The sequence CC shown is that of B*5301. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M58636; AAA36228.1; -; Genomic_DNA. DR EMBL; U90566; AAB96793.1; -; Genomic_DNA. DR EMBL; U63562; AAB05926.1; -; Genomic_DNA. DR EMBL; U63561; AAB05926.1; JOINED; Genomic_DNA. DR EMBL; AF071770; AAC35939.1; -; Genomic_DNA. DR EMBL; AF071769; AAC35939.1; JOINED; Genomic_DNA. DR EMBL; AF198653; AAF20814.1; -; Genomic_DNA. DR EMBL; AF198652; AAF20814.1; JOINED; Genomic_DNA. DR EMBL; AF117773; AAD23461.1; -; Genomic_DNA. DR EMBL; AF117772; AAD23461.1; JOINED; Genomic_DNA. DR EMBL; AF304003; AAG53942.1; -; Genomic_DNA. DR EMBL; AF304002; AAG53942.1; JOINED; Genomic_DNA. DR EMBL; AJ276996; CAB86197.1; -; Genomic_DNA. DR EMBL; AJ293856; CAC05305.1; -; Genomic_DNA. DR EMBL; AJ293857; CAC05305.1; JOINED; Genomic_DNA. DR PIR; A45834; A45834. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR PDB; 1A1M; X-ray; A=25-300. DR PDB; 1A1O; X-ray; A=25-300. DR DIP; DIP:6054N; -. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR LinkHub; P30491; -. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-53 alpha chain. FT /FTId=PRO_0000018856. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 101 101 N -> D (in allele B*5303). FT /FTId=VAR_016524. FT VARIANT 101 101 N -> S (in allele B*5305). FT /FTId=VAR_016525. FT VARIANT 104 105 IA -> TL (in allele B*5303). FT /FTId=VAR_016526. FT VARIANT 118 118 I -> T (in allele B*5307). FT /FTId=VAR_016527. FT VARIANT 123 123 Y -> S (in allele B*5307). FT /FTId=VAR_016528. FT VARIANT 127 127 L -> V (in allele B*5307). FT /FTId=VAR_016529. FT VARIANT 137 138 HD -> YN (in allele B*5307). FT /FTId=VAR_016530. FT VARIANT 140 140 S -> F (in allele B*5304 and allele FT B*5307). FT /FTId=VAR_016531. FT VARIANT 176 176 V -> E (in allele B*5306). FT /FTId=VAR_016532. FT VARIANT 195 195 Y -> H (in allele B*5302 and allele FT B*5306). FT /FTId=VAR_016533. FT STRAND 27 36 FT TURN 39 40 FT STRAND 41 43 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 131 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 172 FT TURN 173 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT TURN 244 245 FT TURN 249 251 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40495 MW; 57BAA748D7854658 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE NLRIALRYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B54_HUMAN Reviewed; 362 AA. AC P30492; Q9TPQ9; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 55. DE HLA class I histocompatibility antigen, B-54 alpha chain precursor DE (MHC class I antigen B*54) (Bw-54) (Bw-22). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5401). RX MEDLINE=92148136; PubMed=1737933; RA Hildebrand W.H., Madrigal J.A., Little A.-M., Parham P.; RT "HLA-Bw22: a family of molecules with identity to HLA-B7 in the alpha RT 1-helix."; RL J. Immunol. 148:1155-1162(1992). RN [2] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5402). RA Juji T., Akesaka T., Kashiwase K., Ishikawa Y.; RT "HLA-B5401V1."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-54 are known: B*5401 and CC B*5402 (B5401V). The sequence shown is that of B*5401. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M77774; AAA03686.1; -; mRNA. DR EMBL; AB032095; BAA84114.1; -; Genomic_DNA. DR PIR; I56130; I56130. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P30474; 1A9E. DR SMR; P30492; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-54 alpha chain. FT /FTId=PRO_0000018857. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 33 33 Y -> H (in allele B*5402). FT /FTId=VAR_016534. FT VARIANT 35 36 AM -> SV (in allele B*5402). FT /FTId=VAR_016535. SQ SEQUENCE 362 AA; 40380 MW; 111730024578515D CRC64; MRVTAPRTLL LLLWGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTWQ TMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B55_HUMAN Reviewed; 362 AA. AC P30493; O78163; P30494; P79489; P79523; Q8MGQ3; Q9GIZ9; Q9GJ00; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 28-NOV-2006, entry version 54. DE HLA class I histocompatibility antigen, B-55 alpha chain precursor DE (MHC class I antigen B*55) (Bw-55) (B-12). GN Name=HLA-B; Synonyms=HLAB; ORFNames=CDABP0067; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*5501 AND B*5502). RX MEDLINE=92148136; PubMed=1737933; RA Hildebrand W.H., Madrigal J.A., Little A.-M., Parham P.; RT "HLA-Bw22: a family of molecules with identity to HLA-B7 in the alpha RT 1-helix."; RL J. Immunol. 148:1155-1162(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE B*5501). RC TISSUE=Leukemia; RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., RA Margolin J.F.; RT "Pediatric leukemia cDNA sequencing project."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ALLELES B*5501 AND B*5512). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5504). RC TISSUE=Blood; RX MEDLINE=97295817; PubMed=9151389; RA Bannai M., Tokunaga K., Tanaka H., Lin L., Kashiwase K., Tokunaga K., RA Juji T.; RT "Five HLA-B22 group alleles in Japanese."; RL Tissue Antigens 49:376-382(1997). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5505). RX MEDLINE=97316880; PubMed=9174154; RA Szmania S., Seurynck K., Baxter-Lowe L.A.; RT "Nucleotide sequence of HLA-B*5505, which expresses a unique HLA class RT I polymorphism."; RL Tissue Antigens 49:537-539(1997). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*5508). RX MEDLINE=20236861; PubMed=10777103; RX DOI=10.1034/j.1399-0039.2000.550311.x; RA Kennedy C.T., Dodd R., Le T., Wallace R., Ng G., Greville W.D., RA Kennedy A., Taverniti A., Moses J.H., Clow N., Watson N., Dunckley H.; RT "Routine HLA-B genotyping with PCR-sequence-specific oligonucleotides RT (PCR-SSO) detects eight new alleles: B*0807, B*0809, B*1551, B*3529, RT B*3532, B*4025, B*5304 and B*5508."; RL Tissue Antigens 55:266-270(2000). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*5509). RX MEDLINE=21466688; PubMed=11580856; RX DOI=10.1034/j.1399-0039.2001.580108.x; RA Voorter C.E., Hepkema B.G., Mulkers E.M.T., Lems S.P.M., RA van den Berg-Loonen E.M.; RT "Identification of two new HLA-B22 variants, HLA-B*5509 and B*5606."; RL Tissue Antigens 58:42-46(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-55 are known: B*5501, CC B*5502, B*5504 (B55.2), B*5505, B*5508 (B*ER), B*5509 and B*5512. CC The sequence shown is that of B*5501. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M77777; AAA03688.1; -; mRNA. DR EMBL; M77778; AAA03687.1; -; mRNA. DR EMBL; AY007140; AAG02001.1; -; mRNA. DR EMBL; AJ310509; CAC34574.1; -; Genomic_DNA. DR EMBL; AJ420106; CAD12250.1; -; Genomic_DNA. DR EMBL; AJ420333; CAD12454.1; -; Genomic_DNA. DR EMBL; D85761; BAA12868.1; -; mRNA. DR EMBL; U63653; AAB40126.1; -; mRNA. DR EMBL; AF091344; AAC61281.1; -; Genomic_DNA. DR EMBL; AF091343; AAC61281.1; JOINED; Genomic_DNA. DR EMBL; AJ250628; CAC12872.1; -; Genomic_DNA. DR EMBL; AJ250629; CAC12873.1; -; Genomic_DNA. DR PIR; I72752; I72752. DR PIR; I72753; I72753. DR HSSP; P30474; 1A9E. DR SMR; P30493; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-55 alpha chain. FT /FTId=PRO_0000018858. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 82 82 E -> A (in allele B*5505). FT /FTId=VAR_016483. FT VARIANT 101 101 S -> N (in allele B*5512). FT /FTId=VAR_016484. FT VARIANT 119 119 W -> L (in allele B*5504 and allele FT B*5508; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016698. FT VARIANT 121 121 T -> R (in allele B*5508). FT /FTId=VAR_016699. FT VARIANT 121 121 T -> S (in allele B*5504). FT /FTId=VAR_016700. FT VARIANT 127 127 L -> V (in allele B*5504 and allele FT B*5508). FT /FTId=VAR_016701. FT VARIANT 140 140 L -> Y (in allele B*5504 and allele FT B*5508). FT /FTId=VAR_016702. FT VARIANT 155 155 S -> R (in allele B*5504 and allele FT B*5508). FT /FTId=VAR_016703. FT VARIANT 176 176 E -> V (in allele B*5502, allele B*5504, FT allele B*5508 and allele B*5512). FT /FTId=VAR_016485. FT VARIANT 180 180 L -> R (in allele B*5509). FT /FTId=VAR_016704. FT VARIANT 187 187 T -> E (in allele B*5509; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016705. FT VARIANT 187 187 T -> L (in allele B*5508; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016706. SQ SEQUENCE 362 AA; 40496 MW; 8F3C1F6D245257C4 CRC64; MRVTAPRTLL LLLWGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTWQ TMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B56_HUMAN Reviewed; 362 AA. AC P30495; O19758; P30496; P79490; Q9GIM3; Q9GJ17; Q9TPR4; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 28-NOV-2006, entry version 54. DE HLA class I histocompatibility antigen, B-56 alpha chain precursor DE (MHC class I antigen B*56) (Bw-56) (Bw-22). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*5601 AND B*5602). RX MEDLINE=92148136; PubMed=1737933; RA Hildebrand W.H., Madrigal J.A., Little A.-M., Parham P.; RT "HLA-Bw22: a family of molecules with identity to HLA-B7 in the alpha RT 1-helix."; RL J. Immunol. 148:1155-1162(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5603). RC TISSUE=Blood; RX MEDLINE=97295817; PubMed=9151389; RA Bannai M., Tokunaga K., Tanaka H., Lin L., Kashiwase K., Tokunaga K., RA Juji T.; RT "Five HLA-B22 group alleles in Japanese."; RL Tissue Antigens 49:376-382(1997). RN [3] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5604). RA Steiner N.K., Lee K.W., Hurley C.K.; RT "Novel HLA-B alleles."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5605). RA Juji T., Akesaka T., Kashiwase K.; RT "HLA-B56V1(B*5605)."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*5606). RX MEDLINE=21466688; PubMed=11580856; RX DOI=10.1034/j.1399-0039.2001.580108.x; RA Voorter C.E., Hepkema B.G., Mulkers E.M.T., Lems S.P.M., RA van den Berg-Loonen E.M.; RT "Identification of two new HLA-B22 variants, HLA-B*5509 and B*5606."; RL Tissue Antigens 58:42-46(2001). RN [6] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5607). RX MEDLINE=20548613; PubMed=11098937; RX DOI=10.1034/j.1399-0039.2000.560409.x; RA Voorter C.E., van der Vlies S., Kik M., van den Berg-Loonen E.M.; RT "Unexpected Bw4 and Bw6 reactivity patterns in new alleles."; RL Tissue Antigens 56:363-370(2000). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-56 are known: B*5601, CC B*5602, B*5603 (B22N), B*5604, B*5605 (B56V1), B*5606 and B*5607. CC The sequence shown is that of B*5601. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M77775; AAA03690.1; -; mRNA. DR EMBL; M77776; AAA03689.1; -; mRNA. DR EMBL; D85762; BAA12869.1; -; mRNA. DR EMBL; U93914; AAB62223.1; -; Genomic_DNA. DR EMBL; U93913; AAB62223.1; JOINED; Genomic_DNA. DR EMBL; AB030574; BAA82677.1; -; Genomic_DNA. DR EMBL; Y18542; CAC12884.1; -; Genomic_DNA. DR EMBL; Y18543; CAC12884.1; JOINED; Genomic_DNA. DR EMBL; Y18544; CAC12896.1; -; Genomic_DNA. DR EMBL; Y18545; CAC12896.1; JOINED; Genomic_DNA. DR PIR; I72754; I72754. DR PIR; I72755; I72755. DR HSSP; P30474; 1A9E. DR SMR; P30495; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-56 alpha chain. FT /FTId=PRO_0000018859. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 69 69 E -> T (in allele B*5606; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016486. FT VARIANT 101 101 S -> N (in allele B*5607). FT /FTId=VAR_016487. FT VARIANT 104 107 NLRG -> TALR (in allele B*5607). FT /FTId=VAR_016488. FT VARIANT 119 119 W -> L (in allele B*5602, allele B*5603 FT and allele B*5604). FT /FTId=VAR_016489. FT VARIANT 121 121 T -> R (in allele B*5602, allele B*5603 FT and allele B*5604). FT /FTId=VAR_016490. FT VARIANT 127 127 L -> V (in allele B*5603, allele B*5604, FT allele B*5605 and allele B*5606). FT /FTId=VAR_016491. FT VARIANT 138 138 N -> D (in allele B*5603). FT /FTId=VAR_016707. FT VARIANT 140 140 L -> S (in allele B*5603). FT /FTId=VAR_016708. FT VARIANT 140 140 L -> Y (in allele B*5605 and allele FT B*5606; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016492. FT VARIANT 176 176 V -> E (in allele B*5603, allele B*5605 FT and allele B*5606). FT /FTId=VAR_016493. FT VARIANT 180 180 L -> W (in allele B*5603). FT /FTId=VAR_016709. FT VARIANT 195 195 Y -> H (in allele B*5605 and allele FT B*5606). FT /FTId=VAR_016494. SQ SEQUENCE 362 AA; 40478 MW; D442225B8A09D667 CRC64; MRVTAPRTLL LLLWGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTWQ TMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B57_HUMAN Reviewed; 362 AA. AC P18465; O62917; P30497; P79496; Q29679; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 20-FEB-2007, entry version 62. DE HLA class I histocompatibility antigen, B-57 alpha chain precursor DE (MHC class I antigen B*57) (Bw-57). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5701). RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*5701). RX MEDLINE=91067476; PubMed=2251138; DOI=10.1093/nar/18.22.6702; RA Isamat M., Girdlestone J., Milstein C.; RT "Nucleotide sequence of an HLA-Bw57 gene."; RL Nucleic Acids Res. 18:6702-6702(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5702). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [4] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5703). RC TISSUE=Blood; RA Petersdorf E.; RT "Molecular diversity of HLA-B."; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5703). RX MEDLINE=97378891; PubMed=9234488; RA Vilches C., Bunce M., de Pablo R., Moreno M.E., Puente S., Sanz L., RA Kreisler M.; RT "The novel HLA-Cw*1802 allele is associated with B*5703 in the Bubi RT population from Equatorial Guinea."; RL Tissue Antigens 49:644-648(1997). RN [6] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5705). RX MEDLINE=21442089; PubMed=11556976; RX DOI=10.1034/j.1399-0039.2001.057005481.x; RA Steiner N.K., Kosman C., Jones P.F., Gans C.P., Rodriguez-Marino S.G., RA Rizzuto G., Baldassarre L.A., Edson S., Koester R., Sese D., RA Mitton W., Ng J., Hartzman R.J., Hurley C.K.; RT "Twenty-nine new HLA-B alleles associated with antigens in the 5C RT CREG."; RL Tissue Antigens 57:481-485(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-57 are known: B*5701, CC B*5702 (Bw57.2), B*5703 (B-57SAU) and B*5705. The sequence shown CC is that of B*5701. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M32318; AAA36231.1; -; mRNA. DR EMBL; X55711; CAA39244.1; -; Genomic_DNA. DR EMBL; X61707; CAA43876.1; -; mRNA. DR EMBL; U18790; AAB60361.1; -; mRNA. DR EMBL; Y09157; CAA70355.1; -; mRNA. DR EMBL; AF061860; AAC32568.1; -; Genomic_DNA. DR EMBL; AF061859; AAC32568.1; JOINED; Genomic_DNA. DR PIR; D35997; D35997. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR PDB; 2BVO; X-ray; A=25-300. DR PDB; 2BVP; X-ray; A=25-300. DR PDB; 2BVQ; X-ray; A=25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-57 alpha chain. FT /FTId=PRO_0000018860. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 121 121 V -> R (in allele B*5705; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016669. FT VARIANT 127 127 V -> L (in allele B*5705). FT /FTId=VAR_016670. FT VARIANT 137 137 H -> Y (in allele B*5705). FT /FTId=VAR_016671. FT VARIANT 138 138 D -> N (in allele B*5702, allele B*5703 FT and allele B*5705). FT /FTId=VAR_016495. FT VARIANT 140 140 S -> Y (in allele B*5702, allele B*5703 FT and allele B*5705). FT /FTId=VAR_016496. FT VARIANT 180 180 L -> R (in allele B*5702 and allele FT B*5705). FT /FTId=VAR_016497. FT STRAND 27 36 FT TURN 39 40 FT STRAND 41 43 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 219 FT TURN 220 221 FT STRAND 222 235 FT STRAND 238 243 FT TURN 244 245 FT HELIX 249 251 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40224 MW; C1EFCF089096AFF9 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRMA PRAPWIEQEG PEYWDGETRN MKASAQTYRE NLRIALRYYN QSEAGSHIIQ VMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B58_HUMAN Reviewed; 362 AA. AC P10319; Q29925; Q9TP35; Q9TPS6; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 20-FEB-2007, entry version 64. DE HLA class I histocompatibility antigen, B-58 alpha chain precursor DE (MHC class I antigen B*58) (Bw-58). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*5801). RX MEDLINE=86008247; PubMed=2995352; RA Ways J.P., Coppin H.L., Parham P.; RT "The complete primary structure of HLA-Bw58."; RL J. Biol. Chem. 260:11924-11933(1985). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*5801). RC TISSUE=Blood; RA Inoue T., Ogawa A.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5802). RX MEDLINE=95282145; PubMed=7761977; RA Browning M.J., Madrigal J.A., Krausa P., Kowalski H., Allsopp C.E., RA Little A.-M., Turner S., Adams E.J., Arnett K.L., Bodmer W.F., RA Parham P.; RT "The HLA-A,B,C genotype of the class I negative cell line Daudi RT reveals novel HLA-A and -B alleles."; RL Tissue Antigens 45:177-187(1995). RN [4] RP NUCLEOTIDE SEQUENCE OF 1-206 (ALLELE B*5804). RX MEDLINE=22282374; PubMed=12392514; RX DOI=10.1034/j.1399-0039.2002.600210.x; RA Williams T.M., Wu J., Bassinger S., Feldman D., Birkos S., Kearns J., RA Kamoun M.; RT "New HLA-B alleles identified and sequences extended in potential bone RT marrow donors: B*5804, B*4418, B*1558, and B*4805."; RL Tissue Antigens 60:186-188(2002). RN [5] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*5805). RX MEDLINE=21442089; PubMed=11556976; RX DOI=10.1034/j.1399-0039.2001.057005481.x; RA Steiner N.K., Kosman C., Jones P.F., Gans C.P., Rodriguez-Marino S.G., RA Rizzuto G., Baldassarre L.A., Edson S., Koester R., Sese D., RA Mitton W., Ng J., Hartzman R.J., Hurley C.K.; RT "Twenty-nine new HLA-B alleles associated with antigens in the 5C RT CREG."; RL Tissue Antigens 57:481-485(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-58 are known: B*5801, CC B*5802, B*5804 and B*5805. The sequence shown is that of B*5801. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M11799; AAA59628.1; -; Genomic_DNA. DR EMBL; AB008102; BAA22916.1; -; mRNA. DR EMBL; L33923; AAA74406.1; -; mRNA. DR EMBL; AF189247; AAF04579.1; -; Genomic_DNA. DR EMBL; AF189245; AAF04579.1; JOINED; Genomic_DNA. DR EMBL; AF189246; AAF04579.1; JOINED; Genomic_DNA. DR EMBL; AF201475; AAF21438.1; -; Genomic_DNA. DR EMBL; AF201474; AAF21438.1; JOINED; Genomic_DNA. DR PIR; I84490; I84490. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P30474; 1A9E. DR SMR; P10319; 25-298. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-58 alpha chain. FT /FTId=PRO_0000018861. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 86 86 G -> E (in allele B*5804). FT /FTId=VAR_016498. FT VARIANT 118 119 II -> TL (in allele B*5802). FT /FTId=VAR_016499. FT VARIANT 121 121 R -> W (in allele B*5802). FT /FTId=VAR_016500. FT VARIANT 171 171 W -> L (in allele B*5805). FT /FTId=VAR_016666. FT VARIANT 176 176 V -> A (in allele B*5805). FT /FTId=VAR_016667. FT VARIANT 187 187 L -> T (in allele B*5805; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016668. SQ SEQUENCE 362 AA; 40337 MW; 2056116240BB9AC0 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDGETRN MKASAQTYRE NLRIALRYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B59_HUMAN Reviewed; 362 AA. AC Q29940; O02957; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 49. DE HLA class I histocompatibility antigen, B-59 alpha chain precursor DE (MHC class I antigen B*59). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5901). RX MEDLINE=93369833; PubMed=8362411; RA Hildebrand W.H., Domena J.D., Parham P.; RT "Primary structure shows HLA-B59 to be a hybrid of HLA-B55 and HLA- RT B51, and not a subtype of HLA-B8."; RL Tissue Antigens 41:190-195(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*5901). RC TISSUE=Blood; RA Lin L., Tokunaga K.; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; L07743; AAA59621.1; -; mRNA. DR EMBL; D50300; BAA08829.1; -; mRNA. DR PIR; I59633; I59633. DR HSSP; P18464; 1E27. DR SMR; Q29940; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-59 alpha chain. FT /FTId=PRO_0000018862. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 362 AA; 40584 MW; F07B384BC182A3B1 CRC64; MRVTAPRTLL LLLWGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE NLRIALRYYN QSEAGSHTWQ TMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B67_HUMAN Reviewed; 362 AA. AC Q29836; Q29678; Q8SNC5; Q95IA6; Q9BD38; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 51. DE HLA class I histocompatibility antigen, B-67 alpha chain precursor DE (MHC class I antigen B*67). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*6701). RX MEDLINE=94294981; PubMed=7517584; RA Little A.-M., Domena J.D., Hildebrand W.H., Shen S.Y., Barber L.D., RA Marsh S.G.E., Bias W.B., Parham P.; RT "HLA-B67: a member of the HLA-B16 family that expresses the ME1 RT epitope."; RL Tissue Antigens 43:38-43(1994). RN [2] RP NUCLEOTIDE SEQUENCE OF 26-205 (ALLELE B*6701). RC TISSUE=Blood; RA Petersdorf E.; RT "Molecular diversity of HLA-B."; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE B*6702). RA Iglehart B.A., Leffell M.S.; RT "HLA-B*6702 (Promoter-3'UTR)."; RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*6702). RA Baldassarre L.A., Hurley C.K.; RT "Novel HLA-B allele (HLA-B*67012 variant)."; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-67 are known: B*6701 (B- CC 67LAV) and B*6702. The sequence shown is that of B*6701. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; L17005; AAC37548.1; -; mRNA. DR EMBL; U18789; AAB60360.1; -; mRNA. DR EMBL; AF487379; AAL93257.1; -; Genomic_DNA. DR EMBL; AF321835; AAK09378.1; -; Genomic_DNA. DR EMBL; AF321834; AAK09378.1; JOINED; Genomic_DNA. DR EMBL; AY050196; AAL18235.1; -; Genomic_DNA. DR EMBL; AY050195; AAL18235.1; JOINED; Genomic_DNA. DR PIR; I59645; I59645. DR HSSP; P30474; 1A9E. DR SMR; Q29836; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR ArrayExpress; Q29836; -. DR GermOnline; ENSG00000204523; Homo sapiens. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-67 alpha chain. FT /FTId=PRO_0000018863. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 69 69 E -> G (in allele B*6702). FT /FTId=VAR_016536. FT VARIANT 76 76 I -> V (in allele B*6702). FT /FTId=VAR_016537. FT VARIANT 87 87 N -> E (in allele B*6702; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016538. FT VARIANT 90 90 I -> K (in allele B*6702). FT /FTId=VAR_016539. FT VARIANT 93 93 A -> R (in allele B*6702; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016540. FT VARIANT 97 97 T -> A (in allele B*6702). FT /FTId=VAR_016541. FT VARIANT 100 100 E -> V (in allele B*6702). FT /FTId=VAR_016542. SQ SEQUENCE 362 AA; 40342 MW; 3F6A17FC10230F70 CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RTYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B73_HUMAN Reviewed; 363 AA. AC Q31612; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 50. DE HLA class I histocompatibility antigen, B-73 alpha chain precursor DE (MHC class I antigen B*73). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*7301). RX MEDLINE=95026796; PubMed=7524186; RA Parham P., Arnett K.L., Adams E.J., Barber L.D., Domena J.D., RA Stewart D., Hildebrand W.H., Little A.-M.; RT "The HLA-B73 antigen has a most unusual structure that defines a RT second lineage of HLA-B alleles."; RL Tissue Antigens 43:302-313(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*7301). RX MEDLINE=94299292; PubMed=7517915; DOI=10.1007/BF00188185; RA Vilches C., de Pablo R., Herrero M.J., Moreno M.E., Kreisler M.; RT "HLA-B73: an atypical HLA-B molecule carrying a Bw6-epitope motif RT variant and a B pocket identical to HLA-B27."; RL Immunogenetics 40:166-166(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*7301). RX MEDLINE=96164742; PubMed=8547229; RA Hoffmann H.J., Kristensen T.J., Jensen T.G., Graugaard B., Lamm L.U.; RT "Antigenic characteristics and cDNA sequences of HLA-B73."; RL Eur. J. Immunogenet. 22:231-240(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*7301). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; U04787; AAA53175.1; -; mRNA. DR EMBL; X77658; CAA54739.1; -; mRNA. DR EMBL; L24373; AAA96733.1; -; mRNA. DR EMBL; AJ311601; CAC35319.2; -; Genomic_DNA. DR PIR; I37512; S42102. DR HSSP; Q29961; 1HSA. DR SMR; Q31612; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR ArrayExpress; Q31612; -. DR GermOnline; ENSG00000204523; Homo sapiens. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 363 HLA class I histocompatibility antigen, FT B-73 alpha chain. FT /FTId=PRO_0000018864. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 363 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT CONFLICT 338 339 SG -> C (in Ref. 4). SQ SEQUENCE 363 AA; 40435 MW; 04522E97C1E11C40 CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI CKAKAQTDRV GLRNLRGYYN QSEDGSHTWQ TMYGCDMGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRHLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL QEPCTLRWKP SSQSTIPIVG IVAGLAVLVV TVAVVAVVAA VMCRRKSSGG KGGSYSQAAS SDSAQGSDVS LTA // ID 1B78_HUMAN Reviewed; 362 AA. AC P30498; O62915; Q29924; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 56. DE HLA class I histocompatibility antigen, B-78 alpha chain precursor DE (MHC class I antigen B*78). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*7801). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*7801). RX MEDLINE=90217537; PubMed=1691230; RA Sekimata M., Hiraiwa M., Andrien M., Dupont E., Karaki S., RA Yamamoto J., Kano K., Takiguchi M.; RT "Allodeterminants and evolution of a novel HLA-B5 CREG antigen, HLA-B RT SNA."; RL J. Immunol. 144:3228-3233(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*7802). RX MEDLINE=97083138; PubMed=8929712; RA Prilliman K., Steiner N.K., Ellexson M., Stewart D., Lau M., RA Terasaki P., Hurley C., Hildebrand W.H.; RT "Novel alleles HLA-B*7802 and B*51022: evidence for convergency in the RT HLA-B5 family."; RL Tissue Antigens 47:49-57(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*7803). RX MEDLINE=21442089; PubMed=11556976; RX DOI=10.1034/j.1399-0039.2001.057005481.x; RA Steiner N.K., Kosman C., Jones P.F., Gans C.P., Rodriguez-Marino S.G., RA Rizzuto G., Baldassarre L.A., Edson S., Koester R., Sese D., RA Mitton W., Ng J., Hartzman R.J., Hurley C.K.; RT "Twenty-nine new HLA-B alleles associated with antigens in the 5C RT CREG."; RL Tissue Antigens 57:481-485(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-78 are known: B*7801 (B CC SNA), B*7802 and B*7803. The sequence shown is that of B*7801. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X61708; CAA43877.1; -; mRNA. DR EMBL; M33573; AAA59644.1; -; Genomic_DNA. DR EMBL; L41214; AAC41980.1; -; mRNA. DR EMBL; AF061856; AAC32566.1; -; Genomic_DNA. DR EMBL; AF061855; AAC32566.1; JOINED; Genomic_DNA. DR PIR; I37522; I37522. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; P18464; 1E27. DR SMR; P30498; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-78 alpha chain. FT /FTId=PRO_0000018865. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 91 91 F -> C (in allele B*7803). FT /FTId=VAR_016672. FT VARIANT 98 98 D -> Y (in allele B*7802). FT /FTId=VAR_016501. SQ SEQUENCE 362 AA; 40478 MW; D2D6142768F28E6C CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTDRE SLRNLRGYYN QSEAGSHTWQ TMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRHLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B81_HUMAN Reviewed; 362 AA. AC Q31610; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 54. DE HLA class I histocompatibility antigen, B-81 alpha chain precursor DE (MHC class I antigen B*81) (B'DT). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*8101). RX MEDLINE=96115676; PubMed=8847228; DOI=10.1016/0198-8859(95)00082-F; RA Ellexson M.E., Zhang G., Stewart D., Lau M., Teresi G., Terasaki P., RA Roe B.A., Hildebrand W.H.; RT "Nucleotide sequence analysis of HLA-B*1523 and B*8101. Dominant RT alpha-helical motifs produce complex serologic recognition patterns RT for the HLA-B''DT'' and HLA-B''NM5'' antigens."; RL Hum. Immunol. 44:103-110(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*8101). RX MEDLINE=97004417; PubMed=8851728; RA Vilches C., Sanz L., de Pablo R., Moreno M.E., Puente S., Kreisler M.; RT "Molecular characterization of the new alleles HLA-B*8101 and RT B*4407."; RL Tissue Antigens 47:139-142(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*8101). RA Hildebrand W.H., Ellexson M.E.; RT "HLA-B'DT', a class I allele most homologous with HLA-B-4801."; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; L37880; AAC41941.1; -; mRNA. DR EMBL; X90390; CAA62035.1; -; mRNA. DR EMBL; U09912; AAF70855.1; -; mRNA. DR UniGene; Hs.650454; -. DR UniGene; Hs.77961; -. DR HSSP; Q29961; 1HSA. DR SMR; Q31610; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR ArrayExpress; Q31610; -. DR GermOnline; ENSG00000204523; Homo sapiens. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-81 alpha chain. FT /FTId=PRO_0000018866. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 362 AA; 40400 MW; CB2660A583C8A0D8 CRC64; MLVMAPRTVL LLLWGAVALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQISQRK LEAARVAEQL RAYLEGECVE WLRRYLENGK DKLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWTA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B82_HUMAN Reviewed; 362 AA. AC Q29718; Q29695; Q29742; Q8MHN4; Q9MY61; Q9MYB8; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 28-NOV-2006, entry version 49. DE HLA class I histocompatibility antigen, B-82 alpha chain precursor DE (MHC class I antigen B*82). GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELE B*8201). RX MEDLINE=96303895; PubMed=8740766; RA Hurley C.K., Steiner N.K., Hoyer R.J., Menchaca E., Mitton W., RA Simonis T., Hartzman R.J., Johnson A.H., Ng J.; RT "Novel HLA-B alleles, B*8201, B*3515 and B*5106, add to the complexity RT of serologic identification of HLA types."; RL Tissue Antigens 47:179-187(1996). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*8201). RA Ellexson M.E., Hildebrand W.H.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE OF 1-24 (ALLELE B*8201). RA Blasczyk R.; RT "Exon 1 sequence of HLA-B*8201."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*8201). RA Chopek M., Nielsen J., Zhang H.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*8202). RX MEDLINE=20470604; PubMed=11019925; RX DOI=10.1034/j.1399-0039.2000.560216.x; RA Cox S.T., Hossain E., McWhinnie A., Prokupek B.M., Madrigal J.A., RA Little A.-M.; RT "HLA-B*8202 identified in a Caucasoid potential bone marrow donor."; RL Tissue Antigens 56:188-191(2000). RN [6] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*8202). RA Diviney M., Hepner J., Cantwell L., Boyle A., Kanaan C., RA Holdsworth R., Tait B.; RT "Confirmation of HLA-B*8202."; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-82 are known: B*8201 and CC B*8202. The sequence shown is that of B*8201. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; U36492; AAB18369.1; -; mRNA. DR EMBL; U29241; AAC50691.1; -; Genomic_DNA. DR EMBL; U38800; AAC99997.1; -; mRNA. DR EMBL; AJ278748; CAC00634.1; -; Genomic_DNA. DR EMBL; U43337; AAA87573.1; -; mRNA. DR EMBL; AJ251755; CAB75360.1; -; Genomic_DNA. DR EMBL; AF525410; AAM83101.1; -; Genomic_DNA. DR EMBL; AF525409; AAM83101.1; JOINED; Genomic_DNA. DR HSSP; P30474; 1A9E. DR SMR; Q29718; 25-300. DR Ensembl; ENSG00000198638; Homo sapiens. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR RZPD-ProtExp; I0319; -. DR RZPD-ProtExp; I0351; -. DR RZPD-ProtExp; I0434; -. DR RZPD-ProtExp; I0528; -. DR RZPD-ProtExp; IOH22114; -. DR RZPD-ProtExp; T2605; -. DR RZPD-ProtExp; T7420; -. DR RZPD-ProtExp; T7434; -. DR RZPD-ProtExp; U0344; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-82 alpha chain. FT /FTId=PRO_0000018867. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 186 186 D -> G (in allele B*8202). FT /FTId=VAR_016543. SQ SEQUENCE 362 AA; 40421 MW; 273D957D582B3673 CRC64; MRVTAPRTLL LLLWGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTLQ RMFGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQD RAYLEDLCVE SLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1C01_GORGO Reviewed; 365 AA. AC P30383; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 46. DE Class I histocompatibility antigen, GOGO-C0101/C0102 alpha chain DE precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60252; CAA42804.1; -; mRNA. DR EMBL; X60250; CAA42802.1; -; mRNA. DR PIR; JH0544; JH0544. DR HSSP; P30504; 1QQD. DR SMR; P30383; 25-302. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 365 Class I histocompatibility antigen, GOGO- FT C0101/C0102 alpha chain. FT /FTId=PRO_0000018905. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40938 MW; 0DAC1859620B778F CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFFTAVAPPG RGEPRFIAVG YVDDTQFVRF DSDAANTRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRKLRGYYN QSEDGSHTFQ RMYGCDVGPD GRLQRGYDQL AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARWAERQ RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEEQTQ DIELVETRPA GDGTFQKWAA MVVPSGEEQR YTCHVQHKGL LEPLTLRWEP SSQPTIPIVG IVAGLAVLAV VFTGTVVAAV MCRRKSSGGK GGSCSQAACS NSAQGSDESL IACKA // ID 1C01_HUMAN Reviewed; 366 AA. AC P30499; O02865; O19676; P30500; Q29986; Q9UQS9; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 58. DE HLA class I histocompatibility antigen, Cw-1 alpha chain precursor DE (MHC class I antigen Cw*1). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0101). RX MEDLINE=89215297; PubMed=2708822; RA Ellis S.A., Strachan T., Palmer M.S., McMichael A.J.; RT "Complete nucleotide sequence of a unique HLA class I C locus product RT expressed on the human choriocarcinoma cell line BeWo."; RL J. Immunol. 142:3281-3285(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE CW*0102). RX MEDLINE=87192941; PubMed=3032784; DOI=10.1007/BF00404424; RA Gussow D., Rein R.S., Meijer I., de Hoog W., Seemann G.H., RA Hochstenbach F.M., Ploegh H.L.; RT "Isolation, expression, and the primary structure of HLA-Cw1 and HLA- RT Cw2 genes: evolutionary aspects."; RL Immunogenetics 25:313-322(1987). RN [3] RP ERRATUM. RA Gussow D., Rein R.S., Meijer I., de Hoog W., Seemann G.H., RA Hochstenbach F.M., Ploegh H.L.; RL Immunogenetics 27:158-158(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0102). RX MEDLINE=93031775; PubMed=1384166; RA Zemmour J., Gumperz J.E., Hildebrand W.H., Ward F.E., Marsh S.G.E., RA Williams R.C., Parham P.; RT "The molecular basis for reactivity of anti-Cw1 and anti-Cw3 RT alloantisera with HLA-B46 haplotypes."; RL Tissue Antigens 39:249-257(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-206 (ALLELE CW*0102). RX MEDLINE=95176330; PubMed=7871529; RA Steinle A., Schendel D.J.; RT "HLA class I alleles of LCL 721 and 174 x CEM.T2 (T2)."; RL Tissue Antigens 44:268-270(1994). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0103). RC TISSUE=Peripheral blood; RX MEDLINE=98335880; PubMed=9672159; RA Wang H., Nakajima F., Tokunaga K., Kashiwase K., Ishikawa Y., Juji T.; RT "Cw*0103, a new allele encoding for a novel HLA-Cw1 split in the RT Japanese population."; RL Tissue Antigens 51:571-573(1998). RN [7] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0104). RA Day S.; RT "Full length sequencing of a new Cw*01 variant allele."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-1 are known: Cw*0101 CC (Cw1.1), Cw*0102 (Cw1.2), Cw*0103 and Cw*0104. The sequence shown CC is that of Cw*0101. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M26429; AAA59701.1; -; mRNA. DR EMBL; M16272; AAA59700.1; -; Genomic_DNA. DR EMBL; M84171; AAA59685.1; -; mRNA. DR EMBL; Z46809; CAA86839.1; -; mRNA. DR EMBL; D64145; BAA19531.1; -; mRNA. DR EMBL; AJ133100; CAB38942.1; -; Genomic_DNA. DR PIR; I37528; I37528. DR PIR; I54430; I54430. DR PIR; I59622; I59622. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1QQD. DR SMR; P30499; 26-302. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-1 alpha chain. FT /FTId=PRO_0000018868. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 5 5 E -> A (in allele Cw*0102, allele CW*0103 FT and allele CW*0104). FT /FTId=VAR_016544. FT VARIANT 92 92 N -> K (in allele Cw*0102, allele CW*0103 FT and allele CW*0104). FT /FTId=VAR_016545. FT VARIANT 138 138 D -> N (in allele CW*0103). FT /FTId=VAR_016546. FT VARIANT 140 140 Y -> F (in allele CW*0103). FT /FTId=VAR_016547. FT VARIANT 140 140 Y -> S (in allele CW*0104). FT /FTId=VAR_016548. FT VARIANT 179 179 E -> Q (in allele Cw*0102, allele Cw*0103 FT and allele CW*0104). FT /FTId=VAR_016549. FT VARIANT 180 180 R -> W (in allele Cw*0104). FT /FTId=VAR_016550. FT VARIANT 202 202 S -> T (in allele Cw*0102, allele CW*0103 FT and allele CW*0104). FT /FTId=VAR_016551. FT VARIANT 243 243 W -> R (in allele CW*0104). FT /FTId=VAR_016552. FT VARIANT 272 272 M -> V (in allele CW*0104). FT /FTId=VAR_016553. FT VARIANT 328 328 V -> M (in allele CW*0104). FT /FTId=VAR_016554. FT VARIANT 364 364 S -> C (in allele Cw*0102, allele CW*0103 FT and allele CW*0104). FT /FTId=VAR_016555. SQ SEQUENCE 366 AA; 40965 MW; 285CCFCB92788744 CRC64; MRVMEPRTLI LLLSGALALT ETWACSHSMK YFFTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YNRQAQTDRV SLRNLRGYYN QSEAGSHTLQ WMCGCDLGPD GRLLRGYDQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEER RAYLEGTCVE WLRRYLENGK ESLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VMVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIASKA // ID 1C01_PANTR Reviewed; 366 AA. AC P30686; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 45. DE CHLA class I histocompatibility antigen, C alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92391104; PubMed=1381540; RA Kato T., Esumi M., Yamashita S., Abe K., Shikata T.; RT "Interferon-inducible gene expression in chimpanzee liver infected RT with hepatitis C virus."; RL Virology 190:856-860(1992). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; D11383; BAA01979.1; ALT_INIT; mRNA. DR HSSP; P30504; 1IM9. DR SMR; P30686; 25-302. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 366 CHLA class I histocompatibility antigen, FT C alpha chain. FT /FTId=PRO_0000018914. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 192 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 366 AA; 40843 MW; 58B25703B3D82C4D CRC64; MRVTAPRTLL LLLSGGLALT ETWAGSHSLR YFDTAVSRPG RREPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV SLRNLRGYYN QSEDGSHTLQ WMYGCDLGPD GRLLRGYGQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQL RAYLEGKRVE SCRRYLENGK ETLQRTECPK THMTHHPVSD HEATLRCWAL AFYPAEITLT WQRDGEDQIQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PEPLTLRWKP TSQPTIPIVG IVAGLAVLAV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LIACKA // ID 1C01_SAGOE Reviewed; 365 AA. AC P30517; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 46. DE Class I histocompatibility antigen, C alpha chain precursor. OS Saguinus oedipus (Cotton-top tamarin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Saguinus. OX NCBI_TaxID=9490; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90111120; PubMed=2104912; RA Watkins D.I., Letvin N.L., Hughes A.L., Tedder T.F.; RT "Molecular cloning of cDNA that encode MHC class I molecules from a RT New World primate (Saguinus oedipus). Natural selection acts at RT positions that may affect peptide presentation to T cells."; RL J. Immunol. 144:1136-1143(1990). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M33477; AAA36953.1; -; mRNA. DR PIR; I72218; I72218. DR HSSP; P30504; 1QQD. DR SMR; P30517; 25-298. DR ArrayExpress; P30517; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 365 Class I histocompatibility antigen, C FT alpha chain. FT /FTId=PRO_0000018922. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 365 AA; 40829 MW; D6A0F974104BA1EE CRC64; MTIMAPRTLL LLLSGALSVT ETWAGSHSMR YFSTTVSRPG RGEPRYIEVG YVDDTQFVRF DSDAASPRME PRAPWVEQEG PEYWVLQTRN SKASAQTFRV NLQTLLGYYN QSEAGFHTIQ WMYGCDLGPD GRLLRGYHQY AYDGKDYIAL NEDLRSWTAA DAAAQITQRK WAEANAAEGM RAYLEGTCVE WLRRHLENGK EMLQRAEPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQAQ DMELVETRPT GNGTFQKWAA VVVLSGEEHK YTCHVQHEGL PEPFTLRWEP PSQPTIPIMG IVAILAILGA VVTGAVVAAV MWRKKSSDKK GGSYSQAARS DSAQGSDVSL TACKV // ID 1C02_GORGO Reviewed; 366 AA. AC P30385; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 47. DE Class I histocompatibility antigen, GOGO-C0201 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60251; CAA42803.1; -; mRNA. DR PIR; JH0545; JH0545. DR HSSP; P30504; 1QQD. DR SMR; P30385; 25-302. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. KW Glycoprotein; Immune response; Membrane; MHC I; Phosphorylation; KW Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 366 Class I histocompatibility antigen, GOGO- FT C0201 alpha chain. FT /FTId=PRO_0000018906. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT MOD_RES 83 83 Phosphotyrosine (By similarity). FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 366 AA; 40954 MW; 05E159364C769FC5 CRC64; MRVMAPRTLI LPLSGALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV NLRKLRGYYN QSEDGSHTLQ SMYGCDLGPD GRLLRGYSQF AYDGKDYIAL NEDLRSWTAA DTAAQVTQRK WEAARVAEQE RAYLEGLCVE WLRRYLENGK ETLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL PEPLTLRWEP SSQPTIPIVG IVVGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LITCKA // ID 1C02_HUMAN Reviewed; 366 AA. AC P30501; P30502; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 58. DE HLA class I histocompatibility antigen, Cw-2 alpha chain precursor DE (MHC class I antigen Cw*2). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0201). RX MEDLINE=89215297; PubMed=2708822; RA Ellis S.A., Strachan T., Palmer M.S., McMichael A.J.; RT "Complete nucleotide sequence of a unique HLA class I C locus product RT expressed on the human choriocarcinoma cell line BeWo."; RL J. Immunol. 142:3281-3285(1989). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0202). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83, AND MASS RP SPECTROMETRY. RX PubMed=16097034; DOI=10.1002/pmic.200401217; RA Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., RA Demol H., Martens L., Goethals M., Vandekerckhove J.; RT "Global phosphoproteome analysis on human HepG2 hepatocytes using RT reversed-phase diagonal LC."; RL Proteomics 5:3589-3599(2005). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-2 are known: Cw*0201 CC (Cw2.1) and Cw*0202 (Cw2.2). The sequence shown is that of CC Cw*0201. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M26430; AAA59703.1; -; mRNA. DR EMBL; M24030; AAA59671.1; -; Genomic_DNA. DR PIR; I61866; I61866. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1IM9. DR SMR; P30501; 26-302. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Phosphorylation; Polymorphism; Signal; Transmembrane; KW Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-2 alpha chain. FT /FTId=PRO_0000018869. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT MOD_RES 83 83 Phosphotyrosine. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 5 5 E -> A (in allele Cw*0202). FT /FTId=VAR_016556. FT VARIANT 10 10 I -> L (in allele Cw*0202). FT /FTId=VAR_016557. FT VARIANT 73 74 GR -> AP (in allele Cw*0202). FT /FTId=VAR_016558. FT VARIANT 92 92 N -> K (in allele Cw*0202). FT /FTId=VAR_016559. FT VARIANT 179 179 E -> Q (in allele Cw*0202). FT /FTId=VAR_016560. FT VARIANT 202 202 K -> T (in allele Cw*0202). FT /FTId=VAR_016561. FT VARIANT 364 364 S -> C (in allele Cw*0202). FT /FTId=VAR_016562. SQ SEQUENCE 366 AA; 41095 MW; AD8025DEB7DA8CE6 CRC64; MRVMEPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPS RGEPHFIAVG YVDDTQFVRF DSDAASPRGE PRGRWVEQEG PEYWDRETQK YNRQAQTDRV NLRKLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEEW RAYLEGECVE WLRRYLENGK EKLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPTEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIASKA // ID 1C03_GORGO Reviewed; 366 AA. AC P30386; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 44. DE Class I histocompatibility antigen, GOGO-C0202 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60249; CAA42801.1; -; mRNA. DR PIR; JH0546; JH0546. DR HSSP; P30504; 1IM9. DR SMR; P30386; 25-302. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 366 Class I histocompatibility antigen, GOGO- FT C0202 alpha chain. FT /FTId=PRO_0000018907. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 366 AA; 40783 MW; 11CCAD1F6091831B CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV NLRKLRGYYN QSEDGSHTLQ SMYGCDLGPD GRLLRGYSQF AYDGKDYIAL NEDLRSWTAA DTAAQITQRK LEAARAAEQQ RAYLEGLCVE SLRRYLENGK ETLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL PEPLTLRWEP SSQPTIPIVG IVVGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LITCKA // ID 1C03_HUMAN Reviewed; 366 AA. AC P04222; O62883; O78060; O78068; O78069; P30503; Q29743; Q29992; AC Q29993; Q9GIK8; Q9TQB4; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 20-FEB-2007, entry version 65. DE HLA class I histocompatibility antigen, Cw-3 alpha chain precursor DE (MHC class I antigen Cw*3). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0304). RX MEDLINE=84207947; PubMed=6609813; RA Sodoyer R., Damotte M., Delovitch T.L., Trucy J., Jordan B.R., RA Strachan T.; RT "Complete nucleotide sequence of a gene encoding a functional human RT class I histocompatibility antigen (HLA-CW3)."; RL EMBO J. 3:879-885(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0302). RX MEDLINE=93031775; PubMed=1384166; RA Zemmour J., Gumperz J.E., Hildebrand W.H., Ward F.E., Marsh S.G.E., RA Williams R.C., Parham P.; RT "The molecular basis for reactivity of anti-Cw1 and anti-Cw3 RT alloantisera with HLA-B46 haplotypes."; RL Tissue Antigens 39:249-257(1992). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELES CW*0303 AND CW*0304). RA Domena J.D.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0303). RC TISSUE=Peripheral blood; RA Wang H., Tokunaga K., Kuwata S.; RT "DNA typing of HLA-C locus alleles in Japanese."; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-206 (ALLELE CW*0304). RX MEDLINE=96217561; PubMed=8613148; DOI=10.1007/s002510050093; RA Zarling A.L., Smith K.D., Lutz C.T., Lee D.R.; RT "Correction of the HLA-Cw3 genomic sequence tentatively identifies it RT as HLA-Cw*0304."; RL Immunogenetics 44:82-83(1996). RN [6] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE CW*0307). RA Balas A., Santos S., Vicario J.L.; RT "Sequencing of a new HLA-C allele."; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES CW*0305; CW*0306; RP CW*0308 AND CW*0309). RX MEDLINE=98349393; PubMed=9686604; RA Turner S., Ellexson M.E., Hickman H.D., Sidebottom D.A., RA Fernandez-Vina M., Confer D.L., Hildebrand W.H.; RT "Sequence-based typing provides a new look at HLA-C diversity."; RL J. Immunol. 161:1406-1413(1998). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE CW*0313). RX MEDLINE=21970278; PubMed=11972880; RX DOI=10.1034/j.1399-0039.2002.590110.x; RA Cox S.T., Ogilvie H., Bohan E.M., Holman R., Prentice H.G., Potter M., RA Madrigal J.A., Little A.-M.; RT "Sequence of two new HLA-Cw alleles: HLA-Cw*0313 and HLA-Cw*1208."; RL Tissue Antigens 59:49-51(2002). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-3 are known: Cw*0302 CC (Cw3.2), Cw*0303, Cw*0304 (Cw3.1), Cw*0305, Cw*0306, Cw*0307, CC Cw*0308, Cw*0309 and Cw*0313. The sequence shown is that of CC Cw*0304. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X00495; CAA25190.1; -; Genomic_DNA. DR EMBL; M84172; AAA59686.1; -; mRNA. DR EMBL; M99389; AAA88088.1; -; mRNA. DR EMBL; M99390; AAA88089.1; -; mRNA. DR EMBL; D50853; BAA32610.1; -; mRNA. DR EMBL; U44064; AAB02773.1; -; Genomic_DNA. DR EMBL; AF039198; AAD37816.1; -; Genomic_DNA. DR EMBL; AF037079; AAC17715.1; -; Genomic_DNA. DR EMBL; AF037078; AAC17715.1; JOINED; Genomic_DNA. DR EMBL; AF003284; AAC17716.1; -; Genomic_DNA. DR EMBL; AF003283; AAC17716.1; JOINED; Genomic_DNA. DR EMBL; AF037075; AAC17717.1; -; Genomic_DNA. DR EMBL; AF037074; AAC17717.1; JOINED; Genomic_DNA. DR EMBL; AF037077; AAC17718.1; -; Genomic_DNA. DR EMBL; AF037076; AAC17718.1; JOINED; Genomic_DNA. DR EMBL; AJ298116; CAC18746.1; -; Genomic_DNA. DR PIR; A02190; HLHUW3. DR PIR; I81231; I81231. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR PDB; 1EFX; X-ray; A=25-302. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-3 alpha chain. FT /FTId=PRO_0000018870. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 90 90 K -> N (in allele Cw*0308). FT /FTId=VAR_016569. FT VARIANT 101 101 S -> N (in allele Cw*0307). FT /FTId=VAR_016565. FT VARIANT 104 104 N -> K (in allele Cw*0307). FT /FTId=VAR_016566. FT VARIANT 115 115 G -> R (in allele Cw*0303 and allele FT Cw*0313). FT /FTId=VAR_016563. FT VARIANT 118 118 I -> T (in allele Cw*0305 and allele FT Cw*0313). FT /FTId=VAR_016564. FT VARIANT 119 119 I -> L (in allele Cw*0302, allele Cw*0305 FT and allele Cw*0313). FT /FTId=VAR_016567. FT VARIANT 121 121 R -> S (in allele Cw*0305). FT /FTId=VAR_016617. FT VARIANT 127 127 V -> L (in allele Cw*0309). FT /FTId=VAR_016618. FT VARIANT 138 138 D -> V (in allele Cw*0306). FT /FTId=VAR_016619. FT VARIANT 140 140 Y -> S (in allele Cw*0302). FT /FTId=VAR_016568. FT CONFLICT 33 33 Y -> C (in Ref. 1). FT CONFLICT 64 65 AA -> DE (in Ref. 1). FT CONFLICT 78 79 QE -> RK (in Ref. 1). FT CONFLICT 93 93 R -> P (in Ref. 1). FT CONFLICT 140 140 Y -> H (in Ref. 1). FT CONFLICT 161 161 D -> N (in Ref. 1). FT CONFLICT 205 205 R -> G (in Ref. 1). FT STRAND 28 36 FT TURN 39 41 FT STRAND 42 43 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT STRAND 69 71 FT STRAND 73 73 FT HELIX 74 77 FT STRAND 78 79 FT HELIX 81 108 FT TURN 109 110 FT STRAND 113 114 FT STRAND 118 128 FT TURN 129 130 FT STRAND 131 150 FT TURN 152 153 FT STRAND 154 155 FT STRAND 157 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 205 205 FT STRAND 210 216 FT STRAND 219 219 FT TURN 220 221 FT STRAND 222 235 FT STRAND 238 243 FT TURN 244 245 FT STRAND 246 247 FT TURN 249 251 FT STRAND 253 254 FT STRAND 258 259 FT STRAND 261 263 FT STRAND 265 266 FT STRAND 268 274 FT TURN 275 276 FT HELIX 277 280 FT STRAND 281 286 FT STRAND 288 289 FT STRAND 291 292 FT STRAND 294 296 SQ SEQUENCE 366 AA; 40861 MW; 47E55680EA1F6D97 CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFYTAVSRPG RGEPHFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHIIQ RMYGCDVGPD GRLLRGYDQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRYLKNGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C04_GORGO Reviewed; 366 AA. AC P30387; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 46. DE Class I histocompatibility antigen, GOGO-C0203 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60248; CAA42800.1; -; mRNA. DR PIR; JH0547; JH0547. DR HSSP; P30504; 1QQD. DR SMR; P30387; 25-302. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 366 Class I histocompatibility antigen, GOGO- FT C0203 alpha chain. FT /FTId=PRO_0000018908. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 366 AA; 40970 MW; EE962C8189CAC001 CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV NLRKLRGYYN QSEDGSHTLQ SMYGCDLGPD GRLLRGYSQF AYDGKDYIAL NEDLRSWTAA DTAAQVTQRK WEAARVAEQE RAYLEGLCVE WLRRYLENGK ETLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL PEPLTLRWEP SSQPTIPIVG IVVGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LITCKA // ID 1C04_HUMAN Reviewed; 366 AA. AC P30504; O78067; O78072; O78090; O78149; Q29921; Q9UM42; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 60. DE HLA class I histocompatibility antigen, Cw-4 alpha chain precursor DE (MHC class I antigen Cw*4). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0401). RX MEDLINE=92269955; PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0401). RX MEDLINE=91277627; PubMed=1711567; DOI=10.1084/jem.174.1.53; RA Grassi F., Meneveri R., Gullberg M., Lopalco L., Rossi G.B., Lanza P., RA de Santis C., Brattsand G., Butto S., Ginelli E., Beretta A., RA Siccardi A.G.; RT "Human immunodeficiency virus type 1 gp120 mimics a hidden monomorphic RT epitope borne by class I major histocompatibility complex heavy RT chains."; RL J. Exp. Med. 174:53-62(1991). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0401). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [4] RP NUCLEOTIDE SEQUENCE OF 1-365 (ALLELE CW*0401). RA Dunn P.P., van Dam M., Crosby I., Carter V.; RT "A sequencing strategy for the rapid sequencing of HLA class I genes RT using random in vitro DNA transposition."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0403). RC TISSUE=B-cell; RX MEDLINE=97037653; PubMed=8883300; RA Little A.-M., Mason A., Marsh S.G.E., Parham P.; RT "HLA-C typing of eleven Papua New Guineans: identification of an HLA- RT Cw4/Cw2 hybrid allele."; RL Tissue Antigens 48:113-117(1996). RN [6] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES CW*0404 AND CW*0405). RX MEDLINE=98349393; PubMed=9686604; RA Turner S., Ellexson M.E., Hickman H.D., Sidebottom D.A., RA Fernandez-Vina M., Confer D.L., Hildebrand W.H.; RT "Sequence-based typing provides a new look at HLA-C diversity."; RL J. Immunol. 161:1406-1413(1998). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE CW*0406). RX MEDLINE=99189031; PubMed=10090622; RX DOI=10.1034/j.1399-0039.1999.530212.x; RA Ren E.C., Haniff F., Loh M.T., Chan S.H., Petersdorf E., Hansen J.; RT "Identification of a novel HLA-C allele, Cw*0406, in a Singapore RT Malay."; RL Tissue Antigens 53:198-200(1999). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE CW*0406). RX MEDLINE=99321038; PubMed=10395115; RX DOI=10.1034/j.1399-0039.1999.530615.x; RA Carbonnelle E., Poirier J.C., Fortier C., Marzais F., Visser C.J.T., RA Borie C., Toubert A., Raffoux C., Charron D., Tamouza R.; RT "Characterization of a novel HLA-Cw*04 variant in a Laotian family: RT HLA-Cw*0406."; RL Tissue Antigens 53:601-603(1999). RN [9] RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I. RX PubMed=11390610; DOI=10.1128/JVI.75.13.6086-6094.2001; RA Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L., RA Mulloy J.C., Jacobson S., Franchini G.; RT "Free major histocompatibility complex class I heavy chain is RT preferentially targeted for degradation by human T-cell RT leukemia/lymphotropic virus type 1 p12(I) protein."; RL J. Virol. 75:6086-6094(2001). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). Interacts with HTLV-1 p12I accessory protein. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-4 are known: Cw*0401 CC Cw*0403, Cw*0404, Cw*0405 and Cw*0406. The sequence shown is that CC of Cw*0401. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M84386; AAA59705.1; -; mRNA. DR EMBL; X58536; CAA41427.1; -; mRNA. DR EMBL; AJ278494; CAB95011.1; -; Genomic_DNA. DR EMBL; AJ238694; CAB41889.2; -; Genomic_DNA. DR EMBL; L54059; AAB04639.1; -; Genomic_DNA. DR EMBL; U96787; AAC17719.1; -; Genomic_DNA. DR EMBL; U96786; AAC17719.1; JOINED; Genomic_DNA. DR EMBL; AF036557; AAC17720.1; -; Genomic_DNA. DR EMBL; AF036556; AAC17720.1; JOINED; Genomic_DNA. DR EMBL; AF076476; AAC27626.1; -; Genomic_DNA. DR EMBL; AF062588; AAC16245.1; -; Genomic_DNA. DR EMBL; AF062587; AAC16245.1; JOINED; Genomic_DNA. DR PIR; A59028; A59028. DR PIR; JH0526; JH0526. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR PDB; 1IM9; X-ray; A/E=25-299. DR PDB; 1QQD; X-ray; A=26-298. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Host-virus interaction; Immune response; KW Membrane; MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-4 alpha chain. FT /FTId=PRO_0000018871. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 33 33 S -> Y (in allele Cw*0403 and allele FT Cw*0406). FT /FTId=VAR_016571. FT VARIANT 35 35 S -> A (in allele Cw*0403 and allele FT Cw*0406). FT /FTId=VAR_016572. FT VARIANT 38 38 W -> R (in allele Cw*0403 and allele FT Cw*0406). FT /FTId=VAR_016573. FT VARIANT 40 40 G -> S (in allele Cw*0403 and allele FT Cw*0406). FT /FTId=VAR_016574. FT VARIANT 45 45 R -> H (in allele Cw*0403 and allele FT Cw*0406). FT /FTId=VAR_016575. FT VARIANT 52 52 V -> L (in allele Cw*0405). FT /FTId=VAR_016576. FT VARIANT 73 73 E -> A (in allele Cw*0403 and allele FT Cw*0406). FT /FTId=VAR_016577. FT VARIANT 180 180 R -> L (in allele Cw*0404 and allele FT Cw*0406). FT /FTId=VAR_016578. FT VARIANT 327 327 M -> V (in allele Cw*0403 and allele FT Cw*0406). FT /FTId=VAR_016579. FT STRAND 27 36 FT TURN 39 40 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 64 66 FT STRAND 70 73 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 131 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 161 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT TURN 244 245 FT HELIX 249 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 366 AA; 40995 MW; E883EB3968658DCB CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFSTSVSWPG RGEPRFIAVG YVDDTQFVRF DSDAASPRGE PREPWVEQEG PEYWDRETQK YKRQAQADRV NLRKLRGYYN QSEDGSHTLQ RMFGCDLGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQR RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWKP SSQPTIPIVG IVAGLAVLAV LAVLGAMVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C05_HUMAN Reviewed; 366 AA. AC Q9TNN7; O02866; O62888; Q9TPV8; Q9TPX2; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 20-FEB-2007, entry version 45. DE HLA class I histocompatibility antigen, Cw-5 alpha chain precursor DE (MHC class I antigen Cw*5). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0501). RA Baurain J.-F., Coulie P.G.; RT "New HLA-C alleles, on the basis of their transmembrane or cytoplasmic RT regions."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0501). RA Ellexson M.E., Zhang W., Hildebrand W.H.; RT "Cw*0501new."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE OF 1-298 (ALLELE CW*0501). RC TISSUE=Peripheral blood; RA Wang H., Tokunaga K.; RT "HLA-C locus polymorphisms in Japanese."; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE CW*0502). RA Santos S., Vicario J.L., Balas A.; RT "Novel HLA-C allele."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0503). RX MEDLINE=20340082; PubMed=10885573; RX DOI=10.1034/j.1399-0039.2000.550515.x; RA Huang L.Q., Boon T., Van Pel A.; RT "Identification of a novel HLA-Cw*05 allele, Cw*0503."; RL Tissue Antigens 55:473-474(2000). RN [6] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE CW*0504). RA Santos S., Balas A., Vicario J.L.; RT "New HLA-Cw5 antigen."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-5 are known: Cw*0501 CC Cw*0502, Cw*0503 and Cw*0504. The sequence shown is that of CC Cw*0501. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; AJ010748; CAA09340.1; -; mRNA. DR EMBL; U57028; AAD11469.1; -; mRNA. DR EMBL; D64148; BAA19534.1; -; mRNA. DR EMBL; AF047367; AAC05205.2; -; Genomic_DNA. DR EMBL; AF047366; AAC05205.2; JOINED; Genomic_DNA. DR EMBL; AF168611; AAD50823.1; -; mRNA. DR EMBL; AF173008; AAD51331.1; -; Genomic_DNA. DR EMBL; AF173007; AAD51331.1; JOINED; Genomic_DNA. DR PIR; A59028; A59028. DR UniGene; Hs.449621; -. DR UniGene; Hs.650454; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1QQD. DR SMR; Q9TNN7; 26-302. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-5 alpha chain. FT /FTId=PRO_0000018872. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 138 138 N -> D (in allele Cw*0504). FT /FTId=VAR_016580. FT VARIANT 140 140 F -> S (in allele Cw*0504). FT /FTId=VAR_016581. FT VARIANT 201 201 K -> E (in allele Cw*0502). FT /FTId=VAR_016582. FT VARIANT 207 208 EH -> DP (in allele Cw*0503). FT /FTId=VAR_016583. FT VARIANT 218 218 V -> I (in allele Cw*0503). FT /FTId=VAR_016584. FT VARIANT 223 223 A -> V (in allele Cw*0503). FT /FTId=VAR_016585. SQ SEQUENCE 366 AA; 40912 MW; 26454A7EE68151DA CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVQF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV NLRKLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DKAAQITQRK WEAAREAEQR RAYLEGTCVE WLRRYLENGK KTLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWGP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C06_HUMAN Reviewed; 366 AA. AC Q29963; O19505; O78063; Q29989; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 20-FEB-2007, entry version 56. DE HLA class I histocompatibility antigen, Cw-6 alpha chain precursor DE (MHC class I antigen Cw*6). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0602). RX MEDLINE=89233298; PubMed=2714853; RA Mizuno S., Kang S.H., Lee H.W., Trapani J.A., Dupont B., Yang S.Y.; RT "Isolation and expression of a cDNA clone encoding HLA-CW6: unique RT characteristics of HLA-C encoded gene products."; RL Immunogenetics 29:323-330(1989). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0602). RX MEDLINE=92285886; PubMed=1598685; RA Steinle A., Noessner E., Schendel D.J.; RT "Isolation and characterization of a genomic HLA-Cw6 clone."; RL Tissue Antigens 39:134-137(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-366 (ALLELE CW*0602). RX MEDLINE=89233295; PubMed=2714852; RA Pohla H., Kuon W., Tabaczewski P., Doerner C., Weiss E.H.; RT "Allelic variation in HLA-B and HLA-C sequences and the evolution of RT the HLA-B alleles."; RL Immunogenetics 29:297-307(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE CW*0603). RX MEDLINE=98349393; PubMed=9686604; RA Turner S., Ellexson M.E., Hickman H.D., Sidebottom D.A., RA Fernandez-Vina M., Confer D.L., Hildebrand W.H.; RT "Sequence-based typing provides a new look at HLA-C diversity."; RL J. Immunol. 161:1406-1413(1998). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE CW*0604). RC TISSUE=Blood; RX MEDLINE=99321026; PubMed=10395103; RX DOI=10.1034/j.1399-0039.1999.530603.x; RA Inoue T., Ogawa A., Tokunaga K., Ishikawa Y., Kashiwase K., Tanaka H., RA Park M.H., Jia G.J., Chimge N.-O., Sideltseva E.W., Akaza T., RA Tadokoro K., Takahashi T., Juji T.; RT "Diversity of HLA-B17 alleles and haplotypes in East Asians and a RT novel Cw6 allele (Cw*0604) associated with B*5701."; RL Tissue Antigens 53:534-544(1999). RN [6] RP ASSOCIATION OF ALLELE HLA-CW*0602 WITH PSORIASIS. RX PubMed=11122018; DOI=10.1046/j.1365-2133.2000.03885.x; RA Mallon E., Bunce M., Savoie H., Rowe A., Newson R., Gotch F., RA Bunker C.B.; RT "HLA-C and guttate psoriasis."; RL Br. J. Dermatol. 143:1177-1182(2000). RN [7] RP ASSOCIATION OF ALLELE HLA-CW*0602 WITH PSORIASIS. RX PubMed=16235096; DOI=10.1007/s00439-005-0048-2; RA Helms C., Saccone N.L., Cao L., Daw J.A.W., Cao K., Hsu T.M., RA Taillon-Miller P., Duan S., Gordon D., Pierce B., Ott J., Rice J., RA Fernandez-Vina M.A., Kwok P.-Y., Menter A., Bowcock A.M.; RT "Localization of PSORS1 to a haplotype block harboring HLA-C and RT distinct from corneodesmosin and HCR."; RL Hum. Genet. 118:466-476(2005). RN [8] RP INVOLVEMENT IN PSORS1. RX PubMed=16642438; DOI=10.1086/503821; RA Nair R.P., Stuart P.E., Nistor I., Hiremagalore R., Chia N.V.C., RA Jenisch S., Weichenthal M., Abecasis G.R., Lim H.W., Christophers E., RA Voorhees J.J., Elder J.T.; RT "Sequence and haplotype analysis supports HLA-C as the psoriasis RT susceptibility 1 gene."; RL Am. J. Hum. Genet. 78:827-851(2006). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-6 are known: Cw*0602 CC Cw*0603 and Cw*0604. Allele HLA-Cw*0602 is a risk factor that CC confers susceptibility to psoriasis. The sequence shown is that of CC Cw*0602. CC -!- DISEASE: Genetic variation in HLA-C is associated with CC susceptibility to psoriasis 1 (PSORS1) [MIM:177900]. Psoriasis is CC a chronic inflammatory dermatosis that affects approximately 2% of CC the population. It is characterized by red, scaly skin lesions CC that are usually found on the scalp, elbows, and knees, and may be CC associated with severe arthritis. The lesions are caused by CC hyperproliferative keratinocytes and infiltration of inflammatory CC cells into the dermis and epidermis. The usual age of onset of CC psoriasis is between 15 and 30 years, although it can present at CC any age. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M28160; AAA36235.1; -; mRNA. DR EMBL; Z22752; CAA80437.1; -; Genomic_DNA. DR EMBL; Z22753; CAA80437.1; JOINED; Genomic_DNA. DR EMBL; Z22754; CAA80437.1; JOINED; Genomic_DNA. DR EMBL; M28206; AAA57258.1; -; mRNA. DR EMBL; AF019568; AAC17721.1; -; Genomic_DNA. DR EMBL; AF019567; AAC17721.1; JOINED; Genomic_DNA. DR EMBL; AB008136; BAA22919.1; -; Genomic_DNA. DR PIR; I68749; I68749. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1QQD. DR SMR; Q29963; 26-298. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR MIM; 177900; phenotype. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-6 alpha chain. FT /FTId=PRO_0000018873. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 33 33 D -> Y (in allele Cw*0603). FT /FTId=VAR_016620. FT VARIANT 180 180 W -> L (in allele Cw*0604). FT /FTId=VAR_016621. FT CONFLICT 33 33 D -> C (in Ref. 3). FT CONFLICT 202 202 T -> S (in Ref. 1). SQ SEQUENCE 366 AA; 40969 MW; 45876CB22256DE80 CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFDTAVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV NLRKLRGYYN QSEDGSHTLQ WMYGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQW RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C07_HUMAN Reviewed; 366 AA. AC P10321; O78061; O78083; Q29631; Q29652; Q29867; Q29990; Q95463; AC Q95603; Q9MY31; Q9TQP9; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 3. DT 20-FEB-2007, entry version 69. DE HLA class I histocompatibility antigen, Cw-7 alpha chain precursor DE (MHC class I antigen Cw*7). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-206 (ALLELE CW*0701). RX MEDLINE=95176330; PubMed=7871529; RA Steinle A., Schendel D.J.; RT "HLA class I alleles of LCL 721 and 174 x CEM.T2 (T2)."; RL Tissue Antigens 44:268-270(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 77-309 (ALLELE CW*0701). RX MEDLINE=89233295; PubMed=2714852; RA Pohla H., Kuon W., Tabaczewski P., Doerner C., Weiss E.H.; RT "Allelic variation in HLA-B and HLA-C sequences and the evolution of RT the HLA-B alleles."; RL Immunogenetics 29:297-307(1989). RN [3] RP NUCLEOTIDE SEQUENCE OF 26-338 (ALLELE CW*0701). RX MEDLINE=99416847; PubMed=10488744; RX DOI=10.1034/j.1399-0039.1999.540208.x; RA van der Vlies S.A., Voorter C.E., van den Berg-Loonen E.M.; RT "There is more to HLA -C than exons 2 and 3: sequencing exons 1, 4 and RT 5."; RL Tissue Antigens 54:169-177(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES CW*0702 AND CW*0704). RC TISSUE=Blood; RX MEDLINE=96232973; PubMed=8655361; DOI=10.1016/0198-8859(95)00150-6; RA Wang H., Tokunaga K., Ishikawa Y., Asahina A., Kuwata S., Akaza T., RA Tadokoro K., Shibata Y., Takiguchi M., Juji T.; RT "Identification and DNA typing of two Cw7 alleles (Cw*0702 and RT Cw*0704) in Japanese, with the corrected sequence of Cw*0702."; RL Hum. Immunol. 45:52-58(1996). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE CW*0702). RX MEDLINE=98099755; PubMed=9435339; DOI=10.1007/s002510050350; RA Cooper S.L., Adams E.J., Wells R.S., Walker C.M., Parham P.; RT "A major histocompatibility complex class I allele shared by two RT species of chimpanzee."; RL Immunogenetics 47:212-217(1998). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELES CW*0702 AND CW*0704). RC TISSUE=Blood; RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-366 (ALLELE CW*0703). RX MEDLINE=86033791; PubMed=3863816; RA Davidson W.F., Kress M., Khoury G., Jay G.; RT "Comparison of HLA class I gene sequences. Derivation of locus- RT specific oligonucleotide probes specific for HLA-A, HLA-B, and HLA-C RT genes."; RL J. Biol. Chem. 260:13414-13423(1985). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0704). RX MEDLINE=96086482; PubMed=7482492; RA Vilches C., Bunce M., de Pablo R., Herrero M.J., Kreisler M.; RT "Anchored PCR cloning of the novel HLA-Cw*0704 allele detected by PCR- RT SSP."; RL Tissue Antigens 46:19-23(1995). RN [9] RP NUCLEOTIDE SEQUENCE (ALLELE CW*0704). RC TISSUE=Melanoma; RA Coulie P.G.; RT "Identification of a new HLA-Cw7 allele."; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0706). RX MEDLINE=97161041; PubMed=9008313; RA Vilches C., Bunce M., Sanz L., de Pablo R., Puente S., Kreisler M.; RT "Molecular cloning of two new HLA-C alleles: Cw*1801 and Cw*0706."; RL Tissue Antigens 48:698-702(1996). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE CW*0709). RX MEDLINE=98349393; PubMed=9686604; RA Turner S., Ellexson M.E., Hickman H.D., Sidebottom D.A., RA Fernandez-Vina M., Confer D.L., Hildebrand W.H.; RT "Sequence-based typing provides a new look at HLA-C diversity."; RL J. Immunol. 161:1406-1413(1998). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0711). RX MEDLINE=99299762; PubMed=10372547; RX DOI=10.1034/j.1399-0039.1999.530508.x; RA Baurain J.-F., Coulie P.G.; RT "Correction of HLA-Cw*0501 and identification of HLA-Cw*0711."; RL Tissue Antigens 53:510-512(1999). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-7 are known: Cw*0701, CC Cw*0702, Cw*0703, Cw*0704, Cw*0706, Cw*0709 and Cw*0711. The CC sequence shown is that of Cw*0702. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; Z46810; CAA86840.1; -; mRNA. DR EMBL; M28207; AAA53259.1; -; mRNA. DR EMBL; Y18533; CAB71800.1; -; Genomic_DNA. DR EMBL; Y18534; CAB71800.1; JOINED; Genomic_DNA. DR EMBL; Y18535; CAB71800.1; JOINED; Genomic_DNA. DR EMBL; Y18536; CAB71800.1; JOINED; Genomic_DNA. DR EMBL; D38526; BAA07531.1; -; mRNA. DR EMBL; D49819; BAA08625.1; -; mRNA. DR EMBL; D49552; BAA08500.1; -; mRNA. DR EMBL; AJ001977; CAA05125.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ293016; CAC04321.1; -; Genomic_DNA. DR EMBL; AJ293017; CAC04322.1; -; Genomic_DNA. DR EMBL; AJ291815; CAC19191.1; -; Genomic_DNA. DR EMBL; M11886; AAA52665.1; -; mRNA. DR EMBL; X83394; CAA58313.1; -; mRNA. DR EMBL; U09853; AAA50217.1; -; mRNA. DR EMBL; X97321; CAA65986.1; -; mRNA. DR EMBL; AF015557; AAC17722.1; -; Genomic_DNA. DR EMBL; AF015556; AAC17722.1; JOINED; Genomic_DNA. DR EMBL; AJ010749; CAA09341.1; -; mRNA. DR PIR; A24512; HLHUC4. DR PIR; I37078; I37078. DR PIR; I37529; I37529. DR PIR; I68750; I68750. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1IM9. DR SMR; P10321; 26-302. DR Ensembl; ENSG00000198479; Homo sapiens. DR KEGG; hsa:3107; -. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR ArrayExpress; P10321; -. DR GermOnline; ENSG00000204525; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-7 alpha chain. FT /FTId=PRO_0000018874. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 90 90 K -> N (in allele Cw*0701). FT /FTId=VAR_016590. FT VARIANT 101 101 S -> N (in allele Cw*0709). FT /FTId=VAR_016591. FT VARIANT 104 104 N -> K (in allele Cw*0709). FT /FTId=VAR_016592. FT VARIANT 119 119 L -> F (in allele Cw*0704 and allele FT Cw*0711). FT /FTId=VAR_016593. FT VARIANT 123 123 S -> Y (in allele Cw*0701). FT /FTId=VAR_016594. FT VARIANT 140 140 S -> F (in allele Cw*0704 and allele FT Cw*0711). FT /FTId=VAR_016595. FT VARIANT 171 171 L -> W (in allele Cw*0703). FT /FTId=VAR_016646. FT VARIANT 180 180 L -> D (in allele Cw*0704 and allele FT Cw*0711; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016596. FT VARIANT 187 187 T -> L (in allele Cw*0703; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016647. FT VARIANT 201 201 E -> K (in allele Cw*0704 and allele FT Cw0711). FT /FTId=VAR_016597. FT VARIANT 331 331 M -> K (in allele Cw*0706). FT /FTId=VAR_016598. FT VARIANT 348 348 A -> V (in allele Cw*0706). FT /FTId=VAR_016599. FT VARIANT 363 363 T -> A (in allele Cw*0711). FT /FTId=VAR_016600. FT CONFLICT 15 16 GG -> AA (in Ref. 8). FT CONFLICT 41 41 R -> A (in Ref. 8). FT CONFLICT 309 309 M -> V (in Ref. 2). SQ SEQUENCE 366 AA; 40649 MW; 59C23D95FD1D0BC8 CRC64; MRVMAPRALL LLLSGGLALT ETWACSHSMR YFDTAVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV SLRNLRGYYN QSEDGSHTLQ RMSGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK LEAARAAEQL RAYLEGTCVE WLRRYLENGK ETLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL QEPLTLSWEP SSQPTIPIMG IVAGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LITCKA // ID 1C08_HUMAN Reviewed; 366 AA. AC P30505; P30506; P30507; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 20-FEB-2007, entry version 57. DE HLA class I histocompatibility antigen, Cw-8 alpha chain precursor DE (MHC class I antigen Cw*8). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES CW*0801 AND CW*0802). RX MEDLINE=93031775; PubMed=1384166; RA Zemmour J., Gumperz J.E., Hildebrand W.H., Ward F.E., Marsh S.G.E., RA Williams R.C., Parham P.; RT "The molecular basis for reactivity of anti-Cw1 and anti-Cw3 RT alloantisera with HLA-B46 haplotypes."; RL Tissue Antigens 39:249-257(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*0803). RX MEDLINE=92269955; PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-8 are known: Cw*0801 CC (Cw8.1), Cw*0802 (Cw8.2) and Cw*0803. The sequence shown is that CC of Cw*0801. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M84173; AAA59687.1; -; mRNA. DR EMBL; M84174; AAA59688.1; -; mRNA. DR EMBL; Z15144; CAA78850.1; -; mRNA. DR PIR; I37135; I37135. DR PIR; I81232; I81232. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1QQD. DR SMR; P30505; 26-302. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-8 alpha chain. FT /FTId=PRO_0000018875. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 162 162 T -> K (in allele Cw*0802). FT /FTId=VAR_016586. FT VARIANT 176 176 T -> E (in allele Cw*0802; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016587. FT VARIANT 180 180 L -> R (in allele Cw*0802). FT /FTId=VAR_016588. FT VARIANT 199 199 G -> R (in allele CW*0803). FT /FTId=VAR_016589. SQ SEQUENCE 366 AA; 40773 MW; 2A84D41389A0486A CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVQF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARTAEQL RAYLEGTCVE WLRRYLENGK KTLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWGP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C12_HUMAN Reviewed; 366 AA. AC P30508; O02863; O19652; O62882; O78062; O78166; O78211; O78214; AC P30509; Q29768; Q31627; Q860R1; Q860R2; Q99528; Q9GIK4; Q9TPS4; AC Q9UM32; Q9UM33; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 20-FEB-2007, entry version 59. DE HLA class I histocompatibility antigen, Cw-12 alpha chain precursor DE (MHC class I antigen Cw*12). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1202). RX MEDLINE=88330144; PubMed=2843461; RA Takata H., Inoko H., Ando A., Haranaka M., Watanabe B., Tsuji K., RA Iri H.; RT "Cloning and analysis of HLA class I cDNA encoding a new HLA-C RT specificity Cx52."; RL Immunogenetics 28:265-270(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE CW*1202). RX MEDLINE=89309827; PubMed=2787363; RA Takiguchi M., Nishimura I., Hayashi H., Karaki S., Kariyone A., RA Kano K.; RT "The structure and expression of genes encoding serologically RT undetected HLA-C locus antigens."; RL J. Immunol. 143:1372-1378(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1202). RX MEDLINE=94131818; PubMed=7905471; DOI=10.1016/0198-8859(93)90509-Y; RA Vilches C., de Pablo R., Herrero M.J., Moreno M.E., Kreisler M.; RT "Molecular cloning and polymerase chain reaction-sequence-specific RT oligonucleotide detection of the allele encoding the novel RT allospecificity HLA-Cw6.2 (Cw*1502) in Spanish gypsies."; RL Hum. Immunol. 37:259-263(1993). RN [4] RP NUCLEOTIDE SEQUENCE OF 1-298 (ALLELE CW*1202). RC TISSUE=Peripheral blood; RA Wang H., Tokunaga K.; RT "HLA-C alleles in Japanese and a novel allele from a non-Japanese RT individual."; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE CW*1202). RA Greville W.D., Ng G., Kennedy A., Kennedy C.T., Le T., Dodd R., RA Wallace R., Dunckley H.; RT "An HLA-Cw allele detected by PCR-SSO."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1203). RC TISSUE=Blood; RX MEDLINE=95141286; PubMed=7839353; RA Cereb N., Choi J.W., Lee S., Maye P., Kong Y., Yang S.Y.; RT "Identification of two new HLA-C alleles, Cw*1203 and Cw*1402, from RT the sequence analysis of seven HLA homozygous cell lines carrying HLA- RT C blank."; RL Tissue Antigens 44:193-195(1994). RN [7] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1203). RA Pablo R.; RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1203). RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [9] RP NUCLEOTIDE SEQUENCE OF 1-298 (ALLELE CW*1203). RC TISSUE=Peripheral blood; RA Wang H., Tokunaga K.; RT "HLA-C locus polymorphisms in Japanese."; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1204). RX MEDLINE=98119598; PubMed=9459510; RA Vilches C., Bunce M., van Dam M., de Pablo R.; RT "A new pair of HLA-C alleles, Cw*12042 and Cw*1203, differing at the RT KIR-related dimorphism of codons 77-80."; RL Tissue Antigens 51:101-105(1998). RN [11] RP NUCLEOTIDE SEQUENCE OF 1-227 (ALLELE CW*1204). RA Tatari Z.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES CW*1204 AND RP CW*1206). RX MEDLINE=98349393; PubMed=9686604; RA Turner S., Ellexson M.E., Hickman H.D., Sidebottom D.A., RA Fernandez-Vina M., Confer D.L., Hildebrand W.H.; RT "Sequence-based typing provides a new look at HLA-C diversity."; RL J. Immunol. 161:1406-1413(1998). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELE CW*1205). RX MEDLINE=98119594; PubMed=9459506; RA Grundschober C., Labonne M., Javaux F., Steiner Q.G., Gebuhrer L., RA Tiercy J.M.; RT "Sequence of four new HLA-Cw alleles: a possible role of interallelic RT recombination."; RL Tissue Antigens 51:72-79(1998). RN [14] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE CW*1207). RA Davey S., Dunn P.P.; RT "Nucleotide sequence of an HLA-Cw*1203 variant allele with a new RT polymorphic position in exon 2."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE CW*1208). RX MEDLINE=21970278; PubMed=11972880; RX DOI=10.1034/j.1399-0039.2002.590110.x; RA Cox S.T., Ogilvie H., Bohan E.M., Holman R., Prentice H.G., Potter M., RA Madrigal J.A., Little A.-M.; RT "Sequence of two new HLA-Cw alleles: HLA-Cw*0313 and HLA-Cw*1208."; RL Tissue Antigens 59:49-51(2002). RN [16] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE CW*1209). RA Day S., Carter V.; RT "Identification of confirmatory sequence of Cw*1209."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-12 are known: Cw*1202, CC Cw*1203, Cw*1204, Cw*1205, Cw*1206, Cw*1207, Cw*1208 and Cw*1209. CC The sequence shown is that of Cw*1202. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M21963; AAA59847.1; -; mRNA. DR EMBL; M28172; AAA59670.1; -; Genomic_DNA. DR EMBL; X70856; CAA50209.1; -; mRNA. DR EMBL; X70857; CAA50210.1; -; mRNA. DR EMBL; D64152; BAA19537.1; -; mRNA. DR EMBL; D83741; BAA32615.1; -; mRNA. DR EMBL; AF189726; AAF04581.1; -; Genomic_DNA. DR EMBL; AF189725; AAF04581.1; JOINED; Genomic_DNA. DR EMBL; U06695; AAA92995.1; -; mRNA. DR EMBL; U06696; AAA92996.1; -; mRNA. DR EMBL; X82122; CAA57634.1; -; mRNA. DR EMBL; AJ420248; CAD12433.1; -; Genomic_DNA. DR EMBL; D64146; BAA19532.1; -; mRNA. DR EMBL; Y11843; CAA72592.1; -; mRNA. DR EMBL; X99704; CAA68035.1; -; mRNA. DR EMBL; AF015559; AAC17724.1; -; Genomic_DNA. DR EMBL; AF015558; AAC17724.1; JOINED; Genomic_DNA. DR EMBL; AF036553; AAC17725.1; -; Genomic_DNA. DR EMBL; AF036552; AAC17725.1; JOINED; Genomic_DNA. DR EMBL; Z83247; CAB05845.1; -; mRNA. DR EMBL; Z80228; CAB02409.1; -; Genomic_DNA. DR EMBL; AJ249163; CAB53538.1; -; Genomic_DNA. DR EMBL; AJ249164; CAB53539.1; -; Genomic_DNA. DR EMBL; AJ304496; CAC19018.1; -; Genomic_DNA. DR EMBL; AJ550622; CAD79471.1; -; Genomic_DNA. DR EMBL; AJ550623; CAD79472.1; -; Genomic_DNA. DR PIR; A59028; A59028. DR PIR; I37526; I37526. DR PIR; I38507; I38507. DR PIR; I72113; I72113. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1QQD. DR SMR; P30508; 26-302. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-12 alpha chain. FT /FTId=PRO_0000018876. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 90 90 K -> N (in allele Cw*1208). FT /FTId=VAR_016622. FT VARIANT 97 97 A -> T (in allele Cw*1205 and allele FT Cw*1209). FT /FTId=VAR_016623. FT VARIANT 101 101 S -> G (in allele Cw*1207). FT /FTId=VAR_016624. FT VARIANT 101 101 S -> N (in allele Cw*1204, allele Cw*1205 FT and allele Cw*1209). FT /FTId=VAR_016625. FT VARIANT 104 104 N -> K (in allele Cw*1204, allele Cw*1205 FT and allele Cw*1209). FT /FTId=VAR_016626. FT VARIANT 121 121 R -> W (in allele Cw*1203, allele FT Cw*1204, allele Cw*1205, allele Cw*1206, FT allele Cw*1207 and allele Cw*1209). FT /FTId=VAR_016627. FT VARIANT 144 144 G -> V (in allele Cw*1206). FT /FTId=VAR_016628. FT VARIANT 180 180 W -> R (in allele Cw*1209). FT /FTId=VAR_016629. FT CONFLICT 25 25 C -> G (in Ref. 1). FT CONFLICT 140 140 S -> V (in Ref. 1). SQ SEQUENCE 366 AA; 40886 MW; 598C8795CD033FB7 CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV SLRNLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQW RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C14_HUMAN Reviewed; 366 AA. AC P30510; O62879; O78178; Q29641; Q30192; Q9MY35; Q9TQJ5; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2003, sequence version 2. DT 20-FEB-2007, entry version 60. DE HLA class I histocompatibility antigen, Cw-14 alpha chain precursor DE (MHC class I antigen Cw*14). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE CW*1402). RX MEDLINE=89309827; PubMed=2787363; RA Takiguchi M., Nishimura I., Hayashi H., Karaki S., Kariyone A., RA Kano K.; RT "The structure and expression of genes encoding serologically RT undetected HLA-C locus antigens."; RL J. Immunol. 143:1372-1378(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1402). RC TISSUE=Blood; RX MEDLINE=95141286; PubMed=7839353; RA Cereb N., Choi J.W., Lee S., Maye P., Kong Y., Yang S.Y.; RT "Identification of two new HLA-C alleles, Cw*1203 and Cw*1402, from RT the sequence analysis of seven HLA homozygous cell lines carrying HLA- RT C blank."; RL Tissue Antigens 44:193-195(1994). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1402). RA Zhang L., Ellexson M.E., Hildebrand W.H.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-298 (ALLELE CW*1402). RC TISSUE=Blood; RX MEDLINE=96387679; PubMed=8795149; RA Wang H., Tokunaga K., Ogawa A., Akaza T., Tadokoro K., Takiguchi M., RA Shibata Y., Juji T.; RT "DNA typing of Cw*14 alleles in Japanese and the corrected sequence of RT Cw*1402."; RL Tissue Antigens 47:442-446(1996). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE CW*1402). RX MEDLINE=98349393; PubMed=9686604; RA Turner S., Ellexson M.E., Hickman H.D., Sidebottom D.A., RA Fernandez-Vina M., Confer D.L., Hildebrand W.H.; RT "Sequence-based typing provides a new look at HLA-C diversity."; RL J. Immunol. 161:1406-1413(1998). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1403). RC TISSUE=Blood; RX MEDLINE=96026856; PubMed=7499177; DOI=10.1016/0198-8859(95)00041-2; RA Wang H., Tokunaga K., Ishikawa Y., Lin L., Kashiwase K., Nakajima F., RA Ogawa A., Kuwata S., Akaza T., Tadokoro K., Shibata Y., Yoshikura H., RA Juji T.; RT "A new HLA-C allele, Cw*1403, associated with HLA-B44 in Japanese."; RL Hum. Immunol. 43:295-300(1995). RN [7] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1403). RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE CW*1404). RX MEDLINE=20367641; PubMed=10912513; DOI=10.1007/s002510000178; RA Santos S., Vicario J.L., Aviles M.J., Garcia-Sanchez F., Balas A.; RT "HLA-Cw*1404: a new HLA-C allele with a hybrid 77Asn-80Asn NK motif."; RL Immunogenetics 51:610-612(2000). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-14 are known: Cw*1402 CC (CB-1), Cw*1403 (CX44), Cw*1404 and Cw*1404. The sequence shown is CC that of Cw*1402. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M28171; AAA59669.1; -; Genomic_DNA. DR EMBL; U06487; AAA92994.1; -; mRNA. DR EMBL; U41386; AAC32743.1; -; mRNA. DR EMBL; D49820; BAA89793.1; -; mRNA. DR EMBL; AF015555; AAC17726.1; -; Genomic_DNA. DR EMBL; AF015554; AAC17726.1; JOINED; Genomic_DNA. DR EMBL; D31817; BAA06604.1; -; mRNA. DR EMBL; AJ420249; CAD12434.1; -; Genomic_DNA. DR EMBL; AF104219; AAD21014.1; -; Genomic_DNA. DR EMBL; AF104218; AAD21014.1; JOINED; Genomic_DNA. DR PIR; I56034; I56034. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1IM9. DR SMR; P30510; 26-302. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-14 alpha chain. FT /FTId=PRO_0000018877. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 45 45 R -> H (in allele Cw*1403). FT /FTId=VAR_016636. FT VARIANT 97 97 T -> A (in allele Cw*1404). FT /FTId=VAR_016637. FT VARIANT 101 101 S -> N (in allele Cw*1403). FT /FTId=VAR_016638. FT CONFLICT 16 16 A -> T (in Ref. 2). FT CONFLICT 43 43 E -> G (in Ref. 2). FT CONFLICT 202 202 T -> S (in Ref. 1). FT CONFLICT 272 272 V -> M (in Ref. 1). SQ SEQUENCE 366 AA; 40838 MW; 792D335D12D6547E CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ WMFGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQR RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C15_HUMAN Reviewed; 366 AA. AC Q07000; O78165; Q29864; Q29991; Q31605; Q9BD28; Q9GJ33; Q9MY49; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 20-FEB-2007, entry version 54. DE HLA class I histocompatibility antigen, Cw-15 alpha chain precursor DE (MHC class I antigen Cw*15). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1502). RX MEDLINE=94131818; PubMed=7905471; DOI=10.1016/0198-8859(93)90509-Y; RA Vilches C., de Pablo R., Herrero M.J., Moreno M.E., Kreisler M.; RT "Molecular cloning and polymerase chain reaction-sequence-specific RT oligonucleotide detection of the allele encoding the novel RT allospecificity HLA-Cw6.2 (Cw*1502) in Spanish gypsies."; RL Hum. Immunol. 37:259-263(1993). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1502). RC TISSUE=Peripheral blood; RA Wang H., Tokunaga K.; RT "HLA-C locus polymorphisms in Japanese."; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1502). RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [4] RP NUCLEOTIDE SEQUENCE OF 1-275 (ALLELE CW*1502). RA Witter K., Zahn R., Scholz S., Albert E.; RT "Group specific amplification and sequencing of HLA-C locus."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1503). RA Domena J.D.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1504). RX MEDLINE=94041472; PubMed=8225443; RA Pablo R., Vilches C., Moreno M.E., Kreisler M.; RT "A novel HLA-C allele (Cw*1504) related to the Cw6.2 phenotype."; RL Immunogenetics 39:79-79(1994). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1505). RX MEDLINE=94364645; PubMed=8082899; DOI=10.1007/BF00189983; RA Vilches C., de Pablo R., Herrero M.J., Moreno M.E., Kreisler M.; RT "Cw*1505: a novel HLA-C allele isolated from a B*7301 haplotype."; RL Immunogenetics 40:313-313(1994). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1505). RX MEDLINE=96369317; PubMed=8773323; RA Sanz L., Vilches C., de Pablo R., Bunce M., Moreno M.E., Kreisler M.; RT "Haplotypic association of two new HLA class I alleles: Cw*15052 and RT B*0706: evolutionary relationships of HLA-Cw*15 alleles."; RL Tissue Antigens 47:329-332(1996). RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE CW*1510). RA Tamouza R., Schaeffer V., Marzais F., Poirier J.C., Fortier C., RA Charron D.; RT "New HLA-Cw*15 sequence."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE CW*1511). RA Greville W.D., Chapman G., Le T., Dodd R., Taverniti A., Dunckley H.; RT "Novel HLA-Cw allele detected by PCR-SSO."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-15 are known: Cw*1502, CC Cw*1503, Cw*1504, Cw*1505, Cw*1510 and Cw*1511. The sequence shown CC is that of Cw*1502. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X67818; CAA48029.1; -; mRNA. DR EMBL; D83031; BAA32614.1; -; mRNA. DR EMBL; AJ420250; CAD12435.1; -; Genomic_DNA. DR EMBL; AJ272049; CAB75584.1; -; Genomic_DNA. DR EMBL; M99388; AAA88087.1; -; mRNA. DR EMBL; X73518; CAA51917.1; -; mRNA. DR EMBL; X78343; CAA55138.1; -; mRNA. DR EMBL; X87841; CAA61110.1; -; mRNA. DR EMBL; AF302134; AAG33823.1; -; Genomic_DNA. DR EMBL; AF302133; AAG33823.1; JOINED; Genomic_DNA. DR EMBL; AF335317; AAK07656.1; -; Genomic_DNA. DR EMBL; AF335316; AAK07656.1; JOINED; Genomic_DNA. DR PIR; I37523; I37523. DR PIR; I37527; I37527. DR PIR; I37544; I37544. DR UniGene; Hs.167805; -. DR UniGene; Hs.622865; -. DR UniGene; Hs.633485; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1IM9. DR SMR; Q07000; 26-302. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-15 alpha chain. FT /FTId=PRO_0000018878. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (Potential). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 40 40 G -> S (in allele Cw*1511). FT /FTId=VAR_016639. FT VARIANT 45 45 H -> R (in allele Cw*1510). FT /FTId=VAR_016640. FT VARIANT 90 90 N -> K (in allele Cw*1511). FT /FTId=VAR_016641. FT VARIANT 97 97 T -> A (in allele Cw*1503). FT /FTId=VAR_016642. FT VARIANT 137 137 H -> Y (in allele Cw*1504). FT /FTId=VAR_016643. FT VARIANT 140 140 L -> F (in allele Cw*1505). FT /FTId=VAR_016644. FT VARIANT 140 140 L -> S (in allele Cw*1504). FT /FTId=VAR_016645. FT CONFLICT 5 5 A -> T (in Ref. 2). SQ SEQUENCE 366 AA; 40863 MW; FDF703B7AFB05FDD CRC64; MRVMAPRTLL LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPHFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQN YKRQAQTDRV NLRKLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQL AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C16_HUMAN Reviewed; 366 AA. AC Q29960; O78091; O78202; Q29862; Q29959; Q9MY74; Q9MYI3; Q9TNZ8; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 53. DE HLA class I histocompatibility antigen, Cw-16 alpha chain precursor DE (MHC class I antigen Cw*16). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1601), AND ALTERNATIVE SPLICING. RX MEDLINE=89122144; PubMed=2914713; RA Cianetti L., Testa U., Scotto L., la Valle R., Simeone A., Boccoli G., RA Giannella G., Peschle C., Boncinelli E.; RT "Three new class I HLA alleles: structure of mRNAs and alternative RT mechanisms of processing."; RL Immunogenetics 29:80-91(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1602). RX MEDLINE=95164264; PubMed=7860363; DOI=10.1016/0198-8859(94)90011-6; RA Vilches C., Herrero M.J., de Pablo R., Moreno M.E., Bunce M., RA Kreisler M.; RT "Molecular characterization of a novel, serologically detectable, HLA- RT C allele: Cw*1602."; RL Hum. Immunol. 41:167-170(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-338 (ALLELE CW*1604). RX MEDLINE=99416847; PubMed=10488744; RX DOI=10.1034/j.1399-0039.1999.540208.x; RA van der Vlies S.A., Voorter C.E., van den Berg-Loonen E.M.; RT "There is more to HLA -C than exons 2 and 3: sequencing exons 1, 4 and RT 5."; RL Tissue Antigens 54:169-177(1999). RN [4] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE CW*1604). RX MEDLINE=98349393; PubMed=9686604; RA Turner S., Ellexson M.E., Hickman H.D., Sidebottom D.A., RA Fernandez-Vina M., Confer D.L., Hildebrand W.H.; RT "Sequence-based typing provides a new look at HLA-C diversity."; RL J. Immunol. 161:1406-1413(1998). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE CW*1604). RX MEDLINE=98119594; PubMed=9459506; RA Grundschober C., Labonne M., Javaux F., Steiner Q.G., Gebuhrer L., RA Tiercy J.M.; RT "Sequence of four new HLA-Cw alleles: a possible role of interallelic RT recombination."; RL Tissue Antigens 51:72-79(1998). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system (By similarity). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; single-pass type I CC membrane protein. Isoform 2: Secreted protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q29960-1; Sequence=Displayed; CC Name=2; CC IsoId=Q29960-2; Sequence=VSP_008096; CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-16 are known: Cw*1601, CC Cw*1602 (CW*CL10V) and Cw*1604. The sequence shown is that of CC Cw*1601. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24097; AAA59656.1; -; mRNA. DR EMBL; M24097; AAA59657.1; -; mRNA. DR EMBL; X76189; CAA53783.1; -; mRNA. DR EMBL; AJ011883; CAB65547.1; -; Genomic_DNA. DR EMBL; Y18657; CAB72095.1; -; Genomic_DNA. DR EMBL; Y18658; CAB72095.1; JOINED; Genomic_DNA. DR EMBL; Y18659; CAB72095.1; JOINED; Genomic_DNA. DR EMBL; Y18139; CAB71932.1; -; Genomic_DNA. DR EMBL; U96789; AAC17728.1; -; Genomic_DNA. DR EMBL; U96788; AAC17728.1; JOINED; Genomic_DNA. DR EMBL; Z75172; CAA99487.1; -; Genomic_DNA. DR PIR; A59028; A59028. DR PIR; S42823; S42823. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1IM9. DR SMR; Q29960; 26-302. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Alternative splicing; Glycoprotein; Host-virus interaction; KW Immune response; Membrane; MHC I; Polymorphism; Signal; Transmembrane; KW Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-16 alpha chain. FT /FTId=PRO_0000018879. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VAR_SEQ 299 338 Missing (in isoform 2). FT /FTId=VSP_008096. FT VARIANT 101 101 S -> N (in allele Cw*1602). FT /FTId=VAR_016630. FT VARIANT 104 104 N -> K (in allele Cw*1602). FT /FTId=VAR_016631. FT VARIANT 153 153 H -> D (in allele Cw*1602 and allele FT Cw*1604). FT /FTId=VAR_016632. FT VARIANT 157 157 C -> W (in allele Cw*1602 and allele FT Cw*1604). FT /FTId=VAR_016633. FT VARIANT 180 180 Q -> W (in allele Cw*1604; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016634. SQ SEQUENCE 366 AA; 40753 MW; 5F8001BB016F1610 CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ WMYGCDLGPD GRLLRGYDQS AYDGKDYIAL NEHLRSCTAA DTAAQITQRK WEAARAAEQQ RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHLVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C17_HUMAN Reviewed; 372 AA. AC Q95604; O02864; O02958; Q29643; Q9MY30; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-FEB-2007, entry version 51. DE HLA class I histocompatibility antigen, Cw-17 alpha chain precursor DE (MHC class I antigen Cw*17). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1701). RA Herrero M.J.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1701). RA Wells R.S., Parham P.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1701). RA Herrero M.J., Vilches C.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1701). RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [5] RP NUCLEOTIDE SEQUENCE OF 26-298 (ALLELE CW*1701). RC TISSUE=Blood; RA Yang S., Cereb N.; RT "Nucleotide sequence analysis of HLA-Cw blank alleles from seven B RT cell lines."; RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE OF 1-289 (ALLELE CW*1702). RC TISSUE=Peripheral blood; RA Wang H., Tokunaga K.; RT "HLA-C locus polymorphisms in Japanese."; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-338 (ALLELE CW*1703). RX MEDLINE=99416847; PubMed=10488744; RX DOI=10.1034/j.1399-0039.1999.540208.x; RA van der Vlies S.A., Voorter C.E., van den Berg-Loonen E.M.; RT "There is more to HLA -C than exons 2 and 3: sequencing exons 1, 4 and RT 5."; RL Tissue Antigens 54:169-177(1999). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-17 are known: Cw*1701, CC Cw*1702 and Cw*1703. The sequence shown is that of Cw*1701. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X98742; CAA67294.1; -; mRNA. DR EMBL; U62824; AAB67322.1; -; mRNA. DR EMBL; Y10520; CAA71531.1; -; mRNA. DR EMBL; AJ420252; CAD12437.1; -; Genomic_DNA. DR EMBL; U06835; AAA17674.1; -; mRNA. DR EMBL; D64149; BAA20857.1; -; mRNA. DR EMBL; Y18537; CAB71837.1; -; Genomic_DNA. DR EMBL; Y18538; CAB71837.1; JOINED; Genomic_DNA. DR EMBL; Y18539; CAB71837.1; JOINED; Genomic_DNA. DR EMBL; Y18540; CAB71837.1; JOINED; Genomic_DNA. DR EMBL; Y18541; CAB71837.1; JOINED; Genomic_DNA. DR PIR; A59028; A59028. DR UniGene; Hs.449621; -. DR UniGene; Hs.652210; -. DR UniGene; Hs.77961; -. DR HSSP; P30504; 1IM9. DR SMR; Q95604; 25-302. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR ArrayExpress; Q95604; -. DR GermOnline; ENSG00000204525; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 372 HLA class I histocompatibility antigen, FT Cw-17 alpha chain. FT /FTId=PRO_0000018880. FT TOPO_DOM 25 317 Extracellular (Potential). FT TRANSMEM 318 338 Potential. FT TOPO_DOM 339 372 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 317 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 7 8 QA -> RT (in allele Cw*1702). FT /FTId=VAR_016648. FT VARIANT 10 10 L -> I (in allele Cw*1702). FT /FTId=VAR_016649. FT VARIANT 24 24 A -> T (in allele Cw*1703). FT /FTId=VAR_016650. SQ SEQUENCE 372 AA; 41238 MW; D5DDCE6361D93AA2 CRC64; MRVMAPQALL LLLSGALALI ETWAGSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV NLRKLRGYYN QSEAGSHTIQ RMYGCDLGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DTAAQISQRK LEAAREAEQL RAYLEGECVE WLRGYLENGK ETLQRAERPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL QEPCTLRWKP SSQPTIPNLG IVSGPAVLAV LAVLAVLAVL GAVVAAVIHR RKSSGGKGGS CSQAASSNSA QGSDESLIAC KA // ID 1C18_HUMAN Reviewed; 366 AA. AC Q29865; O78203; P79498; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 28-NOV-2006, entry version 47. DE HLA class I histocompatibility antigen, Cw-18 alpha chain precursor DE (MHC class I antigen Cw*18). GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1801). RX MEDLINE=97161041; PubMed=9008313; RA Vilches C., Bunce M., Sanz L., de Pablo R., Puente S., Kreisler M.; RT "Molecular cloning of two new HLA-C alleles: Cw*1801 and Cw*0706."; RL Tissue Antigens 48:698-702(1996). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE CW*1801). RX MEDLINE=22512041; PubMed=12622774; RX DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE CW*1801). RX MEDLINE=98119594; PubMed=9459506; RA Grundschober C., Labonne M., Javaux F., Steiner Q.G., Gebuhrer L., RA Tiercy J.M.; RT "Sequence of four new HLA-Cw alleles: a possible role of interallelic RT recombination."; RL Tissue Antigens 51:72-79(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*1802). RX MEDLINE=97378891; PubMed=9234488; RA Vilches C., Bunce M., de Pablo R., Moreno M.E., Puente S., Sanz L., RA Kreisler M.; RT "The novel HLA-Cw*1802 allele is associated with B*5703 in the Bubi RT population from Equatorial Guinea."; RL Tissue Antigens 49:644-648(1997). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment through CC interaction with human herpesvirus 8 MIR1 protein. This targets CC the protein for rapid degradation via the ubiquitin system (By CC similarity). CC -!- POLYMORPHISM: The following alleles of Cw-18 are known: Cw*1801 CC (Cw*04GB) and Cw*1802 (Cw*18GB). The sequence shown is that of CC Cw*1801. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X96582; CAA65401.1; -; mRNA. DR EMBL; AJ420253; CAD12438.1; -; Genomic_DNA. DR EMBL; Z80227; CAB02408.1; -; Genomic_DNA. DR EMBL; Y09156; CAA70354.1; -; mRNA. DR HSSP; P30504; 1IM9. DR SMR; Q29865; 26-299. DR Ensembl; ENSG00000198479; Homo sapiens. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Host-virus interaction; Immune response; Membrane; KW MHC I; Polymorphism; Signal; Transmembrane; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-18 alpha chain. FT /FTId=PRO_0000018881. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Potential. FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 319 319 V -> A (in allele Cw*1802). FT /FTId=VAR_016635. SQ SEQUENCE 366 AA; 40933 MW; 67CE7E948E4327D8 CRC64; MRVMAPRALL LLLSGGLALT ETWACSHSMR YFDTAVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV NLRKLRGYYN QSEDGSHTLQ RMFGCDLGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQR RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWKP SSQPTIPIVG IVAGLAVLVV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C28_PANTR Reviewed; 346 AA. AC P16215; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 31-OCT-2006, entry version 50. DE CHLA class I histocompatibility antigen, CH28 alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90201944; PubMed=1690682; RA Lawlor D.A., Warren E., Ward F.E., Parham P.; RT "Comparison of class I MHC alleles in humans and apes."; RL Immunol. Rev. 113:147-185(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88319000; PubMed=3412487; DOI=10.1038/335268a0; RA Lawlor D.A., Ward F.E., Ennis P.D., Jackson A.P., Parham P.; RT "HLA-A and B polymorphisms predate the divergence of humans and RT chimpanzees."; RL Nature 335:268-271(1988). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M30685; AAA87973.1; -; mRNA. DR HSSP; Q29961; 1HSA. DR SMR; P16215; 22-296. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 21 FT CHAIN 22 346 CHLA class I histocompatibility antigen, FT CH28 alpha chain. FT /FTId=PRO_0000018915. FT TOPO_DOM 22 305 Extracellular (Potential). FT TRANSMEM 306 329 Potential. FT TOPO_DOM 330 346 Cytoplasmic (Potential). FT DOMAIN 206 294 Ig-like C1-type. FT REGION 22 111 Alpha-1. FT REGION 112 203 Alpha-2. FT REGION 204 295 Alpha-3. FT REGION 296 305 Connecting peptide. FT CARBOHYD 107 107 N-linked (GlcNAc...) (By similarity). FT DISULFID 122 185 By similarity. FT DISULFID 224 280 By similarity. SQ SEQUENCE 346 AA; 39085 MW; F83E882D5C2E0971 CRC64; MAPRSLLLLF SGALALTETW AGSHSLRYFS TAVSRPGRGE PRYIAVEYVD DTQFLRFDSD AAIPRMEPRE PWVEQEGPQY WERTTGYAKA NAQTDRVALR NLLRRYNQSE AGSHTLQGMN GCDMGPDGRL LRGYHQHAYD GKDYISLNED LRSWTAADTV AQITQRFYEA EEYAEEFRTY LEGECLELLR RYLENGKETL QRADPPKAHI AHHPISDHEA TLRCWALGFY PAEITLTWQR DGEEQTQDTE LVETRPAGDG NFQKWAAVVV PSGEEQRYTC HVQHEGLPQP LTLRWEQSPQ PTIPIVGIVA GLVVLGAVVT GAVVAAVMWR KKSSDRNRGS YSQAAV // ID 1CPX_DIRIM Reviewed; 235 AA. AC O17433; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 28-NOV-2006, entry version 34. DE 1-Cys peroxiredoxin (EC 1.11.1.15) (Thioredoxin peroxidase) (1- DE CysPxn). OS Dirofilaria immitis (Canine heartworm). OC Eukaryota; Metazoa; Nematoda; Chromadorea; Spirurida; Filarioidea; OC Onchocercidae; Dirofilaria. OX NCBI_TaxID=6287; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA McGonigle S., James E.R.; RT "1-Cys peroxidoxin from Dirofilaria immitis."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Thiol specific antioxidant. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- PTM: Cys-49 is the site of oxidation by H(2)O(2). The oxidized CC intermediate might be Cys-SOH (By similarity). CC -!- SIMILARITY: Belongs to the ahpC/TSA family. Rehydrin 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; AF027387; AAB83998.1; -; mRNA. DR HSSP; P30041; 1PRX. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:EC. DR InterPro; IPR000866; AhpC-TSA. DR InterPro; IPR012336; Thiordxn-like_fd. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR Pfam; PF00578; AhpC-TSA; 1. KW Antioxidant; Oxidoreductase; Peroxidase; Redox-active center. FT CHAIN 1 235 1-Cys peroxiredoxin. FT /FTId=PRO_0000135106. FT ACT_SITE 49 49 By similarity. SQ SEQUENCE 235 AA; 26342 MW; BCC198C87D88FD97 CRC64; MTKGILLGDK FPDFRAETNE GFIPSFYDWI GKDSWAILFS HPRDFTPVCT TELARLVQLA PEFNKRNVKL IGLSCDSAES HRKWVDDIMA VCKMKCNDGD TCCSGNKLPF PIIADENRFL ATELGMMDPD ERDENGNALT ARCVFIIGPE KTLKLSILYP ATTGRNFDEI LRVVDSLQLT AVKLVATPVD WKDGDDCVVL PTIDDTEAKK LFGEKINTIE LPSGKHYLRM VAHPK // ID 1OKO_GORGO Reviewed; 362 AA. AC P30388; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 47. DE Class I histocompatibility antigen, GOGO-OKO alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078860; PubMed=1744581; DOI=10.1084/jem.174.6.1491; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X60692; CAA43100.1; -; mRNA. DR PIR; JH0538; JH0538. DR HSSP; P30474; 1A9E. DR SMR; P30388; 25-299. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I_alpha_A1A2. DR InterPro; IPR010579; MHC_I_alpha_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC I; Signal; Transmembrane. FT SIGNAL 1 24 By similarity. FT CHAIN 25 362 Class I histocompatibility antigen, GOGO- FT OKO alpha chain. FT /FTId=PRO_0000018909. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Potential. FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. SQ SEQUENCE 362 AA; 40756 MW; BFE4D9A72C55649D CRC64; MAVVAPRTLL LLLSGTLALT RTWAGSHSMR YFYTTMSRPG RGEPRFISVG YVDDTQFVRF DSDDASPREE PRAPWMEREG PEYWDRNTQI YKAQAQTDRV DLETLRGYYN QSEGGSHTIQ RMYGCEVGPD GRFLRGYLQD AYDGKDYITL NEDLRSWTAA DMAAQITQRK WEAAREAERL RAYMEGTCVE WLRRHLENGK ETLQRTDPPK THMTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPG GDGTFQKWAA VVVPSGKEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLLGA VITGAVVAAM MWRKKSSGRK GGSYSQAASS DSAQGSDVSL TA // ID 209L2_MACMU Reviewed; 256 AA. AC Q8MIS5; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 31-OCT-2006, entry version 28. DE CD209 antigen-like protein 2. GN Name=CD209L2; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH RP ICAM3; HIV-1 AND SIV. RX MEDLINE=22366247; PubMed=12477827; DOI=10.1128/JVI.77.1.217-227.2003; RA Bashirova A.A., Wu L., Cheng J., Martin T.D., Martin M.P., RA Benveniste R.E., Lifson J.D., Kewalramani V.N., Hughes A., RA Carrington M.; RT "Novel member of the CD209 (DC-SIGN) gene family in primates."; RL J. Virol. 77:217-227(2003). CC -!- FUNCTION: Probable pathogen-recognition receptor involved in CC peripheral immune surveillance in liver. May mediate the CC endocytosis of pathogens which are subsequently degraded in CC lysosomal compartments. Probably recognizes in a calcium-dependent CC manner high mannose N-linked oligosaccharides in a variety of CC pathogen antigens. Is a receptor for ICAM3, probably by binding to CC mannose-like carbohydrates (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type II membrane CC protein (By similarity). CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver and axillary CC lymph nodes. At very low levels also found in other tissues. CC -!- MISCELLANEOUS: In vitro, is a weak receptor for HIV-1 and SIV and CC poorly transmits HIV-1 to permissive T-cells relative to CD209. CC -!- SIMILARITY: Contains 1 C-type lectin 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; AY074781; AAL71882.1; -; mRNA. DR UniGene; Mmu.3664; -. DR SMR; Q8MIS5; 105-235. DR InterPro; IPR002353; AntifreezeII. DR InterPro; IPR001304; Lectin_C. DR Pfam; PF00059; Lectin_C; 1. DR PRINTS; PR00356; ANTIFREEZEII. DR SMART; SM00034; CLECT; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. KW Calcium; Endocytosis; Immune response; Lectin; Mannose-binding; KW Membrane; Metal-binding; Receptor; Signal-anchor; Transmembrane. FT CHAIN 1 256 CD209 antigen-like protein 2. FT /FTId=PRO_0000046631. FT TOPO_DOM 1 50 Cytoplasmic (Potential). FT TRANSMEM 51 71 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 72 240 Extracellular (Potential). FT DOMAIN 114 230 C-type lectin. FT MOTIF 14 15 Endocytosis signal (By similarity). FT METAL 199 199 Calcium (By similarity). FT METAL 201 201 Calcium (By similarity). FT METAL 203 203 Calcium (via carbonyl oxygen) (By FT similarity). FT METAL 206 206 Calcium (By similarity). FT METAL 217 217 Calcium (By similarity). FT METAL 218 218 Calcium (By similarity). FT DISULFID 108 119 By similarity. FT DISULFID 136 229 By similarity. FT DISULFID 208 221 By similarity. SQ SEQUENCE 256 AA; 28867 MW; A07C3BA415B9C022 CRC64; MSDSKEPRAQ PLGLLEEEEL ITSSMNFFPR DFGFRQTRGY KSLAGCLGHA PLVLPLLFFT LFTGLLVAIL VQVSKNPSSQ RLDQSKQDEI SQDLSQLKAA VERLCRPCPW EWTFFQGNCY FISNSQRNWH DSITACQEVG AQLVVIKSAE EQNFLQLQSS RSNRFAWMGL SDLNQEDMWQ WVDDSPLSTS FKQYWNRGEP NNIGEEDCVE FNGNGWNDDK CSAAKFWICK KSAASCSRDE GQLLSSASAS PIAHAA // ID 21KD_DAUCA Reviewed; 193 AA. AC P17407; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 31-OCT-2006, entry version 35. DE 21 kDa protein precursor (1.2 protein). OS Daucus carota (Carrot). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; OC Daucinae; Daucus. OX NCBI_TaxID=4039; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Aleith F.; RL Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X52395; CAA36642.1; -; mRNA. DR PIR; S10911; S10911. DR InterPro; IPR006501; PME_inhib. DR InterPro; IPR007186; PMEI. DR Pfam; PF04043; PMEI; 1. DR TIGRFAMs; TIGR01614; PME_inhib; 1. KW Signal. FT SIGNAL 1 22 Potential. FT CHAIN 23 193 21 kDa protein. FT /FTId=PRO_0000020573. SQ SEQUENCE 193 AA; 21041 MW; 75940F09ACAB9796 CRC64; MKLSKSTLVF SALLVILAAA SAAPANQFIK TSCTLTTYPA VCEQSLSAYA KTIQNNPQEL ASTALQVSLT RTQQAQTFMK RLNKFKGLKA RQYAAIHDCL EEVEDSLDRV SRSCDEMKNL SHAKGNDFTF RMSNVETWVS AALTDETTCM DGFAGKGMDG KIKESVRAQV VAVARVTSNA LALVNNFAAK HKH // ID 21KD_ZYMMO Reviewed; 184 AA. AC P15256; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 31-OCT-2006, entry version 18. DE 20.9 kDa protein (ORF 2). OS Zymomonas mobilis. OG Plasmid pZM2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=542; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 10988 / NCIB 8938 / NRRL B-806 / ZM1; RA Misawa N., Nakamura K.; RT "The nucleotide sequence of the 2.7 kilobase pair plasmid of Zymomonas RT mobilis ATCC 10988."; RL J. Biotechnol. 12:63-70(1989). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14438; CAA32610.1; -; Genomic_DNA. DR PIR; S06695; S06695. KW Plasmid. FT CHAIN 1 184 20.9 kDa protein. FT /FTId=PRO_0000064355. SQ SEQUENCE 184 AA; 20962 MW; 83D50576B6F2802B CRC64; MATKLRKQPI RYDENPFIEG MVVPVKSQRV QLSRLGRDDN ILVNQATGEM QGTHVTTYRR VDSEEFVKLF STNIALTFEL GAAGIKAFSV LVWILQDKGI SKDLVPLDKF VLEDFLNAQE KKLALSQATF ARGLAELEKA KIIAKHVRQG WYFINPNFVF NGDRVAFTTV IERKKTLQKQ DESE // ID 22P1_RAT Reviewed; 176 AA. AC P22282; Q63674; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 20-FEB-2007, entry version 52. DE Cystatin-related protein 1 precursor (CRP-1) (Prostatic 22 kDa DE glycoprotein P22K16/P22K20) (Androgen-regulated 20 kDa protein). GN Name=Andpro; Synonyms=Crp1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Prostate; RX MEDLINE=91125374; PubMed=2280780; RA Winderickx J., Hemschoote K., de Clercq N., van Dijck P., Peeters B., RA Rombauts W., Verhoeven G., Heyns W.; RT "Tissue-specific expression and androgen regulation of different genes RT encoding rat prostatic 22-kilodalton glycoproteins homologous to human RT and rat cystatin."; RL Mol. Endocrinol. 4:657-667(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 32-81. RX MEDLINE=90001187; PubMed=2477055; DOI=10.1021/bi00441a032; RA Ho K.-C., Snoek R., Quarmby V., Viskochil D.H., Rennie P.S., RA Wilson E.M., French F.S., Bruchovsky N.; RT "Primary structure and androgen regulation of a 20-kilodalton protein RT specific to rat ventral prostate."; RL Biochemistry 28:6367-6373(1989). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Wistar; RA Vercaeren I., Winderickx J., Devos A., Peeters B., Heyns W.; RT "An effect of androgens on the length of the poly(A)-tail and RT alternative splicing cause size heterogeneity of the messenger RT ribonucleic acids encoding cystatin-related protein."; RL Endocrinology 131:2496-2502(1992). RN [4] RP ERRATUM. RX MEDLINE=93178358; PubMed=7679983; DOI=10.1210/en.132.3.2496; RA Vercaeren I., Winderickx J., Devos A., Peeters B., Heyns W.; RL Endocrinology 132:2496-2502(1993). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93216117; PubMed=8462870; DOI=10.1016/0378-1119(93)90323-U; RA Devos A., de Clercq N., Vercaeren I., Heyns W., Rombauts W., RA Peeters B.; RT "Structure of rat genes encoding androgen-regulated cystatin-related RT proteins (CRPs): a new member of the cystatin superfamily."; RL Gene 125:159-167(1993). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94086539; PubMed=8262963; RA Ho K.-C., Marschke K.B., Tan J.A., Power S.G.A., Wilson E.M., RA French F.S.; RT "A complex response element in intron 1 of the androgen-regulated 20- RT kDa protein gene displays cell type-dependent androgen receptor RT specificity."; RL J. Biol. Chem. 268:27226-27235(1993). CC -!- TISSUE SPECIFICITY: Prostate and lacrimal gland. CC -!- INDUCTION: By androgens. CC -!- SIMILARITY: Belongs to the cystatin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M58167; AAA63498.1; -; mRNA. DR EMBL; Z13993; CAA78384.1; -; Genomic_DNA. DR EMBL; S48988; AAA12401.1; -; mRNA. DR EMBL; S57980; AAB26027.1; -; Genomic_DNA. DR EMBL; L12454; AAA40732.1; -; Genomic_DNA. DR EMBL; M27901; AAA42345.1; -; mRNA. DR PIR; A49304; A49304. DR UniGene; Rn.9977; -. DR Ensembl; ENSRNOG00000031840; Rattus norvegicus. DR KEGG; rno:25030; -. DR RGD; 2115; Andpro. DR ArrayExpress; P22282; -. DR GermOnline; ENSRNOG00000031840; Rattus norvegicus. DR GO; GO:0005829; C:cytosol; IDA:RGD. DR GO; GO:0005634; C:nucleus; IDA:RGD. DR GO; GO:0030521; P:androgen receptor signaling pathway; IMP:RGD. DR InterPro; IPR000010; Prot_inh_cystat. DR SMART; SM00043; CY; 1. KW Cleavage on pair of basic residues; Direct protein sequencing; KW Glycoprotein; Protease inhibitor; Signal; Thiol protease inhibitor. FT SIGNAL 1 26 Potential. FT PROPEP 27 31 Potential. FT /FTId=PRO_0000006671. FT CHAIN 32 176 Cystatin-related protein 1. FT /FTId=PRO_0000006672. FT CARBOHYD 71 71 N-linked (GlcNAc...). FT DISULFID 129 139 By similarity. FT DISULFID 153 173 By similarity. FT CONFLICT 1 22 Missing (in Ref. 2). FT CONFLICT 23 24 HA -> MQ (in Ref. 2). FT CONFLICT 157 157 V -> L (in Ref. 2, 3 and 6). SQ SEQUENCE 176 AA; 21060 MW; 3D5355EC56E3CBA0 CRC64; MCKTLHGTLL LLAIFVLFLN FSHATAKRTR RGMEIFEKNF IDKNKLKDVY DVFKYLYNTH SADTYLSNIK NESFTMNIWG FGEIEMVKTK CRKIDSDFYK CSFQREFYNL KRTPGETMYY ISLPGSVRCR KLLSKLDNCP FEEQTEQLKR EICYFVVYPD YIEQNIHAVR FDCYTK // ID 22P2_RAT Reviewed; 176 AA. AC P22283; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 23-JAN-2007, entry version 51. DE Cystatin-related protein 2 precursor (Prostatic 22 kDa glycoprotein DE P22K15). GN Name=Crp2; Synonyms=P22k15; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Prostate; RX MEDLINE=91125374; PubMed=2280780; RA Winderickx J., Hemschoote K., de Clercq N., van Dijck P., Peeters B., RA Rombauts W., Verhoeven G., Heyns W.; RT "Tissue-specific expression and androgen regulation of different genes RT encoding rat prostatic 22-kilodalton glycoproteins homologous to human RT and rat cystatin."; RL Mol. Endocrinol. 4:657-667(1990). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Wistar; RA Vercaeren I., Winderickx J., Devos A., Peeters B., Heyns W.; RT "An effect of androgens on the length of the poly(A)-tail and RT alternative splicing cause size heterogeneity of the messenger RT ribonucleic acids encoding cystatin-related protein."; RL Endocrinology 131:2496-2502(1992). RN [3] RP ERRATUM. RX MEDLINE=93178358; PubMed=7679983; DOI=10.1210/en.132.3.2496; RA Vercaeren I., Winderickx J., Devos A., Peeters B., Heyns W.; RL Endocrinology 132:2496-2502(1993). RN [4] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=93216117; PubMed=8462870; DOI=10.1016/0378-1119(93)90323-U; RA Devos A., de Clercq N., Vercaeren I., Heyns W., Rombauts W., RA Peeters B.; RT "Structure of rat genes encoding androgen-regulated cystatin-related RT proteins (CRPs): a new member of the cystatin superfamily."; RL Gene 125:159-167(1993). CC -!- TISSUE SPECIFICITY: Prostate. CC -!- INDUCTION: By androgens. CC -!- SIMILARITY: Belongs to the cystatin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M58169; AAA63499.1; -; mRNA. DR EMBL; Z13994; CAA78385.1; -; Genomic_DNA. DR PIR; JT0616; JT0616. DR UniGene; Rn.43503; -. DR Ensembl; ENSRNOG00000030184; Rattus norvegicus. DR RGD; 727814; P22k15. DR ArrayExpress; P22283; -. DR GermOnline; ENSRNOG00000030184; Rattus norvegicus. DR InterPro; IPR000010; Prot_inh_cystat. DR SMART; SM00043; CY; 1. KW Glycoprotein; Protease inhibitor; Signal; Thiol protease inhibitor. FT SIGNAL 1 26 Potential. FT PROPEP 27 30 Potential. FT /FTId=PRO_0000006673. FT CHAIN 31 176 Cystatin-related protein 2. FT /FTId=PRO_0000006674. FT CARBOHYD 71 71 N-linked (GlcNAc...) (Probable). FT DISULFID 129 139 By similarity. FT DISULFID 153 173 By similarity. FT CONFLICT 149 176 KREICYFQLYPDYIEQNIRSVRFNCYTK -> IERNMLLST FT VS (in Ref. 2). SQ SEQUENCE 176 AA; 21013 MW; 1B8F4FAEBA06B461 CRC64; MYKTLCGTQL LLAIFVLFLN FSHATAKGTR GPMEIFKKNF MEKNKLNDVY DIFKFLYNKF SHDTYLSNIK NQSFTMNTWG FGEIEVVKTK CRKIDSDFYK CSFQWEFCNI KRTPGVTIYY ITLPGSVRCR KLLSKLVNCP FEEQTEQLKR EICYFQLYPD YIEQNIRSVR FNCYTK // ID 23KD_BACST Reviewed; 22 AA. AC P80166; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 31-OCT-2006, entry version 19. DE 23 kDa basic protein (Fragment). OS Bacillus stearothermophilus (Geobacillus stearothermophilus). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1422; RN [1] RP PROTEIN SEQUENCE. RA Vorgias C.E.; RL Submitted (OCT-1992) to Swiss-Prot. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR InterPro; IPR007551; DUF520. DR Pfam; PF04461; DUF520; 1. KW Direct protein sequencing. FT CHAIN 1 >22 23 kDa basic protein. FT /FTId=PRO_0000064356. FT NON_TER 22 22 SQ SEQUENCE 22 AA; 2377 MW; 96C604E42CE0BFFC CRC64; XKESSFDIVS KVDLSEVANA IN // ID 24KD_PLACH Reviewed; 37 AA. AC P14592; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 20-FEB-2007, entry version 20. DE 24 kDa antigen (Fragment). OS Plasmodium chabaudi. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodium; Plasmodium (Vinckeia). OX NCBI_TaxID=5825; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87174746; PubMed=3550696; DOI=10.1093/nar/15.5.2203; RA Langsley G., Sibilli L., Mattei D., Falanga P., Mercereau-Puijalon O.; RT "Karyotype comparison between P. chabaudi and P. falciparum: analysis RT of a P. chabaudi cDNA containing sequences highly repetitive in P. RT falciparum."; RL Nucleic Acids Res. 15:2203-2211(1987). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X04892; CAA28580.1; -; mRNA. KW Malaria. FT CHAIN <1 37 24 kDa antigen. FT /FTId=PRO_0000217175. FT NON_TER 1 1 SQ SEQUENCE 37 AA; 4757 MW; E6F0EB6A45CFEBD5 CRC64; NYCYYMVDYL TFYNIKNYKI YTYAQRLLEI YFSYLSI // ID 25KD_SARPE Reviewed; 258 AA. AC P23170; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 31-OCT-2006, entry version 36. DE Development-specific 25 kDa protein. OS Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea; OC Sarcophagidae; Sarcophaga; Boettcherisca. OX NCBI_TaxID=7386; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=85289142; PubMed=2993269; RA Matsumoto N., Sekimizu K., Soma G., Ohmura Y., Andoh T., Nakanishi Y., RA Obinata M., Natori S.; RT "Structural analysis of a developmentally regulated 25-kDa protein RT gene of Sarcophaga peregrina."; RL J. Biochem. 97:1501-1508(1985). RN [2] RP SEQUENCE REVISION. RX MEDLINE=96235235; PubMed=8647115; RA Horio T., Kubo T., Natori S.; RT "Purification and cDNA cloning of the alcohol dehydrogenase of the RT flesh fly Sarcophaga peregrina. A structural relationship between RT alcohol dehydrogenase and a 25-kDa protein."; RL Eur. J. Biochem. 237:698-703(1996). CC -!- DEVELOPMENTAL STAGE: Expressed in the fat body of middle third- CC instar larvae. 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; X02570; CAA26412.1; -; Genomic_DNA. DR PIR; A24181; A24181. DR HSSP; P10807; 1B16. DR InterPro; IPR002347; ADH_short_C2. DR InterPro; IPR002426; Ceratitis_ADH. DR InterPro; IPR002424; Insect_ADH_fam. DR InterPro; IPR002198; SDR. DR PANTHER; PTHR19410; ADH_short; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR01169; CERATITISADH. DR PRINTS; PR01167; INSADHFAMILY. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. KW Oxidoreductase. FT CHAIN 1 258 Development-specific 25 kDa protein. FT /FTId=PRO_0000054445. FT NP_BIND 10 34 NAD or NADP (By similarity). FT ACT_SITE 151 151 Proton acceptor (By similarity). FT BINDING 138 138 Substrate (By similarity). SQ SEQUENCE 258 AA; 28633 MW; 651CB188A5D1547A CRC64; MMDWNNKNVV YVGGFSGFGY QVCQMMMKKP MKHLIVCSRM ENVEMLKKLQ AINTSVKVMF VQMNIADYAS IVKGVKQVIG HVGHVDVLIN GVGGLADKDV ETTVAVNLTG LINTTLMFMP YMDKTQSGHG GMVVSISSVY GLEPGPAFSV YSAAKHGGIG FTRSMADEHL YHKTGVAFMC ICPAMTSTEL MMNKRDMNWM KWVPHSEEMW KMVMDAKMQT PEECAVNMMT AMEQAKNGAI YICSTSGMKE ITPTVYMH // ID 26KD_BACCE Reviewed; 20 AA. AC P83072; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 23-JAN-2007, entry version 12. DE 26 kDa protein (Fragment). OS Bacillus cereus. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1396; RN [1] RP PROTEIN SEQUENCE, AND INDUCTION. RC STRAIN=NCIMB 11796 / DSM 626; RX PubMed=11872115; DOI=10.1046/j.1365-2672.2002.01541.x; RA Browne N., Dowds B.C.A.; RT "Acid stress in the food pathogen Bacillus cereus."; RL J. Appl. Microbiol. 92:404-414(2002). CC -!- INDUCTION: Under acid-stress, this protein is expressed at a CC higher level in wild type B.cereus than in the acid-sensitive CC mutant strain NB1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Direct protein sequencing. FT CHAIN 1 >20 26 kDa protein. FT /FTId=PRO_0000270968. FT NON_TER 20 20 SQ SEQUENCE 20 AA; 2176 MW; 31B335AF0E538E30 CRC64; MKLIAKTRIL NTLVFSAAGK // ID 28KD_MYCLE Reviewed; 236 AA. AC P19361; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 31-OCT-2006, entry version 35. DE 28 kDa antigen precursor. GN OrderedLocusNames=ML0091; OS Mycobacterium leprae. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1769; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89067516; PubMed=3058804; RA Cherayil B.J., Young R.A.; RT "A 28-kDa protein from Mycobacterium leprae is a target of the human RT antibody response in lepromatous leprosy."; RL J. Immunol. 141:4370-4375(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN; RX MEDLINE=21128732; PubMed=11234002; DOI=10.1038/35059006; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). CC -!- SIMILARITY: To M.tuberculosis ERP. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M23232; AAA25345.1; -; Genomic_DNA. DR EMBL; AL583917; CAC29599.1; -; Genomic_DNA. DR PIR; A30557; A30557. DR GenomeReviews; AL450380_GR; ML0091. DR KEGG; mle:ML0091; -. DR Leproma; ML0091; -. DR BioCyc; MLEP1769:ML0091-MONOMER; -. DR InterPro; IPR008165; XGLTT_domain. DR ProDom; PD003992; XGLTT_domain; 1. KW Complete proteome; Signal. FT SIGNAL 1 22 FT CHAIN 23 236 28 kDa antigen. FT /FTId=PRO_0000020574. SQ SEQUENCE 236 AA; 23784 MW; 5A9760D06ADACDFB CRC64; MPNRRRCKLS TAISTVATLA IASPCAYFLV YEPTASAKPA AKHYEFKQAA SIADLPGEVL DAISQGLSQF GINLPPVPSL TGTDDPGNGL RTPGLTSPDL TNQELGTPVL TAPGTGLTPP VTGSPICTAP DLNLGGTCPS EVPITTPISL DPGTDGTYPI LGDPSTLGGT SPISTSSGEL VNDLLKVANQ LGASQVMDLI KGVVMPAVMQ GVQNGNVAGD LSGSVTPAAI SLIPVT // ID 28KD_TRIFO Reviewed; 29 AA. AC P33405; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 31-OCT-2006, entry version 20. DE 28 kDa protein (Fragment). OS Tritrichomonas foetus (Trichomonas foetus). OC Eukaryota; Parabasalidea; Trichomonada; Trichomonadida; OC Trichomonadidae; Tritrichomonadinae; Tritrichomonas. OX NCBI_TaxID=5724; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=93307628; PubMed=8319888; DOI=10.1016/0378-1097(93)90251-V; RA Irvine J.W., Coombs G.H., North M.J.; RT "Purification of cysteine proteinases from trichomonads using RT bacitracin-sepharose."; RL FEMS Microbiol. Lett. 110:113-120(1993). CC -!- MISCELLANEOUS: Binds to bacitracin. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Direct protein sequencing. FT CHAIN 1 >29 28 kDa protein. FT /FTId=PRO_0000064357. FT UNSURE 12 12 V or Y. FT UNSURE 13 13 V or W. FT NON_TER 29 29 SQ SEQUENCE 29 AA; 3281 MW; 155FEDA75B7496E0 CRC64; ARYAILFAGS NVVYNAXXQA DIYTIYTFL // ID 29C0_ANCSP Reviewed; 50 AA. AC P84001; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 31-OCT-2006, entry version 9. DE Venom protein ANC29C0 (Fragment). OS Ancylometes sp. (South American fishing spider). OC Eukaryota; Metazoa; Arthropoda; Chelicerata; Arachnida; Araneae; OC Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Ancylometes. OX NCBI_TaxID=280265; RN [1] RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS RP SPECTROMETRY. RC TISSUE=Venom; RA Richardson M., Pimenta A.M.C., Bemquerer M.P., Santoro M.M., RA Figueiredo S.G., Cordeiro M.N.; RT "Protein ANC29C0 from venom of South American fishing spider RT (Ancylometes spp.) has sequence similarities to neurotoxic peptide RT Caeron precursor from Bark spider (Caerostris extrusa)."; RL Submitted (JUN-2004) to Swiss-Prot. CC -!- FUNCTION: Possible neurotoxin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- MASS SPECTROMETRY: MW=9571; METHOD=Electrospray; RANGE=1-?; CC NOTE=Ref.1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR InterPro; IPR008197; WAP. DR PRINTS; PR00003; 4DISULPHCORE. KW Direct protein sequencing; Neurotoxin; Toxin. FT CHAIN 1 >50 Venom protein ANC29C0. FT /FTId=PRO_0000087682. FT NON_TER 50 50 SQ SEQUENCE 50 AA; 5679 MW; 3B06738CA0940B53 CRC64; ANACTKQADC AEDECCLDNL FFKRPYCEMR YGAGKRCAAA SVYKEDKDLY // ID 2A5A_ARATH Reviewed; 495 AA. AC O04375; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 23-JAN-2007, entry version 36. DE Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' DE alpha isoform (PP2A, B' subunit, alpha isoform) (AtB' alpha). GN Name=B'ALPHA; OrderedLocusNames=At5g03470; ORFNames=F12E4.240; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX MEDLINE=97274652; PubMed=9128737; RA Latorre K.A., Harris D.M., Rundle S.J.; RT "Differential expression of three Arabidopsis genes encoding the B' RT regulatory subunit of protein phosphatase 2A."; RL Eur. J. Biochem. 245:156-163(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016721; PubMed=11130714; DOI=10.1038/35048507; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP INTERACTION WITH AALPHA. RX MEDLINE=99191692; PubMed=10091592; RX DOI=10.1046/j.1432-1327.1999.00154.x; RA Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S., RA Rundle S.J.; RT "Molecular characterization of the B' regulatory subunit gene family RT of Arabidopsis protein phosphatase 2A."; RL Eur. J. Biochem. 260:127-136(1999). RN [5] RP NOMENCLATURE. RX MEDLINE=22063724; PubMed=12068121; DOI=10.1104/pp.020004; RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.; RT "Molecular characterization and evolution of the protein phosphatase RT 2A B' regulatory subunit family in plants."; RL Plant Physiol. 129:808-822(2002). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families). CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, higher levels in CC leaves. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; U73526; AAB58900.1; -; mRNA. DR EMBL; AL162751; CAB83307.1; -; Genomic_DNA. DR EMBL; BT002933; AAO22747.1; -; mRNA. DR PIR; T48372; T48372. DR UniGene; At.19971; -. DR GenomeReviews; BA000015_GR; AT5G03470. DR KEGG; ath:At5g03470; -. DR TAIR; At5g03470; -. DR ArrayExpress; O04375; -. DR GermOnline; AT5G03470; Arabidopsis thaliana. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. FT CHAIN 1 495 Serine/threonine protein phosphatase 2A FT 57 kDa regulatory subunit B' alpha FT isoform. FT /FTId=PRO_0000071460. SQ SEQUENCE 495 AA; 57536 MW; 545F041C4ACB4A29 CRC64; MFKKIMKGAN RKASKAEAND SSMYGFDPPG RSGPGSNMIV NHASRGSLVP SSPNSMAAAT TQPPPMYSVE PLPLFRDVSV SERQSLFLRK LQICCFQFDF TDTLKNAREK EIKRQTLLEL VDFIQSGAGK LTEVCQEEMV KMISVNIFRC LPPASHENTG QEPADLEEEE PYLEPSWPHL QLIYELLLRY IVPSDTDTKV AKRYIDHSFV LRLLELFETE DPREREYLKT ILHRIYGKFM VHRPFIRKAM NHIFYRFIYE TERHSGIGEL LEILGSIING FALPMKEEHK LFLIRALIPL HKPKPIAMYH QQLSYCIVQF VEKDYKLADT VIRGLLKFWP VTNCTKEVLF LGELEEVLEA TQTVEFQRCM VPLFQQIARC LSSSNFQVAE RALFLWNNEH VVGLIAQNRG VILPIIFASL EKNIESHWNQ AVHGLSANIK RMFMEMDPEL FEECQQQYEE KQAKSKQVEE QRQNRWRRLD EAVEERERED PMITS // ID 2A5A_HUMAN Reviewed; 486 AA. AC Q15172; Q2NL72; Q5VVB2; Q8TBI9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 59. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE alpha isoform (PP2A, B subunit, B' alpha isoform) (PP2A, B subunit, DE B56 alpha isoform) (PP2A, B subunit, PR61 alpha isoform) (PP2A, B DE subunit, R5 alpha isoform). GN Name=PPP2R5A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Mammary cancer; RX MEDLINE=96064678; PubMed=7592815; DOI=10.1074/jbc.270.44.26123; RA McCright B., Virshup D.M.; RT "Identification of a new family of protein phosphatase 2A regulatory RT subunits."; RL J. Biol. Chem. 270:26123-26128(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., RA Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Hippocampus, 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). RN [4] RP PROTEIN SEQUENCE OF 47-56; 129-132; 347-354; 448-462 AND 471-480. RC TISSUE=Brain; RX MEDLINE=96276417; PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [5] RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX MEDLINE=96355607; PubMed=8703017; DOI=10.1074/jbc.271.36.22081; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- INTERACTION: CC Q9BVP2:GNL3; NbExp=1; IntAct=EBI-641666, EBI-641642; CC Q5FBB7:SGOL1; NbExp=1; IntAct=EBI-641666, EBI-989069; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Widely expressed with the highest expression CC in heart and skeletal muscle. CC -!- PTM: Phosphorylated on serine residues. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; L42373; AAC37601.1; -; mRNA. DR EMBL; AL451060; CAH71821.1; -; Genomic_DNA. DR EMBL; AL360091; CAH71821.1; JOINED; Genomic_DNA. DR EMBL; AL360091; CAH73229.1; -; Genomic_DNA. DR EMBL; AL451060; CAH73229.1; JOINED; Genomic_DNA. DR EMBL; BC022474; AAH22474.1; -; mRNA. DR EMBL; BC110883; AAI10884.1; -; mRNA. DR PIR; I55449; I55449. DR UniGene; Hs.497684; -. DR DIP; DIP:459N; -. DR IntAct; Q15172; -. DR OGP; Q15172; -. DR Ensembl; ENSG00000066027; Homo sapiens. DR KEGG; hsa:5525; -. DR H-InvDB; HIX0001568; -. DR HGNC; HGNC:9309; PPP2R5A. DR MIM; 601643; gene. DR ArrayExpress; Q15172; -. DR GermOnline; ENSG00000066027; Homo sapiens. DR RZPD-ProtExp; A0564; -. DR RZPD-ProtExp; IOH11239; -. DR RZPD-ProtExp; RZPDo839C05147; -. DR RZPD-ProtExp; RZPDo839C05148; -. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR002554; B56. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF01603; B56; 1. KW Direct protein sequencing; Phosphorylation. FT CHAIN 1 486 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit alpha isoform. FT /FTId=PRO_0000071448. FT COMPBIAS 2 5 Poly-Ser. FT CONFLICT 52 52 E -> F (in Ref. 4). FT CONFLICT 54 54 H -> S (in Ref. 4). FT CONFLICT 176 176 Q -> R (in Ref. 3; AAH22474). FT CONFLICT 389 389 D -> N (in Ref. 3; AAH22474). FT CONFLICT 451 451 R -> E (in Ref. 4). SQ SEQUENCE 486 AA; 56194 MW; D31407F7032A6D44 CRC64; MSSSSPPAGA ASAAISASEK VDGFTRKSVR KAQRQKRSQG SSQFRSQGSQ AELHPLPQLK DATSNEQQEL FCQKLQQCCI LFDFMDSVSD LKSKEIKRAT LNELVEYVST NRGVIVESAY SDIVKMISAN IFRTLPPSDN PDFDPEEDEP TLEASWPHIQ LVYEFFLRFL ESPDFQPSIA KRYIDQKFVQ QLLELFDSED PRERDFLKTV LHRIYGKFLG LRAFIRKQIN NIFLRFIYET EHFNGVAELL EILGSIINGF ALPLKAEHKQ FLMKVLIPMH TAKGLALFHA QLAYCVVQFL EKDTTLTEPV IRGLLKFWPK TCSQKEVMFL GEIEEILDVI EPTQFKKIEE PLFKQISKCV SSSHFQVAER ALYFWNNEYI LSLIEENIDK ILPIMFASLY KISKEHWNPT IVALVYNVLK TLMEMNGKLF DDLTSSYKAE RQREKKKELE REELWKKLEE LKLKKALEKQ NSAYNMHSIL SNTSAE // ID 2A5A_MOUSE Reviewed; 486 AA. AC Q6PD03; Q8R1U7; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 25. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE alpha isoform (PP2A, B subunit, B' alpha isoform) (PP2A, B subunit, DE B56 alpha isoform) (PP2A, B subunit, PR61 alpha isoform) (PP2A, B DE subunit, R5 alpha isoform) (PR61alpha). GN Name=Ppp2r5a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Embryonic brain, 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 IDENTIFICATION, AND TISSUE SPECIFICITY. RX MEDLINE=23267811; PubMed=15095873; DOI=10.1016/j.jmb.2003.12.047; RA Martens E., Stevens I., Janssens V., Vermeesch J., Goetz J., Goris J., RA Van Hoof C.; RT "Genomic organisation, chromosomal localisation tissue distribution RT and developmental regulation of the PR61/B' regulatory subunits of RT protein phosphatase 2A in mice."; RL J. Mol. Biol. 336:971-986(2004). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in thymus CC and ovary. CC -!- PTM: Phosphorylated on serine residues (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; BC023062; AAH23062.1; ALT_INIT; mRNA. DR EMBL; BC059026; AAH59026.1; -; mRNA. DR EMBL; BK000647; DAA01426.1; -; mRNA. DR UniGene; Mm.205569; -. DR Ensembl; ENSMUSG00000026626; Mus musculus. DR MGI; MGI:2388479; Ppp2r5a. DR ArrayExpress; Q6PD03; -. DR GermOnline; ENSMUSG00000026626; Mus musculus. DR RZPD-ProtExp; IOM20392; -. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR002554; B56. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF01603; B56; 1. KW Phosphorylation. FT CHAIN 1 486 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit alpha isoform. FT /FTId=PRO_0000071449. SQ SEQUENCE 486 AA; 56347 MW; BC9B0B80446C1AD2 CRC64; MSSPSPPAPV ACAAISASEK VDGFTRKSVR KAQRQKRSQG SSQFRSQGSQ AELHPLPQLK DATSNEQQEL FCQKLQQCCV LFDFMDSVSD LKSKEIKRAT LNELVEYVST NRGVIVESAY SDIVKMISAN IFRTLPPSDN PDFDPEEDEP TLEASWPHIQ LVYEFFLRFL ESPDFQPSIA KRYIDQKFVQ QLLELFDSED PRERDFLKTV LHRIYGKFLG LRAFIRKQIN NIFLRFIYET EHFNGVAELL EILGSIINGF ALPLKAEHKQ FLMKVLIPMH TAKGLALFHA QLAYCVVQFL EKDTTLTEPV IRGLLKFWPK TCSQKEVMFL GEIEEILDVI EPTQFKKIEE PLFKQISKCV SSSHFQVAER ALYFWNNEYI LSLIEENIDK ILPIMFASLY KISKEHWNQT IVALVYNVLK TLMEMNGKLF DDLTSSYKAE RQREKKKELE REELWKKLEE LQLKKALEKQ NNAYNMHSIR SSTSAK // ID 2A5B_ARATH Reviewed; 499 AA. AC O04376; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 23-JAN-2007, entry version 36. DE Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' DE beta isoform (PP2A, B' subunit, beta isoform) (AtB' beta). GN Name=B'BETA; OrderedLocusNames=At3g09880; ORFNames=F8A24.7; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX MEDLINE=97274652; PubMed=9128737; RA Latorre K.A., Harris D.M., Rundle S.J.; RT "Differential expression of three Arabidopsis genes encoding the B' RT regulatory subunit of protein phosphatase 2A."; RL Eur. J. Biochem. 245:156-163(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP INTERACTION WITH AALPHA. RX MEDLINE=99191692; PubMed=10091592; RX DOI=10.1046/j.1432-1327.1999.00154.x; RA Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S., RA Rundle S.J.; RT "Molecular characterization of the B' regulatory subunit gene family RT of Arabidopsis protein phosphatase 2A."; RL Eur. J. Biochem. 260:127-136(1999). RN [5] RP NOMENCLATURE. RX MEDLINE=22063724; PubMed=12068121; DOI=10.1104/pp.020004; RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.; RT "Molecular characterization and evolution of the protein phosphatase RT 2A B' regulatory subunit family in plants."; RL Plant Physiol. 129:808-822(2002). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families). CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, higher levels in CC cotyledons and flowers. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; U73527; AAB58901.1; -; mRNA. DR EMBL; AC015985; AAF23248.1; -; Genomic_DNA. DR EMBL; AY113852; AAM44900.1; -; mRNA. DR EMBL; AY072226; AAL60047.1; -; mRNA. DR UniGene; At.44943; -. DR GenomeReviews; BA000014_GR; AT3G09880. DR KEGG; ath:At3g09880; -. DR TAIR; At3g09880; -. DR ArrayExpress; O04376; -. DR GermOnline; AT3G09880; Arabidopsis thaliana. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR002554; B56. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF01603; B56; 1. FT CHAIN 1 499 Serine/threonine protein phosphatase 2A FT 57 kDa regulatory subunit B' beta FT isoform. FT /FTId=PRO_0000071461. FT COMPBIAS 61 65 Poly-Pro. SQ SEQUENCE 499 AA; 57472 MW; BA375FA980286A0F CRC64; MFKKIMKGGH RKPSKSEANE PSSYGIGLPD NRSGPGSNVV VSHASRGALV NSSPSPVTAT PPPPPLGSVE PLPLFRDVPV SERQTLFLRK LQNCCFLFDF TDTIKNARDK EIKRQTLLEL VDFIQSGSSK ISESCQEEMI KMISVNIFRS LPPASHENTG QEPADPEEEE PYLEPSWPHL QLVYELLLRY VVSTDTDTKV AKRYIDHSFV LKLLDLFDSE DPREREYLKT ILHRIYGKFM VHRPFIRKAI NNIFYRFIYE TERHSGIGEL LEILGSIING FALPMKEEHK LFLIRVLIPL HKPKPIVVYH QQLSYCIVQF VEKDYKLADT VIRGLLKYWP VTNCSKENLF LGELEEVLEA TQPVEFQRCM VPLFQQIGRC LTSSHFQVAE RALFLWNNEH IVGLIAQNRS VILPIIYPTL EKNIQSHWNQ AVHGLTTNIK KMFMEMDPEL FEECQRQYEE KQAKSKEVEE QRQYTWKRLA EAAAERDGGG GEEDHMITS // ID 2A5B_HUMAN Reviewed; 497 AA. AC Q15173; Q13853; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 61. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta DE isoform (PP2A, B subunit, B' beta isoform) (PP2A, B subunit, B56 beta DE isoform) (PP2A, B subunit, PR61 beta isoform) (PP2A, B subunit, R5 DE beta isoform). GN Name=PPP2R5B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1). RC TISSUE=Fetal brain; RX MEDLINE=96064678; PubMed=7592815; DOI=10.1074/jbc.270.44.26123; RA McCright B., Virshup D.M.; RT "Identification of a new family of protein phosphatase 2A regulatory RT subunits."; RL J. Biol. Chem. 270:26123-26128(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2), AND PARTIAL PROTEIN RP SEQUENCE. RC TISSUE=Brain; RX MEDLINE=96276417; PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-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 [4] RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX MEDLINE=96355607; PubMed=8703017; DOI=10.1074/jbc.271.36.22081; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Beta-1; CC IsoId=Q15173-1; Sequence=Displayed; CC Name=Beta-2; CC IsoId=Q15173-2; Sequence=VSP_005109; CC -!- TISSUE SPECIFICITY: Highest expression in brain. CC -!- INDUCTION: By retinoic acid; in neuroblastoma cell lines. CC -!- PTM: At least isoform Beta-1 is phosphorylated on serine residues. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; L42374; AAC37602.1; -; mRNA. DR EMBL; Z69028; CAA93152.1; -; mRNA. DR EMBL; BC045619; AAH45619.1; -; mRNA. DR PIR; I70147; I70147. DR UniGene; Hs.75199; -. DR Ensembl; ENSG00000068971; Homo sapiens. DR KEGG; hsa:5526; -. DR HGNC; HGNC:9310; PPP2R5B. DR MIM; 601644; gene. DR LinkHub; Q15173; -. DR ArrayExpress; Q15173; -. DR GermOnline; ENSG00000068971; Homo sapiens. DR RZPD-ProtExp; A0565; -. DR RZPD-ProtExp; IOH27509; -. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Alternative splicing; Direct protein sequencing; Phosphorylation. FT CHAIN 1 497 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit beta isoform. FT /FTId=PRO_0000071450. FT VAR_SEQ 1 19 METKLPPASTPTSPSSPGL -> MITVNPPLPQDTVNLF FT (in isoform Beta-2). FT /FTId=VSP_005109. FT CONFLICT 57 58 QE -> IF (in Ref. 2; AA sequence). FT CONFLICT 177 178 ES -> GA (in Ref. 2; AA sequence). FT CONFLICT 181 181 F -> M (in Ref. 2; AA sequence). FT CONFLICT 184 184 S -> M (in Ref. 2; AA sequence). FT CONFLICT 461 461 W -> E (in Ref. 2; AA sequence). SQ SEQUENCE 497 AA; 57393 MW; 8BEF84F20A77982D CRC64; METKLPPAST PTSPSSPGLS PVPPPDKVDG FSRRSLRRAR PRRSHSSSQF RYQSNQQELT PLPLLKDVPA SELHELLSRK LAQCGVMFDF LDCVADLKGK EVKRAALNEL VECVGSTRGV LIEPVYPDII RMISVNIFRT LPPSENPEFD PEEDEPNLEP SWPHLQLVYE FFLRFLESPD FQPSVAKRYV DQKFVLMLLE LFDSEDPRER EYLKTILHRV YGKFLGLRAY IRKQCNHIFL RFIYEFEHFN GVAELLEILG SIINGFALPL KTEHKQFLVR VLIPLHSVKS LSVFHAQLAY CVVQFLEKDA TLTEHVIRGL LKYWPKTCTQ KEVMFLGEME EILDVIEPSQ FVKIQEPLFK QVARCVSSPH FQVAERALYF WNNEYILSLI EDNCHTVLPA VFGTLYQVSK EHWNQTIVSL IYNVLKTFME MNGKLFDELT ASYKLEKQQE QQKAQERQEL WQGLEELRLR RLQGTQGAKE APLQRLTPQV AASGGQS // ID 2A5B_RABIT Reviewed; 500 AA. AC Q28647; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 33. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta DE isoform (PP2A, B subunit, B' beta isoform) (PP2A, B subunit, B56 beta DE isoform) (PP2A, B subunit, PR61 beta isoform) (PP2A, B subunit, R5 DE beta isoform) (PP2A, B subunit, B'-alpha). GN Name=PPP2R5B; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=New Zealand; RX MEDLINE=96161994; PubMed=8576224; DOI=10.1074/jbc.271.5.2578; RA Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.; RT "High complexity in the expression of the B' subunit of protein RT phosphatase 2A0. Evidence for the existence of at least seven novel RT isoforms."; RL J. Biol. Chem. 271:2578-2588(1996). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in brain. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 CC family. CC -!- CAUTION: Nomenclature used in Ref.1 refers to PP2A B subunit B' CC alpha isoform, which is cited as PP2A B subunit beta-PR61 isoform CC in later publications. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U37769; AAC48527.1; -; mRNA. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Nuclear protein. FT CHAIN 1 500 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit beta isoform. FT /FTId=PRO_0000071451. SQ SEQUENCE 500 AA; 57709 MW; 001CA9360E4C04B0 CRC64; METKLPPAST PTSPSSPGLS PVPPADKVDG FSRRSLRRAR PRRSHSSSQF RYQSNQQELT PLPLLKDVPA SELHDLLSRK LAQCGVMFDF LDCVADLKGK EVKRAALNEL VECVGSTRGV LIEPVYPDII RMISVNIFRT LPPSENPEFD PEEDEPNLEP SWPHLQLVYE FFLRFLESPD FQPSVAKRYV DQKFVLMLLE LFDSEDPRER EYLKTILHRV YGKFLGLRAY IRKQCNHIFL RFIYEFEHFN GVAELLEILG SIINGFALPL KTEHKQFLVR VLIPLHSVKS LSVFHAQLAY CVVQFLEKDA TLTEHVIRGL LKYWPKTCTQ KEVMFLGEVE EILDVIEPSQ FVKIQEPLFK QVARCVSSPH FQVAERALYF WNNEYILSLI EDNCHTVLPA VFGTLYQVSK EHWNQTIVSL IYNVLKTFME MNGKLFDELT ASYKLEKQQE QQKARERQEL WQGLEELRLR RLQGTQGTQG AREAPLQRFV PQVAATGGQS // ID 2A5D_ARATH Reviewed; 477 AA. AC Q9ZQY6; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 20-FEB-2007, entry version 36. DE Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B' DE delta isoform (PP2A, B' subunit, delta isoform) (AtB' delta). GN Name=B'DELTA; OrderedLocusNames=At3g26030; ORFNames=MPE11.23; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH RP AALPHA. RC STRAIN=cv. Columbia; RX MEDLINE=99191692; PubMed=10091592; RX DOI=10.1046/j.1432-1327.1999.00154.x; RA Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S., RA Rundle S.J.; RT "Molecular characterization of the B' regulatory subunit gene family RT of Arabidopsis protein phosphatase 2A."; RL Eur. J. Biochem. 260:127-136(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20277480; PubMed=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NOMENCLATURE. RX MEDLINE=22063724; PubMed=12068121; DOI=10.1104/pp.020004; RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.; RT "Molecular characterization and evolution of the protein phosphatase RT 2A B' regulatory subunit family in plants."; RL Plant Physiol. 129:808-822(2002). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families). CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; AF062396; AAD02810.1; -; mRNA. DR EMBL; AB023041; BAB01066.1; -; Genomic_DNA. DR EMBL; AY091037; AAM13858.1; -; mRNA. DR EMBL; AY117349; AAM51424.1; -; mRNA. DR UniGene; At.6325; -. DR UniGene; At.68656; -. DR GenomeReviews; BA000014_GR; AT3G26030. DR KEGG; ath:At3g26030; -. DR TAIR; At3g26030; -. DR GermOnline; AT3G26030; Arabidopsis thaliana. DR GO; GO:0005737; C:cytoplasm; IDA:TAIR. DR GO; GO:0005730; C:nucleolus; IDA:TAIR. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR002554; B56. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF01603; B56; 1. FT CHAIN 1 477 Serine/threonine protein phosphatase 2A FT 55 kDa regulatory subunit B' delta FT isoform. FT /FTId=PRO_0000071463. SQ SEQUENCE 477 AA; 55240 MW; 232DD0C6DD844414 CRC64; MFKQILGKLP KKTSAKFWDN GESQTLDNNN NQGGGDEVLS QRTSSNGDTS LDCVSSFDVL PRLRDVSISE KQELFLKKLR LCCLVFDFVA EPQQNFKEKE IKRQTLLEVV DYVISSGNGK FPESVIQEAT KMISANLFSN PHRQWKNKTP EALDLEEEEG SLNPSWPHLQ IVYEFLLRIV ASPNTDPKIS KKYIDHTFVL KLLDLFDSED PREREYLKTI LHRIYGRFMV HRPFIRKTMN NILYDFIFET GKHSGIAEFL EVLGSIINGF ALPLKEEHKL FLTRVLIPLH KLKCLPNYHQ QLSYCVIQFV EKDCKLADTV IRGMLKYWPV TNSAKEIMFL NELEEILEAT QLTEFERCMV PLSRQIAQCL SSSHFQVAER ALYLWNNDHV TNLVRQNSRI ILPIVFPALE KNGSSHWNQA VKNLTENVLK VLSDTNPDLF EECLHKFQED QQKAEDTKKK NGETWRQLEE IVASMAK // ID 2A5D_HUMAN Reviewed; 602 AA. AC Q14738; O00494; O00696; Q15171; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 78. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE delta isoform (PP2A, B subunit, B' delta isoform) (PP2A, B subunit, DE B56 delta isoform) (PP2A, B subunit, PR61 delta isoform) (PP2A, B DE subunit, R5 delta isoform). GN Name=PPP2R5D; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA-1). RC TISSUE=Fetal brain; RX MEDLINE=96355607; PubMed=8703017; DOI=10.1074/jbc.271.36.22081; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DELTA-1 AND DELTA-3). RC TISSUE=Brain cortex; RX MEDLINE=97324098; PubMed=9180267; DOI=10.1016/S0014-5793(97)00392-X; RA Tanabe O., Gomez G.A., Nishito Y., Usui H., Takeda M.; RT "Molecular heterogeneity of the cDNA encoding a 74-kDa regulatory RT subunit (B'' or delta) of human protein phosphatase 2A."; RL FEBS Lett. 408:52-56(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA-2), AND PROTEIN SEQUENCE OF RP 501-508; 550-559; 573-580 AND 584-601 (DELTA-1). RC TISSUE=Bone marrow, and Brain cortex; RX MEDLINE=96159032; PubMed=8566219; DOI=10.1016/0014-5793(95)01500-0; RA Tanabe O., Nagase T., Murakami T., Nozaki H., Usui H., Nishito Y., RA Hayashi H., Kagamiyama H., Takeda M.; RT "Molecular cloning of a 74-kDa regulatory subunit (B'' or delta) of RT human protein phosphatase 2A."; RL FEBS Lett. 379:107-111(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS DELTA-1 AND DELTA-2). RC TISSUE=Colon, Eye, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, AND MASS RP SPECTROMETRY. RX PubMed=16565220; DOI=10.1073/pnas.0507066103; RA Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; RT "Phosphoproteome analysis of the human mitotic spindle."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- INTERACTION: CC P30307:CDC25C; NbExp=1; IntAct=EBI-396563, EBI-974439; CC Q13136:PPFIA1; NbExp=1; IntAct=EBI-396563, EBI-745426; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear in CC interphase, nuclear during mitosis. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Delta-1; CC IsoId=Q14738-1; Sequence=Displayed; CC Name=Delta-2; CC IsoId=Q14738-2; Sequence=VSP_005111; CC Name=Delta-3; CC IsoId=Q14738-3; Sequence=VSP_005110; CC -!- TISSUE SPECIFICITY: Isoform Delta-2 is widely expressed. Isoform CC Delta-1 is highly expressed in brain. CC -!- INDUCTION: By retinoic acid; in neuroblastoma cell lines. CC -!- PTM: At least isoform Delta-1 is phosphorylated on serine CC residues. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; L76702; AAB69751.1; -; mRNA. DR EMBL; AB000634; BAA20381.1; -; mRNA. DR EMBL; AB000635; BAA20382.1; -; mRNA. DR EMBL; D78360; BAA11372.1; -; mRNA. DR EMBL; BC001095; AAH01095.1; -; mRNA. DR EMBL; BC001175; AAH01175.1; -; mRNA. DR EMBL; BC010692; AAH10692.1; -; mRNA. DR PIR; S68686; S68686. DR UniGene; Hs.533308; -. DR IntAct; Q14738; -. DR Ensembl; ENSG00000112640; Homo sapiens. DR KEGG; hsa:5528; -. DR H-InvDB; HIX0005889; -. DR HGNC; HGNC:9312; PPP2R5D. DR MIM; 601646; gene. DR Reactome; REACT_1505.1; Integration of pathways involved in energy metabolism. DR Reactome; REACT_1919.2; Dephosphorylation of pChREBP by PP2A. DR LinkHub; Q14738; -. DR ArrayExpress; Q14738; -. DR GermOnline; ENSG00000112640; Homo sapiens. DR RZPD-ProtExp; C0421; -. DR RZPD-ProtExp; IOH43173; -. DR RZPD-ProtExp; IOH4724; -. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Alternative splicing; Direct protein sequencing; Nuclear protein; KW Phosphorylation; Repeat. FT CHAIN 1 602 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit delta isoform. FT /FTId=PRO_0000071452. FT REPEAT 37 38 1. FT REPEAT 39 40 2. FT REPEAT 41 42 3. FT REPEAT 43 44 4. FT REPEAT 45 46 5. FT REPEAT 47 48 6; approximate. FT REPEAT 49 50 7; approximate. FT REPEAT 51 52 8. FT REGION 37 52 8 X 2 AA approximate tandem repeats of Q- FT P. FT MOTIF 523 530 SH3-binding; class I (Potential). FT MOTIF 548 565 Nuclear localization signal (Potential). FT MOD_RES 598 598 Phosphoserine. FT VAR_SEQ 11 116 Missing (in isoform Delta-3). FT /FTId=VSP_005110. FT VAR_SEQ 85 116 Missing (in isoform Delta-2). FT /FTId=VSP_005111. SQ SEQUENCE 602 AA; 69992 MW; F15F71AF4E565387 CRC64; MPYKLKKEKE PPKVAKCTAK PSSSGKDGGG ENTEEAQPQP QPQPQPQAQS QPPSSNKRPS NSTPPPTQLS KIKYSGGPQI VKKERRQSSS RFNLSKNREL QKLPALKDSP TQEREELFIQ KLRQCCVLFD FVSDPLSDLK FKEVKRAGLN EMVEYITHSR DVVTEAIYPE AVTMFSVNLF RTLPPSSNPT GAEFDPEEDE PTLEAAWPHL QLVYEFFLRF LESPDFQPNI AKKYIDQKFV LALLDLFDSE DPRERDFLKT ILHRIYGKFL GLRAYIRRQI NHIFYRFIYE TEHHNGIAEL LEILGSIING FALPLKEEHK MFLIRVLLPL HKVKSLSVYH PQLAYCVVQF LEKESSLTEP VIVGLLKFWP KTHSPKEVMF LNELEEILDV IEPSEFSKVM EPLFRQLAKC VSSPHFQVAE RALYYWNNEY IMSLISDNAA RVLPIMFPAL YRNSKSHWNK TIHGLIYNAL KLFMEMNQKL FDDCTQQYKA EKQKGRFRMK EREEMWQKIE ELARLNPQYP MFRAPPPLPP VYSMETETPT AEDIQLLKRT VETEAVQMLK DIKKEKVLLR RKSELPQDVY TIKALEAHKR AEEFLTASQE AL // ID 2A5D_RABIT Reviewed; 586 AA. AC Q28653; Q28655; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 45. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE delta isoform (PP2A, B subunit, B' delta isoform) (PP2A, B subunit, DE B56 delta isoform) (PP2A, B subunit, PR61 delta isoform) (PP2A, B DE subunit, R5 delta isoform) (PP2A, B subunit, B'-gamma). GN Name=PPP2R5D; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=New Zealand; TISSUE=Brain, and Skeletal muscle; RX MEDLINE=96161994; PubMed=8576224; DOI=10.1074/jbc.271.5.2578; RA Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.; RT "High complexity in the expression of the B' subunit of protein RT phosphatase 2A0. Evidence for the existence of at least seven novel RT isoforms."; RL J. Biol. Chem. 271:2578-2588(1996). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in brain. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 CC family. CC -!- CAUTION: Nomenclature used in Ref.1 refers to PP2A B subunit B' CC gamma isoform, which is cited as PP2A B subunit delta-PR61 isoform CC in later publications. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U38193; AAC48532.1; -; mRNA. DR EMBL; U38195; AAC48534.1; -; mRNA. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Nuclear protein; Phosphorylation; Repeat. FT CHAIN 1 586 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit delta isoform. FT /FTId=PRO_0000071453. FT REPEAT 21 22 1. FT REPEAT 23 24 2. FT REPEAT 25 26 3. FT REPEAT 27 28 4. FT REPEAT 29 30 5. FT REPEAT 31 32 6. FT REPEAT 33 34 7; approximate. FT REPEAT 35 36 8. FT REGION 21 36 8 X 2 AA approximate tandem repeats of Q- FT P. FT MOTIF 507 514 SH3-binding; class I (Potential). FT MOTIF 532 549 Nuclear localization signal (Potential). FT MOD_RES 582 582 Phosphoserine (By similarity). SQ SEQUENCE 586 AA; 68090 MW; E149A309CDDA7495 CRC64; MSPSPSSSGK DGGGENAEEA QPQPQPQPQP QPQSQPPSSN KRPSNSTPPP TQLSKIKYSG GPQIVKKERR QSSSRFNLSK NRELQKLPAL KDSPTQEREE LFIQKLRQCC VLFDFVSDPL SDLKFKEVKR AGLNEMVEYI THSRDVVTEA IYPEAVTMFS VNLFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLALLDL FDSEDPRERD FLKTILHRIY GKFLGLRAYI RRQINHIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKMFLIRV LLPLHKVKSL SVYHPQLAYC VVQFLEKESS LTEPVIVGLL KFWPKTHSPK EVMFLNELEE ILDVIEPSEF SKVMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS DNAARVLPIM FPALYRNSKS HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QYKAEKQKGR FRMKEREEMW QKIEELARLN PQYPMFRAPP PLPPVYSMET ETPTAEDIQL LKRTVETEAV QMLKDIKKEK VLLRRKSELP QDVYTIKALE AHKRAEEFLT ASQEAL // ID 2A5D_YEAST Reviewed; 757 AA. AC P38903; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 20-FEB-2007, entry version 51. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE delta isoform (PP2A, B subunit, B' delta isoform) (Protein RTS1) DE (Protein SCS1). GN Name=RTS1; Synonyms=SCS1; OrderedLocusNames=YOR014W; ORFNames=OR26.04; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96271526; PubMed=8846889; RA Evangelista C.C. Jr., Rodriguez Torres A.M., Limbach M.P., RA Zitomer R.S.; RT "Rox3 and Rts1 function in the global stress response pathway in RT baker's yeast."; RL Genetics 142:1083-1093(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION. RX MEDLINE=96009589; PubMed=7565713; RA Shu Y., Hallberg R.L.; RT "SCS1, a multicopy suppressor of hsp60-ts mutant alleles, does not RT encode a mitochondrially targeted protein."; RL Mol. Cell. Biol. 15:5618-5626(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97313270; PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., RA Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., RA Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., RA Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., RA Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., RA Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., RA Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., RA Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., RA Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., RA Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., RA Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., RA Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., RA Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., RA Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., RA Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). RN [4] RP FUNCTION, SUBUNIT, AND PHOSPHORYLATION. RX MEDLINE=97299674; PubMed=9154823; RA Shu Y., Yang H., Hallberg E., Hallberg R.; RT "Molecular genetic analysis of Rts1p, a B' regulatory subunit of RT Saccharomyces cerevisiae protein phosphatase 2A."; RL Mol. Cell. Biol. 17:3242-3253(1997). RN [5] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-272, AND MASS RP SPECTROMETRY. RX PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., RA Mann M., Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone RT signaling pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- FUNCTION: Multicopy suppressor of ROX3 and HSP60. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- INTERACTION: CC P47135:JSN1; NbExp=1; IntAct=EBI-1931, EBI-9422; CC P53958:YNL042W; NbExp=1; IntAct=EBI-1931, EBI-28694; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- PTM: Phosphorylated. CC -!- MISCELLANEOUS: Present with 300 molecules/cell. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B 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; U06630; AAB38372.1; -; Genomic_DNA. DR EMBL; S79635; AAB35312.1; -; Genomic_DNA. DR EMBL; X87331; CAA60763.1; -; Genomic_DNA. DR EMBL; Z74922; CAA99203.1; -; Genomic_DNA. DR PIR; S54620; S54620. DR DIP; DIP:4191N; -. DR IntAct; P38903; -. DR Ensembl; YOR014W; Saccharomyces cerevisiae. DR GenomeReviews; Y13140_GR; YOR014W. DR KEGG; sce:YOR014W; -. DR CYGD; YOR014w; -. DR SGD; S000005540; RTS1. DR BioCyc; SCER-S28-01:SCER-S28-01-005466-MONOMER; -. DR LinkHub; P38903; -. DR GermOnline; YOR014W; Saccharomyces cerevisiae. DR GO; GO:0005935; C:bud neck; IDA:SGD. DR GO; GO:0000780; C:condensed nuclear chromosome, pericentric r...; IDA:SGD. DR GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:SGD. DR GO; GO:0005816; C:spindle pole body; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IMP:SGD. DR GO; GO:0006470; P:protein amino acid dephosphorylation; TAS:SGD. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Complete proteome; Nuclear protein; Phosphorylation. FT CHAIN 1 757 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit delta isoform. FT /FTId=PRO_0000071471. FT COMPBIAS 16 22 Poly-Ser. FT COMPBIAS 46 51 Poly-Ser. FT COMPBIAS 98 110 Poly-Ser. FT COMPBIAS 143 147 Poly-Ser. FT COMPBIAS 202 213 Poly-Asn. FT MOD_RES 272 272 Phosphothreonine. FT CONFLICT 95 95 T -> S (in Ref. 2). FT CONFLICT 529 529 L -> F (in Ref. 1). FT CONFLICT 581 581 A -> R (in Ref. 1). SQ SEQUENCE 757 AA; 85335 MW; 5A7476C30140331C CRC64; MMRGFKQRLI KKTTGSSSSS SSKKKDKEKE KEKSSTTSST SKKPASASSS SHGTTHSSAS STGSKSTTEK GKQSGSVPSQ GKHHSSSTSK TKTATTPSSS SSSSRSSSVS RSGSSSTKKT SSRKGQEQSK QSQQPSQSQK QGSSSSSAAI MNPTPVLTVT KDDKSTSGED HAHPTLLGAV SAVPSSPISN ASGTAVSSDV ENGNSNNNNM NINTSNTQDA NHASSQSIDI PRSSHSFERL PTPTKLNPDT DLELIKTPQR HSSSRFEPSR YTPLTKLPNF NEVSPEERIP LFIAKVDQCN TMFDFNDPSF DIQGKEIKRS TLDELIEFLV TNRFTYTNEM YAHVVNMFKI NLFRPIPPPV NPVGDIYDPD EDEPVNELAW PHMQAVYEFF LRFVESPDFN HQIAKQYIDQ DFILKLLELF DSEDIRERDC LKTTLHRIYG KFLSLRSFIR RSMNNIFLQF IYETEKFNGV AELLEILGSI INGFALPLKE EHKVFLVRIL IPLHKVRCLS LYHPQLAYCI VQFLEKDPLL TEEVVMGLLR YWPKINSTKE IMFLNEIEDI FEVIEPLEFI KVEVPLFVQL AKCISSPHFQ VAEKVLSYWN NEYFLNLCIE NAEVILPIIF PALYELTSQL ELDTANGEDS ISDPYMLVEQ AINSGSWNRA IHAMAFKALK IFLETNPVLY ENCNALYLSS VKETQQRKVQ REENWSKLEE YVKNLRINND KDQYTIKNPE LRNSFNTASE NNTLNEENEN DCDSEIQ // ID 2A5E_ARATH Reviewed; 497 AA. AC Q9SV41; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 23-JAN-2007, entry version 28. DE Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' DE epsilon isoform (PP2A, B' subunit, epsilon isoform) (AtB' epsilon). GN Name=B'EPSILON; OrderedLocusNames=At3g54930; ORFNames=F28P10.90; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND RP NOMENCLATURE. RX MEDLINE=22063724; PubMed=12068121; DOI=10.1104/pp.020004; RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.; RT "Molecular characterization and evolution of the protein phosphatase RT 2A B' regulatory subunit family in plants."; RL Plant Physiol. 129:808-822(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families) (By similarity). CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; AJ276037; CAC16085.1; -; Genomic_DNA. DR EMBL; AL049655; CAB41091.1; -; Genomic_DNA. DR EMBL; BT010562; AAQ65185.1; -; mRNA. DR EMBL; AK175667; BAD43430.1; -; mRNA. DR PIR; T06727; T06727. DR UniGene; At.35066; -. DR GenomeReviews; BA000014_GR; AT3G54930. DR KEGG; ath:At3g54930; -. DR TAIR; At3g54930; -. DR ArrayExpress; Q9SV41; -. DR GermOnline; AT3G54930; Arabidopsis thaliana. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR002554; B56. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF01603; B56; 1. FT CHAIN 1 497 Serine/threonine protein phosphatase 2A FT 57 kDa regulatory subunit B' epsilon FT isoform. FT /FTId=PRO_0000071464. FT COMPBIAS 23 29 Poly-Asn. SQ SEQUENCE 497 AA; 57545 MW; 87ACF0065F81C338 CRC64; MFNKIIKLGQ KKFNKSDQHH QDNNNNNNNT STNTVVRGSR TTTPAPSSVS NGESQTTAQS PSQTPNHPMF TTTPILEVLP LLKDVSSSDR PLLFMKKAHM CSCHCDFSDT LIMPREKEIK RQTLLELVDF LHSSSGKVNE TMQSELIRMV SANIFRCLPP AYHENTGAPP EGNDPEEEEP YLEPWWPHLQ LVYELLLRYV VSSEIEPKTA KKFINHTFVS RLLDLFDSED PREREYLKTV LHRIYGKFIF HRPFIRCSIY NIFYKFLYET ERCIGIGELL EILGSVINGF TVPMREEHRL YLVKAILPLH KSKGISIYHQ QLAYCVTQFV EKDYKLADTV IRGLLKFWPL TNCQKEVLFL GELEEVLDAT EPSEFQQCVV PLFTQIGKCL NSAHFQVAER ALFLWNNEHI VGLIAQNKDV IFPIIFEALE RNMKGHWNQA VHGLSENVRR MFLEMDTELF EECEKQYLEN EAKACELLEQ RELTWKRLEE AASLAAN // ID 2A5E_HUMAN Reviewed; 467 AA. AC Q16537; Q52LW4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 06-FEB-2007, entry version 51. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE epsilon isoform (PP2A, B subunit, B' epsilon isoform) (PP2A, B DE subunit, B56 epsilon isoform) (PP2A, B subunit, PR61 epsilon isoform) DE (PP2A, B subunit, R5 epsilon isoform). GN Name=PPP2R5E; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 449-455. RC TISSUE=Fetal retina; RX MEDLINE=96276417; PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetal brain; RX MEDLINE=96355607; PubMed=8703017; DOI=10.1074/jbc.271.36.22081; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). 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: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: Phosphorylated on serine residues. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; Z69029; CAA93153.1; -; mRNA. DR EMBL; L76703; AAB69752.1; -; mRNA. DR EMBL; BC093766; AAH93766.1; -; mRNA. DR UniGene; Hs.334868; -. DR IntAct; Q16537; -. DR Ensembl; ENSG00000154001; Homo sapiens. DR KEGG; hsa:5529; -. DR HGNC; HGNC:9313; PPP2R5E. DR MIM; 601647; gene. DR ArrayExpress; Q16537; -. DR GermOnline; ENSG00000154001; Homo sapiens. DR RZPD-ProtExp; IOH29856; -. DR RZPD-ProtExp; M0207; -. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Direct protein sequencing; Phosphorylation. FT CHAIN 1 467 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit epsilon FT isoform. FT /FTId=PRO_0000071454. SQ SEQUENCE 467 AA; 54699 MW; DD9CE11433F499CF CRC64; MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPSSEQP ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQEFQPS IAKKYIDQKF VLQLLELFDS EDPRERDYLK TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE LLEILGSIIN GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK CVSSPHFQVA ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN PAIVALVYNV LKAFMEMNST MFDELTATYK SDRQREKKKE KEREELWKKL EDLELKRGLR RDGIIPT // ID 2A5E_MOUSE Reviewed; 467 AA. AC Q61151; Q3V1I5; Q571M6; Q8C2M2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 3. DT 23-JAN-2007, entry version 41. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE epsilon isoform (PP2A, B subunit, B' epsilon isoform) (PP2A, B DE subunit, B56 epsilon isoform) (PP2A, B subunit, PR61 epsilon isoform) DE (PP2A, B subunit, R5 epsilon isoform). GN Name=Ppp2r5e; Synonyms=Kiaa4006; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin, 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; 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 1-436. RC TISSUE=Embryonic tail; RX MEDLINE=22579291; 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 [MRNA] OF 51-437. RC TISSUE=Embryonic fibroblast; RX MEDLINE=97042488; PubMed=8887688; RA Okamoto K., Kamibayashi C., Serrano M., Prives C., Mumby M.C., RA Beach D.; RT "p53-dependent association between cyclin G and the B' subunit of RT protein phosphatase 2A."; RL Mol. Cell. Biol. 16:6593-6602(1996). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. Interacts with cyclin G in vitro. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 CC family. CC -!- CAUTION: Ref.4 (AAB37234) sequence differs from that shown due to CC frameshifts in positions 162, 180 and 185. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK088366; BAC40306.1; -; mRNA. DR EMBL; AK132432; BAE21166.1; -; mRNA. DR EMBL; BC085149; AAH85149.1; -; mRNA. DR EMBL; AK220163; BAD90335.1; ALT_INIT; mRNA. DR EMBL; U49728; AAB37234.1; ALT_FRAME; mRNA. DR UniGene; Mm.259626; -. DR Ensembl; ENSMUSG00000021051; Mus musculus. DR KEGG; mmu:26932; -. DR MGI; MGI:1349473; Ppp2r5e. DR ArrayExpress; Q61151; -. DR GermOnline; ENSMUSG00000021051; Mus musculus. DR GO; GO:0005737; C:cytoplasm; TAS:MGI. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. FT CHAIN 1 467 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit epsilon FT isoform. FT /FTId=PRO_0000071455. FT CONFLICT 74 74 F -> C (in Ref. 4). FT CONFLICT 162 162 L -> W (in Ref. 4). FT CONFLICT 388 388 F -> S (in Ref. 4). FT CONFLICT 409 409 N -> T (in Ref. 4). SQ SEQUENCE 467 AA; 54713 MW; 77DA129F9A4EC6AC CRC64; MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPTSEQP ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQEFQPS IAKKYIDQKF VLQLLELFDS EDPRERDYLK TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE LLEILGSIIN GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK CVSSPHFQVA ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN PAIVALVYNV LKAFMEMNST MFDELTATYK SDRQREKKKE KEREELWKKL EDLELKRGLR RDGIIPT // ID 2A5E_RABIT Reviewed; 165 AA. AC Q28654; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 33. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE epsilon isoform (PP2A, B subunit, B' epsilon isoform) (PP2A, B DE subunit, B56 epsilon isoform) (PP2A, B subunit, PR61 epsilon isoform) DE (PP2A, B subunit, R5 epsilon isoform) (PP2A, B subunit, B'-delta) DE (Fragment). GN Name=PPP2R5E; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=New Zealand; TISSUE=Brain; RX MEDLINE=96161994; PubMed=8576224; DOI=10.1074/jbc.271.5.2578; RA Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.; RT "High complexity in the expression of the B' subunit of protein RT phosphatase 2A0. Evidence for the existence of at least seven novel RT isoforms."; RL J. Biol. Chem. 271:2578-2588(1996). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in testis, lung and brain. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 CC family. CC -!- CAUTION: Nomenclature used in Ref.1 refers to PP2A B subunit B' CC delta isoform, which is cited as PP2A B subunit epsilon-PR61 CC isoform in later publications. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U38194; AAC48533.1; -; mRNA. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. FT CHAIN 1 >165 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit epsilon FT isoform. FT /FTId=PRO_0000071456. FT NON_TER 165 165 SQ SEQUENCE 165 AA; 19048 MW; 6F4A6E32D0D85B7D CRC64; MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPSSEQP ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQ // ID 2A5G_ARATH Reviewed; 522 AA. AC Q8RW96; O04377; O23394; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 2. DT 20-FEB-2007, entry version 24. DE Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' DE gamma isoform (PP2A, B' subunit, gamma isoform) (AtB' gamma). GN Name=B'GAMMA; OrderedLocusNames=At4g15415; GN ORFNames=dl3750w, FCAALL.118; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION. RX MEDLINE=97274652; PubMed=9128737; RA Latorre K.A., Harris D.M., Rundle S.J.; RT "Differential expression of three Arabidopsis genes encoding the B' RT regulatory subunit of protein phosphatase 2A."; RL Eur. J. Biochem. 245:156-163(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=98121113; PubMed=9461215; DOI=10.1038/35140; RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., RA Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., RA Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., RA Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., RA Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., RA Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., RA Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., RA Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., RA Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., RA Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., RA Klosterman S., Schueller C., Chalwatzis N.; RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of RT Arabidopsis thaliana."; RL Nature 391:485-488(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP INTERACTION WITH AALPHA. RX MEDLINE=99191692; PubMed=10091592; RX DOI=10.1046/j.1432-1327.1999.00154.x; RA Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S., RA Rundle S.J.; RT "Molecular characterization of the B' regulatory subunit gene family RT of Arabidopsis protein phosphatase 2A."; RL Eur. J. Biochem. 260:127-136(1999). RN [7] RP NOMENCLATURE. RX MEDLINE=22063724; PubMed=12068121; DOI=10.1104/pp.020004; RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.; RT "Molecular characterization and evolution of the protein phosphatase RT 2A B' regulatory subunit family in plants."; RL Plant Physiol. 129:808-822(2002). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families). CC -!- TISSUE SPECIFICITY: Expressed ubiquitously at low levels. CC -!- INDUCTION: By heat-shock. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 CC family. CC -!- CAUTION: Ref.2 and Ref.3 sequences differ from that shown due to CC erroneous gene model prediction. The predicted gene At4g15410 has CC been split into 2 genes: At4g15410 and At4g15415. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U73528; AAB58902.1; -; mRNA. DR EMBL; Z97338; CAB10320.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161541; CAB78583.1; ALT_SEQ; Genomic_DNA. DR EMBL; AY093761; AAM10385.1; -; mRNA. DR EMBL; BT020581; AAW80854.1; -; mRNA. DR PIR; F71418; F71418. DR UniGene; At.4343; -. DR HSSP; O35987; 1JRU. DR GenomeReviews; CT486007_GR; AT4G15415. DR KEGG; ath:At4g15415; -. DR TAIR; At4g15415; -. DR GermOnline; AT4G15415; Arabidopsis thaliana. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR002554; B56. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF01603; B56; 1. FT CHAIN 1 522 Serine/threonine protein phosphatase 2A FT 59 kDa regulatory subunit B' gamma FT isoform. FT /FTId=PRO_0000071462. FT COMPBIAS 14 69 Ser-rich. FT CONFLICT 384 384 F -> L (in Ref. 4). SQ SEQUENCE 522 AA; 59157 MW; AACF6C94287760EA CRC64; MIKQIFGKLP RKPSKSSHND SNPNGEGGVN SYYIPNSGIS SISKPSSKSS ASNSNGANGT VIAPSSTSSN RTNQVNGVYE ALPSFRDVPT SEKPNLFIKK LSMCCVVFDF NDPSKNLREK EIKRQTLLEL VDYIATVSTK LSDAAMQEIA KVAVVNLFRT FPSANHESKI LETLDVDDEE PALEPAWPHL QVVYELLLRF VASPMTDAKL AKRYIDHSFV LKLLDLFDSE DQREREYLKT ILHRIYGKFM VHRPFIRKAI NNIFYRFIFE TEKHNGIAEL LEILGSIING FALPLKEEHK LFLIRALIPL HRPKCASAYH QQLSYCIVQF VEKDFKLADT VIRGLLKYWP VTNSSKEVMF LGELEEVLEA TQAAEFQRCM VPLFRQIARC LNSSHFQVAE RALFLWNNDH IRNLITQNHK VIMPIVFPAM ERNTRGHWNQ AVQSLTLNVR KVMAETDQIL FDECLAKFQE DEANETEVVA KREATWKLLE ELAASKSVSN EAVLVPRFSS SVTLATGKTS GS // ID 2A5G_HUMAN Reviewed; 524 AA. AC Q13362; Q14391; Q15060; Q15174; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 20-FEB-2007, entry version 61. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE gamma isoform (PP2A, B subunit, B' gamma isoform) (PP2A, B subunit, DE B56 gamma isoform) (PP2A, B subunit, PR61 gamma isoform) (PP2A, B DE subunit, R5 gamma isoform) (Renal carcinoma antigen NY-REN-29). GN Name=PPP2R5C; Synonyms=KIAA0044; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-3). RC TISSUE=Umbilical vein; RX MEDLINE=96214950; PubMed=8617797; DOI=10.1074/jbc.271.9.5164; RA Tehrani M.A., Mumby M.C., Kamibayashi C.; RT "Identification of a novel protein phosphatase 2A regulatory subunit RT highly expressed in muscle."; RL J. Biol. Chem. 271:5164-5170(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-1). RC TISSUE=Fetal retina; RX MEDLINE=96276417; PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-524 (ISOFORM GAMMA-2). RC TISSUE=Bone marrow; RX MEDLINE=96051398; PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-524 (ISOFORM GAMMA-1). RX MEDLINE=96064678; PubMed=7592815; DOI=10.1074/jbc.270.44.26123; RA McCright B., Virshup D.M.; RT "Identification of a new family of protein phosphatase 2A regulatory RT subunits."; RL J. Biol. Chem. 270:26123-26128(1995). RN [5] RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX MEDLINE=96355607; PubMed=8703017; DOI=10.1074/jbc.271.36.22081; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). RN [6] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX MEDLINE=99438124; PubMed=10508479; RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal- RT cell carcinoma."; RL Int. J. Cancer 83:456-464(1999). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus. Isoform 3: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Gamma-3; CC IsoId=Q13362-1; Sequence=Displayed; CC Name=Gamma-1; CC IsoId=Q13362-2; Sequence=VSP_005112; CC Name=Gamma-2; CC IsoId=Q13362-3; Sequence=VSP_005113; CC -!- TISSUE SPECIFICITY: Highest levels in heart, skeletal muscle and CC brain. Lower levels in pancreas, kidney, lung and placenta. Very CC low levels in liver. CC -!- PTM: At least isoform Gamma-3 is phosphorylated on serine residues CC while isoform Gamma-1 is not. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; U37352; AAC50387.1; ALT_INIT; mRNA. DR EMBL; Z69030; CAA93154.1; -; mRNA. DR EMBL; D26445; BAA05465.1; -; mRNA. DR EMBL; L42375; AAC37603.1; -; mRNA. DR UniGene; Hs.368264; -. DR Ensembl; ENSG00000078304; Homo sapiens. DR KEGG; hsa:5527; -. DR HGNC; HGNC:9311; PPP2R5C. DR MIM; 601645; gene. DR LinkHub; Q13362; -. DR ArrayExpress; Q13362; -. DR GermOnline; ENSG00000078304; Homo sapiens. DR RZPD-ProtExp; IOH13592; -. DR RZPD-ProtExp; IOH42153; -. DR RZPD-ProtExp; T0580; -. DR RZPD-ProtExp; T2624; -. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000159; C:protein phosphatase type 2A complex; NAS:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; NAS:UniProtKB. DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB. KW Alternative splicing; Nuclear protein; Phosphorylation. FT CHAIN 1 524 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit gamma isoform. FT /FTId=PRO_0000071457. FT MOTIF 416 422 Nuclear localization signal (Potential). FT VAR_SEQ 443 524 YTVYSQASTMSIPVAMETDGPLFEDVQMLRKTVKDEAHQAQ FT KDPKKDRPLARRKSELPQDPHTKKALEAHCRADELASQDGR FT -> VLKKRIT (in isoform Gamma-1). FT /FTId=VSP_005112. FT VAR_SEQ 443 481 Missing (in isoform Gamma-2). FT /FTId=VSP_005113. FT CONFLICT 494 494 R -> L (in Ref. 1). SQ SEQUENCE 524 AA; 61061 MW; B9CBF54550D713F8 CRC64; MLTCNKAGSR MVVDAANSNG PFQPVVLLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA VNMFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK LKMKEREEAW VKIENLAKAN PQYTVYSQAS TMSIPVAMET DGPLFEDVQM LRKTVKDEAH QAQKDPKKDR PLARRKSELP QDPHTKKALE AHCRADELAS QDGR // ID 2A5G_MOUSE Reviewed; 524 AA. AC Q60996; O35708; Q99KW8; Q99N67; Q99N68; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 2. DT 20-FEB-2007, entry version 48. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE gamma isoform (PP2A, B subunit, B' gamma isoform) (PP2A, B subunit, DE B56 gamma isoform) (PP2A, B subunit, PR61 gamma isoform) (PP2A, B DE subunit, R5 gamma isoform) (PP2A, B subunit, B'alpha3 isoform). GN Name=Ppp2r5c; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-524 (ISOFORMS 2 AND 3). RX PubMed=12507892; RA Ito A., Koma Y., Watabe K., Nagano T., Endo Y., Nojima H., RA Kitamura Y.; RT "A truncated isoform of the protein phosphatase 2A B56gamma regulatory RT subunit may promote genetic instability and cause tumor progression."; RL Am. J. Pathol. 162:81-91(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-524 (ISOFORM 1). RC TISSUE=T-cell; RX MEDLINE=96214950; PubMed=8617797; DOI=10.1074/jbc.271.9.5164; RA Tehrani M.A., Mumby M.C., Kamibayashi C.; RT "Identification of a novel protein phosphatase 2A regulatory subunit RT highly expressed in muscle."; RL J. Biol. Chem. 271:5164-5170(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-524 (ISOFORM 1). RC STRAIN=C57BL/6; RX MEDLINE=96354596; PubMed=8752144; RA Francia G., Mitchell S.D., Moss S.E., Hanby A.M., Marshall J.F., RA Hart I.R.; RT "Identification by differential display of annexin-VI, a gene RT differentially expressed during melanoma progression."; RL Cancer Res. 56:3855-3858(1996). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. Interacts with cyclin G in vitro. Isoform 3 may CC damage the checkpoint, which may then allow the acquisition of CC genetic alterations that promote metastasis. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=2; Synonyms=Gamma-2; CC IsoId=Q60996-1; Sequence=Displayed; CC Name=1; Synonyms=Gamma-1; CC IsoId=Q60996-2; Sequence=VSP_014719, VSP_014720; CC Note=No experimental confirmation available; CC Name=3; Synonyms=Gamma-3; CC IsoId=Q60996-3; Sequence=VSP_014718; CC -!- TISSUE SPECIFICITY: Highest levels in heart, liver and brain. CC Lower levels in skeletal muscle, spleen, kidney and lung. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; BC003979; AAH03979.1; -; mRNA. DR EMBL; AB055635; BAB32447.1; -; mRNA. DR EMBL; AB055636; BAB32448.1; -; mRNA. DR EMBL; U37353; AAC52435.1; -; mRNA. DR EMBL; U59418; AAB70857.1; -; mRNA. DR UniGene; Mm.240396; -. DR UniGene; Mm.391677; -. DR DIP; DIP:24181N; -. DR Ensembl; ENSMUSG00000017843; Mus musculus. DR KEGG; mmu:26931; -. DR MGI; MGI:1349475; Ppp2r5c. DR LinkHub; Q60996; -. DR ArrayExpress; Q60996; -. DR GermOnline; ENSMUSG00000017843; Mus musculus. DR RZPD-ProtExp; IOM15958; -. DR GO; GO:0005634; C:nucleus; TAS:MGI. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Alternative splicing. FT CHAIN 1 524 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit gamma isoform. FT /FTId=PRO_0000071458. FT VAR_SEQ 442 480 Missing (in isoform 3). FT /FTId=VSP_014718. FT VAR_SEQ 443 452 YAVYSQASAV -> VLKKRVTREC (in isoform 1). FT /FTId=VSP_014719. FT VAR_SEQ 453 524 Missing (in isoform 1). FT /FTId=VSP_014720. FT CONFLICT 17 19 SSN -> APT (in Ref. 2). FT CONFLICT 32 32 D -> N (in Ref. 4). FT CONFLICT 72 72 A -> S (in Ref. 3 and 4). SQ SEQUENCE 524 AA; 60824 MW; A22DFD34A1FFBD01 CRC64; MLTCNKAGSG MVVDAASSNG PFQPVALLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEAVHMFA VNMFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK LKMKEREEAW VKIENLAKAN PQYAVYSQAS AVSIPVAMET DGPQFEDVQM LKKTVSDEAR QAQKELKKDR PLVRRKSELP QDPHTEKALE AHCRASELLS QDGR // ID 2A5G_RABIT Reviewed; 524 AA. AC Q28651; Q28648; Q28650; Q28652; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 39. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE gamma isoform (PP2A, B subunit, B' gamma isoform) (PP2A, B subunit, DE B56 gamma isoform) (PP2A, B subunit, PR61 gamma isoform) (PP2A, B DE subunit, R5 gamma isoform) (PP2A, B subunit, B' beta isoform). GN Name=PPP2R5C; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA-1; GAMMA-3; GAMMA-4 AND RP GAMMA-5). RC STRAIN=New Zealand; TISSUE=Skeletal muscle; RX MEDLINE=96161994; PubMed=8576224; DOI=10.1074/jbc.271.5.2578; RA Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.; RT "High complexity in the expression of the B' subunit of protein RT phosphatase 2A0. Evidence for the existence of at least seven novel RT isoforms."; RL J. Biol. Chem. 271:2578-2588(1996). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=Gamma-3; Synonyms=Beta-3; CC IsoId=Q28651-1; Sequence=Displayed; CC Name=Gamma-1; Synonyms=Beta-4; CC IsoId=Q28651-2; Sequence=VSP_005116; CC Name=Gamma-4; Synonyms=Beta-1; CC IsoId=Q28651-3; Sequence=VSP_005114; CC Name=Gamma-5; Synonyms=Beta-2; CC IsoId=Q28651-4; Sequence=VSP_005115; CC -!- TISSUE SPECIFICITY: Highly expressed in testis, heart and spleen. CC Also found in brain and skeletal muscle. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; U38191; AAC48530.1; -; mRNA. DR EMBL; U37770; AAC48528.1; -; mRNA. DR EMBL; U38190; AAC48529.1; -; mRNA. DR EMBL; U38192; AAC48531.1; -; mRNA. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Alternative splicing; Nuclear protein. FT CHAIN 1 524 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit gamma isoform. FT /FTId=PRO_0000071459. FT MOTIF 472 489 Nuclear localization signal (Potential). FT VAR_SEQ 443 524 YSLCSHASTVSMPLAMETDGPLFEDVQMLRKTVSDEARQAQ FT KDPKKERPLARRKSELPQDPHTKKALEAHCRADELVPQDGR FT -> VLKKRAI (in isoform Gamma-1). FT /FTId=VSP_005116. FT VAR_SEQ 482 524 AQKDPKKERPLARRKSELPQDPHTKKALEAHCRADELVPQD FT GR -> QLVGRKAVSSTQVRKV (in isoform Gamma- FT 4). FT /FTId=VSP_005114. FT VAR_SEQ 482 524 AQKDPKKERPLARRKSELPQDPHTKKALEAHCRADELVPQD FT GR -> VKVPG (in isoform Gamma-5). FT /FTId=VSP_005115. SQ SEQUENCE 524 AA; 60985 MW; DC4520D122DAF386 CRC64; MLTCNKAGSR MVVDAASSNG PFQPVALLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA VNMFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK LKMKEREEAW VKIENLAKAN PQYSLCSHAS TVSMPLAMET DGPLFEDVQM LRKTVSDEAR QAQKDPKKER PLARRKSELP QDPHTKKALE AHCRADELVP QDGR // ID 2A5I_ARATH Reviewed; 500 AA. AC Q93YV6; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 20-FEB-2007, entry version 24. DE Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' DE iota isoform (PP2A, B' subunit, iota isoform) (AtB' iota). GN Name=B'IOTA; OrderedLocusNames=At5g25510; ORFNames=T14C9.50; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016721; PubMed=11130714; DOI=10.1038/35048507; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families) (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; AC006601; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY059748; AAL24096.1; -; mRNA. DR EMBL; AY142557; AAN13126.1; -; mRNA. DR UniGene; At.21464; -. DR GenomeReviews; BA000015_GR; AT5G25510. DR KEGG; ath:At5g25510; -. DR TAIR; At5g25510; -. DR ArrayExpress; Q93YV6; -. DR GermOnline; AT5G25510; Arabidopsis thaliana. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. FT CHAIN 1 500 Serine/threonine protein phosphatase 2A FT 57 kDa regulatory subunit B' iota FT isoform. FT /FTId=PRO_0000071468. FT COMPBIAS 13 56 Ser-rich. SQ SEQUENCE 500 AA; 56422 MW; 9CDCCDA0311BA9D1 CRC64; MFKQFLSKLP RKSSKSDSGE LNRSSSGPVS SPVQRSGTSG GGSGPVRSNS GKRMSSAVFP ASVVAGIEPL VPFKDVPSSE KLNLFVSKVS LCCVTFDFSD PGKNSIEKDV KRQTLLELLD FVASGSVKFT EPAILAMCRM CAVNLFRVFP PNYRSSSGGE NDDDEPMFDP AWPHLQIVYD LLLKFITSPC LDAKVAKKYL DHAFIVRLLD LFDSEDPRER ECLKTILHRV YGKFMVHRPF VRKSMSNIFY RFVFETEKHS GIAELLEIFG SIVSGFALPL KEEHKIFLWR VLIPLHKPKS VGNYFQQLSY CITQFIDKEP KLGSVVIKGL LKFWPITNSQ KEVMFLGEVE EIVEAMSVME FQKIMVPLFL RIACCVTSSH FQVSERALFL WNNDQIVNLI GHNRQAILPI MFTALEKNAQ NHWNQSVLNL TLNVRKMFCE MDEALFMSCH ARFKEDEAKQ CSAAEKRKEV WARLENAASM KPITGKTAVL VTPRATSIAC // ID 2A5N_ARATH Reviewed; 510 AA. AC Q9LU89; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 23-JAN-2007, entry version 29. DE Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' DE eta isoform (PP2A, B' subunit, eta isoform) (AtB' eta). GN Name=B'ETA; OrderedLocusNames=At3g26020; ORFNames=MPE11.19; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20277480; PubMed=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP NOMENCLATURE. RX MEDLINE=22063724; PubMed=12068121; DOI=10.1104/pp.020004; RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.; RT "Molecular characterization and evolution of the protein phosphatase RT 2A B' regulatory subunit family in plants."; RL Plant Physiol. 129:808-822(2002). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families) (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; AB023041; BAB01065.1; -; Genomic_DNA. DR EMBL; AF367267; AAK56256.1; -; mRNA. DR EMBL; AY059158; AAL15383.1; -; mRNA. DR UniGene; At.6324; -. DR GenomeReviews; BA000014_GR; AT3G26020. DR KEGG; ath:At3g26020; -. DR TAIR; At3g26020; -. DR GermOnline; AT3G26020; Arabidopsis thaliana. DR InterPro; IPR002554; B56. DR InterPro; IPR002197; HTH_Fis. DR Pfam; PF01603; B56; 1. DR PRINTS; PR01590; HTHFIS. FT CHAIN 1 510 Serine/threonine protein phosphatase 2A FT 59 kDa regulatory subunit B' eta isoform. FT /FTId=PRO_0000071466. FT COMPBIAS 28 66 Ser-rich. FT COMPBIAS 78 85 Poly-Asn. SQ SEQUENCE 510 AA; 58758 MW; 02D36540CB860D28 CRC64; MWKQILSKLP NKKSSKHEHR GREHGGHSSS SSHTSGASTS KSTDNGAAKS HAKNASPAGK SAASDSGFKD GNLKSSGNNN NNNNNGVFTP YEALPSFKDV PNTEKQNLFI KKLNLCRVVF DFTDPTKNIK EKDIKRQTLL ELVDYVNSPN GKFSEVGIQE VVRMVSANIF RTLNPQPREN KVIDALDLEE EEPSMDLAWP HLQLVYELFL RFVASPETDT KLAKRYIDQS FVLRLLDLFD SEDPRERDCL KTILHRIYGK FMVHRPFIRK SINNIFYRFV FETEKHNGIA EFLEILGSII NGFALPLKDE HKVFLVRVLI PLHKPKCLQM YHQQLSYCIT QFVEKDCKLA DTVIRGLLKY WPVTNSSKEV MFLNELEEVL EATQPPEFQR CMVPLFRQIA RCLNSLHFQV AERALFLWNN NHIENLIMQN RKVILPIIFP ALERNAQKHW NQAVHSLTLN VRKIFHDLDP ELFKECLAKF KEDESKAAET EAKREATWKR LEELGVRKAS // ID 2A5R_MOUSE Reviewed; 491 AA. AC Q9Z176; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 20-FEB-2007, entry version 46. DE Protein phosphatase 2A, 59 kDa regulatory subunit B (PP2A PR59) (PP2A DE B''-PR59). GN Name=Ppp2r3a; Synonyms=Ppp2r6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Teratocarcinoma; RX MEDLINE=99124398; PubMed=9927208; DOI=10.1038/sj.onc.1202316; RA Voorhoeve P.M., Hijmans E.M., Bernards R.; RT "Functional interaction between a novel protein phosphatase 2A RT regulatory subunit, PR59, and the retinoblastoma-related p107 RT protein."; RL Oncogene 18:515-524(1999). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. Interacts with retinoblastoma-related protein p107 CC (in vivo). May target PP2A core dimer to p107 resulting in CC dephosphorylation of p107. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- TISSUE SPECIFICITY: Expressed in testis, kidney, liver, lung, CC spleen, brain and heart. CC -!- SIMILARITY: Contains 1 EF-hand 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; AF050165; AAC98973.1; -; mRNA. DR UniGene; Mm.271249; -. DR UniGene; Mm.429754; -. DR Ensembl; ENSMUSG00000057459; Mus musculus. DR KEGG; mmu:19054; -. DR MGI; MGI:1335093; Ppp2r3a. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; IPI:MGI. DR GO; GO:0000080; P:G1 phase of mitotic cell cycle; IDA:MGI. DR GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA:MGI. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR002048; EF_hand_Ca_bd. DR Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; FALSE_NEG. KW Calcium. FT CHAIN 1 491 Protein phosphatase 2A, 59 kDa regulatory FT subunit B. FT /FTId=PRO_0000071445. FT DOMAIN 331 366 EF-hand. FT CA_BIND 344 355 Potential. FT COMPBIAS 464 469 Poly-Asp. SQ SEQUENCE 491 AA; 55706 MW; 4B4BAB5C864FB683 CRC64; MPERPPIRAL RRDPDDPAVA QALASLARGS DLVFPSRFQK WLRDFRQVHA HRKEEPPPQS PPPGHTVPAF YFPCGRPPPR PQDTEDAIAL VECAFEGLPR GRAGLGDMAV VAKACGCPLY WKAPLFYAAG GERTGSVSVH MFVAMWRKVL LTCHDDAARF VRLLGHPGCS GLIQEDFVPF LQDVVNSHPG LAFLRAAKDF HSRYITTVIQ RIFYTVNRSW SGMISREELR RSSFLQAVSQ LEVEPDINRM TSFFSYEHFY VIYCKFWELD LDRDLTIDRS DLARHGDGAI SSRMIDRIFS GAVTRARLPR KVGKLSYADF VWFLLSEEDK TTPTSTEYWF RCMDLDGDGA LSMFELEFFY EEQAQRMAAR GVEPLPFHDL ARQVLDLVAP RCPGRITLRD LKQCGLAGEF FDAFFNVDKY LAREQREQAG TPQDTDSDPA ASAWDRYAAE EYDFLVAEEA MAEDDDDHDE GSDPIDLYGL ADEDCDDLEP L // ID 2A5T_ARATH Reviewed; 492 AA. AC Q8LF36; Q9FX52; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 2. DT 20-FEB-2007, entry version 23. DE Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' DE theta isoform (PP2A, B' subunit, theta isoform) (AtB' theta). GN Name=B'THETA; OrderedLocusNames=At1g13460; ORFNames=T6J4.19; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NOMENCLATURE. RX MEDLINE=22063724; PubMed=12068121; DOI=10.1104/pp.020004; RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.; RT "Molecular characterization and evolution of the protein phosphatase RT 2A B' regulatory subunit family in plants."; RL Plant Physiol. 129:808-822(2002). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families) (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; AC011810; AAG09562.1; -; Genomic_DNA. DR EMBL; AY085069; AAM61625.1; -; mRNA. DR UniGene; At.42029; -. DR GenomeReviews; CT485782_GR; AT1G13460. DR KEGG; ath:At1g13460; -. DR TAIR; At1g13460; -. DR GermOnline; AT1G13460; Arabidopsis thaliana. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. FT CHAIN 1 492 Serine/threonine protein phosphatase 2A FT 57 kDa regulatory subunit B' theta FT isoform. FT /FTId=PRO_0000071467. FT COMPBIAS 13 39 Ser-rich. FT CONFLICT 34 34 S -> G (in Ref. 2). FT CONFLICT 42 42 Q -> K (in Ref. 2). FT CONFLICT 488 488 Q -> K (in Ref. 2). SQ SEQUENCE 492 AA; 56510 MW; E49174DE756FE2CE CRC64; MWKQILSKLP KKSSSKNHSS SSSSTSKSSD NGASKSGNSQ TQNAPPVKPS ADSGFKEGNL KGNGNGFTPY EALPGFKDVP NAEKQNLFVR KLSLCCVVFD FSDPTKNVKE KDIKRQTLLE LVDYVASPNG KFSETVIQEV VRMVSVNIFR TLNPQPRENK VIDALDLEEE EPSMDPTWPH LQLVYEILLR LIASPETDTK LAKKYIDQSF VSRLLDLFDS EDPRERDCLK TVLHRIYGKF MVHRPFIRKS INNIFYRFVF ETEKHNGIAE FLEILGSIIN GFALPLKDEH KVFLVRALVP LHKPKSLQMY HQQLSYCITQ FVEKDCKLAD TVIRGLLKSW PVTNSSKEVM FLNELEEVLE ATQPPEFQRC MVPLFRQVAR CLNSLHFQVA ERALFLWNND HIENLIMQNR KVILPIIFPA LERNTQKHWN QAVHSLTLNV QKIFNDIDAE LFKDCLAKFR EDESKEAEIG AKREATWKRL EEIGNQKQKS SL // ID 2A5Z_ARATH Reviewed; 518 AA. AC Q9LVE2; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 23-JAN-2007, entry version 25. DE Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' DE zeta isoform (PP2A, B' subunit, zeta isoform) (AtB' zeta). GN Name=B'ZETA; OrderedLocusNames=At3g21650; ORFNames=MIL23.22; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20277480; PubMed=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). RN [2] RP NOMENCLATURE. RX MEDLINE=22063724; PubMed=12068121; DOI=10.1104/pp.020004; RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.; RT "Molecular characterization and evolution of the protein phosphatase RT 2A B' regulatory subunit family in plants."; RL Plant Physiol. 129:808-822(2002). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families) (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 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; AB019232; BAB02360.1; -; Genomic_DNA. DR KEGG; ath:At3g21650; -. DR TAIR; At3g21650; -. DR GermOnline; AT3G21650; Arabidopsis thaliana. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. FT CHAIN 1 518 Serine/threonine protein phosphatase 2A FT 59 kDa regulatory subunit B' zeta FT isoform. FT /FTId=PRO_0000071465. SQ SEQUENCE 518 AA; 58933 MW; 0F8DED600EF1B8F7 CRC64; MIKQIFGKLP RKPSKSLQND SNGEGASGSR VANGTLAPNS MSSNRNTNQG KKPLGGDAVV QAGPFPSSGG VYEALPSFRD VPISEKPNLF IGKLSMCCVV FDFSDPSKNL KEKEIKRQTL LELVDYVASV GFKFNDVSMQ ELTKMVAVNL FRTFPSANHE SKILEIHDMD DEEPSLEPAW PHVQVVYEIL LRFVASPMTD AKLAKRYIDH SFVLKLLDLF DSEDQREREY LKTILHRVYG KFMVHRPYIR KAINNIFYRF ISETEKHNGI AELLEILGSI INGFALPLKE EHKLFLLRAL IPLHKPKCSS VYHQQLSYCI VQFVEKDFKL ADTVIRGLLK YWPVTNSSKE VMFLGELEEV LEATQAAEFQ RCMVPLSRQI ARCLNSSHFQ VAERALFLWN NDHIRNLITQ NHKVIMPIVF PALERNTRGH WNQAVQSLTI NVRKVLCEID QVLFDECLAK FQVEEVNKTE VKAKRERTWQ RLEDLATSKT VVTNEAVLVP RFVSSVNLTT SSSESTGS // ID 2AAA_ARATH Reviewed; 588 AA. AC Q38845; Q38855; Q38952; Q56WI3; Q570B7; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 45. DE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A DE alpha isoform (PP2A, subunit A, alpha isoform) (PR-65 A) (AtA alpha) DE (Protein enhanced ethylene-response 1) (Protein ROOTS CURL IN DE NAPHTHYLPHTHALAMIC ACID 1). GN Name=PP2AA1; Synonyms=EER1, RCN1, REGA; OrderedLocusNames=At1g25490; GN ORFNames=F2J7.19; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf; RX MEDLINE=95111096; PubMed=7811971; RA Slabas A.R., Fordham-Skelton A.P., Fletcher D., Martinez-Rivas J.M., RA Swinhoe R., Croy R.R.D., Evans I.M.; RT "Characterisation of cDNA and genomic clones encoding homologues of RT the 65 kDa regulatory subunit of protein phosphatase 2A in Arabidopsis RT thaliana."; RL Plant Mol. Biol. 26:1125-1138(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX MEDLINE=96208498; PubMed=8641277; RA Garbers C., DeLong A., Deruere J., Bernasconi P., Soell D.; RT "A mutation in protein phosphatase 2A regulatory subunit A affects RT auxin transport in Arabidopsis."; RL EMBO J. 15:2115-2124(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=cv. Columbia; RX MEDLINE=96343945; PubMed=8756607; RA Corum J.W. III, Hartung A.J., Stamey R.T., Rundle S.J.; RT "Characterization of DNA sequences encoding a novel isoform of the 55 RT kDa B regulatory subunit of the type 2A protein serine/threonine RT phosphatase of Arabidopsis thaliana."; RL Plant Mol. Biol. 31:419-427(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-588. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP INTERACTION WITH PP2A SUBUNITS B AND C. RX MEDLINE=99191692; PubMed=10091592; RX DOI=10.1046/j.1432-1327.1999.00154.x; RA Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S., RA Rundle S.J.; RT "Molecular characterization of the B' regulatory subunit gene family RT of Arabidopsis protein phosphatase 2A."; RL Eur. J. Biochem. 260:127-136(1999). RN [8] RP INTERACTION WITH CYP20-1/ROC7. RX MEDLINE=20092489; PubMed=10628867; DOI=10.1007/s004380051147; RA Jackson K., Soell D.; RT "Mutations in a new Arabidopsis cyclophilin disrupt its interaction RT with protein phosphatase 2A."; RL Mol. Gen. Genet. 262:830-838(1999). RN [9] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=20074779; PubMed=10607292; RX DOI=10.1046/j.1365-313x.1999.00607.x; RA Deruere J., Jackson K., Garbers C., Soell D., Delong A.; RT "The RCN1-encoded A subunit of protein phosphatase 2A increases RT phosphatase activity in vivo."; RL Plant J. 20:389-399(1999). RN [10] RP FUNCTION. RX MEDLINE=21342512; PubMed=11449059; DOI=10.1105/tpc.13.7.1683; RA Rashotte A.M., DeLong A., Muday G.K.; RT "Genetic and chemical reductions in protein phosphatase activity alter RT auxin transport, gravity response, and lateral root growth."; RL Plant Cell 13:1683-1697(2001). RN [11] RP FUNCTION. RX MEDLINE=21107275; PubMed=11161061; DOI=10.1104/pp.125.2.1061; RA Larsen P.B., Chang C.; RT "The Arabidopsis eer1 mutant has enhanced ethylene responses in the RT hypocotyl and stem."; RL Plant Physiol. 125:1061-1073(2001). RN [12] RP FUNCTION. RX MEDLINE=22305406; PubMed=12417706; DOI=10.1105/tpc.003335; RA Kwak J.M., Moon J.-H., Murata Y., Kuchitsu K., Leonhardt N., RA DeLong A., Schroeder J.I.; RT "Disruption of a guard cell-expressed protein phosphatase 2A RT regulatory subunit, RCN1, confers abscisic acid insensitivity in RT Arabidopsis."; RL Plant Cell 14:2849-2861(2002). RN [13] RP FUNCTION. RX MEDLINE=22674160; PubMed=12787251; RX DOI=10.1046/j.1365-313X.2003.01762.x; RA Larsen P.B., Cancel J.D.; RT "Enhanced ethylene responsiveness in the Arabidopsis eer1 mutant RT results from a loss-of-function mutation in the protein phosphatase 2A RT A regulatory subunit, RCN1."; RL Plant J. 34:709-718(2003). RN [14] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=14973165; DOI=10.1105/tpc.018994; RA Zhou H.-W., Nussbaumer C., Chao Y., DeLong A.; RT "Disparate roles for the regulatory A subunit isoforms in Arabidopsis RT protein phosphatase 2A."; RL Plant Cell 16:709-722(2004). RN [15] RP INTERACTION WITH PHOSPHATIDIC ACID. RX PubMed=15272872; DOI=10.1111/j.1365-313X.2004.02152.x; RA Testerink C., Dekker H.L., Lim Z.-Y., Johns M.K., Holmes A.B., RA De Koster C.G., Ktistakis N.T., Munnik T.; RT "Isolation and identification of phosphatidic acid targets from RT plants."; RL Plant J. 39:527-536(2004). CC -!- FUNCTION: The A subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit. Seems to act as a CC positive regulator of PP2A catalytic activity. Confers resistance CC to phosphatase inhibitors such as okadaic acid and cantharidin. CC Involved during developmental process such as seedling and floral CC developments, root gravitropism, and stomatal opening regulation. CC Involved in the regulation of auxin efflux, especially during CC basipetal (tips to base) auxin transport in roots, and appears to CC contribute to the perception of auxin efflux inhibitors such as 1- CC N-naphthylphthalamic acid (NPA) and to semicarbazone I CC (substituted phenylsemicarbazone of 2-acetylarylcarboxylic acids) CC (SCB-I). Modulates the magnitude of ethylene response in the CC hypocotyl and stem, and functions as a general positive transducer CC of early ABA signaling. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (subunit A), that associates with a CC variety of regulatory subunits such as subunits B (the CC R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families). CC Interacts with CYP20-1/ROC7. Also interacts with phosphatidic acid CC (PA), a lipid signaling molecule. CC -!- TISSUE SPECIFICITY: Mostly expressed in cell-dividing tissues such CC as apical meristems. Ubiquitous, with higher levels in roots and CC flowers (at protein level). CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure (By CC similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 14 HEAT 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; X82001; CAA57527.1; -; Genomic_DNA. DR EMBL; U21557; AAC49255.1; -; mRNA. DR EMBL; U27299; AAB60713.1; -; mRNA. DR EMBL; AC079281; AAG50801.1; -; Genomic_DNA. DR EMBL; AY120757; AAM53315.1; -; mRNA. DR EMBL; BT000108; AAN15427.1; -; mRNA. DR EMBL; AK220793; BAD94039.1; -; mRNA. DR EMBL; AK222057; BAD94840.1; -; mRNA. DR PIR; B86385; B86385. DR PIR; S51807; S51807. DR PIR; S69215; S69215. DR UniGene; At.160; -. DR HSSP; P30153; 1B3U. DR GenomeReviews; CT485782_GR; AT1G25490. DR KEGG; ath:At1g25490; -. DR TAIR; At1g25490; -. DR ArrayExpress; Q38845; -. DR GermOnline; AT1G25490; Arabidopsis thaliana. DR GO; GO:0009738; P:abscisic acid mediated signaling; TAS:TAIR. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 12. DR PROSITE; PS50077; HEAT_REPEAT; 12. KW Abscisic acid signaling pathway; Auxin signaling pathway; KW Ethylene signaling pathway; Repeat. FT CHAIN 1 588 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A alpha FT isoform. FT /FTId=PRO_0000071409. FT REPEAT 2 42 HEAT 1. FT REPEAT 44 80 HEAT 2. FT REPEAT 81 119 HEAT 3. FT REPEAT 158 196 HEAT 4. FT REPEAT 197 235 HEAT 5. FT REPEAT 236 274 HEAT 6. FT REPEAT 275 313 HEAT 7. FT REPEAT 315 352 HEAT 8. FT REPEAT 353 391 HEAT 9. FT REPEAT 393 430 HEAT 10. FT REPEAT 432 469 HEAT 11. FT REPEAT 470 508 HEAT 12. FT REPEAT 509 547 HEAT 13. FT REPEAT 549 586 HEAT 14. FT CONFLICT 104 104 E -> G (in Ref. 1). FT CONFLICT 270 270 E -> K (in Ref. 1). FT CONFLICT 435 435 D -> Y (in Ref. 1). FT CONFLICT 457 457 A -> AAA (in Ref. 1 and 3). SQ SEQUENCE 588 AA; 65494 MW; F27E294E85B8DAFA CRC64; MAMVDEPLYP IAVLIDELKN DDIQLRLNSI RRLSTIARAL GEERTRKELI PFLSENSDDD DEVLLAMAEE LGVFIPFVGG IEFAHVLLPP LESLCTVEET CVREKAVESL CKIGSQMKEN DLVESFVPLV KRLAGGEWFA ARVSACGIFH VAYQGCTDVL KTELRATYSQ LCKDDMPMVR RAAASNLGKF ATTVESTFLI AEIMTMFDDL TKDDQDSVRL LAVEGCAALG KLLEPQDCVA RILPVIVNFS QDKSWRVRYM VANQLYELCE AVGPDCTRTD LVPAYVRLLR DNEAEVRIAA AGKVTKFCRL LNPELAIQHI LPCVKELSSD SSQHVRSALA SVIMGMAPIL GKDSTIEHLL PIFLSLLKDE FPDVRLNIIS KLDQVNQVIG IDLLSQSLLP AIVELAEDRH WRVRLAIIEY VPLLASQLGI GFFDDKLGAL CMQWLQDKVY SIREAAANNL KRLAEEFGPE WAMQHLVPQV LDMVNNPHYL HRMMVLRAIS LMAPVMGSEI TCSKFLPVVV EASKDRVPNI KFNVAKLLQS LIPIVDQSVV DKTIRQCLVD LSEDPDVDVR YFANQALNSI DGSTAAQS // ID 2AAA_CAEEL Reviewed; 590 AA. AC Q09543; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2003, sequence version 2. DT 20-FEB-2007, entry version 43. DE Probable serine/threonine-protein phosphatase PP2A regulatory subunit DE (Protein phosphatase PP2A regulatory subunit A). GN Name=paa-1; ORFNames=F48E8.5; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [2] RP SEQUENCE REVISION. RG WormBase consortium; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit (By similarity). CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which CC consist of a core composed of a catalytic subunit associated with CC a 65 kDa regulatory subunit (PR65) (subunit A). The core complex CC associates with a third, variable subunit (subunit B), which CC confers distinct properties to the holoenzyme (By similarity). CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 14 HEAT 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; U23514; AAC46541.2; -; Genomic_DNA. DR PIR; T16411; T16411. DR UniGene; Cel.24358; -. DR HSSP; P30153; 1B3U. DR Ensembl; F48E8.5; Caenorhabditis elegans. DR KEGG; cel:F48E8.5; -. DR WormBase; WBGene00003901; paa-1. DR WormPep; F48E8.5; CE30997. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 9. DR PROSITE; PS50077; HEAT_REPEAT; 8. KW Complete proteome; Repeat. FT CHAIN 1 590 Probable serine/threonine-protein FT phosphatase PP2A regulatory subunit. FT /FTId=PRO_0000071407. FT REPEAT 37 73 HEAT 1. FT REPEAT 74 111 HEAT 2. FT REPEAT 113 150 HEAT 3. FT REPEAT 151 188 HEAT 4. FT REPEAT 189 227 HEAT 5. FT REPEAT 228 266 HEAT 6. FT REPEAT 267 305 HEAT 7. FT REPEAT 306 344 HEAT 8. FT REPEAT 349 387 HEAT 9. FT REPEAT 388 426 HEAT 10. FT REPEAT 427 465 HEAT 11. FT REPEAT 466 504 HEAT 12. FT REPEAT 505 543 HEAT 13. FT REPEAT 544 582 HEAT 14. FT COMPBIAS 186 189 Poly-Ala. SQ SEQUENCE 590 AA; 66149 MW; E9B6F7DFFEB973E2 CRC64; MSVVEEATDD ALYPIAVLID ELRNEDVTLR LNSIRKLSTI ALALGVERTR NELIQFLTDT IYDEDEVLLV LAEQLGNFTP LVGGPDHVHC LLLPLENLAT VEETVVRDKA VESLRKIADK HSSASLEEHF VPMLRRLATG DWFTSRTSAC GLFSVVYPRV SPAIKSELKS MFRTLCRDDT PMVRRAAAAK LGEFAKVFEK TAVIEGLHSS LTDLHVDEQD SVRLLTVESA IAFGTLLDKA NKKKLIEPIL IELFDDKSWR VRYMVAEKLI EIQNVLGEDM DTTHLVNMYT NLLKDPEGEV RCAATQRLQE FALNLPEDKR QNIICNSLLN VAKELVTDGN QLVKSELAGV IMGLAPLIGK EQTVSELLPI YMQLLNDQTP EVRLNIISSL DKVNEVIGAA QLSTSLLPAI VGLAEDGKWR VRLAIVQFMP LLASQLGQEF FDEKLLPLCL NWLTDHVFSI REASTLIMKE LTQKFGGQWA STNIVPKMQK LQKDTNYLQR MTCLFCLNTL SEAMTQEQIL KEIMPIVKDL VEDDVPNVRF NAAKSLKRIG KNLTPSTLTS EVKPLLEKLG KDSDFDVRYF SEEAKNSLGL // ID 2AAA_DROME Reviewed; 591 AA. AC P36179; Q2MGK6; Q9VLN3; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 20-FEB-2007, entry version 54. DE Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit DE (Protein phosphatase PP2A regulatory subunit A) (PR65). GN Name=Pp2A-29B; ORFNames=CG17291; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC TISSUE=Embryo; RX MEDLINE=92329996; PubMed=1320961; RA Mayer-Jaekel R.E., Baumgartner S., Bilbe G., Ohkura H., Glover D.M., RA Hemmings B.A.; RT "Molecular cloning and developmental expression of the catalytic and RT 65-kDa regulatory subunits of protein phosphatase 2A in Drosophila."; RL Mol. Biol. Cell 3:287-298(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit (By similarity). CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which CC consist of a core composed of a catalytic subunit associated with CC a 65 kDa regulatory subunit (PR65) (subunit A). The core complex CC associates with a third, variable subunit (subunit B), which CC confers distinct properties to the holoenzyme. CC -!- INTERACTION: CC Q9VGY3:CG14684; NbExp=1; IntAct=EBI-139308, EBI-110589; CC Q9VPA3:csn3; NbExp=1; IntAct=EBI-139308, EBI-107823; CC -!- TISSUE SPECIFICITY: Expression varies in tissues throughout CC development. Highly distributed expression in early embryos. In CC late embryonal development, found at high levels in nervous system CC and gonads. In third instar larvae, found in brain, imaginal disks CC and salivary glands. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. CC Expressed at lower levels in larvae and adult. CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT 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; M86442; AAA28304.1; -; mRNA. DR EMBL; AE014134; AAF52650.2; -; Genomic_DNA. DR UniGene; Dm.1532; -. DR HSSP; P30153; 1B3U. DR SMR; P36179; 4-591. DR IntAct; P36179; -. DR Ensembl; CG33297; Drosophila melanogaster. DR KEGG; dme:Dmel_CG17291; -. DR FlyBase; FBgn0005776; Pp2A-29B. DR GermOnline; CG17291; Drosophila melanogaster. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 12. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW Acetylation; Complete proteome; Repeat. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 591 Serine/threonine-protein phosphatase PP2A FT 65 kDa regulatory subunit. FT /FTId=PRO_0000071408. FT REPEAT 10 48 HEAT 1. FT REPEAT 49 86 HEAT 2. FT REPEAT 87 125 HEAT 3. FT REPEAT 126 163 HEAT 4. FT REPEAT 164 202 HEAT 5. FT REPEAT 203 241 HEAT 6. FT REPEAT 242 280 HEAT 7. FT REPEAT 281 323 HEAT 8. FT REPEAT 324 362 HEAT 9. FT REPEAT 363 401 HEAT 10. FT REPEAT 402 440 HEAT 11. FT REPEAT 441 479 HEAT 12. FT REPEAT 480 518 HEAT 13. FT REPEAT 519 557 HEAT 14. FT REPEAT 558 591 HEAT 15. FT MOD_RES 2 2 N-acetylalanine (By similarity). FT CONFLICT 232 232 S -> T (in Ref. 1). SQ SEQUENCE 591 AA; 65424 MW; 13948F39796662AC CRC64; MAASDKSVDD SLYPIAVLID ELKNEDVQLR LNSIKKLSTI ALALGEERTR SELIPFLTET IYDEDEVLLA LADQLGNFTS LVGGPEFAMY LIPPLESLAT VEETVVRDKA VESLRTVAAE HSAQDLEIHV VPTLQRLVSG DWFTSRTSAC GLFSVCYPRV TQPVKAELRA NFRKLCQDET PMVRRAAANK LGEFAKVVET EYLKSDLIPN FVQLAQDDQD SVRLLAVEAC VSIAQLLPQD DVEHLVLPTL RQCASDSSWR VRYMVAEKFV DLQKAVGPEI TRVDLVPAFQ YLLKDAEAEV RAAVATKVKD FCANLDKVNQ VQIILSSILP YVRDLVSDPN PHVKSALASV IMGLSPMLGA YQTVEQLLPL FLIQLKDECP EVRLNIISNL DCVNDVIGIQ QLSQSLLPAI VELAEDSKWR VRLAIIEYMP ALAGQLGQEF FDQKLRGLCM GWLNDHVYAI REAATLNMKK LVEQFGAPWA EQAIIPMILV MSRNKNYLHR MTCLFCLNVL AEVCGTDITT KLLLPTVLLL AADPVANVRF NVAKTLQKIS PFLEASVIDA QVKPTLDKLN TDTDVDVKHF AAQAIAGIAA A // ID 2AAA_HUMAN Reviewed; 589 AA. AC P30153; Q13773; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 66. DE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A DE alpha isoform (PP2A, subunit A, PR65-alpha isoform) (PP2A, subunit A, DE R1-alpha isoform) (Medium tumor antigen-associated 61 kDa protein). GN Name=PPP2R1A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 242-255. RC TISSUE=Placenta; RX MEDLINE=90046854; PubMed=2554323; RA Walter G., Ferre F., Espiritu O., Carbone-Wiley A.; RT "Molecular cloning and sequence of cDNA encoding polyoma medium tumor RT antigen-associated 61-kDa protein."; RL Proc. Natl. Acad. Sci. U.S.A. 86:8669-8672(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90241887; PubMed=2159327; DOI=10.1021/bi00465a002; RA Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., RA Merlevede W., Hofsteenge J., Stone S.R.; RT "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A RT have a similar 39 amino acid repeating structure."; RL Biochemistry 29:3166-3173(1990). RN [3] RP PROTEIN SEQUENCE OF 204-214; 261-272 AND 521-527. RX MEDLINE=96276417; PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [4] RP BINDING DOMAINS. RX MEDLINE=94076400; PubMed=8254721; RA Ruediger R., Hentz M., Fait J., Mumby M., Walter G.; RT "Molecular model of the A subunit of protein phosphatase 2A: RT interaction with other subunits and tumor antigens."; RL J. Virol. 68:123-129(1994). RN [5] RP INTERACTION WITH IPO9. RX PubMed=12670497; DOI=10.1016/S0006-291X(03)00434-0; RA Lubert E.J., Sarge K.D.; RT "Interaction between protein phosphatase 2A and members of the RT importin beta superfamily."; RL Biochem. Biophys. Res. Commun. 303:908-913(2003). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX MEDLINE=99142607; PubMed=9989501; DOI=10.1016/S0092-8674(00)80963-0; RA Groves M.R., Hanlon N., Turowski P., Hemmings B.A., Barford D.; RT "The structure of the protein phosphatase 2A PR65/A subunit reveals RT the conformation of its 15 tandemly repeated HEAT motifs."; RL Cell 96:99-110(1999). CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. Interacts with IPO9. CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT 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; M31786; AAA35531.1; -; mRNA. DR EMBL; J02902; AAA36399.1; -; mRNA. DR PIR; A34541; A34541. DR UniGene; Hs.467192; -. DR PDB; 1B3U; X-ray; A=1-589. DR PDB; 2IE4; X-ray; A=1-589. DR IntAct; P30153; -. DR OGP; P30153; -. DR REPRODUCTION-2DPAGE; P30153; HUMAN. DR Ensembl; ENSG00000105568; Homo sapiens. DR KEGG; hsa:5518; -. DR HGNC; HGNC:9302; PPP2R1A. DR MIM; 605983; gene. DR Reactome; REACT_1505.1; Integration of pathways involved in energy metabolism. DR Reactome; REACT_1919.2; Dephosphorylation of pChREBP by PP2A. DR ArrayExpress; P30153; -. DR GermOnline; ENSG00000105568; Homo sapiens. DR RZPD-ProtExp; C0281; -. DR RZPD-ProtExp; IOH13670; -. DR RZPD-ProtExp; RZPDo834D1214; -. DR RZPD-ProtExp; RZPDo839E0964; -. DR GO; GO:0005829; C:cytosol; TAS:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; NAS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; NAS:UniProtKB. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:UniProtKB. DR GO; GO:0005625; C:soluble fraction; NAS:UniProtKB. DR GO; GO:0003823; F:antigen binding; IPI:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:UniProtKB. DR GO; GO:0006672; P:ceramide metabolic process; NAS:UniProtKB. DR GO; GO:0000188; P:inactivation of MAPK activity; NAS:UniProtKB. DR GO; GO:0006917; P:induction of apoptosis; TAS:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB. DR GO; GO:0042518; P:negative regulation of tyrosine phosphoryla...; NAS:UniProtKB. DR GO; GO:0006470; P:protein amino acid dephosphorylation; TAS:UniProtKB. DR GO; GO:0006461; P:protein complex assembly; TAS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; NAS:UniProtKB. DR GO; GO:0045595; P:regulation of cell differentiation; NAS:UniProtKB. DR GO; GO:0006275; P:regulation of DNA replication; NAS:UniProtKB. DR GO; GO:0000074; P:regulation of progression through cell cycle; TAS:UniProtKB. DR GO; GO:0045449; P:regulation of transcription; NAS:UniProtKB. DR GO; GO:0030111; P:regulation of Wnt receptor signaling pathway; NAS:UniProtKB. DR GO; GO:0010033; P:response to organic substance; NAS:UniProtKB. DR GO; GO:0008380; P:RNA splicing; NAS:UniProtKB. DR GO; GO:0019932; P:second-messenger-mediated signaling; NAS:UniProtKB. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 11. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW 3D-structure; Acetylation; Direct protein sequencing; Polymorphism; KW Repeat. FT INIT_MET 1 1 Removed. FT CHAIN 2 589 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A alpha FT isoform. FT /FTId=PRO_0000071400. FT REPEAT 8 46 HEAT 1. FT REPEAT 47 84 HEAT 2. FT REPEAT 85 123 HEAT 3. FT REPEAT 124 161 HEAT 4. FT REPEAT 162 200 HEAT 5. FT REPEAT 201 239 HEAT 6. FT REPEAT 240 278 HEAT 7. FT REPEAT 279 321 HEAT 8. FT REPEAT 322 360 HEAT 9. FT REPEAT 361 399 HEAT 10. FT REPEAT 400 438 HEAT 11. FT REPEAT 439 477 HEAT 12. FT REPEAT 478 516 HEAT 13. FT REPEAT 517 555 HEAT 14. FT REPEAT 556 589 HEAT 15. FT REGION 8 399 PP2A subunit B binding. FT REGION 47 321 Polyoma small and medium T antigens FT Binding. FT REGION 85 239 SV40 small T antigen binding. FT REGION 400 589 PP2A subunit C binding. FT MOD_RES 2 2 N-acetylalanine. FT VARIANT 87 87 H -> R (in lung). FT /FTId=VAR_006383. FT CONFLICT 130 130 P -> A (in Ref. 1). FT CONFLICT 258 258 A -> R (in Ref. 1). FT CONFLICT 272 272 K -> R (in Ref. 3). FT TURN 6 8 FT HELIX 11 19 FT TURN 20 21 FT HELIX 25 33 FT TURN 34 34 FT HELIX 35 41 FT HELIX 44 49 FT TURN 50 50 FT HELIX 51 57 FT TURN 58 58 FT HELIX 63 73 FT TURN 74 75 FT HELIX 78 80 FT TURN 81 81 FT HELIX 83 89 FT HELIX 90 96 FT TURN 97 98 FT HELIX 102 116 FT TURN 117 118 FT HELIX 121 126 FT TURN 127 127 FT HELIX 128 136 FT TURN 137 137 FT HELIX 141 147 FT HELIX 148 150 FT HELIX 151 154 FT TURN 155 157 FT HELIX 160 174 FT TURN 175 175 FT HELIX 179 194 FT TURN 195 195 FT HELIX 198 203 FT TURN 204 204 FT HELIX 205 213 FT TURN 214 214 FT HELIX 218 221 FT TURN 222 223 FT HELIX 224 234 FT HELIX 237 239 FT HELIX 240 243 FT TURN 244 244 FT HELIX 245 252 FT TURN 253 253 FT HELIX 257 265 FT TURN 266 266 FT HELIX 267 274 FT HELIX 276 281 FT TURN 282 282 FT HELIX 283 291 FT TURN 292 292 FT HELIX 296 311 FT TURN 312 312 FT TURN 315 317 FT HELIX 318 324 FT TURN 325 325 FT HELIX 326 334 FT TURN 335 335 FT HELIX 339 346 FT TURN 347 348 FT HELIX 349 352 FT HELIX 353 356 FT HELIX 358 364 FT TURN 365 365 FT HELIX 366 373 FT TURN 374 374 FT HELIX 378 385 FT TURN 386 387 FT HELIX 389 394 FT HELIX 397 412 FT TURN 413 413 FT HELIX 417 434 FT HELIX 436 438 FT HELIX 441 449 FT HELIX 450 452 FT HELIX 456 473 FT HELIX 475 481 FT TURN 482 482 FT HELIX 483 488 FT TURN 489 491 FT HELIX 495 520 FT TURN 521 521 FT HELIX 522 527 FT HELIX 528 530 FT HELIX 534 547 FT HELIX 548 550 FT HELIX 553 567 FT TURN 568 569 FT HELIX 573 585 FT TURN 586 587 SQ SEQUENCE 589 AA; 65223 MW; E5E8850ABE6D5E95 CRC64; MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ AAEDKSWAVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA AASHKVKEFC ENLSADCREN VIMSQILPCI KELVSDANQH VKSALASVIM GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA // ID 2AAA_MOUSE Reviewed; 589 AA. AC Q76MZ3; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 30. DE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A DE alpha isoform (PP2A, subunit A, PR65-alpha isoform) (PP2A, subunit A, DE R1-alpha isoform). GN Name=Ppp2r1a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10100624; DOI=10.1016/S0014-5793(99)00189-1; RA Nanahoshi M., Tsujishita Y., Tokunaga C., Inui S., Sakaguchi N., RA Hara K., Yonezawa K.; RT "Alpha4 protein as a common regulator of type 2A-related RT serine/threonine protein phosphatases."; RL FEBS Lett. 446:108-112(1999). RN [2] 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 [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: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. Interacts with IPO9 (By similarity). CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT 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; AB021743; BAA75478.1; -; mRNA. DR EMBL; AK054239; BAC35700.1; -; mRNA. DR EMBL; AK078135; BAC37143.1; -; mRNA. DR EMBL; BC006606; AAH06606.1; -; mRNA. DR UniGene; Mm.294138; -. DR SMR; Q76MZ3; 2-589. DR IntAct; Q76MZ3; -. DR KEGG; mmu:51792; -. DR MGI; MGI:1926334; Ppp2r1a. DR ArrayExpress; Q76MZ3; -. DR GermOnline; ENSMUSG00000007564; Mus musculus. DR RZPD-ProtExp; IOM18900; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 11. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW Acetylation; Repeat. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 589 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A alpha FT isoform. FT /FTId=PRO_0000071401. FT REPEAT 8 46 HEAT 1. FT REPEAT 47 84 HEAT 2. FT REPEAT 85 123 HEAT 3. FT REPEAT 124 161 HEAT 4. FT REPEAT 162 200 HEAT 5. FT REPEAT 201 239 HEAT 6. FT REPEAT 240 278 HEAT 7. FT REPEAT 279 321 HEAT 8. FT REPEAT 322 360 HEAT 9. FT REPEAT 361 399 HEAT 10. FT REPEAT 400 438 HEAT 11. FT REPEAT 439 477 HEAT 12. FT REPEAT 478 516 HEAT 13. FT REPEAT 517 555 HEAT 14. FT REPEAT 556 589 HEAT 15. FT MOD_RES 2 2 N-acetylalanine (By similarity). SQ SEQUENCE 589 AA; 65323 MW; 5175409E4D50A366 CRC64; MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA AASHKVKEFC ENLSADCREN VIMTQILPCI KELVSDANQH VKSALASVIM GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA // ID 2AAA_PEA Reviewed; 395 AA. AC P36875; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 28-NOV-2006, entry version 34. DE Protein phosphatase PP2A regulatory subunit A (PR65) (Fragment). OS Pisum sativum (Garden pea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Vicieae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. JI 813; RX MEDLINE=94207195; PubMed=8155887; RA Evans I.M., Fawcett T., Boulter D., Fordham-Skelton A.P.; RT "A homologue of the 65 kDa regulatory subunit of protein phosphatase RT 2A in early pea (Pisum sativum L.) embryos."; RL Plant Mol. Biol. 24:689-695(1994). CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit (By similarity). CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which CC consist of a core composed of a catalytic subunit associated with CC a 65 kDa regulatory subunit (PR65) (subunit A). The core complex CC associates with a third, variable subunit (subunit B), which CC confers distinct properties to the holoenzyme. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains at least 8 HEAT 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; Z25888; CAA81107.1; -; mRNA. DR PIR; S43776; S40171. DR HSSP; P30153; 1B3U. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 9. DR PROSITE; PS50077; HEAT_REPEAT; 8. KW Repeat. FT CHAIN <1 395 Protein phosphatase PP2A regulatory FT subunit A. FT /FTId=PRO_0000071412. FT REPEAT 44 81 HEAT 1. FT REPEAT 83 120 HEAT 2. FT REPEAT 122 159 HEAT 3. FT REPEAT 161 198 HEAT 4. FT REPEAT 200 237 HEAT 5. FT REPEAT 239 276 HEAT 6. FT REPEAT 279 316 HEAT 7. FT REPEAT 318 355 HEAT 8. FT NON_TER 1 1 SQ SEQUENCE 395 AA; 43912 MW; F444DBDC935F8A04 CRC64; VEAAHLKTDI MSVFDDLTQD DQDSFRFLAV EGCAALGKLL EPQDCLAHIL PVIVNFSQDK SWRVRYMVAN QLYELCEAVG PDSTKTELVP AYVRLLRDNV AEVRIAAAGK VSKFSRILSP ELAIQHILPC VKELSTDSSQ HVRSALASVI MGMAPVLGKD ATIEQLLPIF LSLLKDEFPD VRLNIISKLD QVNQVIGIDL LSQSLLPAIV ELAEDRHWRV RLAIIEYIPL LASQLGVGFF DDKLGALIMQ WLKDKEYSIR NAAANNVKRL AAEEFGPEWA MQHIIPQVLD MINDPHYLYR MTILHAISLL APVLGSEITS TNLLPLVVNA SKDRVPNIKF NVAKVLQSLI PIVDESVVES TIRPCLVELS EDPDVDVRFF ASQALQSSDQ VKMSS // ID 2AAA_PIG Reviewed; 589 AA. AC P54612; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 38. DE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A DE alpha isoform (PP2A, subunit A, PR65-alpha isoform) (PP2A, subunit A, DE R1-alpha isoform). GN Name=PPP2R1A; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Mayer-Jaekel R.E.; RL Thesis (1992), Friedrich Miescher Institut / Basel, Switzerland. CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. Interacts with IPO9 (By similarity). CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT 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; Z34955; CAA84414.1; -; mRNA. DR UniGene; Ssc.102; -. DR HSSP; P30153; 1B3U. DR SMR; P54612; 2-589. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 11. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW Acetylation; Repeat. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 589 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A alpha FT isoform. FT /FTId=PRO_0000071402. FT REPEAT 8 46 HEAT 1. FT REPEAT 47 84 HEAT 2. FT REPEAT 85 123 HEAT 3. FT REPEAT 124 161 HEAT 4. FT REPEAT 162 200 HEAT 5. FT REPEAT 201 239 HEAT 6. FT REPEAT 240 278 HEAT 7. FT REPEAT 279 321 HEAT 8. FT REPEAT 322 360 HEAT 9. FT REPEAT 361 399 HEAT 10. FT REPEAT 400 438 HEAT 11. FT REPEAT 439 477 HEAT 12. FT REPEAT 478 516 HEAT 13. FT REPEAT 517 555 HEAT 14. FT REPEAT 556 589 HEAT 15. FT MOD_RES 2 2 N-acetylalanine (By similarity). SQ SEQUENCE 589 AA; 65323 MW; 5175409E4D50A366 CRC64; MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA AASHKVKEFC ENLSADCREN VIMTQILPCI KELVSDANQH VKSALASVIM GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA // ID 2AAA_SCHPO Reviewed; 590 AA. AC Q9UT08; Q10293; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 28-NOV-2006, entry version 33. DE Protein phosphatase PP2A regulatory subunit A (PR65) (Protein DE phosphatase 2A 65 kDa regulatory subunit). GN Name=paa1; ORFNames=SPAP8A3.09c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=97233175; PubMed=9078365; RA Kinoshita K., Nemoto T., Nabeshima K., Kondoh H., Niwa H., RA Yanagida M.; RT "The regulatory subunits of fission yeast protein phosphatase 2A RT (PP2A) affect cell morphogenesis, cell wall synthesis and RT cytokinesis."; RL Genes Cells 1:29-45(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Phosphatase 2A affects a variety of biological processes CC in the cell such as transcription, cell cycle progression and CC cellular morphogenesis, and provides an initial identification of CC critical substrates for this phosphatase. The regulatory subunit CC may direct the catalytic subunit to distinct, albeit overlapping, CC subsets of substrates (By similarity). CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which CC consist of a core composed of a catalytic subunit associated with CC a 65 kDa (PR65) (Subunit A) and a 55 kDa (PR55) (Subunit B) CC regulatory subunit. CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 11 HEAT 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; D63916; BAA09946.1; -; Genomic_DNA. DR EMBL; AL117210; CAB55176.1; -; Genomic_DNA. DR PIR; T39246; T39246. DR PIR; T44416; T44416. DR HSSP; P30153; 1B3U. DR GeneDB_Spombe; SPAP8A3.09c; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-003009-MONOMER; -. DR ArrayExpress; Q9UT08; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 11. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW Complete proteome; Repeat. FT CHAIN 1 590 Protein phosphatase PP2A regulatory FT subunit A. FT /FTId=PRO_0000071413. FT REPEAT 12 50 HEAT 1. FT REPEAT 89 127 HEAT 2. FT REPEAT 206 244 HEAT 3. FT REPEAT 246 284 HEAT 4. FT REPEAT 285 323 HEAT 5. FT REPEAT 324 362 HEAT 6. FT REPEAT 363 401 HEAT 7. FT REPEAT 402 440 HEAT 8. FT REPEAT 480 518 HEAT 9. FT REPEAT 519 551 HEAT 10. FT REPEAT 562 590 HEAT 11. FT CONFLICT 2 5 QTEN -> LDNS (in Ref. 1). FT CONFLICT 89 89 L -> R (in Ref. 1). SQ SEQUENCE 590 AA; 66617 MW; 7F6337739B98CDC3 CRC64; MQTENQVNDL YPIAVLIDEL KHDEITYRLN ALERLSTIAL ALGPERTRDE LIPFLDESID DEDEVLSALA DQLGNFVDYV GGPEYAHVLL SPLENLAATE ETVVRDKAVD SLNKVCICLS QEQLEQYFVP LVQRLSTAEW FTSRASSAGL YCAAYSQSEN PAVKVSLRQS FSHLCHDEAP MVRRPAATNC AKFVFLVTKQ EAIDEFIPLF NSLSNDDQDS VRLLSFDIMV SLAEVLKSDS EIRHYLLQPL RSFVSDSSWR TRYMVAANFV KLAKVVGPSL IKDELIKPFV LLMKDTEQEV RRAIATQIPG FCELLDKRIV LEEIIPVIQE LINDPAQHVR AALGMNIGAL APQLGKEKTT EYLLPMFLEL LKDENPEVRL NIISKLEVVN KVVGIELLSQ SLLPAIVTLA EDKQWRVRLA IIDYIPLLAQ QLGVEFFNEK MGNLCMSWLE DHVYSIREAA IKNLRKLTEI FGLEWATETI IPKFLAMRSH PNYLYRMTTI FAISEIAPAL NAEVIEKQIL PTLEQLVNDP IPNIRFNVAK AFEVLKPVLA AGGDSTVYEQ QIIPLLEQLT KDNDPDVQYF ATQALEQTND // ID 2AAA_YEAST Reviewed; 635 AA. AC P31383; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 20-FEB-2007, entry version 59. DE Protein phosphatase PP2A regulatory subunit A (PR65). GN Name=TPD3; OrderedLocusNames=YAL016W; ORFNames=FUN32; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=93024440; PubMed=1328868; RA van Zyl W., Huang W., Sneddon A.A., Stark M., Camier S., Werner M., RA Marck C., Sentenac A., Broach J.R.; RT "Inactivation of the protein phosphatase 2A regulatory subunit A RT results in morphological and transcriptional defects in Saccharomyces RT cerevisiae."; RL Mol. Cell. Biol. 12:4946-4959(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=93209532; PubMed=8458570; RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., RA Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.; RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of RT a 32 kb region between the LTE1 and SPO7 genes."; RL Genome 36:32-42(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=94193531; PubMed=8144453; RA Barton A.B., Kaback D.B.; RT "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae: RT analysis of the genes in the FUN38-MAK16-SPO7 region."; RL J. Bacteriol. 176:1872-1880(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=95249563; PubMed=7731988; RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., RA Storms R.K.; RT "The nucleotide sequence of chromosome I from Saccharomyces RT cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995). RN [5] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Phosphatase 2A affects a variety of biological processes CC in the cell such as transcription, cell cycle progression and CC cellular morphogenesis, and provides an initial identification of CC critical substrates for this phosphatase. The regulatory subunit CC may direct the catalytic subunit to distinct, albeit overlapping, CC subsets of substrates. CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which CC consist of a core composed of a catalytic subunit associated with CC a 65 kDa regulatory subunit (PR65) (subunit A). The core complex CC associates with a third, variable subunit (subunit B), which CC confers distinct properties to the holoenzyme. CC -!- INTERACTION: CC Q03375:CWC21; NbExp=1; IntAct=EBI-1936, EBI-30409; CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- MISCELLANEOUS: Present with 16900 molecules/cell. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT 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; L05146; AAC04941.1; -; Genomic_DNA. DR EMBL; M98389; AAA35163.1; -; Genomic_DNA. DR PIR; S36718; S36718. DR HSSP; P30153; 1B3U. DR DIP; DIP:2010N; -. DR IntAct; P31383; -. DR Ensembl; YAL016W; Saccharomyces cerevisiae. DR GenomeReviews; U00091_GR; YAL016W. DR KEGG; sce:YAL016W; -. DR CYGD; YAL016w; -. DR SGD; S000000014; TPD3. DR LinkHub; P31383; -. DR GermOnline; YAL016W; Saccharomyces cerevisiae. DR GO; GO:0005935; C:bud neck; IDA:SGD. DR GO; GO:0005934; C:bud tip; IDA:SGD. DR GO; GO:0043332; C:mating projection tip; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:SGD. DR GO; GO:0005816; C:spindle pole body; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007015; P:actin filament organization; TAS:SGD. DR GO; GO:0007117; P:budding cell bud growth; TAS:SGD. DR GO; GO:0007094; P:mitotic spindle checkpoint; IMP:SGD. DR GO; GO:0006470; P:protein amino acid dephosphorylation; TAS:SGD. DR GO; GO:0006412; P:translation; IMP:SGD. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 12. DR PROSITE; PS50077; HEAT_REPEAT; 9. KW Complete proteome; Repeat. FT CHAIN 1 635 Protein phosphatase PP2A regulatory FT subunit A. FT /FTId=PRO_0000071414. FT REPEAT 34 72 HEAT 1. FT REPEAT 73 111 HEAT 2. FT REPEAT 112 150 HEAT 3. FT REPEAT 151 189 HEAT 4. FT REPEAT 190 228 HEAT 5. FT REPEAT 229 273 HEAT 6. FT REPEAT 274 316 HEAT 7. FT REPEAT 317 356 HEAT 8. FT REPEAT 357 395 HEAT 9. FT REPEAT 396 434 HEAT 10. FT REPEAT 435 473 HEAT 11. FT REPEAT 474 512 HEAT 12. FT REPEAT 513 553 HEAT 13. FT REPEAT 554 598 HEAT 14. FT REPEAT 599 632 HEAT 15. FT CONFLICT 611 611 F -> C (in Ref. 1). SQ SEQUENCE 635 AA; 70951 MW; 7B8305FB20633DC8 CRC64; MSGARSTTAG AVPSAATTST TSTTSNSKDS DSNESLYPLA LLMDELKHDD IANRVEAMKK LDTIALALGP ERTRNELIPF LTEVAQDDED EVFAVLAEQL GKFVPYIGGP QYATILLPVL EILASAEETL VREKAVDSLN NVAQELSQEQ LFSDFVPLIE HLATADWFSS KVSACGLFKS VIVRIKDDSL RKNILALYLQ LAQDDTPMVK RAVGKNLPIL IDLLTQNLGL STDEDWDYIS NIFQKIINDN QDSVKFLAVD CLISILKFFN AKGDESHTQD LLNSAVKLIG DEAWRVRYMA ADRFSDLASQ FSSNQAYIDE LVQPFLNLCE DNEGDVREAV AKQVSGFAKF LNDPSIILNK ILPAVQNLSM DESETVRSAL ASKITNIVLL LNKDQVINNF LPILLNMLRD EFPDVRLNII ASLKVVNDVI GIELLSDSLL PAITELAKDV NWRVRMAIIE YIPILAEQLG MQFFDQQLSD LCLSWLWDTV YSIREAAVNN LKRLTEIFGS DWCRDEIISR LLKFDLQLLE NFVSRFTILS ALTTLVPVVS LDVVTEQLLP FISHLADDGV PNIRFNVAKS YAVIVKVLIK DEAKYDALIK NTILPSLQTL FQDEDVDVKY FAKKSLAECQ ELLKN // ID 2AAB_ARATH Reviewed; 587 AA. AC Q38950; Q9LRZ9; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 2. DT 28-NOV-2006, entry version 39. DE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A DE beta isoform (PP2A, subunit A, beta isoform) (AtA beta). GN Name=PP2AA2; Synonyms=DF1; OrderedLocusNames=At3g25800; GN ORFNames=K13N2.14; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf; RX MEDLINE=95111096; PubMed=7811971; RA Slabas A.R., Fordham-Skelton A.P., Fletcher D., Martinez-Rivas J.M., RA Swinhoe R., Croy R.R.D., Evans I.M.; RT "Characterisation of cDNA and genomic clones encoding homologues of RT the 65 kDa regulatory subunit of protein phosphatase 2A in Arabidopsis RT thaliana."; RL Plant Mol. Biol. 26:1125-1138(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20277480; PubMed=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=14973165; DOI=10.1105/tpc.018994; RA Zhou H.-W., Nussbaumer C., Chao Y., DeLong A.; RT "Disparate roles for the regulatory A subunit isoforms in Arabidopsis RT protein phosphatase 2A."; RL Plant Cell 16:709-722(2004). CC -!- FUNCTION: The A subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit. Involved during CC developmental process such as seedling and floral developments. CC Seems to act as a negative regulator of PP2A catalytic activity. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (subunit A), that associates with a CC variety of regulatory subunits such as subunits B (the CC R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) (By CC similarity). CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in roots and CC flowers (at protein level). CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure (By CC similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 14 HEAT 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; X82002; CAA57528.1; -; mRNA. DR EMBL; AB028607; BAA95767.1; -; Genomic_DNA. DR EMBL; BT002488; AAO00848.1; -; mRNA. DR EMBL; BT008356; AAP37715.1; -; mRNA. DR PIR; S51808; S51808. DR UniGene; At.159; -. DR HSSP; P30153; 1B3U. DR GenomeReviews; BA000014_GR; AT3G25800. DR KEGG; ath:At3g25800; -. DR GeneFarm; 5171; -. DR TAIR; At3g25800; -. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 12. DR PROSITE; PS50077; HEAT_REPEAT; 13. KW Repeat. FT CHAIN 1 587 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A beta isoform. FT /FTId=PRO_0000071410. FT REPEAT 2 42 HEAT 1. FT REPEAT 44 80 HEAT 2. FT REPEAT 81 119 HEAT 3. FT REPEAT 158 196 HEAT 4. FT REPEAT 197 235 HEAT 5. FT REPEAT 236 274 HEAT 6. FT REPEAT 275 313 HEAT 7. FT REPEAT 315 352 HEAT 8. FT REPEAT 353 391 HEAT 9. FT REPEAT 393 430 HEAT 10. FT REPEAT 432 469 HEAT 11. FT REPEAT 470 508 HEAT 12. FT REPEAT 509 547 HEAT 13. FT REPEAT 549 586 HEAT 14. FT CONFLICT 319 319 H -> D (in Ref. 1). SQ SEQUENCE 587 AA; 65598 MW; DD754EE7E514CA7F CRC64; MSMIDEPLYP IAVLIDELKN DDIQLRLNSI RRLSTIARAL GEERTRKELI PFLSENNDDD DEVLLAMAEE LGVFIPYVGG VEYAHVLLPP LETLSTVEET CVREKAVESL CRVGSQMRES DLVDHFISLV KRLAAGEWFT ARVSACGVFH IAYPSAPDML KTELRSLYTQ LCQDDMPMVR RAAATNLGKF AATVESAHLK TDVMSMFEDL TQDDQDSVRL LAVEGCAALG KLLEPQDCVQ HILPVIVNFS QDKSWRVRYM VANQLYELCE AVGPEPTRTE LVPAYVRLLR DNEAEVRIAA AGKVTKFCRI LNPEIAIQHI LPCVKELSSD SSQHVRSALA SVIMGMAPVL GKDATIEHLL PIFLSLLKDE FPDVRLNIIS KLDQVNQVIG IDLLSQSLLP AIVELAEDRH WRVRLAIIEY IPLLASQLGV GFFDDKLGAL CMQWLQDKVH SIRDAAANNL KRLAEEFGPE WAMQHIVPQV LEMVNNPHYL YRMTILRAVS LLAPVMGSEI TCSKLLPVVM TASKDRVPNI KFNVAKVLQS LIPIVDQSVV EKTIRPGLVE LSEDPDVDVR FFANQALQSI DNVMMSS // ID 2AAB_HUMAN Reviewed; 601 AA. AC P30154; O75620; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 20-FEB-2007, entry version 66. DE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A DE beta isoform (PP2A, subunit A, PR65-beta isoform) (PP2A, subunit A, DE R1-beta isoform). GN Name=PPP2R1B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=99014242; PubMed=9795170; DOI=10.1016/S0378-1119(98)00350-3; RA Baysal B.E., Farr J.E., Goss J.R., Devlin B., Richard C.W. III; RT "Genomic organization and precise physical location of protein RT phosphatase 2A regulatory subunit A beta isoform gene on chromosome RT band 11q23."; RL Gene 217:107-116(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=21214715; PubMed=11313745; DOI=10.1038/sj/ejhg/5200585; RA Baysal B.E., Willett-Brozick J.E., Taschner P.E.M., Dauwerse J.G., RA Devilee P., Devlin B.; RT "A high-resolution integrated map spanning the SDHD gene at 11q23: a RT 1.1-Mb BAC contig, a partial transcript map and 15 new repeat RT polymorphisms in a tumour-suppressor region."; RL Eur. J. Hum. Genet. 9:121-129(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-601. RX MEDLINE=90241887; PubMed=2159327; DOI=10.1021/bi00465a002; RA Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., RA Merlevede W., Hofsteenge J., Stone S.R.; RT "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A RT have a similar 39 amino acid repeating structure."; RL Biochemistry 29:3166-3173(1990). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-8; SER-65; ASP-90; RP PRO-101; GLU-343; ALA-448; GLY-504 AND ALA-545. RX MEDLINE=98438696; PubMed=9765152; DOI=10.1126/science.282.5387.284; RA Wang S.S., Esplin E.D., Li J.L., Huang L., Gazdar A., Minna J., RA Evans G.A.; RT "Alterations of the PPP2R1B gene in human lung and colon cancer."; RL Science 282:284-287(1998). RN [5] RP INTERACTION WITH IPO9. RX PubMed=12670497; DOI=10.1016/S0006-291X(03)00434-0; RA Lubert E.J., Sarge K.D.; RT "Interaction between protein phosphatase 2A and members of the RT importin beta superfamily."; RL Biochem. Biophys. Res. Commun. 303:908-913(2003). RN [6] RP VARIANT ASP-90. RX PubMed=10597236; DOI=10.1038/sj.onc.1203070; RA Campbell I.G., Manolitsas T.; RT "Absence of PPP2R1B gene alterations in primary ovarian cancers."; RL Oncogene 18:6367-6369(1999). RN [7] RP VARIANTS ALA-15; PRO-365; GLU-498; ILE-499 AND GLY-500. RX MEDLINE=20357135; PubMed=10896920; DOI=10.1136/gut.47.2.268; RA Takagi Y., Futamura M., Yamaguchi K., Aoki S., Takahashi T., Saji S.; RT "Alterations of the PPP2R1B gene located at 11q23 in human colorectal RT cancers."; RL Gut 47:268-271(2000). RN [8] RP VARIANT ASP-90. RX MEDLINE=21992605; PubMed=11996789; DOI=10.1016/S0165-4608(01)00597-0; RA Hemmer S., Wasenius V.M., Haglund C., Zhu Y., Knuutila S., RA Franssila K., Joensuu H.; RT "Alterations in the suppressor gene PPP2R1B in parathyroid RT hyperplasias and adenomas."; RL Cancer Genet. Cytogenet. 134:13-17(2002). CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. Interacts with IPO9. CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- DISEASE: Defects in PPP2R1B might be a cause of some lung and CC colorectal cancers. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT 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; AF083439; AAC63525.1; -; Genomic_DNA. DR EMBL; AF083425; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083426; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083427; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083428; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083429; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083430; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083431; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083432; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083433; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083434; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083435; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083436; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083437; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083438; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF163473; AAG39644.1; -; mRNA. DR EMBL; M65254; AAA59983.1; -; mRNA. DR EMBL; AF087438; AAC69624.1; -; mRNA. DR UniGene; Hs.584790; -. DR HSSP; P30153; 1B3U. DR SMR; P30154; 14-601. DR IntAct; P30154; -. DR Ensembl; ENSG00000137713; Homo sapiens. DR KEGG; hsa:5519; -. DR HGNC; HGNC:9303; PPP2R1B. DR HPA; CAB004034; -. DR MIM; 603113; gene. DR Reactome; REACT_1505.1; Integration of pathways involved in energy metabolism. DR Reactome; REACT_1919.2; Dephosphorylation of pChREBP by PP2A. DR ArrayExpress; P30154; -. DR GermOnline; ENSG00000137713; Homo sapiens. DR RZPD-ProtExp; IOH11362; -. DR RZPD-ProtExp; IOH42140; -. DR RZPD-ProtExp; W0293; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB. DR GO; GO:0005625; C:soluble fraction; ISS:UniProtKB. DR GO; GO:0003823; F:antigen binding; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; ISS:UniProtKB. DR GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB. DR GO; GO:0000188; P:inactivation of MAPK activity; ISS:UniProtKB. DR GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB. DR GO; GO:0042518; P:negative regulation of tyrosine phosphoryla...; ISS:UniProtKB. DR GO; GO:0006470; P:protein amino acid dephosphorylation; ISS:UniProtKB. DR GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB. DR GO; GO:0045595; P:regulation of cell differentiation; ISS:UniProtKB. DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB. DR GO; GO:0000074; P:regulation of progression through cell cycle; ISS:UniProtKB. DR GO; GO:0045449; P:regulation of transcription; ISS:UniProtKB. DR GO; GO:0030111; P:regulation of Wnt receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0010033; P:response to organic substance; ISS:UniProtKB. DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB. DR GO; GO:0019932; P:second-messenger-mediated signaling; ISS:UniProtKB. DR PROSITE; PS50077; HEAT_REPEAT; 12. KW Polymorphism; Repeat. FT CHAIN 1 601 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A beta isoform. FT /FTId=PRO_0000071403. FT REPEAT 20 58 HEAT 1. FT REPEAT 59 96 HEAT 2. FT REPEAT 97 135 HEAT 3. FT REPEAT 136 173 HEAT 4. FT REPEAT 174 212 HEAT 5. FT REPEAT 213 251 HEAT 6. FT REPEAT 252 290 HEAT 7. FT REPEAT 291 333 HEAT 8. FT REPEAT 334 372 HEAT 9. FT REPEAT 373 411 HEAT 10. FT REPEAT 412 450 HEAT 11. FT REPEAT 451 489 HEAT 12. FT REPEAT 490 528 HEAT 13. FT REPEAT 529 567 HEAT 14. FT REPEAT 568 601 HEAT 15. FT VARIANT 8 8 G -> R (in a lung cancer patient). FT /FTId=VAR_022895. FT VARIANT 15 15 G -> A (in a colorectal cancer patient). FT /FTId=VAR_022896. FT VARIANT 65 65 P -> S (in a lung cancer patient). FT /FTId=VAR_022897. FT VARIANT 90 90 G -> D (in a lung cancer patient; FT dbSNP:rs1805076). FT /FTId=VAR_006384. FT VARIANT 101 101 L -> P (in a colon adenocarcinoma). FT /FTId=VAR_022898. FT VARIANT 343 343 K -> E (in a lung cancer patient). FT /FTId=VAR_022899. FT VARIANT 365 365 S -> P (in a colorectal cancer patient). FT /FTId=VAR_022900. FT VARIANT 448 448 V -> A (in a colon adenocarcinoma). FT /FTId=VAR_022901. FT VARIANT 498 498 V -> E (in a colorectal cancer patient). FT /FTId=VAR_022902. FT VARIANT 499 499 L -> I (in a colorectal cancer patient). FT /FTId=VAR_022903. FT VARIANT 500 500 V -> G (in a colorectal cancer patient). FT /FTId=VAR_022904. FT VARIANT 504 504 D -> G (in a lung cancer patient). FT /FTId=VAR_022905. FT VARIANT 545 545 V -> A (in a colon adenocarcinoma). FT /FTId=VAR_022906. FT CONFLICT 27 30 VLID -> EFRP (in Ref. 3). FT CONFLICT 74 74 E -> V (in Ref. 3). FT CONFLICT 178 178 I -> T (in Ref. 1; AAC63525, 2; AAG39644 FT and 3; AAA59983). FT CONFLICT 411 411 Q -> R (in Ref. 3). SQ SEQUENCE 601 AA; 66214 MW; 86AB20D7505210B0 CRC64; MAGASELGTG PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI ALALGVERTR SELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC LLPPLENLAT VEETVVRDKA VESLRQISQE HTPVALEAYF VPLVKRLASG DWFTSRTSAC GLFSVCYPRA SNAVKAEIRQ QFRSLCSDDT PMVRRAAASK LGEFAKVLEL DSVKSEIVPL FTSLASDEQD SVRLLAVEAC VSIAQLLSQD DLETLVMPTL RQAAEDKSWR VRYMVADRFS ELQKAMGPKI TLNDLIPAFQ NLLKDCEAEV RAAAAHKVKE LGENLPIEDR ETIIMNQILP YIKELVSDTN QHVKSALASV IMGLSTILGK ENTIEHLLPL FLAQLKDECP DVRLNIISNL DCVNEVIGIR QLSQSLLPAI VELAEDAKWR VRLAIIEYMP LLAGQLGVEF FDEKLNSLCM AWLVDHVYAI REAATNNLMK LVQKFGTEWA QNTIVPKVLV MANDPNYLHR MTTLFCINAL SEACGQEITT KQMLPIVLKM AGDQVANVRF NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL A // ID 2AAB_MOUSE Reviewed; 601 AA. AC Q7TNP2; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 20-FEB-2007, entry version 27. DE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A DE beta isoform (PP2A, subunit A, PR65-beta isoform) (PP2A, subunit A, DE R1-beta isoform). GN Name=Ppp2r1b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] 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 -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. Interacts with IPO9 (By similarity). CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT 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; BC056218; AAH56218.1; -; mRNA. DR UniGene; Mm.7726; -. DR HSSP; P30153; 1B3U. DR SMR; Q7TNP2; 14-601. DR Ensembl; ENSMUSG00000032058; Mus musculus. DR MGI; MGI:1920949; Ppp2r1b. DR ArrayExpress; Q7TNP2; -. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 11. DR PROSITE; PS50077; HEAT_REPEAT; 12. KW Repeat. FT CHAIN 1 601 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A beta isoform. FT /FTId=PRO_0000071404. FT REPEAT 20 58 HEAT 1. FT REPEAT 59 96 HEAT 2. FT REPEAT 97 135 HEAT 3. FT REPEAT 136 173 HEAT 4. FT REPEAT 174 212 HEAT 5. FT REPEAT 213 251 HEAT 6. FT REPEAT 252 290 HEAT 7. FT REPEAT 291 333 HEAT 8. FT REPEAT 334 372 HEAT 9. FT REPEAT 373 411 HEAT 10. FT REPEAT 412 450 HEAT 11. FT REPEAT 451 489 HEAT 12. FT REPEAT 490 528 HEAT 13. FT REPEAT 529 567 HEAT 14. FT REPEAT 568 601 HEAT 15. SQ SEQUENCE 601 AA; 65949 MW; 1ED17643006AFBD1 CRC64; MAGAAGPGSG PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI ALALGVERTR TELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC LLPPLESLAT VEETVVRDKA VESLRQISQE HTPVALEAHF VPLVKRLASG DWFMSRTSAC GLFSVCYPRA SNAVKAEIRQ HFRSLCSDDT PMERRAAASK LGEFAKVLEL DSVKTEIVPL FTNLASDEQD SVRLLAVEAC VSIAQLLSQE DLEALVIPTL RQAAEDKSWR VRYMVADKFS ELQKAVGPKI ALSDLIPAFQ SLLRDCEAEV RAAAAHKVRE LCENLPAEGR ETVIMNQILP YIKELVSDTS QHVKSALASV IMGLSTVLGK ENTIEHLLPL FLAQLKDECP EVRLNIISNL DCVNEVIGIR QLSQSLLPAI VELAEDAKWR VRLAIIEYMP LLAGQLGVEF FDEKLNSLCM AWLVDHVYAI REAATNNLMK LVQKFGTEWA QNTIVPKVLV MANDPNYLHR MTTLFCINAL SEACGKEITT KQMLPIVLKM AGDQVANVRF NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL A // ID 2AAB_PIG Reviewed; 602 AA. AC P54613; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 40. DE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A DE beta isoform (PP2A, subunit A, PR65-beta isoform) (PP2A, subunit A, DE R1-beta isoform) (Fragment). GN Name=PPP2R1B; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Mayer-Jaekel R.E.; RL Thesis (1992), Friedrich Miescher Institut / Basel, Switzerland. CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit. CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which CC consist of a core composed of a catalytic subunit associated with CC a 65 kDa regulatory subunit (PR65) (subunit A). The core complex CC associates with a third, variable subunit (subunit B), which CC confers distinct properties to the holoenzyme. Interacts with IPO9 CC (By similarity). CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT 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; Z34931; CAA84403.1; -; mRNA. DR PIR; D34541; D34541. DR UniGene; Ssc.731; -. DR HSSP; P30153; 1B3U. DR SMR; P54613; 15-602. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB. DR GO; GO:0005625; C:soluble fraction; ISS:UniProtKB. DR GO; GO:0003823; F:antigen binding; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; ISS:UniProtKB. DR GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB. DR GO; GO:0000188; P:inactivation of MAPK activity; ISS:UniProtKB. DR GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB. DR GO; GO:0042518; P:negative regulation of tyrosine phosphoryla...; ISS:UniProtKB. DR GO; GO:0006470; P:protein amino acid dephosphorylation; ISS:UniProtKB. DR GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB. DR GO; GO:0045595; P:regulation of cell differentiation; ISS:UniProtKB. DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB. DR GO; GO:0000074; P:regulation of progression through cell cycle; ISS:UniProtKB. DR GO; GO:0045449; P:regulation of transcription; ISS:UniProtKB. DR GO; GO:0030111; P:regulation of Wnt receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0010033; P:response to organic substance; ISS:UniProtKB. DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB. DR GO; GO:0019932; P:second-messenger-mediated signaling; ISS:UniProtKB. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 11. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW Repeat. FT CHAIN <1 602 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A beta isoform. FT /FTId=PRO_0000071405. FT REPEAT 21 59 HEAT 1. FT REPEAT 60 97 HEAT 2. FT REPEAT 98 136 HEAT 3. FT REPEAT 137 174 HEAT 4. FT REPEAT 175 213 HEAT 5. FT REPEAT 214 252 HEAT 6. FT REPEAT 253 291 HEAT 7. FT REPEAT 292 334 HEAT 8. FT REPEAT 335 373 HEAT 9. FT REPEAT 374 412 HEAT 10. FT REPEAT 413 451 HEAT 11. FT REPEAT 452 490 HEAT 12. FT REPEAT 491 529 HEAT 13. FT REPEAT 530 568 HEAT 14. FT REPEAT 569 602 HEAT 15. FT NON_TER 1 1 SQ SEQUENCE 602 AA; 66214 MW; D71EAD46C2B7BB03 CRC64; NSAGAAAPGT GPVAAGGDGD DSLYPIAVLI DELRNEDVQL RLNSIKKLST IALALGVERT RTELLPFLTD TIYDEDEVLL ALAEQLGNFT GLVGGPDFAH CLLPPLESLA TVEETVVRDK AVESLRQISQ EHTPVALEAH FVPLVKRLAS GDWFTSRTSA CGLFSVCYPR ASNAVKAEIR QHFRSLCSDD TPMVRRAAAS KLGEFAKVLE LDSVKSEIVP LFTNLASDEQ DSVRLLAVEA CVSIAQLLSQ DDLEALVMPT LRQAAEDKSW RVRYMVADKF SELQRAVGPK ITLNDLIPAF QNLLKDCEAE VRAAAAHKVK ELCENLPIEG RETIIMNQIL PCIKELVSDT NQHVKSALAS VIMGLSTILG KENTIEHLLP LFLAQLKDEC PEVRLNIISN LDCVNEVIGI RQLSQSLLPA IVELAEDAKW RVRLAIIEYM PLLAGQLGVE FFDEKLNSLC MAWLVDHVYA IREAATNNLM KLVQKFGTEW AQNTIVPKVL VMANDPNYLH RMTTLFCINV LSEACGQEIT TKQMLPIVLK MAGDQVANVR FNVAKSLQKI GPILDTDALQ EEVKPVLQKL GQDEDMDVKY FAQEAISVLA LA // ID 2AAB_RAT Reviewed; 601 AA. AC Q4QQT4; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 28-NOV-2006, entry version 13. DE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A DE beta isoform (PP2A, subunit A, PR65-beta isoform) (PP2A, subunit A, DE R1-beta isoform). GN Name=Ppp2r1b; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] 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 PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. Interacts with IPO9 (By similarity). CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT 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; BC098007; AAH98007.1; -; mRNA. DR UniGene; Rn.163017; -. DR SMR; Q4QQT4; 14-601. DR RGD; 1304764; Ppp2r1b. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 11. DR PROSITE; PS50077; HEAT_REPEAT; 12. KW Repeat. FT CHAIN 1 601 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A beta isoform. FT /FTId=PRO_0000071406. FT REPEAT 20 58 HEAT 1. FT REPEAT 59 96 HEAT 2. FT REPEAT 97 135 HEAT 3. FT REPEAT 136 173 HEAT 4. FT REPEAT 174 212 HEAT 5. FT REPEAT 213 251 HEAT 6. FT REPEAT 252 290 HEAT 7. FT REPEAT 291 333 HEAT 8. FT REPEAT 334 372 HEAT 9. FT REPEAT 373 411 HEAT 10. FT REPEAT 412 450 HEAT 11. FT REPEAT 451 489 HEAT 12. FT REPEAT 490 528 HEAT 13. FT REPEAT 529 567 HEAT 14. FT REPEAT 568 601 HEAT 15. SQ SEQUENCE 601 AA; 66006 MW; DA2A0BA19FC5A46D CRC64; MAGAAGPGTV PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI ALALGVERTR TELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC LLPPLESLAT VEETVVRDKA VESLRQISQE HTPVALEAHF VPLVKRLASG DWFTSRTSAC GLFSVCYPRA SNAVKAEIRQ HFRSLCSDDT PMVRRAAASK LGEFAKVLEL DSVKTEIVPL FTNLASDEQD SVRLLAVEAC VSIAQLLSQD DLEALVMPTL RQAAEDKSWR VRYMVADKFS ELQKAVGPKI ALSDLIPAFQ SLLRDCEAEV RAAAAHKVRE LCENLPTEGR ETVIMNQILP YIKELVSDTN QHVKSALASV IMGLSTVLGK ENTIEHLLPL FLAQLKDECP EVRLNIISNL DCVNEVIGIR QLSQSLLPAI VELAEDAKWR VRLAIIEYMP LLAGQLGVEF FDEKLNSLCM AWLVDHVYAI REAATNNLMK LVQKFGTEWA QNTIVPKVLV MANDPNYLHR MTTLFCINAL SEACGKEITT KQMLPIVLKM AGDQVANVRF NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL A // ID 2AAG_ARATH Reviewed; 587 AA. AC Q38951; Q8LPH9; Q9FX65; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 2. DT 28-NOV-2006, entry version 37. DE Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A DE gamma isoform (PP2A, subunit A, gamma isoform) (AtA gamma). GN Name=PP2AA3; Synonyms=DF2; OrderedLocusNames=At1g13320; GN ORFNames=T6J4.8; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-587. RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf; RX MEDLINE=95111096; PubMed=7811971; RA Slabas A.R., Fordham-Skelton A.P., Fletcher D., Martinez-Rivas J.M., RA Swinhoe R., Croy R.R.D., Evans I.M.; RT "Characterisation of cDNA and genomic clones encoding homologues of RT the 65 kDa regulatory subunit of protein phosphatase 2A in Arabidopsis RT thaliana."; RL Plant Mol. Biol. 26:1125-1138(1994). RN [4] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=14973165; DOI=10.1105/tpc.018994; RA Zhou H.-W., Nussbaumer C., Chao Y., DeLong A.; RT "Disparate roles for the regulatory A subunit isoforms in Arabidopsis RT protein phosphatase 2A."; RL Plant Cell 16:709-722(2004). RN [5] RP TISSUE SPECIFICITY. RX PubMed=16166256; DOI=10.1104/pp.105.063743; RA Czechowski T., Stitt M., Altmann T., Udvardi M.K., Scheible W.R.; RT "Genome-wide identification and testing of superior reference genes RT for transcript normalization in Arabidopsis."; RL Plant Physiol. 139:5-17(2005). CC -!- FUNCTION: The A subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit. Involved during CC developmental process such as seedling and floral developments. CC Seems to act as a negative regulator of PP2A catalytic activity. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (subunit A), that associates with a CC variety of regulatory subunits such as subunits B (the CC R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed ubiquitously at stable levels. CC However, higher protein levels in roots and flowers (at protein CC level). CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure (By CC similarity). CC -!- MISCELLANEOUS: Due to the stability of its transcription, Ref.5 CC proposed this gene as a reference gene for transcript CC normalization. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 14 HEAT repeats. CC -!- CAUTION: Ref.1 sequence differs from that shown due to erroneous CC 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; AC011810; AAG09551.1; ALT_SEQ; Genomic_DNA. DR EMBL; AY099760; AAM20611.1; -; mRNA. DR EMBL; BT002601; AAO00961.1; -; mRNA. DR EMBL; X82003; CAA57529.1; -; mRNA. DR PIR; H86267; H86267. DR PIR; S51809; S51809. DR UniGene; At.16123; -. DR HSSP; P30153; 1B3U. DR GenomeReviews; CT485782_GR; AT1G13320. DR KEGG; ath:At1g13320; -. DR TAIR; At1g13320; -. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 12. DR PROSITE; PS50077; HEAT_REPEAT; 12. KW Repeat. FT CHAIN 1 587 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A gamma FT isoform. FT /FTId=PRO_0000071411. FT REPEAT 2 42 HEAT 1. FT REPEAT 44 80 HEAT 2. FT REPEAT 81 119 HEAT 3. FT REPEAT 158 194 HEAT 4. FT REPEAT 197 235 HEAT 5. FT REPEAT 236 274 HEAT 6. FT REPEAT 276 313 HEAT 7. FT REPEAT 314 352 HEAT 8. FT REPEAT 353 391 HEAT 9. FT REPEAT 393 430 HEAT 10. FT REPEAT 432 469 HEAT 11. FT REPEAT 470 508 HEAT 12. FT REPEAT 509 547 HEAT 13. FT REPEAT 549 586 HEAT 14. FT CONFLICT 290 290 C -> R (in Ref. 3). SQ SEQUENCE 587 AA; 65517 MW; 741159FDEB9589B9 CRC64; MSMVDEPLYP IAVLIDELKN DDIQRRLNSI KRLSIIARAL GEERTRKELI PFLSENNDDD DEVLLAMAEE LGGFILYVGG VEYAYVLLPP LETLSTVEET CVREKAVDSL CRIGAQMRES DLVEHFTPLA KRLSAGEWFT ARVSACGIFH IAYPSAPDVL KTELRSIYGQ LCQDDMPMVR RAAATNLGKF AATIESAHLK TDIMSMFEDL TQDDQDSVRL LAVEGCAALG KLLEPQDCVA HILPVIVNFS QDKSWRVRYM VANQLYELCE AVGPEPTRTD LVPAYARLLC DNEAEVRIAA AGKVTKFCRI LNPELAIQHI LPCVKELSSD SSQHVRSALA SVIMGMAPVL GKDATIEHLL PIFLSLLKDE FPDVRLNIIS KLDQVNQVIG IDLLSQSLLP AIVELAEDRH WRVRLAIIEY IPLLASQLGV GFFDEKLGAL CMQWLQDKVH SIREAAANNL KRLAEEFGPE WAMQHIVPQV LEMINNPHYL YRMTILRAVS LLAPVMGSEI TCSKLLPAVI TASKDRVPNI KFNVAKMMQS LIPIVDQAVV ENMIRPCLVE LSEDPDVDVR YFANQALQSI DNVMMSS // ID 2ABA_ARATH Reviewed; 513 AA. AC Q38821; Q8L842; Q9C8H8; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 2. DT 31-OCT-2006, entry version 44. DE Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B DE alpha isoform (PP2A, subunit B, alpha isoform) (AtB alpha). GN Name=PP2AB1; OrderedLocusNames=At1g51690; ORFNames=F19C24.10; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX MEDLINE=95322588; PubMed=7599311; RA Rundle S.J., Hartung A.J., Corum J.W. III, O'Neill M.; RT "Characterization of a cDNA encoding the 55 kDa B regulatory subunit RT of Arabidopsis protein phosphatase 2A."; RL Plant Mol. Biol. 28:257-266(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families) (By similarity). CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 6 WD repeats. CC -!- CAUTION: Ref.2 sequence differs from that shown due to erroneous CC 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; U18129; AAA86695.1; -; mRNA. DR EMBL; AC025294; AAG50878.1; ALT_SEQ; Genomic_DNA. DR EMBL; AY120756; AAM53314.1; -; mRNA. DR EMBL; BT000109; AAN15428.1; -; mRNA. DR PIR; G96555; G96555. DR PIR; S55889; S55889. DR UniGene; At.1589; -. DR GenomeReviews; CT485782_GR; AT1G51690. DR KEGG; ath:At1g51690; -. DR GeneFarm; 3008; 267. DR TAIR; At1g51690; -. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 5. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 513 Serine/threonine protein phosphatase 2A FT 55 kDa regulatory subunit B alpha FT isoform. FT /FTId=PRO_0000071438. FT REPEAT 36 75 WD 1. FT REPEAT 112 153 WD 2. FT REPEAT 232 270 WD 3. FT REPEAT 281 321 WD 4. FT REPEAT 340 378 WD 5. FT REPEAT 483 513 WD 6. FT CONFLICT 165 165 G -> R (in Ref. 1). SQ SEQUENCE 513 AA; 56935 MW; 2AF84BE214172D19 CRC64; MNGGDEVVAA SADPSLPLEW RFSQVFGERS AGEEVQEVDI ISAIEFDNSG NHLATGDRGG RVVLFERTDT NNSSGTRREL EEADYPLRHP EFRYKTEFQS HDPEFDYLKS LEIEEKINKI RWCQTANGAL FLLSTNDKTI KFWKVQDKKI KKICDMNSDP SRTVGNGTVA SSSNSNITNS CLVNGGVSEV NNSLCNDFSL PAGGISSLRL PVVVTSHESS PVARCRRVYA HAHDYHINSI SNNSDGETFI SADDLRINLW NLEISNQSFN IVDVKPAKME DLSEVITSAE FHPTHCNMLA YSSSKGSIRL IDLRQSALCD SHSKLFEEPE QAGPKSFFTE IIASVSDIKF AKEGRYLLSR DYMTLKLWDI NMDAGPVATF QVHEYLKPKL CDLYENDSIF DKFECCISGN GLRAATGSYS NLFRVFGVAP GSTETATLEA SRNPMRRHVP IPSRPSRALS SITRVVSRGS ESPGVDGNTN ALDYTTKLLH LAWHPNENSI ACAAANSLYM YYA // ID 2ABA_CANTR Reviewed; 508 AA. AC P53031; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 31-OCT-2006, entry version 38. DE Protein phosphatase PP2A regulatory subunit B (PR55) (Cell division DE control protein 55). GN Name=CDC55; OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5482; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NCYC 2512; RX MEDLINE=97082501; PubMed=8923737; RX DOI=10.1002/(SICI)1097-0061(199610)12:13<1321::AID-YEA27>3.0.CO;2-6; RA Rodriguez P.L., Ali R., Serrano R.; RT "CtCdc55p and CtHa13p: two putative regulatory proteins from Candida RT tropicalis with long acidic domains."; RL Yeast 12:1321-1329(1996). CC -!- FUNCTION: Phosphatase 2A affects a variety of biological processes CC in the cell such as transcription, cell cycle progression and CC cellular morphogenesis, and provides an initial identification of CC critical substrates for this phosphatase. The regulatory subunit CC may direct the catalytic subunit to distinct, albeit overlapping, CC subsets of substrates (By similarity). CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which CC consist of a core composed of a catalytic subunit associated with CC a 65 kDa (PR65) (Subunit A) and a 55 kDa (PR55) (Subunit B) CC regulatory subunit. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; X88899; CAA61361.1; -; Genomic_DNA. DR PIR; S57751; S57751. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 2. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Cell cycle; Repeat; WD repeat. FT CHAIN 1 508 Protein phosphatase PP2A regulatory FT subunit B. FT /FTId=PRO_0000071440. FT REPEAT 19 58 WD 1. FT REPEAT 81 122 WD 2. FT REPEAT 166 204 WD 3. FT REPEAT 215 255 WD 4. FT REPEAT 274 312 WD 5. FT REPEAT 329 370 WD 6. FT REPEAT 477 507 WD 7. FT COMPBIAS 396 407 Poly-Asp. SQ SEQUENCE 508 AA; 57914 MW; 619B4C78BBC7A324 CRC64; MNLDFSQCFG DKGDIENITE ADIISTVEFD HTGDFLATGD KGGRVVLFER NQSKKKQSCE YKFFTEFQSH DAEFDYLKSL EIEEKINKIK WLKSANDSLC LLSTNDKTIK LWKIQERQIK LVSENNLNGL NHLPSSNIGI ESLKLPQLQL HDKLISAQPK KIYANAHAYH INSISVNSDQ ETYLSADDLR INLWNLGIAD QSFNIVDIKP ANMEELTEVI TSAEFHPLQC NLFMYSSSKG TIKLSDMRSN SLCDSHAKIF EEYLDPSSHN FFTEITSSIS DVKFSHDGRY IASRDYMTVK IWDLAMENKP IKTIDVHEHL RERLCDTYEN DAIFDKFEVQ FGGDNKSVMT GSYNNQFVIY PNAVNTGNDD KPKFKSAFKN SSKRSKKNGF STRTTDDDDD DDDDDDDEEA DDEFDEEVPA TKNSPGSQLE DDDEQEEIIL QADKSAFKSK KSGQHPMRRR MTSGVGSNLG REFDDVDFKK SILHLSWHPR ENSVAIAATN NLYIFSTL // ID 2ABA_DROME Reviewed; 499 AA. AC P36872; Q9VH21; Q9VH22; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 20-FEB-2007, entry version 73. DE Protein phosphatase PP2A 55 kDa regulatory subunit (Protein DE phosphatase PP2A regulatory subunit B) (PR55) (Twins protein). GN Name=tws; Synonyms=aar, Pp2A-85F; ORFNames=CG6235; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING. RX MEDLINE=93177843; PubMed=8382567; DOI=10.1016/0092-8674(93)90080-A; RA Mayer-Jaekel R.E., Ohkura H., Gomes R., Sunkel C.E., Baumgartner S., RA Hemmings B.A., Glover D.M.; RT "The 55 kd regulatory subunit of Drosophila protein phosphatase 2A is RT required for anaphase."; RL Cell 72:621-633(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). RC STRAIN=Oregon-R; TISSUE=Eye imaginal disk; RX MEDLINE=93194062; PubMed=8383623; RA Uemura T., Shiomi K., Togashi S., Takeichi M.; RT "Mutation of twins encoding a regulator of protein phosphatase 2A RT leads to pattern duplication in Drosophila imaginal discs."; RL Genes Dev. 7:429-440(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: Could perform a substrate recognition function or could CC be responsible for targeting the enzyme complex to the appropriate CC subcellular compartment. CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which CC consist of a core composed of a catalytic subunit associated with CC a 65 kDa regulatory subunit (PR65) (subunit A). The core complex CC associates with a third, variable subunit (subunit B), which CC confers distinct properties to the holoenzyme. CC -!- INTERACTION: CC Q9V4Z9:lin; NbExp=1; IntAct=EBI-215615, EBI-126412; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=F; CC IsoId=P36872-1; Sequence=Displayed; CC Name=B; Synonyms=C; CC IsoId=P36872-2; Sequence=VSP_005105, VSP_005106; CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD repeats. CC -!- CAUTION: It is uncertain whether Met-1, Met-18, Met-33 or Met-44 CC 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; D13004; BAA02367.1; -; mRNA. DR EMBL; L07581; AAA99870.1; -; mRNA. DR EMBL; L07583; AAA99871.1; -; mRNA. DR EMBL; L07585; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L07586; AAB00371.1; -; Genomic_DNA. DR EMBL; L12544; AAB00371.1; JOINED; Genomic_DNA. DR EMBL; L07586; AAB00372.1; -; Genomic_DNA. DR EMBL; L12544; AAB00372.1; JOINED; Genomic_DNA. DR EMBL; AE014297; AAF54498.1; -; Genomic_DNA. DR EMBL; AE014297; AAF54499.3; -; Genomic_DNA. DR EMBL; AY061152; AAL28700.1; -; mRNA. DR PIR; A45778; A45778. DR UniGene; Dm.3826; -. DR DIP; DIP:19897N; -. DR IntAct; P36872; -. DR Ensembl; CG6235; Drosophila melanogaster. DR KEGG; dme:Dmel_CG6235; -. DR FlyBase; FBgn0004889; tws. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-010875-MONOMER; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-010876-MONOMER; -. DR GermOnline; CG6235; Drosophila melanogaster. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0000158; F:protein phosphatase type 2A activity; IDA:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; ISS:UniProtKB. DR GO; GO:0001700; P:embryonic development (sensu Insecta); IMP:FlyBase. DR GO; GO:0007447; P:imaginal disc pattern formation; IMP:UniProtKB. DR GO; GO:0000090; P:mitotic anaphase; IMP:FlyBase. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA:UniProtKB. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase tr...; IMP:UniProtKB. DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase. DR GO; GO:0016055; P:Wnt receptor signaling pathway; IGI:FlyBase. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 7. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Alternative splicing; Complete proteome; Repeat; WD repeat. FT CHAIN 1 499 Protein phosphatase PP2A 55 kDa FT regulatory subunit. FT /FTId=PRO_0000071437. FT REPEAT 79 118 WD 1. FT REPEAT 144 185 WD 2. FT REPEAT 228 266 WD 3. FT REPEAT 277 317 WD 4. FT REPEAT 336 374 WD 5. FT REPEAT 391 432 WD 6. FT REPEAT 467 498 WD 7. FT VAR_SEQ 1 56 Missing (in isoform B). FT /FTId=VSP_005105. FT VAR_SEQ 57 59 PAS -> MAG (in isoform B). FT /FTId=VSP_005106. FT CONFLICT 211 211 K -> M (in Ref. 1; AAA99871). SQ SEQUENCE 499 AA; 56967 MW; D871A7E3058B7286 CRC64; MGRWGRQSPV LEPPDPQMQT TPPPPTLPPR TFMRQSSITK IGNMLNTAIN INGAKKPASN GEASWCFSQI KGALDDDVTD ADIISCVEFN HDGELLATGD KGGRVVIFQR DPASKAANPR RGEYNVYSTF QSHEPEFDYL KSLEIEEKIN KIRWLQQKNP VHFLLSTNDK TVKLWKVSER DKSFGGYNTK EENGLIRDPQ NVTALRVPSV KQIPLLVEAS PRRTFANAHT YHINSISVNS DQETFLSADD LRINLWHLEV VNQSYNIVDI KPTNMEELTE VITAAEFHPT ECNVFVYSSS KGTIRLCDMR SAALCDRHSK QFEEPENPTN RSFFSEIISS ISDVKLSNSG RYMISRDYLS IKVWDLHMET KPIETYPVHE YLRAKLCSLY ENDCIFDKFE CCWNGKDSSI MTGSYNNFFR VFDRNSKKDV TLEASRDIIK PKTVLKPRKV CTGGKRKKDE ISVDCLDFNK KILHTAWHPE ENIIAVAATN NLFIFQDKF // ID 2ABA_HUMAN Reviewed; 447 AA. AC P63151; P50409; Q00007; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2004, sequence version 1. DT 20-FEB-2007, entry version 29. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE alpha isoform (PP2A, subunit B, B-alpha isoform) (PP2A, subunit B, DE B55-alpha isoform) (PP2A, subunit B, PR55-alpha isoform) (PP2A, DE subunit B, R2-alpha isoform). GN Name=PPP2R2A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Lung fibroblast; RX MEDLINE=91198016; PubMed=1849734; DOI=10.1021/bi00229a001; RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J., RA Merlevede W., Hofsteenge J., Hemmings B.A.; RT "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: RT evidence for a neuronal-specific isoform."; RL Biochemistry 30:3589-3597(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Blood; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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 B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- TISSUE SPECIFICITY: In all tissues examined. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; M64929; AAA36490.1; -; mRNA. DR EMBL; BC041071; AAH41071.1; -; mRNA. DR PIR; A38351; A38351. DR UniGene; Hs.146339; -. DR IntAct; P63151; -. DR REPRODUCTION-2DPAGE; P63151; HUMAN. DR Ensembl; ENSG00000104762; Homo sapiens. DR HGNC; HGNC:9304; PPP2R2A. DR MIM; 604941; gene. DR LinkHub; P63151; -. DR ArrayExpress; P63151; -. DR GermOnline; ENSG00000147459; Homo sapiens. DR RZPD-ProtExp; C0310; -. DR RZPD-ProtExp; W2328; -. DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0000158; F:protein phosphatase type 2A activity; IDA:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:UniProtKB. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA:UniProtKB. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 7. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 447 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B alpha FT isoform. FT /FTId=PRO_0000071415. FT REPEAT 26 65 WD 1. FT REPEAT 91 132 WD 2. FT REPEAT 175 213 WD 3. FT REPEAT 224 264 WD 4. FT REPEAT 283 321 WD 5. FT REPEAT 338 379 WD 6. FT REPEAT 414 446 WD 7. SQ SEQUENCE 447 AA; 51692 MW; F4D407FF7ADA4ED6 CRC64; MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL HTAWHPKENI IAVATTNNLY IFQDKVN // ID 2ABA_MACFA Reviewed; 447 AA. AC Q4R7Z4; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 31-OCT-2006, entry version 11. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE alpha isoform (PP2A, subunit B, B-alpha isoform) (PP2A, subunit B, DE B55-alpha isoform) (PP2A, subunit B, PR55-alpha isoform) (PP2A, DE subunit B, R2-alpha isoform). GN Name=PPP2R2A; ORFNames=QtsA-14009; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; AB168667; BAE00778.1; -; mRNA. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 7. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 447 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B alpha FT isoform. FT /FTId=PRO_0000071416. FT REPEAT 26 65 WD 1. FT REPEAT 91 132 WD 2. FT REPEAT 175 213 WD 3. FT REPEAT 224 264 WD 4. FT REPEAT 283 321 WD 5. FT REPEAT 338 379 WD 6. FT REPEAT 414 446 WD 7. SQ SEQUENCE 447 AA; 51692 MW; F4D407FF7ADA4ED6 CRC64; MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL HTAWHPKENI IAVATTNNLY IFQDKVN // ID 2ABA_MOUSE Reviewed; 447 AA. AC Q6P1F6; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 27. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE alpha isoform (PP2A, subunit B, B-alpha isoform) (PP2A, subunit B, DE B55-alpha isoform) (PP2A, subunit B, PR55-alpha isoform) (PP2A, DE subunit B, R2-alpha isoform). GN Name=Ppp2r2a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6, and C57BL/6J; TISSUE=Brain, and 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: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; BC065100; AAH65100.1; -; mRNA. DR EMBL; BC080692; AAH80692.1; -; mRNA. DR UniGene; Mm.273997; -. DR MGI; MGI:1919228; Ppp2r2a. DR ArrayExpress; Q6P1F6; -. DR GermOnline; ENSMUSG00000022052; Mus musculus. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 7. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 447 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B alpha FT isoform. FT /FTId=PRO_0000071417. FT REPEAT 26 65 WD 1. FT REPEAT 91 132 WD 2. FT REPEAT 175 213 WD 3. FT REPEAT 224 264 WD 4. FT REPEAT 283 321 WD 5. FT REPEAT 338 379 WD 6. FT REPEAT 414 446 WD 7. SQ SEQUENCE 447 AA; 51692 MW; F4D407FF7ADA4ED6 CRC64; MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL HTAWHPKENI IAVATTNNLY IFQDKVN // ID 2ABA_ORYSA Reviewed; 581 AA. AC Q5Z8Z7; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 2. DT 28-NOV-2006, entry version 18. DE Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B DE alpha isoform (PP2A, subunit B, alpha isoform). GN OrderedLocusNames=Os06g0563300, LOC_Os06g36770; ORFNames=P0656E03.30; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RG The international rice genome sequencing project (IRGSP) consortium; RT "Oryza sativa nipponbare chromosome 6 genomic DNA sequence."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=22752273; PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families) (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 6 WD repeats. CC -!- CAUTION: Ref.1 sequence differs from that shown due to erroneous CC 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; AP003714; BAD53757.1; ALT_SEQ; Genomic_DNA. DR EMBL; AK111494; -; NOT_ANNOTATED_CDS; mRNA. DR Gramene; Q5Z8Z7; -. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 581 Serine/threonine protein phosphatase 2A FT 55 kDa regulatory subunit B alpha FT isoform. FT /FTId=PRO_0000247272. FT REPEAT 47 86 WD 1. FT REPEAT 123 164 WD 2. FT REPEAT 241 279 WD 3. FT REPEAT 290 330 WD 4. FT REPEAT 349 387 WD 5. FT REPEAT 492 530 WD 6. FT CONFLICT 422 422 H -> Q (in Ref. 2). FT CONFLICT 551 551 M -> L (in Ref. 2). SQ SEQUENCE 581 AA; 64752 MW; 0E8BB1DA93211BBF CRC64; MMNPDGGDGD RLEAAGAGSS SAQQGHPTME WRFAQVFGER AAGEDVQEVD IISAIEFDKS GDHLATGDRG GRVVLFERTD ARDNASRREM ERQDAPITRH PEFRYKSEFQ SHEPEFDYLK SLEIEEKINK IRWCQTANNS LSLLSTNDKT IKYWKVQEKK VKQVSVMNLD SRSVGTGTSS SASTSSSRGL LPNGGCSDKS SFLNSDILFP PGGYPSLRLP VVVASQDVNL VARCRRVYAH AHDYHINSIS TNSDGETYIS ADDLRINLWN LEINNQSFNI VDVKPPNMED LTEVITCAEF HPTHCNTLAY SSSKGSIRLI DLRQSALCDN HSKIFEEHEA PGSRSFFTEI IASISDIKFS RDGRYILSRD YMTLKLWDLN MDSGPVSTFQ VHEHLRPKLC DLYENDSIFD KFECCLSGDG LHVATGSYGN LFRVFGCTPG STEATTLEAS RNPMRRQIVN PTRPTRTLTS LARGVRRGGE NQGVDANGNS FDFSTKLLHL AWHPTENSIA CAAANSLYMY YARRCLRKFI VFGSLLEAAC LHMQPEIWCR MLSSIPPLGP KEAVDAHKMA FVAVTASLLI L // ID 2ABA_PIG Reviewed; 426 AA. AC Q29090; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 42. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE alpha isoform (PP2A, subunit B, B-alpha isoform) (PP2A, subunit B, DE B55-alpha isoform) (PP2A, subunit B, PR55-alpha isoform) (PP2A, DE subunit B, R2-alpha isoform) (Fragment). GN Name=PPP2R2A; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Mayer-Jaekel R.E.; RL Thesis (1992), Friedrich Miescher Institut / Basel, Switzerland. CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; Z34932; CAA84404.1; -; mRNA. DR UniGene; Ssc.104; -. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 7. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN <1 426 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B alpha FT isoform. FT /FTId=PRO_0000071418. FT REPEAT 5 44 WD 1. FT REPEAT 70 111 WD 2. FT REPEAT 154 192 WD 3. FT REPEAT 203 243 WD 4. FT REPEAT 262 300 WD 5. FT REPEAT 317 358 WD 6. FT REPEAT 393 425 WD 7. FT NON_TER 1 1 SQ SEQUENCE 426 AA; 49614 MW; 3AAD7EB338B03534 CRC64; DDDVAEADII STVEFNHSGE LLATGDKGGR VVIFQQEQEN KIQSHSRGEY NVYSTFQSHE PEFDYLKSLE IEEKINKIRW LPQKNAAQFL LSTNDKTIKL WKISERDKRP EGYNLKEEDG RYRDPTTVTT LRVPVFRPMD LMVEASPRRI FANAHTYHIN SISINSDYET YLSADDLRIN LWHLEITDRS FNIVDIKPAN MEELTEVITA AEFHPNSCNT FVYSSSKGTI RLCDMRASAL CDRHSKLFEE PEDPSNRSFF SEIISSISDV KFSHSGRYMM TRDYLSVKIW DLNMENRPVE TYQVHEYLRS KLCSLYENDC IFDKFECCWN GSDSVVMTGS YNNFFRMFDR NTKRDITLEA SRENNKPRTV LKPRKVCASG KRKKDEISVD SLDFNKKILH TAWHPKENII AVATTNNLYI FQDKVN // ID 2ABA_RABIT Reviewed; 447 AA. AC P63150; P50409; Q00007; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2004, sequence version 1. DT 31-OCT-2006, entry version 17. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE alpha isoform (PP2A, subunit B, B-alpha isoform) (PP2A, subunit B, DE B55-alpha isoform) (PP2A, subunit B, PR55-alpha isoform) (PP2A, DE subunit B, R2-alpha isoform). GN Name=PPP2R2A; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=New Zealand white; TISSUE=Skeletal muscle; RA Depaoli-Roach A.A.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; U09356; AAA18497.1; -; mRNA. DR KEGG; hsa:5520; -. DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB. DR GO; GO:0005515; F:protein binding; ISS:UniProtKB. DR GO; GO:0000158; F:protein phosphatase type 2A activity; ISS:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; ISS:UniProtKB. DR GO; GO:0006470; P:protein amino acid dephosphorylation; ISS:UniProtKB. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 7. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 447 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B alpha FT isoform. FT /FTId=PRO_0000071419. FT REPEAT 26 65 WD 1. FT REPEAT 91 132 WD 2. FT REPEAT 175 213 WD 3. FT REPEAT 224 264 WD 4. FT REPEAT 283 321 WD 5. FT REPEAT 338 379 WD 6. FT REPEAT 414 446 WD 7. SQ SEQUENCE 447 AA; 51692 MW; F4D407FF7ADA4ED6 CRC64; MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL HTAWHPKENI IAVATTNNLY IFQDKVN // ID 2ABA_RAT Reviewed; 447 AA. AC P36876; O35512; P36878; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 23-JAN-2007, entry version 53. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE alpha isoform (PP2A, subunit B, B-alpha isoform) (PP2A, subunit B, DE B55-alpha isoform) (PP2A, subunit B, PR55-alpha isoform) (PP2A, DE subunit B, R2-alpha isoform) (PP2A, subunit B, BRA isoform). GN Name=Ppp2r2a; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92114192; PubMed=1370560; RA Pallas D.C., Weller W., Jaspers S., Miller T.B. Jr., Lane W.S., RA Roberts T.M.; RT "The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton RT protein which is apparently substituted for by T antigens in complexes RT with the 36- and 63-kilodalton PP2A subunits, bears little resemblance RT to T antigens."; RL J. Virol. 66:886-893(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-272. RC STRAIN=Fischer 344; RX MEDLINE=93279382; PubMed=8389301; DOI=10.1016/0014-5793(93)81535-8; RA Hatano Y., Shima H., Haneji T., Miura A.B., Sugimura T., Nagao M.; RT "Expression of PP2A B regulatory subunit beta isotype in rat testis."; RL FEBS Lett. 324:71-75(1993). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- TISSUE SPECIFICITY: Brain. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; M83298; AAA41910.1; -; mRNA. DR EMBL; M83297; AAA41909.1; -; mRNA. DR EMBL; D14419; BAA21904.1; -; mRNA. DR PIR; A41805; A41805. DR UniGene; Rn.81155; -. DR Ensembl; ENSRNOG00000011158; Rattus norvegicus. DR KEGG; rno:117104; -. DR RGD; 620919; Ppp2r2a. DR ArrayExpress; P36876; -. DR GermOnline; ENSRNOG00000011158; Rattus norvegicus. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 7. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 447 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B alpha FT isoform. FT /FTId=PRO_0000071420. FT REPEAT 26 65 WD 1. FT REPEAT 91 132 WD 2. FT REPEAT 175 213 WD 3. FT REPEAT 224 264 WD 4. FT REPEAT 283 321 WD 5. FT REPEAT 338 379 WD 6. FT REPEAT 414 446 WD 7. FT VARIANT 60 60 E -> ESFKVHAALREASNLSMQ. FT CONFLICT 105 105 K -> E (in Ref. 1; AAA41909). FT CONFLICT 105 105 K -> R (in Ref. 2). FT CONFLICT 213 213 N -> S (in Ref. 2). FT CONFLICT 222 222 M -> V (in Ref. 2). SQ SEQUENCE 447 AA; 51678 MW; 180AC837D9DA4ECE CRC64; MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM MTRDYLSVKV WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL HTAWHPKENI IAVATTNNLY IFQDKVN // ID 2ABA_SCHPO Reviewed; 463 AA. AC Q12702; Q9UTD2; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 2. DT 20-FEB-2007, entry version 52. DE Protein phosphatase PP2A regulatory subunit B (PR55) (Protein DE phosphatase 2A 55 kDa regulatory subunit). GN Name=pab1; ORFNames=SPAC227.07c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT. RX MEDLINE=97233175; PubMed=9078365; RA Kinoshita K., Nemoto T., Nabeshima K., Kondoh H., Niwa H., RA Yanagida M.; RT "The regulatory subunits of fission yeast protein phosphatase 2A RT (PP2A) affect cell morphogenesis, cell wall synthesis and RT cytokinesis."; RL Genes Cells 1:29-45(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Phosphatase 2A affects a variety of biological processes CC in the cell such as transcription, cell cycle progression and CC cellular morphogenesis, and provides an initial identification of CC critical substrates for this phosphatase. The regulatory subunit CC may direct the catalytic subunit to distinct, albeit overlapping, CC subsets of substrates. CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which CC consist of a core composed of a catalytic subunit associated with CC a 65 kDa (PR65) (Subunit A) and a 55 kDa (PR55) (Subunit B) CC regulatory subunit. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 6 WD 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; D63915; BAA09945.1; -; Genomic_DNA. DR EMBL; AL133156; CAB61456.1; -; Genomic_DNA. DR PIR; T50163; T50163. DR GeneDB_Spombe; SPAC227.07c; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-000688-MONOMER; -. DR ArrayExpress; Q12702; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0000902; P:cell morphogenesis; IMP:GeneDB_SPombe. DR GO; GO:0009272; P:cell wall biosynthetic process (sensu Fungi); IMP:GeneDB_SPombe. DR GO; GO:0000910; P:cytokinesis; IMP:GeneDB_SPombe. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 5. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Complete proteome; Repeat; WD repeat. FT CHAIN 1 463 Protein phosphatase PP2A regulatory FT subunit B. FT /FTId=PRO_0000071441. FT REPEAT 27 66 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 174 212 WD 3. FT REPEAT 223 263 WD 4. FT REPEAT 282 320 WD 5. FT REPEAT 337 378 WD 6. FT CONFLICT 126 126 K -> R (in Ref. 1). FT CONFLICT 145 145 L -> V (in Ref. 1). SQ SEQUENCE 463 AA; 52795 MW; 43B289222A2D8CC3 CRC64; MDDIEDSLDQ WKFAQCFGDK GDVEDITEAD IISAVEFDHT GDYLATGDKG GRVVLFERNH SKKGCEYKFF TEFQSHEPEF DYLKSLEIEE KINKIRWCKR TNRAHFLLST NDKTIKLWKL YEKNLKVVAE NNLSDSFHSP MQGPLTTPSQ LRLPRLNHHD MIIAAYPRRV YANAHAYHIN SISVNSDAET YISADDLRIN LWNLSISDHS FNIVDIKPEN MEELTEVITS AEFHPINCNH LMYSSSKGNI KLLDLRQSAL CDNPCKLFED QEDQDSKSFF SEIISSISDV KFSQNGRYIL SRDYLTLKIW DVNMEKAPVK TIPLHDVLRS KLCDLYENDC IFDKFECTFS GDDKHVLSGS YSNNFGIYPT DSSLPGDRGQ IVLQADKAAF RARKSAANNV PKLNAVKNND WRSQPQAAMG SASVGLDPDN LDYNKKILHA SWHPFEDSVA IAATNNLFVF SKL // ID 2ABA_YEAST Reviewed; 526 AA. AC Q00362; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 20-FEB-2007, entry version 61. DE Protein phosphatase PP2A regulatory subunit B (PR55) (Cell division DE control protein 55). GN Name=CDC55; OrderedLocusNames=YGL190C; ORFNames=G1345; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92017858; PubMed=1656238; RA Healy A.M., Zolnierowicz S., Stapleton A.E., Goebl M., RA Depaoli-Roach A.A., Pringle J.R.; RT "CDC55, a Saccharomyces cerevisiae gene involved in cellular RT morphogenesis: identification, characterization, and homology to the B RT subunit of mammalian type 2A protein phosphatase."; RL Mol. Cell. Biol. 11:5767-5780(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97197971; PubMed=9046087; RX DOI=10.1002/(SICI)1097-0061(199701)13:1<55::AID-YEA48>3.3.CO;2-0; RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., RA Bruschi C.V.; RT "Sequencing of a 40.5 kb fragment located on the left arm of RT chromosome VII from Saccharomyces cerevisiae."; RL Yeast 13:55-64(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97313265; PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., RA Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., RA Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., RA Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., RA Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., RA Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., RA Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., RA Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., RA Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., RA Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., RA Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., RA Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., RA Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., RA Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., RA Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., RA Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., RA Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., RA Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., RA Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., RA van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., RA Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., RA Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., RA Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Phosphatase 2A affects a variety of biological processes CC in the cell such as transcription, cell cycle progression and CC cellular morphogenesis, and provides an initial identification of CC critical substrates for this phosphatase. The regulatory subunit CC may direct the catalytic subunit to distinct, albeit overlapping, CC subsets of substrates. CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which CC consist of a core composed of a catalytic subunit associated with CC a 65 kDa (PR65) (Subunit A) and a 55 kDa (PR55) (Subunit B) CC regulatory subunit. CC -!- INTERACTION: CC Q03018:ESP1; NbExp=1; IntAct=EBI-1942, EBI-6657; CC Q05934:VID22; NbExp=1; IntAct=EBI-1942, EBI-30350; CC P54786:ZDS2; NbExp=1; IntAct=EBI-1942, EBI-29637; CC -!- MISCELLANEOUS: Present with 8600 molecules/cell. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; M72716; AAA34482.1; -; Genomic_DNA. DR EMBL; X91837; CAA62954.1; -; Genomic_DNA. DR EMBL; X91489; CAA62785.1; -; Genomic_DNA. DR EMBL; Z72712; CAA96902.1; -; Genomic_DNA. DR PIR; A41698; A41698. DR DIP; DIP:2281N; -. DR IntAct; Q00362; -. DR Ensembl; YGL190C; Saccharomyces cerevisiae. DR GenomeReviews; Y13135_GR; YGL190C. DR KEGG; sce:YGL190C; -. DR CYGD; YGL190c; -. DR SGD; S000003158; CDC55. DR BioCyc; SCER-S28-01:SCER-S28-01-002190-MONOMER; -. DR LinkHub; Q00362; -. DR GermOnline; YGL190C; Saccharomyces cerevisiae. DR GO; GO:0005935; C:bud neck; IDA:SGD. DR GO; GO:0005934; C:bud tip; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0000158; F:protein phosphatase type 2A activity; TAS:SGD. DR GO; GO:0007015; P:actin filament organization; TAS:SGD. DR GO; GO:0007117; P:budding cell bud growth; TAS:SGD. DR GO; GO:0007094; P:mitotic spindle checkpoint; IMP:SGD. DR GO; GO:0006470; P:protein amino acid dephosphorylation; TAS:SGD. DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD. DR GO; GO:0006412; P:translation; IMP:SGD. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 2. DR Pfam; PF00400; WD40; 2. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 5. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Cell cycle; Complete proteome; Repeat; WD repeat. FT CHAIN 1 526 Protein phosphatase PP2A regulatory FT subunit B. FT /FTId=PRO_0000071442. FT REPEAT 23 62 WD 1. FT REPEAT 82 123 WD 2. FT REPEAT 182 220 WD 3. FT REPEAT 231 271 WD 4. FT REPEAT 290 328 WD 5. FT REPEAT 345 386 WD 6. FT REPEAT 495 525 WD 7. FT COMPBIAS 416 419 Poly-Ser. FT CONFLICT 500 500 I -> N (in Ref. 1). SQ SEQUENCE 526 AA; 59662 MW; 6DA12C2805FA6A82 CRC64; MAQNNFDFKF SQCFGDKADI VVTEADLITA VEFDYTGNYL ATGDKGGRVV LFERSNSRHC EYKFLTEFQS HDAEFDYLKS LEIEEKINEI KWLRPTQRSH FLLSTNDKTI KLWKVYEKNI KLVSQNNLTE GVTFAKKGKP DNHNSRGGSV RAVLSLQSLK LPQLSQHDKI IAATPKRIYS NAHTYHINSI SLNSDQETFL SADDLRINLW NLDIPDQSFN IVDIKPTNME ELTEVITSAE FHPQECNLFM YSSSKGTIKL CDMRQNSLCD NKTKTFEEYL DPINHNFFTE ITSSISDIKF SPNGRYIASR DYLTVKIWDV NMDNKPLKTI NIHEQLKERL SDTYENDAIF DKFEVNFSGD SSSVMTGSYN NNFMIYPNVV TSGDNDNGIV KTFDEHNAPN SNSNKNIHNS IQNKDSSSSG NSHKRRSNGR NTGMVGSSNS SRSSIAGGEG ANSEDSGTEM NEIVLQADKT AFRNKRYGSL AQRSARNKDW GDDIDFKKNI LHFSWHPREN SIAVAATNNL FIFSAL // ID 2ABB_ARATH Reviewed; 501 AA. AC Q39247; Q9FZ61; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 48. DE Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B DE beta isoform (PP2A, subunit B, beta isoform) (AtB beta). GN Name=PP2AB2; OrderedLocusNames=At1g17720; ORFNames=F11A6.6; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC STRAIN=cv. Columbia; RX MEDLINE=96343945; PubMed=8756607; RA Corum J.W. III, Hartung A.J., Stamey R.T., Rundle S.J.; RT "Characterization of DNA sequences encoding a novel isoform of the 55 RT kDa B regulatory subunit of the type 2A protein serine/threonine RT phosphatase of Arabidopsis thaliana."; RL Plant Mol. Biol. 31:419-427(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families) (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q39247-1; Sequence=Displayed; CC Name=2; CC IsoId=Q39247-2; Sequence=VSP_017095; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 6 WD 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; U40161; AAB60777.1; -; mRNA. DR EMBL; AC034257; AAF99812.1; -; Genomic_DNA. DR EMBL; AF370519; AAK43896.1; -; mRNA. DR EMBL; AY045665; AAK74023.1; -; mRNA. DR EMBL; BT000645; AAN18211.1; -; mRNA. DR EMBL; BT002183; AAN72194.1; -; mRNA. DR PIR; B86312; B86312. DR UniGene; At.19970; -. DR GenomeReviews; CT485782_GR; AT1G17720. DR KEGG; ath:At1g17720; -. DR GeneFarm; 3009; 267. DR TAIR; At1g17720; -. DR GermOnline; AT1G17720; Arabidopsis thaliana. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 5. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Alternative splicing; Repeat; WD repeat. FT CHAIN 1 501 Serine/threonine protein phosphatase 2A FT 55 kDa regulatory subunit B beta isoform. FT /FTId=PRO_0000071439. FT REPEAT 34 73 WD 1. FT REPEAT 110 151 WD 2. FT REPEAT 220 258 WD 3. FT REPEAT 269 309 WD 4. FT REPEAT 328 366 WD 5. FT REPEAT 471 501 WD 6. FT VAR_SEQ 200 200 Missing (in isoform 2). FT /FTId=VSP_017095. SQ SEQUENCE 501 AA; 56275 MW; 030B7997B730F581 CRC64; MNGGDDAATS GPPPSLEWRF SQVFGERTAG EEVQEVDIIS AIEFDKSGDH LATGDRGGRV VLFERTDTKD HGGSRKDLEQ TDYPVRHPEF RYKTEFQSHE PEFDYLKSLE IEEKINKIRW CQPANGALFL LSTNDKTIKY WKVQEKKIKK ISEMNIDPSE SSNIPPQLVT NGLPADKGHD YLSKDFSFPP GGIPSLRLPV VVTSQETNLV ARCRRVYAHA HDYHINSISN SSDGETFISA DDLRVNLWNL EISNQSFNIV DVKPTNMEDL TEVITSAEFH PIHCNMLAYS SSKGSIRLID MRQSALCDSH TKLFEEPEAP GSRSFFTEII ASISDIKFSK DGRYILSRDY MTLKLWDINM DSGPVASYQV HEHLRPRLCD LYENDSIFDK FECCLSGDGL RVATGSYSNL FRVFGASQGS TEAATLEASK NPMRRQIQTP ARPSRSIGSM TRVVRRGSES PGTEANGNAY DFTTKLLHMA WHPTENSIAC AAANSLYMYY A // ID 2ABB_HUMAN Reviewed; 443 AA. AC Q00005; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 23-JAN-2007, entry version 69. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform). GN Name=PPP2R2B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetal brain; RX MEDLINE=91198016; PubMed=1849734; DOI=10.1021/bi00229a001; RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J., RA Merlevede W., Hofsteenge J., Hemmings B.A.; RT "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: RT evidence for a neuronal-specific isoform."; RL Biochemistry 30:3589-3597(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 DISEASE. RX MEDLINE=20047763; PubMed=10581021; DOI=10.1038/70493; RA Holmes S.E., O'Hearn E.E., McInnis M.G., Gorelick-Feldman D.A., RA Kleiderlein J.J., Callahan C., Kwak N.G., Ingersoll-Ashworth R.G., RA Sherr M., Sumner A.J., Sharp A.H., Ananth U., Seltzer W.K., Boss M.A., RA Vieria-Saecker A.-M., Epplen J.T., Riess O., Ross C.A., Margolis R.L.; RT "Expansion of a novel CAG trinucleotide repeat in the 5' region of RT PPP2R2B is associated with SCA12."; RL Nat. Genet. 23:391-392(1999). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- TISSUE SPECIFICITY: Brain. CC -!- DISEASE: Defects in PPP2R2B are the cause of spinocerebellar CC ataxia 12 (SCA12) [MIM:604326]. Spinocerebellar ataxia is a CC clinically and genetically heterogeneous group of autosomal CC dominant cerebellar ataxias (ADCA). Patients show progressive CC incoordination of gait and often poor coordination of hands, CC speech and eye movements. Spinocerebellar ataxia is caused by CC degeneration of the cerebellum with variable involvement of the CC brainstem and spinal cord. The molecular defect in SCA12 is the CC expansion of a CAG repeat in the 5'UTR of the gene. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD repeats. CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=PPP2R2B". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M64930; AAA36493.1; -; mRNA. DR EMBL; BC031790; AAH31790.1; -; mRNA. DR PIR; B38351; B38351. DR UniGene; Hs.193825; -. DR Ensembl; ENSG00000156475; Homo sapiens. DR KEGG; hsa:5521; -. DR H-InvDB; HIX0021292; -. DR HGNC; HGNC:9305; PPP2R2B. DR MIM; 604325; gene. DR MIM; 604326; phenotype. DR ArrayExpress; Q00005; -. DR GermOnline; ENSG00000156475; Homo sapiens. DR RZPD-ProtExp; C0311; -. DR RZPD-ProtExp; IOH22211; -. DR RZPD-ProtExp; IOH43154; -. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Neurodegeneration; Repeat; Spinocerebellar ataxia; WD repeat. FT CHAIN 1 443 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B beta isoform. FT /FTId=PRO_0000071421. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 442 WD 7. SQ SEQUENCE 443 AA; 51710 MW; C383C834B2852B8F CRC64; MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABB_MACFA Reviewed; 443 AA. AC Q4R8L3; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 31-OCT-2006, entry version 10. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform). GN Name=PPP2R2B; ORFNames=QtsA-12205; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; AB168439; BAE00559.1; -; mRNA. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 443 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B beta isoform. FT /FTId=PRO_0000071422. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 442 WD 7. SQ SEQUENCE 443 AA; 51710 MW; C383C834B2852B8F CRC64; MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABB_MOUSE Reviewed; 443 AA. AC Q6ZWR4; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 33. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform). GN Name=Ppp2r2b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; 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 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: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; AK039592; BAC30395.1; -; mRNA. DR EMBL; BC088979; AAH88979.1; -; mRNA. DR UniGene; Mm.26134; -. DR Ensembl; ENSMUSG00000024500; Mus musculus. DR MGI; MGI:1920180; Ppp2r2b. DR ArrayExpress; Q6ZWR4; -. DR GermOnline; ENSMUSG00000024500; Mus musculus. DR RZPD-ProtExp; IOM17153; -. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 443 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B beta isoform. FT /FTId=PRO_0000071423. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 442 WD 7. SQ SEQUENCE 443 AA; 51710 MW; C383C834B2852B8F CRC64; MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABB_ORYSA Reviewed; 525 AA. AC Q6Z8B7; O82774; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 21. DE Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B DE beta isoform (PP2A, subunit B, beta isoform). GN OrderedLocusNames=Os02g0224200, LOC_Os02g13110; ORFNames=P0470A03.14; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Indica / IR36; TISSUE=Seed; RA Chang M.C., Chen X.C., Daughetee S., Wu R.; RT "Molecular cloning and characterization of cDNA and genomic DNA RT encodes the homologue of the 55 kDa B regulatory subunit of protein RT phosphatase 2A in rice (Oryza sativa L.)."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RG The international rice genome sequencing project (IRGSP) consortium; RT "Oryza sativa nipponbare chromosome 2 genomic DNA sequence."; RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=22752273; PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). CC -!- FUNCTION: The B regulatory subunit may modulate substrate CC selectivity and catalytic activity, and also may direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of CC a catalytic subunit (subunits C), a constant regulatory subunit CC (subunit A), and a variety of regulatory subunits such as subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families) (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 6 WD 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; AF081923; AAC32205.1; -; mRNA. DR EMBL; AF081922; AAC32204.1; -; Genomic_DNA. DR EMBL; AP004779; BAD17063.1; -; Genomic_DNA. DR EMBL; AK101100; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; T02952; T02952. DR UniGene; Os.8042; -. DR Gramene; Q6Z8B7; -. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 525 Serine/threonine protein phosphatase 2A FT 55 kDa regulatory subunit B beta isoform. FT /FTId=PRO_0000247273. FT REPEAT 48 87 WD 1. FT REPEAT 124 165 WD 2. FT REPEAT 244 282 WD 3. FT REPEAT 293 333 WD 4. FT REPEAT 352 390 WD 5. FT REPEAT 495 525 WD 6. FT COMPBIAS 182 189 Poly-Ser. FT CONFLICT 4 4 S -> F (in Ref. 1). FT CONFLICT 28 28 Q -> QPQ (in Ref. 1). FT CONFLICT 525 525 A -> AYITG (in Ref. 1). SQ SEQUENCE 525 AA; 58980 MW; C1F1A87846320803 CRC64; MDPSSKSPDD DDLRPEAEAA RRPQPQPQPR EWRFAQVFGE RAAGEDVQEV DIISAIEFDK SGDHLATGDR GGRVVLFERT DSRDSASRSE LERQDYPIAR HPEFRYKTEF QSHEPEFDYL KSLEIEEKIN KIKWCQTANN ALFLLSTNDK TIKYWKVQER KVKRISVMNL NTSQSSGNGT TSSSSSSSSR AILPNGGCSE KLYNFPNNDL LFPPGGCTSL RLPVVVTGQD LNLVPRCRRV YSHAHDYHIN SISNNSDGET YISADDLRIN LWNLEISNQS FNIVDVKPAN MEDLTEVITC AEFHPTHCNT LAYSSSKGSI RLIDLRQSAL CDNHAKLFEE HEAPGSRSFF TEIIASVSDI KFARDGRHIL SRDYMTLKLW DINMDSGPVA TFQVHEYLRP KLCDLYENDS IFDKFECCLS GDGLRVATGS YSNLFRVFGC TPGSAEATTL EASRNPMRRQ VANPTRPART LTSLTRAVRR GGENPGVDAN GNSYDLSTKL LHLAWHPTEN SIACAAANSL YMYYA // ID 2ABB_PIG Reviewed; 443 AA. AC P54614; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 31-OCT-2006, entry version 40. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform). GN Name=PPP2R2B; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Mayer-Jaekel R.E.; RL Thesis (1992), Friedrich Miescher Institut / Basel, Switzerland. CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- TISSUE SPECIFICITY: Brain. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; Z34933; CAA84405.1; -; mRNA. DR UniGene; Ssc.103; -. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 5. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 443 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B beta isoform. FT /FTId=PRO_0000071424. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 442 WD 7. SQ SEQUENCE 443 AA; 51460 MW; F8562FC696719F41 CRC64; MEEDIDTRKI NNSFLRDHSY ATEADIISAV EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI ADIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASACVTG TPNFLKEPED PSNRSFSLKL SSSISDVKFS QQWEDIMTRD YLTVKVWDLN MENRPIETYQ VHNYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABB_PONPY Reviewed; 443 AA. AC Q5R4A2; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 31-OCT-2006, entry version 14. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform). GN Name=PPP2R2B; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; CR861353; CAH93414.1; -; mRNA. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 443 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B beta isoform. FT /FTId=PRO_0000071425. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 442 WD 7. SQ SEQUENCE 443 AA; 51710 MW; C383C834B2852B8F CRC64; MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABB_RABIT Reviewed; 413 AA. AC Q00006; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 46. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform) (Fragment). GN Name=PPP2R2B; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetal brain; RX MEDLINE=91198016; PubMed=1849734; DOI=10.1021/bi00229a001; RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J., RA Merlevede W., Hofsteenge J., Hemmings B.A.; RT "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: RT evidence for a neuronal-specific isoform."; RL Biochemistry 30:3589-3597(1991). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- TISSUE SPECIFICITY: Brain. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; M64931; AAA31458.1; -; mRNA. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 5. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN <1 413 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B beta isoform. FT /FTId=PRO_0000071426. FT REPEAT <1 31 WD 1. FT REPEAT 57 98 WD 2. FT REPEAT 141 179 WD 3. FT REPEAT 190 230 WD 4. FT REPEAT 249 287 WD 5. FT REPEAT 304 345 WD 6. FT REPEAT 380 412 WD 7. FT NON_TER 1 1 SQ SEQUENCE 413 AA; 48243 MW; 49237B7817EB8FE2 CRC64; EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABB_RAT Reviewed; 443 AA. AC P36877; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 20-FEB-2007, entry version 56. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform) (PP2A, subunit B, BRB isoform). GN Name=Ppp2r2b; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX MEDLINE=95331316; PubMed=7607250; RA Akiyama N., Shima H., Hatano Y., Osawa Y., Sugimura T., Nagao M.; RT "cDNA cloning of BR gamma, a novel brain-specific isoform of the B RT regulatory subunit of type-2A protein phosphatase."; RL Eur. J. Biochem. 230:766-772(1995). 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 [MRNA] OF 8-177. RC TISSUE=Testis; RX MEDLINE=93279382; PubMed=8389301; DOI=10.1016/0014-5793(93)81535-8; RA Hatano Y., Shima H., Haneji T., Miura A.B., Sugimura T., Nagao M.; RT "Expression of PP2A B regulatory subunit beta isotype in rat testis."; RL FEBS Lett. 324:71-75(1993). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- TISSUE SPECIFICITY: Brain and testis. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; D38260; BAA07412.1; -; mRNA. DR EMBL; BC078834; AAH78834.1; -; mRNA. DR EMBL; D14421; BAA03313.1; -; mRNA. DR PIR; S33257; S33257. DR UniGene; Rn.44437; -. DR Ensembl; ENSRNOG00000018851; Rattus norvegicus. DR KEGG; rno:60660; -. DR RGD; 631441; Ppp2r2b. DR ArrayExpress; P36877; -. DR GermOnline; ENSRNOG00000018851; Rattus norvegicus. DR GO; GO:0007286; P:spermatid development; IEP:RGD. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 443 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B beta isoform. FT /FTId=PRO_0000071427. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 442 WD 7. SQ SEQUENCE 443 AA; 51668 MW; 0089EF6E8ED53082 CRC64; MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD YLTAKVWDLN MENRPVETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABD_CHICK Reviewed; 451 AA. AC Q5ZIY5; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 31-OCT-2006, entry version 15. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE delta isoform (PP2A, subunit B, B-delta isoform) (PP2A, subunit B, DE B55-delta isoform) (PP2A, subunit B, PR55-delta isoform) (PP2A, DE subunit B, R2-delta isoform). GN Name=PPP2R2D; ORFNames=RCJMB04_22l15; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., RA Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., RA Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; AJ720649; CAG32308.1; -; mRNA. DR UniGene; Gga.1129; -. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 451 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B delta FT isoform. FT /FTId=PRO_0000071436. FT REPEAT 30 69 WD 1. FT REPEAT 95 136 WD 2. FT REPEAT 179 217 WD 3. FT REPEAT 228 268 WD 4. FT REPEAT 287 325 WD 5. FT REPEAT 342 383 WD 6. FT REPEAT 418 451 WD 7. FT COMPBIAS 6 11 Poly-Gly. SQ SEQUENCE 451 AA; 52016 MW; 3AE312A5077A0BF6 CRC64; MAGVAGGGGN GNDFQWCFSQ VQGAVDEDVA EADIISTVEF NYSGDLLATG DKGGRVVIFQ REQENKSRPH SRGEYNVYST FQSHEPEFDY LKSLEIEEKI NKIRWLPQQN AAHFLLSTND KTIKLWKISE RDKRAEGYNL KDEDGRLRDP FKITALRVPI LKPMDLMVEA SPRRIFANAH TYHINSISVN SDHETYLSAD DLRINLWHLE ITDRSFNIVD IKPANMEELT EVITAAEFHP HHCNVFVYSS SKGTIRLCDM RSSALCDRHS KFFEEPEDPS SRSFFSEIIS SISDVKFSHS GRYMMTRDYL SVKVWDLNME NRPVETYQVH EYLRSKLCSL YENDCIFDKF ECCWNGSDGA IMTGSYNNFF RMFDRNTRRD ITLEASRESS KPRAILKPRK VCTGGKRKKD EINVDSLDFN KKILHTAWHP MENIIAVAAT NNLYIFQDKI N // ID 2ABD_HUMAN Reviewed; 453 AA. AC Q66LE6; Q5SQJ2; Q9P1Y7; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 23-JAN-2007, entry version 25. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE delta isoform (PP2A, subunit B, B-delta isoform) (PP2A, subunit B, DE B55-delta isoform) (PP2A, subunit B, PR55-delta isoform) (PP2A, DE subunit B, R2-delta isoform). GN Name=PPP2R2D; Synonyms=KIAA1541; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). 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 34-453. RC TISSUE=Brain; RX MEDLINE=20277482; PubMed=10819331; DOI=10.1093/dnares/7.2.143; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 7:143-150(2000). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD repeats. CC -!- CAUTION: Ref.1 sequence differs from that shown due to erroneous CC 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; AL732395; CAI16703.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC047379; AAH47379.1; -; mRNA. DR EMBL; AB040974; BAA96065.1; ALT_INIT; mRNA. DR UniGene; Hs.380372; -. DR Ensembl; ENSG00000175470; Homo sapiens. DR HGNC; HGNC:23732; PPP2R2D. DR LinkHub; Q66LE6; -. DR ArrayExpress; Q66LE6; -. DR GermOnline; ENSG00000175470; Homo sapiens. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 7. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 453 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B delta FT isoform. FT /FTId=PRO_0000071433. FT REPEAT 32 71 WD 1. FT REPEAT 97 138 WD 2. FT REPEAT 181 219 WD 3. FT REPEAT 230 270 WD 4. FT REPEAT 289 327 WD 5. FT REPEAT 344 385 WD 6. FT REPEAT 420 452 WD 7. FT COMPBIAS 3 8 Poly-Gly. SQ SEQUENCE 453 AA; 52042 MW; 0669CDB80AF4400E CRC64; MAGAGGGGCP AGGNDFQWCF SQVKGAIDED VAEADIISTV EFNYSGDLLA TGDKGGRVVI FQREQENKSR PHSRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAHFLLST NDKTIKLWKI SERDKRAEGY NLKDEDGRLR DPFRITALRV PILKPMDLMV EASPRRIFAN AHTYHINSIS VNSDHETYLS ADDLRINLWH LEITDRSFNI VDIKPANMEE LTEVITAAEF HPHQCNVFVY SSSKGTIRLC DMRSSALCDR HSKFFEEPED PSSRSFFSEI ISSISDVKFS HSGRYMMTRD YLSVKVWDLN MESRPVETHQ VHEYLRSKLC SLYENDCIFD KFECCWNGSD SAIMTGSYNN FFRMFDRDTR RDVTLEASRE SSKPRASLKP RKVCTGGKRR KDEISVDSLD FNKKILHTAW HPVDNVIAVA ATNNLYIFQD KIN // ID 2ABD_MOUSE Reviewed; 453 AA. AC Q925E7; Q6ZPN5; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 23-JAN-2007, entry version 41. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE delta isoform (PP2A, subunit B, B-delta isoform) (PP2A, subunit B, DE B55-delta isoform) (PP2A, subunit B, PR55-delta isoform) (PP2A, DE subunit B, R2-delta isoform). GN Name=Ppp2r2d; Synonyms=D7Ertd753e, Kiaa1541; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RA Chang H., Lee S., Park K.; RT "Analysis of mDRA (Mouse Down-regulated in Adenoma) interaction in RT yeast two-hybrid system."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Natural killer cell; RX MEDLINE=22977043; 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 SEQUENCE REVISION. RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. 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). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; AF366393; AAK53703.1; -; mRNA. DR EMBL; AK129386; BAC98196.2; ALT_INIT; mRNA. DR EMBL; BC066022; AAH66022.1; -; mRNA. DR UniGene; Mm.258739; -. DR Ensembl; ENSMUSG00000041769; Mus musculus. DR KEGG; mmu:52432; -. DR MGI; MGI:1289252; Ppp2r2d. DR ArrayExpress; Q925E7; -. DR GermOnline; ENSMUSG00000041769; Mus musculus. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 7. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 453 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B delta FT isoform. FT /FTId=PRO_0000071434. FT REPEAT 32 71 WD 1. FT REPEAT 97 138 WD 2. FT REPEAT 181 219 WD 3. FT REPEAT 230 270 WD 4. FT REPEAT 289 327 WD 5. FT REPEAT 344 385 WD 6. FT REPEAT 420 452 WD 7. FT COMPBIAS 3 8 Poly-Gly. SQ SEQUENCE 453 AA; 51957 MW; C4B474AA28397576 CRC64; MAGAGGGGCP AGGNDFQWCF SQVKGAVDED VAEADIISTV EFNYSGDLLA TGDKGGRVVI FQREQENKGR AHSRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAHFLLST NDKTIKLWKI SERDKRAEGY NLKDEDGRLR DPFRITALRV PILKPMDLMV EASPRRIFAN AHTYHINSIS VNSDHETYLS ADDLRINLWH LEITDRSFNI VDIKPANMEE LTEVITAAEF HPHQCNVFVY SSSKGTIRLC DMRSSALCDR HAKFFEEPED PSSRSFFSEI ISSISDVKFS HSGRYMMTRD YLSVKVWDLN MEGRPVETHQ VHEYLRSKLC SLYENDCIFD KFECCWNGSD SAIMTGSYNN FFRMFDRNTR RDVTLEASRE NSKPRASLKP RKVCTGGKRK KDEISVDSLD FNKKILHTAW HPMESIIAVA ATNNLYIFQD KIN // ID 2ABD_RAT Reviewed; 453 AA. AC P56932; Q66HR7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 20-FEB-2007, entry version 49. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE delta isoform (PP2A, subunit B, B-delta isoform) (PP2A, subunit B, DE B55-delta isoform) (PP2A, subunit B, PR55-delta isoform) (PP2A, DE subunit B, R2-delta isoform). GN Name=Ppp2r2d; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX MEDLINE=20026081; PubMed=10556517; DOI=10.1016/S0014-5793(99)01377-0; RA Strack S., Chang D., Zaucha J.A., Colbran R.J., Wadzinski B.E.; RT "Cloning and characterization of B delta, a novel regulatory subunit RT of protein phosphatase 2A."; RL FEBS Lett. 460:462-466(1999). 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: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in brain, CC heart, placenta, skeletal muscle, testis, thymus and spleen. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; AF180350; AAF08536.1; -; mRNA. DR EMBL; BC081720; AAH81720.1; -; mRNA. DR UniGene; Rn.116122; -. DR Ensembl; ENSRNOG00000016940; Rattus norvegicus. DR RGD; 708356; Ppp2r2d. DR GermOnline; ENSRNOG00000016940; Rattus norvegicus. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 7. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 453 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B delta FT isoform. FT /FTId=PRO_0000071435. FT REPEAT 32 71 WD 1. FT REPEAT 97 138 WD 2. FT REPEAT 181 219 WD 3. FT REPEAT 230 270 WD 4. FT REPEAT 289 327 WD 5. FT REPEAT 344 385 WD 6. FT REPEAT 420 452 WD 7. FT COMPBIAS 3 8 Poly-Gly. FT CONFLICT 330 330 H -> Q (in Ref. 2). SQ SEQUENCE 453 AA; 51982 MW; 733E80A93A5BC2BB CRC64; MAGAGGGGCP TGGNDFQWCF SQVKGAVDED VAEADIISTV EFNYSGDLLA TGDKGGRVVI FQREQENKGR AHSRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAHFLLST NDKTIKLWKI SERDKRAEGY NLKDEDGRLR DPFRITALRV PILKPMDLMV EASPRRIFAN AHTYHINSIS VNSDHETYLS ADDLRINLWH LEITDRSFNI VDIKPANMEE LTEVITAAEF HPHQCNVFVY SSSKGTIRLC DMRSSALCDR HAKFFEEPED PSSRSFFSEI ISSISDVKFS HSGRYMMTRD YLSVKVWDLN MEGRPVETHH VHEYLRSKLC SLYENDCIFD KFECCWNGSD SAIMTGSYNN FFRMFDRNTR RDVTLEASRE NSKPRASLKP RKVCSGGKRK KDEISVDSLD FNKKILHTAW HPMESIIAVA ATNNLYIFQD KIN // ID 2ABG_HUMAN Reviewed; 447 AA. AC Q9Y2T4; Q9H3G7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 3. DT 20-FEB-2007, entry version 56. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE gamma isoform (PP2A, subunit B, B-gamma isoform) (PP2A, subunit B, DE B55-gamma isoform) (PP2A, subunit B, PR55-gamma isoform) (PP2A, DE subunit B, R2-gamma isoform) (IMYPNO1). GN Name=PPP2R2C; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=20039617; PubMed=10574460; DOI=10.1093/dnares/6.5.323; RA Torres R., Ide S.E., Dehejia A., Baras A., Polymeropoulos M.H.; RT "Genomic structure and localization of the human phosphatase 2A BR RT gamma regulatory subunit."; RL DNA Res. 6:323-327(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=20399570; PubMed=10945473; DOI=10.1006/geno.2000.6219; RA Hu P., Yu L., Zhang M., Zheng L., Zhao Y., Fu Q., Zhao S.; RT "Molecular cloning and mapping of the brain-abundant B1gamma subunit RT of protein phosphatase 2A, PPP2R2C, to human chromosome 4p16."; RL Genomics 67:83-86(2000). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD repeats. CC -!- CAUTION: The EMBL entry for Ref.1 is not complete, the paper shows CC the rest of the sequence (residues 1 to 23). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF096160; AAD20987.1; -; Genomic_DNA. DR EMBL; AF096153; AAD20987.1; JOINED; Genomic_DNA. DR EMBL; AF096154; AAD20987.1; JOINED; Genomic_DNA. DR EMBL; AF096155; AAD20987.1; JOINED; Genomic_DNA. DR EMBL; AF096156; AAD20987.1; JOINED; Genomic_DNA. DR EMBL; AF096157; AAD20987.1; JOINED; Genomic_DNA. DR EMBL; AF096158; AAD20987.1; JOINED; Genomic_DNA. DR EMBL; AF096159; AAD20987.1; JOINED; Genomic_DNA. DR EMBL; AF086924; AAG39636.1; -; mRNA. DR UniGene; Hs.479069; -. DR Ensembl; ENSG00000074211; Homo sapiens. DR KEGG; hsa:5522; -. DR HGNC; HGNC:9306; PPP2R2C. DR MIM; 605997; gene. DR ArrayExpress; Q9Y2T4; -. DR GermOnline; ENSG00000074211; Homo sapiens. DR RZPD-ProtExp; IOH22415; -. DR GO; GO:0000159; C:protein phosphatase type 2A complex; NAS:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; NAS:UniProtKB. DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 447 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B gamma FT isoform. FT /FTId=PRO_0000071428. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 446 WD 7. FT CONFLICT 24 24 Missing (in Ref. 1). FT CONFLICT 66 66 D -> E (in Ref. 1). FT CONFLICT 253 253 P -> R (in Ref. 1). FT CONFLICT 293 293 D -> G (in Ref. 1). SQ SEQUENCE 447 AA; 51500 MW; 76FFE2A76410FD24 CRC64; MGEDTDTRKI NHSFLRDHSY VTEADIISTV EFNHTGELLA TGDKGGRVVI FQREPESKNA PHSQGDYDVY STFQSHEPEF DYLKSLEIEE KINKIKWLPQ QNAAHSLLST NDKTIKLWKI TERDKRPEGY NLKDEEGKLK DLSTVTSLQV PVLKPMDLMV EVSPRRIFAN GHTYHINSIS VNSDCETYMS ADDLRINLWH LAITDRSFNI VDIKPANMED LTEVITASEF HPHHCNLFVY SSSKGSLRLC DMPAAALCDK HSKLFEEPED PSNRSFFSEI ISSVSDVKFS HSDRYMLTRD YLTVKVWDLN MEARPIETYQ VHDYLRSKLC SLYENDCIFD KFECAWNGSD SVIMTGAYNN FFRMFDRNTK RDVTLEASRE SSKPRAVLKP RRVCVGGKRR RDDISVDSLD FTKKILHTAW HPAENIIAIA ATNNLYIFQD KVNSDMH // ID 2ABG_MACFA Reviewed; 447 AA. AC Q95LP0; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 31-OCT-2006, entry version 25. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE gamma isoform (PP2A, subunit B, B-gamma isoform) (PP2A, subunit B, DE B55-gamma isoform) (PP2A, subunit B, PR55-gamma isoform) (PP2A, DE subunit B, R2-gamma isoform). GN Name=PPP2R2C; ORFNames=QtsA-16028; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M., RA Terao K., Sugano S., Hashimoto K.; RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes RT in the human genome sequence."; RL BMC Genomics 3:36-36(2002). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; AB072748; BAB69717.1; -; mRNA. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 447 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B gamma FT isoform. FT /FTId=PRO_0000071429. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 446 WD 7. SQ SEQUENCE 447 AA; 51350 MW; FAD1F20D29CEB149 CRC64; MGLSFFSKHL PIQEGQPWAS KTPADIISTV EFNHTGELLA TGDKGGRVVI FQREPESKNA PHSQGEYDVY STFQSHEPEF DYLKSLEIEE KINKIKWLPQ QNAAHSLLST NDKTIKLWKI TERDKRPEGY NLKDEEGKLK DLSTVTSLQV PVLKPMDLMV EVSPRRIFAN GHTYHINSIS VNSDCETYMS ADDLRINLWH LAITDRSFNI VDIKPANMED LTEVITASEF HPHHCNLFVY SSSKGSLRLC DMRAAALCDK HSKLFEEPED PSNRSFFSEI ISSVSDVKFS HSGRYMLTRD YLTVKVWDLN MEARPIETYQ VHDYLRSKLC SLYENDCIFD KFECAWNGSD SVIMTGAYNN FFRMFDRNTK RDVTLEASRE SSKPRAVLKP RRVCVGGKRR RDDISVDSLD FTKKILHTAW HPAENIIAIA ATNNLYIFQD KVNSDMH // ID 2ABG_MOUSE Reviewed; 447 AA. AC Q8BG02; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 23-JAN-2007, entry version 34. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE gamma isoform (PP2A, subunit B, B-gamma isoform) (PP2A, subunit B, DE B55-gamma isoform) (PP2A, subunit B, PR55-gamma isoform) (PP2A, DE subunit B, R2-gamma isoform). GN Name=Ppp2r2c; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RA Zhou G., Huang X., Yu L.; RT "Cloning of mouse protein phosphatase 2 (formerly 2A), regulatory RT subunit B."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Hippocampus, 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 [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: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment (By similarity). CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules (By similarity). CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; AY348866; AAQ55226.1; -; mRNA. DR EMBL; AK032023; BAC27654.1; -; mRNA. DR EMBL; AK049830; BAC33942.1; -; mRNA. DR EMBL; BC059811; AAH59811.1; -; mRNA. DR UniGene; Mm.41694; -. DR Ensembl; ENSMUSG00000029120; Mus musculus. DR MGI; MGI:2442660; Ppp2r2c. DR ArrayExpress; Q8BG02; -. DR GermOnline; ENSMUSG00000029120; Mus musculus. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 447 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B gamma FT isoform. FT /FTId=PRO_0000071430. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 446 WD 7. SQ SEQUENCE 447 AA; 51462 MW; D94D0156CB4A3035 CRC64; MGEDTDTRKI NHSFLRDHSY VTEADVISTV EFNHTGELLA TGDKGGRVVI FQREPESKNA PHSQGEYDVY STFQSHEPEF DYLKSLEIEE KINKIKWLPQ QNAAHSLLST NDKTIKLWKI TERDKRPEGY NLKDEEGKLK DLSTVTSLQV PVLKPMDLMV EVSPRRTFAN GHTYHINSIS VNSDCETYMS ADDLRINLWH LAITDRSFNI VDIKPANMED LTEVITASEF HPHHCNLFVY SSSKGSLRLC DMRAAALCDK HSKLFEEPED PSNRSFFSEI ISSVSDVKFS HSGRYMLTRD YLTVKVWDLN MEARPIETYQ VHDYLRSKLC SLYESDCIFD KFECAWNGSD SVIMTGAYNN FFRMFDRNTK RDVTLEASRE SSKPRAVLKP RRVCVGGKRR RDDISVDSLD FTKKILHTAW HPAENIIAIA ATNNLYIFQD KVNSDMH // ID 2ABG_RABIT Reviewed; 447 AA. AC P50410; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 31-OCT-2006, entry version 44. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE gamma isoform (PP2A, subunit B, B-gamma isoform) (PP2A, subunit B, DE B55-gamma isoform) (PP2A, subunit B, PR55-gamma isoform) (PP2A, DE subunit B, R2-gamma isoform). GN Name=PPP2R2C; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=New Zealand white; TISSUE=Brain, and Skeletal muscle; RX MEDLINE=95001896; PubMed=7918404; DOI=10.1021/bi00205a023; RA Zolnierowicz S., Csortos C., Bondor J., Verin A., Mumby M.C., RA Depaoli-Roach A.A.; RT "Diversity in the regulatory B-subunits of protein phosphatase 2A: RT identification of a novel isoform highly expressed in brain."; RL Biochemistry 33:11858-11867(1994). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- TISSUE SPECIFICITY: Highly expressed in brain. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; U09355; AAA58956.1; -; mRNA. DR EMBL; U09354; AAA58955.1; -; mRNA. DR PIR; A55836; A55836. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 447 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B gamma FT isoform. FT /FTId=PRO_0000071431. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 446 WD 7. SQ SEQUENCE 447 AA; 51469 MW; C6847C2381E41A7A CRC64; MGEDTDTRKI NHSFLRDHSY VTEADIISTV EFNHTGELLA TGDKGGRVVI FQREPESKNA PHSQGEYDVY STFQSHEPEF DYLKSLEIEE KINKIKWLPQ QNAAHSLLST NDKTIKLWKI TERDKRPEGY NLKDEEGKLK DLSTVTSLQV PVLKPMDLMV EVSPRRIFAN GHTYHINSIS VNSDCETYMS ADDLRINLWH LAVTDRSFNI VDIKPANMED LTEVITASEF HPHHCNLFVY SSSKGSLRLC DMRAAALCDK HSKLFEEPED PSNRSFFSEI ISSVSDVKFS HSGRYMLTRD YLTVKVWDLN MEARPIETYQ VHDYLRSKLC SLYENDCIFD KFECAWNGSD SVIMTGAYNN FFRMFDRNTK RDVTLEASRE SSKPRAVLKP RRVCVGGKRR RDDISVDSLD FTKKILHTAW HPAENIIAIA ATNNLYIFQD KVNSDVH // ID 2ABG_RAT Reviewed; 447 AA. AC P97888; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 23-JAN-2007, entry version 49. DE Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B DE gamma isoform (PP2A, subunit B, B-gamma isoform) (PP2A, subunit B, DE B55-gamma isoform) (PP2A, subunit B, PR55-gamma isoform) (PP2A, DE subunit B, R2-gamma isoform) (PP2A, subunit B, BRgamma isoform). GN Name=Ppp2r2c; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX MEDLINE=95331316; PubMed=7607250; RA Akiyama N., Shima H., Hatano Y., Osawa Y., Sugimura T., Nagao M.; RT "cDNA cloning of BR gamma, a novel brain-specific isoform of the B RT regulatory subunit of type-2A protein phosphatase."; RL Eur. J. Biochem. 230:766-772(1995). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- TISSUE SPECIFICITY: Highly expressed in brain. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B CC family. CC -!- SIMILARITY: Contains 7 WD 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; D38261; BAA07413.1; -; mRNA. DR UniGene; Rn.54550; -. DR KEGG; rno:117256; -. DR RGD; 620920; Ppp2r2c. DR InterPro; IPR000009; Pp2A_PR55. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR PANTHER; PTHR11871; Pp2A_PR55; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG. KW Repeat; WD repeat. FT CHAIN 1 447 Serine/threonine-protein phosphatase 2A FT 55 kDa regulatory subunit B gamma FT isoform. FT /FTId=PRO_0000071432. FT REPEAT 22 61 WD 1. FT REPEAT 87 128 WD 2. FT REPEAT 171 209 WD 3. FT REPEAT 220 260 WD 4. FT REPEAT 279 317 WD 5. FT REPEAT 334 375 WD 6. FT REPEAT 410 446 WD 7. SQ SEQUENCE 447 AA; 51474 MW; DE16E4EFC775F3C5 CRC64; MGEDTDTRKI NHSFLRDHSY VTEADVISTV EFNHTGELLA TGDKGGRVVI FQREPESKNA PHSQGEYDVY STFQSHEPEF DYLKSLEIEE KINKIKWLPQ QNAAHSLLST NDKTIKLWKI TERDKRPEGY NLKDEEGKLK DLSTVTSLQV PVLKPMDLMV EVSPRRIFAN GHTYHINSIS VNSDCETYMS ADDLRINLWH LAITDRSFNI VDIKPANMED LTEVITASEF HPHHCNLFVY SSSKGSLRLC DMRAAALCDK HSKLFEEPED PSNRSFFSEI ISSVSDVKFS HSGRYMLTRD YLTVKVWDLN MEARPIETYQ VHDYLRSKLC SLYESDCIFD KFECAWNGSD SVIMTGAYNN FFRMFDRNTK RDVTLEASRE SSKPRAVLKP RRVCVGGKRR RDDISVDSLD FTKKILHTAW HPAENIIAIA ATNNLYIFQD KVNSDMH // ID 2ACA_HUMAN Reviewed; 1150 AA. AC Q06190; Q06189; Q9NPQ5; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 23-JAN-2007, entry version 62. DE Serine/threonine-protein phosphatase 2A 72/130 kDa regulatory subunit DE B (PP2A, subunit B, B''-PR72/PR130) (PP2A, subunit B, B72/B130 DE isoforms) (PP2A, subunit B, PR72/PR130 isoforms) (PP2A, subunit B, R3 DE isoform). GN Name=PPP2R3A; Synonyms=PPP2R3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ALTERNATIVE RP SPLICING. RC TISSUE=Fetal brain; RX MEDLINE=93315512; PubMed=8392071; RA Hendrix P., Mayer-Jaekel R.E., Cron P., Goris J., Hofsteenge J., RA Merlevede W., Hemmings B.A.; RT "Structure and expression of a 72-kDa regulatory subunit of protein RT phosphatase 2A. Evidence for different size forms produced by RT alternative splicing."; RL J. Biol. Chem. 268:15267-15276(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 768-1150. RG The European IMAGE consortium; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=PR130; Synonyms=130 kDa; CC IsoId=Q06190-1; Sequence=Displayed; CC Name=PR72; Synonyms=72 kDa; CC IsoId=Q06190-2; Sequence=VSP_005107, VSP_005108; CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, CC muscle and kidney. 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; L07590; AAB02613.1; -; mRNA. DR EMBL; L12146; AAB02614.1; -; mRNA. DR EMBL; AL389975; CAB97532.1; -; mRNA. DR PIR; A47114; A47114. DR PIR; B47114; B47114. DR UniGene; Hs.518155; -. DR Ensembl; ENSG00000073711; Homo sapiens. DR KEGG; hsa:5523; -. DR HGNC; HGNC:9307; PPP2R3A. DR MIM; 604944; gene. DR LinkHub; Q06190; -. DR ArrayExpress; Q06190; -. DR GermOnline; ENSG00000073711; Homo sapiens. DR RZPD-ProtExp; C0756; -. DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc. DR GO; GO:0006470; P:protein amino acid dephosphorylation; ISS:UniProtKB. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR002048; EF_hand_Ca_bd. DR Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1. DR Pfam; PF00036; efhand; 1. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; 2. KW Alternative splicing; Calcium; Direct protein sequencing; KW Polymorphism; Repeat. FT CHAIN 1 1150 Serine/threonine-protein phosphatase 2A FT 72/130 kDa regulatory subunit B. FT /FTId=PRO_0000071443. FT DOMAIN 758 793 EF-hand 1. FT DOMAIN 972 1007 EF-hand 2. FT CA_BIND 985 996 Potential. FT COMPBIAS 670 695 Pro-rich. FT VAR_SEQ 1 621 Missing (in isoform PR72). FT /FTId=VSP_005107. FT VAR_SEQ 622 665 MQILQETLTTSSQANLSVCRSPVGDKAKDTTSAVLIQQTPE FT VIK -> MMIKETSLRRDPDLRGELAFLARGCDFVLPSRFK FT KRLKSFQQTQ (in isoform PR72). FT /FTId=VSP_005108. FT VARIANT 745 745 D -> N (in dbSNP:rs16843645). FT /FTId=VAR_022095. SQ SEQUENCE 1150 AA; 130278 MW; 97A31BA4206518A3 CRC64; MAATYRLVVS TVNHYSSVVI DRRFEQAIHY CTGTCHTFTH GIDCIVVHHS VCADLLHIPV SQFKDADLNS MFLPHENGLS SAEGDYPQQA FTGIPRVKRG STFQNTYNLK DIAGEAISFA SGKIKEFSFE KLKNSNHAAY RKGRKVKSDS FNRRSVDLDL LCGHYNNDGN APSFGLLRSS SVEEKPLSHR NSLDTNLTSM FLQNFSEEDL VTQILEKHKI DNFSSGTDIK MCLDILLKCS EDLKKCTDII KQCIKKKSGS SISEGSGNDT ISSSETVYMN VMTRLASYLK KLPFEFMQSG NNEALDLTEL ISNMPSLQLT PFSPVFGTEQ PPKYEDVVQL SASDSGRFQT IELQNDKPNS RKMDTVQSIP NNSTNSLYNL EVNDPRTLKA VQVQSQSLTM NPLENVSSDD LMETLYIEEE SDGKKALDKG QKTENGPSHE LLKVNEHRAE FPEHATHLKK CPTPMQNEIG KIFEKSFVNL PKEDCKSKVS KFEEGDQRDF TNSSSQEEID KLLMDLESFS QKMETSLREP LAKGKNSNFL NSHSQLTGQT LVDLEPKSKV SSPIEKVSPS CLTRIIETNG HKIEEEDRAL LLRILESIED FAQELVECKS SRGSLSQEKE MMQILQETLT TSSQANLSVC RSPVGDKAKD TTSAVLIQQT PEVIKIQNKP EKKPGTPLPP PATSPSSPRP LSPVPHVNNV VNAPLSINIP RFYFPEGLPD TCSNHEQTLS RIETAFMDIE EQKADIYEMG KIAKVCGCPL YWKAPMFRAA GGEKTGFVTA QSFIAMWRKL LNNHHDDASK FICLLAKPNC SSLEQEDFIP LLQDVVDTHP GLTFLKDAPE FHSRYITTVI QRIFYTVNRS WSGKITSTEI RKSNFLQTLA LLEEEEDINQ ITDYFSYEHF YVIYCKFWEL DTDHDLYISQ ADLSRYNDQA SSSRIIERIF SGAVTRGKTI QKEGRMSYAD FVWFLISEED KRNPTSIEYW FRCMDVDGDG VLSMYELEYF YEEQCERMEA MGIEPLPFHD LLCQMLDLVK PAVDGKITLR DLKRCRMAHI FYDTFFNLEK YLDHEQRDPF AVQKDVENDG PEPSDWDRFA AEEYETLVAE ESAQAQFQEG FEDYETDEPA SPSEFGNKSN KILSASLPEK CGKLQSVDEE // ID 2ACC_HUMAN Reviewed; 414 AA. AC Q9Y5P8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 20-FEB-2007, entry version 54. DE Serine/threonine-protein phosphatase 2A 48 kDa regulatory subunit B DE (PP2A, subunit B, PR48 isoform). GN Name=PPP2R3B; Synonyms=PPP2R3L; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX MEDLINE=20094981; PubMed=10629059; RX DOI=10.1128/MCB.20.3.1021-1029.2000; RA Yan Z., Fedorov S.A., Mumby M.C., Williams R.S.; RT "PR48, a novel regulatory subunit of protein phosphatase 2A, interacts RT with cdc6 and modulates DNA replication in human cells."; RL Mol. Cell. Biol. 20:1021-1029(2000). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. Interacts with amino-terminal region (AA 2 to 181) of CC CDC6. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Contains 1 EF-hand 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; AF135016; AAD38515.1; -; mRNA. DR UniGene; Hs.124942; -. DR Ensembl; ENSG00000167393; Homo sapiens. DR HGNC; HGNC:13417; PPP2R3B. DR MIM; 300339; gene. DR LinkHub; Q9Y5P8; -. DR ArrayExpress; Q9Y5P8; -. DR GermOnline; ENSG00000167393; Homo sapiens. DR RZPD-ProtExp; IOH10291; -. DR RZPD-ProtExp; IOH3323; -. DR RZPD-ProtExp; T2829; -. DR RZPD-ProtExp; U0613; -. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0000158; F:protein phosphatase type 2A activity; ISS:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; ISS:UniProtKB. DR GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc. DR GO; GO:0006470; P:protein amino acid dephosphorylation; ISS:UniProtKB. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR002048; EF_hand_Ca_bd. DR Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; 1. KW Calcium; Nuclear protein. FT CHAIN 1 414 Serine/threonine-protein phosphatase 2A FT 48 kDa regulatory subunit B. FT /FTId=PRO_0000071444. FT DOMAIN 227 262 EF-hand. FT CA_BIND 240 251 Potential. SQ SEQUENCE 414 AA; 47661 MW; FF8592E7B2E4F2B5 CRC64; MDDMGLVAKA CGCPLYWKGP LFYGAGGERT GSVSVHKFVA MWRKILQNCH DDAAKFVHLL MSPGCNYLVQ EDFVPFLQDV VNTHPGLSFL KEASEFHSRY ITTVIQRIFY AVNRSWSGRI TCAELRRSSF LQNVALLEEE ADINQLTEFF SYEHFYVIYC KFWELDTDHD LLIDADDLAR HNDHALSTKM IDRIFSGAVT RGRKVQKEGK ISYADFVWFL ISEEDKKTPT SIEYWFRCMD LDGDGALSMF ELEYFYEEQC RRLDSMAIEA LPFQDCLCQM LDLVKPRTEG KITLQDLKRC KLANVFFDTF FNIEKYLDHE QKEQISLLRD GDSGGPELSD WEKYAAEEYD ILVAEETAGE PWEDGFEAEL SPVEQKLSAL RSPLAQRPFF EAPSPLGAVD LYEYACGDED LEPL // ID 2AD1_SCHPO Reviewed; 548 AA. AC Q10428; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 23-JAN-2007, entry version 43. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE delta 1 isoform (PP2A, B subunit, B' delta 1 isoform). GN Name=par1; Synonyms=pbp1; ORFNames=SPCC188.02; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=20221714; PubMed=10757751; RA Jiang W., Hallberg R.L.; RT "Isolation and characterization of par1(+) and par2(+): two RT Schizosaccharomyces pombe genes encoding B' subunits of protein RT phosphatase 2A."; RL Genetics 154:1025-1038(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [3] RP IDENTIFICATION, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX MEDLINE=21275457; PubMed=11380623; RA Tanabe O., Hirata D., Usui H., Nishito Y., Miyakawa T., Igarashi K., RA Takeda M.; RT "Fission yeast homologues of the B' subunit of protein phosphatase 2A: RT multiple roles in mitotic cell division and functional interaction RT with calcineurin."; RL Genes Cells 6:455-473(2001). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. Has a role in cell shape control and septum CC formation. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- INTERACTION: CC Q9P7A0:sgo1; NbExp=1; IntAct=EBI-989357, EBI-989427; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B 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; AL049662; CAB41222.1; -; Genomic_DNA. DR PIR; T41182; T41182. DR IntAct; Q10428; -. DR KEGG; spo:SPCC188.02; -. DR GeneDB_Spombe; SPCC188.02; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-000142-MONOMER; -. DR ArrayExpress; Q10428; -. DR GO; GO:0000935; C:barrier septum; IDA:GeneDB_SPombe. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0005816; C:spindle pole body; IDA:GeneDB_SPombe. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0031029; P:regulation of septation initiation signaling; IMP:GeneDB_SPombe. DR GO; GO:0006950; P:response to stress; IMP:GeneDB_SPombe. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Complete proteome; Nuclear protein. FT CHAIN 1 548 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit delta 1 FT isoform. FT /FTId=PRO_0000071469. SQ SEQUENCE 548 AA; 63346 MW; A15FD882D516F88A CRC64; MKGIKSKMLS RGKSQDTQKS SKKKESKKSN SHDSSKAPKE SPSTDPNGSV IGAQNDFLTV PKHSGKKVPI DTTPTPRDEI LLENVRTVRK QRSSLYHISE NRNLVRLPSF TDVPVNKWHS LALEKLEQCC VVFDFNDPST DLYGKEVKRE ALQDLIDLIS VRKEAIDESL YPSIVHMFAV NVFRPLPPPS NPPGEIMDLE EDEPALEVAW PHLHLVYDFF LRFFESPSLN TSVAKVYINQ KFIRKLLVLF DSEDPRERDF LKTTLHRIYG KFLSLRAFIR RSINNLFLQF VYENEQFNGI AELLEILGSI INGFALPLKE EHKIFLSRVL IPLHKAKSLP LYYPQIAYGI VQFVEKDSSV TEEVVLGLLR YWPKVNSSKE VLFLNEIEDI IEVMEPSEFL KIQVPLFHKL ATSISSQNFQ VAERALYFFN NDYFVHLVEE NVDIILPIIY PALFEISKSH WNRVIHSMVC NVLKLFMDIN PSLFDEVDAE YSESRRKKED EEIIREERWT ILENIAKENA MKLKSQNPTT VHSTTERLKK LSLDYTNG // ID 2AD2_SCHPO Reviewed; 627 AA. AC P78759; DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1999, sequence version 2. DT 23-JAN-2007, entry version 39. DE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit DE delta 2 isoform (PP2A, B subunit, B' delta 2 isoform). GN Name=par2; Synonyms=pbp2; ORFNames=SPAC6F12.12; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR RP LOCATION. RX MEDLINE=21275457; PubMed=11380623; RA Tanabe O., Hirata D., Usui H., Nishito Y., Miyakawa T., Igarashi K., RA Takeda M.; RT "Fission yeast homologues of the B' subunit of protein phosphatase 2A: RT multiple roles in mitotic cell division and functional interaction RT with calcineurin."; RL Genes Cells 6:455-473(2001). RN [2] RP NUCLEOTIDE SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=20221714; PubMed=10757751; RA Jiang W., Hallberg R.L.; RT "Isolation and characterization of par1(+) and par2(+): two RT Schizosaccharomyces pombe genes encoding B' subunits of protein RT phosphatase 2A."; RL Genetics 154:1025-1038(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 215-627. RC STRAIN=PR745; RX MEDLINE=98162722; PubMed=9501991; DOI=10.1093/dnares/4.6.363; RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.; RT "Identification of open reading frames in Schizosaccharomyces pombe RT cDNAs."; RL DNA Res. 4:363-369(1997). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. Has a role in cell shape control and septum CC formation. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B 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; AB041232; BAB40598.1; -; Genomic_DNA. DR EMBL; Z98533; CAB11096.1; -; Genomic_DNA. DR EMBL; D89107; BAA13770.1; -; mRNA. DR GeneDB_Spombe; SPAC6F12.12; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-000997-MONOMER; -. DR ArrayExpress; P78759; -. DR GO; GO:0000935; C:barrier septum; IDA:GeneDB_SPombe. DR GO; GO:0051286; C:cell tip; IDA:GeneDB_SPombe. DR GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:GeneDB_SPombe. DR GO; GO:0031029; P:regulation of septation initiation signaling; IMP:GeneDB_SPombe. DR GO; GO:0006950; P:response to stress; IMP:GeneDB_SPombe. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR002554; B56. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF01603; B56; 1. KW Complete proteome; Nuclear protein. FT CHAIN 1 627 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit delta 2 FT isoform. FT /FTId=PRO_0000071470. SQ SEQUENCE 627 AA; 72465 MW; 82AD6FD5EA5097C3 CRC64; MKGLRSKFVK ALSLKDEQGS HKNGHSKSHY ISKNGSYVET DDVKHTDTHH SSKHELKKLK SHFLKDTLKH KRNHHANSNN EKHENSDKKI HTTVLASGHE DSDYSTFLPV IETSKVKDAN HFPPNYPEPK NDSVSSNIDE FPNDSISSAS FLSVPQSTPP YLVSQPTPLN KFLAGAENVD IPHSLRPVPR REHSSQFQVS EKRTLVRLPS FDDVHTSERE ELFIKKLEQC NIIFDFNDPS SDLASKEIKR EALLQMIDYV SENRGISSAS LFPYVVNTFS LNVFRPISPA LNDYSSDMFA LDDEPFLEPA WPHLEEVYLL FIKFLESPDF RASKAKSLVD RRFFNRLLAL FDTEDPRERE LLKTTLHRIY GKFLNLRSYI RKSMNNVFLQ FIYEREKFHG IAELLEILGS IINGFAVPLK EEHKIFLSKV LIPLHQTKSV FLYHPQLTYC IVQFIDKDPS LTKAVLTGIL KYWPRINSFK ELLFLNEIED IFEVLEPSEF VNIMSPLFQQ LARSISSMHF QVAERALCLW SNEYFTSLVS QNVVTLLPII YPSLYKTANE HWNSTIQAIA CNVLQIFVDM DADFFNGLVE DYKQAIIKQE EVMIIRKQQW CQIEALAAEN KPTDYLR // ID 2AMD_PSEPS Reviewed; 54 AA. AC P81593; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 1. DT 31-OCT-2006, entry version 22. DE 2-aminomuconate deaminase (EC 3.5.99.5) (Fragment). OS Pseudomonas pseudoalcaligenes. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=330; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=JS45; RX MEDLINE=98233748; PubMed=9573204; RA He Z., Spain J.C.; RT "A novel 2-aminomuconate deaminase in the nitrobenzene degradation RT pathway of Pseudomonas pseudoalcaligenes JS45."; RL J. Bacteriol. 180:2502-2506(1998). CC -!- FUNCTION: Converts 2-aminomuconate to 4-oxalocrotonate, an CC intermediate step in the biodegradation of nitrobenzene. CC -!- CATALYTIC ACTIVITY: 2-aminomuconate + H(2)O = 4-oxalocrotonate + CC NH(3). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=67 uM for 2-aminomuconate; CC Vmax=125 umol/min/mg enzyme with glucose as substrate; CC pH dependence: CC Optimum pH is 6.6; CC -!- PATHWAY: Nitrobenzene degradation. CC -!- SUBUNIT: Homohexamer. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR GO; GO:0050540; F:2-aminomuconate deaminase activity; IEA:EC. DR InterPro; IPR013813; YjgF/chorismate_mutase-like. KW Direct protein sequencing; Hydrolase. FT CHAIN 1 >54 2-aminomuconate deaminase. FT /FTId=PRO_0000064358. FT NON_TER 54 54 SQ SEQUENCE 54 AA; 5582 MW; E4DA7200DA1FCEA3 CRC64; STLSSNDAKV VDGKATPLGS FPHVKRAGDF LYVSGTSSRR PDNTIAGAEL DSTS // ID 2B11_HUMAN Reviewed; 266 AA. AC P04229; O62869; P13758; Q06662; Q30116; Q30117; Q95461; Q9BCL7; AC Q9GIK5; Q9MXZ0; Q9MXZ5; Q9TQ91; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2003, sequence version 2. DT 23-JAN-2007, entry version 66. DE HLA class II histocompatibility antigen, DRB1-1 beta chain precursor DE (MHC class I antigen DRB1*1) (DR-1) (DR1). GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*0101). RX MEDLINE=85216509; PubMed=3858829; RA Bell J.I., Estess P., St John T., Saiki R., Watling D.L., Erlich H.A., RA McDevitt H.O.; RT "DNA sequence and characterization of human class II major RT histocompatibility complex beta chains from the DR1 haplotype."; RL Proc. Natl. Acad. Sci. U.S.A. 82:3405-3409(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*0101). RX MEDLINE=86055719; PubMed=2998758; RA Tonnelle C., Demars R., Long E.O.; RT "DO beta: a new beta chain gene in HLA-D with a distinct regulation of RT expression."; RL EMBO J. 4:2839-2847(1985). RN [3] RP NUCLEOTIDE SEQUENCE OF 1-29. RX MEDLINE=93216303; PubMed=8462990; DOI=10.1007/BF00216386; RA Louis P., Eliaou J.F., Kerlan-Candon S., Pinet V., Vincent R., RA Clot J.; RT "Polymorphism in the regulatory region of HLA-DRB genes correlating RT with haplotype evolution."; RL Immunogenetics 38:21-26(1993). RN [4] RP NUCLEOTIDE SEQUENCE OF 43-115 (DRB1*0101 AND DRB1*0102). RC TISSUE=Blood; RA Arnaiz-Villena A.; RT "HLA class II polymorphism."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-266 (DRB1*0102). RX MEDLINE=88229101; PubMed=2453563; RA Hurley C.K., Ziff B.L., Silver J., Gregersen P.K., Hartzman R., RA Johnson A.H.; RT "Polymorphism of the HLA-DR1 haplotype in American blacks. RT Identification of a DR1 beta-chain determinant recognized in the mixed RT lymphocyte reaction."; RL J. Immunol. 140:4019-4023(1988). RN [6] RP NUCLEOTIDE SEQUENCE OF 35-122 (DRB1*0102). RA Hashemi S., Couture C., Cole R., Buyse I.; RT "Identification and sequencing of a novel DRB1*01 allele."; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*0103). RX MEDLINE=90111153; PubMed=1688595; RA Coppin H.L., Avoustin P., Fabron J., Huchenq A., Garnier J.-M., RA Thomsen M., De Preval C.; RT "Evolution of the HLA-DR1 gene family. Structural and functional RT analysis of the new allele 'DR-BON'."; RL J. Immunol. 144:984-989(1990). RN [8] RP NUCLEOTIDE SEQUENCE OF 30-266 (DRB1*0104). RA Middleton D., Versluis L.F., Tilanus M.G.J.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE OF 35-123 (DRB1*0105). RA Kashiwase K., Akaza T., Juji T.; RT "HLA-DRB1 new alleles."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (DRB1*0106). RX MEDLINE=99217676; PubMed=10203026; RX DOI=10.1034/j.1399-0039.1999.530313.x; RA Palou E., Mongay L., Arias M.T., Isart F., Suarez B., Masso M., RA Fabregat V., Martorell J., Gaya A.; RT "Identification of a novel DRB1-allele (DRB1*0106) by sequence-based RT typing."; RL Tissue Antigens 53:308-310(1999). RN [11] RP NUCLEOTIDE SEQUENCE OF 35-123 (DRB1*0107). RA Dormoy A., Froelich N., Leisenbach R., Tongio M.M.; RT "A new HLA-DRB1*01 allele."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE OF 35-123 (DRB1*0107). RA Voorter C.E., Hepkema B., Lems S., van den Berg-Loonen E.; RT "A new HLA DRB1 allele identified by sequence based typing."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [13] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219. RX MEDLINE=94195388; PubMed=8145819; DOI=10.1038/368215a0; RA Stern L.J., Brown J.H., Jardetzky T.J., Gorga J.C., Urban R.G., RA Strominger J.L., Wiley D.C.; RT "Crystal structure of the human class II MHC protein HLA-DR1 complexed RT with an influenza virus peptide."; RL Nature 368:215-221(1994). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219. RX MEDLINE=93302847; PubMed=8316295; DOI=10.1038/364033a0; RA Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G., RA Strominger J.L., Wiley D.C.; RT "Three-dimensional structure of the human class II histocompatibility RT antigen HLA-DR1."; RL Nature 364:33-39(1993). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH SEB. RX MEDLINE=94203282; PubMed=8152483; DOI=10.1038/368711a0; RA Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., RA Chi Y.I., Stauffacher C., Strominger J.L., Wiley D.C.; RT "Three-dimensional structure of a human class II histocompatibility RT molecule complexed with superantigen."; RL Nature 368:711-718(1994). RN [16] RP DISEASE. RX MEDLINE=22870318; PubMed=14508706; DOI=10.1086/378097; RA Rossman M.D., Thompson B., Frederick M., Maliarik M., Iannuzzi M.C., RA Rybicki B.A., Pandey J.P., Newman L.S., Magira E., Beznik-Cizman B., RA Monos D.; RT "HLA-DRB1*1101: a significant risk factor for sarcoidosis in blacks RT and whites."; RL Am. J. Hum. Genet. 73:720-735(2003). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The following alleles of DRB1-1 are known: CC DRB1*0101, DRB1*0102, DRB1*0103, DRB1*0104, DRB1*0105, DRB1*0106 CC and DRB1*0107. The sequence shown is that of DRB1*0101. CC -!- DISEASE: Allelic variation at the HLA-DRB1 locus is a major CC contributor to genetic predisposition for sarcoidosis CC [MIM:181000]. Sarcoidosis is a disease of unknown aetiology in CC which there are chronic inflammatory granulomatous lesions in CC lymph nodes and other organs. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M11161; AAA59781.1; -; mRNA. DR EMBL; X03069; CAA26873.1; -; mRNA. DR EMBL; X64547; CAA45845.1; -; Genomic_DNA. DR EMBL; AF029288; AAF65497.1; -; Genomic_DNA. DR EMBL; AF029293; AAF65502.1; -; Genomic_DNA. DR EMBL; M21008; AAA59780.1; -; mRNA. DR EMBL; Z50871; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M33600; AAA59782.1; -; mRNA. DR EMBL; X99896; CAA68171.1; -; mRNA. DR EMBL; AB015184; BAA28761.1; -; Genomic_DNA. DR EMBL; AF089723; AAD51131.1; -; Genomic_DNA. DR EMBL; AJ303118; CAC19693.1; -; Genomic_DNA. DR EMBL; AJ276206; CAC27123.1; -; Genomic_DNA. DR PIR; D24669; HLHU1B. DR PIR; I56072; I56072. DR PIR; PH0147; PH0147. DR UniGene; Hs.534322; -. DR PDB; 1AQD; X-ray; B/E/H/K=30-227. DR PDB; 1BX2; X-ray; B/E=32-222. DR PDB; 1DLH; X-ray; B/E=32-219. DR PDB; 1FYT; X-ray; B=30-221. DR PDB; 1JWM; X-ray; B=30-219. DR PDB; 1JWS; X-ray; B=30-219. DR PDB; 1JWU; X-ray; B=30-219. DR PDB; 1KG0; X-ray; B=32-219. DR PDB; 1KLG; X-ray; B=30-219. DR PDB; 1KLU; X-ray; B=30-219. DR PDB; 1LO5; X-ray; B=30-219. DR PDB; 1SEB; X-ray; B/F=30-221. DR PDB; 1SJE; X-ray; B=30-219. DR PDB; 1SJH; X-ray; B=30-219. DR PDB; 1T5W; X-ray; B/E=30-219. DR PDB; 1T5X; X-ray; B=30-219. DR Ensembl; ENSG00000196126; Homo sapiens. DR KEGG; hsa:3123; -. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR MIM; 181000; phenotype. DR LinkHub; P04229; -. DR ArrayExpress; P04229; -. DR GermOnline; ENSG00000196126; Homo sapiens. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Immune response; Membrane; MHC II; KW Polymorphism; Signal; Transmembrane. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-1 beta chain. FT /FTId=PRO_0000018949. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Potential. FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. FT VARIANT 39 39 Q -> E (in allele DRB1*0107). FT /FTId=VAR_016740. FT VARIANT 74 74 G -> R (in allele DRB1*0105). FT /FTId=VAR_016741. FT VARIANT 96 96 L -> I (in allele DRB1*0103). FT /FTId=VAR_016710. FT VARIANT 99 99 Q -> D (in allele DRB1*0103; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016711. FT VARIANT 100 100 R -> A (in allele DRB1*0106; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016742. FT VARIANT 100 100 R -> E (in allele DRB1*0103; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016712. FT VARIANT 106 106 T -> N (in allele DRB1*0104). FT /FTId=VAR_016713. FT VARIANT 114 114 V -> A (in allele DRB1*0102). FT /FTId=VAR_016714. FT VARIANT 115 115 G -> V (in allele DRB1*0102, allele FT DRB1*0104 and allele DRB1*0106). FT /FTId=VAR_016715. FT VARIANT 253 253 Q -> E (in allele DRB1*0102). FT /FTId=VAR_016716. FT CONFLICT 25 25 P -> R (in Ref. 1). FT CONFLICT 80 80 T -> E (in Ref. 1). FT CONFLICT 100 103 RRAA -> KRGQ (in Ref. 1). FT CONFLICT 192 192 T -> I (in Ref. 1). FT STRAND 36 47 FT TURN 48 51 FT STRAND 52 61 FT TURN 62 63 FT STRAND 64 70 FT TURN 71 73 FT STRAND 75 80 FT HELIX 81 83 FT HELIX 84 92 FT HELIX 94 101 FT TURN 102 102 FT HELIX 103 106 FT TURN 107 107 FT HELIX 108 115 FT TURN 116 121 FT STRAND 127 134 FT STRAND 138 140 FT STRAND 142 154 FT STRAND 157 162 FT TURN 163 164 FT TURN 169 170 FT STRAND 171 173 FT STRAND 180 182 FT STRAND 184 192 FT TURN 196 197 FT STRAND 199 205 FT TURN 207 208 FT STRAND 213 218 SQ SEQUENCE 266 AA; 29914 MW; CC9CC7E2D0DD036C CRC64; MVCLKLPGGS CMTALTVTLM VLSSPLALAG DTRPRFLWQL KFECHFFNGT ERVRLLERCI YNQEESVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQR RAAVDTYCRH NYGVGESFTV QRRVEPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B14_HUMAN Reviewed; 266 AA. AC P13760; O19717; O19739; P13759; Q29875; Q30145; Q9GIX9; Q9GIY4; AC Q9MY13; Q9XRY5; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 20-FEB-2007, entry version 70. DE HLA class II histocompatibility antigen, DRB1-4 beta chain precursor DE (MHC class I antigen DRB1*4) (DR-4) (DR4). GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (DRB1*0401). RX MEDLINE=87250499; PubMed=3036826; RA Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A., RA Rask L.; RT "Class II genes of the human major histocompatibility complex. RT Organization and evolutionary relationship of the DR beta genes."; RL J. Biol. Chem. 262:8748-8758(1987). RN [2] RP ERRATUM, AND SEQUENCE REVISION. RA Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A., RA Rask L.; RL J. Biol. Chem. 263:8551-8551(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (DRB1*0401). RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (DRB1*0401). RX MEDLINE=87317627; PubMed=3476943; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (DRB1*0401). RX MEDLINE=85270485; PubMed=3860851; RA Spies T., Sorrentino R., Boss J.M., Okada K., Strominger J.L.; RT "Structural organization of the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 82:5165-5169(1985). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (DRB1*0401). RX MEDLINE=97253496; PubMed=9098937; RA Thonnard J., Gervais T., Heusterpreute M., Mersch G., De Canck I., RA De Greef C., Demanet C., Van Waeyenberge C.; RT "A new silent mutation at codon 35 in exon 2 yielding a DRB1*04012 RT allele."; RL Tissue Antigens 49:274-276(1997). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*0402). RX MEDLINE=22246460; PubMed=12358860; RX DOI=10.1046/j.1365-2370.2002.00354.x; RA Ramon D., Corell A., Cox S.T., Soteriou B., Madrigal J.A., RA Marsh S.G.E.; RT "Complete cDNA sequences of the HLA-DRB1*0402 and DRB1*11041 RT alleles."; RL Eur. J. Immunogenet. 29:453-455(2002). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115 (DRB1*0403). RC TISSUE=Blood; RA Arnaiz-Villena A.; RT "HLA class II polymorphism."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-122 (DRB1*0403). RA Greville W.D., van Eijck A., Dunckley H.; RT "New HLA class II (DRB1) alleles detected by sequencing-based RT typing."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (DRB1*0403). RA Guttridge M.G., Hammond L.; RT "Confirmatory sequence of HLA-DRB1*04032."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*0404). RX MEDLINE=85296375; PubMed=3875800; DOI=10.1038/317166a0; RA Cairns J.S., Curtsinger J.M., Dahl C.A., Freeman S., Alter B.J., RA Bach F.H.; RT "Sequence polymorphism of HLA DR beta 1 alleles relating to T-cell- RT recognized determinants."; RL Nature 317:166-168(1985). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-123 (DRB1*0404). RX MEDLINE=86206008; PubMed=3458223; RA Gregersen P.K., Shen M., Song Q.-L., Merryman P., Degar S., Seki T., RA Maccari J., Goldberg D., Murphy H., Schwenzer J., Wang C.Y., RA Winchester R.J., Nepom G.T., Silver J.; RT "Molecular diversity of HLA-DR4 haplotypes."; RL Proc. Natl. Acad. Sci. U.S.A. 83:2642-2646(1986). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*0411). RA Zhao W., Fernandez-Vina M.A., Stastny P.; RT "Full cDNA sequence of HLA-DRB1*0411."; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [14] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH A COLLAGEN RP PEPTIDE. RX MEDLINE=98014591; PubMed=9354468; DOI=10.1016/S1074-7613(00)80369-6; RA Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C.; RT "X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed RT with a peptide from human collagen II."; RL Immunity 7:473-481(1997). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The following alleles of DRB1-4 are known: CC DRB1*0401, DRB1*0402, DRB1*0403, DRB1*0404 and DRB1*0411. The CC sequence shown is that of DRB1*0401. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M20548; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M20549; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M20550; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137064; CAC19360.1; -; Genomic_DNA. DR EMBL; M17381; AAA59805.1; -; mRNA. DR EMBL; K02776; AAA59808.1; -; Genomic_DNA. DR EMBL; X96851; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ297586; CAC08826.2; -; mRNA. DR EMBL; AF029269; AAF65479.1; -; Genomic_DNA. DR EMBL; AF112876; AAD29581.1; -; Genomic_DNA. DR EMBL; AJ295845; CAC08181.1; -; Genomic_DNA. DR EMBL; X02902; CAA26660.1; -; mRNA. DR EMBL; M15069; AAA59809.1; -; mRNA. DR EMBL; L42143; AAA67104.1; -; mRNA. DR PIR; A94681; A29310. DR PIR; I79419; I79419. DR UniGene; Hs.534322; -. DR UniGene; Hs.652969; -. DR PDB; 1D5M; X-ray; B=30-221. DR PDB; 1D5X; X-ray; B=30-221. DR PDB; 1D5Z; X-ray; B=30-221. DR PDB; 1D6E; X-ray; B=30-221. DR PDB; 1J8H; X-ray; B=30-221. DR PDB; 2SEB; X-ray; B=30-221. DR IntAct; P13760; -. DR Ensembl; ENSG00000196753; Homo sapiens. DR KEGG; hsa:3126; -. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR LinkHub; P13760; -. DR ArrayExpress; P13760; -. DR GermOnline; ENSG00000196126; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; TAS:UniProtKB. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR GO; GO:0009405; P:pathogenesis; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Immune response; Membrane; MHC II; KW Polymorphism; Signal; Transmembrane. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-4 beta chain. FT /FTId=PRO_0000018950. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Potential. FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. FT VARIANT 86 86 D -> S (in allele DRB1*0411; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016673. FT VARIANT 96 96 L -> I (in allele DRB1*0402). FT /FTId=VAR_016674. FT VARIANT 99 99 Q -> D (in allele DRB1*0402; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016675. FT VARIANT 100 100 K -> E (in allele DRB1*0402). FT /FTId=VAR_016676. FT VARIANT 100 100 K -> R (in allele DRB1*0403, allele FT DRB1*0404 and allele DRB1*0411). FT /FTId=VAR_016677. FT VARIANT 103 103 A -> E (in allele DRB1*0403 and allele FT DRB1*0411). FT /FTId=VAR_016678. FT VARIANT 115 115 G -> V (in allele DRB1*0402, allele FT DRB1*0403, allele DRB1*0404 and allele FT DRB1*0411). FT /FTId=VAR_016679. FT CONFLICT 154 154 G -> A (in Ref. 4). FT STRAND 36 47 FT TURN 48 51 FT STRAND 52 61 FT TURN 62 63 FT STRAND 64 70 FT TURN 71 73 FT STRAND 75 80 FT HELIX 81 83 FT HELIX 84 91 FT TURN 92 92 FT HELIX 94 101 FT TURN 102 102 FT HELIX 103 106 FT TURN 107 107 FT HELIX 108 115 FT HELIX 116 118 FT TURN 119 121 FT STRAND 127 132 FT STRAND 143 154 FT STRAND 157 162 FT TURN 163 164 FT STRAND 169 173 FT STRAND 180 182 FT STRAND 184 191 FT TURN 196 197 FT STRAND 199 205 FT TURN 207 208 FT STRAND 213 218 SQ SEQUENCE 266 AA; 30112 MW; 8116E91DA38294E5 CRC64; MVCLKFPGGS CMAALTVTLM VLSSPLALAG DTRPRFLEQV KHECHFFNGT ERVRFLDRYF YHQEEYVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQK RAAVDTYCRH NYGVGESFTV QRRVYPEVTV YPAKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKTG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSLT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B17_HUMAN Reviewed; 266 AA. AC P13761; O46699; O46872; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 20-FEB-2007, entry version 61. DE HLA class II histocompatibility antigen, DRB1-7 beta chain precursor DE (MHC class I antigen DRB1*7) (DR-7) (DR7). GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*0701). RX MEDLINE=87260902; PubMed=3110774; RA Young J.A.T., Wilkinson D., Bodmer W.F., Trowsdale J.; RT "Sequence and evolution of HLA-DR7- and -DRw53-associated beta-chain RT genes."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4929-4933(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (DRB1*0701). RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 OF 35-115 (DRB1*0703). RC TISSUE=Blood; RA Buyse I.M., Couture C., Ouellet S., Hashemi-tavoularis S.; RT "Identification of novel DR7, DRB5 and DQB1*03 alleles using the RT CANTYPE assay."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-117 (DRB1*704). RC TISSUE=Blood; RX MEDLINE=21017543; PubMed=11144299; RX DOI=10.1034/j.1399-0039.2000.560514.x; RA Darke C., Guttridge M.G., Street J., Thompson J., Thomas M.; RT "Molecular, serological and genetic studies on two new HLA-DRB1 RT alleles - HLA-DRB1*0704 and HLA-DRB1*1507."; RL Tissue Antigens 56:467-469(2000). RN [5] RP ASSOCIATION WITH SUSCEPTIBILITY TO HEPATITIS C VIRUS. RX MEDLINE=20075909; PubMed=10609818; DOI=10.1016/S0140-6736(99)91443-5; RG Hepatitis C European Network for Cooperative Research; RA Thursz M., Yallop R., Goldin R., Trepo C., Thomas H.C.; RT "Influence of MHC class II genotype on outcome of infection with RT hepatitis C virus."; RL Lancet 354:2119-2124(1999). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The following alleles of DRB1-7 are known: CC DRB1*0701, DRB1*0703 and DRB1*0704 (DRB1*07ROS). The sequence CC shown is that of DRB1*0701. Allele DRB1*0701 is associated with CC persistent hepatitis C virus (HCV) infections [MIM:609532]. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M16941; AAA36282.1; -; mRNA. DR EMBL; BC001023; AAH01023.1; -; mRNA. DR EMBL; Y13785; CAA74112.1; -; Genomic_DNA. DR EMBL; Y16224; CAA76123.1; -; Genomic_DNA. DR PIR; A28031; A28031. DR UniGene; Hs.534322; -. DR HSSP; P01903; 1JWU. DR SMR; P13761; 30-219. DR Ensembl; ENSG00000196753; Homo sapiens. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR MIM; 609532; phenotype. DR ArrayExpress; P13761; -. DR GermOnline; ENSG00000196126; Homo sapiens. DR GO; GO:0016020; C:membrane; TAS:UniProtKB. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR GO; GO:0006955; P:immune response; TAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Polymorphism; Signal; KW Transmembrane. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-7 beta chain. FT /FTId=PRO_0000018951. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Potential. FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 216 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. FT VARIANT 58 58 R -> S (in allele DRB1*0703). FT /FTId=VAR_016680. FT VARIANT 106 106 T -> N (in allele DRB1*0704). FT /FTId=VAR_016681. FT VARIANT 107 107 V -> Y (in allele DRB1*0704; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016682. SQ SEQUENCE 266 AA; 29822 MW; 439B6AFA553F162C CRC64; MVCLKLPGGS CMAALTVTLM VLSSPLALAG DTQPRFLWQG KYKCHFFNGT ERVQFLERLF YNQEEFVRFD SDVGEYRAVT ELGRPVAESW NSQKDILEDR RGQVDTVCRH NYGVGESFTV QRRVHPEVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVM SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B18_HUMAN Reviewed; 266 AA. AC Q30134; O19718; O19788; Q29968; Q30108; Q30115; Q9BCP0; Q9BCP1; AC Q9BCP2; Q9BD33; Q9TQ37; Q9UIM9; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2003, sequence version 2. DT 20-FEB-2007, entry version 49. DE HLA class II histocompatibility antigen, DRB1-8 beta chain precursor DE (MHC class I antigen DRB1*8) (DR-8) (DR8) (DRw8). GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*0802). RX MEDLINE=89233296; PubMed=2497068; RA Jonsson A.K., Andersson L., Rask L.; RT "A cellular and functional split in the DRw8 haplotype is due to a RT single amino acid replacement (DR beta ser 57- asp 57)."; RL Immunogenetics 29:308-316(1989). RN [2] RP NUCLEOTIDE SEQUENCE OF 1-21. RX MEDLINE=94148705; PubMed=8106268; DOI=10.1016/0198-8859(93)90531-5; RA Emery P., Mach B., Reith W.; RT "The different level of expression of HLA-DRB1 and -DRB3 genes is RT controlled by conserved isotypic differences in promoter sequence."; RL Hum. Immunol. 38:137-147(1993). RN [3] RP NUCLEOTIDE SEQUENCE OF 32-115 (DRB1*0801). RX MEDLINE=87317627; PubMed=3476943; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123. RX MEDLINE=91065701; PubMed=1979063; RA Van Kerckhove C., Melin-Aldana H., Elma M.S., Luyrink L., Donnelly P., RA Taylor J., Maksymowych W.P., Lovell D.J., Choi E., Glass D.N.; RT "A distinct HLA-DRw8 haplotype characterizes patients with juvenile RT rheumatoid arthritis."; RL Immunogenetics 32:304-308(1990). RN [5] RP NUCLEOTIDE SEQUENCE OF 35-123 (DRB1*0801). RA Dormoy A., Froelich N., Weschler B., Tongio M.M.; RT "A new DRB1*08 allele."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE OF 35-123 (DRB1*0804). RC TISSUE=Blood; RA Hurley C., Tang T., Li L.; RT "Human leukocyte antigen class II DRB1*0804 variant."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE OF 35-208 (DRB1*0801). RA Greville W.D.; RT "SBT of DRB1*0801, exons two and three."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-115 (DRB1*0803). RX MEDLINE=90077529; PubMed=2592019; RA Abe A., Ito I., Ohkubo M., Kaneko T., Ito K., Kato H., Kashiwagi N., RA Obata F.; RT "Two distinct subtypes of the HLA-DRw12 haplotypes in the Japanese RT population detected by nucleotide sequence analysis and RT oligonucleotide genotyping."; RL Immunogenetics 30:422-426(1989). RN [9] RP NUCLEOTIDE SEQUENCE OF 43-120 (DRB1*0801). RA Eberle M., Asu U., Taylor M., Hunter J.B., Fuller T.C., Maurer D.; RT "Identification of a putative DR8 founder haplotype containing a novel RT DRB1*08 allele."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-122 (DRB1*0804). RC TISSUE=Blood; RX MEDLINE=94295583; PubMed=8023844; RA Titus-Trachtenberg E.A., Rickards O., De Stefano G.F., Erlich H.A.; RT "Analysis of HLA class II haplotypes in the Cayapa Indians of Ecuador: RT a novel DRB1 allele reveals evidence for convergent evolution and RT balancing selection at position 86."; RL Am. J. Hum. Genet. 55:160-167(1994). RN [11] RP NUCLEOTIDE SEQUENCE OF 124-217. RX MEDLINE=89278667; PubMed=2471740; RA Gorski J.; RT "HLA-DR beta-chain polymorphism. Second domain polymorphism reflects RT evolutionary relatedness of alleles and may explain public serologic RT epitopes."; RL J. Immunol. 143:329-333(1989). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 256-266. RX MEDLINE=86206008; PubMed=3458223; RA Gregersen P.K., Shen M., Song Q.-L., Merryman P., Degar S., Seki T., RA Maccari J., Goldberg D., Murphy H., Schwenzer J., Wang C.Y., RA Winchester R.J., Nepom G.T., Silver J.; RT "Molecular diversity of HLA-DR4 haplotypes."; RL Proc. Natl. Acad. Sci. U.S.A. 83:2642-2646(1986). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The following alleles of DRB1-8 are known: DRB1*0801 CC (Dw8.1), DRB1*0802 (Dw8.2; DRB1L), DRB1*0803 (Dw8.3) and CC DRB1*0804. The sequence shown is that of DRB1*0801. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M26038; AAA59794.1; -; mRNA. DR EMBL; S69987; AAD14052.1; -; Genomic_DNA. DR EMBL; M17386; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M60216; AAA36298.1; -; Genomic_DNA. DR EMBL; AJ249626; CAB56284.1; -; Genomic_DNA. DR EMBL; AF330103; AAK08504.1; -; Genomic_DNA. DR EMBL; AY028515; AAK31608.1; -; Genomic_DNA. DR EMBL; AY028514; AAK31608.1; JOINED; Genomic_DNA. DR EMBL; AY028517; AAK31609.1; -; Genomic_DNA. DR EMBL; AY028516; AAK31609.1; JOINED; Genomic_DNA. DR EMBL; AY028519; AAK31610.1; -; Genomic_DNA. DR EMBL; AY028518; AAK31610.1; JOINED; Genomic_DNA. DR EMBL; M27511; AAA59817.1; -; Genomic_DNA. DR EMBL; AF144105; AAD38374.1; -; Genomic_DNA. DR EMBL; L10402; AAA51400.1; -; Genomic_DNA. DR EMBL; M15074; AAA59810.1; -; mRNA. DR PIR; A45856; A45856. DR PIR; F60748; F60748. DR PIR; I51875; I51875. DR PIR; I54473; I54473. DR PIR; I68778; I68778. DR PIR; PH0160; PH0160. DR PIR; PT0161; PT0161. DR UniGene; Hs.534322; -. DR HSSP; P01903; 1JWU. DR SMR; Q30134; 34-220. DR Ensembl; ENSG00000196444; Homo sapiens. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR RZPD-ProtExp; I0328; -. DR RZPD-ProtExp; I0335; -. DR RZPD-ProtExp; IOH13934; -. DR RZPD-ProtExp; IOH14748; -. DR RZPD-ProtExp; IOH21889; -. DR RZPD-ProtExp; IOH27972; -. DR RZPD-ProtExp; IOH3310; -. DR RZPD-ProtExp; IOH4220; -. DR RZPD-ProtExp; IOH6782; -. DR RZPD-ProtExp; IOH7183; -. DR RZPD-ProtExp; T7421; -. DR RZPD-ProtExp; T7448; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Polymorphism; Signal; KW Transmembrane. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-8 beta chain. FT /FTId=PRO_0000018952. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Potential. FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. FT VARIANT 86 86 S -> D (in allele DRB1*0802 and allele FT DRB1*0804; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016683. FT VARIANT 96 96 F -> I (in allele DRB1*0803). FT /FTId=VAR_016684. FT VARIANT 115 115 G -> V (in allele DRB1*0804). FT /FTId=VAR_016685. SQ SEQUENCE 266 AA; 30004 MW; D452D1C3A75CEA31 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TGECYFFNGT ERVRFLDRYF YNQEEYVRFD SDVGEYRAVT ELGRPSAEYW NSQKDFLEDR RALVDTYCRH NYGVGESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWSAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B19_HUMAN Reviewed; 266 AA. AC Q9TQE0; Q30149; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 23-JAN-2007, entry version 41. DE HLA class II histocompatibility antigen, DRB1-9 beta chain precursor DE (MHC class I antigen DRB1*9) (DR-9) (DR9). GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*0901). RC TISSUE=Blood; RX MEDLINE=98450507; PubMed=9777332; RX DOI=10.1046/j.1365-2370.1998.00105.x; RA Martinez-Quiles N., Martin-Villa J.M., Ferre-Lopez S., RA Moreno-Pelayo M.A., Martinez-Laso J., Perez-Blas M., Alegre R., RA Arnaiz-Villena A.; RT "Complete cDNA sequence of the HLA-DRB1*09012 allele."; RL Eur. J. Immunogenet. 25:307-309(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-115 (DRB1*0901). RX MEDLINE=87317627; PubMed=3476943; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-115. RX PubMed=2023919; RA Gyllensten U.B., Sundvall M., Erlich H.A.; RT "Allelic diversity is generated by intraexon sequence exchange at the RT DRB1 locus of primates."; RL Proc. Natl. Acad. Sci. U.S.A. 88:3686-3690(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-266. RX PubMed=3466180; RA Gregersen P.K., Moriuchi T., Karr R.W., Obata F., Moriuchi J., RA Maccari J., Goldberg D., Winchester R.J., Silver J.; RT "Polymorphism of HLA-DR beta chains in DR4, -7, and -9 haplotypes: RT implications for the mechanisms of allelic variation."; RL Proc. Natl. Acad. Sci. U.S.A. 83:9149-9153(1986). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The only allele of DRB1-9 known is DRB1*0901 which CC is shown here. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; U66826; AAD43829.1; -; mRNA. DR EMBL; M17387; AAA36297.1; -; mRNA. DR PIR; A25925; A25925. DR PIR; C28515; C28515. DR HSSP; P01903; 1JWU. DR SMR; Q9TQE0; 30-219. DR Ensembl; ENSG00000196753; Homo sapiens. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR ArrayExpress; Q9TQE0; -. DR GermOnline; ENSG00000198502; Homo sapiens. DR RZPD-ProtExp; I0328; -. DR RZPD-ProtExp; I0335; -. DR RZPD-ProtExp; IOH13934; -. DR RZPD-ProtExp; IOH14748; -. DR RZPD-ProtExp; IOH21889; -. DR RZPD-ProtExp; IOH27972; -. DR RZPD-ProtExp; IOH3310; -. DR RZPD-ProtExp; IOH4220; -. DR RZPD-ProtExp; IOH6782; -. DR RZPD-ProtExp; IOH7183; -. DR RZPD-ProtExp; T7421; -. DR RZPD-ProtExp; T7448; -. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Signal; KW Transmembrane. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-9 beta chain. FT /FTId=PRO_0000018953. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Potential. FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 216 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. SQ SEQUENCE 266 AA; 29826 MW; AD46B4AD27BAD8F2 CRC64; MVCLKLPGGS CMAALTVTLM VLSSPLALAG DTQPRFLKQD KFECHFFNGT ERVRYLHRGI YNQEENVRFD SDVGEYRAVT ELGRPVAESW NSQKDFLERR RAEVDTVCRH NYGVGESFTV QRRVHPEVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVM SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B1A_HUMAN Reviewed; 266 AA. AC Q30167; Q9MYF5; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 28-NOV-2006, entry version 42. DE HLA class II histocompatibility antigen, DRB1-10 beta chain precursor DE (MHC class I antigen DRB1*10) (DRw10). GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*1001). RX MEDLINE=88170832; PubMed=2450924; RA Merryman P., Gregersen P.K., Lee S., Silver J., Nunez-Roldan A., RA Crapper R., Winchester R.; RT "Nucleotide sequence of a DRw10 beta chain cDNA clone. Identity of the RT third D region with that of the DRw53 allele of the beta 2 locus and RT as the probable site encoding a polymorphic MHC class II epitope."; RL J. Immunol. 140:2447-2452(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (DRB1*1001). RA Woelpl A.; RT "Sequence of an HLA-DRB gene."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The only allele of DRB1-10 known is DRB1*1001 which CC is shown here. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M20138; AAA59832.1; -; mRNA. DR EMBL; AF225565; AAF65542.1; -; Genomic_DNA. DR HSSP; P01903; 1D5M. DR SMR; Q30167; 30-219. DR Ensembl; ENSG00000196753; Homo sapiens. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Signal; KW Transmembrane. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-10 beta chain. FT /FTId=PRO_0000018954. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Potential. FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 216 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. SQ SEQUENCE 266 AA; 30074 MW; 378B630DA8C214E5 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEEV KFECHFFNGT ERVRLLERRV HNQEEYARYD SDVGEYRAVT ELGRPDAEYW NSQKDLLERR RAAVDTYCRH NYGVGESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKTG VVSTGLIQNE DWTFQTLVML ETVPQSGEVY TCQVEHPSVM SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLP PTGFLS // ID 2B1B_HUMAN Reviewed; 266 AA. AC P20039; Q30006; Q9GIX8; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 20-FEB-2007, entry version 57. DE HLA class II histocompatibility antigen, DRB1-11 beta chain precursor DE (MHC class I antigen DRB1*11) (DR-5) (DR5) (DRw11). GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*1101). RX MEDLINE=86140021; PubMed=3456344; RA Tieber V.L., Abruzzini L.F., Didier D.K., Schwartz B.D., Rotwein P.; RT "Complete characterization and sequence of an HLA class II DR beta RT chain cDNA from the DR5 haplotype."; RL J. Biol. Chem. 261:2738-2742(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (DRB1*1103). RX MEDLINE=88314191; PubMed=3137159; RA Steimle V., Hinkkanen A., Schlesier M., Epplen J.T.; RT "A novel HLA-DR beta I sequence from the DRw11 haplotype."; RL Immunogenetics 28:208-210(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB1*1104). RX MEDLINE=22246460; PubMed=12358860; RX DOI=10.1046/j.1365-2370.2002.00354.x; RA Ramon D., Corell A., Cox S.T., Soteriou B., Madrigal J.A., RA Marsh S.G.E.; RT "Complete cDNA sequences of the HLA-DRB1*0402 and DRB1*11041 RT alleles."; RL Eur. J. Immunogenet. 29:453-455(2002). RN [4] RP NUCLEOTIDE SEQUENCE OF 124-217. RX MEDLINE=89278667; PubMed=2471740; RA Gorski J.; RT "HLA-DR beta-chain polymorphism. Second domain polymorphism reflects RT evolutionary relatedness of alleles and may explain public serologic RT epitopes."; RL J. Immunol. 143:329-333(1989). RN [5] RP ASSOCIATION WITH SUSCEPTIBILITY TO HEPATITIS C VIRUS. RX MEDLINE=20075909; PubMed=10609818; DOI=10.1016/S0140-6736(99)91443-5; RG Hepatitis C European Network for Cooperative Research; RA Thursz M., Yallop R., Goldin R., Trepo C., Thomas H.C.; RT "Influence of MHC class II genotype on outcome of infection with RT hepatitis C virus."; RL Lancet 354:2119-2124(1999). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The following alleles of DRB1-11 are known: CC DRB1*1101, DRB1*1103 and DRB1*1104. The sequence shown is that of CC DRB1*1101. Allele DRB1*1101 is associated with self-limiting CC hepatitis C virus (HCV) infections [MIM:609532]. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M11867; AAA36274.1; -; mRNA. DR EMBL; M22050; AAA59713.1; -; Genomic_DNA. DR EMBL; M21966; AAA59713.1; JOINED; Genomic_DNA. DR EMBL; M22047; AAA59713.1; JOINED; Genomic_DNA. DR EMBL; M22048; AAA59713.1; JOINED; Genomic_DNA. DR EMBL; M22049; AAA59713.1; JOINED; Genomic_DNA. DR EMBL; AJ297587; CAC08827.1; -; mRNA. DR PIR; A25324; A25324. DR PIR; F60748; F60748. DR PIR; I54448; I54448. DR PIR; PH0153; PH0153. DR UniGene; Hs.534322; -. DR HSSP; P01903; 1JWU. DR SMR; P20039; 34-220. DR Ensembl; ENSG00000196444; Homo sapiens. DR KEGG; hsa:3127; -. DR H-InvDB; HIX0005754; -. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR MIM; 609532; phenotype. DR LinkHub; P20039; -. DR RZPD-ProtExp; I0328; -. DR RZPD-ProtExp; I0335; -. DR RZPD-ProtExp; IOH13934; -. DR RZPD-ProtExp; IOH14748; -. DR RZPD-ProtExp; IOH21889; -. DR RZPD-ProtExp; IOH27972; -. DR RZPD-ProtExp; IOH3310; -. DR RZPD-ProtExp; IOH4220; -. DR RZPD-ProtExp; IOH6782; -. DR RZPD-ProtExp; IOH7183; -. DR RZPD-ProtExp; T7421; -. DR RZPD-ProtExp; T7448; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Polymorphism; Signal; KW Transmembrane. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-11 beta chain. FT /FTId=PRO_0000018955. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Potential. FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. FT VARIANT 100 100 R -> E (in allele DRB1*1103; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016717. FT VARIANT 115 115 G -> V (in allele DRB1*1103 and allele FT DRB1*1104). FT /FTId=VAR_016718. SQ SEQUENCE 266 AA; 30160 MW; 6CFC0D44391B1059 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TSECHFFNGT ERVRFLDRYF YNQEEYVRFD SDVGEFRAVT ELGRPDEEYW NSQKDFLEDR RAAVDTYCRH NYGVGESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PRGFLS // ID 2B31_HUMAN Reviewed; 266 AA. AC P79483; Q95359; Q96H16; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 31-OCT-2006, entry version 46. DE HLA class II histocompatibility antigen, DRB3-1 beta chain precursor DE (MHC class I antigen DRB3*1). GN Name=HLA-DRB3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (DRB3*0101). RX MEDLINE=86257409; PubMed=3459965; RA Gorski J., Mach B.; RT "Polymorphism of human Ia antigens: gene conversion between two DR RT beta loci results in a new HLA-D/DR specificity."; RL Nature 322:67-70(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB3*0101). RA Kim K.H., Kang J.H., Maeng C.Y., Han H., Park J.H., Hahm K.S., RA Kim K.L.; RT "Cloning and nucleotide sequence analysis of HLA-DRB3*01012 from EBV- RT transformed Korean B-cell line by sequence based typing."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB3*0101). RC TISSUE=Blood; RX MEDLINE=97378895; PubMed=9234492; RA Martinez-Quiles N., Martin-Villa J.M., Martinez-Laso J., RA Perez-Blas M., Ferre-Lopez S., Moreno-Pelayo M.A., Alvarez-Tejado M., RA Arnaiz-Villena A.; RT "Description of two new HLA-DRB alleles (DRB1*0310 and DRB3*01012) RT found in a Spanish infant."; RL Tissue Antigens 49:658-661(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (DRB3*0101). RA Steiner N.K., Coquillard G.J., Hurley C.K.; RT "Novel HLA-DRB3 allele."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (DRB3*0101). RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (DRB3*0101). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-117 (DRB3*0102). RX MEDLINE=97378897; PubMed=9234494; RA Guttridge M.G., Hudson L., Williams H., Dunn P., Duy S., Darke C.; RT "Identification and nucleotide sequence of two novel DRB3 alleles, RT DRB3*0102 and DRB3*010133."; RL Tissue Antigens 49:665-667(1997). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-217. RX MEDLINE=89278667; PubMed=2471740; RA Gorski J.; RT "HLA-DR beta-chain polymorphism. Second domain polymorphism reflects RT evolutionary relatedness of alleles and may explain public serologic RT epitopes."; RL J. Immunol. 143:329-333(1989). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The following alleles of DRB3-1 are known: DRB3*0301 CC and DRB3*0102. The sequence shown is that of DRB3*0101. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X04055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X04058; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U95819; AAD00819.1; -; mRNA. DR EMBL; U66825; AAD43828.1; -; mRNA. DR EMBL; AF199236; AAF13065.2; -; mRNA. DR EMBL; Z84814; CAB06607.1; -; Genomic_DNA. DR EMBL; BC008987; AAH08987.1; -; mRNA. DR EMBL; Y08063; CAA69301.1; -; Genomic_DNA. DR PIR; B60748; B60748. DR PIR; PT0164; PT0164. DR UniGene; Hs.534322; -. DR HSSP; P01903; 1JWU. DR SMR; P79483; 34-220. DR Ensembl; ENSG00000196101; Homo sapiens. DR KEGG; hsa:3125; -. DR HGNC; HGNC:4951; HLA-DRB3. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Polymorphism; Signal; KW Transmembrane. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB3-1 beta chain. FT /FTId=PRO_0000018956. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Potential. FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. FT VARIANT 40 40 R -> C (in allele DRB3*0102). FT /FTId=VAR_016686. SQ SEQUENCE 266 AA; 29962 MW; 2FC3AE68D3B10EAD CRC64; MVCLKLPGGS SLAALTVTLM VLSSRLAFAG DTRPRFLELR KSECHFFNGT ERVRYLDRYF HNQEEFLRFD SDVGEYRAVT ELGRPVAESW NSQKDLLEQK RGRVDNYCRH NYGVGESFTV QRRVHPQVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SALTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B32_HUMAN Reviewed; 266 AA. AC P01913; O78049; P79663; Q29721; Q29809; Q30144; Q9MYA4; Q9MYH3; AC Q9MYH4; Q9TPB5; Q9TQ21; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2003, sequence version 3. DT 20-FEB-2007, entry version 60. DE HLA class II histocompatibility antigen, DRB3-2 beta chain precursor DE (MHC class I antigen DRB3*2). GN Name=HLA-DRB3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (DRB3*0201). RX PubMed=11894954; RA Long E.O., Wake C.T., Gorski J., Mach B.; RT "Complete sequence of an HLA-DR beta chain deduced from a cDNA clone RT and identification of multiple non-allelic DR beta chain genes."; RL EMBO J. 2:389-394(1983). RN [2] RP NUCLEOTIDE SEQUENCE OF 30-266 (DRB3*0201). RX MEDLINE=84031722; PubMed=6414998; DOI=10.1016/0198-8859(83)90089-7; RA Long E.O., Gorski J., Rollini P., Wake C.T., Strubin M., RA Rabourdin-Combe C., Mach B.; RT "Molecular analysis of the genes for human class II antigens of the RT major histocompatibility complex."; RL Hum. Immunol. 8:113-121(1983). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (DRB3*0201). RX MEDLINE=87317627; PubMed=3476943; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [4] RP NUCLEOTIDE SEQUENCE OF 35-122 (DRB3*0202). RA Greville W.D., Ng G., Kennedy A., Dunckley H.; RT "New HLA class II (DRB3) allele detected by sequencing-based typing."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE OF 43-120 (DRB3*0202). RA Eberle M., Asu U., Taylor M., Hunter J.B., Fuller T.C., Maurer D.; RT "Identification of a putative DR8 founder haplotype containing a novel RT DRB1*0801 allele."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (DRB3*0205). RX MEDLINE=97306279; PubMed=9162096; DOI=10.1007/s002510050248; RA Robbins F., Hurley C.K., Tang T., Yao H., Lin Y.S., Wade J., RA Goeken N., Hartzman R.J.; RT "Diversity associated with the second expressed HLA-DRB locus in the RT human population."; RL Immunogenetics 46:104-110(1997). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (DRB3*0206). RX MEDLINE=97387748; PubMed=9243765; RA Hashemi-Tavoularis S., Couture C., Buyse I.M.; RT "Identification of new DRB1*01 (DRB1*01022), DRB1*14 (DRB1*1428) and RT DRB3* (DRB3*0206) alleles."; RL Tissue Antigens 50:89-93(1997). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (DRB3*0207). RX MEDLINE=98049199; PubMed=9389331; RA Voorter C.E., Hentges F., van den Berg-Loonen E.M.; RT "Identification of a new DRB3*02 allele (DRB3*0207) by sequence-based RT typing."; RL Tissue Antigens 50:552-554(1997). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (DRB3*0208). RC TISSUE=Blood; RX MEDLINE=99017598; PubMed=9802612; RA Hashemi-tavoularis S., Ouellet S., Sengar D.P.S., Buyse I.M.; RT "A novel DRB3 allele (DRB3*0208), a new allelic variant of DRB1*1502 RT (DRB1*15023) and two new DQB1 (DQB1*03012 and DQB1*0614) alleles."; RL Tissue Antigens 52:294-299(1998). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (DRB3*0209). RX MEDLINE=20412567; PubMed=10958362; RX DOI=10.1034/j.1399-0039.2000.560113.x; RA Morabito A., Pera C., Longo A., Delfino L., Ferrara G.B.; RT "Identification of a new DRB3*02 allelic variant (DRB3*0209) by high- RT resolution sequence-based typing."; RL Tissue Antigens 56:90-94(2000). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (DRB3*0210 AND DRB3*0211). RX MEDLINE=20548616; PubMed=11098940; RX DOI=10.1034/j.1399-0039.2000.560412.x; RA Balas A., Santos S., Aviles M.J., Garcia-Sanchez F., Lillo R., RA Vicario J.L.; RT "Identification by sequencing based typing and complete coding region RT analysis of three new HLA class II alleles: DRB3*0210, DRB3*0211 and RT DQB1*0310."; RL Tissue Antigens 56:380-384(2000). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The following alleles of DRB3-2 are known: CC DRB3*0201, DRB3*0202, DRB3*0205, DRB3*0206, DRB3*0207, DRB3*0208, CC DRB3*0209, DRB3*0210 and DRB3*0211. The sequence shown is that of CC DRB3*0202. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; V00522; CAA23781.1; -; mRNA. DR EMBL; A06800; CAA00596.1; -; Unassigned_RNA. DR EMBL; M17380; AAA59804.1; -; mRNA. DR EMBL; AF177216; AAD53911.1; -; Genomic_DNA. DR EMBL; AF152845; AAD45286.1; -; Genomic_DNA. DR EMBL; U36826; AAB63531.1; -; Genomic_DNA. DR EMBL; X95760; CAA65066.1; -; Genomic_DNA. DR EMBL; Y10180; CAA71253.1; -; Genomic_DNA. DR EMBL; AJ001255; CAA04629.1; -; Genomic_DNA. DR EMBL; AF148518; AAF67837.1; -; Genomic_DNA. DR EMBL; AF192258; AAF26358.1; -; mRNA. DR EMBL; AF192259; AAF26359.1; -; mRNA. DR PIR; E28043; E28043. DR PIR; I37469; HLHU5D. DR PIR; PT0165; PT0165. DR UniGene; Hs.534322; -. DR HSSP; P01903; 1JWU. DR SMR; P01913; 30-219. DR Ensembl; ENSG00000196101; Homo sapiens. DR HGNC; HGNC:4951; HLA-DRB3. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0032395; F:MHC class II receptor activity; NAS:UniProtKB. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Polymorphism; Signal; KW Transmembrane. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB3-2 beta chain. FT /FTId=PRO_0000018957. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Potential. FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. FT VARIANT 59 59 H -> S (in allele DRB3*0210; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016687. FT VARIANT 59 59 H -> Y (in allele DRB3*0205). FT /FTId=VAR_016688. FT VARIANT 66 66 Y -> N (in allele DRB3*0206). FT /FTId=VAR_016689. FT VARIANT 80 80 R -> T (in allele DRB3*0209 and allele FT DRB3*0210). FT /FTId=VAR_016690. FT VARIANT 86 86 D -> S (in allele DRB3*0208; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016691. FT VARIANT 86 86 D -> V (in allele DRB3*0207 and allele FT DRB3*0209). FT /FTId=VAR_016692. FT VARIANT 89 89 Y -> S (in allele DRB3*0209). FT /FTId=VAR_016693. FT VARIANT 96 96 L -> I (in allele DRB3*0211). FT /FTId=VAR_016694. FT VARIANT 115 115 G -> V (in allele DRB3*0201). FT /FTId=VAR_016695. FT VARIANT 193 193 F -> V (in allele DRB3*0210 and allele FT DRB3*0211). FT /FTId=VAR_016696. FT CONFLICT 154 154 G -> A (in Ref. 3). SQ SEQUENCE 266 AA; 29989 MW; F09B5876FDD9484A CRC64; MVCLKLPGGS SLAALTVTLM VLSSRLAFAG DTRPRFLELL KSECHFFNGT ERVRFLERHF HNQEEYARFD SDVGEYRAVR ELGRPDAEYW NSQKDLLEQK RGQVDNYCRH NYGVGESFTV QRRVHPQVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETFPRSGEVY TCQVEHPSVT SPLTVEWSAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2C_DICDI Reviewed; 98 AA. AC P15648; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 31-OCT-2006, entry version 35. DE Protein 2C. GN Name=2C; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=AX2; RX MEDLINE=90205618; PubMed=2157129; RA Ramji D.P., Richards A.J., Jagger P., Bleasby A., Hames B.D.; RT "Two cyclic AMP-regulated genes from Dictyostelium discoideum encode RT homologous proteins."; RL Mol. Microbiol. 4:129-135(1990). CC -!- DEVELOPMENTAL STAGE: Expressed only late in development. Its CC expression ceases upon cell disaggregation but is fully restored CC by exogenous cAMP. CC -!- DOMAIN: May form an extended coil structure. CC -!- SIMILARITY: To D.discoideum protein 7E. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X16827; CAA34727.1; -; mRNA. DR PIR; S08137; S08137. DR DictyBase; DDB0001896; 2C. DR InterPro; IPR008455; Coiled. DR Pfam; PF05710; Coiled; 1. FT CHAIN 1 98 Protein 2C. FT /FTId=PRO_0000064359. FT COMPBIAS 5 26 Ser-rich. FT COMPBIAS 40 94 Gly-rich. SQ SEQUENCE 98 AA; 8836 MW; BD7BFDF649EB1D50 CRC64; MTLFSSISSM SSSMTSSRSS FSSFGSGTSM GSNSIACSVG SGGGGCGSGS GGCGDLTGGA KSSGGSCGGK GGPHNHGHGN GHGPHGHGGK GSGGSCSC // ID 2DMA_HUMAN Reviewed; 261 AA. AC P28067; Q29639; Q29640; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 20-FEB-2007, entry version 65. DE HLA class II histocompatibility antigen, DM alpha chain precursor (MHC DE class II antigen DMA). GN Name=HLA-DMA; Synonyms=DMA, RING6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (DMA*0101). RX MEDLINE=92018223; PubMed=1922365; DOI=10.1038/353571a0; RA Kelly A.P., Monaco J.J., Cho S., Trowsdale J.; RT "A new human HLA class II-related locus, DM."; RL Nature 353:571-573(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-218 (DMA*0102). RX MEDLINE=94041464; PubMed=8225438; DOI=10.1007/BF00171797; RA Sanderson F., Powis S.H., Kelly A.P., Trowsdale J.; RT "Limited polymorphism in HLA-DM does not involve the peptide binding RT groove."; RL Immunogenetics 39:56-58(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-217 (DMA*0103 AND DMA*0104). RX MEDLINE=94299291; PubMed=8026867; DOI=10.1007/BF00188184; RA Carrington M., Harding A.; RT "Sequence analysis of two novel HLA-DMA alleles."; RL Immunogenetics 40:165-165(1994). RN [4] RP FUNCTION. RX MEDLINE=97002457; PubMed=8849454; DOI=10.1126/science.274.5287.618; RA Weber D.A., Evavold B.D., Jensen P.E.; RT "Enhanced dissociation of HLA-DR-bound peptides in the presence of RT HLA-DM."; RL Science 274:618-620(1996). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-230. RX MEDLINE=98439693; PubMed=9768757; DOI=10.1016/S1074-7613(00)80620-2; RA Mosyak L., Zaller D.M., Wiley D.C.; RT "The structure of HLA-DM, the peptide exchange catalyst that loads RT antigen onto class II MHC molecules during antigen presentation."; RL Immunity 9:377-383(1998). CC -!- FUNCTION: Plays a critical role in catalyzing the release of class CC II HLA-associated invariant chain-derived peptides (CLIP) from CC newly synthesized class II HLA molecules and freeing the peptide CC binding site for acquisition of antigenic peptides. CC -!- SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain CC (DMB). CC -!- SUBCELLULAR LOCATION: Endosome; late endosome; late endosomal CC membrane; single-pass type I membrane protein. Lysosome; lysosomal CC membrane; single-pass type I membrane protein. Note=Localizes to CC late endocytic compartment. Associates with lysosome membranes. CC -!- POLYMORPHISM: The following alleles of DMA are known: DMA*0101, CC DMA*0102, DMA*0103 (DMA3.2) and DMA*0104 (DMA3.4). The sequence CC shown is that of DMA*0101. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X62744; CAA44606.1; -; mRNA. DR EMBL; Z24753; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U04878; AAA56994.1; -; Genomic_DNA. DR EMBL; U04877; AAA56993.1; -; Genomic_DNA. DR PIR; I38490; I38490. DR PIR; S17886; S17886. DR UniGene; Hs.351279; -. DR PDB; 1HDM; X-ray; A=27-230. DR DIP; DIP:6184N; -. DR Ensembl; ENSG00000124546; Homo sapiens. DR KEGG; hsa:3108; -. DR H-InvDB; HIX0005763; -. DR HGNC; HGNC:4934; HLA-DMA. DR MIM; 142855; gene. DR ArrayExpress; P28067; -. DR GermOnline; ENSG00000204257; Homo sapiens. DR RZPD-ProtExp; I0353; -. DR RZPD-ProtExp; I0531; -. DR RZPD-ProtExp; IOH12744; -. DR RZPD-ProtExp; RZPDo834A052; -. DR RZPD-ProtExp; RZPDo834G061; -. DR RZPD-ProtExp; RZPDo839F0665; -. DR RZPD-ProtExp; RZPDo839F0675; -. DR GO; GO:0005515; F:protein binding; TAS:ProtInc. DR InterPro; IPR013151; Ig. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001003; MHC_II_alpha_N. DR Pfam; PF00047; ig; 1. DR Pfam; PF00993; MHC_II_alpha; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Immune response; Membrane; MHC II; KW Polymorphism; Signal; Transmembrane. FT SIGNAL 1 26 Potential. FT CHAIN 27 261 HLA class II histocompatibility antigen, FT DM alpha chain. FT /FTId=PRO_0000018958. FT TOPO_DOM 27 233 Lumenal (Potential). FT TRANSMEM 234 254 Potential. FT TOPO_DOM 255 261 Cytoplasmic (Potential). FT DOMAIN 121 215 Ig-like C1-type. FT REGION 27 124 Alpha-1. FT REGION 125 217 Alpha-2. FT REGION 218 233 Connecting peptide (Potential). FT CARBOHYD 41 41 N-linked (GlcNAc...) (Potential). FT DISULFID 147 202 By similarity. FT VARIANT 162 162 H -> Q (in allele DMA*0103 and allele FT DMA*0104). FT /FTId=VAR_016746. FT VARIANT 163 163 D -> H (in allele DMA*0103 and allele FT DMA*0104). FT /FTId=VAR_016747. FT VARIANT 166 166 V -> I (in allele DMA*0102 and allele FT DMA*0104). FT /FTId=VAR_016748. FT VARIANT 181 181 G -> A (in allele DMA*0103). FT /FTId=VAR_016749. FT VARIANT 210 210 R -> C (in allele DMA*0104). FT /FTId=VAR_016750. FT VARIANT 210 210 R -> H (in allele DMA*0103). FT /FTId=VAR_016751. FT STRAND 41 63 FT TURN 64 65 FT STRAND 66 72 FT TURN 73 76 FT STRAND 77 82 FT HELIX 83 88 FT TURN 89 90 FT HELIX 98 111 FT TURN 117 119 FT STRAND 128 135 FT TURN 139 140 FT STRAND 143 155 FT STRAND 157 163 FT TURN 164 165 FT STRAND 174 179 FT TURN 180 182 FT STRAND 183 192 FT TURN 196 197 FT STRAND 200 206 FT TURN 207 210 FT STRAND 211 217 SQ SEQUENCE 261 AA; 29194 MW; 1986C3C1989F02E9 CRC64; MGHEQNQGAA LLQMLPLLWL LPHSWAVPEA PTPMWPDDLQ NHTFLHTVYC QDGSPSVGLS EAYDEDQLFF FDFSQNTRVP RLPEFADWAQ EQGDAPAILF DKEFCEWMIQ QIGPKLDGKI PVSRGFPIAE VFTLKPLEFG KPNTLVCFVS NLFPPMLTVN WHDHSVPVEG FGPTFVSAVD GLSFQAFSYL NFTPEPSDIF SCIVTHEIDR YTAIAYWVPR NALPSDLLEN VLCGVAFGLG VLGIIVGIVL IIYFRKPCSG D // ID 2DMA_MOUSE Reviewed; 261 AA. AC P28078; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 20-FEB-2007, entry version 62. DE Class II histocompatibility antigen, M alpha chain precursor. GN Name=H2-DMa; Synonyms=H2-Ma, Ma; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; RX MEDLINE=92018224; PubMed=1922366; DOI=10.1038/353573a0; RA Cho S., Attaya M., Monaco J.J.; RT "New class II-like genes in the murine MHC."; RL Nature 353:573-576(1991). CC -!- FUNCTION: Plays a critical role in catalyzing the release of class CC II HLA-associated invariant chain-derived peptides (CLIP) from CC newly synthesized class II HLA molecules and freeing the peptide CC binding site for acquisition of antigenic peptides. CC -!- SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain CC (DMB). CC -!- INTERACTION: CC Q31099:H2-DMb2; NbExp=1; IntAct=EBI-1027262, EBI-1027288; CC -!- SUBCELLULAR LOCATION: Endosome; late endosome; late endosomal CC membrane; single-pass type I membrane protein. Lysosome; lysosomal CC membrane; single-pass type I membrane protein. Note=Localizes to CC late endocytic compartment. Associates with lysosome membranes. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X62742; CAA44604.1; -; mRNA. DR PIR; S17888; S17888. DR UniGene; Mm.16373; -. DR PDB; 1K8I; X-ray; A=30-220. DR IntAct; P28078; -. DR Ensembl; ENSMUSG00000037649; Mus musculus. DR KEGG; mmu:14998; -. DR MGI; MGI:95921; H2-DMa. DR ArrayExpress; P28078; -. DR GermOnline; ENSMUSG00000037649; Mus musculus. DR RZPD-ProtExp; IOM16740; -. DR RZPD-ProtExp; IOM18259; -. DR RZPD-ProtExp; IOM18262; -. DR GO; GO:0010008; C:endosome membrane; IDA:MGI. DR GO; GO:0005765; C:lysosomal membrane; IDA:MGI. DR GO; GO:0005771; C:multivesicular body; IDA:MGI. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0019886; P:antigen processing and presentation of exog...; IDA:MGI. DR GO; GO:0051085; P:chaperone cofactor-dependent protein folding; IDA:MGI. DR GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI. DR GO; GO:0050778; P:positive regulation of immune response; IMP:MGI. DR GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:MGI. DR GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI. DR GO; GO:0006461; P:protein complex assembly; IDA:MGI. DR GO; GO:0015031; P:protein transport; IDA:MGI. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001003; MHC_II_alpha_N. DR Gene3D; G3DSA:3.10.320.10; MHC_II_alpha_N; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00993; MHC_II_alpha; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Immune response; Membrane; MHC II; Signal; KW Transmembrane. FT SIGNAL 1 26 Potential. FT CHAIN 27 261 Class II histocompatibility antigen, M FT alpha chain. FT /FTId=PRO_0000018959. FT TOPO_DOM 27 231 Lumenal (Potential). FT TRANSMEM 232 252 Potential. FT TOPO_DOM 253 261 Cytoplasmic (Potential). FT DOMAIN 114 215 Ig-like C1-type. FT REGION 27 124 Alpha-1. FT REGION 125 217 Alpha-2. FT REGION 218 231 Connecting peptide (Potential). FT CARBOHYD 41 41 N-linked (GlcNAc...) (Potential). FT DISULFID 147 202 By similarity. FT STRAND 41 63 FT TURN 64 65 FT STRAND 66 72 FT TURN 73 76 FT STRAND 77 82 FT TURN 83 86 FT HELIX 87 90 FT HELIX 95 110 FT TURN 111 111 FT HELIX 112 116 FT TURN 118 119 FT STRAND 128 135 FT TURN 139 140 FT STRAND 143 155 FT STRAND 157 163 FT TURN 164 165 FT STRAND 166 168 FT STRAND 175 179 FT TURN 180 182 FT STRAND 183 192 FT TURN 196 197 FT STRAND 200 206 FT TURN 207 209 FT STRAND 212 217 SQ SEQUENCE 261 AA; 28950 MW; C8403C76CB54A55C CRC64; MEHEQKSGAV LLRLLRLLWL LPHSWAVLEA STPVLWDDPQ NHTFRHTLFC QDGIPNIGLS ETYDEDELFS FDFSQNTRVP RLPDFAEWAQ GQGDASAIAF GKSFCEMLMR EVSPKLEGQI PVSRGLSVAE VFTLKPLEFG KPNTLVCFIS NLFPPTLTVN WQLHSAPVEG ASPTSISAVD GLTFQAFSYL NFTPEPFDLY SCTVTHEIDR YTAIAYWVPQ NALPSDLLEN ALCGVAFALG VLGTIIGIVF FLCSQRPCSG D // ID 2DMB_HUMAN Reviewed; 263 AA. AC P28068; O77936; Q13012; Q29751; Q9XRX2; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 09-JAN-2007, entry version 68. DE HLA class II histocompatibility antigen, DM beta chain precursor (MHC DE class II antigen DMB). GN Name=HLA-DMB; Synonyms=DMB, RING7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE DMB*0101). RX MEDLINE=92018223; PubMed=1922365; DOI=10.1038/353571a0; RA Kelly A.P., Monaco J.J., Cho S., Trowsdale J.; RT "A new human HLA class II-related locus, DM."; RL Nature 353:571-573(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DMB*0101). RX MEDLINE=94308138; PubMed=8034636; RA Radley E., Alderton R.P., Kelly A., Trowsdale J., Beck S.; RT "Genomic organization of HLA-DMA and HLA-DMB. Comparison of the gene RT organization of all six class II families in the human major RT histocompatibility complex."; RL J. Biol. Chem. 269:18834-18838(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DMB*0101). RX MEDLINE=96144827; PubMed=8568858; DOI=10.1006/jmbi.1996.0001; RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., RA Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., RA Radley E., Thorpe K.L., Trowsdale J.; RT "Evolutionary dynamics of non-coding sequences within the class II RT region of the human MHC."; RL J. Mol. Biol. 255:1-13(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DMB*0101). RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 114-207 (ALLELES DMB*0102 AND RP DMB*0103). RX MEDLINE=94041464; PubMed=8225438; DOI=10.1007/BF00171797; RA Sanderson F., Powis S.H., Kelly A.P., Trowsdale J.; RT "Limited polymorphism in HLA-DM does not involve the peptide binding RT groove."; RL Immunogenetics 39:56-58(1994). RN [6] RP NUCLEOTIDE SEQUENCE OF 121-200 (ALLELE DMB*0104). RX MEDLINE=94011096; PubMed=8406617; DOI=10.1007/BF00184526; RA Carrington M., Yeager M., Mann D.; RT "Characterization of HLA-DMB polymorphism."; RL Immunogenetics 38:446-449(1993). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-207 (ALLELE DMB*0105). RC TISSUE=Blood; RX MEDLINE=97012872; PubMed=9157091; DOI=10.1016/0198-8859(95)00171-9; RA Kim T.-G., Carrington M., Choi H.B., Kim H.Y., Han H.; RT "Three HLA-DMB variants in Korean patients with autoimmune diseases."; RL Hum. Immunol. 46:58-60(1996). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-112 AND 152-207 (ALLELE RP DMB*0106). RX MEDLINE=20340081; PubMed=10885572; RX DOI=10.1034/j.1399-0039.2000.550514.x; RA McTernan C.L., Mijovic C.H., Cockram C.S., Barnett A.H.; RT "The nucleotide sequence of a new DMB allele, DMB*0106."; RL Tissue Antigens 55:470-472(2000). RN [9] RP FUNCTION. RX MEDLINE=97002457; PubMed=8849454; DOI=10.1126/science.274.5287.618; RA Weber D.A., Evavold B.D., Jensen P.E.; RT "Enhanced dissociation of HLA-DR-bound peptides in the presence of RT HLA-DM."; RL Science 274:618-620(1996). RN [10] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-248 AND LEU-251. RX MEDLINE=96338165; PubMed=8757605; RA Copier J., Kleijmeer M.J., Ponnambalam S., Oorschot V., Potter P., RA Trowsdale J., Kelly A.; RT "Targeting signal and subcellular compartments involved in the RT intracellular trafficking of HLA-DMB."; RL J. Immunol. 157:1017-1027(1996). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110, AND MASS RP SPECTROMETRY. RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-218. RX MEDLINE=98439693; PubMed=9768757; DOI=10.1016/S1074-7613(00)80620-2; RA Mosyak L., Zaller D.M., Wiley D.C.; RT "The structure of HLA-DM, the peptide exchange catalyst that loads RT antigen onto class II MHC molecules during antigen presentation."; RL Immunity 9:377-383(1998). CC -!- FUNCTION: Plays a critical role in catalyzing the release of class CC II HLA-associated invariant chain-derived peptides (CLIP) from CC newly synthesized class II HLA molecules and freeing the peptide CC binding site for acquisition of antigenic peptides. CC -!- SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain CC (DMB). CC -!- SUBCELLULAR LOCATION: Endosome; late endosome; late endosomal CC membrane; single-pass type I membrane protein. Lysosome; lysosomal CC membrane; single-pass type I membrane protein. Note=Localizes to CC late endocytic compartment. Associates with lysosome membranes. CC -!- DOMAIN: The YXXZ (Tyr-Xaa-Xaa-Zaa, where Zaa is a hydrophobic CC residue) motif mediates the targeting to the lysosomal CC compartments. CC -!- POLYMORPHISM: The following alleles of DMB are known: DMB*0101, CC DMB*0102, DMB*0103, DMB*0104 (DMB3.4), DMB*0105 and DMB*0106. The CC sequence shown is that of DMB*0101. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; Z23139; CAA80670.1; -; mRNA. DR EMBL; U15085; AAB60387.1; -; mRNA. DR EMBL; X76776; CAA54171.1; -; Genomic_DNA. DR EMBL; X87344; CAA60782.1; -; Genomic_DNA. DR EMBL; BC027175; AAH27175.1; -; mRNA. DR EMBL; Z24750; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z24751; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U00700; AAA03296.1; -; Genomic_DNA. DR EMBL; U16762; AAC50514.1; -; Genomic_DNA. DR EMBL; AF134890; AAD30279.1; -; Genomic_DNA. DR EMBL; AF072680; AAC26112.1; -; Genomic_DNA. DR PIR; I37533; I37533. DR UniGene; Hs.351279; -. DR PDB; 1HDM; X-ray; B=19-218. DR DIP; DIP:6185N; -. DR Ensembl; ENSG00000112091; Homo sapiens. DR KEGG; hsa:3109; -. DR H-InvDB; HIX0005762; -. DR HGNC; HGNC:4935; HLA-DMB. DR MIM; 142856; gene. DR ArrayExpress; P28068; -. DR InterPro; IPR013151; Ig. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001003; MHC_II_alpha_N. DR InterPro; IPR000353; MHC_II_beta_N. DR Gene3D; G3DSA:3.10.320.10; MHC_II_alpha_N; 1. DR Pfam; PF00047; ig; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Glycoprotein; Immune response; Membrane; MHC II; KW Polymorphism; Signal; Transmembrane. FT SIGNAL 1 18 Potential. FT CHAIN 19 263 HLA class II histocompatibility antigen, FT DM beta chain. FT /FTId=PRO_0000018960. FT TOPO_DOM 19 218 Lumenal (Potential). FT TRANSMEM 219 239 Potential. FT TOPO_DOM 240 263 Cytoplasmic (Potential). FT DOMAIN 114 208 Ig-like C1-type. FT REGION 19 112 Beta-1. FT REGION 113 207 Beta-2. FT REGION 208 218 Connecting peptide (Potential). FT MOTIF 248 251 YXXZ motif. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT VARIANT 45 45 S -> F (in allele DMB*0106). FT /FTId=VAR_016752. FT VARIANT 162 162 A -> E (in allele DMB*0102 and allele FT DMB*0106). FT /FTId=VAR_016753. FT VARIANT 162 162 A -> V (in allele DMB*0104 and allele FT DMB*0105). FT /FTId=VAR_016754. FT VARIANT 197 197 I -> T (in allele DMB*0103, allele FT DMB*0104 and allele DMB*0106; FT dbSNP:rs1042337). FT /FTId=VAR_016755. FT MUTAGEN 248 248 Y->A: Abolishes targeting to endosomes FT and results in relocalization to the cell FT membrane. FT MUTAGEN 251 251 L->A: Abolishes targeting to endosomes FT and results in relocalization to the cell FT membrane. FT STRAND 22 32 FT TURN 33 34 FT STRAND 37 46 FT TURN 47 48 FT STRAND 49 55 FT TURN 56 59 FT STRAND 60 63 FT HELIX 71 81 FT TURN 82 82 FT HELIX 84 89 FT HELIX 93 101 FT TURN 102 104 FT HELIX 105 109 FT TURN 110 110 FT STRAND 116 121 FT STRAND 126 128 FT STRAND 130 143 FT STRAND 146 151 FT TURN 152 153 FT STRAND 170 172 FT STRAND 174 182 FT TURN 186 187 FT STRAND 190 195 FT TURN 197 198 FT STRAND 199 201 FT STRAND 203 207 SQ SEQUENCE 263 AA; 28943 MW; 9B50F6CC22B3A4BA CRC64; MITFLPLLLG LSLGCTGAGG FVAHVESTCL LDDAGTPKDF TYCISFNKDL LTCWDPEENK MAPCEFGVLN SLANVLSQHL NQKDTLMQRL RNGLQNCATH TQPFWGSLTN RTRPPSVQVA KTTPFNTREP VMLACYVWGF YPAEVTITWR KNGKLVMPHS SAHKTAQPNG DWTYQTLSHL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGVISW RRAGHSSYTP LPGSNYSEGW HIS // ID 2DMB_MOUSE Reviewed; 261 AA. AC P35737; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 20-FEB-2007, entry version 58. DE Class II histocompatibility antigen, M beta 1 chain precursor (H2-M DE beta 1 chain). GN Name=H2-DMb1; Synonyms=H-2Mb1, Mb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; RX MEDLINE=92018224; PubMed=1922366; DOI=10.1038/353573a0; RA Cho S., Attaya M., Monaco J.J.; RT "New class II-like genes in the murine MHC."; RL Nature 353:573-576(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BALB/c; RX MEDLINE=96163020; PubMed=8575819; DOI=10.1007/s002510050047; RA Peleraux A., Karlsson L., Chambers J., Peterson P.A.; RT "Genomic organization of a mouse MHC class II region including the H2- RT M and Lmp2 loci."; RL Immunogenetics 43:204-214(1996). RN [3] RP SUBCELLULAR LOCATION. RX MEDLINE=96074232; PubMed=7584146; DOI=10.1016/1074-7613(95)90127-2; RA Lindstedt R., Liljedahl M., Peleraux A., Peterson P.A., Karlsson L.; RT "The MHC class II molecule H2-M is targeted to an endosomal RT compartment by a tyrosine-based targeting motif."; RL Immunity 3:561-572(1995). CC -!- FUNCTION: Plays a critical role in catalyzing the release of class CC II HLA-associated invariant chain-derived peptides (CLIP) from CC newly synthesized class II HLA molecules and freeing the peptide CC binding site for acquisition of antigenic peptides. CC -!- SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain CC (DMB). CC -!- SUBCELLULAR LOCATION: Endosome; late endosome; late endosomal CC membrane; single-pass type I membrane protein. Lysosome; lysosomal CC membrane; single-pass type I membrane protein. Note=Localizes to CC late endocytic compartment. Associates with lysosome membranes. CC -!- DOMAIN: The YXXZ (Tyr-Xaa-Xaa-Zaa, where Zaa is a hydrophobic CC residue) motif mediates the targeting to the lysosomal CC compartments. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X62743; CAA44605.1; -; mRNA. DR EMBL; U35323; AAA98931.1; -; Genomic_DNA. DR PIR; S17889; S17889. DR UniGene; Mm.16373; -. DR UniGene; Mm.195060; -. DR HSSP; Q31099; 1K8I. DR SMR; P35737; 20-209. DR Ensembl; ENSMUSG00000037548; Mus musculus. DR KEGG; mmu:14999; -. DR MGI; MGI:95922; H2-DMb1. DR ArrayExpress; P35737; -. DR GermOnline; ENSMUSG00000037548; Mus musculus. DR RZPD-ProtExp; IOM16740; -. DR RZPD-ProtExp; IOM18259; -. DR GO; GO:0019886; P:antigen processing and presentation of exog...; IDA:MGI. DR GO; GO:0051085; P:chaperone cofactor-dependent protein folding; IDA:MGI. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001003; MHC_II_alpha_N. DR InterPro; IPR000353; MHC_II_beta_N. DR Gene3D; G3DSA:3.10.320.10; MHC_II_alpha_N; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Signal; KW Transmembrane. FT SIGNAL 1 18 Potential. FT CHAIN 19 261 Class II histocompatibility antigen, M FT beta 1 chain. FT /FTId=PRO_0000018961. FT TOPO_DOM 19 218 Lumenal (Potential). FT TRANSMEM 219 239 Potential. FT TOPO_DOM 240 261 Cytoplasmic (Potential). FT DOMAIN 114 204 Ig-like C1-type. FT REGION 19 112 Beta-1. FT REGION 113 207 Beta-2. FT REGION 208 218 Connecting peptide (Potential). FT MOTIF 248 251 YXXZ motif. FT CARBOHYD 75 75 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 261 AA; 28899 MW; 4986A222912286D9 CRC64; MAALWLLLLV LSLHCMGAGG FVAHVESTCV LDDAGTPQDF TYCVSFNKDL LACWDPIVGK IVPCEFGVLY PLAENFSRIL NKEESLLQRL QNGLPDCASH TQPFWNALTH RTRPPSVRVA QTTPFNTREP VMLACYVWGF YPADVTITWM KNGQLVPSHS NKEKTAQPNG DWTYQTVSYL ALTPSYGDVY TCVVQHSGTS EPIRGDWTPG LSPIQTVKVS VSAATLGLGF IIFCVGFFRW RKSHSSSYTP LSGSTYPEGR H // ID 2DOA_HUMAN Reviewed; 250 AA. AC P06340; Q9TQC6; Q9TQC7; Q9TQC8; Q9TQC9; Q9TQD0; Q9TQD1; Q9TQD2; AC Q9TQD3; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 20-FEB-2007, entry version 67. DE HLA class II histocompatibility antigen, DO alpha chain precursor (MHC DE class II antigen DOA) (MHC DZ alpha) (MHC DN-alpha). GN Name=HLA-DOA; Synonyms=HLA-DNA, HLA-DZA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DOA*0101). RX MEDLINE=86081729; PubMed=3000765; RA Trowsdale J., Kelly A.; RT "The human HLA class II alpha chain gene DZ alpha is distinct from RT genes in the DP, DQ and DR subregions."; RL EMBO J. 4:2231-2237(1985). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE DOA*0101). RX MEDLINE=89277432; PubMed=2499532; RA Jonsson A.-K., Rask L.; RT "Human class II DNA and DOB genes display low sequence variability."; RL Immunogenetics 29:411-413(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DOA*0101). RX MEDLINE=90316607; PubMed=2370084; RA Young J.A., Trowsdale J.; RT "The HLA-DNA (DZA) gene is correctly expressed as a 1.1 kb mature mRNA RT transcript."; RL Immunogenetics 31:386-388(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DOA*0101). RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DOA*0101). RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 29-250 (ALLELE DOA*0101). RX MEDLINE=99254919; PubMed=10323340; RX DOI=10.1034/j.1399-0039.1999.530406.x; RA Naruse T.K., Kawata H., Anzai T., Takashige N., Kagiya M., Nose Y., RA Nabeya N., Isshiki G., Tatsumi N., Inoko H.; RT "Limited polymorphism in the HLA-DOA gene."; RL Tissue Antigens 53:359-365(1999). CC -!- FUNCTION: Important modulator in the HLA class II restricted CC antigen presentation pathway by interaction with the HLA-DM CC molecule. CC -!- SUBUNIT: Heterodimer of an alpha chain (DOA) and a beta chain CC (DOB). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The only allele of DOA known is DOA*0101 which is CC shown here. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X02882; CAA26635.1; -; Genomic_DNA. DR EMBL; M26039; AAA59716.1; -; mRNA. DR EMBL; M31525; AAA60075.1; -; mRNA. DR EMBL; Z81310; CAB03594.1; -; Genomic_DNA. DR EMBL; BC013183; AAH13183.1; -; mRNA. DR EMBL; AB005991; BAA81787.1; -; Genomic_DNA. DR EMBL; AB005992; BAA81788.1; -; Genomic_DNA. DR EMBL; AB005993; BAA81789.1; -; Genomic_DNA. DR EMBL; AB005994; BAA81790.1; -; Genomic_DNA. DR EMBL; AB005995; BAA81791.1; -; Genomic_DNA. DR EMBL; AB005996; BAA81792.1; -; Genomic_DNA. DR EMBL; AB005997; BAA81793.1; -; Genomic_DNA. DR EMBL; AB005998; BAA81794.1; -; Genomic_DNA. DR PIR; A02216; HLHUDZ. DR UniGene; Hs.631991; -. DR HSSP; P04228; 1F3J. DR Ensembl; ENSG00000112095; Homo sapiens. DR KEGG; hsa:3111; -. DR H-InvDB; HIX0020250; -. DR HGNC; HGNC:4936; HLA-DOA. DR MIM; 142930; gene. DR ArrayExpress; P06340; -. DR GermOnline; ENSG00000204252; Homo sapiens. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001003; MHC_II_alpha_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00993; MHC_II_alpha; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Signal; KW Transmembrane. FT SIGNAL 1 25 Potential. FT CHAIN 26 250 HLA class II histocompatibility antigen, FT DO alpha chain. FT /FTId=PRO_0000018962. FT TOPO_DOM 26 217 Extracellular (Potential). FT TRANSMEM 218 240 Potential. FT TOPO_DOM 241 250 Cytoplasmic (Potential). FT DOMAIN 113 205 Ig-like C1-type. FT REGION 26 110 Alpha-1. FT REGION 111 204 Alpha-2. FT REGION 205 217 Connecting peptide. FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT CARBOHYD 144 144 N-linked (GlcNAc...) (Potential). FT DISULFID 133 189 By similarity. SQ SEQUENCE 250 AA; 27599 MW; FA9482197A02AC85 CRC64; MALRAGLVLG FHTLMTLLSP QEAGATKADH MGSYGPAFYQ SYGASGQFTH EFDEEQLFSV DLKKSEAVWR LPEFGDFARF DPQGGLAGIA AIKAHLDILV ERSNRSRAIN VPPRVTVLPK SRVELGQPNI LICIVDNIFP PVINITWLRN GQTVTEGVAQ TSFYSQPDHL FRKFHYLPFV PSAEDVYDCQ VEHWGLDAPL LRHWELQVPI PPPDAMETLV CALGLAIGLV GFLVGTVLII MGTYVSSVPR // ID 2DOB_HUMAN Reviewed; 273 AA. AC P13765; Q29746; Q29825; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 20-FEB-2007, entry version 69. DE HLA class II histocompatibility antigen, DO beta chain precursor (MHC DE class II antigen DOB). GN Name=HLA-DOB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (DOB*0101). RX MEDLINE=86055719; PubMed=2998758; RA Tonnelle C., Demars R., Long E.O.; RT "DO beta: a new beta chain gene in HLA-D with a distinct regulation of RT expression."; RL EMBO J. 4:2839-2847(1985). RN [2] RP NUCLEOTIDE SEQUENCE (DOB*0101). RX MEDLINE=89277432; PubMed=2499532; RA Jonsson A.-K., Rask L.; RT "Human class II DNA and DOB genes display low sequence variability."; RL Immunogenetics 29:411-413(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (DOB*0101). RX MEDLINE=93085727; PubMed=1453454; RA Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P., RA Trowsdale J.; RT "DNA sequence analysis of 66 kb of the human MHC class II region RT encoding a cluster of genes for antigen processing."; RL J. Mol. Biol. 228:433-441(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (DOB*0101). RC TISSUE=B-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 NUCLEOTIDE SEQUENCE (DOB*0102). RX MEDLINE=87250500; PubMed=3036827; RA Servenius B., Rask L., Peterson P.A.; RT "Class II genes of the human major histocompatibility complex. The DO RT beta gene is a divergent member of the class II beta gene family."; RL J. Biol. Chem. 262:8759-8766(1987). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (DOB*0103). RX MEDLINE=96144827; PubMed=8568858; DOI=10.1006/jmbi.1996.0001; RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., RA Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., RA Radley E., Thorpe K.L., Trowsdale J.; RT "Evolutionary dynamics of non-coding sequences within the class II RT region of the human MHC."; RL J. Mol. Biol. 255:1-13(1996). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-273 (DOB*0104). RX MEDLINE=22337832; PubMed=12445321; RX DOI=10.1034/j.1399-0039.2002.590608.x; RA Naruse T.K., Kawata H., Inoko H., Isshiki G., Yamano K., Hino M., RA Tatsumi N.; RT "The HLA-DOB gene displays limited polymorphism with only one amino RT acid substitution."; RL Tissue Antigens 59:512-519(2002). CC -!- FUNCTION: Important modulator in the HLA class II restricted CC antigen presentation pathway by interaction with the HLA-DM CC molecule. CC -!- SUBUNIT: Heterodimer of an alpha chain (DOA) and a beta chain CC (DOB). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The following alleles of DOB are known: DOB*0101, CC DOB*0102, DOB*0103 and DOB*0104. The sequence shown is that of CC DOB*0101. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; X03066; CAA26870.1; -; mRNA. DR EMBL; M26040; AAA59718.1; -; mRNA. DR EMBL; X66401; CAA47028.1; -; Genomic_DNA. DR EMBL; BC006097; AAH06097.1; -; mRNA. DR EMBL; L29472; AAA59717.1; -; Genomic_DNA. DR EMBL; X87344; CAA60789.1; -; Genomic_DNA. DR EMBL; AB035252; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; S27335; A24669. DR UniGene; Hs.1802; -. DR HSSP; P01903; 1HXY. DR Ensembl; ENSG00000168399; Homo sapiens. DR KEGG; hsa:3112; -. DR H-InvDB; HIX0005756; -. DR HGNC; HGNC:4937; HLA-DOB. DR MIM; 142920; gene. DR ArrayExpress; P13765; -. DR GermOnline; ENSG00000204273; Homo sapiens. DR RZPD-ProtExp; Q0403; -. DR RZPD-ProtExp; RZPDo834A0832; -. DR RZPD-ProtExp; RZPDo834G0831; -. DR GO; GO:0005764; C:lysosome; IDA:MGI. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Polymorphism; Signal; KW Transmembrane. FT SIGNAL 1 26 FT CHAIN 27 273 HLA class II histocompatibility antigen, FT DO beta chain. FT /FTId=PRO_0000018963. FT TOPO_DOM 27 224 Extracellular (Potential). FT TRANSMEM 225 245 Potential. FT TOPO_DOM 246 273 Cytoplasmic (Potential). FT DOMAIN 123 213 Ig-like C1-type. FT REGION 27 120 Beta-1. FT REGION 121 214 Beta-2. FT REGION 215 224 Connecting peptide. FT CARBOHYD 45 45 N-linked (GlcNAc...) (Potential). FT DISULFID 41 105 By similarity. FT DISULFID 143 199 By similarity. FT VARIANT 18 18 R -> Q (in allele DOB*0102). FT /FTId=VAR_016743. FT VARIANT 234 234 L -> F (in allele DOB*0104). FT /FTId=VAR_016745. FT VARIANT 244 244 V -> I (in allele DOB*0103). FT /FTId=VAR_016744. SQ SEQUENCE 273 AA; 30822 MW; C06A1360DCC4AD26 CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSRQA VDGVCRHNYR LGAPFTVGRK VQPEVTVYPE RTPLLHQHNL LHCSVTGFYP GDIKIKWFLN GQEERAGVMS TGPIRNGDWT FQTVVMLEMT PELGHVYTCL VDHSSLLSPV SVEWRAQSEY SWRKMLSGIA AFLLGLIFLL VGIVIQLRAQ KGYVRTQMSG NEVSRAVLLP QSC // ID 2DOB_PANTR Reviewed; 273 AA. AC P18467; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 31-OCT-2006, entry version 43. DE CHLA class II histocompatibility antigen, DO beta chain precursor (MHC DE class II antigen DOB). GN Name=HLA-DOB; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89307404; PubMed=2744808; RA Kasahara M., Klein D., Klein J.; RT "Nucleotide sequence of a chimpanzee DOB cDNA clone."; RL Immunogenetics 30:66-68(1989). CC -!- FUNCTION: Important modulator in the HLA class II restricted CC antigen presentation pathway by interaction with the HLA-DM CC molecule. CC -!- SUBUNIT: Heterodimer of an alpha chain (DOA) and a beta chain CC (DOB). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; M24358; AAA35409.1; -; mRNA. DR PIR; A45879; A45879. DR HSSP; P01903; 1HXY. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR000353; MHC_II_beta_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Signal; KW Transmembrane. FT SIGNAL 1 26 FT CHAIN 27 273 CHLA class II histocompatibility antigen, FT DO beta chain. FT /FTId=PRO_0000018964. FT TOPO_DOM 27 224 Extracellular (Potential). FT TRANSMEM 225 245 Potential. FT TOPO_DOM 246 273 Cytoplasmic (Potential). FT DOMAIN 123 213 Ig-like C1-type. FT REGION 27 120 Beta-1. FT REGION 121 214 Beta-2. FT REGION 215 224 Connecting peptide. FT CARBOHYD 45 45 N-linked (GlcNAc...) (Potential). FT DISULFID 41 105 By similarity. FT DISULFID 143 199 By similarity. SQ SEQUENCE 273 AA; 30922 MW; 8AC0A1F56A06D30D CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSRQA VDGVCRHNYR LGAPFTVGRK VQPEVTVYPE RTPLLHQHNL LHCSVTGFYP GDIKIRWFLN GQEERARVMS TGPIRNGDWT FQTVVMLEMT PELGHVYTCL VDHSSLLSPV SVEWRAQSEY SWKKMLSGIA AFLLGLIFLL VGIVIQLRAQ KGYVRTQMSG NEVSRAVLLP QSC // ID 2DRA_HUMAN Reviewed; 254 AA. AC P01903; Q30160; Q6IAZ1; Q861I2; Q9TP70; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 20-FEB-2007, entry version 75. DE HLA class II histocompatibility antigen, DR alpha chain precursor (MHC DE class II antigen DRA). GN Name=HLA-DRA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=83221632; PubMed=6304715; RA Das H.K., Lawrance S.K., Weissman S.M.; RT "Structure and nucleotide sequence of the heavy chain gene of HLA- RT DR."; RL Proc. Natl. Acad. Sci. U.S.A. 80:3543-3547(1983). RN [2] RP ERRATUM, AND SEQUENCE REVISION. RA Das H.K., Lawrance S.K., Weissman S.M.; RL Proc. Natl. Acad. Sci. U.S.A. 80:7024-7024(1983). RN [3] RP PROTEIN SEQUENCE OF 26-204. RX MEDLINE=82263347; PubMed=6955253; RA Yang C.-Y., Kratzin H., Gotz H., Thinnes F.P., Kruse T., Egert G., RA Pauly E., Kolbel S., Wernet P., Hilschmann N.; RT "Primary structure of class II human histocompatibility antigens. 2nd RT Communication. Amino acid sequence of the N-terminal 179 residues of RT the alpha-chain of an HLA-Dw2/DR2 alloantigen."; RL Hoppe-Seyler's Z. Physiol. Chem. 363:671-676(1982). RN [4] RP PROTEIN SEQUENCE OF 26-60, AND NUCLEOTIDE SEQUENCE [MRNA] OF 32-202 RP AND 204-254. RX MEDLINE=83025073; PubMed=6812963; DOI=10.1016/0092-8674(82)90021-6; RA Larhammar D., Gustafsson K., Claesson L., Bill P., Wiman K., RA Schenning L., Sundelin J., Widmark E., Peterson P.A., Rask L.; RT "Alpha chain of HLA-DR transplantation antigens is a member of the RT same protein superfamily as the immunoglobulins."; RL Cell 30:153-161(1982). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (DR*0101). RX MEDLINE=84057142; PubMed=6416803; RA Kajimura Y., Toyoda H., Sato M., Miyakoshi S., Kaplan S.A., Ike Y., RA Goyert S.M., Silver J., Hawke D., Shively J.E., Suggs S.V., RA Wallace R.B., Itakura K.; RT "Cloning the heavy chain of human HLA-DR antigen using synthetic RT oligodeoxyribonucleotides as hybridization probes."; RL DNA 2:175-182(1983). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84169507; PubMed=6324094; DOI=10.1093/nar/11.24.8663; RA Schamboeck A., Korman A.J., Kamb A., Strominger J.L.; RT "Organization of the transcriptional unit of a human class II RT histocompatibility antigen: HLA-DR heavy chain."; RL Nucleic Acids Res. 11:8663-8675(1983). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (DR*0101). RX MEDLINE=83013020; PubMed=6811954; DOI=10.1038/299750a0; RA Lee J.S., Trowsdale J., Travers P.J., Carey J., Grosveld F., RA Jenkins J., Bodmer W.F.; RT "Sequence of an HLA-DR alpha-chain cDNA clone and intron-exon RT organization of the corresponding gene."; RL Nature 299:750-752(1982). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-242. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-242. RC TISSUE=Blood, 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 [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-254 (DRA*0102). RX MEDLINE=83299916; PubMed=6821129; RA Korman A.J., Auffray C., Schamboeck A., Strominger J.L.; RT "The amino acid sequence and gene organization of the heavy chain of RT the HLA-DR antigen: homology to immunoglobulins."; RL Proc. Natl. Acad. Sci. U.S.A. 79:6013-6017(1982). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] (DRA*0102). RX MEDLINE=91010755; PubMed=2212658; RA Koppelman B., Cresswell P.; RT "Rapid nonlysosomal degradation of assembled HLA class II RT glycoproteins incorporating a mutant DR alpha-chain."; RL J. Immunol. 145:2730-2736(1990). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-254 (DRA*0102). RC TISSUE=Blood; RX MEDLINE=22337845; PubMed=12445311; RX DOI=10.1034/j.1399-0039.2002.600310.x; RA Kralovicova J., Marsh S.G., Waller M.J., Hammarstrom L., RA Vorechovsky I.; RT "The HLA-DRA*0102 allele: correct nucleotide sequence and associated RT HLA haplotypes."; RL Tissue Antigens 60:266-267(2002). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-207. RX MEDLINE=94195388; PubMed=8145819; DOI=10.1038/368215a0; RA Stern L.J., Brown J.H., Jardetzky T.J., Gorga J.C., Urban R.G., RA Strominger J.L., Wiley D.C.; RT "Crystal structure of the human class II MHC protein HLA-DR1 complexed RT with an influenza virus peptide."; RL Nature 368:215-221(1994). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-207. RX MEDLINE=93302847; PubMed=8316295; DOI=10.1038/364033a0; RA Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G., RA Strominger J.L., Wiley D.C.; RT "Three-dimensional structure of the human class II histocompatibility RT antigen HLA-DR1."; RL Nature 364:33-39(1993). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH SEB. RX MEDLINE=94203282; PubMed=8152483; DOI=10.1038/368711a0; RA Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., RA Chi Y.I., Stauffacher C., Strominger J.L., Wiley D.C.; RT "Three-dimensional structure of a human class II histocompatibility RT molecule complexed with superantigen."; RL Nature 368:711-718(1994). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS). RX MEDLINE=96085023; PubMed=7477400; DOI=10.1038/378457a0; RA Ghosh P., Amaya M., Mellins E., Wiley D.C.; RT "The structure of an intermediate in class II MHC maturation: CLIP RT bound to HLA-DR3."; RL Nature 378:457-462(1995). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH PEPTIDE FROM RP COLLAGEN. RX MEDLINE=98014591; PubMed=9354468; DOI=10.1016/S1074-7613(00)80369-6; RA Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C.; RT "X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed RT with a peptide from human collagen II."; RL Immunity 7:473-481(1997). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH PEPTIDE FROM RP MYELIN BASIC PROTEIN. RX MEDLINE=99000672; PubMed=9782128; DOI=10.1084/jem.188.8.1511; RA Smith K.J., Pyrdol J., Gauthier L., Wiley D.C., Wucherpfennig K.W.; RT "Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a RT peptide from human myelin basic protein."; RL J. Exp. Med. 188:1511-1520(1998). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- POLYMORPHISM: The following alleles of DRA are known: DRA*0101 and CC DRA*0102. The sequence shown is that of DRA*0101. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; J00204; AAA36302.1; -; Genomic_DNA. DR EMBL; J00203; AAA36302.1; JOINED; Genomic_DNA. DR EMBL; V00523; CAA23782.1; -; mRNA. DR EMBL; K01171; AAA59785.1; -; mRNA. DR EMBL; X00274; CAA25076.1; ALT_INIT; Genomic_DNA. DR EMBL; J00194; AAA36275.1; -; mRNA. DR EMBL; CR457013; CAG33294.1; -; mRNA. DR EMBL; Z84814; CAB06609.1; -; Genomic_DNA. DR EMBL; AL670296; CAI17571.1; -; Genomic_DNA. DR EMBL; AL662796; CAI18266.1; -; Genomic_DNA. DR EMBL; AL935032; CAI18476.1; -; Genomic_DNA. DR EMBL; BC032350; AAH32350.1; -; mRNA. DR EMBL; BC071659; AAH71659.1; -; mRNA. DR EMBL; J00201; AAA36301.1; -; Genomic_DNA. DR EMBL; M60334; AAA59783.1; -; mRNA. DR EMBL; AF481359; AAO23887.1; -; Genomic_DNA. DR PIR; A93952; HLHUDA. DR UniGene; Hs.520048; -. DR PDB; 1A6A; X-ray; A=30-205. DR PDB; 1AQD; X-ray; A/D/G/J=26-217. DR PDB; 1BX2; X-ray; A/D=27-206. DR PDB; 1D5M; X-ray; A=26-206. DR PDB; 1D5X; X-ray; A=26-206. DR PDB; 1D5Z; X-ray; A=26-206. DR PDB; 1D6E; X-ray; A=26-206. DR PDB; 1DLH; X-ray; A/D=28-207. DR PDB; 1FV1; X-ray; A/D=26-206. DR PDB; 1FYT; X-ray; A=26-206. DR PDB; 1H15; X-ray; A/D=26-207. DR PDB; 1HQR; X-ray; A=26-206. DR PDB; 1J8H; X-ray; A=26-206. DR PDB; 1JWM; X-ray; A=26-207. DR PDB; 1JWS; X-ray; A=26-207. DR PDB; 1JWU; X-ray; A=26-207. DR PDB; 1KG0; X-ray; A=28-207. DR PDB; 1KLG; X-ray; A=29-205. DR PDB; 1KLU; X-ray; A=29-207. DR PDB; 1LO5; X-ray; A=26-207. DR PDB; 1SEB; X-ray; A/E=26-206. DR PDB; 1SJE; X-ray; A=28-207. DR PDB; 1SJH; X-ray; A=28-207. DR PDB; 1T5W; X-ray; A/D=27-206. DR PDB; 1T5X; X-ray; A=27-207. DR PDB; 1YMM; X-ray; A=26-216. DR PDB; 1ZGL; X-ray; A/D/G/J=26-206. DR PDB; 2SEB; X-ray; A=26-206. DR DIP; DIP:6063N; -. DR IntAct; P01903; -. DR KEGG; hsa:3122; -. DR H-InvDB; HIX0005752; -. DR HGNC; HGNC:4947; HLA-DRA. DR MIM; 142860; gene. DR LinkHub; P01903; -. DR ArrayExpress; P01903; -. DR RZPD-ProtExp; I0500; -. DR RZPD-ProtExp; RZPDo834G105; -. DR RZPD-ProtExp; RZPDo839D06127; -. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0005764; C:lysosome; IDA:MGI. DR GO; GO:0032395; F:MHC class II receptor activity; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001003; MHC_II_alpha_N. DR Gene3D; G3DSA:3.10.320.10; MHC_II_alpha_N; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00993; MHC_II_alpha; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW 3D-structure; Direct protein sequencing; Glycoprotein; KW Immune response; Membrane; MHC II; Polymorphism; Signal; KW Transmembrane. FT SIGNAL 1 25 FT CHAIN 26 254 HLA class II histocompatibility antigen, FT DR alpha chain. FT /FTId=PRO_0000018947. FT TOPO_DOM 26 216 Extracellular (Potential). FT TRANSMEM 217 239 Potential. FT TOPO_DOM 240 254 Cytoplasmic (Potential). FT DOMAIN 112 204 Ig-like C1-type. FT REGION 26 109 Alpha-1. FT REGION 110 203 Alpha-2. FT REGION 204 216 Connecting peptide. FT CARBOHYD 103 103 N-linked (GlcNAc...). FT CARBOHYD 143 143 N-linked (GlcNAc...). FT DISULFID 132 188 By similarity. FT VARIANT 242 242 V -> L (in allele DRA*0102; FT dbSNP:rs7192). FT /FTId=VAR_004399. FT CONFLICT 28 29 EE -> AD (in Ref. 4). FT CONFLICT 33 33 I -> T (in Ref. 4). FT CONFLICT 34 35 QA -> YP (in Ref. 4). FT CONFLICT 48 48 M -> Q (in Ref. 4). FT CONFLICT 54 54 D -> T (in Ref. 4). FT CONFLICT 67 67 V -> A (in Ref. 3). FT CONFLICT 149 149 N -> E (in Ref. 3). FT STRAND 30 40 FT TURN 41 43 FT STRAND 44 51 FT TURN 52 53 FT STRAND 54 60 FT TURN 61 64 FT STRAND 65 70 FT HELIX 71 73 FT TURN 74 76 FT TURN 81 81 FT HELIX 82 101 FT TURN 102 104 FT STRAND 113 120 FT TURN 124 125 FT STRAND 128 140 FT STRAND 143 148 FT TURN 149 150 FT STRAND 151 153 FT TURN 155 156 FT TURN 166 167 FT STRAND 170 178 FT STRAND 186 191 FT TURN 193 194 FT STRAND 199 203 SQ SEQUENCE 254 AA; 28607 MW; 3CD1CDBA952B2350 CRC64; MAISGVPVLG FFIIAVLMSA QESWAIKEEH VIIQAEFYLN PDQSGEFMFD FDGDEIFHVD MAKKETVWRL EEFGRFASFE AQGALANIAV DKANLEIMTK RSNYTPITNV PPEVTVLTNS PVELREPNVL ICFIDKFTPP VVNVTWLRNG KPVTTGVSET VFLPREDHLF RKFHYLPFLP STEDVYDCRV EHWGLDEPLL KHWEFDAPSP LPETTENVVC ALGLTVGLVG IIIGTIFIIK GVRKSNAAER RGPL // ID 2DRA_MACMU Reviewed; 254 AA. AC Q30631; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 28-NOV-2006, entry version 43. DE HLA class II histocompatibility antigen, DR alpha chain precursor (MHC DE class II antigen DRA). GN Name=HLA-DRA; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96053521; PubMed=7558932; DOI=10.1016/0198-8859(94)00155-J; RA Lekutis C., Letvin N.L.; RT "Biochemical and molecular characterization of rhesus monkey major RT histocompatibility complex class II DR."; RL Hum. Immunol. 43:72-80(1995). CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC 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; L27739; AAB63305.1; -; mRNA. DR HSSP; P01903; 1SEB. DR SMR; Q30631; 28-206. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001003; MHC_II_alpha_N. DR Gene3D; G3DSA:3.10.320.10; MHC_II_alpha_N; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00993; MHC_II_alpha; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. KW Glycoprotein; Immune response; Membrane; MHC II; Signal; KW Transmembrane. FT SIGNAL 1 25 By similarity. FT CHAIN 26 254 HLA class II histocompatibility antigen, FT DR alpha chain. FT /FTId=PRO_0000018948. FT TOPO_DOM 26 216 Extracellular (Potential). FT TRANSMEM 217 239 Potential. FT TOPO_DOM 240 254 Cytoplasmic (Potential). FT DOMAIN 112 204 Ig-like C1-type. FT REGION 26 109 Alpha-1. FT REGION 110 203 Alpha-2. FT REGION 204 216 Connecting peptide. FT CARBOHYD 103 103 N-linked (GlcNAc...) (Potential). FT DISULFID 132 188 By similarity. SQ SEQUENCE 254 AA; 28405 MW; 8587C99E22944443 CRC64; MAESGVPVLG FFIIAVLMSA QESWAIKEEH VIIQAEFYLN PDQSGEFMFD FDGDEIFHVD MAKKETVWRL EEFGRFASFE AQGALANIAV DKANLEIMTK RSNNTPITNV PPEVTVLTNS PVELGEPNVL ICFIDKFSPP VVKVTWLKNG KPVTTGVSET VFLPREDHLF RKFHYLPFLP STEDIYDCKV EHWCLDAPLL KHWEFDAPSP LPETTENVVC ALGLIVGLVG IIVGTVFIIK GVRKSNAAER RGPL // ID 2ENR_CLOTY Reviewed; 30 AA. AC P11887; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 31-OCT-2006, entry version 30. DE 2-enoate reductase (EC 1.3.1.31) (Fragment). OS Clostridium tyrobutyricum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1519; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=85225966; PubMed=4005048; RA Kuno S., Bacher A., Simon H.; RT "Structure of enoate reductase from a Clostridium tyrobutyricum (C. RT spec. La1)."; RL Biol. Chem. Hoppe-Seyler 366:463-472(1985). CC -!- FUNCTION: Involved in fermentation of amino acids (Stickland CC reaction) such as leucine, isoleucine, valine and phenylalanine. CC -!- CATALYTIC ACTIVITY: Butanoate + NAD(+) = 2-butenoate + NADH. CC -!- COFACTOR: Iron-sulfur cluster. CC -!- COFACTOR: FAD or FMN. CC -!- SUBUNIT: Dodecamer; tetramer of trimers. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A22498; A22498. DR GO; GO:0047540; F:2-enoate reductase activity; IEA:EC. KW Direct protein sequencing; Flavoprotein; Iron; Iron-sulfur; KW Metal-binding; NAD; Oxidoreductase. FT CHAIN 1 >30 2-enoate reductase. FT /FTId=PRO_0000064360. FT NON_TER 30 30 SQ SEQUENCE 30 AA; 3303 MW; AD96FB5BB2080920 CRC64; MKNKSLFEVI KIGKVEVXXK IXMAVMGAFG // ID 2NPD_NEUCR Reviewed; 378 AA. AC Q01284; Q7RV78; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 44. DE 2-nitropropane dioxygenase precursor (EC 1.13.11.32) (Nitroalkane DE oxidase) (2-NPD). GN Name=ncd-2; ORFNames=G17A4.200, NCU03949; OS Neurospora crassa. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=5141; RN [1] RP NUCLEOTIDE SEQUENCE, AND CHARACTERIZATION. RC STRAIN=ATCC 10337 / IFO 6067 / FGSC 1758 / IMI 53239; RX MEDLINE=98162064; PubMed=9501443; RA Gorlatova N., Tchorzewski M., Kurihara T., Soda K., Esaki N.; RT "Purification, characterization, and mechanism of a flavin RT mononucleotide-dependent 2-nitropropane dioxygenase from Neurospora RT crassa."; RL Appl. Environ. Microbiol. 64:1029-1033(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX MEDLINE=22542210; PubMed=12655011; DOI=10.1093/nar/gkg293; RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., RA Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., RA Schulte U.; RT "What's in the genome of a filamentous fungus? Analysis of the RT Neurospora genome sequence."; RL Nucleic Acids Res. 31:1944-1954(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554; RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., RA Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., RA Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., RA Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., RA Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., RA Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., RA Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., RA Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., RA Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.; RT "The genome sequence of the filamentous fungus Neurospora crassa."; RL Nature 422:859-868(2003). CC -!- FUNCTION: Catalyzes the oxidation of nitroalkanes to produce the CC corresponding carbonyl compounds. It acts on 2-nitropropane better CC than on nitroethane and 1-nitropropane, and anionic forms of CC nitroalkanes are much better substrates than are neutral forms. CC -!- CATALYTIC ACTIVITY: 2 2-nitropropane + O(2) = 2 acetone + 2 CC nitrite. CC -!- COFACTOR: FMN. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: To FAD-dependent 2-nitropropane dioxygenase. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U22530; AAA64218.1; -; mRNA. DR EMBL; BX908812; CAF06155.1; -; Genomic_DNA. DR EMBL; AABX01000719; EAA28352.1; -; Genomic_DNA. DR PIR; T46693; T46693. DR BioCyc; NCRA-XX3-01:NCRA-XX3-01-007697-MONOMER; -. DR GO; GO:0018580; F:2-nitropropane dioxygenase activity; IEA:EC. DR InterPro; IPR004136; 2Npropane_dOase. DR Pfam; PF03060; NPD; 1. KW Dioxygenase; Flavoprotein; FMN; Oxidoreductase. FT PROPEP 1 15 Potential. FT /FTId=PRO_0000020575. FT CHAIN 16 378 2-nitropropane dioxygenase. FT /FTId=PRO_0000020576. SQ SEQUENCE 378 AA; 39916 MW; E453EB43FD23E441 CRC64; MHFPGHSSKK EESAQAALTK LNSWFPTTKN PVIISAPMYL IANGTLAAEV SKAGGIGFVA GGSDFRPGSS HLTALSTELA SARSRLGLTD RPLTPLPGIG VGLILTHTIS VPYVTDTVLP ILIEHSPQAV WLFANDPDFE ASSEPGAKGT AKQIIEALHA SGFVVFFQVG TVKDARKAAA DGADVIVAQG IDAGGHQLAT GSGIVSLVPE VRDMLDREFK EREVVVVAAG GVADGRGVVG ALGLGAEGVV LGTRFTVAVE ASTPEFRRKV ILETNDGGLN TVKSHFHDQI NCNTIWHNVY DGRAVRNASY DDHAAGVPFE ENHKKFKEAA SSGDNSRAVT WSGTAVGLIK DQRPAGDIVR ELREEAKERI KKIQAFAA // ID 2NPD_WILMR Reviewed; 374 AA. AC Q12723; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 25. DE 2-nitropropane dioxygenase (EC 1.13.11.32) (Nitroalkane oxidase) (2- DE NPD). OS Williopsis mrakii (Yeast) (Hansenula mrakii). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Williopsis. OX NCBI_TaxID=4963; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=IFO 0895; RX MEDLINE=95112848; PubMed=7813473; RA Tchorzewski M., Kurihara T., Esaki N., Soda K.; RT "Unique primary structure of 2-nitropropane dioxygenase from Hansenula RT mrakii."; RL Eur. J. Biochem. 226:841-846(1994). CC -!- FUNCTION: Catalyzes the oxygenative denitrification of various CC anionic nitroalkanes. CC -!- CATALYTIC ACTIVITY: 2 2-nitropropane + O(2) = 2 acetone + 2 CC nitrite. CC -!- COFACTOR: FAD. CC -!- SIMILARITY: To FMN-dependent 2-nitropropane dioxygenase. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U13900; AAA64484.1; -; Genomic_DNA. DR PIR; S50891; S50891. DR GO; GO:0018580; F:2-nitropropane dioxygenase activity; IEA:EC. DR InterPro; IPR004136; 2Npropane_dOase. DR Pfam; PF03060; NPD; 1. KW Dioxygenase; FAD; Flavoprotein; Oxidoreductase. FT CHAIN 1 374 2-nitropropane dioxygenase. FT /FTId=PRO_0000064361. SQ SEQUENCE 374 AA; 41467 MW; 63F82BA7453E43F0 CRC64; MRSQIQSFLK TFEVRYPIIQ APMAGASTLE LAATVTRLGG IGSIPMGSLS EKCDAIETQL ENFDELVGDS GRIVNLNFFA HKEPRSGRAD VNEEWLKKYD KIYGKAGIEF DKKELKLLYP SFRSIVDPQH PTVRLLKNLK PKIVSFHFGL PHEAVIESLQ ASDIKIFVTV TNLQEFQQAY ESKLDGVVLQ GWEAGGHRGN FKANDVEDGQ LKTLDLVSTI VDYIDSASIS NPPFIIAAGG IHDDESIKEL LQFNIAAVQL GTVWLPSSQA TISPEHLKMF QSPKSDTMMT AAISGRNLRT ISTPFLRDLH QSSPLASIPD YPLPYDSFKS LANDAKQSGK GPQYSAFLAG SNYHKSWKDT RSTEEIFSIL VQDL // ID 2PS_GERHY Reviewed; 402 AA. AC P48391; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 2. DT 23-JAN-2007, entry version 42. DE 2-pyrone synthase (EC 2.3.1.-) (2-PS) (G2ps1). GN Name=2PS; Synonyms=CHS2; OS Gerbera hybrida. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; campanulids; Asterales; Asteraceae; Mutisioideae; Mutisieae; OC Gerbera. OX NCBI_TaxID=18101; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Corolla; RX MEDLINE=95306791; PubMed=7787187; RA Helariutta Y., Elomaa P., Kotilainen M., Griesbach R.J., Schroeder J., RA Teeri T.H.; RT "Chalcone synthase-like genes active during corolla development are RT differentially expressed and encode enzymes with different catalytic RT properties in Gerbera hybrida (Asteraceae)."; RL Plant Mol. Biol. 28:47-60(1995). RN [2] RP SEQUENCE REVISION TO 259. RA Teeri T.H.; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION. RA Eckermann S., Schroeder G., Schmidt J., Strack D., Edrada R.A., RA Helariutta Y., Elomaa P., Kotilainen M., Kilpelaeinen I., Proksch P., RA Teeri T.H., Schroeder J.; RT "New pathway to polyketides in plants."; RL Nature 396:387-390(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH RP ACETOACETYL-COA. RX MEDLINE=20579515; PubMed=11137815; DOI=10.1016/S1074-5521(00)00041-7; RA Jez J.M., Austin M.B., Ferrer J.-L., Bowman M.E., Schroeder J., RA Noel J.P.; RT "Structural control of polyketide formation in plant-specific RT polyketide synthases."; RL Chem. Biol. 7:919-930(2000). CC -!- FUNCTION: Polyketide synthase, which uses acetyl-CoA and two CC condensation reactions with malonyl-CoA to form triacetic acid CC lactone (also called methylpyrone), a precursor of phytoalexin. CC May participate in insect and pathogen resistance. CC -!- SIMILARITY: Belongs to the chalcone/stilbene synthases family. CC -!- CAUTION: Ref.3 has shown that this is not a chalcone synthase, but CC a pyrone synthase. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z38097; CAA86219.2; -; mRNA. DR PDB; 1EE0; X-ray; A/B=1-402. DR PDB; 1QLV; X-ray; A/B=1-402. DR InterPro; IPR012328; Chal_sti_synt_C. DR InterPro; IPR001099; Chal_sti_synt_N. DR InterPro; IPR011141; PKS_III. DR Pfam; PF02797; Chal_sti_synt_C; 1. DR Pfam; PF00195; Chal_sti_synt_N; 1. DR PIRSF; PIRSF000451; PKS_III; 1. DR ProDom; PD000453; N-C_synthase; 1. DR PROSITE; PS00441; CHALCONE_SYNTH; 1. KW 3D-structure; Acyltransferase; Transferase. FT CHAIN 1 402 2-pyrone synthase. FT /FTId=PRO_0000216092. FT ACT_SITE 169 169 By similarity. FT STRAND 23 30 FT STRAND 35 37 FT HELIX 38 48 FT TURN 49 50 FT TURN 52 53 FT HELIX 55 67 FT TURN 68 68 FT STRAND 72 74 FT HELIX 79 84 FT HELIX 86 89 FT TURN 91 92 FT HELIX 96 122 FT HELIX 126 128 FT STRAND 131 135 FT STRAND 141 143 FT HELIX 145 153 FT TURN 154 154 FT TURN 157 158 FT STRAND 160 164 FT TURN 169 170 FT HELIX 171 185 FT TURN 187 188 FT STRAND 191 197 FT HELIX 199 202 FT TURN 208 209 FT HELIX 211 216 FT TURN 217 219 FT STRAND 223 232 FT TURN 235 237 FT STRAND 242 251 FT TURN 253 254 FT HELIX 256 258 FT STRAND 259 264 FT TURN 265 266 FT TURN 274 275 FT HELIX 276 292 FT HELIX 293 295 FT TURN 296 296 FT HELIX 300 302 FT STRAND 303 307 FT HELIX 312 321 FT TURN 322 323 FT TURN 326 329 FT HELIX 330 339 FT HELIX 343 345 FT HELIX 346 360 FT TURN 361 362 FT TURN 366 366 FT TURN 368 369 FT STRAND 370 379 FT TURN 380 382 FT STRAND 383 391 SQ SEQUENCE 402 AA; 43749 MW; 593257F979EE45A8 CRC64; MGSYSSDDVE VIREAGRAQG LATILAIGTA TPPNCVAQAD YADYYFRVTK SEHMVDLKEK FKRICEKTAI KKRYLALTED YLQENPTMCE FMAPSLNARQ DLVVTGVPML GKEAAVKAID EWGLPKSKIT HLIFCTTAGV DMPGADYQLV KLLGLSPSVK RYMLYQQGCA AGGTVLRLAK DLAENNKGSR VLIVCSEITA ILFHGPNENH LDSLVAQALF GDGAAALIVG SGPHLAVERP IFEIVSTDQT ILPDTEKAMK LHLREGGLTF QLHRDVPLMV AKNIENAAEK ALSPLGITDW NSVFWMVHPG GRAILDQVER KLNLKEDKLR ASRHVLSEYG NLISACVLFI IDEVRKRSMA EGKSTTGEGL DCGVLFGFGP GMTVETVVLR SVRVTAAVAN GN // ID 2SS1_ARATH Reviewed; 164 AA. AC P15457; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 23-JAN-2007, entry version 61. DE 2S seed storage protein 1 precursor (2S albumin storage protein) DE (NWMU2-2S albumin 1) [Contains: 2S seed storage protein 1 small DE subunit; 2S seed storage protein 1 large subunit]. GN Name=AT2S1; OrderedLocusNames=At4g27140; ORFNames=T24A18.90; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-73 AND RP 84-162. RC STRAIN=cv. C24; RA Krebbers E., Herdies L., de Clercq A., Seurinck J., Leemans J., RA van Damme J., Segura M., Gheysen G., van Montagu M., RA Vandekerckhove J.; RT "Determination of the processing sites of an Arabidopsis 2S albumin RT and characterization of the complete gene family."; RL Plant Physiol. 87:859-866(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. C24; RX PubMed=8012403; RA da Silva Conceicao A., Krebbers E.; RT "A cotyledon regulatory region is responsible for the different RT spatial expression patterns of Arabidopsis 2S albumin genes."; RL Plant J. 5:493-505(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- FUNCTION: This is a 2S seed storage protein. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- MISCELLANEOUS: This is the most abundant isoform of 2S albumin in CC Arabidopsis. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M22032; AAA32743.1; -; Genomic_DNA. DR EMBL; Z24745; CAA80870.1; -; Genomic_DNA. DR EMBL; AL035680; CAB38844.1; -; Genomic_DNA. DR EMBL; AL161566; CAB79569.1; -; Genomic_DNA. DR EMBL; AF370541; AAK48968.1; -; mRNA. DR EMBL; AY072508; AAL66923.1; -; mRNA. DR PIR; JA0161; NWMU1. DR UniGene; At.158; -. DR HSSP; P24565; 1PNB. DR GenomeReviews; CT486007_GR; AT4G27140. DR KEGG; ath:At4g27140; -. DR TAIR; At4g27140; -. DR ArrayExpress; P15457; -. DR GermOnline; AT4G27140; Arabidopsis thaliana. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR ProDom; PD002498; Napin; 1. DR SMART; SM00499; AAI; 1. KW Direct protein sequencing; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 21 FT PROPEP 22 37 FT /FTId=PRO_0000032088. FT CHAIN 38 73 2S seed storage protein 1 small subunit. FT /FTId=PRO_0000032089. FT PROPEP 74 83 FT /FTId=PRO_0000032090. FT CHAIN 84 162 2S seed storage protein 1 large subunit. FT /FTId=PRO_0000032091. FT PROPEP 163 164 FT /FTId=PRO_0000032092. SQ SEQUENCE 164 AA; 19014 MW; 2BF28CB474D9832B CRC64; MANKLFLVCA ALALCFLLTN ASIYRTVVEF EEDDATNPIG PKMRKCRKEF QKEQHLRACQ QLMLQQARQG RSDEFDFEDD MENPQGQQQE QQLFQQCCNE LRQEEPDCVC PTLKQAAKAV RLQGQHQPMQ VRKIYQTAKH LPNVCDIPQV DVCPFNIPSF PSFY // ID 2SS1_BRANA Reviewed; 133 AA. AC P01091; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 31-OCT-2006, entry version 46. DE Napin-1 precursor (1.7S seed storage protein) [Contains: Napin-1 small DE chain; Napin-1 large chain] (Fragment). OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Brassica. OX NCBI_TaxID=3708; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Tower; RX MEDLINE=84113267; PubMed=6689334; RA Crouch M.L., Tenbarge K.M., Simon A.E., Ferl R.; RT "cDNA clones for Brassica napus seed storage proteins: evidence from RT nucleotide sequence analysis that both subunits of napin are cleaved RT from a precursor polypeptide."; RL J. Mol. Appl. Genet. 2:273-283(1983). CC -!- FUNCTION: The small, basic, water-soluble napins are one of the CC two major kinds of storage proteins synthesized in the seed during CC its maturation. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- TISSUE SPECIFICITY: Cotyledons and the axis. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K01544; AAA33005.1; -; mRNA. DR PIR; A01330; NWRP1. DR HSSP; P24565; 1PNB. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR ProDom; PD002498; Napin; 1. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Storage protein. FT CHAIN <1 30 Napin-1 small chain. FT /FTId=PRO_0000032110. FT PROPEP 31 49 FT /FTId=PRO_0000032111. FT CHAIN 50 130 Napin-1 large chain. FT /FTId=PRO_0000032112. FT PROPEP 131 133 Potential. FT /FTId=PRO_0000032113. FT NON_TER 1 1 SQ SEQUENCE 133 AA; 15294 MW; 5FDFC7ECE3E22ACB CRC64; PKCRKEFQQA QHLKACQQWL HKQAMQSGGG PSWTLDGEFD FEDDMEKQGP QQRPPLHQQY CNELQQEEPL CVCPTLRGAS KAVKQQIQQQ EQQQGKQQMV NRIYQTATHL PKVCNIPQVS VCPFQKTMPG PSY // ID 2SS1_SESIN Reviewed; 148 AA. AC Q9XHP1; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 31-OCT-2006, entry version 26. DE 2S seed storage protein 1 precursor (beta-globulin) (2S albumin DE storage protein) [Contains: 2S seed storage protein 1 small subunit; DE 2S seed storage protein 1 large subunit]. OS Sesamum indicum (Oriental sesame) (Gingelly). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Lamiales; Pedaliaceae; Sesamum. OX NCBI_TaxID=4182; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Tainan 1; TISSUE=Seed; RX MEDLINE=20074970; PubMed=10606554; DOI=10.1021/jf990366z; RA Tai S.S.K., Wu L.S.H., Chen E.C.F., Tzen J.T.C.; RT "Molecular cloning of 11S globulin and 2S albumin, the two major seed RT storage proteins in sesame."; RL J. Agric. Food Chem. 47:4932-4938(1999). CC -!- FUNCTION: Seed storage protein. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF091841; AAD42943.1; -; mRNA. DR GO; GO:0042735; C:protein body; NAS:UniProtKB. DR GO; GO:0045735; F:nutrient reservoir activity; NAS:UniProtKB. DR GO; GO:0051259; P:protein oligomerization; NAS:UniProtKB. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 19 Potential. FT PROPEP 20 38 By similarity. FT /FTId=PRO_0000043211. FT CHAIN 39 68 2S seed storage protein 1 small subunit FT (By similarity). FT /FTId=PRO_0000043212. FT PROPEP 69 76 By similarity. FT /FTId=PRO_0000043213. FT CHAIN 77 146 2S seed storage protein 1 large subunit FT (By similarity). FT /FTId=PRO_0000043214. FT PROPEP 147 148 By similarity. FT /FTId=PRO_0000043215. FT DISULFID 42 97 Interchain (between small and large FT chains) (By similarity). FT DISULFID 54 86 Interchain (between small and large FT chains) (By similarity). FT DISULFID 87 133 By similarity. FT DISULFID 99 141 By similarity. SQ SEQUENCE 148 AA; 17524 MW; BA46B033BA13E3DE CRC64; MARFTIVLAV LFAAALVSAS AHKTVVTTSV AEEGEEENQR GCEWESRQCQ MRHCMQWMRS MRGQYEESFL RSAEANQGQF EHFRECCNEL RDVKSHCRCE ALRCMMRQMQ QEYGMEQEMQ QMQQMMQYLP RMCGMSYPTE CRMRPIFA // ID 2SS2_ARATH Reviewed; 170 AA. AC P15458; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 23-JAN-2007, entry version 60. DE 2S seed storage protein 2 precursor (2S albumin storage protein) DE (NWMU2-2S albumin 2) [Contains: 2S seed storage protein 2 small DE subunit; 2S seed storage protein 2 large subunit]. GN Name=AT2S2; OrderedLocusNames=At4g27150; ORFNames=T24A18.100; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. C24; RA Krebbers E., Herdies L., de Clercq A., Seurinck J., Leemans J., RA van Damme J., Segura M., Gheysen G., van Montagu M., RA Vandekerckhove J.; RT "Determination of the processing sites of an Arabidopsis 2S albumin RT and characterization of the complete gene family."; RL Plant Physiol. 87:859-866(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. C24; RX PubMed=8012403; RA da Silva Conceicao A., Krebbers E.; RT "A cotyledon regulatory region is responsible for the different RT spatial expression patterns of Arabidopsis 2S albumin genes."; RL Plant J. 5:493-505(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-90 AND 118-170. RC STRAIN=cv. Columbia; TISSUE=Green siliques; RX MEDLINE=94108489; PubMed=8281187; RX DOI=10.1046/j.1365-313X.1993.04061051.x; RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., RA Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., RA Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., RA de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., RA Bardet C., Tremousaygue D., Lescure B.; RT "An inventory of 1152 expressed sequence tags obtained by partial RT sequencing of cDNAs from Arabidopsis thaliana."; RL Plant J. 4:1051-1061(1993). CC -!- FUNCTION: This is a 2S seed storage protein. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M22034; AAA32744.1; -; Genomic_DNA. DR EMBL; Z24745; CAA80871.1; -; Genomic_DNA. DR EMBL; AL035680; CAB38845.1; -; Genomic_DNA. DR EMBL; AL161566; CAB79570.1; -; Genomic_DNA. DR EMBL; BT002073; AAN72084.1; -; mRNA. DR EMBL; BT006557; AAP21365.1; -; mRNA. DR EMBL; Z17598; CAA79010.1; -; mRNA. DR EMBL; Z17594; CAA79008.1; -; mRNA. DR PIR; JA0162; NWMU2. DR UniGene; At.43652; -. DR HSSP; P24565; 1PNB. DR GenomeReviews; CT486007_GR; AT4G27150. DR KEGG; ath:At4g27150; -. DR TAIR; At4g27150; -. DR ArrayExpress; P15458; -. DR GermOnline; AT4G27150; Arabidopsis thaliana. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR ProDom; PD002498; Napin; 1. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 21 FT PROPEP 22 37 FT /FTId=PRO_0000032093. FT CHAIN 38 72 2S seed storage protein 2 small subunit FT (By similarity). FT /FTId=PRO_0000032094. FT PROPEP 73 88 FT /FTId=PRO_0000032095. FT CHAIN 89 170 2S seed storage protein 2 large subunit FT (By similarity). FT /FTId=PRO_0000032096. SQ SEQUENCE 170 AA; 19361 MW; 0A0562D5FAB56275 CRC64; MANKLFLVCA TFALCFLLTN ASIYRTVVEF DEDDASNPMG PRQKCQKEFQ QSQHLRACQK LMRMQMRQGR GGGPSLDDEF DLEDDIENPQ GPQQGHQILQ QCCSELRQEE PVCVCPTLRQ AARAVSLQGQ HGPFQSRKIY KTAKYLPNIC KIQQVGECPF QTTIPFFPPY // ID 2SS2_BRANA Reviewed; 178 AA. AC P01090; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 2. DT 28-NOV-2006, entry version 47. DE Napin-2 precursor (1.7S seed storage protein) [Contains: Napin-2 small DE chain; Napin-2 large chain]. OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Brassica. OX NCBI_TaxID=3708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87308224; PubMed=3624251; RA Josefsson L.-G., Lenman M., Ericson M.L., Rask L.; RT "Structure of a gene encoding the 1.7 S storage protein, napin, from RT Brassica napus."; RL J. Biol. Chem. 262:12196-12201(1987). RN [2] RP SEQUENCE REVISION. RA Josefsson L.-G.; RL Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87033665; PubMed=3771543; RA Ericson M.L., Roedin J., Lenman M., Glimelius K., Josefsson L.-G., RA Rask L.; RT "Structure of the rapeseed 1.7 S storage protein, napin, and its RT precursor."; RL J. Biol. Chem. 261:14576-14581(1986). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Tower; RX MEDLINE=84113267; PubMed=6689334; RA Crouch M.L., Tenbarge K.M., Simon A.E., Ferl R.; RT "cDNA clones for Brassica napus seed storage proteins: evidence from RT nucleotide sequence analysis that both subunits of napin are cleaved RT from a precursor polypeptide."; RL J. Mol. Appl. Genet. 2:273-283(1983). CC -!- FUNCTION: The small, basic, water-soluble napins are one of the CC two major kinds of storage proteins synthesized in the seed during CC its maturation. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- TISSUE SPECIFICITY: Cotyledons and the axis. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K01545; AAA33006.1; -; mRNA. DR EMBL; J02586; AAA32997.1; -; mRNA. DR EMBL; J02798; AAA87348.1; -; Genomic_DNA. DR PIR; A01329; NWRP2. DR PIR; A29801; A25997. DR HSSP; P24565; 1PNB. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR ProDom; PD002498; Napin; 1. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 21 FT PROPEP 22 38 FT /FTId=PRO_0000032114. FT CHAIN 39 74 Napin-2 small chain. FT /FTId=PRO_0000032115. FT PROPEP 75 94 FT /FTId=PRO_0000032116. FT CHAIN 95 175 Napin-2 large chain. FT /FTId=PRO_0000032117. FT PROPEP 176 178 Potential. FT /FTId=PRO_0000032118. FT CONFLICT 37 37 D -> N (in Ref. 4). FT CONFLICT 76 76 S -> N (in Ref. 4). SQ SEQUENCE 178 AA; 20104 MW; 734E561971B539FF CRC64; MANKLFLVSA TLAFFFLLTN ASIYRTVVEF DEDDATDSAG PFRIPKCRKE FQQAQHLRAC QQWLHKQAMQ SGGGPSWTLD GEFDFEDDME NPQGPQQRPP LLQQCCNELH QEEPLCVCPT LKGASKAVKQ QIQQQGQQQG KQQMVSRIYQ TATHLPKVCN IPQVSVCPFQ KTMPGPSY // ID 2SS2_CAPMA Reviewed; 155 AA. AC P30233; O04774; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 3. DT 20-FEB-2007, entry version 52. DE Sweet protein mabinlin-2 precursor (Mabinlin II) (MAB II) [Contains: DE Sweet protein mabinlin-2 chain A; Sweet protein mabinlin-2 chain B]. OS Capparis masaikai (Mabinlang). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Capparidaceae; Capparis. OX NCBI_TaxID=13395; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Seed; RX MEDLINE=97128796; PubMed=8973336; DOI=10.1016/S0378-1119(96)00465-9; RA Nirasawa S., Masuda Y., Nakaya K., Kurihara Y.; RT "Cloning and sequencing of a cDNA encoding a heat-stable sweet RT protein, mabinlin II."; RL Gene 181:225-227(1996). RN [2] RP PROTEIN SEQUENCE OF 36-68 AND 83-154. RC TISSUE=Seed; RX MEDLINE=93145958; PubMed=8425538; RA Liu X., Maeda S., Hu Z., Aiuchi T., Nakaya K., Kurihara Y.; RT "Purification, complete amino acid sequence and structural RT characterization of the heat-stable sweet protein, mabinlin II."; RL Eur. J. Biochem. 211:281-287(1993). RN [3] RP PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS. RX MEDLINE=94002261; PubMed=8399391; DOI=10.1016/0167-4838(93)90016-K; RA Nirasawa S., Liu X., Nishino T., Kurihara Y.; RT "Disulfide bridge structure of the heat-stable sweet protein mabinlin RT II."; RL Biochim. Biophys. Acta 1202:277-280(1993). CC -!- FUNCTION: Heat stable 2S seed storage protein having sweetness- CC inducing activity. CC -!- SUBUNIT: Heterodimer of a small A and a large B chain linked by CC disulfide bonds. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D83997; BAA12204.1; -; mRNA. DR PIR; JC5379; JC5379. DR HSSP; P24565; 1PNB. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR ProDom; PD002498; Napin; 1. DR SMART; SM00499; AAI; 1. KW Direct protein sequencing; Pyrrolidone carboxylic acid; KW Seed storage protein; Signal; Storage protein; KW Taste-modifying protein. FT SIGNAL 1 20 Potential. FT PROPEP 21 35 FT /FTId=PRO_0000032137. FT CHAIN 36 68 Sweet protein mabinlin-2 chain A. FT /FTId=PRO_0000032138. FT PROPEP 69 82 FT /FTId=PRO_0000032139. FT CHAIN 83 154 Sweet protein mabinlin-2 chain B. FT /FTId=PRO_0000032140. FT PROPEP 155 155 FT /FTId=PRO_0000032141. FT MOD_RES 36 36 Pyrrolidone carboxylic acid. FT MOD_RES 83 83 Pyrrolidone carboxylic acid. FT DISULFID 40 103 FT DISULFID 53 92 FT DISULFID 93 141 FT DISULFID 105 149 FT CONFLICT 148 148 A -> T (in Ref. 1). FT CONFLICT 153 153 A -> T (in Ref. 1). SQ SEQUENCE 155 AA; 18089 MW; 72E885DEDCC2D46A CRC64; MAKLIFLFAT LALFVLLANA SIQTTVIEVD EEEDNQLWRC QRQFLQHQRL RACQRFIHRR AQFGGQPDEL EDEVEDDNDD ENQPRRPALR QCCNQLRQVD RPCVCPVLRQ AAQQVLQRQI IQGPQQLRRL FDAARNLPNI CNIPNIGACP FRAWP // ID 2SS3_ARATH Reviewed; 164 AA. AC P15459; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 23-JAN-2007, entry version 61. DE 2S seed storage protein 3 precursor (2S albumin storage protein) DE (NWMU2-2S albumin 3) [Contains: 2S seed storage protein 3 small DE subunit; 2S seed storage protein 3 large subunit]. GN Name=AT2S3; OrderedLocusNames=At4g27160; ORFNames=T24A18.110; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. C24; RA Krebbers E., Herdies L., de Clercq A., Seurinck J., Leemans J., RA van Damme J., Segura M., Gheysen G., van Montagu M., RA Vandekerckhove J.; RT "Determination of the processing sites of an Arabidopsis 2S albumin RT and characterization of the complete gene family."; RL Plant Physiol. 87:859-866(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. C24; RX PubMed=8012403; RA da Silva Conceicao A., Krebbers E.; RT "A cotyledon regulatory region is responsible for the different RT spatial expression patterns of Arabidopsis 2S albumin genes."; RL Plant J. 5:493-505(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-164. RC STRAIN=cv. Columbia; TISSUE=Green siliques; RX MEDLINE=94108489; PubMed=8281187; RX DOI=10.1046/j.1365-313X.1993.04061051.x; RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., RA Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., RA Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., RA de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., RA Bardet C., Tremousaygue D., Lescure B.; RT "An inventory of 1152 expressed sequence tags obtained by partial RT sequencing of cDNAs from Arabidopsis thaliana."; RL Plant J. 4:1051-1061(1993). CC -!- FUNCTION: This is a 2S seed storage protein. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M22035; AAA32745.1; -; Genomic_DNA. DR EMBL; Z24744; CAA80868.1; -; Genomic_DNA. DR EMBL; AL035680; CAB38846.1; -; Genomic_DNA. DR EMBL; AL161566; CAB79571.1; -; Genomic_DNA. DR EMBL; AY080779; AAL87263.1; -; mRNA. DR EMBL; AY117157; AAM51232.1; -; mRNA. DR EMBL; Z17580; CAA79001.1; -; mRNA. DR PIR; JA0163; NWMU3. DR UniGene; At.19908; -. DR HSSP; P24565; 1PNB. DR GenomeReviews; CT486007_GR; AT4G27160. DR KEGG; ath:At4g27160; -. DR TAIR; At4g27160; -. DR ArrayExpress; P15459; -. DR GermOnline; AT4G27160; Arabidopsis thaliana. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR ProDom; PD002498; Napin; 1. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 21 FT PROPEP 22 37 FT /FTId=PRO_0000032097. FT CHAIN 38 72 2S seed storage protein 3 small subunit FT (By similarity). FT /FTId=PRO_0000032098. FT PROPEP 73 81 FT /FTId=PRO_0000032099. FT CHAIN 82 164 2S seed storage protein 3 large subunit FT (By similarity). FT /FTId=PRO_0000032100. SQ SEQUENCE 164 AA; 18762 MW; C9BEB6718549F248 CRC64; MANKLFLVCA TLALCFLLTN ASIYRTVVEF EEDDASNPVG PRQRCQKEFQ QSQHLRACQR WMSKQMRQGR GGGPSLDDEF DFEGPQQGYQ LLQQCCNELR QEEPVCVCPT LKQAARAVSL QGQHGPFQSR KIYQSAKYLP NICKIQQVGE CPFQTTIPFF PPYY // ID 2SS4_ARATH Reviewed; 166 AA. AC P15460; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 23-JAN-2007, entry version 68. DE 2S seed storage protein 4 precursor (2S albumin storage protein) DE (NWMU2-2S albumin 4) [Contains: 2S seed storage protein 4 small DE subunit; 2S seed storage protein 4 large subunit]. GN Name=AT2S4; OrderedLocusNames=At4g27170; ORFNames=T24A18.120; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. C24; RA Krebbers E., Herdies L., de Clercq A., Seurinck J., Leemans J., RA van Damme J., Segura M., Gheysen G., van Montagu M., RA Vandekerckhove J.; RT "Determination of the processing sites of an Arabidopsis 2S albumin RT and characterization of the complete gene family."; RL Plant Physiol. 87:859-866(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. C24; RX PubMed=8012403; RA da Silva Conceicao A., Krebbers E.; RT "A cotyledon regulatory region is responsible for the different RT spatial expression patterns of Arabidopsis 2S albumin genes."; RL Plant J. 5:493-505(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; TISSUE=Green siliques; RX MEDLINE=94108489; PubMed=8281187; RX DOI=10.1046/j.1365-313X.1993.04061051.x; RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., RA Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., RA Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., RA de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., RA Bardet C., Tremousaygue D., Lescure B.; RT "An inventory of 1152 expressed sequence tags obtained by partial RT sequencing of cDNAs from Arabidopsis thaliana."; RL Plant J. 4:1051-1061(1993). CC -!- FUNCTION: This is a 2S seed storage protein. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M22033; AAA32746.1; -; Genomic_DNA. DR EMBL; Z24744; CAA80869.1; -; Genomic_DNA. DR EMBL; AL035680; CAB38847.1; -; Genomic_DNA. DR EMBL; AL161566; CAB79572.1; -; Genomic_DNA. DR EMBL; AF446894; AAL38627.1; -; mRNA. DR EMBL; AY052682; AAK96586.1; -; mRNA. DR EMBL; Z17597; CAA79009.1; -; mRNA. DR EMBL; Z17601; CAA79011.1; -; mRNA. DR PIR; JA0164; NWMU4. DR UniGene; At.28758; -. DR HSSP; P24565; 1PNB. DR GenomeReviews; CT486007_GR; AT4G27170. DR KEGG; ath:At4g27170; -. DR TAIR; At4g27170; -. DR ArrayExpress; P15460; -. DR GermOnline; AT4G27170; Arabidopsis thaliana. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR ProDom; PD002498; Napin; 1. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 21 FT PROPEP 22 37 FT /FTId=PRO_0000032101. FT CHAIN 38 72 2S seed storage protein 4 small subunit FT (By similarity). FT /FTId=PRO_0000032102. FT PROPEP 73 88 FT /FTId=PRO_0000032103. FT CHAIN 89 166 2S seed storage protein 4 large subunit FT (By similarity). FT /FTId=PRO_0000032104. SQ SEQUENCE 166 AA; 19169 MW; 6E136F2D11F5039E CRC64; MANKLFLVCA ALALCFILTN ASVYRTVVEF DEDDASNPIG PIQKCQKEFQ QDQHLRACQR WMRKQMWQGR GGGPSLDDEF DMEDDIENPQ RRQLLQKCCS ELRQEEPVCV CPTLRQAAKA VRFQGQQHQP EQVRKIYQAA KYLPNICKIQ QVGVCPFQIP SIPSYY // ID 2SS4_BRANA Reviewed; 180 AA. AC P17333; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 12-DEC-2006, entry version 42. DE Napin precursor (1.7S seed storage protein) [Contains: Napin small DE chain; Napin large chain]. GN Name=NAP1; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Brassica. OX NCBI_TaxID=3708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Westar; TISSUE=Leaf; RX MEDLINE=91346654; PubMed=2102844; RA Baszczynski C.L., Fallis L.; RT "Isolation and nucleotide sequence of a genomic clone encoding a new RT Brassica napus napin gene."; RL Plant Mol. Biol. 14:633-635(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Topas; RX MEDLINE=95161697; PubMed=7858212; RA Boutilier K.A., Gines M.J., Demoor J.M., Huang B., Baszczynski C.L., RA Iyer V.N., Miki B.L.A.; RT "Expression of the BnmNAP subfamily of napin genes coincides with the RT induction of Brassica microspore embryogenesis."; RL Plant Mol. Biol. 26:1711-1723(1994). CC -!- FUNCTION: The small, basic, water-soluble napins are one of the CC two major kinds of storage proteins synthesized in the seed during CC its maturation. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- TISSUE SPECIFICITY: Cotyledons and the axis. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X17542; CAA35580.1; -; Genomic_DNA. DR EMBL; U04945; AAA81909.1; -; mRNA. DR PIR; S10018; S10018. DR HSSP; P24565; 1PNB. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR ProDom; PD002498; Napin; 1. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 21 FT PROPEP 22 38 FT /FTId=PRO_0000032119. FT CHAIN 39 74 Napin small chain. FT /FTId=PRO_0000032120. FT PROPEP 75 94 FT /FTId=PRO_0000032121. FT CHAIN 95 180 Napin large chain. FT /FTId=PRO_0000032122. SQ SEQUENCE 180 AA; 20318 MW; 6F3883CBED55FB26 CRC64; MANKLFLVSA TLAFFFLLTN ASIYRTIVEV DEDDATNPAG PFRIPKCRKE FQQAQHLKAC QQWLHKQAMQ SGSGPSWTLD GEFDFEDDME NPQGPQQRPP LLQQCCNELH QEEPLCVCPT LKGASKAVKQ QVRQQQGQQG QQLQQVISRI YQTATHLPKV CNIPQVSVCP FQKTMPGPSY // ID 2SS5_HELAN Reviewed; 295 AA. AC P15461; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 31-OCT-2006, entry version 48. DE 2S seed storage protein precursor (2S albumin storage protein). GN Name=HAG5; OS Helianthus annuus (Common sunflower). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; OC Heliantheae; Helianthus. OX NCBI_TaxID=4232; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 162-173. RC STRAIN=cv. Giant grey stripe; RX MEDLINE=88142538; PubMed=2830455; RA Allen R.D., Cohen E.A., Vonder Haar R.A., Adams C.A., Ma D.P., RA Nessler C.L., Thomas T.L.; RT "Sequence and expression of a gene encoding an albumin storage protein RT in sunflower."; RL Mol. Gen. Genet. 210:211-218(1987). CC -!- FUNCTION: This is a 2S seed storage protein. CC -!- PTM: The 38 kDa precursor may be cleaved into two polypeptides of CC approximately the same size. The mature protein is composed of a CC single polypeptide containing one or more intra-molecular CC disulfide linkages. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X06410; CAA29699.1; -; Genomic_DNA. DR PIR; S01062; S01062. DR HSSP; P24565; 1PNB. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 2. DR PRINTS; PR00496; NAPIN. DR SMART; SM00499; AAI; 2. KW Direct protein sequencing; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 20 Potential. FT PROPEP 21 161 Potential. FT /FTId=PRO_0000032151. FT CHAIN 162 295 2S seed storage protein. FT /FTId=PRO_0000032152. SQ SEQUENCE 295 AA; 34071 MW; 8958A106805142A1 CRC64; MAKQIVLALA FAALVAFATA HTTIITTTIE DENPISGQRQ VSQRIQGQRL NQCRMFLQQG QNIPREFDNP QMGRQQEQQL QQCCQELQNI EGQCQCEAVK QVFREAQQQV QQQQGRQLVP FRGSQQTQQL KQKAQILPNV CNLQSRRCEI GTITTTVTES NIDIPFRDRP FGTGSQQCRE TEIQRPVGEC QRFVEQQMQQ SPRSTRPYQQ RPGQQQQQQR GLQQQCCNEL QNVKRECHCE AIQEVARRVM RQPQQQQQQR RGQFGGQEME TARRVIQNLP NQCDLEVQQC TTCTG // ID 2SS8_HELAN Reviewed; 141 AA. AC P23110; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 31-OCT-2006, entry version 43. DE Albumin-8 precursor (Methionine-rich 2S protein) (SFA8). OS Helianthus annuus (Common sunflower). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; OC Heliantheae; Helianthus. OX NCBI_TaxID=4232; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 39-141. RC TISSUE=Seed; RX MEDLINE=91146568; PubMed=1997318; RA Kortt A.A., Caldwell J.B., Lilley G.G., Higgins T.J.V.; RT "Amino acid and cDNA sequences of a methionine-rich 2S protein from RT sunflower seed (Helianthus annuus L.)."; RL Eur. J. Biochem. 195:329-334(1991). RN [2] RP PROTEIN SEQUENCE OF 39-141. RC STRAIN=cv. Hybrid 246; TISSUE=Seed; RX MEDLINE=97072195; PubMed=8915004; DOI=10.1016/0014-5793(96)01117-9; RA Egorov T.A., Odintsova T.I., Musolyamov A.K., Fido R., Tatham A.S., RA Shewry P.R.; RT "Disulphide structure of a sunflower seed albumin: conserved and RT variant disulphide bonds in the cereal prolamin superfamily."; RL FEBS Lett. 396:285-288(1996). CC -!- FUNCTION: This is a 2S seed storage protein. CC -!- SUBUNIT: Heterodimer; disulfide-linked. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X56686; CAA40015.1; -; mRNA. DR PIR; S14259; S14259. DR PDB; 1S6D; NMR; A=39-141. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR SMART; SM00499; AAI; 1. KW 3D-structure; Direct protein sequencing; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 25 FT PROPEP 26 38 FT /FTId=PRO_0000032153. FT CHAIN 39 141 Albumin-8. FT /FTId=PRO_0000032154. FT DISULFID 49 100 Potential. FT DISULFID 62 89 Potential. FT DISULFID 90 132 Potential. FT DISULFID 102 139 Potential. FT CONFLICT 67 67 M -> N (in Ref. 2). FT STRAND 46 48 FT HELIX 49 55 FT TURN 56 56 FT TURN 59 60 FT HELIX 61 66 FT TURN 67 70 FT STRAND 77 79 FT HELIX 87 95 FT HELIX 98 100 FT HELIX 103 108 FT TURN 109 110 FT TURN 112 113 FT TURN 117 117 FT HELIX 118 131 FT TURN 132 133 FT STRAND 134 137 SQ SEQUENCE 141 AA; 16090 MW; 1E5723B9122C9BD4 CRC64; MARFSIVFAA AGVLLLVAMA PVSEASTTTI ITTIIEENPY GRGRTESGCY QQMEEAEMLN HCGMYLMKNL GERSQVSPRM REEDHKQLCC MQLKNLDEKC MCPAIMMMLN EPMWIRMRDQ VMSMAHNLPI ECNLMSQPCQ M // ID 2SSB_BRANA Reviewed; 178 AA. AC P27740; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 31-OCT-2006, entry version 41. DE Napin-B precursor (1.7S seed storage protein) [Contains: Napin-B small DE chain; Napin-B large chain]. GN Name=NAPB; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Brassica. OX NCBI_TaxID=3708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Svalofs Karat 20516-K; RX MEDLINE=91231016; PubMed=2029903; RA Ericson M.L., Muren E., Gustavsson H.O., Josefsson L.G., Rask L.; RT "Analysis of the promoter region of napin genes from Brassica napus RT demonstrates binding of nuclear protein in vitro to a conserved RT sequence motif."; RL Eur. J. Biochem. 197:741-746(1991). CC -!- FUNCTION: The small, basic, water-soluble napins are one of the CC two major kinds of storage proteins synthesized in the seed during CC its maturation. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- TISSUE SPECIFICITY: Cotyledons and the axis. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X58142; CAA41150.1; -; Genomic_DNA. DR PIR; S15382; S15382. DR HSSP; P24565; 1PNB. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR ProDom; PD002498; Napin; 1. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 21 By similarity. FT PROPEP 22 38 By similarity. FT /FTId=PRO_0000032123. FT CHAIN 39 74 Napin-B small chain (By similarity). FT /FTId=PRO_0000032124. FT PROPEP 75 94 By similarity. FT /FTId=PRO_0000032125. FT CHAIN 95 178 Napin-B large chain (By similarity). FT /FTId=PRO_0000032126. SQ SEQUENCE 178 AA; 20114 MW; 96CE0ADB7CD966E9 CRC64; MANKLFLVSA TLAFFFLLTN ASIYRTVVEF DEDDATNPAG PFRIPKCRKE FQQAQHLKAC QQWLHKQAMQ SGSGPSWTLD GEFDFEDDME NPQGPQQRPP LLQQCCNELH QEEPLCVCPT LKGASKAVKQ QIQQQGQQQG KLQMVSRIYQ TATHLPKVCK IPQVSVCPFQ KTMPGPSY // ID 2SSE_BRANA Reviewed; 186 AA. AC P09893; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 31-OCT-2006, entry version 43. DE Napin embryo-specific precursor (1.7S seed storage protein) [Contains: DE Napin embryo-specific small chain; Napin embryo-specific large chain]. OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Brassica. OX NCBI_TaxID=3708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87308225; PubMed=3040733; RA Scofield S.R., Crouch M.L.; RT "Nucleotide sequence of a member of the napin storage protein family RT from Brassica napus."; RL J. Biol. Chem. 262:12202-12208(1987). CC -!- FUNCTION: The small, basic, water-soluble napins are one of the CC two major kinds of storage proteins synthesized in the seed during CC its maturation. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- TISSUE SPECIFICITY: Cotyledons and the axis. CC -!- DEVELOPMENTAL STAGE: Embryo. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J02782; AAA33007.1; -; Genomic_DNA. DR PIR; A29802; A29802. DR HSSP; P24565; 1PNB. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00496; NAPIN. DR ProDom; PD002498; Napin; 1. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 21 FT PROPEP 22 38 FT /FTId=PRO_0000032127. FT CHAIN 39 76 Napin embryo-specific small chain. FT /FTId=PRO_0000032128. FT PROPEP 77 97 FT /FTId=PRO_0000032129. FT CHAIN 98 186 Napin embryo-specific large chain. FT /FTId=PRO_0000032130. SQ SEQUENCE 186 AA; 21013 MW; 9CAE63D84B160AB3 CRC64; MANKLFLVSA TLALFFLLTN ASVYRTVVEV DEDDATNPAG PFRIPKCRKE FQQAQHLRAC QQWLHKQAMQ PGGGSGPSWT LDGEFDFEDD VENQQQGPQQ RPPPPQQCCN ELHQEEPLCV CPTLKGASKA VRQQVRQQQG QQMQGQQMQQ VISRVYQTAT HLPRVCNIRQ VSICPFQKTM PGPGFY // ID 2SSL_PICGL Reviewed; 172 AA. AC P26986; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 31-OCT-2006, entry version 31. DE 2S seed storage-like protein precursor. OS Picea glauca (White spruce). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Coniferopsida; Coniferales; Pinaceae; Picea. OX NCBI_TaxID=3330; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=PG118; RA Newton C.H.; RL Submitted (NOV-1991) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X63193; CAA44875.1; -; mRNA. DR PIR; S18871; S18871. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Signal; Storage protein. FT SIGNAL 1 35 Potential. FT CHAIN 36 172 2S seed storage-like protein. FT /FTId=PRO_0000032166. SQ SEQUENCE 172 AA; 20393 MW; 4C29E343B61003FB CRC64; MGVFSPSTTR LTLKWFSLSV ALFLLFHWGI PSVDGHEDNM YGEEIQQQRR SCDPQRDPQR LSSCRDYLER RREQPSERCC EELQRMSPQC RCQAIQQMLD QSLSYDSFMD SDSQEDAPLN QRRRRREGRG REEEEAMERA AYLPNTCNVR EPPRRCDIQR HSRYSMTGSS FK // ID 2SS_BEREX Reviewed; 146 AA. AC P04403; P04402; Q9LRC2; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 2. DT 31-OCT-2006, entry version 61. DE 2S sulfur-rich seed storage protein precursor (Allergen Ber e 1) DE [Contains: 2S sulfur-rich seed storage protein small chain (2S albumin DE small subunit); 2S sulfur-rich seed storage protein large chain 1B (2S DE albumin large subunit)]. GN Name=BE2S1; GN and GN Name=BE2S2; OS Bertholletia excelsa (Brazil nut). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; Ericales; Lecythidaceae; Bertholletia. OX NCBI_TaxID=3645; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Altenbach S.B., Pearson K.W., Leung F.W., Sun S.S.M.; RT "Cloning and sequence analysis of a cDNA encoding a Brazil nut protein RT exceptionally rich in methionine."; RL Plant Mol. Biol. 8:239-250(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Bassuener R.; RL Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91370890; PubMed=1840683; RA Gander E.S., Holmstroem K.O., de Paiva G.R., de Castro L.A.B., RA Carneiro M., Grossi de Sa M.F.; RT "Isolation, characterization and expression of a gene coding for a 2S RT albumin from Bertholletia excelsa (Brazil nut)."; RL Plant Mol. Biol. 16:437-448(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Yamauchi D.; RT "Brazil nut 2S albumin was synthesized in a transgenic French bean RT seed with a promoter of the gene for canavalin, 7S globulin from RT Canavalia gladiata."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP PROTEIN SEQUENCE OF 37-64 AND 70-142. RX MEDLINE=87004679; PubMed=3758080; RA Ampe C., van Damme J., de Castro L.A.B., Sampaio M.J.A.M., RA van Montagu M., Vandekerckhove J.; RT "The amino-acid sequence of the 2S sulphur-rich proteins from seeds of RT Brazil nut (Bertholletia excelsa H.B.K.)."; RL Eur. J. Biochem. 159:597-604(1986). RN [6] RP 3D-STRUCTURE MODELING, GLYCOSYLATION, AND DISULFIDE BONDS. RX MEDLINE=22309196; PubMed=12421566; DOI=10.1016/S0022-2836(02)01061-6; RA Alcocer M.J., Murtagh G.J., Bailey K., Dumoulin M., Meseguer A.S., RA Parker M.J., Archer D.B.; RT "The disulphide mapping, folding and characterisation of recombinant RT Ber e 1, an allergenic protein, and SFA8, two sulphur-rich 2S plant RT albumins."; RL J. Mol. Biol. 324:165-175(2002). CC -!- FUNCTION: This is a 2S seed storage protein. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by disulfide bonds. CC -!- ALLERGEN: Causes an allergic reaction in human. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M17146; AAA33010.1; -; mRNA. DR EMBL; X57027; CAA40343.1; -; Genomic_DNA. DR EMBL; X57028; CAA40344.1; -; Genomic_DNA. DR EMBL; X54490; CAA38362.1; -; Genomic_DNA. DR EMBL; X54491; CAA38363.1; ALT_SEQ; Genomic_DNA. DR EMBL; AB044391; BAA96554.1; -; Genomic_DNA. DR PIR; A25802; A25802. DR PIR; S14946; S14946. DR PDB; 1GYS; Model; A=37-64, B=69-142. DR InterPro; IPR006106; Allergen/soft/tryp_amyl_inhib. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00808; AMLASEINHBTR. DR PRINTS; PR00496; NAPIN. DR SMART; SM00499; AAI; 1. KW 3D-structure; Allergen; Direct protein sequencing; Polymorphism; KW Pyrrolidone carboxylic acid; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 22 FT PROPEP 23 36 FT /FTId=PRO_0000032105. FT CHAIN 37 64 2S sulfur-rich seed storage protein small FT chain. FT /FTId=PRO_0000032106. FT PROPEP 65 69 FT /FTId=PRO_0000032107. FT CHAIN 70 142 2S sulfur-rich seed storage protein large FT chain 1B. FT /FTId=PRO_0000032108. FT PROPEP 143 146 FT /FTId=PRO_0000032109. FT MOD_RES 37 37 Pyrrolidone carboxylic acid. FT DISULFID 40 92 Interchain (between small and large FT chains). FT DISULFID 53 81 Interchain (between small and large FT chains). FT DISULFID 82 130 FT DISULFID 94 137 FT VARIANT 91 91 S -> E (in variant 1A). FT CONFLICT 38 39 EE -> QQ (in Ref. 5). FT CONFLICT 102 103 MR -> RM (in Ref. 4). FT CONFLICT 107 107 E -> K (in Ref. 4). FT CONFLICT 122 122 L -> M (in Ref. 5). FT CONFLICT 126 126 I -> L (in Ref. 5). FT HELIX 38 46 FT TURN 47 47 FT TURN 52 53 FT HELIX 54 59 FT TURN 60 61 FT HELIX 76 78 FT HELIX 80 86 FT TURN 87 88 FT TURN 90 98 FT HELIX 99 104 FT TURN 108 109 FT TURN 115 117 FT HELIX 118 125 FT TURN 128 131 FT STRAND 133 135 SQ SEQUENCE 146 AA; 16911 MW; A7DF778FD766410D CRC64; MAKISVAAAA LLVLMALGHA TAFRATVTTT VVEEENQEEC REQMQRQQML SHCRMYMRQQ MEESPYQTMP RRGMEPHMSE CCEQLEGMDE SCRCEGLRMM MMRMQQEEMQ PRGEQMRRMM RLAENIPSRC NLSPMRCPMG GSIAGF // ID 2SS_CUCMA Reviewed; 141 AA. AC Q39649; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-JAN-2007, entry version 35. DE 2S albumin precursor [Contains: 2S albumin small chain; 2S albumin DE large chain]. OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3661; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-56 AND 75-94, AND RP SUBCELLULAR LOCATION. RC STRAIN=cv. Kurokawa Amakuri Nankin; TISSUE=Cotyledon; RX MEDLINE=94100993; PubMed=8275099; RA Hara-Nishimura I., Takeuchi Y., Inoue K., Nishimura M.; RT "Vesicle transport and processing of the precursor to 2S albumin in RT pumpkin."; RL Plant J. 4:793-800(1993). RN [2] RP PROTEIN SEQUENCE OF 36-45 AND 75-84. RC TISSUE=Cotyledon; RX MEDLINE=92077151; PubMed=1743299; DOI=10.1016/0014-5793(91)81349-D; RA Hara-Nishimura I., Inoue K., Nishimura M.; RT "A unique vacuolar processing enzyme responsible for conversion of RT several proprotein precursors into the mature forms."; RL FEBS Lett. 294:89-93(1991). CC -!- FUNCTION: This is a 2S seed storage protein. CC -!- SUBUNIT: The mature protein consists of a small and a large chain CC linked by 2 disulfide bonds. CC -!- SUBCELLULAR LOCATION: Vacuole; aleurone grain. Vacuole. CC Note=Cotyledonary membrane-bound vacuolar protein bodies. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D16560; BAA03993.1; -; mRNA. DR HSSP; P01089; 1PSY. DR GO; GO:0000322; C:storage vacuole; IDA:UniProtKB. DR GO; GO:0045735; F:nutrient reservoir activity; TAS:UniProtKB. DR InterPro; IPR000480; Glutelin. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00211; GLUTELIN. DR PRINTS; PR00496; NAPIN. DR SMART; SM00499; AAI; 1. KW Direct protein sequencing; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 22 FT PROPEP 23 35 FT /FTId=PRO_0000032146. FT CHAIN 36 ? 2S albumin small chain. FT /FTId=PRO_0000032147. FT CHAIN 75 141 2S albumin large chain. FT /FTId=PRO_0000032148. FT DISULFID 43 97 Interchain (between small and large FT chains) (By similarity). FT DISULFID 55 86 Interchain (between small and large FT chains) (By similarity). FT DISULFID 87 132 By similarity. FT DISULFID 99 139 By similarity. SQ SEQUENCE 141 AA; 16597 MW; 3E812A81C5E67EB5 CRC64; MARLTSIIAL FAVALLVADA YAYRTTITTV EVEENRQGRE ERCRQMSARE ELRSCEQYLR QQSRDVLQMR GIENPWRREG GSFDECCREL KNVDEECRCD MLEEIAREEQ RQARGQEGRQ MLQKARNLPS MCGIRPQRCD F // ID 2SS_RICCO Reviewed; 258 AA. AC P01089; Q9S872; Q9S873; Q9S874; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 2. DT 20-FEB-2007, entry version 62. DE 2S albumin precursor (Allergen Ric c 1/3) [Contains: Allergen Ric c 3 DE small chain (4.7 kDa napin-like protein small chain) (RS1A) (CB-1A DE small chain); Allergen Ric c 3 large chain (RL1) (CB-1A large chain); DE Allergen Ric c 1 small chain (2S albumin small chain) (4 kDa napin- DE like protein small chain) (RS2B); Allergen Ric c 1 large chain (2S DE albumin large chain) (7.3 kDa napin-like protein large chain) (RL2)]. OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Malpighiales; Euphorbiaceae; Acalyphoideae; OC Acalypheae; Ricinus. OX NCBI_TaxID=3988; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROCESSING OF PRECURSOR, BLOCKAGE RP OF N-TERMINUS, VARIANT THR-74, AND DEVELOPMENTAL STAGE. RC TISSUE=Endosperm; RX MEDLINE=91109729; PubMed=2274038; RA Irwin S.D., Keen J.N., Findlay J.B.C., Lord J.M.; RT "The Ricinus communis 2S albumin precursor: a single preproprotein may RT be processed into two different heterodimeric storage proteins."; RL Mol. Gen. Genet. 222:400-408(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Endosperm; RX MEDLINE=91016940; PubMed=2216785; DOI=10.1093/nar/18.19.5890; RA Irwin S.D., Lord J.M.; RT "Nucleotide sequence of a Ricinus communis 2S albumin precursor RT gene."; RL Nucleic Acids Res. 18:5890-5890(1990). RN [3] RP PROTEIN SEQUENCE OF 157-190 AND 194-258. RX MEDLINE=83082772; PubMed=7174664; RA Sharief F.S., Li S.S.-L.; RT "Amino acid sequence of small and large subunits of seed storage RT protein from Ricinus communis."; RL J. Biol. Chem. 257:14753-14759(1982). RN [4] RP PROTEIN SEQUENCE OF 36-76; 157-190 AND 194-258, AND PHOSPHORYLATION. RX MEDLINE=97135090; PubMed=8980648; DOI=10.1016/S0167-4838(96)00133-1; RA Neumann G.M., Condron R., Polya G.M.; RT "Purification and sequencing of napin-like protein small and large RT chains from Momordica charantia and Ricinus communis seeds and RT determination of sites phosphorylated by plant Ca(2+)-dependent RT protein kinase."; RL Biochim. Biophys. Acta 1298:223-240(1996). RN [5] RP PROTEIN SEQUENCE OF 36-72; 87-153; 157-190 AND 194-258, BLOCKAGE OF RP N-TERMINUS, AND NOMENCLATURE. RX MEDLINE=98090364; PubMed=9430499; DOI=10.1159/000023833; RA Bashir M.E., Hubatsch I., Leinenbach H.P., Zeppezauer M., RA Panzani R.C., Hussein I.H.; RT "Ric c 1 and Ric c 3, the allergenic 2S albumin storage proteins of RT Ricinus communis: complete primary structures and phylogenetic RT relationships."; RL Int. Arch. Allergy Immunol. 115:73-82(1998). RN [6] RP SIMILARITY TO PROTEINASE INHIBITORS. RX MEDLINE=83308577; PubMed=6615448; RA Odani S., Koide T., Ono T., Ohnishi K.; RT "Structural relationship between barley (Hordeum vulgare) trypsin RT inhibitor and castor-bean (Ricinus communis) storage protein."; RL Biochem. J. 213:543-545(1983). RN [7] RP STRUCTURE BY NMR OF 36-156, AND DISULFIDE BONDS. RX PubMed=14636051; DOI=10.1021/bi0352217; RA Pantoja-Uceda D., Bruix M., Gimenez-Gallego G., Rico M., Santoro J.; RT "Solution structure of RicC3, a 2S albumin storage protein from RT Ricinus communis."; RL Biochemistry 42:13839-13847(2003). CC -!- FUNCTION: 2S seed storage proteins. CC -!- SUBUNIT: The 2 mature proteins consist of heterodimers of a small CC and a large chain; disulfide-linked. CC -!- DEVELOPMENTAL STAGE: Expressed in ripening seeds during testa CC formation and desiccation. CC -!- PTM: The N-terminus of both large chains is blocked. CC -!- PTM: The C-terminus of the allergen Ric c 1 and allergen Ric c 3 CC small chains are heterogeneous and the length of the chains can CC vary from 33 to 36 amino acids and from 36 to 40 amino acids CC respectively. CC -!- ALLERGEN: Causes an allergic reaction in human. CC -!- BIOTECHNOLOGY: Ric C 3 constitutes the peptidic component of the CC immunomodulator Inmunoferon. CC -!- MISCELLANEOUS: The allergen Ric c 1 small chain acts as a CC calmodulin (CaM) antagonist that inhibits CaM-dependent myosin CC light chain kinase with IC(50)= 0.25 uM. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X54158; CAA38097.1; -; Genomic_DNA. DR PIR; S11499; RZCS. DR PDB; 1PSY; NMR; A=36-156. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000617; Napin. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 2. DR PRINTS; PR00496; NAPIN. DR SMART; SM00499; AAI; 2. KW 3D-structure; Allergen; Cleavage on pair of basic residues; KW Direct protein sequencing; Phosphorylation; Polymorphism; KW Pyrrolidone carboxylic acid; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 24 Potential. FT PROPEP 25 35 FT /FTId=PRO_0000032162. FT CHAIN 36 76 Allergen Ric c 3 small chain. FT /FTId=PRO_0000041857. FT PROPEP 77 86 FT /FTId=PRO_0000041858. FT CHAIN 87 153 Allergen Ric c 3 large chain. FT /FTId=PRO_0000041859. FT PROPEP 154 156 FT /FTId=PRO_0000041860. FT CHAIN 157 190 Allergen Ric c 1 small chain. FT /FTId=PRO_0000032163. FT PROPEP 191 193 FT /FTId=PRO_0000032164. FT CHAIN 194 258 Allergen Ric c 1 large chain. FT /FTId=PRO_0000032165. FT MOD_RES 69 69 Phosphoserine. FT MOD_RES 87 87 Pyrrolidone carboxylic acid (Probable). FT MOD_RES 194 194 Pyrrolidone carboxylic acid. FT DISULFID 49 108 Interchain (between Ric c 3 small and Ric FT c 3 large chains). FT DISULFID 61 97 Interchain (between Ric c 3 small and Ric FT c 3 large chains). FT DISULFID 98 145 FT DISULFID 110 149 FT DISULFID 162 212 Interchain (between Ric c 1 small and Ric FT c 1 large chains) (By similarity). FT DISULFID 175 201 Interchain (between Ric c 1 small and Ric FT c 1 large chains) (By similarity). FT DISULFID 202 249 By similarity. FT DISULFID 214 256 By similarity. FT VARIANT 74 74 P -> T. FT CONFLICT 194 194 Q -> E (in Ref. 4). FT CONFLICT 222 222 E -> Q (in Ref. 3). FT CONFLICT 226 229 Missing (in Ref. 3). FT CONFLICT 234 234 D -> N (in Ref. 3). FT CONFLICT 255 255 E -> Q (in Ref. 3). FT STRAND 44 48 FT HELIX 49 53 FT TURN 54 55 FT TURN 57 58 FT HELIX 61 66 FT STRAND 67 69 FT STRAND 84 86 FT STRAND 88 90 FT HELIX 92 101 FT TURN 102 103 FT HELIX 108 123 FT TURN 124 125 FT TURN 128 129 FT HELIX 132 145 FT TURN 146 146 FT TURN 149 151 SQ SEQUENCE 258 AA; 29290 MW; 27874CFC50E41072 CRC64; MAKLIPTIAL VSVLLFIIAN ASFAYRTTIT TIEIDESKGE REGSSSQQCR QEVQRKDLSS CERYLRQSSS RRSPGEEVLR MPGDENQQQE SQQLQQCCNQ VKQVRDECQC EAIKYIAEDQ IQQGQLHGEE SERVAQRAGE IVSSCGVRCM RQTRTNPSQQ GCRGQIQEQQ NLRQCQEYIK QQVSGQGPRR SDNQERSLRG CCDHLKQMQS QCRCEGLRQA IEQQQSQGQL QGQDVFEAFR TAANLPSMCG VSPTECRF // ID 2SS_SOYBN Reviewed; 158 AA. AC P19594; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 20-FEB-2007, entry version 47. DE 2S albumin precursor (GM2S-1) [Contains: 2S albumin small chain DE (Aspartic acid-rich peptide); 2S albumin large chain (8 kDa DE methionine-rich protein) (8 kDa MRP)]. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Hodgson 78; TISSUE=Cotyledon; RA Galvez A.F., Revilleza M.J.R., de Lumen B.O.; RT "A novel methionine-rich protein from soybean cotyledon: cloning and RT characterization of cDNA."; RL (er) Plant Gene Register PGR97-103. RN [2] RP PROTEIN SEQUENCE OF 22-64. RC TISSUE=Seed; RX MEDLINE=87280104; PubMed=3611081; RA Odani S., Koide T., Ono T.; RT "Amino acid sequence of a soybean (Glycine max) seed polypeptide RT having a poly(L-aspartic acid) structure."; RL J. Biol. Chem. 262:10502-10505(1987). RN [3] RP PROTEIN SEQUENCE OF 82-96. RA Revilleza M.J., Galvez A.F., Krenz D.C., de Lumen B.O.; RT "An 8 kDa methionine-rich protein (MRP) from soybean (Glycine max) RT cotyledon: identification, purification and N-terminal sequence."; RL J. Agric. Food Chem. 44:2930-2935(1996). CC -!- FUNCTION: This is a 2S seed storage protein. CC -!- SUBUNIT: The protein consists of two chains linked by 2 disulfide CC bonds. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF005030; AAB71140.1; -; mRNA. DR PIR; T05710; T05710. DR UniGene; Gma.7113; -. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR013771; Trypsin/amylase_inhib. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR SMART; SM00499; AAI; 1. KW Direct protein sequencing; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 21 FT CHAIN 22 64 2S albumin small chain. FT /FTId=PRO_0000032158. FT PROPEP 65 81 FT /FTId=PRO_0000032159. FT CHAIN 82 158 2S albumin large chain. FT /FTId=PRO_0000032160. FT MOTIF 54 56 Cell attachment site (Potential). FT COMPBIAS 56 64 Poly-Asp. FT COMPBIAS 88 91 Poly-Glu. SQ SEQUENCE 158 AA; 18460 MW; C1F42723B0F62D81 CRC64; MTKFTILLIS LLFCIAHTCS ASKWQHQQDS CRKQLQGVNL TPCEKHIMEK IQGRGDDDDD DDDDNHILRT MRGRINYIRR NEGKDEDEEE EGHMQKCCTE MSELRSPKCQ CKALQKIMEN QSEELEEKQK KKMEKELINL ATMCRFGPMI QCDLSSDD // ID 32C7_ANCSP Reviewed; 37 AA. AC P84027; DT 30-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 31-OCT-2006, entry version 10. DE Neurotoxin ANC32C7 (Fragment). OS Ancylometes sp. (South American fishing spider). OC Eukaryota; Metazoa; Arthropoda; Chelicerata; Arachnida; Araneae; OC Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Ancylometes. OX NCBI_TaxID=280265; RN [1] RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS RP SPECTROMETRY. RC TISSUE=Venom; RA Richardson M., Pimenta A.M.C., Bemquerer M.P., Santoro M.M., RA Figueiredo S.G., Cordeiro M.N.; RT "Protein ANC32C7 from venom of South American fishing spider RT (Ancylometes spp.) has sequence similarities to omega agatoxins and RT other neurotoxins."; RL Submitted (JUN-2004) to Swiss-Prot. CC -!- FUNCTION: Omega-agatoxins are antagonists of voltage-sensitive CC calcium channels. They block neuromuscular transmission CC presynaptically. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- MASS SPECTROMETRY: MW=8825.5; METHOD=Electrospray; RANGE=1-?; CC NOTE=Ref.1. CC -!- SIMILARITY: Belongs to the omega-agatoxin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR InterPro; IPR013605; Toxin_34. DR Pfam; PF08396; Toxin_34; 1. DR PROSITE; PS60023; OMEGA_AGA_II_III; 1. KW Calcium channel inhibitor; Direct protein sequencing; KW Ionic channel inhibitor; Neurotoxin; Presynaptic neurotoxin; Toxin. FT CHAIN 1 >37 Neurotoxin ANC32C7. FT /FTId=PRO_0000087611. FT NON_TER 37 37 SQ SEQUENCE 37 AA; 4066 MW; 1EAE19832B32148C CRC64; SDNEFPSGCI EFGKECDLDK GNCQCCRRNG YCSCAVN // ID 34KD_BACCE Reviewed; 10 AA. AC P83064; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 09-JAN-2007, entry version 14. DE 34 kDa protein (Fragment). OS Bacillus cereus. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1396; RN [1] RP PROTEIN SEQUENCE, AND INDUCTION. RC STRAIN=NCIMB 11796 / DSM 626; RX PubMed=11851817; DOI=10.1046/j.1365-2672.2001.01478.x; RA Browne N., Dowds B.C.A.; RT "Heat and salt stress in the food pathogen Bacillus cereus."; RL J. Appl. Microbiol. 91:1085-1094(2001). CC -!- INDUCTION: By salt stress and heat shock. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Direct protein sequencing; Heat shock. FT CHAIN 1 >10 34 kDa protein. FT /FTId=PRO_0000270969. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1124 MW; D471FF9B01A69862 CRC64; MLVGMTEMVN // ID 34KD_MYCBO Reviewed; 303 AA. AC P65638; P71556; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 31-OCT-2006, entry version 14. DE 34 kDa antigenic protein homolog. GN OrderedLocusNames=Mb0979; OS Mycobacterium bovis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1765; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX MEDLINE=22709107; PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., RA Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., RA Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., RA Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (Potential). CC -!- SIMILARITY: To M.paratuberculosis 34 kDa antigenic protein. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX248337; CAD93840.1; -; Genomic_DNA. DR GenomeReviews; BX248333_GR; Mb0979. DR KEGG; mbo:Mb0979; -. KW Complete proteome; Membrane; Transmembrane. FT CHAIN 1 303 34 kDa antigenic protein homolog. FT /FTId=PRO_0000064362. FT TRANSMEM 42 62 Potential. FT TRANSMEM 77 97 Potential. FT TRANSMEM 102 122 Potential. FT TRANSMEM 134 154 Potential. SQ SEQUENCE 303 AA; 30204 MW; 4FE18A077FDFD8B5 CRC64; MTYSPGNPGY PQAQPAGSYG GVTPSFAHAD EGASKLPMYL NIAVAVLGLA AYFASFGPMF TLSTELGGGD GAVSGDTGLP VGVALLAALL AGVALVPKAK SHVTVVAVLG VLGVFLMVSA TFNKPSAYST GWALWVVLAF IVFQAVAAVL ALLVETGAIT APAPRPKFDP YGQYGRYGQY GQYGVQPGGY YGQQGAQQAA GLQSPGPQQS PQPPGYGSQY GGYSSSPSQS GSGYTAQPPA QPPAQSGSQQ SHQGPSTPPT GFPSFSPPPP VSAGTGSQAG SAPVNYSNPS GGEQSSSPGG APV // ID 34KD_MYCPA Reviewed; 298 AA. AC Q04959; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 31-OCT-2006, entry version 38. DE 34 kDa antigenic protein. GN OrderedLocusNames=MAP_0900; OS Mycobacterium paratuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=1770; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93328703; PubMed=8335649; RA Gilot P., de Kesel M., Machtelinckx L., Coene M., Cocito C.; RT "Isolation and sequencing of the gene coding for an antigenic 34- RT kilodalton protein of Mycobacterium paratuberculosis."; RL J. Bacteriol. 175:4930-4935(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10; RX PubMed=16116077; DOI=10.1073/pnas.0505662102; RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., RA Banerji N., Kanjilal S., Kapur V.; RT "The complete genome sequence of Mycobacterium avium subspecies RT paratuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein. CC -!- SIMILARITY: To M.tuberculosis RV0954. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X68102; CAA48221.1; -; Genomic_DNA. DR EMBL; AE016958; AAS03217.1; -; Genomic_DNA. DR PIR; A40616; A40616. DR GenomeReviews; AE016958_GR; MAP_0900. DR KEGG; mpa:MAP0900; -. KW Complete proteome; Membrane; Transmembrane. FT CHAIN 1 298 34 kDa antigenic protein. FT /FTId=PRO_0000064363. FT TRANSMEM 42 62 Potential. FT TRANSMEM 77 97 Potential. FT TRANSMEM 102 122 Potential. FT TRANSMEM 134 154 Potential. SQ SEQUENCE 298 AA; 29565 MW; B2E57AA2077F0D3D CRC64; MTYSPGSPGY PPAQSGGTYA GATPSFAKDD DGKSKLPLYL NIAVVALGFA AYLLNFGPTF TIGADLGPGI GGRAGDAGTA VVVALLAALL AGLGLLPKAK SYVGVVAVVA VLAALLAITE TINLPAGFAI GWAMWPLVAC VVLQAIAAVV VVLLDAGVIT APAPRPKYDP YAQYGQYGQY GQYGQQPYYG QPGGQPGGQP GGQQHSPQGY GSQYGGYGQG GAPTGGFGAQ PSPQSGPQQS AQQQGPSTPP TGFPSFSPPP NVGGGSDSGS ATANYSEQAG GQQSYGQEPS SPSGPTPA // ID 34KD_MYCTU Reviewed; 303 AA. AC P65637; P71556; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 31-OCT-2006, entry version 16. DE 34 kDa antigenic protein homolog. GN OrderedLocusNames=Rv0954, MT0981; ORFNames=MTCY10D7.20c; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (Potential). CC -!- SIMILARITY: To M.paratuberculosis 34 kDa antigenic protein. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX842575; CAB01996.1; -; Genomic_DNA. DR EMBL; AE000516; AAK45229.1; -; Genomic_DNA. DR PIR; H70716; H70716. DR GenomeReviews; AE000516_GR; MT0981. DR GenomeReviews; AL123456_GR; Rv0954. DR KEGG; mtc:MT0981; -. DR KEGG; mtu:Rv0954; -. DR TIGR; MT0981; -. DR TubercuList; Rv0954; -. KW Complete proteome; Membrane; Transmembrane. FT CHAIN 1 303 34 kDa antigenic protein homolog. FT /FTId=PRO_0000064364. FT TRANSMEM 42 62 Potential. FT TRANSMEM 77 97 Potential. FT TRANSMEM 102 122 Potential. FT TRANSMEM 134 154 Potential. SQ SEQUENCE 303 AA; 30204 MW; 4FE18A077FDFD8B5 CRC64; MTYSPGNPGY PQAQPAGSYG GVTPSFAHAD EGASKLPMYL NIAVAVLGLA AYFASFGPMF TLSTELGGGD GAVSGDTGLP VGVALLAALL AGVALVPKAK SHVTVVAVLG VLGVFLMVSA TFNKPSAYST GWALWVVLAF IVFQAVAAVL ALLVETGAIT APAPRPKFDP YGQYGRYGQY GQYGVQPGGY YGQQGAQQAA GLQSPGPQQS PQPPGYGSQY GGYSSSPSQS GSGYTAQPPA QPPAQSGSQQ SHQGPSTPPT GFPSFSPPPP VSAGTGSQAG SAPVNYSNPS GGEQSSSPGG APV // ID 35KD_MYCTU Reviewed; 270 AA. AC P31511; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 31-OCT-2006, entry version 44. DE 35 kDa protein. GN OrderedLocusNames=Rv2744c, MT2815; ORFNames=MTV002.09c; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 25177 / H37Ra; RX MEDLINE=90378140; PubMed=2119046; DOI=10.1016/0923-2508(90)90068-2; RA O'Connor S.P., Rumschlag H.S., Mayer L.W.; RT "Nucleotide sequence of the gene encoding the 35-kDa protein of RT Mycobacterium tuberculosis."; RL Res. Microbiol. 141:407-423(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the pspA/IM30 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M69187; AAA73065.1; -; Genomic_DNA. DR EMBL; BX842580; CAE55517.1; -; Genomic_DNA. DR EMBL; AE000516; AAK47135.1; -; Genomic_DNA. DR PIR; A60176; A60176. DR GenomeReviews; AE000516_GR; MT2815. DR GenomeReviews; AL123456_GR; Rv2744c. DR KEGG; mtc:MT2815; -. DR KEGG; mtu:Rv2744c; -. DR TIGR; MT2815; -. DR TubercuList; Rv2744c; -. DR LinkHub; P31511; -. DR InterPro; IPR007157; PspA_IM30. DR Pfam; PF04012; PspA_IM30; 1. KW Complete proteome. FT CHAIN 1 270 35 kDa protein. FT /FTId=PRO_0000166290. SQ SEQUENCE 270 AA; 29258 MW; AB018731FF7DEC40 CRC64; MANPFVKAWK YLMALFSSKI DEHADPKVQI QQAIEEAQRT HQALTQQAAQ VIGNQRQLEM RLNRQLADIE KLQVNVRQAL TLADQATAAG DAAKATEYNN AAEAFAAQLV TAEQSVEDLK TLHDQALSAA AQAKKAVERN AMVLQQKIAE RTKLLSQLEQ AKMQEQVSAS LRSMSELAAP GNTPSLDEVR DKIERRYANA IGSAELAESS VQGRMLEVEQ AGIQMAGHSR LEQIRASMRG EALPAGGTTA TPRPATETSG GAIAEQPYGQ // ID 3BHD_COMTE Reviewed; 254 AA. AC P19871; Q52587; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 23-JAN-2007, entry version 53. DE 3-beta-hydroxysteroid dehydrogenase (EC 1.1.1.51). OS Comamonas testosteroni (Pseudomonas testosteroni). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=285; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 11996 / DSM 50244 / JCM 5832 / NCIB 8955 / NCTC 10698; RX MEDLINE=93176721; PubMed=8382516; DOI=10.1016/0960-0760(93)90020-W; RA Abalain J.H., di Stefano S., Amet Y., Quemener E., RA Abalain-Colloc M.L., Floch H.H.; RT "Cloning, DNA sequencing and expression of (3-17)beta hydroxysteroid RT dehydrogenase from Pseudomonas testosteroni."; RL J. Steroid Biochem. Mol. Biol. 44:133-139(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 11996 / DSM 50244 / JCM 5832 / NCIB 8955 / NCTC 10698; RX PubMed=15026087; DOI=10.1016/j.jsbmb.2003.10.010; RA Pruneda-Paz J.L., Linares M., Cabrera J.E., Genti-Raimondi S.; RT "Identification of a novel steroid inducible gene associated with the RT beta hsd locus of Comamonas testosteroni."; RL J. Steroid Biochem. Mol. Biol. 88:91-100(2004). RN [3] RP PROTEIN SEQUENCE OF 2-254. RX MEDLINE=91224127; PubMed=2026158; RA Yin S.-J., Vagelopoulos N., Lundquist G., Joernvall H.; RT "Pseudomonas 3 beta-hydroxysteroid dehydrogenase. Primary structure RT and relationships to other steroid dehydrogenases."; RL Eur. J. Biochem. 197:359-365(1991). RN [4] RP CRYSTALLIZATION, AND SUBUNIT. RC STRAIN=ATCC 11996 / DSM 50244 / JCM 5832 / NCIB 8955 / NCTC 10698; RX MEDLINE=96184891; PubMed=8617258; RA Benach J., Knapp S., Oppermann U.C.T., Haegllund O., Joernvall H., RA Ladenstein R.; RT "Crystallization and crystal packing of recombinant 3 (or 17) beta- RT hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996."; RL Eur. J. Biochem. 236:144-148(1996). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS). RX PubMed=12475215; DOI=10.1021/bi0203684; RA Benach J., Filling C., Oppermann U.C.T., Roversi P., Bricogne G., RA Berndt K.D., Joernvall H., Ladenstein R.; RT "Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at RT 1.2 A resolution: a model for multiple steroid recognition."; RL Biochemistry 41:14659-14668(2002). CC -!- CATALYTIC ACTIVITY: Testosterone + NAD(P)(+) = androst-4-ene-3,17- CC dione + NAD(P)H. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- WEB RESOURCE: NAME=Worthington enzyme manual; CC URL="http://www.worthington-biochem.com/STDH/". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X63379; CAA44977.1; -; Genomic_DNA. DR EMBL; U41265; AAA25742.1; -; Genomic_DNA. DR PIR; S48129; S48129. DR PDB; 1HXH; X-ray; A/B/C/D=1-254. DR GO; GO:0030283; F:3(or 17)beta-hydroxysteroid dehydrogenase a...; IEA:EC. DR InterPro; IPR002347; ADH_short_C2. DR InterPro; IPR002198; SDR. DR PANTHER; PTHR19410; ADH_short; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. KW 3D-structure; Direct protein sequencing; Lipid metabolism; NAD; KW Oxidoreductase; Steroid metabolism. FT INIT_MET 1 1 Removed. FT CHAIN 2 254 3-beta-hydroxysteroid dehydrogenase. FT /FTId=PRO_0000054446. FT NP_BIND 12 40 NAD (By similarity). FT ACT_SITE 152 152 Proton acceptor (By similarity). FT BINDING 61 61 NAD (By similarity). FT BINDING 139 139 Substrate (By similarity). FT BINDING 156 156 NAD; ribose group (By similarity). FT CONFLICT 14 15 GG -> VV (in Ref. 1). FT CONFLICT 41 41 Missing (in Ref. 1). FT CONFLICT 178 178 R -> RR (in Ref. 1). FT CONFLICT 241 241 S -> G (in Ref. 3). FT TURN 4 7 FT STRAND 9 12 FT TURN 13 16 FT HELIX 18 29 FT TURN 30 31 FT STRAND 33 37 FT HELIX 41 51 FT TURN 53 54 FT STRAND 55 58 FT TURN 62 63 FT HELIX 65 79 FT STRAND 84 87 FT TURN 97 99 FT HELIX 102 112 FT TURN 113 113 FT HELIX 114 127 FT TURN 128 130 FT STRAND 132 137 FT HELIX 140 142 FT TURN 143 143 FT TURN 147 148 FT HELIX 150 173 FT TURN 174 174 FT STRAND 177 187 FT HELIX 190 195 FT TURN 198 199 FT HELIX 202 205 FT TURN 209 211 FT TURN 213 214 FT HELIX 220 231 FT HELIX 233 235 FT TURN 236 237 FT STRAND 242 248 FT TURN 250 253 SQ SEQUENCE 254 AA; 26952 MW; FB6EC90B151975DB CRC64; MTNRLQGKVA LVTGGASGVG LEVVKLLLGE GAKVAFSDIN EAAGQQLAAE LGERSMFVRH DVSSEADWTL VMAAVQRRLG TLNVLVNNAG ILLPGDMETG RLEDFSRLLK INTESVFIGC QQGIAAMKET GGSIINMASV SSWLPIEQYA GYSASKAAVS ALTRAAALSC RKQGYAIRVN SIHPDGIYTP MMQASLPKGV SKEMVLHDPK LNRAGRAYMP ERIAQLVLFL ASDESSVMSG SELHADNSIL GMGL // ID 3BHS1_HUMAN Reviewed; 373 AA. AC P14060; Q14545; Q8IV65; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 06-FEB-2007, entry version 80. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I (3- DE beta-HSD I) (Trophoblast antigen FDO161G) [Includes: 3-beta-hydroxy- DE Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene DE steroid dehydrogenase) (Progesterone reductase); Steroid Delta- DE isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)]. GN Name=HSD3B1; Synonyms=3BH, HSDB3A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-30. RX MEDLINE=89384668; PubMed=2779585; RA Luu-The V., Lachance Y., Labrie F., Leblanc G., Thomas J.L., RA Strickler R.C., Labrie C.; RT "Full length cDNA structure and deduced amino acid sequence of human 3 RT beta-hydroxy-5-ene steroid dehydrogenase."; RL Mol. Endocrinol. 3:1310-1312(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX MEDLINE=90228249; PubMed=2139411; RA Lorence M.C., Murry B.A., Trant J.M., Mason J.I.; RT "Human 3 beta-hydroxysteroid dehydrogenase/delta 5-->4isomerase from RT placenta: expression in nonsteroidogenic cells of a protein that RT catalyzes the dehydrogenation/isomerization of C21 and C19 steroids."; RL Endocrinology 126:2493-2498(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91186993; PubMed=2082186; RA Lorence M.C., Corbin C.J., Kamimura N., Mahendroo M.S., Mason J.I.; RT "Structural analysis of the gene encoding human 3 beta-hydroxysteroid RT dehydrogenase/delta 5-->4-isomerase."; RL Mol. Endocrinol. 4:1850-1855(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91056097; PubMed=2243100; RA Lachance Y., Luu-The V., Labrie C., Simard J., Dumont M., RA Launoit Y.D., Guerin S., Leblanc G., Labrie F.; RT "Characterization of human 3 beta-hydroxysteroid dehydrogenase/delta RT 5-delta 4-isomerase gene and its expression in mammalian cells."; RL J. Biol. Chem. 265:20469-20475(1990). RN [5] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Placenta; RX MEDLINE=92015040; PubMed=1920284; RA Nickson D.A., McBride M.W., Zeinali S., Hawes C.S., Petropoulos A., RA Mueller U.W., Sutcliffe R.G.; RT "Molecular cloning and expression of human trophoblast antigen FDO161G RT and its identification as 3 beta-hydroxy-5-ene steroid RT dehydrogenase."; RL J. Reprod. Fertil. 93:149-156(1991). RN [6] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=93018017; PubMed=1401999; DOI=10.1111/1523-1747.ep12616131; RA Dumont M., Van L.T., Dupont E., Pelletier G., Labrie F.; RT "Characterization, expression, and immunohistochemical localization of RT 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase in human RT skin."; RL J. Invest. Dermatol. 99:415-421(1992). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-367. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 VARIANTS VAL-79 AND LEU-286. RX MEDLINE=99318093; PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [9] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: Placenta and skin. Predominantly expressed in CC mammary gland tissue. 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; M27137; AAA36015.1; -; mRNA. DR EMBL; M28392; AAA36001.1; ALT_SEQ; Genomic_DNA. DR EMBL; M28162; AAA36001.1; JOINED; Genomic_DNA. DR EMBL; M28391; AAA36001.1; JOINED; Genomic_DNA. DR EMBL; M35493; AAA51538.1; -; mRNA. DR EMBL; M63397; AAA51662.1; -; Genomic_DNA. DR EMBL; M63395; AAA51662.1; JOINED; Genomic_DNA. DR EMBL; M63396; AAA51662.1; JOINED; Genomic_DNA. DR EMBL; M38180; AAA51831.1; -; Genomic_DNA. DR EMBL; X53321; CAA37408.1; -; mRNA. DR EMBL; X55997; CAA39469.1; -; mRNA. DR EMBL; S45679; AAB23543.1; -; mRNA. DR EMBL; BC031999; AAH31999.1; -; mRNA. DR PIR; A36551; DEHUHS. DR UniGene; Hs.364941; -. DR Ensembl; ENSG00000175511; Homo sapiens. DR KEGG; hsa:3283; -. DR H-InvDB; HIX0000948; -. DR HGNC; HGNC:5217; HSD3B1. DR MIM; 109715; gene. DR DrugBank; APRD01276; Trilostane. DR LinkHub; P14060; -. DR ArrayExpress; P14060; -. DR GermOnline; ENSG00000203857; Homo sapiens. DR RZPD-ProtExp; C0104; -. DR RZPD-ProtExp; C0341; -. DR RZPD-ProtExp; IOH22178; -. DR RZPD-ProtExp; IOH27459; -. DR GO; GO:0005792; C:microsome; IDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB. DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase...; ISS:UniProtKB. DR GO; GO:0004769; F:steroid delta-isomerase activity; ISS:UniProtKB. DR GO; GO:0006702; P:androgen biosynthetic process; TAS:UniProtKB. DR GO; GO:0006703; P:estrogen biosynthetic process; TAS:UniProtKB. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Direct protein sequencing; Endoplasmic reticulum; Isomerase; Membrane; KW Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; KW Polymorphism; Steroidogenesis; Transmembrane. FT INIT_MET 1 1 Removed. FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type I. FT /FTId=PRO_0000087774. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). FT VARIANT 79 79 I -> V (in dbSNP:rs6201). FT /FTId=VAR_014174. FT VARIANT 286 286 F -> L (in dbSNP:rs6205). FT /FTId=VAR_014175. FT VARIANT 367 367 T -> N (in dbSNP:rs1047303). FT /FTId=VAR_000005. SQ SEQUENCE 373 AA; 42252 MW; 2C76616E7EA7433A CRC64; MTGWSCLVTG AGGFLGQRII RLLVKEKELK EIRVLDKAFG PELREEFSKL QNKTKLTVLE GDILDEPFLK RACQDVSVII HTACIIDVFG VTHRESIMNV NVKGTQLLLE ACVQASVPVF IYTSSIEVAG PNSYKEIIQN GHEEEPLENT WPAPYPHSKK LAEKAVLAAN GWNLKNGGTL YTCALRPMYI YGEGSRFLSA SINEALNNNG ILSSVGKFST VNPVYVGNVA WAHILALRAL QDPKKAPSIR GQFYYISDDT PHQSYDNLNY TLSKEFGLRL DSRWSFPLSL MYWIGFLLEI VSFLLRPIYT YRPPFNRHIV TLSNSVFTFS YKKAQRDLAY KPLYSWEEAK QKTVEWVGSL VDRHKETLKS KTQ // ID 3BHS1_MESAU Reviewed; 373 AA. AC Q60555; Q60556; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 42. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I (3- DE beta-HSD I) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN Name=HSD3B1; OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Adrenal gland; RX MEDLINE=96135293; PubMed=8547173; DOI=10.1016/0960-0760(95)00197-2; RA Rogerson F.M., Lehoux J.-G., Mason J.I.; RT "Expression and characterization of isoforms of 3 beta-hydroxysteroid RT dehydrogenase/delta 5-->4-isomerase in the hamster."; RL J. Steroid Biochem. Mol. Biol. 55:481-487(1995). 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 CC hormonal steroids. Also able to act as 3-keto-reductase reducing CC 5-alpha-dihydrotestosterone to the corresponding 3-beta-androstan- CC 3-beta,17beta-diol. 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: High levels in adrenal, kidney and male liver. CC Low levels in female 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; L38709; AAB52546.1; -; mRNA. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type I. FT /FTId=PRO_0000087777. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). SQ SEQUENCE 373 AA; 41754 MW; 4975BC9F2D93D159 CRC64; MPGWSCLVTG AGGFLGQRII RMLVQEKELQ EVRALDKVFR PETREEFCKL QTKTKVTVLE GDILDAQCLR RACQGISVVI HTAAAIDVFG AIPRQTIIDI NLKGTLNLLE ACVQASVPAF IYTSSIDVAG PNSYKEIVLN GHEEQQHEST WSDPYPYSKK MAEKAVLAAN GSSLKNGGTL HTCALRPMYI YGEKSPLISV TIIRAVKNSG ILDVTGKFST VNPVYVNNAA WAHILAARGL QDPRKSPNIQ GQFYYISDDT PHQSYDDLNY VLSKDWGLRP DSSWRPPVAL LYWLGFLLEL VSFLLRPVYN YQPPFNRHLV TLSNTVFTFS YKKAQRDLGY EPLVGWEEAR ENTSEWIGSL VEQHKGTLNT KAQ // 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 23-JAN-2007, entry version 52. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I (3- DE beta-HSD I) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; RX MEDLINE=92020952; PubMed=1924345; 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane 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 UniGene; Mm.140811; -. DR Ensembl; ENSMUSG00000027871; Mus musculus. DR KEGG; mmu:15492; -. DR MGI; MGI:96233; Hsd3b1. DR ArrayExpress; P24815; -. DR GermOnline; ENSMUSG00000027871; Mus musculus. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type I. FT /FTId=PRO_0000087780. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). FT CONFLICT 128 128 V -> A (in Ref. 2). FT CONFLICT 319 319 L -> S (in Ref. 2). 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 3BHS1_RAT Reviewed; 373 AA. AC P22071; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 54. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I (3- DE beta-HSD I) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN Name=Hsd3b1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91093186; PubMed=1985917; RA Zhao H.-F., Labrie C., Simard J., de Launoit Y., Trudel C., Martel C., RA Rheaume E., Dupont E., Luu-The V., Pelletier G., Labrie F.; RT "Characterization of rat 3 beta-hydroxysteroid dehydrogenase/delta 5- RT delta 4 isomerase cDNAs and differential tissue-specific expression of RT the corresponding mRNAs in steroidogenic and peripheral tissues."; RL J. Biol. Chem. 266:583-593(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RX MEDLINE=92064139; PubMed=1955079; DOI=10.1016/0303-7207(91)90139-J; RA Lorence M.C., Naville D., Graham-Lorence S.E., Mack S.O., Murry B.A., RA Trant J.M., Mason J.I.; RT "3 beta-hydroxysteroid dehydrogenase/delta 5-->4-isomerase expression RT in rat and characterization of the testis isoform."; RL Mol. Cell. Endocrinol. 80:21-31(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: Adrenal glands, testes and ovaries. 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; M38178; AAA63474.1; -; mRNA. DR EMBL; BC086578; AAH86578.1; -; mRNA. DR PIR; A39051; DERTH1. DR UniGene; Rn.128814; -. DR Ensembl; ENSRNOG00000019454; Rattus norvegicus. DR RGD; 67377; Hsd3b1. DR ArrayExpress; P22071; -. DR GermOnline; ENSRNOG00000019454; Rattus norvegicus. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type I. FT /FTId=PRO_0000087787. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). SQ SEQUENCE 373 AA; 42037 MW; 1BB058B5171C2F24 CRC64; MPGWSCLVTG AGGFVGQRII RMLVQEKELQ EVRALDKVFR PETKEEFSKL QTKAKVTMLE GDILDAQYLR RACQGISVVI HTAAVIDVSH VLPRQTILDV NLKGTQNILE ACVEASVPAF IYCSTVDVAG PNSYKKIILN GHEEEHHEST WSDAYPYSKR MAEKAVLAAN GSILKNGGTL HTCALRPMYI YGERSPFLSV MILAALKNKG ILNVTGKFSI ANPVYVGNVA WAHILAARGL RDPKKSQNVQ GQFYYISDDT PHQSYDDLNC TLSKEWGLRL DSSWSLPLPL LYWLAFLLET VSFLLRPFYN YRPPFNCHLV TLSNSKFTFS YKKAQRDLGY VPLVSWEEAK QKTSEWIGTL VEQHRETLDT KSQ // ID 3BHS2_HUMAN Reviewed; 372 AA. AC P26439; Q16010; Q53GD4; Q6LDB9; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-FEB-2007, entry version 74. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II (3- DE beta-HSD II) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN Name=HSD3B2; Synonyms=HSDB3B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Adrenal gland; RX MEDLINE=92049394; PubMed=1944309; RA Rheaume E., Lachance Y., Zhao H.-F., Breton N., Dumont M., RA de Launoit Y., Trudel C., Luu-The V., Simard J., Labrie F.; RT "Structure and expression of a new complementary DNA encoding the RT almost exclusive 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4- RT isomerase in human adrenals and gonads."; RL Mol. Endocrinol. 5:1147-1157(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92075161; PubMed=1741954; RA Lachance Y., Luu-The V., Verreault H., Dumont M., Rheaume E., RA Leblanc G., Labrie F.; RT "Structure of the human type II 3 beta-hydroxysteroid RT dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD) gene: adrenal and RT gonadal specificity."; RL DNA Cell Biol. 10:701-711(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Small intestine; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., RA Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). 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). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-205. RX PubMed=1363812; DOI=10.1038/ng0792-239; RA Rheaume E., Simard J., Morel Y., Mebarki F., Zachmann M., Forest M.G., RA New M.I., Labrie F.; RT "Congenital adrenal hyperplasia due to point mutations in the type II RT 3 beta-hydroxysteroid dehydrogenase gene."; RL Nat. Genet. 1:239-245(1992). RN [7] RP INVOLVEMENT IN PCOS. RX PubMed=14764797; DOI=10.1210/jc.2003-030934; RA Carbunaru G., Prasad P., Scoccia B., Shea P., Hopwood N., Ziai F., RA Chang Y.T., Myers S.E., Mason J.I., Pang S.; RT "The hormonal phenotype of nonclassic 3 beta-hydroxysteroid RT dehydrogenase (HSD3B) deficiency in hyperandrogenic females is RT associated with insulin-resistant polycystic ovary syndrome and is not RT a variant of inherited HSD3B2 deficiency."; RL J. Clin. Endocrinol. Metab. 89:783-794(2004). RN [8] RP VARIANTS AH2 LYS-142; PRO-245 AND ASN-253. RX MEDLINE=93302780; PubMed=8316254; DOI=10.1210/me.7.5.716; RA Simard J., Rheaume E., Sanchez R., Laflamme N., de Launoit Y., RA Luu-The V., van Seters A.P., Gordon R.D., Bettendorf M., Heinrich U., RA Moshang T., New M.I., Labrie F.; RT "Molecular basis of congenital adrenal hyperplasia due to 3 beta- RT hydroxysteroid dehydrogenase deficiency."; RL Mol. Endocrinol. 7:716-728(1993). RN [9] RP VARIANTS AH2 TRP-108 AND LEU-186. RX MEDLINE=95135422; PubMed=7833923; DOI=10.1093/hmg/3.9.1639; RA Sanchez R., Mebarki F., Rheaume E., Laflamme N., Forest M.G., RA Bey-Omar F., David M., Morel Y., Labrie F., Simard J.; RT "Functional characterization of the novel L108W and P186L mutations RT detected in the type II 3 beta-hydroxysteroid dehydrogenase gene of a RT male pseudohermaphrodite with congenital adrenal hyperplasia."; RL Hum. Mol. Genet. 3:1639-1645(1994). RN [10] RP VARIANT AH2 ASP-254. RX MEDLINE=94171959; PubMed=8126127; DOI=10.1210/jc.78.3.561; RA Sanchez R., Rheaume E., Laflamme N., Rosenfield R.L., Labrie F., RA Simard J.; RT "Detection and functional characterization of the novel missense RT mutation Y254D in type II 3 beta-hydroxysteroid dehydrogenase (3 beta RT HSD) gene of a female patient with nonsalt-losing 3 beta HSD RT deficiency."; RL J. Clin. Endocrinol. Metab. 78:561-567(1994). RN [11] RP VARIANT AH2 ARG-129. RX MEDLINE=95051232; PubMed=7962268; DOI=10.1210/jc.79.4.1012; RA Rheaume E., Sanchez R., Simard J., Chang Y.T., Wang J., Pang S., RA Labrie F.; RT "Molecular basis of congenital adrenal hyperplasia in two siblings RT with classical nonsalt-losing 3 beta-hydroxysteroid dehydrogenase RT deficiency."; RL J. Clin. Endocrinol. Metab. 79:1012-1018(1994). RN [12] RP VARIANT AH2 THR-82. RX MEDLINE=94242228; PubMed=8185809; RA Mendonca B.B., Russell A.J., Vasconcelos-Leite M., Arnhold I.J., RA Bloise W., Wajchenberg B.L., Nicolau W., Sutcliffe R.G., Wallace A.M.; RT "Mutation in 3 beta-hydroxysteroid dehydrogenase type II associated RT with pseudohermaphroditism in males and premature pubarche or cryptic RT expression in females."; RL J. Mol. Endocrinol. 12:119-122(1994). RN [13] RP VARIANT AH2 ARG-173. RX MEDLINE=94338525; PubMed=8060486; RA Russell A.J., Wallace A.M., Forest M.G., Donaldson M.D., Edwards C.R., RA Sutcliffe R.G.; RT "Mutation in the human gene for 3 beta-hydroxysteroid dehydrogenase RT type II leading to male pseudohermaphroditism without salt loss."; RL J. Mol. Endocrinol. 12:225-237(1994). RN [14] RP VARIANT AH2 ASP-15. RX MEDLINE=95200911; PubMed=7893703; DOI=10.1021/bi00009a020; RA Rheaume E., Sanchez R., Mebarki F., Gagnon E., Carel J.C., RA Chaussain J.-L., Morel Y., Labrie F., Simard J.; RT "Identification and characterization of the G15D mutation found in a RT male patient with 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) RT deficiency: alteration of the putative NAD-binding domain of type II 3 RT beta-HSD."; RL Biochemistry 34:2893-2900(1995). RN [15] RP VARIANT AH2 PRO-205. RX MEDLINE=95359984; PubMed=7633426; DOI=10.1093/hmg/4.4.745; RA Katsumata N., Tanae A., Yasunaga T., Horikawa R., Tanaka T., Hibi I.; RT "A novel missense mutation in the type II 3 beta-hydroxysteroid RT dehydrogenase gene in a family with classical salt-wasting congenital RT adrenal hyperplasia due to 3 beta-hydroxysteroid dehydrogenase RT deficiency."; RL Hum. Mol. Genet. 4:745-746(1995). RN [16] RP VARIANT AH2 ARG-259. RX MEDLINE=95360019; PubMed=7633460; DOI=10.1093/hmg/4.5.969; RA Tajima T., Fujieda K., Nakae J., Shinohara N., Yoshimoto M., Baba T., RA Kinoshita E., Igarashi Y., Oomura T.; RT "Molecular analysis of type II 3 beta-hydroxysteroid dehydrogenase RT gene in Japanese patients with classical 3 beta-hydroxysteroid RT dehydrogenase deficiency."; RL Hum. Mol. Genet. 4:969-971(1995). RN [17] RP VARIANT AH2 SER-100. RX MEDLINE=95332416; PubMed=7608265; DOI=10.1210/jc.80.7.2127; RA Mebarki F., Sanchez R., Rheaume E., Laflamme N., Simard J., RA Forest M.G., Bey-Omar F., David M., Labrie F., Morel Y.; RT "Nonsalt-losing male pseudohermaphroditism due to the novel homozygous RT N100S mutation in the type II 3 beta-hydroxysteroid dehydrogenase RT gene."; RL J. Clin. Endocrinol. Metab. 80:2127-2134(1995). RN [18] RP VARIANT AH2 SER-236. RX MEDLINE=98387937; PubMed=9719627; DOI=10.1006/mgme.1998.2715; RA Nayak S., Lee P.A., Witchel S.F.; RT "Variants of the type II 3beta-hydroxysteroid dehydrogenase gene in RT children with premature pubic hair and hyperandrogenic adolescents."; RL Mol. Genet. Metab. 64:184-192(1998). RN [19] RP VARIANTS AH2. RX MEDLINE=20066679; PubMed=10599696; DOI=10.1210/jc.84.12.4410; RA Moisan A.M., Ricketts M.L., Tardy V., Desrochers M., Mebarki F., RA Chaussain J.-L., Cabrol S., Raux-Demay M.C., Forest M.G., RA Sippell W.G., Peter M., Morel Y., Simard J.; RT "New insight into the molecular basis of 3beta-hydroxysteroid RT dehydrogenase deficiency: identification of eight mutations in the RT HSD3B2 gene in eleven patients from seven new families and comparison RT of the functional properties of twenty-five mutant enzymes."; RL J. Clin. Endocrinol. Metab. 84:4410-4425(1999). RN [20] RP VARIANTS AH2 ARG-129; GLN-222 AND MET-259. RX MEDLINE=20191658; PubMed=10651755; RA Marui S., Castro M., Latronico A.C., Elias L.L., Arnhold I.J., RA Moreira A.C., Mendonca B.B.; RT "Mutations in the type II 3beta-hydroxysteroid dehydrogenase (HSD3B2) RT gene can cause premature pubarche in girls."; RL Clin. Endocrinol. (Oxf.) 52:67-75(2000). RN [21] RP VARIANT AH2 GLU-10. RX MEDLINE=20300169; PubMed=10843183; DOI=10.1210/jc.85.5.1968; RA Alos N., Moisan A.M., Ward L., Desrochers M., Legault L., Leboeuf G., RA van Vliet G., Simard J.; RT "A novel A10E homozygous mutation in the HSD3B2 gene causing severe RT salt-wasting 3beta-hydroxysteroid dehydrogenase deficiency in 46,XX RT and 46,XY French-Canadians: evaluation of gonadal function after RT puberty."; RL J. Clin. Endocrinol. Metab. 85:1968-1974(2000). RN [22] RP VARIANTS AH2 LYS-142 AND THR-222. RX MEDLINE=22045346; PubMed=12050213; DOI=10.1210/jc.87.6.2556; RA Pang S., Wang W., Rich B., David R., Chang Y.T., Carbunaru G., RA Myers S.E., Howie A.F., Smillie K.J., Mason J.I.; RT "A novel nonstop mutation in the stop codon and a novel missense RT mutation in the type II 3-beta-hydroxysteroid dehydrogenase (3-beta- RT HSD) gene causing, respectively, nonclassic and classic 3-beta-HSD RT deficiency congenital adrenal hyperplasia."; RL J. Clin. Endocrinol. Metab. 87:2556-2563(2002). 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: Adrenal glands, testes and ovaries. CC -!- DISEASE: Defects in HSD3B2 are the cause of adrenal hyperplasia CC type 2 (AH2) [MIM:201810]. AH2 is a form of congenital adrenal CC hyperplasia, a common recessive disease due to defective synthesis CC of cortisol. Congenital adrenal hyperplasia is characterized by CC androgen excess leading to ambiguous genitalia in affected CC females, rapid somatic growth during childhood in both sexes with CC premature closure of the epiphyses and short adult stature. Four CC clinical types: 'salt wasting' (SW, the most severe type), 'simple CC virilizing' (SV, less severely affected patients), with normal CC aldosterone biosynthesis, 'non-classic form' or late onset (NC or CC LOAH), and 'cryptic' (asymptomatic). In AH2, virilization is much CC less marked or does not occur. AH2 is frequently lethal in early CC life. CC -!- DISEASE: Associated with polycystic ovarian syndrome (PCOS) CC [MIM:184700]. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC -!- CAUTION: Ref.6 (AAC60600) sequence differs from that shown due to CC a frameshift in position 186. The frameshift is caused by a single CC nucleotide insertion which is found in AH2. CC -!- WEB RESOURCE: NAME=GeneDis; NOTE=CAH; CC URL="http://life2.tau.ac.il/GeneDis/Tables/CAH/cah.html". CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=HSD3B2". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M67466; AAA36016.1; -; mRNA. DR EMBL; M77144; AAA36014.1; -; Genomic_DNA. DR EMBL; AK222997; BAD96717.1; -; mRNA. DR EMBL; AL359553; CAC19799.1; -; Genomic_DNA. DR EMBL; BC038419; AAH38419.1; -; mRNA. DR EMBL; S60309; AAC60599.1; -; Genomic_DNA. DR EMBL; S60310; AAC60600.1; ALT_FRAME; Genomic_DNA. DR PIR; A39488; DEHUH2. DR UniGene; Hs.364941; -. DR Ensembl; ENSG00000196766; Homo sapiens. DR KEGG; hsa:3284; -. DR HGNC; HGNC:5218; HSD3B2. DR MIM; 184700; phenotype. DR MIM; 201810; gene+phenotype. DR ArrayExpress; P26439; -. DR GermOnline; ENSG00000203859; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB. DR GO; GO:0005792; C:microsome; ISS:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB. DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase...; IDA:UniProtKB. DR GO; GO:0004769; F:steroid delta-isomerase activity; IDA:UniProtKB. DR GO; GO:0006702; P:androgen biosynthetic process; ISS:UniProtKB. DR GO; GO:0006703; P:estrogen biosynthetic process; ISS:UniProtKB. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Congenital adrenal hyperplasia; Disease mutation; KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Polymorphism; KW Steroidogenesis; Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 372 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type II. FT /FTId=PRO_0000087775. FT TRANSMEM 287 307 Potential. FT NP_BIND 5 36 NAD (Potential). FT VARIANT 10 10 A -> E (in AH2; activity abolished). FT /FTId=VAR_010517. FT VARIANT 10 10 A -> V (in AH2; nonsalt-wasting form). FT /FTId=VAR_010518. FT VARIANT 15 15 G -> D (in AH2; activity abolished). FT /FTId=VAR_010519. FT VARIANT 82 82 A -> T (in AH2). FT /FTId=VAR_010520. FT VARIANT 94 94 E -> Q (in dbSNP:rs6211). FT /FTId=VAR_014818. FT VARIANT 100 100 N -> S (in AH2; nonsalt-wasting form). FT /FTId=VAR_010521. FT VARIANT 108 108 L -> W (in AH2; activity abolished). FT /FTId=VAR_010522. FT VARIANT 129 129 G -> R (in AH2; nonsalt-wasting form). FT /FTId=VAR_010523. FT VARIANT 142 142 E -> K (in AH2; activity abolished). FT /FTId=VAR_000006. FT VARIANT 155 155 P -> L (in AH2; nonsalt-wasting form). FT /FTId=VAR_010524. FT VARIANT 167 167 A -> V (in AH2; late onset; almost normal FT activity). FT /FTId=VAR_010525. FT VARIANT 173 173 L -> R (in AH2; nonsalt-wasting form). FT /FTId=VAR_010526. FT VARIANT 186 186 P -> L (in AH2; activity abolished). FT /FTId=VAR_010527. FT VARIANT 205 205 L -> P (in AH2). FT /FTId=VAR_000007. FT VARIANT 213 213 S -> G (in AH2; late onset; partial loss FT of activity). FT /FTId=VAR_010528. FT VARIANT 216 216 K -> E (in AH2; late onset; partial loss FT of activity). FT /FTId=VAR_010529. FT VARIANT 222 222 P -> H (in AH2; nonsalt-wasting form; FT activity abolished). FT /FTId=VAR_010530. FT VARIANT 222 222 P -> Q (in AH2; activity abolished). FT /FTId=VAR_010531. FT VARIANT 222 222 P -> T (in AH2). FT /FTId=VAR_015411. FT VARIANT 231 238 Missing (in AH2; activity abolished). FT /FTId=VAR_010532. FT VARIANT 236 236 L -> S (in AH2; mild; 100% of activity). FT /FTId=VAR_010533. FT VARIANT 245 245 A -> P (in AH2; loss of 88% of activity). FT /FTId=VAR_000008. FT VARIANT 253 253 Y -> N (in AH2; activity abolished). FT /FTId=VAR_000009. FT VARIANT 254 254 Y -> D (in AH2; activity abolished). FT /FTId=VAR_000010. FT VARIANT 259 259 T -> M (in AH2; activity abolished). FT /FTId=VAR_010534. FT VARIANT 259 259 T -> R (in AH2; activity abolished). FT /FTId=VAR_000011. FT VARIANT 294 294 G -> V (in AH2; nonsalt-wasting form; FT activity abolished). FT /FTId=VAR_010535. FT CONFLICT 232 232 H -> L (in Ref. 3). SQ SEQUENCE 372 AA; 42052 MW; 8E0D933488988451 CRC64; MGWSCLVTGA GGLLGQRIVR LLVEEKELKE IRALDKAFRP ELREEFSKLQ NRTKLTVLEG DILDEPFLKR ACQDVSVVIH TACIIDVFGV THRESIMNVN VKGTQLLLEA CVQASVPVFI YTSSIEVAGP NSYKEIIQNG HEEEPLENTW PTPYPYSKKL AEKAVLAANG WNLKNGDTLY TCALRPTYIY GEGGPFLSAS INEALNNNGI LSSVGKFSTV NPVYVGNVAW AHILALRALR DPKKAPSVRG QFYYISDDTP HQSYDNLNYI LSKEFGLRLD SRWSLPLTLM YWIGFLLEVV SFLLSPIYSY QPPFNRHTVT LSNSVFTFSY KKAQRDLAYK PLYSWEEAKQ KTVEWVGSLV DRHKETLKSK TQ // ID 3BHS2_MESAU Reviewed; 373 AA. AC Q64421; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 44. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II (3- DE beta-HSD II) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN Name=HSD3B2; OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney, and Liver; RX MEDLINE=96135293; PubMed=8547173; DOI=10.1016/0960-0760(95)00197-2; RA Rogerson F.M., Lehoux J.-G., Mason J.I.; RT "Expression and characterization of isoforms of 3 beta-hydroxysteroid RT dehydrogenase/delta 5-->4-isomerase in the hamster."; RL J. Steroid Biochem. Mol. Biol. 55:481-487(1995). CC -!- FUNCTION: The 3-beta-HSD is a bifunctional enzyme, that catalyzes CC the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, CC and the oxidative conversion of ketosteroids. The 3-beta-HSD CC enzymatic system plays a crucial role in the biosynthesis of all CC classes of hormonal steroids. Also able to act as 3-keto-reductase CC reducing 5-alpha-dihydrotestosterone to the corresponding 3-beta- CC androstan-3-beta,17beta-diol. 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: High levels in adrenal, kidney and male liver. CC Low levels in female 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; L38710; AAA96606.1; -; mRNA. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type II. FT /FTId=PRO_0000087778. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). SQ SEQUENCE 373 AA; 41903 MW; FE2B53A62717897A CRC64; MPGWSCLVTG AGGFLGQRII HLLVQEKDLE EVRLLDKVFR PETREEFFKL QTKTKVTVLE GDILDAQCLR RACQGISVVI HTAAAIDVWG IIPRQTIIDI NVKGTLNLLE ACVQASVPAF IYTSSIDVAG PNSYKEIVLN GHEEQQHEST WSDPYPYSKM MAEKAVLAAN GSFLKNGGTL HTCALRPMYI YGEKSSILSG IMIRAIKNNG ILKVTGKFST VNPVYVSNAA WAHILAARGL QDPKKSPNIQ GQFYYISDDT PHQSYDDLNN TLSKKWGLRP DSSWRPPVAL LYWLGFLLEL VNFLLRPVYN YQPPFTRYLV TISNTVFTFS YKKAQRDLGY EPLVGWEEAR ENTSEWIGSL VEQHKGTLNT KAQ // ID 3BHS2_MOUSE Reviewed; 373 AA. AC P26149; Q8R0J6; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 49. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II (3- DE beta-HSD II) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 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. OX NCBI_TaxID=10090; RN [1] 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-373. RC STRAIN=BALB/c; RX MEDLINE=92020952; PubMed=1924345; 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane 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; BC026757; AAH26757.1; -; mRNA. DR EMBL; BC040397; AAH40397.1; -; mRNA. DR EMBL; M75886; -; NOT_ANNOTATED_CDS; mRNA. DR UniGene; Mm.196405; -. DR Ensembl; ENSMUSG00000063730; Mus musculus. DR KEGG; mmu:15493; -. DR MGI; MGI:96234; Hsd3b2. DR ArrayExpress; P26149; -. DR GermOnline; ENSMUSG00000063730; Mus musculus. DR RZPD-ProtExp; IOM15562; -. DR GO; GO:0004769; F:steroid delta-isomerase activity; IEA:EC. DR InterPro; IPR002225; 3Beta_HSD. DR Pfam; PF01073; 3Beta_HSD; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type II. FT /FTId=PRO_0000087781. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). SQ SEQUENCE 373 AA; 41995 MW; 40EEA59227611D77 CRC64; MPGWSCLVTG AKGFLGQRII QLLVQEEDLE EIRVLDKVFR PETRKEFFNL ETSNKVTVLE 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 3BHS2_RAT Reviewed; 373 AA. AC P22072; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 54. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II (3- DE beta-HSD II) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91093186; PubMed=1985917; RA Zhao H.-F., Labrie C., Simard J., de Launoit Y., Trudel C., Martel C., RA Rheaume E., Dupont E., Luu-The V., Pelletier G., Labrie F.; RT "Characterization of rat 3 beta-hydroxysteroid dehydrogenase/delta 5- RT delta 4 isomerase cDNAs and differential tissue-specific expression of RT the corresponding mRNAs in steroidogenic and peripheral tissues."; RL J. Biol. Chem. 266:583-593(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=92049388; PubMed=1944305; RA Naville D., Keeney D.S., Jenkin G., Murry B.A., Head J.R., Mason J.I.; RT "Regulation of expression of male-specific rat liver microsomal 3 RT beta-hydroxysteroid dehydrogenase."; RL Mol. Endocrinol. 5:1090-1100(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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: Adrenal glands, testes and ovaries. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC -!- CAUTION: Rat 3-beta-HSD type II may possess only one transmembrane CC 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; M38179; AAA63475.1; -; mRNA. DR EMBL; S63167; AAB20228.1; -; mRNA. DR PIR; A40378; DERTHM. DR PIR; B39051; DERTH2. DR UniGene; Rn.128814; -. DR Ensembl; ENSRNOG00000019454; Rattus norvegicus. DR ArrayExpress; P22072; -. DR GermOnline; ENSRNOG00000019454; Rattus norvegicus. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type II. FT /FTId=PRO_0000087788. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). FT CONFLICT 115 115 A -> T (in Ref. 2). FT CONFLICT 165 165 A -> S (in Ref. 2). FT CONFLICT 341 341 E -> V (in Ref. 2). SQ SEQUENCE 373 AA; 42277 MW; 0F922E9632DE9526 CRC64; MPGWSCLVTG AGGFVGQRII RMLVQEKELQ EVRALDKVFR PETKEEFSKL QTKAKVTMLE GDILDAQYLR RACQGISVVI HTASVMDFSR VLPRQTILDV NLKGTQNLLE AGIHASVPAF IYCSTVDVAG PNSYKKTILN GREEEHHEST WSNPYPYSKK MAEKAVLAAN GSILKNGGTL HTCALRPMYI YGERGQFLSR IIIMALKNKG VLNVTGKFSI VNPVYVGNVA WAHILAARGL RDPKKSQNIQ GQFYYISDDT PHQSYDDLNC TLSKEWGLRL DSSWSLPLPL LYWLAFLLET VSFLLRPFYN YRPPFNCHLV TLSNSKFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL VEQHRETLDT KSQ // ID 3BHS3_MESAU Reviewed; 373 AA. AC O35296; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 42. DE 3 beta-hydroxysteroid dehydrogenase type 3 (3 beta-hydroxysteroid DE dehydrogenase type III) (3-beta-HSD III) (NADP-dependent 3-beta- DE hydroxy-Delta(5)-steroid dehydrogenase) (EC 1.1.1.-) (3-beta-hydroxy- DE 5-ene steroid dehydrogenase) (Progesterone reductase). GN Name=HSD3B3; OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=96135293; PubMed=8547173; DOI=10.1016/0960-0760(95)00197-2; RA Rogerson F.M., Lehoux J.-G., Mason J.I.; RT "Expression and characterization of isoforms of 3 beta-hydroxysteroid RT dehydrogenase/delta 5-->4-isomerase in the hamster."; RL J. Steroid Biochem. Mol. Biol. 55:481-487(1995). 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. This isoform possesses no isomerase activity CC but functions as a 3-ketosteroid reductase with a preference for CC NADP. CC -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-Delta(5)-steroid + NADP(+) = 3- CC oxo-Delta(5)-steroid + NADPH. CC -!- PATHWAY: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: High levels in adrenal, kidney and male liver. CC Low levels in female 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; AF017636; AAB70302.1; -; mRNA. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Membrane; Mitochondrion; NADP; Oxidoreductase; KW Steroidogenesis; Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase type FT 3. FT /FTId=PRO_0000087779. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NADP (Potential). SQ SEQUENCE 373 AA; 41806 MW; B588DDC2D3F15DF1 CRC64; MPAWSCLVTG AGGFLGQRII RMLAQEKELQ EVRTLFRSFT PKHREELSKL QTKTKVTVLE GDILDAQCLR RACQGISVVI HTAAAIDVFG AIPRQTVIDI NLKGTQHLLD ACIGARVPVF IYSSSVAVAG PNSYKVIIQN GSEEENHEST WSDPYAYSKK MAEKAVLAAN GSTLKDGGTL HTCALRLPFI YGEKSKFISD TMDRALKNNG LINGFSRFSV ISSVYVNNAA WAHVLAARGL QDPKKSPNIQ GQFYYISDDT PHQSYDDLCY TLSKDWGLRP DSSWKPPVAL LYWFGFLLET VSFLLRPVYN YQPPFNRHLV TLLNSVFTFS YKKAQRDLGY EPLVSWEEAR EKTSEWIGSL VEQHKGTLNI KAQ // 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 20-FEB-2007, entry version 52. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type III (3- DE beta-HSD III) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; RX MEDLINE=92020952; PubMed=1924345; 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane 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 UniGene; Mm.158717; -. DR Ensembl; ENSMUSG00000062410; Mus musculus. DR MGI; MGI:96235; Hsd3b3. DR ArrayExpress; P26150; -. DR GermOnline; ENSMUSG00000062410; Mus musculus. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type III. FT /FTId=PRO_0000087782. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). 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 20-FEB-2007, entry version 55. DE 3 beta-hydroxysteroid dehydrogenase type 4 (3 beta-hydroxysteroid DE dehydrogenase type IV) (3-beta-HSD IV) (NADPH-dependent 3-beta- DE hydroxy-Delta(5)-steroid dehydrogenase) (EC 1.1.1.-) (3-beta-hydroxy- DE 5-ene steroid dehydrogenase) (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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR (CD-1); TISSUE=Kidney; RX MEDLINE=94195314; 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane 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 UniGene; Mm.14309; -. DR UniGene; Mm.425143; -. DR Ensembl; ENSMUSG00000038092; Mus musculus. DR KEGG; mmu:15495; -. DR MGI; MGI:96236; Hsd3b4. DR GermOnline; ENSMUSG00000056351; Mus musculus. DR GermOnline; ENSMUSG00000074380; Mus musculus. DR RZPD-ProtExp; IOM16443; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Membrane; Mitochondrion; NADP; Oxidoreductase; KW Steroidogenesis; Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase type FT 4. FT /FTId=PRO_0000087783. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NADP (Potential). 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 3BHS4_RAT Reviewed; 373 AA. AC Q62878; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 49. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type IV (3- DE beta-HSD IV) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Ovary; RX MEDLINE=93374963; PubMed=7690038; RA Simard J., Couet J., Durocher F., Labrie Y., Sanchez R., Breton N., RA Turgeon C., Labrie F.; RT "Structure and tissue-specific expression of a novel member of the rat RT 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta- RT HSD) family. The exclusive 3 beta-HSD gene expression in the skin."; RL J. Biol. Chem. 268:19659-19668(1993). 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: Skin, placenta, also detectable in ovary and CC adrenal gland. 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; L17138; AAA40606.1; -; mRNA. DR PIR; A48769; A48769. DR UniGene; Rn.109394; -. DR Ensembl; ENSRNOG00000019441; Rattus norvegicus. DR KEGG; rno:29632; -. DR ArrayExpress; Q62878; -. DR GermOnline; ENSRNOG00000019441; Rattus norvegicus. DR GO; GO:0030283; F:3(or 17)beta-hydroxysteroid dehydrogenase a...; TAS:RGD. DR GO; GO:0016853; F:isomerase activity; TAS:RGD. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Microsome; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type IV. FT /FTId=PRO_0000087790. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). SQ SEQUENCE 373 AA; 41985 MW; F9303C8C1EF38876 CRC64; MPGWSCLVTG AGGFLGQRIV QLLVQEKDLK EVRVLDKVFR PETREEFFNL GTSIKVTVLE GDILDTQCLR RACQGISVVI HTAALIDVTG VNPRQTILDV NLKGTQNLLE ACVQASVPAF IYCSTVDVAG PNSYKKIILN GHEEEHHEST WSNPYPYSKK MAEKAVLAAN GSILKNGGTL HTCALRPMYI YGERSPFLSV MILAALKNKG ILNVTGKFSI ANPVYVGNVA WAHILAARGL RDPKKSQNVQ GQFYYISDDT PHQSYDDLNY TLSKEWGLHL DSSWSLPLPL LYWLAFLLEI VSFFLHPVYN YRPSFNRHLV TLSNSKFTFS 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 20-FEB-2007, entry version 56. DE 3 beta-hydroxysteroid dehydrogenase type 5 (3 beta-hydroxysteroid DE dehydrogenase type V) (3-beta-HSD V) (NADPH-dependent 3-beta-hydroxy- DE Delta(5)-steroid dehydrogenase) (EC 1.1.1.-) (3-beta-hydroxy-5-ene DE steroid dehydrogenase) (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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX MEDLINE=96064303; 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-42; LYS-60 AND LYS-362, AND RP MASS SPECTROMETRY. 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). 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in the liver of male beginning in CC late 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 UniGene; Mm.17910; -. DR Ensembl; ENSMUSG00000038092; Mus musculus. DR KEGG; mmu:15496; -. DR MGI; MGI:104645; Hsd3b5. DR ArrayExpress; Q61694; -. DR GermOnline; ENSMUSG00000038092; Mus musculus. DR RZPD-ProtExp; IOM16443; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR InterPro; IPR002225; 3Beta_HSD. DR Pfam; PF01073; 3Beta_HSD; 1. KW Acetylation; Endoplasmic reticulum; Membrane; Mitochondrion; NADP; KW Oxidoreductase; Steroidogenesis; Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase type FT 5. FT /FTId=PRO_0000087784. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NADP (Potential). FT MOD_RES 42 42 N6-acetyllysine. FT MOD_RES 60 60 N6-acetyllysine. FT MOD_RES 362 362 N6-acetyllysine. FT CONFLICT 89 89 L -> R (in Ref. 1). FT CONFLICT 147 147 R -> H (in Ref. 1). FT CONFLICT 285 285 S -> R (in Ref. 1). FT CONFLICT 316 316 N -> T (in Ref. 1). 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 3BHS5_RAT Reviewed; 373 AA. AC P27364; Q569C6; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 54. DE 3 beta-hydroxysteroid dehydrogenase type 5 (3 beta-hydroxysteroid DE dehydrogenase type V) (3-beta-HSD V) (NADPH-dependent 3-beta-hydroxy- DE Delta(5)-steroid dehydrogenase) (EC 1.1.1.-) (3-beta-hydroxy-5-ene DE steroid dehydrogenase) (Progesterone reductase). GN Name=Hsd3b5; Synonyms=Hsd3b; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=91065302; PubMed=2249649; RA Zhao H.-F., Rheaume E., Trudel C., Couet J., Labrie F., Simard J.; RT "Structure and sexual dimorphic expression of a liver-specific rat 3 RT beta-hydroxysteroid dehydrogenase/isomerase."; RL Endocrinology 127:3237-3239(1990). 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: 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. Exhibits CC only 3-ketosteroid reductase activity in the presence of NADPH and CC does not function as an isomerase. CC -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-Delta(5)-steroid + NADP(+) = 3- CC oxo-Delta(5)-steroid + NADPH. CC -!- PATHWAY: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed predominantly in male 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; M67465; AAA41352.1; -; mRNA. DR EMBL; BC092571; AAH92571.1; -; mRNA. DR PIR; A37404; A37404. DR UniGene; Rn.34902; -. DR Ensembl; ENSRNOG00000019417; Rattus norvegicus. DR KEGG; rno:24470; -. DR RGD; 2838; Hsd3b. DR ArrayExpress; P27364; -. DR GermOnline; ENSRNOG00000019417; Rattus norvegicus. DR GO; GO:0016229; F:steroid dehydrogenase activity; TAS:RGD. DR GO; GO:0006694; P:steroid biosynthetic process; TAS:RGD. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Acetylation; Endoplasmic reticulum; Membrane; Mitochondrion; NADP; KW Oxidoreductase; Steroidogenesis; Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase type FT 5. FT /FTId=PRO_0000087789. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NADP (Potential). FT MOD_RES 42 42 N6-acetyllysine (By similarity). FT CONFLICT 180 180 F -> L (in Ref. 2; AAH92571). FT CONFLICT 204 204 R -> T (in Ref. 2; AAH92571). SQ SEQUENCE 373 AA; 42206 MW; B96538F2EF056935 CRC64; MPGWSCLVTG AGGFLGQRIV QMLVQEKELQ EVRVLYRTFS PKHKEELSKL QTKAKVTVLR GDIVDAQFLR RACQGMSVII HTAAALDIAG FLPRQTILDV NVKGTQLLLD ACVEASVPAF IYSSSTGVAG PNSYKETILN DREEEHREST WSNPYPYSKR MAEKAVLAAN GSILKNGGTF HTCALRLPFI YGEESQIIST MVNRALKNNS IIKRHATFSI ANPVYVGNAA WAHILAARGL RDPEKSQSIQ GQFYYISDDT PHQSYDDLNY TLSKEWGFCL DSSWSLPLPL LYWLAFLLET VSFLLRPFYN YRPPFNRFMV TILNSVFTIS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL VEQHRETLDT KSQ // ID 3BHS6_MOUSE Reviewed; 373 AA. AC O35469; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 46. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type VI (3- DE beta-HSD VI) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX MEDLINE=97230115; 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). 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in the skin and also is expressed in CC the 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 UniGene; Mm.14435; -. DR Ensembl; ENSMUSG00000027869; Mus musculus. DR KEGG; mmu:15497; -. DR MGI; MGI:109598; Hsd3b6. DR GermOnline; ENSMUSG00000027869; Mus musculus. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type VI. FT /FTId=PRO_0000087785. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). SQ SEQUENCE 373 AA; 41876 MW; A9718D6A5832C52D CRC64; MPGWSCLVTG AGGFLGQRIV QLLMQEKDLE EIRVLDKFFR PETREQFFNL DTNIKVTVLE GDILDTQYLR KACQGISVVI HTAAVIDVTG VIPRQTILDV NLKGTQNLLE ACIQASVPAF IFSSSVDVAG PNSYKEIILN GNEEEHHESI WSDPYPYSKK MAEKAVLAAN GSMLKIGGTL HTCALRPMFI YGERSPFISN TIITALKNKN ILGCTGKFST ANPVYVGNVA WAHILAARGL RDPKKSPNIQ GEFYYISDDT PHQSYDDLNY TLSKEWGFCP DSSWSLPVPL LYWLAFMLET VSFLLSPIYR FIPPFNRHLV TLTGSTFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL VEQHRATLDT TSQ // ID 3BHS7_HUMAN Reviewed; 369 AA. AC Q9H2F3; Q9BSN9; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 2. DT 20-FEB-2007, entry version 35. DE 3 beta-hydroxysteroid dehydrogenase type 7 (3 beta-hydroxysteroid DE dehydrogenase type VII) (3-beta-HSD VII) (3-beta-hydroxy-Delta(5)-C27 DE steroid oxidoreductase) (EC 1.1.1.-) (C(27) 3-beta-HSD). GN Name=HSD3B7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND DISEASE. RX MEDLINE=20521690; PubMed=11067870; 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=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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 7alpha-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 -!- PATHWAY: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; multi-pass membrane protein. CC -!- DISEASE: Defects in HSD3B7 are the cause of progressive familial CC intrahepatic cholestasis type 4 (PFIC4) [MIM:607765]; also known CC as neonatal progressive intrahepatic cholestasis. PFIC4 is an CC autosomal recessive form of severe cholestatic liver disease. It CC presents in infancy with intermittent jaundice and cholestasis and CC progresses to end-stage liver disease and death in childhood. 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; AF277719; AAG37824.1; -; mRNA. DR EMBL; BC004929; AAH04929.1; -; mRNA. DR UniGene; Hs.460618; -. DR Ensembl; ENSG00000099377; Homo sapiens. DR KEGG; hsa:80270; -. DR HGNC; HGNC:18324; HSD3B7. DR MIM; 607764; gene. DR MIM; 607765; phenotype. DR ArrayExpress; Q9H2F3; -. DR GermOnline; ENSG00000099377; Homo sapiens. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase...; NAS:UniProtKB. DR GO; GO:0006699; P:bile acid biosynthetic process; TAS:UniProtKB. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Membrane; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT CHAIN 1 369 3 beta-hydroxysteroid dehydrogenase type FT 7. FT /FTId=PRO_0000087791. FT TRANSMEM 289 309 Potential. FT TRANSMEM 311 331 Potential. FT CONFLICT 250 250 T -> A (in Ref. 1). FT CONFLICT 265 265 Y -> H (in Ref. 1). FT CONFLICT 329 329 T -> A (in Ref. 1). SQ SEQUENCE 369 AA; 41016 MW; 7254A5DAAFAC23E7 CRC64; MADSAQAQKL VYLVTGGCGF LGEHVVRMLL QREPRLGELR VFDQHLGPWL EELKTGPVRV TAIQGDVTQA HEVAAAVAGA HVVIHTAGLV DVFGRASPKT IHEVNVQGTR NVIEACVQTG TRFLVYTSSM EVVGPNTKGH PFYRGNEDTP YEAVHRHPYP CSKALAEWLV LEANGRKVRG GLPLVTCALR PTGIYGEGHQ IMRDFYRQGL RLGGWLFRAI PASVEHGRVY VGNVAWMHVL AARELEQRAT LMGGQVYFCY DGSPYRSYED FNMEFLGPCG LRLVGARPLL PYWLLVFLAA LNALLQWLLR PLVLYAPLLN PYTLAVANTT FTVSTDKAQR HFGYEPLFSW EDSRTRTILW VQAATGSAQ // ID 3BHS7_MOUSE Reviewed; 369 AA. AC Q9EQC1; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 23-JAN-2007, entry version 33. DE 3 beta-hydroxysteroid dehydrogenase type 7 (3 beta-hydroxysteroid DE dehydrogenase type VII) (3-beta-HSD VII) (3-beta-hydroxy-Delta(5)-C27 DE steroid oxidoreductase) (EC 1.1.1.-) (C(27) 3-beta-HSD). 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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J X 129/SvEv; RX MEDLINE=20521690; PubMed=11067870; 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). 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 7alpha-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 -!- PATHWAY: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; multi-pass 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 UniGene; Mm.157103; -. DR Ensembl; ENSMUSG00000042289; Mus musculus. DR KEGG; mmu:101502; -. DR MGI; MGI:2141879; Hsd3b7. DR ArrayExpress; Q9EQC1; -. DR GermOnline; ENSMUSG00000042289; Mus musculus. DR RZPD-ProtExp; IOM17281; -. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Membrane; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT CHAIN 1 369 3 beta-hydroxysteroid dehydrogenase type FT 7. FT /FTId=PRO_0000087792. FT TRANSMEM 289 309 Potential. FT TRANSMEM 312 334 Potential. 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 3BHS7_RAT Reviewed; 338 AA. AC O35048; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 09-JAN-2007, entry version 24. DE 3 beta-hydroxysteroid dehydrogenase type 7 (3 beta-hydroxysteroid DE dehydrogenase type VII) (3-beta-HSD VII) (3-beta-hydroxy-Delta(5)-C27 DE steroid oxidoreductase) (EC 1.1.1.-) (C(27) 3-beta-HSD) (Confluent 3Y1 DE cell-associated 2). GN Name=Hsd3b7; Synonyms=Cca2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX MEDLINE=97342547; PubMed=9199244; DOI=10.1016/S0167-4781(97)00051-1; RA Hayashi Y., Kiyono T., Fujita M., Ishibashi M.; RT "Isolation of a novel cDNA whose corresponding mRNA is accumulated in RT growth-arrested confluent but not in growing sub-confluent rat 3Y1 RT cells."; RL Biochim. Biophys. Acta 1352:145-150(1997). 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 7alpha-hydroxylated sterols. Does not CC metabolize several different C(19/21) steroids as substrates. CC Involved in bile acid synthesis (By similarity). CC -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = 3- CC oxo-Delta(5)-steroid + NADH. CC -!- PATHWAY: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; multi-pass membrane protein (By similarity). CC -!- TISSUE SPECIFICITY: High levels in liver and lung, moderate levels CC in spleen, brain, heart, kidney, jejunum and testis. Up-regulated CC in 3Y1 cells upon growth arrest. 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; AB000199; BAA22931.1; -; mRNA. DR RGD; 628727; Hsd3b7. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Membrane; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT CHAIN 1 338 3 beta-hydroxysteroid dehydrogenase type FT 7. FT /FTId=PRO_0000248461. FT TRANSMEM 258 278 Potential. FT TRANSMEM 280 300 Potential. SQ SEQUENCE 338 AA; 37781 MW; 72FC828235D0BFD5 CRC64; MADSAQVPAL VYLVTGGCGF LGEHIVRMLL EWEPRLRELR VFDLHLSSWL EELKTGPVQV TAIQGDVTQA HEVAAAMAGS HVVIHTAGLV DVFGKASPET IHKVNVQGTQ NVIDACVQTG TRLLVYTSSM EVVGPNVKGH PFYRGNEDTP YEAIHRHPYP CSKALAEQLV LEANGRKGLR FGGRLFRAIP ASVEHGRVYV GNVAWMHILV ARELEQRAAL MGGQVYFCYD KSPYKSYEDF NMEFLSPCGL RLIGTHPLLP YWLLVLLTAL NALLQWLLRP LVLYTPLLNP YTLAVANTTF TVSTNKAQRH FGYKPLFSWE ESRARTIHWV QAMEGSAW // ID 3BHS_BOVIN Reviewed; 373 AA. AC P14893; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-FEB-2007, entry version 54. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (3-beta-HSD) DE [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN Name=HSD3B; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RX MEDLINE=90092517; PubMed=2599102; DOI=10.1016/0014-5793(89)81516-9; RA Zhao H.-F., Simard J., Labrie C., Breton N., Rheaume E., Luu-The V., RA Labrie F.; RT "Molecular cloning, cDNA structure and predicted amino acid sequence RT of bovine 3 beta-hydroxy-5-ene steroid dehydrogenase/delta 5-delta 4 RT isomerase."; RL FEBS Lett. 259:153-157(1989). RN [2] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Adrenal gland; RX MEDLINE=91329389; PubMed=1868086; DOI=10.1021/bi00247a003; RA Rutherfurd K.J., Chen S., Shively J.E.; RT "Isolation and amino acid sequence analysis of bovine adrenal 3 beta- RT hydroxysteroid dehydrogenase/steroid isomerase."; RL Biochemistry 30:8108-8116(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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. 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; X17614; CAA35615.1; -; mRNA. DR PIR; S07102; DEBOHS. DR UniGene; Bt.64737; -. DR KEGG; bta:281824; -. DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase...; ISS:UniProtKB. DR GO; GO:0004769; F:steroid delta-isomerase activity; ISS:UniProtKB. DR GO; GO:0006694; P:steroid biosynthetic process; ISS:UniProtKB. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Direct protein sequencing; Endoplasmic reticulum; Isomerase; Membrane; KW Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; KW Steroidogenesis; Transmembrane. FT INIT_MET 1 1 Removed. FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase. FT /FTId=PRO_0000087771. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). SQ SEQUENCE 373 AA; 42220 MW; B9BDB817E7B5A1D1 CRC64; MAGWSCLVTG GGGFLGQRII CLLVEEKDLQ EIRVLDKVFR PEVREEFSKL QSKIKLTLLE GDILDEQCLK GACQGTSVVI HTASVIDVRN AVPRETIMNV NVKGTQLLLE ACVQASVPVF IHTSTIEVAG PNSYREIIQD GREEEHHESA WSSPYPYSKK LAEKAVLGAN GWALKNGGTL YTCALRPMYI YGEGSPFLSA YMHGALNNNG ILTNHCKFSR VNPVYVGNVA WAHILALRAL RDPKKVPNIQ GQFYYISDDT PHQSYDDLNY TLSKEWGFCL DSRMSLPISL QYWLAFLLEI VSFLLSPIYK YNPCFNRHLV TLSNSVFTFS YKKAQRDLGY EPLYTWEEAK QKTKEWIGSL VKQHKETLKT KIH // ID 3BHS_CANFA Reviewed; 373 AA. AC Q5IFP1; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 06-FEB-2007, entry version 16. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (3-beta-HSD) DE [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN Name=HSD3B; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Corpus luteum; RA Kowalewski M.P., Taubert A., Hoffmann B.; RT "Expression of 3-beta-hydroxysteroid dehydrogenase in canine corpus RT luteum during dioestrus."; RL Submitted (SEP-2004) 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 (By similarity). 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein (By similarity). CC Mitochondrion; mitochondrial membrane; single-pass membrane CC protein (By similarity). 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; AY739720; AAW31741.1; -; mRNA. DR UniGene; Cfa.13172; -. DR Ensembl; ENSCAFG00000010039; Canis familiaris. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase...; ISS:UniProtKB. DR GO; GO:0004769; F:steroid delta-isomerase activity; ISS:UniProtKB. DR GO; GO:0006694; P:steroid biosynthetic process; ISS:UniProtKB. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed. FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase. FT /FTId=PRO_0000087772. FT TRANSMEM 288 308 Potential. SQ SEQUENCE 373 AA; 42378 MW; EB12CB016D650A5B CRC64; MAGWSCLVTG AGGFLGQRIV HLLAEEKELQ EIRALDKAFR PELLEEFSKL QSKTKLTMVE GDILDEQCLK RACQGTSVVI HTASVIDVMN VIHRETIMNV NLKGTQLLLE ACAQASVPIF IYTSTIEVAG PNSYRDIIQN AHEEEHLEST WSAPYPYSKK LAEKAVLAAN GWALKNGGTL HTCALRPMYI YGEGSIFLYN YIYKALRNNG ILTHHSKFSI VNPVYVGNVA WAHILALRAL QDPKKAPSVQ GQFYYISDDT PHQSYDDLNY NLSKEWGFSL DSRMSLPISL EYWLAFLLEI VSFLLSPIYK YQPPFNRHMV TLSNSIFTFS YKKAQRDLGY KPLFSWEEAK QKTTEWIGSL VKQHKETLKT KTH // ID 3BHS_FOWPV Reviewed; 370 AA. AC Q67477; Q9J5F8; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 2. DT 28-NOV-2006, entry version 36. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (3-beta-HSD) DE [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN OrderedLocusNames=FPV046; OS Fowlpox virus (FPV). OC Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; OC Avipoxvirus. OX NCBI_TaxID=10261; OH NCBI_TaxID=7742; Vertebrata. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=FP-9 / Isolate HP-438; RX MEDLINE=94358756; PubMed=8077953; RA Skinner M.A., Moore J.B., Binns M.M., Smith G.L., Boursnell M.E.G.; RT "Deletion of fowlpox virus homologues of vaccinia virus genes between RT the 3 beta-hydroxysteroid dehydrogenase (A44L) and DNA ligase (A50R) RT genes."; RL J. Gen. Virol. 75:2495-2498(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=20193820; PubMed=10729156; RX DOI=10.1128/JVI.74.8.3815-3831.2000; RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.; RT "The genome of fowlpox virus."; RL J. Virol. 74:3815-3831(2000). 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 (By similarity). 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: Steroid biosynthesis. 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; Z29716; CAA82802.1; -; Genomic_DNA. DR EMBL; AF198100; AAF44390.1; -; Genomic_DNA. DR PIR; S41971; S41971. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Isomerase; Multifunctional enzyme; NAD; Oxidoreductase; KW Steroidogenesis. FT CHAIN 1 370 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase. FT /FTId=PRO_0000087797. FT CONFLICT 38 43 IRIDQW -> LDRPM (in Ref. 1). FT CONFLICT 251 251 N -> K (in Ref. 1). SQ SEQUENCE 370 AA; 42349 MW; 730FE72BA84FA681 CRC64; MRTLVYVVTG GCGFLGRHII NNLILFESSL KEVRVYDIRI DQWLLDLVEK CNIIKIVPVI GDVRNKSTLD EALRSADVVI HIASINDVAG KFTNDSIMDV NINGTKNVVD SCLYNGVRVL VYTSSYSAVG PNFLGDAMIR GNENTYYQSN HKEAYPLSKQ LSEKYILEAN GTMSNIGLRL CTCALRPLGV FGEYCPVLET LYRRSYKSRK MYKYADDKVF HSRVYAGNVA WMHILAARNM IENGQHSPLC NNVYYCYDTS PTEHYHDFNM HFFNQLGMDL RNTCLPLWCL RFIANINKGL RVLLSPICSY TPLLNPYTLI KECTTFTIET DKAFKDFGYV PLYTWEESRS KTQLWIRELE AKSSSQKPKS // ID 3BHS_HORSE Reviewed; 373 AA. AC O46516; P79437; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 45. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (3-beta-HSD) DE [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN Name=HSD3B; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovarian follicle membrane; RX MEDLINE=20575290; PubMed=11133676; RA Boerboom D., Sirois J.; RT "Equine P450 cholesterol side-chain cleavage and 3 beta-hydroxysteroid RT dehydrogenase/delta(5)-delta(4) isomerase: molecular cloning and RT regulation of their messenger ribonucleic acids in equine follicles RT during the ovulatory process."; RL Biol. Reprod. 64:206-215(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Hasegawa T., Ishida M., Harigaya T., Ishida N., Mukoyama H.; RT "Molecular cloning, nucleotide sequence and tissue distribution of RT equine testicular 3 beta-hydroxysteroid dehydrogenase/delta5-delta4 RT isomerase messenger ribonucleic acid."; RL J. Equine Sci. 9:45-52(1998). 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. 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; AF031665; AAC04701.1; -; mRNA. DR EMBL; D89666; BAA32698.1; -; mRNA. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase. FT /FTId=PRO_0000087773. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). SQ SEQUENCE 373 AA; 42411 MW; 837A04E3C681417C CRC64; MAGWSCLVTG AGGFLGQRIV RLLVEEKEVQ EIRALDKVFR PELREEFSKL QSKVKLTVLE GDILDEQFLK RACQGASAVI HTASIIDVTN LFNPQVTMNV NVEGTQLLLE ACSQASVPIF IYTSSVAVAG PNSYREIIQN GHEEAHLETK WSSPYPYSKK LAEKAVLAAN GLPLKNGGTL YTCALRPMFI YGEGSPTLYY LMHEGLNNNG ILTHNCKFSR ANPVYVGNIA WAHIMALRAL RDPKKAPSIQ GQFYYISDDT PPQSYDDLTY TLSKKWGFCL DSRMRLPIFL KYWLAFLLEI VSFLLSPIYK YRPPFDRHLV TWQNSVFTFS YKKAQRDMGY EPLFSWEEAK KRTTEWIDAL VEPHQEALKT KTL // ID 3BHS_MACMU Reviewed; 373 AA. AC P27365; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 06-FEB-2007, entry version 43. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (3-beta-HSD) DE [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RX MEDLINE=91267292; PubMed=2050270; DOI=10.1016/0303-7207(91)90224-G; RA Simard J., Melner M.H., Breton N., Low K.G., Zhao H.-F., Periman L.M., RA Labrie F.; RT "Characterization of macaque 3 beta-hydroxy-5-ene steroid RT dehydrogenase/delta 5-delta 4 isomerase: structure and expression in RT steroidogenic and peripheral tissues in primate."; RL Mol. Cell. Endocrinol. 75:101-110(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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. CC -!- TISSUE SPECIFICITY: Adrenal glands, testes and ovaries. 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; M67467; AAA36847.1; -; mRNA. DR PIR; A54325; A54325. DR LinkHub; P27365; -. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase...; ISS:UniProtKB. DR GO; GO:0004769; F:steroid delta-isomerase activity; ISS:UniProtKB. DR GO; GO:0006694; P:steroid biosynthetic process; ISS:UniProtKB. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase. FT /FTId=PRO_0000087776. FT TRANSMEM 288 308 Potential. FT NP_BIND 6 37 NAD (Potential). SQ SEQUENCE 373 AA; 42005 MW; 9B6C172F319B5BB9 CRC64; MTGWSCLVTG AGGFLGQRIV RLLVEEKELK EIRVLDKAFR PELREEFSKL QNKTKLTVLE GDILDEPFLK RACQDVSVVI HTACIIDVFG VTHRESIMNV NVKGTQLLLE ACVQASVPVF IYTSTLEVAG PNSYKEIIQN GHEEEPLENT WPAPYPYSKK LAEKAVLAAN GWTLKNGGTL YTCALRPMYI YGEGGPFLSA SINEALNNNG ILSSVGKFST VNPVYVGNVA WAHILALRAL RDPKKAPSVQ GQFYYISDDT PHQSYDNLNY ILSKEFGLCL DSRWSLPLAL MYWIGFLLEV VSFLLSPVYS YQPPFNRHTV TLSNSVFTFS YKKAQRDLAY KPLYSWEEAK QKTVEWVGSL VDRHKETLKS KTQ // ID 3BHS_PIG Reviewed; 373 AA. AC Q9N119; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 23-JAN-2007, entry version 30. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (3-beta-HSD) DE [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN Name=HSD3B; Synonyms=3b-HSD; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Adipose tissue; RX MEDLINE=21540582; PubMed=11683717; RA von Teichman A., Joerg H., Werner P., Brenig B., Stranzinger G.; RT "cDNA cloning and physical mapping of porcine 3 beta-hydroxysteroid RT dehydrogenase/Delta 5-delta 4 isomerase."; RL Anim. Genet. 32:298-302(2001). 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: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; single-pass membrane protein. Mitochondrion; CC mitochondrial membrane; single-pass membrane protein. 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; AF232699; AAF37295.2; -; mRNA. DR UniGene; Ssc.14393; -. DR GO; GO:0004769; F:steroid delta-isomerase activity; IEA:EC. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase. FT /FTId=PRO_0000087786. FT TRANSMEM 292 309 Potential. FT NP_BIND 6 37 NAD (Potential). SQ SEQUENCE 373 AA; 41882 MW; 8BD4FEEF0117F6FF CRC64; MAGWSCLVTG GGGFLGQRIV HLLLEEKDLQ EIRVLDKVFK PEVREEFSKL QSKIKLTMLE GDILDEQCLK GACQGASVVI HTASIIDVVN AVGRETVMKV NVKGTQLLLE ACVQASVPVF IHTSSIEVAG PNSYREVIQN ACEEDRLETA WSAPYPLSKK LAEKAVLEAN GWALQNGGTL HTCALRPMYI YGEGSPFIFA HMNKALENNG VLTHNSKFSR VNPVYVGNVA WAHILALRAL RDPRKALSVQ GQFYYVADDT PPQSYDDLNY TLGKEWGFCL DSRRSLPPSL RYWLAFLLEI VSFLLSPIYN YQPPFNRHFV TLCNSVFTVS YKKAQRDLGY EPLFTWEEAK QKTKAWVGSL VKQHKEALKT KTH // ID 3BHS_VACCA Reviewed; 346 AA. AC O57245; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 28-NOV-2006, entry version 29. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (3-beta-HSD) DE [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN OrderedLocusNames=MVA157L, ACAM3000_MVA_157; OS Vaccinia virus (strain Ankara) (VACV). OC Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; OC Orthopoxvirus. OX NCBI_TaxID=126794; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=98263813; PubMed=9601507; DOI=10.1006/viro.1998.9123; RA Antoine G., Scheiflinger F., Dorner F., Falkner F.G.; RT "The complete genomic sequence of the modified vaccinia Ankara strain: RT comparison with other orthopoxviruses."; RL Virology 244:365-396(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate Acambis 3000; RA Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., RA Osborne J., Khristova M., Wohlhueter R.M.; RL Submitted (APR-2004) 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. 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: Steroid biosynthesis. 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; U94848; AAB96479.1; -; Genomic_DNA. DR EMBL; AY603355; AAT10555.1; -; Genomic_DNA. DR PIR; T37430; T37430. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Isomerase; Multifunctional enzyme; NAD; Oxidoreductase; KW Steroidogenesis. FT CHAIN 1 346 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase. FT /FTId=PRO_0000087793. SQ SEQUENCE 346 AA; 39397 MW; 8A5F09E596B98C7E CRC64; MAVYAVTGGA GFLGRYIVKL LISADDVQEI RVIDIVEDPQ PITSKVKVIN YIQCDINDFD KVREALDGVN LIIHTAALVD VFGKYTDNEI MKVNYYGTQT ILAACVDLGI KYLIYTSSME AIGPNKHGDP FIGHEHTLYD ISPGHVYAKS KRMAEQLVMK ANNSVIMNGA KLYTCCLRPT GIYGEGDKLM KVFYEQCKQH GNIMYRTVDD NAVHSRVYVG NAAWMHVLAA KYIQYPGSEI KGNAYFCYDY SPSCSYDMFN LLLMKPLGIE QGSRIPRWML KMYACKNDMK RILFRKPSLL NNYTLKISNT TFEVRTNNAE LDFNYSPIFN VDVAFERTRK WLEESE // ID 3BHS_VACCC Reviewed; 346 AA. AC P21097; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 28-NOV-2006, entry version 42. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (3-beta-HSD) DE [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN ORFNames=A44L; OS Vaccinia virus (strain Copenhagen) (VACV). OC Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; OC Orthopoxvirus. OX NCBI_TaxID=10249; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=91021027; PubMed=2219722; RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., RA Paoletti E.; RT "The complete DNA sequence of vaccinia virus."; RL Virology 179:247-266(1990). RN [2] RP COMPLETE GENOME. RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., RA Paoletti E.; RT "Appendix to 'The complete DNA sequence of vaccinia virus'."; RL Virology 179:517-563(1990). 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: Steroid biosynthesis. 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; M35027; AAA48175.1; -; Genomic_DNA. DR PIR; A42522; WMVZ1W. DR InterPro; IPR002225; 3Beta_HSD. DR InterPro; IPR012272; 3Beta_HSD_II. DR Pfam; PF01073; 3Beta_HSD; 1. DR PIRSF; PIRSF036679; 3Beta-HSD_II; 1. KW Isomerase; Multifunctional enzyme; NAD; Oxidoreductase; KW Steroidogenesis. FT CHAIN 1 346 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase. FT /FTId=PRO_0000087794. SQ SEQUENCE 346 AA; 39366 MW; F308D8BC9C811469 CRC64; MAVYAVTGGA GFLGRYIVKL LISADDVQEI RVIDIVEDPQ PITSKVKVIN YIQCDINDFD KVREALDGVN LIIHTAALVD VFGKYTDNEI MKVNYYGTQT ILAACVDLGI KYLIYTSSME AIGPNKHGDP FIGHEHTLYD ISPGHVYAKS KRMAEQLVMK ANNSVIMNGA KLYTCCLRPT GIYGEGDKLT KVFYEQCKQH GNIMYRTVDD NAVHSRVYVG NAAWMHVLAA KYIQYPGSKI KGNAYFCYDY SPSCSYDMFN LLLMKPLGIE QGSRIPRWML KMYACKNDMK RILFRKPSLL NNYTLKISNT TFEVRTNNAE LDFNYSPIFD VDVAFKRTRK WLEESE // ID 3BHS_VACCV Reviewed; 346 AA. AC P26670; Q76ZN3; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 09-JAN-2007, entry version 39. DE 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (3-beta-HSD) DE [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN OrderedLocusNames=VACWR170; ORFNames=SALF7L; OS Vaccinia virus (strain Western Reserve / WR) (VACV). OC Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; OC Orthopoxvirus. OX NCBI_TaxID=10254; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91332999; PubMed=1870190; RA Blasco R., Cole N.B., Moss B.; RT "Sequence analysis, expression, and deletion of a vaccinia virus gene RT encoding a homolog of profilin, a eukaryotic actin-binding protein."; RL J. Virol. 65:4598-4608(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91259063; PubMed=2045793; RA Smith G.L., Chan Y.S., Howard S.T.; RT "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near RT the right inverted terminal repeat."; RL J. Gen. Virol. 72:1349-1376(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., RA Osborne J., Wohlhueter R.; RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold RT redundancy and an error rate of 0.16/10kb."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION. RX MEDLINE=92258409; PubMed=1582424; RA Moore J.B., Smith G.L.; RT "Steroid hormone synthesis by a vaccinia enzyme: a new type of virus RT virulence factor."; RL EMBO J. 11:1973-1980(1992). 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: Steroid biosynthesis. 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; M72474; AAA48311.1; -; Genomic_DNA. DR EMBL; D11079; BAA01818.1; -; Genomic_DNA. DR EMBL; AY243312; AAO89449.1; -; Genomic_DNA. DR PIR; E40897; WMVZ2W. DR InterPro; IPR002225; 3Beta_HSD. DR Pfam; PF01073; 3Beta_HSD; 1. KW Isomerase; Multifunctional enzyme; NAD; Oxidoreductase; KW Steroidogenesis. FT CHAIN 1 346 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase. FT /FTId=PRO_0000087795. SQ SEQUENCE 346 AA; 39396 MW; 3107A2B7F442CCD9 CRC64; MAVYAVTGGA GFLGRYIVKL LISADDVQEI RVIDIVEDPQ PITSKVKVIN YIQCDINDFD KVREALDGVN LIIHTAALVD VFGKYTDNEI MKVNYYGTQT ILAACVDLGI KYLIYTSSME AIGPNKHGDP FIGHEHTLYD ISPGHVYAKS KRMAEQLVMK ANNSVIMNGA KLYTCCLRPT GIYGEGDKLT KVFYEQCKQH GNIMYRTVDD DAVHSRVYVG NVAWMHVLAA KYIQYPGSEI KGNAYFCYDY SPSCSYDMFN LLLMKPLGIE QGSRIPRWML KMYACKNDMK RILFRKPSLL NNYTLKISNT TFEVRTNNAE LDFNYSPIFN VDVAFERTRK WLEESE // ID 3BHS_VARV Reviewed; 61 AA. AC P33794; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 28-NOV-2006, entry version 26. DE Truncated 3-beta hydroxy-5-ene steroid dehydrogenase homolog. GN ORFNames=A50L; OS Variola virus. OC Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; OC Orthopoxvirus. OX NCBI_TaxID=10255; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=India-1967 / Isolate Ind3; RX MEDLINE=93202281; PubMed=8384129; DOI=10.1016/0014-5793(93)80041-R; RA Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.; RT "Genes of variola and vaccinia viruses necessary to overcome the host RT protective mechanisms."; RL FEBS Lett. 319:80-83(1993). CC -!- DOMAIN: Corresponds to the N-terminal domain of vaccinia virus 3- CC beta-HSD. 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; X69198; CAA49097.1; -; Genomic_DNA. DR PIR; F36853; F36853. DR InterPro; IPR002225; 3Beta_HSD. DR Pfam; PF01073; 3Beta_HSD; 1. FT CHAIN 1 61 Truncated 3-beta hydroxy-5-ene steroid FT dehydrogenase homolog. FT /FTId=PRO_0000087796. SQ SEQUENCE 61 AA; 6849 MW; 2563A2FAE6CCABD6 CRC64; MTVYAVTGGA EFLGRYIVKL LISADDVQEI RVINVVEDPQ PLVSKVKVIN YIQCDINDLI R // ID 3BP1_HUMAN Reviewed; 701 AA. AC Q9Y3L3; Q6IBZ2; Q6ZVL9; Q96HQ5; Q9NSQ9; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 3. DT 20-FEB-2007, entry version 60. DE SH3 domain-binding protein 1 (3BP-1). GN Name=SH3BP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=20057165; PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-701 (ISOFORM 1). RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 360-701 (ISOFORM 1). RC TISSUE=Melanoma; RG The German cDNA consortium; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Binds differentially to the SH3 domains of certain CC proteins of signal transduction pathways. This protein binds CC preferentially to the ABL1 proto-oncogene, SRC and GRB2. Shows GAP CC activity for Rac-related proteins but not for Rho- or Ras-related CC proteins. It inhibits PDGF-induced membrane ruffling mediated by CC Rac (By similarity). CC -!- INTERACTION: CC P08631:HCK; NbExp=1; IntAct=EBI-346869, EBI-346340; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y3L3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y3L3-2; Sequence=VSP_011373, VSP_011374; CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 Rho-GAP domain. CC -!- CAUTION: Ref.2 (BAC85842) sequence differs from that shown due to CC a stop codon in position 56 which was translated as Cys to extend CC the 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; CR456576; CAG30462.1; -; mRNA. DR EMBL; AK124370; BAC85842.1; ALT_INIT; mRNA. DR EMBL; Z83844; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008282; AAH08282.1; ALT_INIT; mRNA. DR EMBL; AL157480; CAB75671.2; -; mRNA. DR PIR; T46916; T46916. DR UniGene; Hs.601143; -. DR HSSP; Q98935; 1F7C. DR IntAct; Q9Y3L3; -. DR Ensembl; ENSG00000100092; Homo sapiens. DR KEGG; hsa:23616; -. DR HGNC; HGNC:10824; SH3BP1. DR HPA; HPA000757; -. DR ArrayExpress; Q9Y3L3; -. DR GermOnline; ENSG00000100092; Homo sapiens. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR004148; BAR. DR InterPro; IPR008936; Rho_GAP. DR InterPro; IPR000198; RhoGAP. DR Gene3D; G3DSA:1.10.555.10; RhoGAP; 1. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00324; RhoGAP; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50238; RHOGAP; 1. KW Alternative splicing; GTPase activation; Polymorphism; SH3-binding. FT CHAIN 1 701 SH3 domain-binding protein 1. FT /FTId=PRO_0000056723. FT DOMAIN 17 262 BAR. FT DOMAIN 276 469 Rho-GAP. FT MOTIF 617 625 SH3-binding (By similarity). FT VAR_SEQ 440 452 DQAQLDAASVSSI -> TEPARELGSQTLC (in FT isoform 2). FT /FTId=VSP_011373. FT VAR_SEQ 453 701 Missing (in isoform 2). FT /FTId=VSP_011374. FT VARIANT 431 431 L -> P (in dbSNP:rs929038). FT /FTId=VAR_019642. SQ SEQUENCE 701 AA; 75713 MW; 877D144E81F0F974 CRC64; MMKRQLHRMR QLAQTGSLGR TPETAEFLGE DLLQVEQRLE PAKRAAHNIH KRLQACLQGQ SGADMDKRVK KLPLMALSTT MAESFKELDP DSSMGKALEM SCAIQNQLAR ILAEFEMTLE RDVLQPLSRL SEEELPAILK HKKSLQKLVS DWNTLKSRLS QATKNSGSSQ GLGGSPGSHS HTTMANKVET LKEEEEELKR KVEQCRDEYL ADLYHFVTKE DSYANYFIRL LEIQADYHRR SLSSLDTALA ELRENHGQAD HSPSMTATHF PRVYGVSLAT HLQELGREIA LPIEACVMML LSEGMKEEGL FRLAAGASVL KRLKQTMASD PHSLEEFCSD PHAVAGALKS YLRELPEPLM TFDLYDDWMR AASLKEPGAR LQALQEVCSR LPPENLSNLR YLMKFLARLA EEQEVNKMTP SNIAIVLGPN LLWPPEKEGD QAQLDAASVS SIQVVGVVEA LIQSADTLFP GDINFNVSGL FSAVTLQDTV SDRLASEELP STAVPTPATT PAPAPAPAPA PAPALASAAT KERTESEVPP RPASPKVTRS PPETAAPVED MARRTKRPAP ARPTMPPPQV SGSRSSPPAP PLPPGSGSPG TPQALPRRLV GSSLRAPTVP PPLPPTPPQP ARRQSRRSPA SPSPASPGPA SPSPVSLSNP AQVDLGAATA EGGAPEAISG VPTPPAIPPQ PRPRSLASET N // ID 3BP1_MOUSE Reviewed; 601 AA. AC P55194; Q99KK8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 59. DE SH3 domain-binding protein 1 (3BP-1). GN Name=Sh3bp1; Synonyms=3bp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95347339; PubMed=7621827; RA Cicchetti P., Ridley A.J., Zheng Y., Cerione R.A., Baltimore D.; RT "3BP-1, an SH3 domain binding protein, has GAP activity for Rac and RT inhibits growth factor-induced membrane ruffling in fibroblasts."; RL EMBO J. 14:3127-3135(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). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 263-601. RX MEDLINE=92358242; PubMed=1379745; RA Cicchetti P., Mayer B.J., Thiel G., Baltimore D.; RT "Identification of a protein that binds to the SH3 region of Abl and RT is similar to Bcr and GAP-rho."; RL Science 257:803-806(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 528-537. RX MEDLINE=93174278; PubMed=8438166; RA Ren R., Mayer B.J., Cicchetti P., Baltimore D.; RT "Identification of a ten-amino acid proline-rich SH3 binding site."; RL Science 259:1157-1161(1993). CC -!- FUNCTION: Binds differentially to the SH3 domains of certain CC proteins of signal transduction pathways. This protein binds CC preferentially to the ABL1 proto-oncogene, SRC and GRB2. Shows GAP CC activity for Rac-related proteins but not for Rho- or Ras-related CC proteins. It inhibits PDGF-induced membrane ruffling mediated by CC Rac. CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest CC levels found in spleen and brain, lowest in heart and liver. CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 Rho-GAP 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; X87671; CAA61011.1; -; mRNA. DR EMBL; BC004598; AAH04598.1; -; mRNA. DR PIR; S56144; S56144. DR UniGene; Mm.4462; -. DR PDB; 1ABO; X-ray; C/D=528-537. DR KEGG; mmu:20401; -. DR MGI; MGI:104603; Sh3bp1. DR LinkHub; P55194; -. DR ArrayExpress; P55194; -. DR GermOnline; ENSMUSG00000022436; Mus musculus. DR InterPro; IPR004148; BAR. DR InterPro; IPR008936; Rho_GAP. DR InterPro; IPR000198; RhoGAP. DR Gene3D; G3DSA:1.10.555.10; RhoGAP; 1. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00324; RhoGAP; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50238; RHOGAP; 1. KW 3D-structure; GTPase activation; SH3-binding. FT CHAIN 1 601 SH3 domain-binding protein 1. FT /FTId=PRO_0000056724. FT DOMAIN 1 182 BAR. FT DOMAIN 196 390 Rho-GAP. FT MOTIF 529 537 SH3-binding. FT CONFLICT 46 48 RSG -> PLS (in Ref. 2). FT CONFLICT 229 229 Missing (in Ref. 2). FT CONFLICT 261 261 G -> D (in Ref. 2). FT CONFLICT 592 593 PA -> RP (in Ref. 2). FT STRAND 530 531 SQ SEQUENCE 601 AA; 65260 MW; 0FBBF357EEB02ECE CRC64; MAESFKELDP DSSMGKALEM TCAIQNQLAR ILAEFEMTLE RDVLQRSGRL SEEELPAILK HKKSLQKLVS DWNTLKSRLS QAAKNSGSNQ GLGGASGSHT HTTTANKVEM LKEEEEELKK KVEQCKDEYL ADLYHFSTKE DSYANYFIHL LEIQADYHRK SLTSLDTALA ELRDNHNQAD HSPLTTAAPF SRVYGVSLRT HLQDLGRDIA LPIEACVLLL LSEGMQEEEG LFRLAAGASV LKRLKQTMAS DPHSLEEFCS GPHAVAGALK SYLRELPEPL MTSDLYDDWM RAASLKEPGA RLEALHDVCS RLPQENFNNL RYLMKFLALL AEEQDVNKMT PSNIAIVLGP NLLWPPEKEG DQAQLDAASV SSIQVVGVVE ALIQNADTLF PGDINFNVSG IFPGLAPQEK VSSQQVSEEL PPVTVPAPAT TPAPTLAPAS MAVRERTEAD LPKPTSPKVS RNPTETAASA EDMTRKTKRP APARPTMPPP QPSSTRSSPP APSLPPGSVS PGTPQALPRR LVGTSLRAPT MPPPLPPVPP QPARRQSRRL PASPVISNMP AQVDQGVATE DREGPEAVGG HPPPPALPPQ PPARGLISET E // ID 3BP2_HUMAN Reviewed; 561 AA. AC P78314; O00500; O15373; P78315; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 20-FEB-2007, entry version 63. DE SH3 domain-binding protein 2 (3BP-2). GN Name=SH3BP2; Synonyms=3BP2; ORFNames=RES4-23; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG). RX MEDLINE=97446134; PubMed=9299232; DOI=10.1006/geno.1997.4849; RA Bell S.M., Shaw M., Jou Y.-S., Myers R.M., Knowles M.A.; RT "Identification and characterization of the human homologue of SH3BP2, RT an SH3 binding domain protein within a common region of deletion at RT 4p16.3 involved in bladder cancer."; RL Genomics 44:163-170(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX MEDLINE=98403881; PubMed=9734812; DOI=10.1093/dnares/5.3.177; RA Hadano S., Ishida Y., Ikeda J.-E.; RT "The primary structure and genomic organization of five novel RT transcripts located close to the Huntington's disease gene on human RT chromosome 4p16.3."; RL DNA Res. 5:177-186(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG). RC TISSUE=Tonsil; RA Gokemeijer J., Deligiannidis K.E., Ligris K., Ernst T.J.; RT "3BP2 binds to phosphatidylinositols; linking the hemopoietic tyrosine RT kinase c-FES to the cytoplasmic membrane in a phosphorylation RT dependent mechanism."; RL Blood 88:473A-473A(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RC TISSUE=Cervix; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004). RN [6] RP VARIANTS CRBM GLN-415; PRO-415; ARG-418; HIS-418; LEU-418; ARG-420 AND RP GLU-420. RX MEDLINE=21275962; PubMed=11381256; DOI=10.1038/88832; RA Ueki Y., Tiziani V., Santanna C., Fukai N., Maulik C., Garfinkle J., RA Ninomiya C., doAmaral C., Peters H., Habal M., Rhee-Morris L., RA Doss J.B., Kreiborg S., Olsen B.R., Reichenberger E.; RT "Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause RT cherubism."; RL Nat. Genet. 28:125-126(2001). RN [7] RP VARIANT CRBM ARG-420. RX MEDLINE=22781491; PubMed=12900899; DOI=10.1002/ajmg.a.20226; RA Lo B., Faiyaz-Ul-Haque M., Kennedy S., Aviv R., Tsui L.C., Teebi A.S.; RT "Novel mutation in the gene encoding c-Abl-binding protein SH3BP2 RT causes cherubism."; RL Am. J. Med. Genet. A 121:37-40(2003). RN [8] RP VARIANT CRBM ARG-418. RX PubMed=14577811; DOI=10.1597/1545-1569(2003)040<0632:AMMITS>2.0.CO;2; RA Imai Y., Kanno K., Moriya T., Kayano S., Seino H., Matsubara Y., RA Yamada A.; RT "A missense mutation in the SH3BP2 gene on chromosome 4p16.3 found in RT a case of nonfamilial cherubism."; RL Cleft Palate Craniofac. J. 40:632-638(2003). CC -!- FUNCTION: Binds differentially to the SH3 domains of certain CC proteins of signal transduction pathways. Binds to CC phosphatidylinositols; linking the hemopoietic tyrosine kinase fes CC to the cytoplasmic membrane in a phosphorylation dependent CC mechanism. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P78314-1; Sequence=Displayed; CC Name=Short; CC IsoId=P78314-2; Sequence=VSP_004085, VSP_004086; 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; CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues including CC lung, liver, skeletal muscle, kidney and pancreas. CC -!- DISEASE: Defects in SH3BP2 are the cause of cherubism (CRBM) CC [MIM:118400]. CRBM is an autosomal dominant inherited syndrome CC characterized by excessive bone degradation of the upper and lower CC jaws, which often begins around three years of age. It is followed CC by development of fibrous tissue masses, which causes a CC characteristic facial swelling. CC -!- SIMILARITY: Contains 1 PH domain. CC -!- SIMILARITY: Contains 1 SH2 domain. CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=SH3BP2". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U56386; AAB72034.1; -; mRNA. DR EMBL; AB000462; BAA19119.1; -; mRNA. DR EMBL; AB000463; BAA19120.1; -; mRNA. DR EMBL; AF000936; AAB59973.1; -; mRNA. DR EMBL; BC022996; AAH22996.1; -; mRNA. DR UniGene; Hs.167679; -. DR PDB; 2CR4; NMR; A=444-558. DR Ensembl; ENSG00000087266; Homo sapiens. DR KEGG; hsa:6452; -. DR H-InvDB; HIX0004037; -. DR HGNC; HGNC:10825; SH3BP2. DR MIM; 118400; phenotype. DR MIM; 602104; gene. DR ArrayExpress; P78314; -. DR GermOnline; ENSG00000087266; Homo sapiens. DR RZPD-ProtExp; IOH10666; -. DR RZPD-ProtExp; M0173; -. DR GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR001849; PH. DR InterPro; IPR011993; PH_type. DR InterPro; IPR000980; SH2. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Gene3D; G3DSA:3.30.505.10; SH2; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00017; SH2; 1. DR ProDom; PD000093; SH2; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00252; SH2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50001; SH2; 1. KW 3D-structure; Alternative splicing; Disease mutation; SH2 domain; KW SH3-binding. FT CHAIN 1 561 SH3 domain-binding protein 2. FT /FTId=PRO_0000064365. FT DOMAIN 26 130 PH. FT DOMAIN 457 555 SH2. FT MOTIF 201 210 SH3-binding. FT COMPBIAS 205 212 Poly-Pro. FT COMPBIAS 236 240 Poly-Pro. FT VAR_SEQ 81 97 VMRAAEETTSNNVFPFK -> QPRPQPAQALSQTEAGP FT (in isoform Short). FT /FTId=VSP_004085. FT VAR_SEQ 98 561 Missing (in isoform Short). FT /FTId=VSP_004086. FT VARIANT 415 415 R -> P (in CRBM). FT /FTId=VAR_013257. FT VARIANT 415 415 R -> Q (in CRBM). FT /FTId=VAR_013258. FT VARIANT 418 418 P -> H (in CRBM). FT /FTId=VAR_013259. FT VARIANT 418 418 P -> L (in CRBM). FT /FTId=VAR_013260. FT VARIANT 418 418 P -> R (in CRBM). FT /FTId=VAR_013261. FT VARIANT 420 420 G -> E (in CRBM). FT /FTId=VAR_013262. FT VARIANT 420 420 G -> R (in CRBM). FT /FTId=VAR_013263. FT CONFLICT 27 27 V -> L (in Ref. 3). FT CONFLICT 224 224 H -> N (in Ref. 3). FT CONFLICT 249 249 L -> R (in Ref. 3). FT CONFLICT 251 251 A -> P (in Ref. 3). SQ SEQUENCE 561 AA; 62244 MW; 69E6846A4F6D8F15 CRC64; MAAEEMHWPV PMKAIGAQNL LTMPGGVAKA GYLHKKGGTQ LQLLKWPLRF VIIHKRCVYY FKSSTSASPQ GAFSLSGYNR VMRAAEETTS NNVFPFKIIH ISKKHRTWFF SASSEEERKS WMALLRREIG HFHEKKDLPL DTSDSSSDTD SFYGAVERPV DISLSPYPTD NEDYEHDDED DSYLEPDSPE PGRLEDALMH PPAYPPPPVP TPRKPAFSDM PRAHSFTSKG PGPLLPPPPP KHGLPDVGLA AEDSKRDPLC PRRAEPCPRV PATPRRMSDP PLSTMPTAPG LRKPPCFRES ASPSPEPWTP GHGACSTSSA AIMATATSRN CDKLKSFHLS PRGPPTSEPP PVPANKPKFL KIAEEDPPRE AAMPGLFVPP VAPRPPALKL PVPEAMARPA VLPRPEKPQL PHLQRSPPDG QSFRSFSFEK PRQPSQADTG GDDSDEDYEK VPLPNSVFVN TTESCEVERL FKATSPRGEP QDGLYCIRNS STKSGKVLVV WDETSNKVRN YRIFEKDSKF YLEGEVLFVS VGSMVEHYHT HVLPSHQSLL LRHPYGYTGP R // ID 3BP2_MOUSE Reviewed; 559 AA. AC Q06649; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 45. DE SH3 domain-binding protein 2 (3BP-2). GN Name=Sh3bp2; Synonyms=3bp2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93174278; PubMed=8438166; RA Ren R., Mayer B.J., Cicchetti P., Baltimore D.; RT "Identification of a ten-amino acid proline-rich SH3 binding site."; RL Science 259:1157-1161(1993). CC -!- FUNCTION: Binds differentially to the SH3 domains of certain CC proteins of signal transduction pathways. Binds to CC phosphatidylinositols; linking the hemopoietic tyrosine kinase fes CC to the cytoplasmic membrane in a phosphorylation dependent CC mechanism (By similarity). CC -!- SIMILARITY: Contains 1 PH domain. CC -!- SIMILARITY: Contains 1 SH2 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; L14543; AAA37121.1; -; mRNA. DR PIR; I49444; I49444. DR UniGene; Mm.5012; -. DR HSSP; Q9HB21; 1EAZ. DR SMR; Q06649; 442-558. DR Ensembl; ENSMUSG00000054520; Mus musculus. DR KEGG; mmu:24055; -. DR MGI; MGI:1346349; Sh3bp2. DR ArrayExpress; Q06649; -. DR GermOnline; ENSMUSG00000054520; Mus musculus. DR InterPro; IPR001849; PH. DR InterPro; IPR011993; PH_type. DR InterPro; IPR000980; SH2. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Gene3D; G3DSA:3.30.505.10; SH2; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00017; SH2; 1. DR ProDom; PD000093; SH2; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00252; SH2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50001; SH2; 1. KW SH2 domain; SH3-binding. FT CHAIN 1 559 SH3 domain-binding protein 2. FT /FTId=PRO_0000064366. FT DOMAIN 26 130 PH. FT DOMAIN 455 553 SH2. FT MOTIF 201 210 SH3-binding. FT COMPBIAS 205 212 Poly-Pro. FT COMPBIAS 236 240 Poly-Pro. SQ SEQUENCE 559 AA; 62208 MW; EDFE1F11B259646E CRC64; MAAEEMQWPV PMKAIGAQNL LTMPGGVAKA GYLHKKGGTQ LQLLKWPLRF VIIHKRCIYY FKSSTSASPQ GAFSLSGYNR VMRAAEETTS NNVFPFKIIH ISKKHRTWFF SASSEDERKS WMAFVRREIG HFHEKKELPL DTSDSSSDTD SFYGAVERPI DISLSSYPMD NEDYEHEDED DSYLEPDSPG PMKLEDALTY PPAYPPPPVP VPRKPAFSDL PRAHSFTSKS PSPLLPPPPP KRGLPDTGSA PEDAKDALGL RRVEPGLRVP ATPRRMSDPP MSNVPTVPNL RKHPCFRDSV NPGLEPWTPG HGTSSVSSST TMAVATSRNC DKLKSFHLSS RGPPTSEPPP VPANKPKFLK IAEEPSPREA AKFAPVPPVA PRPPVQKMPM PEATVRPAVL PRPENTPLPH LQRSPPDGQS FRGFSFEKAR QPSQADTGEE DSDEDYEKVP LPNSVFVNTT ESCEVERLFK ATDPRGEPQD GLYCIRNSST KSGKVLVVWD ESSNKVRNYR IFEKDSKFYL EGEVLFASVG SMVEHYHTHV LPSHQSLLLR HPYGYAGPR // ID 3BP5_DROME Reviewed; 476 AA. AC Q9V785; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2003, sequence version 3. DT 23-JAN-2007, entry version 41. DE SH3 domain-binding protein 5-like (Protein parcase). GN Name=pcs; ORFNames=CG7761; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- INTERACTION: CC Q9W3Y7:Pat1; NbExp=1; IntAct=EBI-194451, EBI-115606; CC Q9VME5:slam; NbExp=1; IntAct=EBI-194451, EBI-191523; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- CAUTION: Ref.1 sequence differs from that shown due to erroneous CC 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; AE003812; AAF58174.4; -; Genomic_DNA. DR EMBL; AY058328; AAL13557.1; -; mRNA. DR UniGene; Dm.4202; -. DR IntAct; Q9V785; -. DR Ensembl; CG7761; Drosophila melanogaster. DR KEGG; dme:Dmel_CG7761; -. DR FlyBase; FBgn0033988; pcs. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-004705-MONOMER; -. DR GermOnline; CG7761; Drosophila melanogaster. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR007940; SH3_bd_5. DR Pfam; PF05276; SH3BP5; 1. KW Complete proteome; Hypothetical protein; SH3-binding. FT CHAIN 1 476 SH3 domain-binding protein 5-like. FT /FTId=PRO_0000064367. FT CONFLICT 34 34 L -> LE (in Ref. 3). SQ SEQUENCE 476 AA; 53637 MW; E070E9311060B191 CRC64; MSSAEDGELD PQIQIELENL NSATDEINKL EIELEANSTF RILLNESTRR LKVSSKKLGN CIEKARPYYE ALDKAREAQI ECQKAAVKFQ RANEIHAAAK ETVALAEQRF MSNSHEWQFD NAWQEMLNHA TQKVMDAETQ KADCHAEHQR LTKLFNAAEQ KLQQLEDRFR RSINKSRPYF EEKQVCQDQL QTQKNRIQEL QQQVAGAKST YSTALRNLER ISEDIHRQRG DFPTPPGPRE PGVGAELNSP TSSALPSLPD FQLELEKCDY PSIAGSQMSL GAKTPQAAAE TEDEEDACDY DETGAGELRG VVDERDLEAL RQKVKILAVR PIEGGDGQQQ NDVWEHELKA TVDKLDHLMM LKETAKRQQT NRLKSTEQRP DSLGAEALKR HCDVVEVKVT SCATTASLPV TPHHQLNHLA PPTPIKKLQQ QLAPLPSVNV SMRELPLLAR LSNELLDRSS AAFGGVRKTL RRRSLE // ID 3BP5_HUMAN Reviewed; 455 AA. AC O60239; Q5JWV9; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-FEB-2007, entry version 49. DE SH3 domain-binding protein 5 (SH3 domain-binding protein that DE preferentially associates with BTK). GN Name=SH3BP5; Synonyms=SAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; RG The German cDNA consortium; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 10-455, FUNCTION, INTERACTION WITH BTK, RP AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX MEDLINE=98238637; PubMed=9571151; DOI=10.1006/bbrc.1998.8420; RA Matsushita M., Yamadori T., Kato S., Takemoto Y., Inazawa J., Baba Y., RA Hashimoto S., Sekine S., Arai S., Kunikata T., Kurimoto M., RA Kishimoto T., Tsukada S.; RT "Identification and characterization of a novel SH3-domain binding RT protein, Sab, which preferentially associates with Bruton's tyrosine RT kinase (Btk)."; RL Biochem. Biophys. Res. Commun. 245:337-343(1998). RN [4] RP INTERACTION WITH MAPK8; MAPK9 AND MAPK10, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF LEU-347; LEU-349; LEU-434 AND LEU-436. RX MEDLINE=22280328; PubMed=12167088; DOI=10.1042/BJ20020553; RA Wiltshire C., Matsushita M., Tsukada S., Gillespie D.A., May G.H.; RT "A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab RT (SH3BP5), associates with mitochondria."; RL Biochem. J. 367:577-585(2002). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASS RP SPECTROMETRY. RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). CC -!- FUNCTION: Inhibits the auto- and transphosphorylation activity of CC BTK. Plays a negative regulatory role in BTK-related cytoplasmic CC signaling in B-cells. May be involved in BCR-induced apoptotic CC cell death. CC -!- SUBUNIT: Interacts with BTK. Interacts with all isoforms of MAPK8, CC MAPK9, MAPK10 and MAPK12. CC -!- INTERACTION: CC Q06187:BTK; NbExp=3; IntAct=EBI-624860, EBI-624835; CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- TISSUE SPECIFICITY: Highly expressed in testis and ovaries. It is CC also expressed in a variety of tissues including spleen, lymph CC node, thymus, bone marrow, fetal liver, colon, small intestine and CC prostate. CC -!- SIMILARITY: Belongs to the SH3BP5 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL117422; CAI46220.1; -; mRNA. DR EMBL; BC010123; AAH10123.2; -; mRNA. DR EMBL; AB005047; BAA25922.1; ALT_INIT; mRNA. DR PIR; JE0086; JE0086. DR UniGene; Hs.257761; -. DR IntAct; O60239; -. DR Ensembl; ENSG00000131370; Homo sapiens. DR KEGG; hsa:9467; -. DR H-InvDB; HIX0003100; -. DR HGNC; HGNC:10827; SH3BP5. DR MIM; 605612; gene. DR ArrayExpress; O60239; -. DR GermOnline; ENSG00000131370; Homo sapiens. DR RZPD-ProtExp; IOH13842; -. DR RZPD-ProtExp; P0046; -. DR RZPD-ProtExp; RZPDo839B0576; -. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:MGI. DR GO; GO:0007242; P:intracellular signaling cascade; IDA:MGI. DR InterPro; IPR007940; SH3_bd_5. DR Pfam; PF05276; SH3BP5; 1. KW Mitochondrion; Phosphorylation; SH3-binding. FT CHAIN 1 455 SH3 domain-binding protein 5. FT /FTId=PRO_0000064368. FT COMPBIAS 36 40 Poly-Glu. FT COMPBIAS 278 421 Ser-rich. FT COMPBIAS 405 410 Poly-Ser. FT MOD_RES 351 351 Phosphoserine (by MAPK12 and MAPK9) (By FT similarity). FT MOD_RES 421 421 Phosphoserine (by MAPK12) (By FT similarity). FT MUTAGEN 347 347 L->A: Loss of phosphorylation and binding FT by phospho-JNK; when associated with A- FT 349. FT MUTAGEN 349 349 L->A: Loss of phosphorylation and binding FT by phospho-JNK; when associated with A- FT 347. FT MUTAGEN 434 434 L->A: No change of phosphorylation or FT binding by phospho-JNK; when associated FT with A-436. FT MUTAGEN 436 436 L->A: No change of phosphorylation or FT binding by phospho-JNK; when associated FT with A-434. SQ SEQUENCE 455 AA; 50425 MW; 5C8CA4861D66346B CRC64; MDAALKRSRS EEPAEILPPA RDEEEEEEEG MEQGLEEEEE VDPRIQGELE KLNQSTDDIN RRETELEDAR QKFRSVLVEA TVKLDELVKK IGKAVEDSKP YWEARRVARQ AQLEAQKATQ DFQRATEVLR AAKETISLAE QRLLEDDKRQ FDSAWQEMLN HATQRVMEAE QTKTRSELVH KETAARYNAA MGRMRQLEKK LKRAINKSKP YFELKAKYYV QLEQLKKTVD DLQAKLTLAK GEYKMALKNL EMISDEIHER RRSSAMGPRG CGVGAEGSST SVEDLPGSKP EPDAISVASE AFEDDSCSNF VSEDDSETQS VSSFSSGPTS PSEMPDQFPA VVRPGSLDLP SPVSLSEFGM MFPVLGPRSE CSGASSPECE VERGDRAEGA ENKTSDKANN NRGLSSSSGS GGSSKSQSST SPEGQALENR MKQLSLQCSK GRDGIIADIK MVQIG // ID 3BP5_MOUSE Reviewed; 463 AA. AC Q9Z131; Q3TTD6; Q8C903; Q8VCZ0; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 43. DE SH3 domain-binding protein 5 (SH3 domain-binding protein that DE preferentially associates with BTK). GN Name=Sh3bp5; Synonyms=Sab; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Cerebellum, 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 2). RC TISSUE=Embryo, 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-458 (ISOFORM 2), AND FUNCTION. RC STRAIN=C57BL/6; TISSUE=Spleen; RX MEDLINE=99272695; PubMed=10339589; DOI=10.1073/pnas.96.11.6341; RA Yamadori T., Baba Y., Mastushita M., Hashimoto S., Kurosaki M., RA Kurosaki T., Kishimoto T., Tsukada S.; RT "Bruton's tyrosine kinase activity is negatively regulated by Sab, the RT Btk-SH3 domain-binding protein."; RL Proc. Natl. Acad. Sci. U.S.A. 96:6341-6346(1999). CC -!- FUNCTION: Inhibits the auto- and transphosphorylation activity of CC BTK. Plays a negative regulatory role in BTK-related cytoplasmic CC signaling in B-cells. May be involved in BCR-induced apoptotic CC cell death. CC -!- SUBUNIT: Interacts with BTK. Interacts with all isoforms of MAPK8, CC MAPK9, MAPK10 and MAPK12 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9Z131-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=2; CC IsoId=Q9Z131-2; Sequence=VSP_010882; CC Name=3; CC IsoId=Q9Z131-3; Sequence=VSP_022572, VSP_010882; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the SH3BP5 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK043375; BAC31530.1; ALT_INIT; mRNA. DR EMBL; AK161427; BAE36389.1; -; mRNA. DR EMBL; BC018237; AAH18237.2; -; mRNA. DR EMBL; BC053741; AAH53741.2; -; mRNA. DR EMBL; AB016835; BAA75641.1; -; mRNA. DR UniGene; Mm.383198; -. DR Ensembl; ENSMUSG00000021892; Mus musculus. DR KEGG; mmu:24056; -. DR MGI; MGI:1344391; Sh3bp5. DR ArrayExpress; Q9Z131; -. DR GermOnline; ENSMUSG00000021892; Mus musculus. DR RZPD-ProtExp; IOM20255; -. DR GO; GO:0005737; C:cytoplasm; IC:MGI. DR GO; GO:0017124; F:SH3 domain binding; TAS:UniProtKB. DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB. DR InterPro; IPR007940; SH3_bd_5. DR InterPro; IPR011990; TPR-like_helical. DR Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1. DR Pfam; PF05276; SH3BP5; 1. KW Alternative splicing; Mitochondrion; Phosphorylation; SH3-binding. FT CHAIN 1 463 SH3 domain-binding protein 5. FT /FTId=PRO_0000064369. FT COMPBIAS 38 43 Poly-Glu. FT MOD_RES 354 354 Phosphoserine (by MAPK12 and MAPK9) (By FT similarity). FT MOD_RES 424 424 Phosphoserine (by MAPK12) (By FT similarity). FT VAR_SEQ 1 70 MDTALKRSRSDEPAELPPPAREVEEKEEEEERMEQGLEEEE FT EEVDPRIQGELEKLNQSTDDINRRETELE -> MDWARTVM FT ASTGLAPASAAPHTGSRAQPCLFLAPVPPHFAWFIFLDPAL FT PCSTLAQSVSFKPCCGVVK (in isoform 3). FT /FTId=VSP_022572. FT VAR_SEQ 455 463 IFIFYTFLQ -> VQIG (in isoform 2 and FT isoform 3). FT /FTId=VSP_010882. FT CONFLICT 299 299 S -> SS (in Ref. 1; BAC31530). SQ SEQUENCE 463 AA; 51807 MW; A4274A91DDD91670 CRC64; MDTALKRSRS DEPAELPPPA REVEEKEEEE ERMEQGLEEE EEEVDPRIQG ELEKLNQSTD DINRRETELE DARQKFRSVL VEATVKLDEL AKKIGKAVED SKPYWEARRV ARQAQLEAQK ATQDFQRATE VLRAAKETIS LAEQRLLEDD KRQFDSAWQE MLNHATQRVM EAEQTKTRSE LVHKETAARY NAAMGRMRQL EKKLKRAINK SKPYFELKAK YYVQLEQLKK TVDDLQAKLA LAKGEYKAAL KSLERISDEI HERRRSNAMG PRGCGVGAEG SIASVENLPV SKPEPDAISV ASEAFEDDNC SNLVSEDDSE TQSVSSFSSG PTSPSEMPDQ FPAVARPGSL DLPSPVSLSE FGMMFPILGP RSECSGASSP ECEVERGDRA EGAENKMSDK ANNNRVLGST NGGSGRSRSQ SSTSLESQAL ETRMKQLSLQ CSKGRDGIIA DIKMIFIFYT FLQ // ID 3BP5_RAT Reviewed; 457 AA. AC Q91Y80; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-FEB-2007, entry version 36. DE SH3 domain-binding protein 5 (Vascular endothelial cell-specific DE protein 18). GN Name=Sh3bp5; Synonyms=Sab, Vesp18; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Aoki T., Toyoda H., Nishimoto S., Tawara J., Komurasaki T.; RT "Identification of VESP18, a vascular endothelial cell specific RT protein."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP INTERACTION WITH MAPK9 AND MAPK12, PHOSPHORYLATION AT SER-353 AND RP SER-423, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-353 AND SER-423. RX PubMed=15158451; DOI=10.1016/j.bbrc.2004.04.148; RA Court N.W., Kuo I., Quigley O., Bogoyevitch M.A.; RT "Phosphorylation of the mitochondrial protein Sab by stress-activated RT protein kinase 3."; RL Biochem. Biophys. Res. Commun. 319:130-137(2004). CC -!- FUNCTION: Inhibits the auto- and transphosphorylation activity of CC BTK. Plays a negative regulatory role in BTK-related cytoplasmic CC signaling in B-cells. May be involved in BCR-induced apoptotic CC cell death (By similarity). CC -!- SUBUNIT: Interacts with BTK. Interacts with all isoforms of MAPK8, CC MAPK9, MAPK10 and MAPK12. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the SH3BP5 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB027562; BAB47152.1; ALT_INIT; mRNA. DR UniGene; Rn.163321; -. DR Ensembl; ENSRNOG00000019475; Rattus norvegicus. DR KEGG; rno:117186; -. DR RGD; 620220; Sh3bp5. DR GermOnline; ENSRNOG00000019475; Rattus norvegicus. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR InterPro; IPR007940; SH3_bd_5. DR InterPro; IPR011990; TPR-like_helical. DR Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1. DR Pfam; PF05276; SH3BP5; 1. KW Mitochondrion; Phosphorylation; SH3-binding. FT CHAIN 1 457 SH3 domain-binding protein 5. FT /FTId=PRO_0000064370. FT COMPBIAS 38 42 Poly-Glu. FT MOD_RES 353 353 Phosphoserine (by MAPK12 and MAPK9). FT MOD_RES 423 423 Phosphoserine (by MAPK12). FT MUTAGEN 353 353 S->A: Large decrease in phosphorylation FT by SAPK3. FT MUTAGEN 423 423 S->A: Slight decrease in phosphorylation FT by SAPK3. SQ SEQUENCE 457 AA; 50829 MW; 68339F6993950B7C CRC64; MDTALKRSRS EEPVELPPPA REAEEKEEEE ERMEQGLEEE EEVDPRIQGE LEKLNQSTDD INRRETELED ARQKFRSVLV EATVKLDELA KKIGKAVEDS KPYWEARRVA RQAQLEAQKA TQDFQRATEV LRAAKETISL AEQRLLEDDK RQFDSAWQEM LNHATQRVME AEQTKTRSEL VHKETAARYN AAMGRMRQLE KKLKRAINKS KPYFELKAKY YVQLEQLKKT VDDLQAKLAL AKGEYKAALK SLERISDEIH ERRRSNAMGP RGCGVGAEGS ITSVENLPAS KPEPDAISVA SEAFEDDNCG NLVSEDDSET QSVSSFSSGP TSPSEMPDQF PAVARPGSLD LPSPVSLSEF GMMFPILGPR SECSGASSPE CEVERGDRAE GAENKMSDKA NNNRVLSSTS AGGGRSRSQS STSLEGQALE TRMKQLSLQC SKGREGIIAD IKTVQIG // ID 3CL_HUMAN Reviewed; 51 AA. AC Q13412; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 22. DE Pre-T/NK cell-associated protein 3Cl. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=94044805; PubMed=8228263; RA Ranes-Goldberg M.G., Hori T., Mohan-Peterson S., Spits H.; RT "Identification of human pre-T/NK cell-associated genes."; RL J. Immunol. 151:5810-5821(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L17328; AAB02341.1; -; mRNA. DR UniGene; Hs.258563; -. DR LinkHub; Q13412; -. DR GO; GO:0030097; P:hemopoiesis; NAS:UniProtKB. FT CHAIN 1 51 Pre-T/NK cell-associated protein 3Cl. FT /FTId=PRO_0000064371. SQ SEQUENCE 51 AA; 6457 MW; B5DF6295FAAEAA79 CRC64; MICCQETVYS CEYWRTFKRY FSSWRFKIRS WLTYLSWGLL CTSWYCKVKM S // ID 3CP1_STRS9 Reviewed; 21 AA. AC P37046; Q7M104; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 16-FEB-2004, sequence version 2. DT 20-FEB-2007, entry version 33. DE Tricyclic peptide RP 71955. OS Streptomyces sp. (strain SP9440). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=72594; RN [1] RP PROTEIN SEQUENCE, AND STRUCTURE BY NMR. RX MEDLINE=94114512; PubMed=8286361; DOI=10.1021/bi00167a006; RA Frechet D., Guitton J.D., Herman F., Faucher D., Helynck G., RA Monegier du Sorbier B., Ridoux J.P., James-Surcouf E., Vuilhorgne M.; RT "Solution structure of RP 71955, a new 21 amino acid tricyclic peptide RT active against HIV-1 virus."; RL Biochemistry 33:42-50(1994). CC -!- FUNCTION: Active against HIV-1 virus. CC -!- CAUTION: The isopeptide linked residue 9 is shown as Asn rather CC than Asp as mentioned in Ref.1, because it is not known whether CC Asp or Asn is encoded and the isopeptide bonds are almost always CC formed between the amides Asn or Gln and N6-lysine or alpha amino CC groups, with the liberation of an ammonia that makes the reaction CC essentially irreversible. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A53630; A53630. DR PDB; 1RPB; NMR; @=1-21. DR PDB; 1RPC; NMR; @=1-21. KW 3D-structure; Antiviral defense; Direct protein sequencing. FT PEPTIDE 1 21 Tricyclic peptide RP 71955. FT /FTId=PRO_0000044214. FT DISULFID 1 13 FT DISULFID 7 19 FT CROSSLNK 1 9 Isoaspartyl cysteine isopeptide (Cys- FT Asn). FT STRAND 5 7 FT STRAND 9 13 FT STRAND 15 18 SQ SEQUENCE 21 AA; 2185 MW; EF94FAA21E96FF91 CRC64; CLGIGSCNNF AGCGYAVVCF W // ID 3CP2_STRSQ Reviewed; 21 AA. AC P85078; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 20-FEB-2007, entry version 1. DE Tricyclic peptide MS-271. OS Streptomyces sp. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1931; RN [1] RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, D-AMINO ACID AT TRP-21, RP AND DISULFIDE BONDS. RC STRAIN=M-271; RX PubMed=8689231; RA Yano K., Toki S., Nakanishi S., Ochiai K., Ando K., Yoshida M., RA Matsuda Y., Yamasaki M.; RT "MS-271, a novel inhibitor of calmodulin-activated myosin light chain RT kinase from Streptomyces sp. -- I. Isolation, structural determination RT and biological properties of MS-271."; RL Bioorg. Med. Chem. 4:115-120(1996). RN [2] RP STRUCTURE BY NMR OF 1-21. RX PubMed=8689232; RA Katahira R., Yamasaki M., Matsuda Y., Yoshida M.; RT "MS-271, a novel inhibitor of calmodulin-activated myosin light chain RT kinase from Streptomyces sp. -- II. Solution structure of MS-271: RT characteristic features of the 'lasso' structure."; RL Bioorg. Med. Chem. 4:121-129(1996). CC -!- FUNCTION: Inhibits chicken myosin light chain kinase with an CC IC(50) of 8 M. Does not inhibit bovine cAMP-dependent protein CC kinase or rat protein kinase C. Antibacterial activity against the CC Gram-positive bacteria B.subtilis, E.faecium and S.aureus. No CC antibacterial activity against the Gram-negative bacteria E.coli, CC K.pneumoniae, P.aeruginosa, P.vulgaris, S.sonnei and S.typhosa. No CC antifungal activity against C.albicans. CC -!- MASS SPECTROMETRY: MW=2168.8596; METHOD=FAB; RANGE=1-21; CC NOTE=Ref.1. CC -!- CAUTION: The isopeptide linked residue 9 is shown as Asn rather CC than Asp as mentioned in Ref.1, because it is not known whether CC Asp or Asn is encoded and the isopeptide bonds are almost always CC formed between the amides Asn or Gln and N6-lysine or alpha amino CC groups, with the liberation of an ammonia that makes the reaction CC essentially irreversible. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Antibiotic; Antimicrobial; D-amino acid; Direct protein sequencing; KW Protein kinase inhibitor. FT PEPTIDE 1 21 Tricyclic peptide MS-271. FT /FTId=PRO_0000278145. FT MOD_RES 21 21 D-tryptophan. FT DISULFID 1 13 FT DISULFID 7 19 FT CROSSLNK 1 9 Isoaspartyl cysteine isopeptide (Cys- FT Asn). SQ SEQUENCE 21 AA; 2185 MW; EF8296720C06FF91 CRC64; CLGVGSCNNF AGCGYAIVCF W // ID 3DHQ_ACIAD Reviewed; 272 AA. AC Q59087; Q6FBK7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 06-FEB-2007, entry version 49. DE Catabolic 3-dehydroquinate dehydratase (EC 4.2.1.10) (3- DE dehydroquinase). GN Name=quiB; OrderedLocusNames=ACIAD1713; OS Acinetobacter sp. (strain ADP1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RX MEDLINE=96011389; PubMed=7592351; RA Elsemore D.A., Ornston L.N.; RT "Unusual ancestry of dehydratases associated with quinate catabolism RT in Acinetobacter calcoaceticus."; RL J. Bacteriol. 177:5971-5978(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., RA Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., RA Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. RT ADP1, a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). CC -!- FUNCTION: Catalyzes the catabolic dehydration of dehydroquinate to CC dehydroshikimate. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate CC biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1. CC -!- INDUCTION: By protocatechuate. CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L05770; AAC37158.1; ALT_INIT; Genomic_DNA. DR EMBL; CR543861; CAG68555.1; ALT_INIT; Genomic_DNA. DR HSSP; P24670; 1L9W. DR GenomeReviews; CR543861_GR; ACIAD1713. DR KEGG; aci:ACIAD1713; -. DR BioCyc; MetaCyc:MONOMER-33; -. DR GO; GO:0016089; P:aromatic amino acid family biosynthetic pro...; IEA:HAMAP. DR HAMAP; MF_00214; -; 1. DR InterPro; IPR001381; DHquinase_I. DR Gene3D; G3DSA:3.20.20.250; DHquinase_I; 1. DR Pfam; PF01487; DHquinase_I; 1. DR ProDom; PD005337; DHquinase_I; 1. DR TIGRFAMs; TIGR01093; aroD; 1. DR PROSITE; PS01028; DEHYDROQUINASE_I; 1. KW Complete proteome; Lyase; Quinate metabolism; Schiff base. FT CHAIN 1 272 Catabolic 3-dehydroquinate dehydratase. FT /FTId=PRO_0000138842. FT ACT_SITE 163 163 Proton acceptor (By similarity). FT ACT_SITE 190 190 Schiff-base intermediate with substrate FT (By similarity). SQ SEQUENCE 272 AA; 29899 MW; 98646DC5E88BF6D3 CRC64; MSLPILSTTY AAENTVPASK STYVVKNLNI GDLPVKTLVP ITAKTREQAL AQAKVIAENK DADIAEFRID LLEFASDTKK VIALGQELNQ ILKDKPLLAT IRTSNEGGKL KVTDQEYEKI YSEYLKKPFM QLLDIEMFRD QAAVAKLTKL AHQKKVLVVM SNHDFDKTPS EQEIVSRLLK QDQMGADILK IAVMPKSKQD VFTLMNATLK VSEQSTKPLL TMSMGRLGTI SRIATANMGG SLSFGMIGEA SAPGQIDVTA LKQFLKTVQP TP // ID 3DHQ_EMENI Reviewed; 153 AA. AC P05147; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 2. DT 28-NOV-2006, entry version 46. DE Catabolic 3-dehydroquinase (EC 4.2.1.10) (3-dehydroquinate DE dehydratase). GN Name=qutE; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89181521; PubMed=2976880; RA Hawkins A.R., Lamb H.K., Smith M., Keyte J.W., Roberts C.F.; RT "Molecular organisation of the quinic acid utilization (QUT) gene RT cluster in Aspergillus nidulans."; RL Mol. Gen. Genet. 214:224-231(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=R153; RX MEDLINE=87127965; PubMed=2949740; RA da Silva A.J.F., Whittington H., Clements J., Roberts C.F., RA Hawkins A.R.; RT "Sequence analysis and transformation by the catabolic 3- RT dehydroquinase (QUTE) gene from Aspergillus nidulans."; RL Biochem. J. 240:481-488(1986). RN [3] RP SEQUENCE REVISION. RA Hawkins A.R.; RL Submitted (APR-1987) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is involved in the catabolism of quinate. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate CC biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1. CC -!- SUBUNIT: Homododecamer (Probable). CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X13525; CAA31881.1; -; Genomic_DNA. DR EMBL; X04696; CAA28401.1; -; Genomic_DNA. DR PIR; S08501; S08501. DR HSSP; P15474; 1GU1. DR InterPro; IPR001874; DHquinase_II. DR Gene3D; G3DSA:3.40.50.9100; DHquinase_II; 1. DR Pfam; PF01220; DHquinase_II; 1. DR ProDom; PD004527; DHquinase_II; 1. DR TIGRFAMs; TIGR01088; aroQ; 1. DR PROSITE; PS01029; DEHYDROQUINASE_II; 1. KW Lyase; Quinate metabolism. FT CHAIN 1 153 Catabolic 3-dehydroquinase. FT /FTId=PRO_0000159947. FT REGION 102 103 Substrate binding (By similarity). FT ACT_SITE 24 24 Proton acceptor (By similarity). FT ACT_SITE 101 101 Proton donor (By similarity). FT BINDING 75 75 Substrate (By similarity). FT BINDING 81 81 Substrate (By similarity). FT BINDING 88 88 Substrate (By similarity). FT BINDING 112 112 Substrate (By similarity). FT SITE 19 19 Transition state stabilizer (By FT similarity). FT CONFLICT 60 60 E -> D (in Ref. 2). SQ SEQUENCE 153 AA; 16517 MW; 9DACD00961799E46 CRC64; MEKSILLING PNLNLLGTRE PHIYGSTTLS DVEESSKGHA ASLGASLQTF QSNHEGAIVE RIHAARGNTD AIIINPGAYT HTSVAIRDAL LGVEIPFIEL HVSNVHAREP FRHHSYFSDK ASGIIVGLGV YGYKVAVEHV ALNFKPLEKK AAL // ID 3DHQ_NEUAF Reviewed; 168 AA. AC Q58HK4; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 28-NOV-2006, entry version 7. DE Catabolic 3-dehydroquinase (EC 4.2.1.10) (3-dehydroquinate DE dehydratase). GN Name=qa-2; OS Neurospora africana. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=5143; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Arnett D.R., Shevchuk J.A., Asch D.K.; RT "Comparative sequencing of the qa-2 gene of Neurospora africana."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is involved in the catabolism of quinate (By CC similarity). CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate CC biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1. CC -!- SUBUNIT: Homododecamer (Probable). CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY948979; AAX51222.1; -; Genomic_DNA. DR InterPro; IPR002110; ANK. DR InterPro; IPR001874; DHquinase_II. DR Gene3D; G3DSA:3.40.50.9100; DHquinase_II; 1. DR Pfam; PF01220; DHquinase_II; 1. DR PRINTS; PR01415; ANKYRIN. DR ProDom; PD004527; DHquinase_II; 1. DR TIGRFAMs; TIGR01088; aroQ; 1. DR PROSITE; PS01029; DEHYDROQUINASE_II; 1. KW Lyase; Quinate metabolism. FT CHAIN 1 168 Catabolic 3-dehydroquinase. FT /FTId=PRO_0000260167. FT REGION 124 125 Substrate binding (By similarity). FT ACT_SITE 26 26 Proton acceptor (By similarity). FT ACT_SITE 123 123 Proton donor (By similarity). FT BINDING 97 97 Substrate (By similarity). FT BINDING 103 103 Substrate (By similarity). FT BINDING 110 110 Substrate (By similarity). FT BINDING 134 134 Substrate (By similarity). FT SITE 21 21 Transition state stabilizer (By FT similarity). SQ SEQUENCE 168 AA; 17961 MW; BA8A8E88AD19E826 CRC64; MASRHHILLI NGPNLNLLGT REPQIYGSTT LHDIEQAAQT QASSLDLRLT TFQSNHEGAI IDRIHQAAGF FPSPSGPATI AEADPGAGEK VSAIIINPGA YTHTSVGIRD ALLGTGIPFV EVHVSNVHAR EAFRHHSYLS DKAVAVICGL GPYGYSAALE FVGRHMKF // ID 3DHQ_NEUCR Reviewed; 173 AA. AC P05195; Q7RVA3; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 2. DT 23-JAN-2007, entry version 56. DE Catabolic 3-dehydroquinase (EC 4.2.1.10) (3-dehydroquinate DE dehydratase). GN Name=qa-2; ORFNames=NCU06023; OS Neurospora crassa. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=5141; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX MEDLINE=89293848; PubMed=2525625; RA Geever R.F., Huiet L., Baum J.A., Tyler B.M., Patel V.B., RA Rutledge B.J., Case M.E., Giles N.H.; RT "DNA sequence, organization and regulation of the qa gene cluster of RT Neurospora crassa."; RL J. Mol. Biol. 207:15-34(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554; RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., RA Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., RA Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., RA Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., RA Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., RA Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., RA Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., RA Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., RA Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.; RT "The genome sequence of the filamentous fungus Neurospora crassa."; RL Nature 422:859-868(2003). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-124. RX MEDLINE=82197615; PubMed=6210913; RA Alton N.K., Buxton F., Patel V., Giles N.H., Vapnek D.; RT "5'-Untranslated sequences of two structural genes in the qa gene RT cluster of Neurospora crassa."; RL Proc. Natl. Acad. Sci. U.S.A. 79:1955-1959(1982). CC -!- FUNCTION: Is involved in the catabolism of quinate. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate CC biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1. CC -!- SUBUNIT: Homododecamer (Probable). CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14603; CAA32749.1; -; Genomic_DNA. DR EMBL; V00869; CAA24237.1; -; Genomic_DNA. DR EMBL; AABX01000367; EAA30377.1; -; Genomic_DNA. DR PIR; S04251; A31277. DR HSSP; P15474; 1GU1. DR BioCyc; NCRA-XX3-01:NCRA-XX3-01-009771-MONOMER; -. DR InterPro; IPR001874; DHquinase_II. DR Gene3D; G3DSA:3.40.50.9100; DHquinase_II; 1. DR Pfam; PF01220; DHquinase_II; 1. DR ProDom; PD004527; DHquinase_II; 1. DR TIGRFAMs; TIGR01088; aroQ; 1. DR PROSITE; PS01029; DEHYDROQUINASE_II; 1. KW Lyase; Quinate metabolism. FT CHAIN 1 173 Catabolic 3-dehydroquinase. FT /FTId=PRO_0000159948. FT REGION 129 130 Substrate binding (By similarity). FT ACT_SITE 26 26 Proton acceptor (By similarity). FT ACT_SITE 128 128 Proton donor (By similarity). FT BINDING 102 102 Substrate (By similarity). FT BINDING 108 108 Substrate (By similarity). FT BINDING 115 115 Substrate (By similarity). FT BINDING 139 139 Substrate (By similarity). FT SITE 21 21 Transition state stabilizer (By FT similarity). FT CONFLICT 25 29 IYGST -> STAQS (in Ref. 3). SQ SEQUENCE 173 AA; 18272 MW; 6A6EC7594DD46F1B CRC64; MASPRHILLI NGPNLNLLGT REPQIYGSTT LHDIEQASQT LASSLGLRLT TFQSNHEGAI IDRIHQAAGF VPSPPSPSPS SAATTTEAGL GPGDKVSAII INPGAYTHTS IGIRDALLGT GIPFVEVHVS NVHAREAFRH HSYLSDKAVA VICGLGPFGY SAALDFLGRH MKF // ID 3F_DICDI Reviewed; 215 AA. AC P13475; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 20-FEB-2007, entry version 38. DE Protein 3F precursor (Fragment). GN Name=pspG; Synonyms=3F; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=AX2; RX MEDLINE=90045966; PubMed=2813070; DOI=10.1093/nar/17.20.8374; RA Widdowson D.C.C., Jagger P.S., Hames B.D.; RT "Nucleotide sequence of a late developmentally regulated prespore- RT enriched Dictyostelium discoideum gene."; RL Nucleic Acids Res. 17:8374-8374(1989). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X16124; CAA34255.1; -; mRNA. DR PIR; S06595; S06595. DR DictyBase; DDB0001894; pspG. DR InterPro; IPR008972; Cupredoxin. KW Glycoprotein; Repeat; Signal. FT SIGNAL 1 19 Potential. FT CHAIN 20 >215 Protein 3F. FT /FTId=PRO_0000020577. FT REPEAT 145 153 1. FT REPEAT 154 162 2. FT REPEAT 163 171 3. FT REPEAT 172 176 4; truncated. FT REGION 145 176 3.5 X 9 AA tandem repeats of S-P-K-[ST]- FT D-A-K-E-A. FT CARBOHYD 52 52 N-linked (GlcNAc...) (Potential). FT NON_TER 215 215 SQ SEQUENCE 215 AA; 23355 MW; 4D8C16A1B6990F66 CRC64; MKLLSKLILT LALATYASAS ENFRYINWDN PPHDVTFYEG DVLQFTTNEG RNSTITLISD TENGDKSFDG VLNEDQRSFV QKALPPGRYT FKDLNSGSKS IIRVKESKEL AKEVRPIDRL KDNADAANTE NAQKSPNTQS TQKGSPKSDA KEASPKTDAK EASPKSDAKE ASPKTDTKQG SSPKTDTKSS TQKPSSSSDS SKAKAEANTA ANNEE // ID 3HAO_ASHGO Reviewed; 180 AA. AC Q75CP6; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 27. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN Name=BNA1; OrderedLocusNames=ACL127W; OS Ashbya gossypii (Yeast) (Eremothecium gossypii). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=33169; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient RT Saccharomyces cerevisiae genome."; RL Science 304:304-307(2004). 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; pyridine-2,3- CC dicarboxylate from L-kynurenine: step 3. 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; AE016816; AAS51101.1; -; Genomic_DNA. DR AGD; ACL127W; -. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 180 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000245471. FT METAL 49 49 Iron (catalytic) (By similarity). FT METAL 55 55 Iron (catalytic) (By similarity). FT METAL 98 98 Iron (catalytic) (By similarity). FT METAL 127 127 Divalent metal cation (structural) (By FT similarity). FT METAL 130 130 Divalent metal cation (structural) (By FT similarity). FT METAL 164 164 Divalent metal cation (structural) (By FT similarity). FT METAL 167 167 Divalent metal cation (structural) (By FT similarity). FT BINDING 45 45 Dioxygen (By similarity). FT BINDING 55 55 Substrate (By similarity). FT BINDING 102 102 Substrate (By similarity). FT BINDING 112 112 Substrate (By similarity). SQ SEQUENCE 180 AA; 20378 MW; 24B84FC51F52BA85 CRC64; MLNTTPINID AWLAENSHLL QPPVNNFCLH RGGFTVMLVG GPNERTDYHV NPTPEWFYQK TGAMTLRIVD EQLSGAARFR DVTIREGDSF LLPANVPHNP VRYADTVGIV VEQDRPAGHF DQLRWYCRGC RELVCKYEFY MSDLSSQVRE GIERFAASAE DRVCKHCGTL NYPTPQASAT // ID 3HAO_BACC1 Reviewed; 179 AA. AC Q739J0; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 23. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=BCE_2151; OS Bacillus cereus (strain ATCC 10987). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=222523; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14960714; DOI=10.1093/nar/gkh258; RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.; RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic RT adaptations and a large plasmid related to Bacillus anthracis pXO1."; RL Nucleic Acids Res. 32:977-988(2004). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; AE017194; AAS41072.1; -; Genomic_DNA. DR GenomeReviews; AE017194_GR; BCE_2151. DR KEGG; bca:BCE_2151; -. DR TIGR; BCE_2151; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 179 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245473. FT METAL 51 51 Iron (catalytic) (By similarity). FT METAL 57 57 Iron (catalytic) (By similarity). FT METAL 96 96 Iron (catalytic) (By similarity). FT METAL 125 125 Divalent metal cation (structural) (By FT similarity). FT METAL 128 128 Divalent metal cation (structural) (By FT similarity). FT METAL 162 162 Divalent metal cation (structural) (By FT similarity). FT METAL 165 165 Divalent metal cation (structural) (By FT similarity). FT BINDING 47 47 Dioxygen (By similarity). FT BINDING 57 57 Substrate (By similarity). FT BINDING 100 100 Substrate (By similarity). FT BINDING 110 110 Substrate (By similarity). SQ SEQUENCE 179 AA; 21084 MW; 1A4A10AA8AC192AC CRC64; MSKTLQSFNL LKWIDENKEL LKPPVNNKVI WQDSEFIAMI LGGPNRRRDF HVDPSDEFFY QIKGECYVEC ITEEGKREVV TVKEGDVFML PAMVPHSPHR VANTYGLVIE RKRNQGELED FVWFCDECNH EMHRVRVQLS DIEKQVKEAI HSFNSNKEIR ACKNCGHIMP EEVEEWKCE // ID 3HAO_BRARE Reviewed; 287 AA. AC Q5U3F8; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 20-FEB-2007, entry version 21. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN Name=haao; ORFNames=zgc:103585; OS Brachydanio rerio (Zebrafish) (Danio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. 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; pyridine-2,3- CC dicarboxylate from L-kynurenine: step 3. 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; BC085560; AAH85560.1; -; mRNA. DR UniGene; Dr.37102; -. DR Ensembl; ENSDARG00000005928; Danio rerio. DR ZFIN; ZDB-GENE-041114-89; zgc:103585. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 287 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000245466. FT METAL 50 50 Iron (catalytic) (By similarity). FT METAL 56 56 Iron (catalytic) (By similarity). FT METAL 94 94 Iron (catalytic) (By similarity). FT BINDING 46 46 Dioxygen (By similarity). FT BINDING 56 56 Substrate (By similarity). FT BINDING 98 98 Substrate (By similarity). FT BINDING 108 108 Substrate (By similarity). SQ SEQUENCE 287 AA; 33239 MW; A5A2B050B823F038 CRC64; MTNQSLHVNI DKWIAENETS FLPPVCNKLM FFYQLNIMYV GGPNVRKDYH IEEGEELFYQ VRGDMVLKVI ENGKHKDVHI REGEMFLLPA RIPHSPQRQA NTVGLVIERR RLSKETDGLR YFVANSTEVL FERWFYCENL GTQLVPIIKE FMDSKENETG KPDPANPIKP APYPLNTMNV MTPFSFREWV EKQKPVLASG CPVDMFGEQF ETETLLFGSG TSANKRRTDG WIWQLEGLSN VFMNGKEYSL TAGDCLLIFG ETEYKWQRSQ DCVALYVAQD PDRKRPY // ID 3HAO_BURS3 Reviewed; 174 AA. AC Q39LI1; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 2. DT 20-FEB-2007, entry version 15. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=Bcep18194_C7641; OS Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 OS / NCIB 9086 / R18194)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=269483; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of chromosome 3 of Burkholderia sp. 383."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; CP000150; ABB06685.1; ALT_INIT; Genomic_DNA. DR SMR; Q39LI1; 17-189. DR GenomeReviews; CP000150_GR; Bcep18194_C7641. DR KEGG; bur:Bcep18194_C7641; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Gene3D; G3DSA:2.60.120.10; G3DSA:2.60.120.10; 1. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 174 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245474. FT METAL 51 51 Iron (catalytic) (By similarity). FT METAL 57 57 Iron (catalytic) (By similarity). FT METAL 95 95 Iron (catalytic) (By similarity). FT METAL 125 125 Divalent metal cation (structural) (By FT similarity). FT METAL 128 128 Divalent metal cation (structural) (By FT similarity). FT METAL 162 162 Divalent metal cation (structural) (By FT similarity). FT METAL 165 165 Divalent metal cation (structural) (By FT similarity). FT BINDING 47 47 Dioxygen (By similarity). FT BINDING 57 57 Substrate (By similarity). FT BINDING 99 99 Substrate (By similarity). FT BINDING 110 110 Substrate (By similarity). SQ SEQUENCE 174 AA; 20048 MW; FB19D9C29561A99B CRC64; MLKYGTPFNF SRWIDEHAHL LKPPVGNQQV WQDSDFIVTV VGGPNHRTDY HDDPFEEFFY QLRGNAYLHL WIDGKRERVD LKEGDMFLLP PHVRHSPQRP EAGSACLVIE RQRPAGVVDG FEWYCDACGH LVHRVEVQLK SIVDDLPPLF DAFYASDTLR RCAHCGHMHP GKAT // ID 3HAO_CAEBR Reviewed; 280 AA. AC Q60W34; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 20-FEB-2007, entry version 17. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN ORFNames=CBG19288; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6238; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., RA D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., RA Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R., RA Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., RA Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., RA Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R., RA Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for RT comparative genomics."; RL PLoS Biol. 1:166-192(2003). 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; pyridine-2,3- CC dicarboxylate from L-kynurenine: step 3. 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; CAAC01000098; CAE72181.1; -; Genomic_DNA. DR WormBase; WBGene00038535; CBG19288. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 280 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000245469. FT METAL 49 49 Iron (catalytic) (By similarity). FT METAL 55 55 Iron (catalytic) (By similarity). FT METAL 93 93 Iron (catalytic) (By similarity). FT BINDING 45 45 Dioxygen (By similarity). FT BINDING 55 55 Substrate (By similarity). FT BINDING 97 97 Substrate (By similarity). FT BINDING 107 107 Substrate (By similarity). SQ SEQUENCE 280 AA; 31987 MW; 601B8DC727C9FDC0 CRC64; MAGVTAIEIP QWIQDNQGDF VPPVCNKCMF SDQLKVFYVG GPNQRKDFHL EEGEEFFFQR KGDMVLKVIE KGQVRDLVIK QGEMFMLPAR VEHSPQRFAN SIGLVVERER KNTEFDCVRF LVGSSNVTLF ERWFFLTDVV KDLPPLIKEF YNSNEFKTGK PGKGTFACNA PYEARWTDLP VPINRKEFIY DHISEVKNGP VKIYGAPEYK TEVMLLGEGS YDLEAGAVEL IIWLQENTFA VVEESGFTYA LKSETMVRIK PNTKCLLNVK GGFAITIRMP // ID 3HAO_CAEEL Reviewed; 281 AA. AC Q19341; Q21258; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 2. DT 20-FEB-2007, entry version 44. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN ORFNames=K06A4.5; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). 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; pyridine-2,3- CC dicarboxylate from L-kynurenine: step 3. 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; Z70751; CAA94753.1; -; Genomic_DNA. DR EMBL; Z70755; CAA94753.1; JOINED; Genomic_DNA. DR EMBL; Z70755; CAA94787.1; -; Genomic_DNA. DR EMBL; Z70751; CAA94787.1; JOINED; Genomic_DNA. DR PIR; T20743; T20743. DR UniGene; Cel.3124; -. DR IntAct; Q19341; -. DR Ensembl; K06A4.5; Caenorhabditis elegans. DR KEGG; cel:K06A4.5; -. DR WormBase; WBGene00010595; K06A4.5. DR WormPep; K06A4.5; CE06109. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 281 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000245470. FT METAL 49 49 Iron (catalytic) (By similarity). FT METAL 55 55 Iron (catalytic) (By similarity). FT METAL 93 93 Iron (catalytic) (By similarity). FT BINDING 45 45 Dioxygen (By similarity). FT BINDING 55 55 Substrate (By similarity). FT BINDING 97 97 Substrate (By similarity). FT BINDING 107 107 Substrate (By similarity). SQ SEQUENCE 281 AA; 32227 MW; E3DD76D60D5930A9 CRC64; MSGVTAIEIP QWIQDNQEDF VPPVCNKCMF SDQLKVFYVG GPNQRKDFHL EEGEEFFFQR KGDMVLKVIE KGQVRDLVIK QGEMFMLPAR VEHSPQRFSN SIGLVVERER KNTEFDCVRF LVGSSNITLF ERWFYLTDVV KDLPPLIKEF YGSNEFKTGK PGKGTFACNA PYEARWTDLP VPINRKEFIY DHISEVKNGP VRIYGAPEYK TEVMLLGEGS YDLESGTVEL LIWLQENTFA VVEESGFTYA MKSETMVRIK PNTKCLLNVK GGFAITIRMP A // ID 3HAO_HUMAN Reviewed; 286 AA. AC P46952; Q53QZ7; Q8N6N9; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-FEB-2007, entry version 53. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN Name=HAAO; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94245687; PubMed=7514594; RA Malherbe P., Kohler C., da Prada M., Lang G., Kiefer V., Schwarcz R., RA Lahm H., Cesura A.M.; RT "Molecular cloning and functional expression of human 3- RT hydroxyanthranilic-acid dioxygenase."; RL J. Biol. Chem. 269:13792-13797(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-37. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-37. 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 synthesis of the excitotoxin quinolinic CC acid (QUIN) from 3-hydroxyanthranilic acid. The direct product of CC the reaction spontaneously rearrange to QUIN. CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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; Z29481; CAA82618.1; -; mRNA. DR EMBL; CR457063; CAG33344.1; -; mRNA. DR EMBL; AC098824; AAY14701.1; -; Genomic_DNA. DR EMBL; BC029510; AAH29510.1; -; mRNA. DR PIR; A54070; A54070. DR UniGene; Hs.368805; -. DR Ensembl; ENSG00000162882; Homo sapiens. DR KEGG; hsa:23498; -. DR H-InvDB; HIX0018978; -. DR HGNC; HGNC:4796; HAAO. DR MIM; 604521; gene. DR Reactome; REACT_13.1; Metabolism of amino acids and related nitrogen-containing molecules. DR LinkHub; P46952; -. DR ArrayExpress; P46952; -. DR GermOnline; ENSG00000162882; Homo sapiens. DR RZPD-ProtExp; C0601; -. DR RZPD-ProtExp; RZPDo834G0411; -. DR RZPD-ProtExp; RZPDo839F04125; -. DR RZPD-ProtExp; RZPDo839F04126; -. DR GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB. DR GO; GO:0008987; F:quinolinate synthetase A activity; TAS:ProtInc. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Polymorphism. FT CHAIN 1 286 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000064372. 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). FT VARIANT 37 37 V -> I (in dbSNP:rs3816183). FT /FTId=VAR_021507. FT VARIANT 42 42 T -> S (in dbSNP:rs3816182). FT /FTId=VAR_030470. SQ SEQUENCE 286 AA; 32542 MW; 4DA10F20FC635885 CRC64; MERRLGVRAW VKENRGSFQP PVCNKLMHQE QLKVMFVGGP NTRKDYHIEE GEEVFYQLEG DMVLRVLEQG KHRDVVIRQG EIFLLPARVP HSPQRFANTV GLVVERRRLE TELDGLRYYV GDTMDVLFEK WFYCKDLGTQ LAPIIQEFFS SEQYRTGKPI PDQLLKEPPF PLSTRSIMEP MSLDAWLDSH HRELQAGTPL SLFGDTYETQ VIAYGQGSSE GLRQNVDVWL WQLEGSSVVT MGGRRLSLAP DDSLLVLAGT SYAWERTQGS VALSVTQDPA CKKPLG // ID 3HAO_JANSC Reviewed; 180 AA. AC Q28SE8; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 1. DT 20-FEB-2007, entry version 8. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=Jann_1447; OS Jannaschia sp. (strain CCS1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=290400; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., RA Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., RA Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.; RT "Complete sequence of chromosome of Jannaschia sp. CCS1."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; CP000264; ABD54364.1; -; Genomic_DNA. DR GenomeReviews; CP000264_GR; Jann_1447. DR KEGG; jan:Jann_1447; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 180 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245475. FT METAL 50 50 Iron (catalytic) (By similarity). FT METAL 56 56 Iron (catalytic) (By similarity). FT METAL 94 94 Iron (catalytic) (By similarity). FT METAL 124 124 Divalent metal cation (structural) (By FT similarity). FT METAL 127 127 Divalent metal cation (structural) (By FT similarity). FT METAL 161 161 Divalent metal cation (structural) (By FT similarity). FT METAL 164 164 Divalent metal cation (structural) (By FT similarity). FT BINDING 46 46 Dioxygen (By similarity). FT BINDING 56 56 Substrate (By similarity). FT BINDING 98 98 Substrate (By similarity). FT BINDING 109 109 Substrate (By similarity). SQ SEQUENCE 180 AA; 20439 MW; 8D3A2D7DAE75842F CRC64; MARLSAFNFK AWIDEHRHLL KPPVGNKMVY EDADLMVTVV GGPNKRTDYH DDPVEEFFYQ LEGDMVLKLY DGEEFYDVPI REGEIFLLPP HMRHSPQRPQ EGSVGLVIEA KRPEGAADAI EWYCFNCGNL VHRAELMLTS IVDDLPPVYQ AFYASEEART CGSCGEVHPG KEPPEGWVTL // 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 20-FEB-2007, entry version 28. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). 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. 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: Catalyzes the synthesis of the excitotoxin quinolinic CC acid (QUIN) from 3-hydroxyanthranilic acid. The direct product of CC the reaction spontaneously rearrange to QUIN (By similarity). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (By similarity). 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 UniGene; Mm.30100; -. DR MGI; MGI:1349444; Haao. DR ArrayExpress; Q78JT3; -. DR GermOnline; ENSMUSG00000000673; Mus musculus. DR RZPD-ProtExp; IOM20267; -. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 286 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000064373. 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 3HAO_PSEFL Reviewed; 185 AA. AC Q83V26; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 20-FEB-2007, entry version 19. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN Name=nbaC; OS Pseudomonas fluorescens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=294; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=KU-7; RX MEDLINE=22507682; PubMed=12620844; RX DOI=10.1128/AEM.69.3.1564-1572.2003; RA Muraki T., Taki M., Hasegawa Y., Iwaki H., Lau P.C.K.; RT "Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4- RT dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase RT in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens RT strain KU-7."; RL Appl. Environ. Microbiol. 69:1564-1572(2003). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; AB088043; BAC65311.1; -; Genomic_DNA. DR SMR; Q83V26; 2-175. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 185 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000245472. FT METAL 52 52 Iron (catalytic) (By similarity). FT METAL 58 58 Iron (catalytic) (By similarity). FT METAL 96 96 Iron (catalytic) (By similarity). FT METAL 126 126 Divalent metal cation (structural) (By FT similarity). FT METAL 129 129 Divalent metal cation (structural) (By FT similarity). FT METAL 163 163 Divalent metal cation (structural) (By FT similarity). FT METAL 166 166 Divalent metal cation (structural) (By FT similarity). FT BINDING 48 48 Dioxygen (By similarity). FT BINDING 58 58 Substrate (By similarity). FT BINDING 100 100 Substrate (By similarity). FT BINDING 111 111 Substrate (By similarity). SQ SEQUENCE 185 AA; 21245 MW; AC932875CC9D3D7D CRC64; MMFTFGKPLN FQRWLDDHSD LLRPPVGNQQ VWQDSDFIVT VVGGPNFRTD FHDDPMEEFF YQFKGNAYLN IMDRGQMDRV ELKEGDIFLL PPHLRHSPQR PEAGSRCLVI ERQRPKGMLD GFEWYCLSCN GLVYRVDVQL NSIVTDLPPL FDIFYGNVGL RKCPQCGQVH PGKAAIEAVA RGDQP // ID 3HAO_RALEJ Reviewed; 189 AA. AC Q46PT7; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 20-FEB-2007, entry version 12. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=Reut_B5502; OS Ralstonia eutropha (strain JMP134) (Alcaligenes eutrophus). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=264198; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., RA Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.; RT "Complete sequence of chromosome 2 of Ralstonia eutropha JMP134."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; CP000091; AAZ64847.1; -; Genomic_DNA. DR SMR; Q46PT7; 4-175. DR GenomeReviews; CP000091_GR; Reut_B5502. DR KEGG; reu:Reut_B5502; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 189 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245476. FT METAL 53 53 Iron (catalytic) (By similarity). FT METAL 59 59 Iron (catalytic) (By similarity). FT METAL 97 97 Iron (catalytic) (By similarity). FT METAL 127 127 Divalent metal cation (structural) (By FT similarity). FT METAL 130 130 Divalent metal cation (structural) (By FT similarity). FT METAL 165 165 Divalent metal cation (structural) (By FT similarity). FT METAL 168 168 Divalent metal cation (structural) (By FT similarity). FT BINDING 49 49 Dioxygen (By similarity). FT BINDING 59 59 Substrate (By similarity). FT BINDING 101 101 Substrate (By similarity). FT BINDING 112 112 Substrate (By similarity). SQ SEQUENCE 189 AA; 21938 MW; F3EE0A8DCEEEB74E CRC64; MFDLKYGRPL NFKRWLDDHA DKLKPPVGNQ QIWQDSDMMV TVVGGPNERS DFHDDPIEEL FYQFKGNAYL LLWEDGRYER VDLREGDMLL LPPHTLHSPQ RPEADSRCLV VERKRPQGQN DAFQWSCASC GTIVQRHEVT LQSIVADLPP LYEKFYASSE DARRCPGCGE IHPGRDFQAW HRTLARHSS // ID 3HAO_RALME Reviewed; 174 AA. AC Q1LCS4; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 20-FEB-2007, entry version 7. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=Rmet_5193; OS Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839). OG Plasmid megaplasmid. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=266264; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Mergeay M., Benotmane M.A., RA Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., RA van der Lelie D., Richardson P.; RT "Complete sequence of the megaplasmid of Ralstonia metallidurans RT CH34."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND RP IRON, MUTAGENESIS OF ARG-47; ARG-99 AND GLU-110, AND SUBUNIT. RX PubMed=15909978; DOI=10.1021/bi047353l; RA Zhang Y., Colabroy K.L., Begley T.P., Ealick S.E.; RT "Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the RT catalytic mechanism of a complex oxidation involved in NAD RT biosynthesis."; RL Biochemistry 44:7632-7643(2005). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Binds 2 Fe(2+) ions per subunit. CC -!- SUBUNIT: Homodimer. 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; CP000353; ABF12052.1; -; Genomic_DNA. DR PDB; 1YFU; X-ray; A/B=1-174. DR PDB; 1YFW; X-ray; A/B=1-174. DR PDB; 1YFX; X-ray; A/B=1-174. DR PDB; 1YFY; X-ray; A/B=1-174. DR GenomeReviews; CP000353_GR; Rmet_5193. DR KEGG; rme:Rmet_5193; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW 3D-structure; Complete proteome; Dioxygenase; Iron; Metal-binding; KW Oxidoreductase; Plasmid. FT CHAIN 1 174 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000245477. FT METAL 51 51 Iron (catalytic). FT METAL 57 57 Iron (catalytic). FT METAL 95 95 Iron (catalytic). FT METAL 125 125 Iron (structural). FT METAL 128 128 Iron (structural). FT METAL 162 162 Iron (structural). FT METAL 165 165 Iron (structural). FT BINDING 47 47 Dioxygen. FT BINDING 57 57 Substrate. FT BINDING 99 99 Substrate. FT BINDING 110 110 Substrate. FT MUTAGEN 47 47 R->A: Increases Km for 3- FT hydroxyanthranilate 7-fold. Decreases FT activity 1000-fold. FT MUTAGEN 99 99 R->A: Increases Km for 3- FT hydroxyanthranilate 40-fold. Decreases FT activity 5000-fold. FT MUTAGEN 110 110 E->A: Decreases Km for 3- FT hydroxyanthranilate 2-fold. Decreases FT activity 2000-fold. SQ SEQUENCE 174 AA; 20028 MW; 385F2E3DEB3947B8 CRC64; MLTYGAPFNF PRWIDEHAHL LKPPVGNRQV WQDSDFIVTV VGGPNHRTDY HDDPLEEFFY QLRGNAYLNL WVDGRRERAD LKEGDIFLLP PHVRHSPQRP EAGSACLVIE RQRPAGMLDG FEWYCDACGH LVHRVEVQLK SIVTDLPPLF ESFYASEDKR RCPHCGQVHP GRAA // ID 3HAO_RAT Reviewed; 286 AA. AC P46953; P70474; Q5RKK0; Q64556; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 20-FEB-2007, entry version 46. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN Name=Haao; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX MEDLINE=96100955; PubMed=8541664; RA Nakagawa Y., Asai H., Mori H., Kitoh J., Nakano K.; RT "Increase in the level of mRNA for 3-hydroxyanthranilate 3,4- RT dioxygenase in brain of epilepsy-prone El mice."; RL Biosci. Biotechnol. Biochem. 59:2191-2192(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). RN [3] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] OF 44-236, AND PARTIAL PROTEIN RP SEQUENCE. RX MEDLINE=94245687; PubMed=7514594; RA Malherbe P., Kohler C., da Prada M., Lang G., Kiefer V., Schwarcz R., RA Lahm H., Cesura A.M.; RT "Molecular cloning and functional expression of human 3- RT hydroxyanthranilic-acid dioxygenase."; RL J. Biol. Chem. 269:13792-13797(1994). CC -!- FUNCTION: Catalyzes the synthesis of the excitotoxin quinolinic CC acid (QUIN) from 3-hydroxyanthranilic acid. The direct product of CC the reaction spontaneously rearrange to QUIN. CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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; D44494; BAA07937.1; -; mRNA. DR EMBL; BC085739; AAH85739.1; -; mRNA. DR EMBL; D28339; BAA21019.1; -; mRNA. DR UniGene; Rn.48675; -. DR Ensembl; ENSRNOG00000031263; Rattus norvegicus. DR KEGG; rno:56823; -. DR RGD; 71071; Haao. DR ArrayExpress; P46953; -. DR GermOnline; ENSRNOG00000031263; Rattus norvegicus. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR003313; AraC_bd. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Dioxygenase; Direct protein sequencing; Iron; Metal-binding; KW Oxidoreductase. FT CHAIN 1 286 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000064374. 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). FT CONFLICT 29 29 R -> Q (in Ref. 2). FT CONFLICT 44 44 K -> S (in Ref. 3). FT CONFLICT 199 199 S -> F (in Ref. 3). FT CONFLICT 204 204 G -> C (in Ref. 3). FT CONFLICT 214 214 H -> Y (in Ref. 3). FT CONFLICT 229 229 W -> P (in Ref. 3). SQ SEQUENCE 286 AA; 32582 MW; B4F535AD8949DAB7 CRC64; MERCVRVKSW VEENRASFQP PVCNKLMHRE QLKIMFVGGP NTRKDYHIEE GEEVFYQLEG DMVLRVLEQG EHRDVVIRQG EIFLLPARVP HSPQRFANTM GLVIERRRME TELDGLRYYV GDTEDVLFEK WFHCKDLGTQ LAPIIQEFFH SEQYRTGKPN PDQLLKEPPF PLSTRSVMEP MSLKAWLESH SRELQAGTSL SLFGDSYETQ VIAHGQGSSK GPRQDVDVWL WQLEGSSKVT MGGQCVALAP DDSLLVPAGF SYMWERAQGS VALSVTQDPA CKKPLG // ID 3HAO_SILPO Reviewed; 180 AA. AC Q5LSJ4; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 20-FEB-2007, entry version 14. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=SPO1774; OS Silicibacter pomeroyi. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Silicibacter. OX NCBI_TaxID=89184; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3; RX PubMed=15602564; DOI=10.1038/nature03170; RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., RA Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., RA Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A., RA Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., RA Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., RA Haft D.H., Selengut J., Ward N.; RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the RT marine environment."; RL Nature 432:910-913(2004). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; CP000031; AAV95053.1; -; Genomic_DNA. DR GenomeReviews; CP000031_GR; SPO1774. DR KEGG; sil:SPO1774; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 180 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245478. FT METAL 50 50 Iron (catalytic) (By similarity). FT METAL 56 56 Iron (catalytic) (By similarity). FT METAL 94 94 Iron (catalytic) (By similarity). FT METAL 124 124 Divalent metal cation (structural) (By FT similarity). FT METAL 127 127 Divalent metal cation (structural) (By FT similarity). FT METAL 161 161 Divalent metal cation (structural) (By FT similarity). FT METAL 164 164 Divalent metal cation (structural) (By FT similarity). FT BINDING 46 46 Dioxygen (By similarity). FT BINDING 56 56 Substrate (By similarity). FT BINDING 98 98 Substrate (By similarity). FT BINDING 109 109 Substrate (By similarity). SQ SEQUENCE 180 AA; 20575 MW; 53B08A94EFFE38BA CRC64; MARLSAFNFQ KWIDEHKHLL KPPVGNQQVW EDADLMVTVV GGPNKRTDYH DDPVEEFFYQ LKGDMVLKLY EGGEFYDVPI REGDIFLLPP HVRHSPQRPQ EGSIGLVIEP KRPEGAHDAI EWFCFGCGSL VHRAELLLES IVRDLPPVYQ AFYADEQART CPNCGEIHPG KEPPEGWVKL // ID 3HAO_XANAC Reviewed; 176 AA. AC Q8PM31; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 20-FEB-2007, entry version 25. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=XAC1603; OS Xanthomonas axonopodis pv. citri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=92829; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; AE011792; AAM36471.1; -; Genomic_DNA. DR GenomeReviews; AE008923_GR; XAC1603. DR KEGG; xac:XAC1603; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 176 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245479. FT METAL 48 48 Iron (catalytic) (By similarity). FT METAL 54 54 Iron (catalytic) (By similarity). FT METAL 92 92 Iron (catalytic) (By similarity). FT METAL 121 121 Divalent metal cation (structural) (By FT similarity). FT METAL 124 124 Divalent metal cation (structural) (By FT similarity). FT METAL 158 158 Divalent metal cation (structural) (By FT similarity). FT METAL 161 161 Divalent metal cation (structural) (By FT similarity). FT BINDING 44 44 Dioxygen (By similarity). FT BINDING 54 54 Substrate (By similarity). FT BINDING 96 96 Substrate (By similarity). FT BINDING 106 106 Substrate (By similarity). SQ SEQUENCE 176 AA; 20155 MW; FBDAA5A96755F310 CRC64; MLTPPINLHA WIEEHRHLLK PPVGNKCIQQ DGFIIMVVGG PNARTDYHYD EGPEWFFQLE GEMVLKVQDE GVARDIPIRA GEVFLLPPKV PHSPQRADGS IGLVIERERL PTEQDGLQWY CPQCNHKLYE AMFPLKNIET DFPPVFDRFY RSPALRTCSQ CGHLHPAPER YATVEG // ID 3HAO_XANC5 Reviewed; 176 AA. AC Q3BV37; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 20-FEB-2007, entry version 13. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=XCV1645; OS Xanthomonas campestris pv. vesicatoria (strain 85-10). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=316273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005; RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., RA Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., RA Bonas U., Bartels D., Kaiser O.; RT "Insights into genome plasticity and pathogenicity of the plant RT pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed RT by the complete genome sequence."; RL J. Bacteriol. 187:7254-7266(2005). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; AM039952; CAJ23322.1; -; Genomic_DNA. DR GenomeReviews; AM039952_GR; XCV1645. DR KEGG; xcv:XCV1645; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 176 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245480. FT METAL 48 48 Iron (catalytic) (By similarity). FT METAL 54 54 Iron (catalytic) (By similarity). FT METAL 92 92 Iron (catalytic) (By similarity). FT METAL 121 121 Divalent metal cation (structural) (By FT similarity). FT METAL 124 124 Divalent metal cation (structural) (By FT similarity). FT METAL 158 158 Divalent metal cation (structural) (By FT similarity). FT METAL 161 161 Divalent metal cation (structural) (By FT similarity). FT BINDING 44 44 Dioxygen (By similarity). FT BINDING 54 54 Substrate (By similarity). FT BINDING 96 96 Substrate (By similarity). FT BINDING 106 106 Substrate (By similarity). SQ SEQUENCE 176 AA; 20210 MW; F9638C9EA4618289 CRC64; MLIPPINLHA WIEEHRHLLK PPVGNKCIQQ DGFIIMVVGG PNARTDYHYD EGPEWFFQLE GEMVLKVQDE GVARDIPIRA GEVFLLPPKV PHSPQRAAGS IGLVIERERL PNEQDGLQWY CPQCNHKLYE AMFPLKNIET DFPPVFDRFY RSLALRTCSQ CGHLHPAPER YATVED // ID 3HAO_XANC8 Reviewed; 176 AA. AC Q4UT95; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 20-FEB-2007, entry version 13. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=XC_2679; OS Xanthomonas campestris pv. campestris (strain 8004). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=314565; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15899963; DOI=10.1101/gr.3378705; RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., RA Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., RA Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.; RT "Comparative and functional genomic analyses of the pathogenicity of RT phytopathogen Xanthomonas campestris pv. campestris."; RL Genome Res. 15:757-767(2005). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; CP000050; AAY49728.1; -; Genomic_DNA. DR GenomeReviews; CP000050_GR; XC_2679. DR KEGG; xcb:XC_2679; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 176 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245481. FT METAL 48 48 Iron (catalytic) (By similarity). FT METAL 54 54 Iron (catalytic) (By similarity). FT METAL 92 92 Iron (catalytic) (By similarity). FT METAL 121 121 Divalent metal cation (structural) (By FT similarity). FT METAL 124 124 Divalent metal cation (structural) (By FT similarity). FT METAL 158 158 Divalent metal cation (structural) (By FT similarity). FT METAL 161 161 Divalent metal cation (structural) (By FT similarity). FT BINDING 44 44 Dioxygen (By similarity). FT BINDING 54 54 Substrate (By similarity). FT BINDING 96 96 Substrate (By similarity). FT BINDING 106 106 Substrate (By similarity). SQ SEQUENCE 176 AA; 20128 MW; 3C2FDD218C8458D4 CRC64; MLVPPINLHA WVEQHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE GEMVLKVQDD GTARDIPIRA GEIFLLPPKV PHSPQRAAGS IGLVIERERL PHEQDGLQWY CPQCNHKLYE AMFPLENIET DFPPVFDHFY RSLALRTCTQ CGHVHPAPER YAAVEA // ID 3HAO_XANCP Reviewed; 176 AA. AC Q8PAD0; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 20-FEB-2007, entry version 25. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=XCC1555; OS Xanthomonas campestris pv. campestris. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=340; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / NCPPB 528 / LMG 568; RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; AE012256; AAM40850.1; -; Genomic_DNA. DR GenomeReviews; AE008922_GR; XCC1555. DR KEGG; xcc:XCC1555; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 176 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245482. FT METAL 48 48 Iron (catalytic) (By similarity). FT METAL 54 54 Iron (catalytic) (By similarity). FT METAL 92 92 Iron (catalytic) (By similarity). FT METAL 121 121 Divalent metal cation (structural) (By FT similarity). FT METAL 124 124 Divalent metal cation (structural) (By FT similarity). FT METAL 158 158 Divalent metal cation (structural) (By FT similarity). FT METAL 161 161 Divalent metal cation (structural) (By FT similarity). FT BINDING 44 44 Dioxygen (By similarity). FT BINDING 54 54 Substrate (By similarity). FT BINDING 96 96 Substrate (By similarity). FT BINDING 106 106 Substrate (By similarity). SQ SEQUENCE 176 AA; 20128 MW; 3C2FDD218C8458D4 CRC64; MLVPPINLHA WVEQHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE GEMVLKVQDD GTARDIPIRA GEIFLLPPKV PHSPQRAAGS IGLVIERERL PHEQDGLQWY CPQCNHKLYE AMFPLENIET DFPPVFDHFY RSLALRTCTQ CGHVHPAPER YAAVEA // ID 3HAO_XANOM Reviewed; 176 AA. AC Q2P320; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 2. DT 20-FEB-2007, entry version 13. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=XOO2302; OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=342109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.; RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests RT contribution of large numbers of effector genes and insertion RT sequences to its race diversity."; RL Jpn. Agric. Res. Q. 39:275-287(2005). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; AP008229; BAE69057.1; ALT_INIT; Genomic_DNA. DR GenomeReviews; AP008229_GR; XOO2302. DR KEGG; xom:XOO_2302; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Gene3D; G3DSA:2.60.120.10; G3DSA:2.60.120.10; 1. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 176 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245483. FT METAL 48 48 Iron (catalytic) (By similarity). FT METAL 54 54 Iron (catalytic) (By similarity). FT METAL 92 92 Iron (catalytic) (By similarity). FT METAL 121 121 Divalent metal cation (structural) (By FT similarity). FT METAL 124 124 Divalent metal cation (structural) (By FT similarity). FT METAL 158 158 Divalent metal cation (structural) (By FT similarity). FT METAL 161 161 Divalent metal cation (structural) (By FT similarity). FT BINDING 44 44 Dioxygen (By similarity). FT BINDING 54 54 Substrate (By similarity). FT BINDING 96 96 Substrate (By similarity). FT BINDING 106 106 Substrate (By similarity). SQ SEQUENCE 176 AA; 20196 MW; 4274767A24F2B088 CRC64; MLIPPINLHA WIEEHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE GEMVLKVQDD GVARDIPIRA GEIFLLPPRV PHSPQRAAGS IGIVIERVRL PHEQDGLQWY CPQCNHKLYE AMFPLKNIET DFPPVFDHFY RSLALRTCSQ CGHLHPAPER YAAVED // ID 3HAO_XANOR Reviewed; 176 AA. AC Q5H043; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 2. DT 20-FEB-2007, entry version 16. DE Probable 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) DE (3-hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN OrderedLocusNames=XOO2424; OS Xanthomonas oryzae pv. oryzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=64187; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC10331 / KXO85; RX PubMed=15673718; DOI=10.1093/nar/gki206; RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S., RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H., RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S., RA Go S.-J.; RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, RT the bacterial blight pathogen of rice."; RL Nucleic Acids Res. 33:577-586(2005). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (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; AE013598; AAW75678.1; ALT_INIT; Genomic_DNA. DR GenomeReviews; AE013598_GR; XOO2424. DR KEGG; xoo:XOO2424; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:HAMAP. DR HAMAP; MF_00825; -; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Gene3D; G3DSA:2.60.120.10; G3DSA:2.60.120.10; 1. DR Pfam; PF06052; 3-HAO; 1. KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 176 Probable 3-hydroxyanthranilate 3,4- FT dioxygenase. FT /FTId=PRO_0000245484. FT METAL 48 48 Iron (catalytic) (By similarity). FT METAL 54 54 Iron (catalytic) (By similarity). FT METAL 92 92 Iron (catalytic) (By similarity). FT METAL 121 121 Divalent metal cation (structural) (By FT similarity). FT METAL 124 124 Divalent metal cation (structural) (By FT similarity). FT METAL 158 158 Divalent metal cation (structural) (By FT similarity). FT METAL 161 161 Divalent metal cation (structural) (By FT similarity). FT BINDING 44 44 Dioxygen (By similarity). FT BINDING 54 54 Substrate (By similarity). FT BINDING 96 96 Substrate (By similarity). FT BINDING 106 106 Substrate (By similarity). SQ SEQUENCE 176 AA; 20196 MW; 4274767A24F2B088 CRC64; MLIPPINLHA WIEEHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE GEMVLKVQDD GVARDIPIRA GEIFLLPPRV PHSPQRAAGS IGIVIERVRL PHEQDGLQWY CPQCNHKLYE AMFPLKNIET DFPPVFDHFY RSLALRTCSQ CGHLHPAPER YAAVED // ID 3HAO_XENLA Reviewed; 282 AA. AC Q6P7I0; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 21. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN Name=haao; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases. 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; pyridine-2,3- CC dicarboxylate from L-kynurenine: step 3. 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; BC061663; AAH61663.1; -; mRNA. DR UniGene; Xl.34491; -. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 282 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000245467. 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 282 AA; 32450 MW; BF4A6DA45A9BF420 CRC64; MAMAINVKKW IEENTEYFLP PVCNKLMHNQ QLKVMFVGGP NQRKDYHIEE GEELFYQVEG DMCLKIVENG KHKDVHIKQG EMFLLPGRIP HSPQRYADTV GLVFERRRLD TEKDGLRFYV EGSPEVLFEQ WFYCEDLGTQ LAPIMKEFFS SKQYKSGKPD PDQPKAKMPF CLSTEQVMEP FSFQHWLNKH RLEIIQKKCV SLFGDDHETK AVIYGGGESK QSKAQTDVWI WQLEGTSHVT LGNEVLKLGS GDSLLVPEET LFSWTREDGS IALSTSQVPL PM // ID 3HAO_XENTR Reviewed; 280 AA. AC Q6DIZ0; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 20-FEB-2007, entry version 22. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate DE oxygenase). GN Name=haao; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. 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; pyridine-2,3- CC dicarboxylate from L-kynurenine: step 3. 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; BC075395; AAH75395.1; -; mRNA. DR UniGene; Str.24494; -. DR Ensembl; ENSXETG00000015771; Xenopus tropicalis. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 280 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000245468. 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 280 AA; 32335 MW; 4E679AB7C625FA97 CRC64; MAIPVNVKKW IDENREYFLP PVCNKLMQNH QLKVMFVGGP NQRKDYHIEE GEELFYQVQG DMCLKIVENG KHKDVHIKEG EMFLLPGRIP HSPQRYADTV GLVFERRRLD TEKDGLRYYV EGTTEVLFEK WFYCEDLGTQ LAPIMKEFFS SEQYKSGKPD PAQPIGKMPF FLNTEQVMEP FSFQNWLNKH RLEINQKKRV SLFGHNQETK AVVYGSGESK DSKAQTDTWI WQLEGTSCVT LGNEVLKLGS GDSLLIPEKS LYSWIREDCS IALSTSQVPA // ID 3HAO_YEAST Reviewed; 177 AA. AC P47096; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 20-FEB-2007, entry version 52. DE 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-HAO) (3- DE hydroxyanthranilic acid dioxygenase) (3-hydroxyanthranilate oxygenase) DE (Biosynthesis of nicotinic acid protein 1). GN Name=BNA1; Synonyms=HAD1; OrderedLocusNames=YJR025C; ORFNames=J1550; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96109930; PubMed=8619316; DOI=10.1002/yea.320111208; RA Zagulski M., Babinska B., Gromadka R., Migdalski A., Rytka J., RA Sulicka J., Herbert C.J.; RT "The sequence of 24.3 kb from chromosome X reveals five complete open RT reading frames, all of which correspond to new genes, and a tandem RT insertion of a Ty1 transposon."; RL Yeast 11:1179-1186(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=96208490; PubMed=8641269; RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., RA Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., RA Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., RA Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., RA Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., RA Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., RA Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., RA Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., RA Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., RA Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., RA Zollner A., Karpfinger-Hartl L.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT X."; RL EMBO J. 15:2031-2049(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RA Marsischky G., Rolfs A., Richardson A., Kane M., Baqui M., Taycher E., RA Hu Y., Vannberg F., Weger J., Kramer J., Moreira D., Kelley F., RA Zuo D., Raphael J., Hogle C., Jepson D., Williamson J., Camargo A., RA Gonzaga L., Vasconcelos A.T., Simpson A., Kolodner R., Harlow E., RA LaBaer J.; RT "Creation of the YFLEX clone resource: cloning of Saccharomyces RT cerevisiae ORFs in the Gateway recombinational cloning system."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP CATALYTIC ACTIVITY, AND PATHWAY. RX MEDLINE=98198537; PubMed=9539135; DOI=10.1016/S0014-5793(98)00153-7; RA Kucharczyk R., Zagulski M., Rytka J., Herbert C.J.; RT "The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid RT dioxygenase and is involved in nicotinic acid biosynthesis."; RL FEBS Lett. 424:127-130(1998). RN [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASS RP SPECTROMETRY. RX PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., RA Mann M., Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone RT signaling pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-175 IN COMPLEX WITH RP DIVALENT METAL IONS, AND SUBUNIT. RX PubMed=16522801; DOI=10.1110/ps.051967906; RA Li X., Guo M., Fan J., Tang W., Wang D., Ge H., Rong H., Teng M., RA Niu L., Liu Q., Hao Q.; RT "Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from RT Saccharomyces cerevisiae: a special subgroup of the type III extradiol RT dioxygenases."; RL Protein Sci. 15:761-773(2006). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; pyridine-2,3- CC dicarboxylate from L-kynurenine: step 3. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- MISCELLANEOUS: Present with 2330 molecules/cell. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z49525; CAA89550.1; -; Genomic_DNA. DR EMBL; X87297; CAA60720.1; -; Genomic_DNA. DR EMBL; AY558309; AAS56635.1; -; Genomic_DNA. DR PIR; S57043; S57043. DR PDB; 1ZVF; X-ray; A/B=1-175. DR DIP; DIP:4759N; -. DR Ensembl; YJR025C; Saccharomyces cerevisiae. DR GenomeReviews; Y13136_GR; YJR025C. DR KEGG; sce:YJR025C; -. DR CYGD; YJR025c; -. DR SGD; S000003786; BNA1. DR BioCyc; MetaCyc:MONOMER-8161; -. DR BioCyc; SCER-S28-01:SCER-S28-01-003334-MONOMER; -. DR LinkHub; P47096; -. DR GermOnline; YJR025C; Saccharomyces cerevisiae. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IDA:SGD. DR GO; GO:0009435; P:NAD biosynthetic process; IMP:SGD. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR011051; Cupin_RmlC_type. DR Pfam; PF06052; 3-HAO; 1. KW 3D-structure; Complete proteome; Dioxygenase; Iron; Metal-binding; KW Nuclear protein; Oxidoreductase; Phosphorylation. FT CHAIN 1 177 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000064375. FT METAL 49 49 Iron (catalytic). FT METAL 55 55 Iron (catalytic). FT METAL 97 97 Iron (catalytic). FT METAL 126 126 Divalent metal cation (structural). FT METAL 129 129 Divalent metal cation (structural). FT METAL 163 163 Divalent metal cation (structural). FT METAL 166 166 Divalent metal cation (structural). FT BINDING 45 45 Dioxygen (By similarity). FT BINDING 55 55 Substrate (By similarity). FT BINDING 101 101 Substrate (By similarity). FT BINDING 111 111 Substrate (By similarity). FT MOD_RES 176 176 Phosphoserine. FT HELIX 9 16 FT HELIX 17 20 FT STRAND 21 24 FT STRAND 26 30 FT STRAND 32 39 FT STRAND 41 43 FT STRAND 48 50 FT STRAND 55 62 FT STRAND 64 70 FT STRAND 72 75 FT STRAND 77 83 FT TURN 85 86 FT STRAND 87 91 FT TURN 93 94 FT STRAND 97 101 FT TURN 103 104 FT STRAND 106 112 FT STRAND 116 118 FT STRAND 121 125 FT TURN 127 129 FT STRAND 132 137 FT STRAND 140 142 FT TURN 143 144 FT HELIX 145 155 FT TURN 156 156 FT HELIX 158 161 FT TURN 164 166 SQ SEQUENCE 177 AA; 20235 MW; 930D69F486632417 CRC64; MFNTTPINID KWLKENEGLL KPPVNNYCLH KGGFTVMIVG GPNERTGYHI NPTPEWFYQK KGSMLLKVVD ETDAEPKFID IIINEGDSYL LPGNVPHSPV RFADTVGIVV EQDRPGGEND KIRWYCSHCR QVVHESELQM LDLGTQVKEA ILDFENDVEK RTCFHCKTLN YARPQSN // ID 3HIDH_ARATH Reviewed; 347 AA. AC Q9SUC0; Q8LC25; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 30-APR-2003, sequence version 3. DT 23-JAN-2007, entry version 46. DE Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial precursor DE (EC 1.1.1.31) (HIBADH). GN OrderedLocusNames=At4g20930; ORFNames=T13K14.90; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 3-hydroxy-2-methylpropanoate + NAD(+) = 2- CC methyl-3-oxopropanoate + NADH. CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the 3-hydroxyisobutyrate dehydrogenase CC family. CC -!- CAUTION: Ref.1 sequences differ from that shown due to erroneous CC 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; AL080282; CAB45888.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161554; CAB79093.1; ALT_SEQ; Genomic_DNA. DR EMBL; AY086845; AAM63893.1; -; mRNA. DR UniGene; At.32684; -. DR GenomeReviews; CT486007_GR; AT4G20930. DR KEGG; ath:At4g20930; -. DR TAIR; At4g20930; -. DR ArrayExpress; Q9SUC0; -. DR GermOnline; AT4G20930; Arabidopsis thaliana. DR InterPro; IPR011548; 3hydroxisobut_dh. DR InterPro; IPR002204; 3hydroxy_acid_DH. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006115; 6PGD_NAD_bd. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000103; 3hydroxyisobu_dh; 1. DR TIGRFAMs; TIGR01692; HIBADH; 1. DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1. KW Mitochondrion; NAD; Oxidoreductase; Transit peptide. FT TRANSIT 1 34 Mitochondrion (By similarity). FT CHAIN 35 347 Probable 3-hydroxyisobutyrate FT dehydrogenase. FT /FTId=PRO_0000007162. FT NP_BIND 38 66 NAD (Potential). FT ACT_SITE 219 219 By similarity. FT CONFLICT 21 21 S -> F (in Ref. 2). SQ SEQUENCE 347 AA; 37365 MW; 6ED2E87CC3DE191C CRC64; MAIRRAQTLL CLSKFKTNFV SGSLHRFSSS SQNSNQFQNV GFIGLGNMGF RMVNNLIRAG YKVTVHDINR DVMKMFTEMG VSSRETPYEV AQDSEVVITM LPSSSHVMDV YTGTNGLLLG ENDIRPALFI DSSTIDPQTT RKISLAVSNC NLKEKRDNWE KPVMLDAPVS GGVLAAEAGT LTFMVGGPED AYLAARPILQ SMGRTSIYCG GSGNGSAAKI CNNLAMAVSM LGTSEALALG QSLGISASTL TEVLNTSSGR CWSSDAYNPV PGVMKGVPSS RDYNGGFASK LMAKDLNLAA ASAEEVGHKS PLISKAQEIY KKMCEEGHET KDFSCVFRHF YNGKDEV // ID 3HIDH_CAEEL Reviewed; 299 AA. AC Q9XTI0; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 20-FEB-2007, entry version 38. DE Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial DE (EC 1.1.1.31) (HIBADH). GN ORFNames=B0250.5; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- CATALYTIC ACTIVITY: 3-hydroxy-2-methylpropanoate + NAD(+) = 2- CC methyl-3-oxopropanoate + NADH. 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; Z81453; CAB03798.1; -; Genomic_DNA. DR EMBL; AL031630; CAB03798.1; JOINED; Genomic_DNA. DR EMBL; AL031630; CAA21003.1; -; Genomic_DNA. DR EMBL; Z81453; CAA21003.1; JOINED; Genomic_DNA. DR PIR; T18682; T18682. DR UniGene; Cel.9442; -. DR Ensembl; B0250.5; Caenorhabditis elegans. DR KEGG; cel:B0250.5; -. DR WormBase; WBGene00007122; B0250.5. DR WormPep; B0250.5; CE18481. DR InterPro; IPR011548; 3hydroxisobut_dh. DR InterPro; IPR002204; 3hydroxy_acid_DH. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006115; 6PGD_NAD_bd. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000103; 3hydroxyisobu_dh; 1. DR TIGRFAMs; TIGR01692; HIBADH; 1. DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1. KW Complete proteome; Hypothetical protein; Mitochondrion; NAD; KW Oxidoreductase. FT CHAIN 1 299 Probable 3-hydroxyisobutyrate FT dehydrogenase. FT /FTId=PRO_0000173055. FT NP_BIND 2 30 NAD (Potential). FT ACT_SITE 172 172 Probable. SQ SEQUENCE 299 AA; 31217 MW; F30B423A597CABF0 CRC64; MSLTGFIGLG NMGGHMARNL IKNGKKLIVY DVNKAVVQEF KAEGCEVAAH PADIAAASKE IITVLPSSPH VKAVYQGEAG IFKTIQPGTL CMDSSTIDQI VSLEVAQAAA LLKAEYIDAP ISGGVTGAQQ ATLTFMVGAG NDATFKRAEA VLSLMGKNIV NLGAVGNGTA AKICNNMLLG IQMVAVAETM NLGISMGLDA KALAGIVNTS SGRCWSSDTY NPVPGVIENI PSCRGYAGGF GTTLMAKDLS LAQNASTNTQ APTPMGSLAH QIYRILARDP QYQAKDFGVV YQFLKKQNS // ID 3HIDH_DROME Reviewed; 324 AA. AC Q9V8M5; Q0E926; Q86R98; Q9V8M6; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2001, sequence version 2. DT 23-JAN-2007, entry version 53. DE Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial precursor DE (EC 1.1.1.31) (HIBADH). GN ORFNames=CG15093; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 3-hydroxy-2-methylpropanoate + NAD(+) = 2- CC methyl-3-oxopropanoate + NADH. CC -!- INTERACTION: CC Q9W1K6:CG18128; NbExp=1; IntAct=EBI-241464, EBI-178006; CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=B; CC IsoId=Q9V8M5-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=C; CC IsoId=Q9V8M5-2; Sequence=VSP_001281, VSP_001282; CC Note=No experimental confirmation available; 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; AE013599; AAF57638.2; -; Genomic_DNA. DR EMBL; AE013599; AAF57639.2; -; Genomic_DNA. DR EMBL; AY069057; AAL39202.2; ALT_INIT; mRNA. DR UniGene; Dm.21583; -. DR DIP; DIP:22109N; -. DR IntAct; Q9V8M5; -. DR Ensembl; CG15093; Drosophila melanogaster. DR KEGG; dme:Dmel_CG15093; -. DR FlyBase; FBgn0034390; CG15093. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-005425-MONOMER; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-005426-MONOMER; -. DR GermOnline; CG15093; Drosophila melanogaster. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR011548; 3hydroxisobut_dh. DR InterPro; IPR002204; 3hydroxy_acid_DH. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006115; 6PGD_NAD_bd. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000103; 3hydroxyisobu_dh; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR01692; HIBADH; 1. DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1. KW Alternative splicing; Complete proteome; Hypothetical protein; KW Mitochondrion; NAD; Oxidoreductase; Transit peptide. FT TRANSIT 1 25 Mitochondrion (By similarity). FT CHAIN 26 324 Probable 3-hydroxyisobutyrate FT dehydrogenase. FT /FTId=PRO_0000007161. FT NP_BIND 29 57 NAD (Potential). FT ACT_SITE 196 196 By similarity. FT VAR_SEQ 95 227 NAIVDASYDEMTADGVNKDTIFIDSSTISPDLVKSLQKKIS FT AKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVL FT ECMGKKITHCGVYGMGQAAKLCNNMMLAISMIGVSEAMNLA FT VRQGLDANVF -> KCRQGRPRVHGQEDHPLRRLWHGPGRQ FT AVQQHDAGHLDDRCFGGHESGGAPGSRCQCLRRDHQLLHRT FT LLGLGDLQPCARSLPQCPSQQGLRRRFLLGSDHQGSGSGLR FT SGQRFQLTHPAGISGAQGLPVAVR (in isoform C). FT /FTId=VSP_001281. FT VAR_SEQ 228 324 Missing (in isoform C). FT /FTId=VSP_001282. SQ SEQUENCE 324 AA; 33883 MW; A39B534753EAE83E CRC64; MSLRVMSPAM LNAWSQTLVR AMSTQGGAKN IGFVGLGNMG ANMASNLIKA GHKLHVFDIS KPACDGLAAK GATVYAKTSE LAKNSDFVIT MLPNNAIVDA SYDEMTADGV NKDTIFIDSS TISPDLVKSL QKKISAKGAR FIDAPVSGGV PGAEQATLTF MVGGTEAEYN AVKAVLECMG KKITHCGVYG MGQAAKLCNN MMLAISMIGV SEAMNLAVRQ GLDANVFAEI INSSTGRCWA SEIYNPVPGV CPSAPANRDY AGGFSSALIT KDLGLASGVA NASNSPIPLG SLAHKVYQSL CDKGLGNKDF SVVYDLMKKE KFSV // ID 3HIDH_HUMAN Reviewed; 336 AA. AC P31937; Q9UDN3; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2001, sequence version 2. DT 06-FEB-2007, entry version 67. DE 3-hydroxyisobutyrate dehydrogenase, mitochondrial precursor DE (EC 1.1.1.31) (HIBADH). GN Name=HIBADH; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 37-47. RC TISSUE=Liver; RX MEDLINE=94147969; PubMed=8313870; RA Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., RA Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.; RT "Human liver protein map: update 1993."; RL Electrophoresis 14:1216-1222(1993). CC -!- CATALYTIC ACTIVITY: 3-hydroxy-2-methylpropanoate + NAD(+) = 2- CC methyl-3-oxopropanoate + NADH. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. 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; AC007130; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005091; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC032324; AAH32324.1; -; mRNA. DR UniGene; Hs.406758; -. DR PDB; 2GF2; X-ray; A/B/C/D=41-335. DR SWISS-2DPAGE; P31937; HUMAN. DR REPRODUCTION-2DPAGE; P31937; HUMAN. DR Siena-2DPAGE; P31937; -. DR Ensembl; ENSG00000106049; Homo sapiens. DR KEGG; hsa:11112; -. DR HGNC; HGNC:4907; HIBADH. DR Reactome; REACT_13.1; Metabolism of amino acids and related nitrogen-containing molecules. DR ArrayExpress; P31937; -. DR GermOnline; ENSG00000106049; Homo sapiens. DR RZPD-ProtExp; IOH21624; -. DR RZPD-ProtExp; RZPDo839H08123; -. DR RZPD-ProtExp; T7188; -. DR GO; GO:0005739; C:mitochondrion; NAS:UniProtKB. DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; NAS:UniProtKB. DR GO; GO:0006573; P:valine metabolic process; NAS:UniProtKB. DR InterPro; IPR011548; 3hydroxisobut_dh. DR InterPro; IPR002204; 3hydroxy_acid_DH. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006115; 6PGD_NAD_bd. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000103; 3hydroxyisobu_dh; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR01692; HIBADH; 1. DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1. KW 3D-structure; Direct protein sequencing; Mitochondrion; NAD; KW Oxidoreductase; Transit peptide. FT TRANSIT 1 36 Mitochondrion. FT CHAIN 37 336 3-hydroxyisobutyrate dehydrogenase. FT /FTId=PRO_0000007158. FT NP_BIND 40 68 NAD (Potential). FT ACT_SITE 209 209 By similarity. FT STRAND 42 45 FT TURN 49 50 FT HELIX 51 60 FT TURN 61 62 FT STRAND 65 68 FT TURN 72 72 FT HELIX 73 79 FT TURN 80 82 FT HELIX 89 95 FT STRAND 97 101 FT HELIX 106 114 FT TURN 116 117 FT HELIX 119 121 FT TURN 122 122 FT TURN 125 126 FT STRAND 128 131 FT HELIX 137 149 FT TURN 150 151 FT STRAND 153 156 FT STRAND 159 161 FT HELIX 162 168 FT TURN 169 169 FT STRAND 171 177 FT HELIX 179 181 FT HELIX 182 189 FT TURN 190 192 FT STRAND 193 201 FT TURN 202 203 FT HELIX 204 232 FT TURN 233 234 FT HELIX 237 245 FT TURN 246 246 FT TURN 248 249 FT HELIX 252 256 FT TURN 261 263 FT STRAND 265 267 FT HELIX 268 271 FT TURN 272 273 FT STRAND 275 278 FT HELIX 279 295 FT TURN 296 297 FT HELIX 301 314 FT TURN 315 317 FT TURN 319 320 FT HELIX 323 325 FT HELIX 326 330 SQ SEQUENCE 336 AA; 35329 MW; DA3128774A91AF48 CRC64; MAASLRLLGA ASGLRYWSRR LRPAAGSFAA VCSRSVASKT PVGFIGLGNM GNPMAKNLMK HGYPLIIYDV FPDACKEFQD AGEQVVSSPA DVAEKADRII TMLPTSINAI EAYSGANGIL KKVKKGSLLI DSSTIDPAVS KELAKEVEKM GAVFMDAPVS GGVGAARSGN LTFMVGGVED EFAAAQELLG CMGSNVVYCG AVGTGQAAKI CNNMLLAISM IGTAEAMNLG IRLGLDPKLL AKILNMSSGR CWSSDTYNPV PGVMDGVPSA NNYQGGFGTT LMAKDLGLAQ DSATSTKSPI LLGSLAHQIY RMMCAKGYSK KDFSSVFQFL REEETF // 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 06-FEB-2007, entry version 46. DE 3-hydroxyisobutyrate dehydrogenase, mitochondrial precursor DE (EC 1.1.1.31) (HIBADH). 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. 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). CC -!- CATALYTIC ACTIVITY: 3-hydroxy-2-methylpropanoate + NAD(+) = 2- CC methyl-3-oxopropanoate + NADH. 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 UniGene; Mm.286458; -. DR SMR; Q99L13; 40-333. DR REPRODUCTION-2DPAGE; Q99L13; MOUSE. DR Ensembl; ENSMUSG00000029776; Mus musculus. DR KEGG; mmu:58875; -. DR MGI; MGI:1889802; Hibadh. DR ArrayExpress; Q99L13; -. DR GermOnline; ENSMUSG00000029776; Mus musculus. DR RZPD-ProtExp; IOM20452; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR InterPro; IPR011548; 3hydroxisobut_dh. DR InterPro; IPR002204; 3hydroxy_acid_DH. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006115; 6PGD_NAD_bd. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000103; 3hydroxyisobu_dh; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR01692; HIBADH; 1. DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1. KW Mitochondrion; NAD; Oxidoreductase; Transit peptide. FT TRANSIT 1 35 Mitochondrion (By similarity). FT CHAIN 36 335 3-hydroxyisobutyrate dehydrogenase. FT /FTId=PRO_0000007159. FT NP_BIND 39 67 NAD (Potential). FT ACT_SITE 208 208 By similarity. FT CONFLICT 2 2 A -> S (in Ref. 1). 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 3HIDH_RABIT Reviewed; 35 AA. AC P32185; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 31-OCT-2006, entry version 36. DE 3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) (HIBADH) (Fragment). GN Name=HIBADH; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Liver; RX MEDLINE=89174651; PubMed=2647728; RA Rougraff P.M., Zhang B., Kuntz M.J., Harris R.A., Crabb D.W.; RT "Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate RT dehydrogenase. Evidence for its evolutionary relationship to other RT pyridine nucleotide-dependent dehydrogenases."; RL J. Biol. Chem. 264:5899-5903(1989). CC -!- CATALYTIC ACTIVITY: 3-hydroxy-2-methylpropanoate + NAD(+) = 2- CC methyl-3-oxopropanoate + NADH. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion. 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 InterPro; IPR002204; 3hydroxy_acid_DH. DR InterPro; IPR006115; 6PGD_NAD_bd. DR Pfam; PF03446; NAD_binding_2; 1. DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1. KW Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase. FT CHAIN 1 >35 3-hydroxyisobutyrate dehydrogenase. FT /FTId=PRO_0000173054. FT NON_TER 35 35 SQ SEQUENCE 35 AA; 3796 MW; C15D62589F84ED64 CRC64; ASKTPVGFIG LGNMGNPMAK NLMKHGYPLI IYDVF // ID 3HIDH_RAT Reviewed; 335 AA. AC P29266; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2001, sequence version 3. DT 20-FEB-2007, entry version 66. DE 3-hydroxyisobutyrate dehydrogenase, mitochondrial precursor DE (EC 1.1.1.31) (HIBADH). GN Name=Hibadh; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX MEDLINE=89174651; PubMed=2647728; RA Rougraff P.M., Zhang B., Kuntz M.J., Harris R.A., Crabb D.W.; RT "Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate RT dehydrogenase. Evidence for its evolutionary relationship to other RT pyridine nucleotide-dependent dehydrogenases."; RL J. Biol. Chem. 264:5899-5903(1989). RN [2] RP PROTEIN SEQUENCE OF 60-75; 297-310 AND 321-330. RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord; RA Lubec G., Afjehi-Sadat L.; RL Submitted (NOV-2006) to Swiss-Prot. RN [3] RP MUTAGENESIS. RX MEDLINE=96335606; PubMed=8766712; DOI=10.1016/0014-5793(96)00597-2; RA Hawes J.W., Harper E.T., Crabb D.W., Harris R.A.; RT "Structural and mechanistic similarities of 6-phosphogluconate and 3- RT hydroxyisobutyrate dehydrogenases reveal a new enzyme family, the 3- RT hydroxyacid dehydrogenases."; RL FEBS Lett. 389:263-267(1996). CC -!- CATALYTIC ACTIVITY: 3-hydroxy-2-methylpropanoate + NAD(+) = 2- CC methyl-3-oxopropanoate + NADH. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- TISSUE SPECIFICITY: Higher level in kidney, liver, and heart than CC in muscle. CC -!- SIMILARITY: Belongs to the 3-hydroxyisobutyrate dehydrogenase CC family. CC -!- CAUTION: Ref.1 (AAA50312) sequence differs from that shown due to CC a frameshift in position 10. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J04628; AAA50312.1; ALT_FRAME; mRNA. DR PIR; A32867; A32867. DR UniGene; Rn.73; -. DR SMR; P29266; 40-334. DR IntAct; P29266; -. DR Ensembl; ENSRNOG00000008063; Rattus norvegicus. DR KEGG; rno:63938; -. DR RGD; 708399; Hibadh. DR ArrayExpress; P29266; -. DR GermOnline; ENSRNOG00000008063; Rattus norvegicus. DR InterPro; IPR011548; 3hydroxisobut_dh. DR InterPro; IPR002204; 3hydroxy_acid_DH. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006115; 6PGD_NAD_bd. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000103; 3hydroxyisobu_dh; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR01692; HIBADH; 1. DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1. KW Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; KW Transit peptide. FT TRANSIT 1 35 Mitochondrion (By similarity). FT CHAIN 36 335 3-hydroxyisobutyrate dehydrogenase. FT /FTId=PRO_0000007160. FT NP_BIND 39 67 NAD (Potential). FT ACT_SITE 208 208 Probable. FT MUTAGEN 68 68 D->R: Decrease of activity with NAD, FT increase of activity with NADP. FT MUTAGEN 208 208 K->A,H,N,R: Complete loss of activity. FT MUTAGEN 212 212 N->Q: Decrease in activity. SQ SEQUENCE 335 AA; 35303 MW; D266A7838500295A CRC64; MAASLGFRGA ASGLRYWSGR RRPVGSLAAV CSRSMASKTP VGFIGLGNMG NPMAKNLIKH GYPLILYDVF PDVCKEFKEA GEQVASSPAD VAEKADRIIT MLPSSMNSIE VYSGANGILK KVKKGSLLID SSTIDPSVSK ELAKEVEKMG AVFMDAPVSG GVGAARSGNL TFMVGGVENE FAAAQELLGC MGSNVLYCGA VGSGQSAKIC NNMLLAISMI GTAEAMNLGI RSGLDPKLLA KILNMSSGRC WSSDTYNPVP GVMDGVPSSN NYQGGFGTTL MAKDLGLAQD SATSTKTPIL LGSVAHQIYR MMCSKGYSKK DFSSVFQYLR EEETF // ID 3MG1_ECOLI Reviewed; 187 AA. AC P05100; Q2M7L0; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 20-FEB-2007, entry version 64. DE DNA-3-methyladenine glycosylase 1 (EC 3.2.2.20) (DNA-3-methyladenine DE glycosylase I) (3-methyladenine-DNA glycosylase I, constitutive) (TAG DE I) (DNA-3-methyladenine glycosidase I). GN Name=tag; OrderedLocusNames=b3549, JW3518; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-29. RX MEDLINE=87057218; PubMed=3536912; RA Sakumi K., Nakabeppu Y., Yamamoto Y., Kawabata S., Iwanaga S., RA Sekiguchi M.; RT "Purification and structure of 3-methyladenine-DNA glycosylase I of RT Escherichia coli."; RL J. Biol. Chem. 261:15761-15766(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86232617; PubMed=3520491; DOI=10.1093/nar/14.9.3763; RA Steinum A.-L., Seeberg E.; RT "Nucleotide sequence of the tag gene from Escherichia coli."; RL Nucleic Acids Res. 14:3763-3772(1986). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=94316500; PubMed=8041620; DOI=10.1093/nar/22.13.2576; RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; RT "Analysis of the Escherichia coli genome. V. DNA sequence of the RT region from 76.0 to 81.5 minutes."; RL Nucleic Acids Res. 22:2576-2586(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine from the damaged DNA polymer formed by CC alkylation lesions. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine. CC -!- ENZYME REGULATION: Activity is controlled by product inhibition. CC -!- INTERACTION: CC P0AFG8:aceE; NbExp=1; IntAct=EBI-558722, EBI-542683; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J02606; AAA24658.1; -; Genomic_DNA. DR EMBL; X03845; CAA27472.1; -; Genomic_DNA. DR EMBL; U00039; AAB18526.1; -; Genomic_DNA. DR EMBL; U00096; AAC76573.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77746.1; -; Genomic_DNA. DR PIR; A24604; DGECM1. DR PDB; 1LMZ; NMR; A=1-187. DR PDB; 1NKU; NMR; A=1-187. DR PDB; 1P7M; NMR; A=1-187. DR DIP; DIP:10950N; -. DR IntAct; P05100; -. DR ECO2DBASE; H021.1; 6TH EDITION. DR GenomeReviews; U00096_GR; b3549. DR GenomeReviews; AP009048_GR; JW3518. DR KEGG; ecj:JW3518; -. DR KEGG; eco:b3549; -. DR EchoBASE; EB0979; -. DR EcoGene; EG10986; tag. DR BioCyc; EcoCyc:EG10986-MONOMER; -. DR LinkHub; P05100; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR005019; Adenine_glyco. DR InterPro; IPR011257; DNA_glycsylse. DR InterPro; IPR004597; Tag. DR Pfam; PF03352; Adenine_glyco; 1. DR TIGRFAMs; TIGR00624; tag; 1. KW 3D-structure; Complete proteome; Direct protein sequencing; KW DNA damage; DNA repair; Hydrolase. FT CHAIN 1 187 DNA-3-methyladenine glycosylase 1. FT /FTId=PRO_0000194877. FT TURN 11 11 FT HELIX 12 19 FT STRAND 20 23 FT HELIX 28 39 FT TURN 40 43 FT HELIX 46 70 FT HELIX 73 81 FT STRAND 82 85 FT HELIX 90 107 FT TURN 108 109 FT HELIX 112 118 FT TURN 119 122 FT TURN 132 134 FT HELIX 140 152 FT TURN 153 153 FT HELIX 159 169 FT TURN 170 170 FT STRAND 171 173 FT TURN 177 178 FT STRAND 179 181 SQ SEQUENCE 187 AA; 21100 MW; 5A305B5CA66A48FE CRC64; MERCGWVSQD PLYIAYHDNE WGVPETDSKK LFEMICLEGQ QAGLSWITVL KKRENYRACF HQFDPVKVAA MQEEDVERLV QDAGIIRHRG KIQAIIGNAR AYLQMEQNGE PFVDFVWSFV NHQPQVTQAT TLSEIPTSTS ASDALSKALK KRGFKFVGTT ICYSFMQACG LVNDHVVGCC CYPGNKP // ID 3MG2_ECOLI Reviewed; 282 AA. AC P04395; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 12-DEC-2006, entry version 76. DE DNA-3-methyladenine glycosylase 2 (EC 3.2.2.21) (DNA-3-methyladenine DE glycosylase II) (3-methyladenine-DNA glycosylase II, inducible) (TAG DE II) (DNA-3-methyladenine glycosidase II). GN Name=alkA; Synonyms=aidA; OrderedLocusNames=b2068, JW2053; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12 AND RP 14-20. RX MEDLINE=85054800; PubMed=6094528; RA Nakabeppu Y., Miyata T., Kondo H., Iwanaga S., Sekiguchi M.; RT "Structure and expression of the alkA gene of Escherichia coli RT involved in adaptive response to alkylating agents."; RL J. Biol. Chem. 259:13730-13736(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97251358; PubMed=9097040; DOI=10.1093/dnares/3.6.379; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., RA Yamamoto Y., Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP CHARACTERIZATION. RX MEDLINE=85054799; PubMed=6389535; RA Nakabeppu Y., Kondo H., Sekiguchi M.; RT "Cloning and characterization of the alkA gene of Escherichia coli RT that encodes 3-methyladenine DNA glycosylase II."; RL J. Biol. Chem. 259:13723-13729(1984). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2. RX MEDLINE=86313568; PubMed=3529081; RA Nakabeppu Y., Sekiguchi M.; RT "Regulatory mechanisms for induction of synthesis of repair enzymes in RT response to alkylating agents: ada protein acts as a transcriptional RT regulator."; RL Proc. Natl. Acad. Sci. U.S.A. 83:6297-6301(1986). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND MUTAGENESIS. RX MEDLINE=96319733; PubMed=8706135; DOI=10.1016/S0092-8674(00)80102-6; RA Yamagata Y., Kato M., Odawara K., Tokuno Y., Nakashima Y., RA Matsushima N., Yasumura K., Tomita K., Ihara K., Fujii Y., RA Nakabeppu Y., Sekiguchi M., Fujii S.; RT "Three-dimensional structure of a DNA repair enzyme, 3-methyladenine RT DNA glycosylase II, from Escherichia coli."; RL Cell 86:311-319(1996). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=96319734; PubMed=8706136; DOI=10.1016/S0092-8674(00)80103-8; RA Labahn J., Scharer O.D., Long A., Ezaz-Nikpay K., Verdine G.L., RA Ellenberger T.E.; RT "Structural basis for the excision repair of alkylation-damaged DNA."; RL Cell 86:321-329(1996). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine, 3-methylguanine, 7-methylguanine, O2- CC methylthymine, and O2-methylcytosine from the damaged DNA polymer CC formed by alkylation lesions. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine, 3-methylguanine, 7-methylguanine and 7- CC methyladenine. CC -!- SUBUNIT: Monomer. CC -!- INTERACTION: CC P06959:aceF; NbExp=1; IntAct=EBI-544077, EBI-542707; CC -!- INDUCTION: When E.coli cells are exposed to doses of DNA CC alkylating agent. It is not inhibited by reaction products. CC -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase alkA family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K02498; AAA23430.1; -; Genomic_DNA. DR EMBL; U00096; AAC75129.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15926.1; -; Genomic_DNA. DR EMBL; M13827; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A00904; DGECMA. DR PDB; 1DIZ; X-ray; A/B=1-282. DR PDB; 1MPG; X-ray; A/B=1-282. DR PDB; 1PVS; X-ray; A/B=1-282. DR DIP; DIP:9084N; -. DR IntAct; P04395; -. DR GenomeReviews; U00096_GR; b2068. DR GenomeReviews; AP009048_GR; JW2053. DR KEGG; ecj:JW2053; -. DR KEGG; eco:b2068; -. DR EchoBASE; EB1204; -. DR EcoGene; EG11222; alkA. DR BioCyc; EcoCyc:EG11222-MONOMER; -. DR LinkHub; P04395; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR000035; AlbDNA_glycsylse. DR InterPro; IPR010316; AlkA_N. DR InterPro; IPR011257; DNA_glycsylse. DR InterPro; IPR003265; Endo_3c. DR InterPro; IPR012294; TFIID_C/glycos_N. DR Gene3D; G3DSA:3.30.310.20; AlkA_N; 1. DR Pfam; PF06029; AlkA_N; 1. DR Pfam; PF00730; HhH-GPD; 1. DR SMART; SM00478; ENDO3c; 1. DR PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1. KW 3D-structure; Complete proteome; Direct protein sequencing; KW DNA damage; DNA repair; Hydrolase. FT CHAIN 1 282 DNA-3-methyladenine glycosylase 2. FT /FTId=PRO_0000194878. FT ACT_SITE 238 238 Proton acceptor. FT SITE 218 218 Determinant for substrate specificity FT and/or activity. FT MUTAGEN 124 124 Q->A: Methylmethane sulfonate-resistant. FT MUTAGEN 218 218 W->A: No catalytic activity, FT methylmethane sulfonate-sensitive. FT MUTAGEN 237 237 D->N: More than 30% catalytic activity, FT methylmethane sulfonate-resistant. FT MUTAGEN 238 238 D->N: No catalytic activity, FT methylmethane sulfonate-sensitive. FT STRAND 2 5 FT HELIX 12 22 FT TURN 25 27 FT STRAND 28 30 FT STRAND 35 41 FT TURN 42 43 FT STRAND 44 53 FT TURN 54 57 FT STRAND 58 63 FT HELIX 65 70 FT HELIX 71 82 FT TURN 83 85 FT HELIX 88 95 FT HELIX 96 99 FT TURN 100 101 FT TURN 103 104 FT HELIX 113 122 FT TURN 123 125 FT HELIX 128 142 FT TURN 150 151 FT HELIX 158 162 FT TURN 163 163 FT HELIX 166 171 FT TURN 172 173 FT HELIX 176 190 FT TURN 191 192 FT HELIX 202 209 FT TURN 210 211 FT TURN 213 214 FT HELIX 217 227 FT TURN 236 237 FT HELIX 239 244 FT TURN 246 247 FT HELIX 250 257 FT HELIX 258 260 FT TURN 261 262 FT HELIX 264 272 FT TURN 273 273 FT TURN 275 276 SQ SEQUENCE 282 AA; 31393 MW; B66BB5E23019899C CRC64; MYTLNWQPPY DWSWMLGFLA ARAVSSVETV ADSYYARSLA VGEYRGVVTA IPDIARHTLH INLSAGLEPV AAECLAKMSR LFDLQCNPQI VNGALGRLGA ARPGLRLPGC VDAFEQGVRA ILGQLVSVAM AAKLTARVAQ LYGERLDDFP EYICFPTPQR LAAADPQALK ALGMPLKRAE ALIHLANAAL EGTLPMTIPG DVEQAMKTLQ TFPGIGRWTA NYFALRGWQA KDVFLPDDYL IKQRFPGMTP AQIRRYAERW KPWRSYALLH IWYTEGWQPD EA // ID 3MGA_BACSU Reviewed; 303 AA. AC P37878; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 28-NOV-2006, entry version 49. DE DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-methyladenine-DNA DE glycosidase). GN Name=alkA; OrderedLocusNames=BSU01800; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=93388534; PubMed=8376346; RA Morohoshi F., Hayashi K., Munakata N.; RT "Bacillus subtilis alkA gene encoding inducible 3-methyladenine DNA RT glycosylase is adjacent to the ada operon."; RL J. Bacteriol. 175:6010-6017(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.; RT "Sequence analysis of the 70kb region between 17 and 23 degree of the RT Bacillus subtilis chromosome."; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine, 3-methylguanine, 7-methylguanine, O2- CC methylthymine, and O2-methylcytosine from the damaged DNA polymer CC formed by alkylation lesions. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine, 3-methylguanine, 7-methylguanine and 7- CC methyladenine. CC -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase alkA family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D14465; BAA03361.1; -; Genomic_DNA. DR EMBL; AB006424; BAA33073.1; -; Genomic_DNA. DR EMBL; Z99104; CAB11956.1; -; Genomic_DNA. DR PIR; E69584; E69584. DR GenomeReviews; AL009126_GR; BSU01800. DR KEGG; bsu:BG10165; -. DR SubtiList; BG10165; alkA. DR BioCyc; BSUB1423:BSU0180-MONOMER; -. DR InterPro; IPR000035; AlbDNA_glycsylse. DR InterPro; IPR010316; AlkA_N. DR InterPro; IPR011257; DNA_glycsylse. DR InterPro; IPR003265; Endo_3c. DR InterPro; IPR012904; OGG_N. DR InterPro; IPR012294; TFIID_C/glycos_N. DR Gene3D; G3DSA:3.30.310.20; AlkA_N; 1. DR Pfam; PF00730; HhH-GPD; 1. DR Pfam; PF07934; OGG_N; 1. DR SMART; SM00478; ENDO3c; 1. DR PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 303 DNA-3-methyladenine glycosylase. FT /FTId=PRO_0000194880. SQ SEQUENCE 303 AA; 35634 MW; 17BEEFC78457A591 CRC64; MTWHEVNDVI VITLPEIFDM NANLGYLTRE KNECMYEIEN NIITKVIAIG EIRSLVQVSV INNKQMIVQF LNDSRPVEQW KREEIVKYIH EWFDLDNDLT PFYEMAKADP LLKMPARKFY GLRVIGIPDL FEALCWGVLG QQINLAFAYS LKKQFVEAFG DSIEWNGKKY WVFPPYERIA RLTPTDLADI KMTVKKSEYI IGIARLMASG ELSREKLMKM NFKDAEKNLI KIRGIGPWTA NYVLMRCLRF PTAFPIDDVG LIHSIKILRN MNRKPTKDEI LEISVPWKEW QSYATFYLWR VLY // ID 3MGA_HAEIN Reviewed; 185 AA. AC P44321; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 31-OCT-2006, entry version 39. DE DNA-3-methyladenine glycosylase (EC 3.2.2.20) (3-methyladenine-DNA DE glycosidase) (TAG). GN Name=tag; OrderedLocusNames=HI0654; OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine from the damaged DNA polymer formed by CC alkylation lesions (By similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22313.1; -; Genomic_DNA. DR PIR; G64084; G64084. DR HSSP; P05100; 1NKU. DR GenomeReviews; L42023_GR; HI0654. DR KEGG; hin:HI0654; -. DR TIGR; HI0654; -. DR BioCyc; HINF71421:HI0654-MONOMER; -. DR LinkHub; P44321; -. DR InterPro; IPR005019; Adenine_glyco. DR InterPro; IPR011257; DNA_glycsylse. DR InterPro; IPR004597; Tag. DR Pfam; PF03352; Adenine_glyco; 1. DR TIGRFAMs; TIGR00624; tag; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 185 DNA-3-methyladenine glycosylase. FT /FTId=PRO_0000194879. SQ SEQUENCE 185 AA; 21193 MW; 03AC41B636BD4321 CRC64; MTTRCPWVGE QSIYIDYHDK EWGKPEFDSQ KLFEKICLEG QQAGLSWITV LKKRESYREA FHQFDPKKIA KMTALDIDAC MQNSGLIRHR AKLEAIVKNA KAYLAMEKCG ENFSDFIWSF VNHKPIVNDV PDLRSVPTKT EVSKALSKAL KKRGFVFIGE TTCYAFMQSM GLVDDHLNDC PCKTS // ID 3MGH_ACIBL Reviewed; 207 AA. AC Q1IHD8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 23-JAN-2007, entry version 6. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Acid345_4712; OS Acidobacteria bacterium (strain Ellin345). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae. OX NCBI_TaxID=204669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Kiss H., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., RA Kuske C., Janssen P.H., Richardson P.; RT "Complete sequence of Acidobacteria bacterium Ellin345."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000360; ABF43712.1; -; Genomic_DNA. DR GenomeReviews; CP000360_GR; Acid345_4712. DR KEGG; aba:Acid345_4712; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 207 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000264992. SQ SEQUENCE 207 AA; 22349 MW; E6834D90907EDAD1 CRC64; MPRSSLAQLA PLPRAFFNRD PRIVGRELLG KVLLRREGRA ILAGRIVECE AYLGADDAAA HSAAGKTARN AVLFGPPGYA YVYFIYGNHF CLNVSCLPDG QAGGILFRAL EPIAGVERMA ANRQLEPSQL RLIASGPGRL AEALAVTRDR DNGKDMVSPK SDLRIVDDGF GAVEVRETPR IGITKSADLP LRYIVAGSPF VSGKRYL // ID 3MGH_AERPE Reviewed; 194 AA. AC Q9Y9P1; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 28-NOV-2006, entry version 33. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=APE2247; OS Aeropyrum pernix. OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Aeropyrum. OX NCBI_TaxID=56636; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K1; RX MEDLINE=99310339; PubMed=10382966; DOI=10.1093/dnares/6.2.83; RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., RA Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., RA Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., RA Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y., RA Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., RA Nomura N., Sako Y., Kikuchi H.; RT "Complete genome sequence of an aerobic hyper-thermophilic RT crenarchaeon, Aeropyrum pernix K1."; RL DNA Res. 6:83-101(1999). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000002; BAA81259.1; -; Genomic_DNA. DR PIR; C72450; C72450. DR HSSP; P29372; 1EWN. DR GenomeReviews; BA000002_GR; APE2247. DR KEGG; ape:APE2247; -. DR BioCyc; APER56636:APE2247-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 194 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100117. SQ SEQUENCE 194 AA; 21276 MW; 1EE737DC6A1406EE CRC64; MGRLLPKSFY YRQPDVVARE LLGKILVSCA SGACMRCMVT EAEAYFGECD PASRARRGRG RIWRALYGEP GRALVYGMHR QWLLNIVAHS EGMAGAVLLR SCQPLEPPRL DPPPIGPGRL ARALSIDRGV DGAPVYERGS PLTLWENPEA VEGFRVACSG RVGVSEDLEL PLRFYIAGNP FVSKARVSPA PKHC // ID 3MGH_AGRT5 Reviewed; 193 AA. AC Q8UAN8; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2002, sequence version 2. DT 28-NOV-2006, entry version 30. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Atu3335, AGR_L_2973; OS Agrobacterium tumefaciens (strain C58 / ATCC 33970). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=176299; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21608550; PubMed=11743193; DOI=10.1126/science.1066804; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., RA Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., RA Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., RA Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C., RA Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., RA Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., RA Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., RA Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., RA Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., RA Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21608551; PubMed=11743194; DOI=10.1126/science.1066803; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., RA Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., RA Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., RA Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., RA Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., RA Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009263; AAL44148.1; -; Genomic_DNA. DR EMBL; AE008348; AAK90056.1; ALT_INIT; Genomic_DNA. DR PIR; AF2966; AF2966. DR HSSP; P29372; 1EWN. DR GenomeReviews; AE007870_GR; AGR_L_2973. DR GenomeReviews; AE008689_GR; Atu3335. DR KEGG; atc:AGR_L_2973; -. DR KEGG; atu:Atu3335; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 193 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100070. SQ SEQUENCE 193 AA; 21053 MW; B86BD2B0645BA3B5 CRC64; MNQSFSPEVP QSFFQRDALD VARALIGAEF RVGKAGGIIV ETEAYHPDDP ASHAFNGQTP RNRAMFGPAG HLYVYRSYGI HWCANFVCAP GSAVLLRAIE PLTGIDMMKL RRGTDKLKLL CSGPGKLCQA MAITGEMDGA PLNAPPFLLR LPKEAAAIST GRRIGISRAV DYPWRFGLEG SAFVSKKFEP DQR // ID 3MGH_ANADE Reviewed; 207 AA. AC Q2IHD7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Adeh_4231; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000251; ABC83995.1; -; Genomic_DNA. DR GenomeReviews; CP000251_GR; Adeh_4231. DR KEGG; ade:Adeh_4231; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 207 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000264993. SQ SEQUENCE 207 AA; 22290 MW; 781C562EDA50157F CRC64; MKLPQAFYAR DTRTVARALL GKVLVHLDGG VRRAARIVET EAYHGPDDRA SHARAGPTPR AAIMFGPPGR AYVYLIYGTS HCMNVVTGPE GFPSAVLIRA AEPIEGCLHS TRGPGNLCRA LAIRREHDNG RDLWGEELFI EDAPAPREAV VTGPRVNVGY AGPWAARPWR FALRGSAWVS RPAPAGARAA RAPAPAPRPR RPRGSGP // ID 3MGH_BACAN Reviewed; 205 AA. AC Q81UJ9; Q6I2S8; Q6KWK9; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 28-NOV-2006, entry version 27. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=BA_0869, GBAA0869, BAS0826; OS Bacillus anthracis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames / isolate Porton; RX MEDLINE=22608414; PubMed=12721629; DOI=10.1038/nature01586; RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L., RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., RA Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., RA Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., RA Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., RA Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., RA Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., RA Hanna P.C., Kolstoe A.-B., Fraser C.M.; RT "The genome sequence of Bacillus anthracis Ames and comparison to RT closely related bacteria."; RL Nature 423:81-86(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor; RA Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., RA Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., RA Fraser C.M.; RT "Bacillus anthracis comparative genomics."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sterne; RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., RA Richardson P., Rubin E., Tice H.; RT "Complete genome sequence of Bacillus anthracis Sterne."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016879; AAP24868.1; -; Genomic_DNA. DR EMBL; AE017334; AAT29981.1; -; Genomic_DNA. DR EMBL; AE017225; AAT53153.1; -; Genomic_DNA. DR GenomeReviews; AE016879_GR; BA_0869. DR GenomeReviews; AE017225_GR; BAS0826. DR GenomeReviews; AE017334_GR; GBAA0869. DR KEGG; ban:BA0869; -. DR KEGG; bar:GBAA0869; -. DR KEGG; bat:BAS0826; -. DR TIGR; BA_0869; -. DR TIGR; GBAA0869; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100071. SQ SEQUENCE 205 AA; 22965 MW; FC334BA99620F67D CRC64; MQAPPSFYEG DTLEVAKKLL GQKLVHIVNG IKRSGIIVEV EAYKGPDDKA AHSYGGRRTD RTEVMFGAPG HAYVYLIYGM YHCFNVITAP VGTPQGVLIR ALEPVDGIEE IKLARYNKTD ITKAQYKNLT NGPGKLCRAL GITLEERGVS LQSDTLHIEL VPEEKHISSQ YKITAGPRIN IDYAEEAVHY PWRFYYEGHP FVSKK // ID 3MGH_BACC1 Reviewed; 205 AA. AC Q73CV5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=BCE_0959; OS Bacillus cereus (strain ATCC 10987). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=222523; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14960714; DOI=10.1093/nar/gkh258; RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.; RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic RT adaptations and a large plasmid related to Bacillus anthracis pXO1."; RL Nucleic Acids Res. 32:977-988(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017194; AAS39890.1; -; Genomic_DNA. DR GenomeReviews; AE017194_GR; BCE_0959. DR KEGG; bca:BCE_0959; -. DR TIGR; BCE_0959; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000264994. SQ SEQUENCE 205 AA; 23026 MW; A6E597773311B1C6 CRC64; MQAPPSFYEG DTLEVAKKLL GQKLVHIVDG IKRSGIIVEV EAYKGPDDKA AHSYGGRRTD RTEVMFGAPG HAYVYLIYGM YHCFNVITAP VGTPQGVLIR ALEPVDGIEE IKLARYNKTD ITKAQYKNLT NGPGKLCRAL GITLEERGVS LQSDTLHIEL VREEEHISSQ YKITAGPRIN IDYAEEAVHY PWRFYYEGHP FVSKK // ID 3MGH_BACCR Reviewed; 205 AA. AC Q81HD0; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 28-NOV-2006, entry version 22. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=BC_0885; OS Bacillus cereus (strain ATCC 14579 / DSM 31). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22608415; PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D., RA Overbeek R., Kyrpides N.C.; RT "Genome sequence of Bacillus cereus and comparative analysis with RT Bacillus anthracis."; RL Nature 423:87-91(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016877; AAP07872.1; -; Genomic_DNA. DR GenomeReviews; AE016877_GR; BC_0885. DR KEGG; bce:BC0885; -. DR BioCyc; BCER226900:BC0885-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100072. SQ SEQUENCE 205 AA; 22979 MW; EED49B0929424163 CRC64; MQAPPSFYEG DTLEVAKKLL GQKLVHIVDG IKRSGIIVEV EAYKGPDDKA AHSYGGRRTD RTEVMFGAPG HAYVYLIYGM YHCFNVITAP VGTPQGVLIR ALEPVDGIEE IKLARYNKTE ITKAQYKNLT NGPGKLCRAL GITLKERGVS LQSDTLHIEL VPKEEHISSQ YKITAGPRIN IDYAEEAVHY PWRFYYEGHP FVSKK // ID 3MGH_BACCZ Reviewed; 205 AA. AC Q63FD4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 12-DEC-2006, entry version 16. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=BCE33L0774; OS Bacillus cereus (strain ZK / E33L). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=288681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000001; AAU19470.1; -; Genomic_DNA. DR GenomeReviews; CP000001_GR; BCE33L0774. DR KEGG; bcz:BCZK0774; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000264995. SQ SEQUENCE 205 AA; 22967 MW; A6E59775919B9BC6 CRC64; MQAPPSFYEG DTLEVAKKLL GQKLVHIVDG IKRSGIIVEV EAYKGPDDKA AHSYGGRRTD RTEVMFGAPG HAYVYLIYGM YHCFNVITAP VGTPQGVLIR ALEPVDGIEE IKLARYNKTD ITKAQYKNLT NGPGKLCRAL GITLEERGVS LQSDTLHIEL VPEEEHISSQ YKITAGPRIN IDYAEEAVHY PWRFYYEGHP FVSKK // ID 3MGH_BACHK Reviewed; 205 AA. AC Q6HMV4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 12-DEC-2006, entry version 19. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=BT9727_0773; OS Bacillus thuringiensis subsp. konkukian. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=180856; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017355; AAT62440.1; -; Genomic_DNA. DR GenomeReviews; AE017355_GR; BT9727_0773. DR KEGG; btk:BT9727_0773; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000264998. SQ SEQUENCE 205 AA; 23025 MW; F15EFD7D34AADC7D CRC64; MQAPPSFYEG DTLEVAKKLL GQKLVHIVNG IKRSGIIVEV EAYKGPDDKA AHSYGGRRTD RTEVMFGAPG HAYVYLIYGM YHCFNVITAP VGTPQGVLIR ALEPVDGIEE IKLARYNKTD ITKAQYKNLT NGPGKLCRAL GITLEERGVS LQSDTLHIEL VREEEHISSQ YKITAGPRIN IDYAEEAVHY PWRFYYEGHP FVSKK // ID 3MGH_BACLD Reviewed; 196 AA. AC Q65DF9; Q62NX9; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 12-DEC-2006, entry version 19. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=BLi04092, BL05369; OS Bacillus licheniformis (strain DSM 13 / ATCC 14580). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., RA Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., RA Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an RT organism with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., RA Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., RA Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., RA Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017333; AAU42905.1; -; Genomic_DNA. DR EMBL; CP000002; AAU25532.1; -; Genomic_DNA. DR GenomeReviews; CP000002_GR; BL05369. DR GenomeReviews; AE017333_GR; BLi04092. DR KEGG; bld:BLi04092; -. DR KEGG; bli:BL05369; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 196 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000264997. SQ SEQUENCE 196 AA; 21988 MW; 54F900931EDB6727 CRC64; MNPAHEPLPL EFYNKPTIEL ARSLLGCLLV KETEEGPASG YIVETEAYKG PGDRAAHSYG NRRTKRTEIM YREAGVVYTY TMHTHTLINV VSGGADEPEA VLIRALEPHE GLALMEKRRS GKKPRDWTNG PGKLTKALSI TMNDYGRPLT GPPLYIAKGY EPQDILSGPR IGIDNSGEAR EYPWRFWIKG NRYVSR // ID 3MGH_BACSK Reviewed; 200 AA. AC Q5WGN4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 12-DEC-2006, entry version 14. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=ABC1936; OS Bacillus clausii (strain KSM-K16). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=66692; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii RT KSM-K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006627; BAD64471.1; -; Genomic_DNA. DR GenomeReviews; AP006627_GR; ABC1936. DR KEGG; bcl:ABC1936; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 200 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000264996. SQ SEQUENCE 200 AA; 22269 MW; 602A6303EE316F5B CRC64; MEQQKALDLS FFEQSTIEVA KGLIGMHLVH ELDGVTLIGR ITETEAYLGV LDRACHSYGR RRTKRTAILY EEAGRCYTYT MHTHCLLNVV CEQKGQPEAV LIRAIEPISG VKEMERLRGK PHTSREFANG PGKLTKAMGI TMADYGRLLT EPPLYFAKGD HTNASIVATK RIGIKGAGPC SHHPWRFIDG NSRAVSAYRP // ID 3MGH_BACSU Reviewed; 196 AA. AC P94378; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 28-NOV-2006, entry version 49. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN Name=yxlJ; OrderedLocusNames=BSU38620; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / BGSC1A1; RX MEDLINE=97124196; PubMed=8969509; RA Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., RA Miwa Y., Fujita Y.; RT "Sequencing of a 65 kb region of the Bacillus subtilis genome RT containing the lic and cel loci, and creation of a 177 kb contig RT covering the gnt-sacXY region."; RL Microbiology 142:3113-3123(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D83026; BAA11741.1; -; Genomic_DNA. DR EMBL; Z99123; CAB15888.1; -; Genomic_DNA. DR PIR; D70082; D70082. DR HSSP; P29372; 1F6O. DR GenomeReviews; AL009126_GR; BSU38620. DR KEGG; bsu:BG12555; -. DR SubtiList; BG12555; yxlJ. DR BioCyc; BSUB1423:BSU3858-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 196 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100073. SQ SEQUENCE 196 AA; 22124 MW; E63A02E6285E4FF0 CRC64; MTREKNPLPI TFYQKTALEL APSLLGCLLV KETDEGTASG YIVETEAYMG AGDRAAHSFN NRRTKRTEIM FAEAGRVYTY VMHTHTLLNV VAAEEDVPQA VLIRAIEPHE GQLLMEERRP GRSPREWTNG PGKLTKALGV TMNDYGRWIT EQPLYIESGY TPEAISTGPR IGIDNSGEAR DYPWRFWVTG NRYVSR // ID 3MGH_BDEBA Reviewed; 192 AA. AC Q6MGX6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 12-DEC-2006, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Bd3793; OS Bdellovibrio bacteriovorus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=959; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15356 / HD100 / DSM 50701 / NCIB 9529; RX PubMed=14752164; DOI=10.1126/science.1093027; RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., RA Sockett R.E., Schuster S.C.; RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a RT genomic perspective."; RL Science 303:689-692(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX842656; CAE81153.1; -; Genomic_DNA. DR GenomeReviews; BX842601_GR; Bd3793. DR KEGG; bba:Bd3793; -. DR BioCyc; BBAC264462:BD3793-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 192 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000264999. SQ SEQUENCE 192 AA; 22260 MW; 341272523DEB22EB CRC64; MILPQEFYFE DTTLVAQSLL GKVLNIRTDS GIQKARIIET EAYLGIEDPA CHTFEDRRTE RTKSMYLDGG HSYVYMIYGM YFCLNFVTRT HQHPEAVLIR AVEPLPAQEN LRKKDLKTNG PGKLCKYYGI TRKHDGLKLW KKSSDLYVTD EDFKVSKKQI IPTARVGVDY AGEAAKWPLR FYLRDHLFVS KK // ID 3MGH_BORAP Reviewed; 186 AA. AC Q0SN86; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 12-DEC-2006, entry version 5. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=BAPKO_0442; OS Borrelia afzelii (strain PKo). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia; OC Borrelia burgdorferi group. OX NCBI_TaxID=390236; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16914037; DOI=10.1186/1471-2164-7-211; RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., RA Suehnel J., Wilske B., Platzer M.; RT "Comparative genome analysis: selection pressure on the Borrelia vls RT cassettes is essential for infectivity."; RL BMC Genomics 7:211-211(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000395; ABH01692.1; -; Genomic_DNA. DR GenomeReviews; CP000395_GR; BAPKO_0442. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 186 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265000. SQ SEQUENCE 186 AA; 21287 MW; 53D0E55B88840DF9 CRC64; MDRYFFLQDA STVAKLLLGN LLIRKIDKKE IVVRIVETEA YMGITDSACH SYSGKRTNRT NAMYNIGGYS YVYIIYGMHH MFNIVTADKN NPQAVLIRSV EPVSPLLGEK CVLTNGPGKL TKFLNIDLAF NKVDLIGNNE LFLQRGLNLD FNIVCSKRIN INYAQEDDIN KLWRFYIEGN KFVSRC // ID 3MGH_BORBU Reviewed; 186 AA. AC O51383; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 28-NOV-2006, entry version 40. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=BB_0422; OS Borrelia burgdorferi (Lyme disease spirochete). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia; OC Borrelia burgdorferi group. OX NCBI_TaxID=139; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680; RX MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., RA Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., RA Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., RA Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., RA Roberts K.M., Hatch B., Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia RT burgdorferi."; RL Nature 390:580-586(1997). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000783; AAC66797.1; -; Genomic_DNA. DR PIR; E70152; E70152. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE000783_GR; BB_0422. DR KEGG; bbu:BB0422; -. DR TIGR; BB_0422; -. DR BioCyc; BBUR139:BB0422-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 186 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100074. SQ SEQUENCE 186 AA; 21382 MW; 65D80390904825EB CRC64; MDRYFFLQDA TTVAKLLLGN LLIRKIDKEE IVTRIVETEA YMGITDSACH SYGGKITNRT SAMYRIGGYS YVYIIYGMHY MFNVVTADKN NPQAVLIRSV EPISPLLGEK SILTNGPGKL TKFLNIDLTF NKVDLIGNNE LFLQRGLNLD FNIVCSKRIN INYAQESDIN KLWRFYIKDN KFVSRR // ID 3MGH_BORGA Reviewed; 186 AA. AC Q661J6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 12-DEC-2006, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=BG0429; OS Borrelia garinii. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia; OC Borrelia burgdorferi group. OX NCBI_TaxID=29519; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PBi; RX PubMed=15547252; DOI=10.1093/nar/gkh953; RA Gloeckner G., Lehmann R., Romualdi A., Pradella S., RA Schulte-Spechtel U., Schilhabel M., Wilske B., Suehnel J., Platzer M.; RT "Comparative analysis of the Borrelia garinii genome."; RL Nucleic Acids Res. 32:6038-6046(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000013; AAU07275.1; -; Genomic_DNA. DR GenomeReviews; CP000013_GR; BG0429. DR KEGG; bga:BG0429; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 186 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265001. SQ SEQUENCE 186 AA; 21424 MW; 133C00C591ED0094 CRC64; MDRYFFLQDA TTVARLLLGN LLIRKINKKE IVARIVETEA YMGIADSACH SYGGKRTNRT NAMYSIGGYS YVYMIYGMHY MFNVVTADKN NPQAVLIRSI EPISPLLGKK SALTNGPGKL TKFLNIDLTF NKVDLIGNNE LFLQRDLNLD FNIVCSKRIN INYAQEDDIN KLWRFYIKDN KFVSRR // ID 3MGH_BRAJA Reviewed; 200 AA. AC Q89LR7; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 28-NOV-2006, entry version 23. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=bll4476; OS Bradyrhizobium japonicum. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=375; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USDA 110; RX MEDLINE=22484998; PubMed=12597275; DOI=10.1093/dnares/9.6.189; RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., RA Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., RA Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., RA Tabata S.; RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium RT Bradyrhizobium japonicum USDA110."; RL DNA Res. 9:189-197(2002). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000040; BAC49741.1; -; Genomic_DNA. DR GenomeReviews; BA000040_GR; bll4476. DR KEGG; bja:bll4476; -. DR BioCyc; BJAP224911:BLL4476-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 200 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100075. SQ SEQUENCE 200 AA; 21740 MW; 04F22C30116663D7 CRC64; MAPTSKTSPP RLGKPLKRAF FGRSVREVAH DLIGATMLVD GVGGLIVEVE AYHHTEPAAH SYNGPTPRNH VMFGPPGFAY VYRSYGIHWC VNFVCEAEGS AAAVLIRALE PTHGIAAMRR RRHLQDVHAL CSGPGKLTEA LGITIAHNAL PLDRPPIALH ARTEDLEVAT GIRIGITKAV ELPWRYGVKG SKFLSKPFPK // ID 3MGH_BURCA Reviewed; 207 AA. AC Q1BTJ3; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 23-JAN-2007, entry version 7. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Bcen_2161; OS Burkholderia cenocepacia (strain AU 1054). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331271; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., RA Konstantinidis K., Tiedje J.M., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia AU RT 1054."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000378; ABF77062.1; -; Genomic_DNA. DR GenomeReviews; CP000378_GR; Bcen_2161. DR KEGG; bcn:Bcen_2161; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 207 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265002. SQ SEQUENCE 207 AA; 22192 MW; 6F7236518CE3727A CRC64; MRRSKTAAPW PGTIVPRAFF NRMATEVAPQ LLNKILAAAD GRAGRIVEVE AYAGALDPAA HTYRGKTPRN ATMFGPPGHF YVYFTYGMHW CCNCVCGPDG AGTGVLIRAL EPLHGLEQMR AARPPRTRDR DLCRGPARLT QAMGIGGAQD GVDLVGARDG FAIVDDGMAP PADLAGGPRI GIRVGQDLPW RWSVPGNRYV SGAVPRI // ID 3MGH_BURS3 Reviewed; 207 AA. AC Q39CW7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 12-DEC-2006, entry version 11. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Bcep18194_A6105; OS Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 OS / NCIB 9086 / R18194)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=269483; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia sp. 383."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000151; ABB09699.1; -; Genomic_DNA. DR GenomeReviews; CP000151_GR; Bcep18194_A6105. DR KEGG; bur:Bcep18194_A6105; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 207 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265003. SQ SEQUENCE 207 AA; 22152 MW; DC11B7A78A7F2A90 CRC64; MRRGDPAPRW PGAVLPRAFF DRVATDVAPQ LLNKILAAAD GRAGRIVEVE AYAGAIDPAA HTYRGKTPRN ATMFGPPGHL YVYFTYGMHW CCNCVCGPDG TGTGVLIRAL EPLQGLERMR AARPPQTRDR DLCRGPARLT QAMGIGGAQD GVDLIGAHEG FAIVDDGSAP PADLAGGPRI GIRVGTDLPW RWSVPGNRYV SGPVTRR // ID 3MGH_BURXL Reviewed; 213 AA. AC Q13NQ1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 23-JAN-2007, entry version 5. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Bxeno_B1320; ORFNames=Bxe_B1678; OS Burkholderia xenovorans (strain LB400). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=266265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia xenovorans LB400."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000271; ABE34288.1; -; Genomic_DNA. DR GenomeReviews; CP000271_GR; Bxeno_B1320. DR KEGG; bxe:Bxe_B1678; -. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 213 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265004. SQ SEQUENCE 213 AA; 23453 MW; DA8E3E5370755B9B CRC64; MRNQQLPIVP LLRDELPLDT VELARFMIGK YLVRDLPEGR MSGRIVETEA YPVGDSTSHA FIGRRPYNGS LFLARGHAYV RLTYGLSYML NMSAEAEDVG AGILFRAIEP LEGLPLMEAR RPGVPLRDLA RGPGRLTTAL GIGQAFDGLD LCAGRDLWIG VLERGETLVG VTTRIGLSRE MHRPLRFFEP GSAFVSGPRK LLLTPQPGAR TRA // ID 3MGH_CARHZ Reviewed; 191 AA. AC Q3ABT8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CHY_1567; OS Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Carboxydothermus. OX NCBI_TaxID=246194; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065; RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., RA Eisen J.A.; RT "Life in hot carbon monoxide: the complete genome sequence of RT Carboxydothermus hydrogenoformans Z-2901."; RL PLoS Genet. 1:563-574(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000141; ABB15839.1; -; Genomic_DNA. DR GenomeReviews; CP000141_GR; CHY_1567. DR KEGG; chy:CHY_1567; -. DR TIGR; CHY_1567; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 191 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265005. SQ SEQUENCE 191 AA; 21399 MW; 0F5B9DC72F834B57 CRC64; MLLPRQFYAR DVLIVAKDLL NCYLVREYNG HLLIGKIVET EAYHQNDPAC HAYRGKTKRN EVMFGPPGHA YVYFTYGMHY CFNVVTGAIG RAEAVLIRAL EPVKGIDIIK TLRGGKSERE LLSGPAKLTQ GLAIDLKLNG HDLTGGKILY ITKGEPVAEE DIVVTTRIGI NAGKDLPYRF YLKNNKYVSK K // ID 3MGH_CHLAB Reviewed; 190 AA. AC Q5L6N0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 1. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CAB235; OS Chlamydophila abortus. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila. OX NCBI_TaxID=83555; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S26/3; RX PubMed=15837807; DOI=10.1101/gr.3684805; RA Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., RA Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., RA Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., RA Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.; RT "The Chlamydophila abortus genome sequence reveals an array of RT variable proteins that contribute to interspecies variation."; RL Genome Res. 15:629-640(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR848038; CAH63691.1; -; Genomic_DNA. DR GenomeReviews; CR848038_GR; CAB235. DR KEGG; cab:CAB235; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 190 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265006. SQ SEQUENCE 190 AA; 21978 MW; B879A30895B10A7C CRC64; MLPESFFLND DVLYLAKELL GHVLVTHLEG QRTSGIIIET EAYRGPEDKA CHAYNYRKTQ RNLPMYSRGG IAYIYRCYGM HSLFNVVTGH QDLPHAVLIR AILPYEGEDI MVLRRQWQNK PKHLLTNGPG KVCQALNLTL EYNTHSLSSP QIHISKKKFS GTITQKPRIG IDYAQEYRDL PWRFLLHIKN // ID 3MGH_CHLCH Reviewed; 203 AA. AC Q3APM2; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 12-DEC-2006, entry version 12. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Cag_1802; OS Chlorobium chlorochromatii (strain CaD3). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=340177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Chlorobium chlorochromatii CaD3."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000108; ABB29053.1; -; Genomic_DNA. DR GenomeReviews; CP000108_GR; Cag_1802. DR KEGG; cch:Cag_1802; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 203 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265008. SQ SEQUENCE 203 AA; 22532 MW; 50A3A3890D152D43 CRC64; MEPLPKQFYQ CSTIELTEKL LGKCFVRILP NGTRLAGRIV ETEAYLGEGD EACHAWRSRT PRNEIMFREA GTLYVYFTYG AHYMLNIVSE PEERAGAVLI RAMEPLEGIE FMQQQRNTTK FPNLMSGPGK LTQALAIERS CNGRTLFDGE FFVADAPAIP SHQIGTSGRI GISRSTELPW RKFIMGNAHV SGGKVGGVVS SLQ // ID 3MGH_CHLCV Reviewed; 190 AA. AC Q824B4; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 28-NOV-2006, entry version 23. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CCA_00239; OS Chlamydophila caviae. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila. OX NCBI_TaxID=83557; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GPIC; RX MEDLINE=22569155; PubMed=12682364; DOI=10.1093/nar/gkg321; RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., RA Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., RA White O., Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., RA Bavoil P.M., Fraser C.M.; RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): RT examining the role of niche-specific genes in the evolution of the RT Chlamydiaceae."; RL Nucleic Acids Res. 31:2134-2147(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015925; AAP04990.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE015925_GR; CCA_00239. DR KEGG; cca:CCA00239; -. DR TIGR; CCA_00239; -. DR BioCyc; CCAV227941:CCA00239-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 190 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100076. SQ SEQUENCE 190 AA; 21748 MW; 904EDA7A10661DE6 CRC64; MLPESFFLHD DVLHLAKELL GHILITKISG KITSGFIVET EAYRGPDDKA CHAYNYRKTK RNSPMYSRGG IAYIYRCYGM HSLFNVVTAK QDLPHAVLIR AILPYEGEDI MIQRRQWQNK PKHLLTNGPG KVCQALNLTL EHNTHALTSP HLHISKEKAS GRITQTPRIG IDYAEECKDL PWRFLLNIKD // ID 3MGH_CHLFF Reviewed; 194 AA. AC Q253J9; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CF0767; OS Chlamydophila felis (strain Fe/C-56). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila. OX NCBI_TaxID=264202; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16766509; DOI=10.1093/dnares/dsi027; RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., RA Fukushi H., Hattori M., Kuhara S., Shirai M.; RT "Genome sequence of the cat pathogen, Chlamydophila felis."; RL DNA Res. 13:15-23(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006861; BAE81539.1; -; Genomic_DNA. DR GenomeReviews; AP006861_GR; CF0767. DR KEGG; cfe:CF0767; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 194 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265007. SQ SEQUENCE 194 AA; 22111 MW; DAB210092B99781B CRC64; MLPESFFLND DVLYLAKELL GHSLVTQIEG KTTSGIIIET EAYRGPDDKA CHAYNYRKTQ RNLPMYSRGG IAYIYQCYGM HALFNVVTGS QNLPHAVLIR AIAPQKGEDI MIQRRQWQNK PKHLLTNGPG KVCQALNLTL EHNTQSLTSP QIHISQKKIS GTITQTPRIG IDYAEEYRDL PWRFLLNIKK SKKI // ID 3MGH_CHLPN Reviewed; 196 AA. AC Q9Z847; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 28-NOV-2006, entry version 43. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CPn_0505, CP_0248, CPj0505, CpB0526; OS Chlamydia pneumoniae (Chlamydophila pneumoniae). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila. OX NCBI_TaxID=83558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CWL029; RX MEDLINE=99206606; PubMed=10192388; DOI=10.1038/7716; RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.; RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis."; RL Nat. Genet. 21:385-389(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AR39; RX MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., RA White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., RA Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., RA Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., RA McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia RT pneumoniae AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J138; RX MEDLINE=20330349; PubMed=10871362; DOI=10.1093/nar/28.12.2311; RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.; RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 RT from Japan and CWL029 from USA."; RL Nucleic Acids Res. 28:2311-2314(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW-183; RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.; RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with RT other Chlamydia strains based on whole genome sequence analysis."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001363; AAD18645.1; -; Genomic_DNA. DR EMBL; AE002161; AAF38112.1; -; Genomic_DNA. DR EMBL; BA000008; BAA98711.1; -; Genomic_DNA. DR EMBL; AE017158; AAP98455.1; -; Genomic_DNA. DR PIR; C72071; C72071. DR PIR; E86553; E86553. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE002161_GR; CP_0248. DR GenomeReviews; AE009440_GR; CpB0526. DR GenomeReviews; BA000008_GR; CPj0505. DR GenomeReviews; AE001363_GR; CPn_0505. DR KEGG; cpa:CP0248; -. DR KEGG; cpj:CPj0505; -. DR KEGG; cpn:CPn0505; -. DR KEGG; cpt:CpB0526; -. DR TIGR; CP_0248; -. DR BioCyc; CPNE115711:CP0248-MONOMER; -. DR BioCyc; CPNE115713:CPN0505-MONOMER; -. DR BioCyc; CPNE138677:CPJ0505-MONOMER; -. DR BioCyc; CPNE182082:CPB0526-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 196 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100077. SQ SEQUENCE 196 AA; 22291 MW; 060CA47EF76970DE CRC64; MLQEHFFLSE DVITLAQQLL GHKLITTHEG LITSGYIVET EAYRGPDDKA CHAYNYRKTQ RNRAMYLKGG SAYLYRCYGM HHLLNVVTGP EDIPHAVLIR AILPDQGKEL MIQRRQWRDK PPHLLTNGPG KVCQALGISL ENNRQRLNTP ALYISKEKIS GTLTATARIG IDYAQEYRDV PWRFLLSPED SGKVLS // ID 3MGH_CHLTE Reviewed; 209 AA. AC Q8KBD5; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 28-NOV-2006, entry version 28. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CT1853; OS Chlorobium tepidum. OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=1097; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / TLS; RX MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., RA Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., RA Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., RA Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., RA Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., RA Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a RT photosynthetic, anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006470; AAM73073.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE006470_GR; CT1853. DR KEGG; cte:CT1853; -. DR TIGR; CT1853; -. DR BioCyc; CTEP194439:CT1853-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 209 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100078. SQ SEQUENCE 209 AA; 23160 MW; B7FE6B878509BF44 CRC64; MKRLGADFYQ MPTILLAERL LGKIFVHHEV SGRVTKGRIV ETEAYLGDGD EACHAWRGMT ERNHVMFGPP GHLYIYFSYG CHYLANIVSE QKGIAGAVLL RAMEPIEGIE WMQERRGTTD ERALMSGPGK LTQALGLGPA HYGESLLGDI CWLEEAPDIP PELIGTSPRI GISRSTDLLW RKFIAGSPYI SKTQPGPPPK KRKKGLESS // ID 3MGH_CLOAB Reviewed; 205 AA. AC Q97EY6; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 28-NOV-2006, entry version 32. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CA_C2969; OS Clostridium acetobutylicum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX MEDLINE=21359325; PubMed=11466286; RX DOI=10.1128/JB.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., RA Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., RA Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., RA Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001437; AAK80911.1; -; Genomic_DNA. DR PIR; D97265; D97265. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE001437_GR; CA_C2969. DR KEGG; cac:CAC2969; -. DR BioCyc; CACE1488:CAC2969-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100079. SQ SEQUENCE 205 AA; 23505 MW; A1E575C01454CE55 CRC64; MKLIREFYSR DTIVVAKELL GKVLVHEVNG IRTSGKIVEV EAYRGINDKG AHAYGGRRTP RTEALYGPAG HAYVYFIYGL YYCMNVVAMQ EGIPEGVLIR AIEPIEGIEV MSERRFKKLF NDLTKYQLKN LTNGPSKLCS AMEIRREQNL MDLNGDELYI EEGKNESFEI VEAKRVGIDY AEEAKDYLWR FYIKGNKCVS VLKKD // ID 3MGH_CLOD6 Reviewed; 202 AA. AC Q18C13; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 12-DEC-2006, entry version 6. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CD1493; OS Clostridium difficile (strain 630). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272563; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16804543; DOI=10.1038/ng1830; RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A., RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., RA Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a RT highly mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM180355; CAJ68358.1; -; Genomic_DNA. DR GenomeReviews; AM180355_GR; CD1493. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265009. SQ SEQUENCE 202 AA; 23472 MW; ED208014FFF83DC3 CRC64; MEKDFFRKNG IDLAKSILGK YLIRKYENKV IVTKIIETEA YMGVNDKGAH VYGNKKTDRT KPLYLDGGHI YVYLIYGMYN CLNLSANIEN VPECVLIRGV EPITSLDEIS MNRYNKAYTE LSKYQVKNIT NGPGKLCKAL KIDRSLNSKS IMGEELYISD FYYDDKGKKV FSKDELDIKT SKRINIDYAE EAKDFLWRFY IE // ID 3MGH_CLOP1 Reviewed; 205 AA. AC Q0TM75; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 23-JAN-2007, entry version 7. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CPF_2901; OS Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000246; ABG83330.1; -; Genomic_DNA. DR GenomeReviews; CP000246_GR; CPF_2901. DR KEGG; cpf:CPF_2901; -. DR TIGR; CPF_2901; -. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265010. SQ SEQUENCE 205 AA; 23321 MW; 42B89267BCC74EF6 CRC64; MRLGRDFYNR DTLTVAKELL GKVLVRKING VTLKGKIVET EAYIGAIDKA SHAYGGKRTN RTETLYADPG TVYVYIIYGM YHCLNLISEE KDVAGGVLIR GIEPLEGIEE MSKLRYKKSY EELSSYEKKN FSNGPSKLCM ALGIDKGENG INTISSEEIY VEDDSLIKKD FPIVEAKRIG IDYAEEARDF LWRFYIKDNK FVSKK // ID 3MGH_CLOPE Reviewed; 205 AA. AC Q8XHA9; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 1. DT 28-NOV-2006, entry version 28. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CPE2576; OS Clostridium perfringens. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1502; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13 / Type A; RX MEDLINE=21664373; PubMed=11792842; DOI=10.1073/pnas.022493799; RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., RA Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.; RT "Complete genome sequence of Clostridium perfringens, an anaerobic RT flesh-eater."; RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000016; BAB82282.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR GenomeReviews; BA000016_GR; CPE2576. DR KEGG; cpe:CPE2576; -. DR BioCyc; CPER1502:CPE2576-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100080. SQ SEQUENCE 205 AA; 23310 MW; 2C776FBEED2F9D3E CRC64; MRLGRDFYNR DTVTVAKELL GKVLVRNING VTLKGKIVET EAYIGAIDKA SHAYGGKRTN RTETLYADPG TVYVYIIYGM YHCLNLISEE KDVAGGVLIR GIEPLEGIEE MSKLRYKKSY EELSNYEKKN FSNGPSKLCM ALGIDKGENG INTISSEEIY VEDDSLIKKD FSIVEAKRIG IDYAEEARDF LWRFYIKDNK FVSKK // ID 3MGH_CLOPS Reviewed; 205 AA. AC Q0SPY0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 23-JAN-2007, entry version 7. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CPR_2580; OS Clostridium perfringens (strain SM101 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=289380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000312; ABG86465.1; -; Genomic_DNA. DR GenomeReviews; CP000312_GR; CPR_2580. DR KEGG; cpr:CPR_2580; -. DR TIGR; CPR_2580; -. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265011. SQ SEQUENCE 205 AA; 23327 MW; DE452A1895785BD7 CRC64; MRLGRDFYNR DTLTVAKELL GKVLVRNING VTLKGKIVET EAYIGAIDKA SHAYGGKRTN RTETLYADPG TVYVYIIYGM YHCLNLISEE KDVAGGVLIR GIEPLEGIEE MSKLRYRKNY EELSSYEKKN FSNGPSKLCM ALGIDKGENG INTISSEEIY VEDDSSIKED FSIVEAKRIG IDYAEEARDF LWRFYIKDNK FVSKK // ID 3MGH_CLOTE Reviewed; 203 AA. AC Q896H4; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 28-NOV-2006, entry version 23. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CTC_01030; OS Clostridium tetani. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1513; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Massachusetts / E88; RX MEDLINE=22457253; PubMed=12552129; DOI=10.1073/pnas.0335853100; RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., RA Gottschalk G.; RT "The genome sequence of Clostridium tetani, the causative agent of RT tetanus disease."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015927; AAO35616.1; -; Genomic_DNA. DR GenomeReviews; AE015927_GR; CTC_01030. DR KEGG; ctc:CTC01030; -. DR BioCyc; CTET212717:CTC01030-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 203 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100081. SQ SEQUENCE 203 AA; 23246 MW; 3BE32C0A04A73E96 CRC64; MKIQRKFYEK SALQVAKYLL GKILVNEVEG ITLKGKIVET EAYIGAIDKA SHAYGGKKTE RVMPLYGKPG TAYVYLIYGM YHCFNVITKV EGEAEGVLIR AIEPLEGIEK MAYLRYKKPI SEISKTQFKN LTTGPGKLCI ALNIDKSNNK QDLCNEGTLY IEHNDKEKFN IVESKRIGIE YAEEAKDFLW RFYIEDNPWI SKK // ID 3MGH_COREF Reviewed; 190 AA. AC Q8FUA2; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2004, sequence version 2. DT 28-NOV-2006, entry version 24. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CE0119; OS Corynebacterium efficiens. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=152794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX MEDLINE=22723752; PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., RA Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., RA Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000035; BAC16929.1; ALT_INIT; Genomic_DNA. DR GenomeReviews; BA000035_GR; CE0119. DR KEGG; cef:CE0119; -. DR BioCyc; CEFF196164:CE0119-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 190 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100082. SQ SEQUENCE 190 AA; 20523 MW; 1C59498FB8F8DA06 CRC64; MPIDFLQPAD IVAPQLLGCI FTHDGVSIRL TEVEAYLGAE DAAAHTHRGK TARNAAMFGP GGHMYIYISY GIHRAGNIAC APEGVGQGVL LRAGEVVAGE DIAYRRRGDV PFTRLAQGPG NLGQALNFQL SDNHAPINGT DFQLMEPSER PEWVSGPRVG ITKNADAPLR FWIPGDPTVS VRRGRPKTRK // ID 3MGH_CORGL Reviewed; 189 AA. AC Q8NU33; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2004, sequence version 2. DT 28-NOV-2006, entry version 29. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN Name=mag; OrderedLocusNames=Cgl0116, cg0151; OS Corynebacterium glutamicum (Brevibacterium flavum). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1718; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RA Nakagawa S.; RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., RA Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence RT and its impact on the production of L-aspartate-derived amino acids RT and vitamins."; RL J. Biotechnol. 104:5-25(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000036; BAB97509.1; ALT_INIT; Genomic_DNA. DR EMBL; BX927148; CAF18684.1; -; Genomic_DNA. DR HSSP; P29372; 1F4R. DR GenomeReviews; BX927147_GR; cg0151. DR GenomeReviews; BA000036_GR; Cgl0116. DR KEGG; cgb:cg0151; -. DR KEGG; cgl:NCgl0115; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 189 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100083. SQ SEQUENCE 189 AA; 20162 MW; 0752BA7C882D746C CRC64; MPIDFLQPAD IVAPQLLGCT LTHGGVGIRI TEVEAYLDST DEAAHTYRGK TPRNAAMFGP GGHMYVYISY GIHRAGNIVC GPEGTGQGVL LRAGEVVSGE SIAQSRRGEG IPHARLAQGP GNFGQALGLE ISDNHASVFG PSFLISDRVE TPEIVRGPRI GISKNTEALL RFWIPNDPTV SGRRGYPKE // ID 3MGH_CORJK Reviewed; 213 AA. AC Q4JYA4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 12-DEC-2006, entry version 11. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=jk0054; OS Corynebacterium jeikeium (strain K411). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=306537; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005; RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., RA Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., RA Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., RA Puehler A.; RT "Complete genome sequence and analysis of the multiresistant RT nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring RT bacterium of the human skin flora."; RL J. Bacteriol. 187:4671-4682(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR931997; CAI36203.1; -; Genomic_DNA. DR GenomeReviews; CR931997_GR; jk0054. DR KEGG; cjk:jk0054; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 213 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265012. SQ SEQUENCE 213 AA; 22220 MW; 559A46002634C52D CRC64; MDRSAQRIDF TQPADVVAPL LLGAVLRHGG VAIELTEVEA YLGTADEASH AFNGPTPRCE VMFGPPQHLY VYASYGIHRA GNLVCSPDGE AGGVLLRAGK IIEGLDIARA RRGSKPADEA LARGPGNLGA ALGLNLDLNG SAVDQVFSGA GDSSPTSAPF TLTPRTAIPE ITRGKRIGIS KNADALLRFW VPGDRSVSSP RGRQLGTPLR ASS // ID 3MGH_CYTH3 Reviewed; 198 AA. AC Q11UN5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 23-JAN-2007, entry version 6. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CHU_1611; OS Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469). OC Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales; OC Flexibacteraceae; Cytophaga. OX NCBI_TaxID=269798; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Challacombe J.F., Chertkov O., RA Han S., Tapia R., McBride M.J., Misra M., Myers G.L., Thayer N.N., RA Thompson L.S., Xie G., Gilna P., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Ivanova N., Mavrommatis K., RA Rubin E., Richardson P.; RT "Complete sequence of Cytophaga hutchinsonii ATCC 33406."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000383; ABG58881.1; -; Genomic_DNA. DR GenomeReviews; CP000383_GR; CHU_1611. DR KEGG; chu:CHU_1611; -. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 198 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265013. SQ SEQUENCE 198 AA; 22581 MW; 7FF9375C752B8BC3 CRC64; MFPKLSESFY LRENVQLISK ELLGKVLVTY IDGKYTAGII TETEAYQAPE DKASHAFNNR RTTRTEVFYN KGGIGYVYLC YGIHHLFNVV TNNENIPHAI LIRSVEPLEG VDIMMQRRNK KKLDKTLTAG PGALSQALGI TRLHNKIPLS ANTVWIEDRN IPVESIVSTT RVGIDYAQEY KDKPWRYYIA GNKWISRG // ID 3MGH_DEIGD Reviewed; 209 AA. AC Q1IXS9; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 12-DEC-2006, entry version 7. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Dgeo_1660; OS Deinococcus geothermalis (strain DSM 11300). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=319795; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., RA Zhai M., Richardson P.; RT "Complete sequence of chromosome of geothermalis DSM 11300."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000359; ABF45955.1; -; Genomic_DNA. DR GenomeReviews; CP000359_GR; Dgeo_1660. DR KEGG; dge:Dgeo_1660; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 209 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265014. SQ SEQUENCE 209 AA; 22298 MW; E123619F1A68BE1F CRC64; MATPLSPAFF DRDPVKVARE VLGSTLVRVL PGGEVLSGRV VEVEAYDCPR DPACTAGRFH AARTAEMAIS PGHWLFWTAH GHPLLQVSCR EKGIPASILI RALEPLTGLG SMLTHRPVSR ERELTNGPAK LVSALGLKPA EVVGTRVDSP ALHLLPPPAL LPADAVTVTA RIGIKEGRNL PWRFLLRGNP WVSPGVPSMD LAGPLTAKS // ID 3MGH_DEIRA Reviewed; 190 AA. AC Q9RSQ0; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 28-NOV-2006, entry version 39. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=DR_2074; OS Deinococcus radiodurans. OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=1299; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1; RX MEDLINE=20036896; PubMed=10567266; DOI=10.1126/science.286.5444.1571; RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C., RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., RA Fraser C.M.; RT "Genome sequence of the radioresistant bacterium Deinococcus RT radiodurans R1."; RL Science 286:1571-1577(1999). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000513; AAF11623.1; -; Genomic_DNA. DR PIR; D75319; D75319. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE000513_GR; DR_2074. DR KEGG; dra:DR2074; -. DR TIGR; DR_2074; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 190 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100085. SQ SEQUENCE 190 AA; 20819 MW; 05264B48A76BF6B2 CRC64; MRLARELLGG TLVRVTPDGH RLSGRVVEVE AYDCPRDPAC TAGRFHAARS AEMAIAPGHW LFWFAHGHPL LQVACRQEGV SASVLIRALE PLEGAGKMLD YRPVTRQRDL TSGPAKLVYA LGLDPMQISH RPVNSPELHL LAPETPLADD EVTVTARVGI REGRNLPWRF LIRGNGWVSP AQPSMELAAP // ID 3MGH_DESHY Reviewed; 203 AA. AC Q24R48; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=DSY3705; OS Desulfitobacterium hafniense (strain Y51). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=138119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006; RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., RA Inatomi K., Furukawa K., Inui M., Yukawa H.; RT "Complete genome sequence of the dehalorespiring bacterium RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides RT ethenogenes 195."; RL J. Bacteriol. 188:2262-2274(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008230; BAE85494.1; -; Genomic_DNA. DR GenomeReviews; AP008230_GR; DSY3705. DR KEGG; dsy:DSY3705; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 203 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265015. SQ SEQUENCE 203 AA; 22969 MW; 4D3DE5AE5E8614FB CRC64; MKRLGREFYN RDSLIVAREL LGKVLVHEIE GQKVSARIVE TEAYRGIEDK AAHSYGGKRT PRVEVMYGGP GFSYVFIVYG MHYCFNVVTR EEGNPQAVLI RAAEPREGSE LMAQNRFKKS YHQLNKSQIL GLTNGPGKLC RALSIDKSLN GEDLCGSKLY VAEESQESLS IVTAKRVGID YAEEAKDYPW RFYLEDSQYV SVK // ID 3MGH_EHRCJ Reviewed; 189 AA. AC Q3YR73; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 12-DEC-2006, entry version 13. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Ecaj_0750; OS Ehrlichia canis (strain Jake). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=269484; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16707693; DOI=10.1128/JB.01837-05; RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., RA Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., RA Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., RA Kyrpides N.C.; RT "The genome of the obligately intracellular bacterium Ehrlichia canis RT reveals themes of complex membrane structure and immune evasion RT strategies."; RL J. Bacteriol. 188:4015-4023(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000107; AAZ68782.1; -; Genomic_DNA. DR GenomeReviews; CP000107_GR; Ecaj_0750. DR KEGG; ecn:Ecaj_0750; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 189 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265016. SQ SEQUENCE 189 AA; 21645 MW; 26A680FE80F46763 CRC64; MQYNILKKSF YAQQSLDVAE KLLGKKLLFN KHQGIITETE AYIGHDDPAA HSSHGYTKRT SVMFGDPGFS YVYFIYGMYH CLNVVTEPRG FPAAVLIRGI VLLLEDQPNI IINGPGKLCK ILHITKEHNN IDMTQNYNFC ICNTGINIHN YICTPRIGIS RGKEKFWRFV VSDLTFLQHL KLENKVYSI // ID 3MGH_EHRCR Reviewed; 180 AA. AC Q2GHI5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=ECH_0277; OS Ehrlichia chaffeensis (strain Arkansas). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=205920; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., RA Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., RA Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., RA Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., RA Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., RA Forberger H., Halpin R., Mulligan S., Robinson J., White O., RA Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:E21-E21(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000236; ABD44538.1; -; Genomic_DNA. DR GenomeReviews; CP000236_GR; ECH_0277. DR KEGG; ech:ECH_0277; -. DR TIGR; ECH_0277; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 180 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265017. SQ SEQUENCE 180 AA; 20405 MW; 71222BBE8A164586 CRC64; MPHYILKKSF YEQSSLTVAG KLLGKKLLFN QHQGIITETE AYIGQDDPAA HSARGYTKRT SVMFGSPGFS YVYFIYGMYY CLNVVTEQEG FPAAVLIRGI VLLSENKPNT IINGPGKLCK ILQITKEHNN TDITQKYNFC ICNTDINIDN YICTPRIGIS KGKEKFWRFV IPDLTFLLNV // ID 3MGH_EHRRG Reviewed; 188 AA. AC Q5FG73; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 12-DEC-2006, entry version 14. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=ERGA_CDS_07460; OS Ehrlichia ruminantium (strain Gardel). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=302409; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006; RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., RA Martinez D.; RT "Comparative genomic analysis of three strains of Ehrlichia RT ruminantium reveals an active process of genome size plasticity."; RL J. Bacteriol. 188:2533-2542(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR925677; CAI28198.1; -; Genomic_DNA. DR GenomeReviews; CR925677_GR; ERGA_CDS_07460. DR KEGG; erg:ERGA_CDS_07460; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 188 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265018. SQ SEQUENCE 188 AA; 21226 MW; 98CE6C22BDCB0CBE CRC64; MYNILKKSFY KQKSLDVASS LLGKMLLFNQ HKGIITETEA YIGQDDQAAH SFHGYTKRTA VMFGNPGFSY VYLIYGMYHC LNVVTEPEGF PAAILIRSII LLSKNTPHTK VNGPGKICKI LHITKEHNNI DMTANHSFCI CDTNLNIDDY ICTPRIGISK ATDKFWRLVI PNVTSLQYID TKLVCTLT // ID 3MGH_EHRRU Reviewed; 188 AA. AC Q93FQ6; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 28-NOV-2006, entry version 27. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). OS Ehrlichia ruminantium (Cowdria ruminantium). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=779; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Highway; RX MEDLINE=21472264; PubMed=11587856; DOI=10.1016/S0378-1119(01)00682-5; RA Barbet A.F., Whitmire W.M., Kamper S.M., Simbi B.H., Ganta R.R., RA Moreland A.L., Mwangi D.M., McGuire T.C., Mahan S.M.; RT "A subset of Cowdria ruminantium genes important for immune RT recognition and protection."; RL Gene 275:287-298(2001). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF308674; AAL08847.1; -; Genomic_DNA. DR HSSP; P29372; 1F4R. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW DNA damage; DNA repair; Hydrolase. FT CHAIN 1 188 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100084. SQ SEQUENCE 188 AA; 21242 MW; FB316C3B71479487 CRC64; MYNILKKSFY KQKSLDVASS LLGKMLLFNQ HKGIITETEA YIGQDDQAAH SFHGYTKRTA VMFGNPGFSY VYLIYGMYHC LNVVTEPEGF PAAILIRSII LLSKNTPHTK VNGPGKICKT LHITKEHNNI DMTANHSFCI CNTNLNIDDY ICTPRIGISK ATDKFWRFVI PDVTSLQYID TKLVPTLT // ID 3MGH_EHRRW Reviewed; 188 AA. AC Q5HAG4; Q5FDK1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 12-DEC-2006, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Erum7170, ERWE_CDS_07540; OS Ehrlichia ruminantium (strain Welgevonden). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=254945; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15637156; DOI=10.1073/pnas.0406633102; RA Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., RA Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., RA Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., RA Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., RA Allsopp M.T., Allsopp B.A.; RT "The genome of the heartwater agent Ehrlichia ruminantium contains RT multiple tandem repeats of actively variable copy number."; RL Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006; RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., RA Martinez D.; RT "Comparative genomic analysis of three strains of Ehrlichia RT ruminantium reveals an active process of genome size plasticity."; RL J. Bacteriol. 188:2533-2542(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR767821; CAH58449.1; -; Genomic_DNA. DR EMBL; CR925678; CAI27248.1; -; Genomic_DNA. DR GenomeReviews; CR767821_GR; Erum7170. DR GenomeReviews; CR925678_GR; ERWE_CDS_07540. DR KEGG; eru:Erum7170; -. DR KEGG; erw:ERWE_CDS_07540; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 188 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265019. SQ SEQUENCE 188 AA; 21233 MW; 95A3077020AD27FE CRC64; MYNILKKSFY KQKSLDVASS LLGKMLLFNQ HKGIITETEA YIGQDDQAAH SFHGYTKRTA VMFGNPGFSY VYLIYGMYHC LNVVTEPEGF PAAILIRSII LLSKNTPHTK VNGPGKICKI LDITKEHNNI DMTANHSFCI CDTNLNIDDY ICTPRIGISK ATDKFWRFVI PDVTSLQYID TKLVPTLT // ID 3MGH_ENTFA Reviewed; 229 AA. AC Q833H5; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 28-NOV-2006, entry version 23. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=EF_1978; OS Enterococcus faecalis (Streptococcus faecalis). OC Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus. OX NCBI_TaxID=1351; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=V583 / ATCC 700802; RX MEDLINE=22550857; PubMed=12663927; DOI=10.1126/science.1080613; RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., RA Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., RA Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., RA Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., RA Fraser C.M.; RT "Role of mobile DNA in the evolution of vancomycin-resistant RT Enterococcus faecalis."; RL Science 299:2071-2074(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016830; AAO81724.1; -; Genomic_DNA. DR GenomeReviews; AE016830_GR; EF_1978. DR KEGG; efa:EF1978; -. DR TIGR; EF_1978; -. DR BioCyc; EFAE226185:EF1978-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 229 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100086. SQ SEQUENCE 229 AA; 25762 MW; E9DA349FA8612962 CRC64; MVKEMKETIN IFNTKTTEEV AQYLLGMYLE HETATGVLGG YIVDAEAYLG PDDEAAHSFG LRKTPRLQAM YDKPGTIYLY TMHTHLILNM VTQEQGKPQG VMIRAIEPVE GVDKMIENRQ GRQGVELTNG PGKLVAALGI DKQLYGQSIF SSSLRLVPEK RKFPKKIEAL PRIGIPNKGR WTELPLRYVV AGNPYISKQK RTAVDQIDFG WKDEENEKSN NAHILRGTT // ID 3MGH_FRASC Reviewed; 212 AA. AC Q2J868; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 23-JAN-2007, entry version 11. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Francci3_3167; OS Frankia sp. (strain CcI3). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=106370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., RA Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., RA Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L., RA Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., RA Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., RA Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., RA Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000249; ABD12524.1; -; Genomic_DNA. DR GenomeReviews; CP000249_GR; Francci3_3167. DR KEGG; fra:Francci3_3167; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 212 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265024. SQ SEQUENCE 212 AA; 21891 MW; 71D190EFD32B1AE5 CRC64; MAPTDGAAPD GVDFYDRPVL AVAPALLGAT VWHGPVAVRI TEVEAYGGLD DPASHAYRGP TPRAAVMFGP PGRAYVYLSY GVHWCLNVVC GPVGSASAVL LRSGEVVAGR DLVAGRFPRL VEADLARGPG RLGRALAVTG ALSGTTITGP GPVTVALAGG RGIRPPGPPG ISGGRVRRGP RAGIRVATEW PWRFWLAGEA TVSGPRPPRR PR // ID 3MGH_FRAT1 Reviewed; 193 AA. AC Q14IG1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 12-DEC-2006, entry version 5. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=FTF0666c; OS Francisella tularensis subsp. tularensis (strain FSC 198). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=393115; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Chaudhuri R.R., Ren C.P., Desmond L., Vincent G.A., Silman N.J., RA Brehm J., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., RA Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.; RT "The complete genome sequence of the European Francisella tularensis RT subspecies tularensis isolate FSC 198 suggests that it is derived from RT the archetypal laboratory strain Schu S4, originally isolated in North RT America."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM286280; CAL08682.1; -; Genomic_DNA. DR GenomeReviews; AM286280_GR; FTF0666c. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 193 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265023. SQ SEQUENCE 193 AA; 21912 MW; B669A04AADA610A3 CRC64; MNNLEAILRL KTIDAAKKLL GHFLVSKYNN KILIGKIVET EAYLYNDPAC HSYSNRTKRN SMMYAQAGTS YVYFTYGMHY CFNVVTADVG IGEAILIRAL EPIAGIEQMQ LNRSKTKLMD LCSGPAKLTQ ALNINLKDNG INLLDKDSSI LLRYNNDLIN EIDIVQTQRI GISKAKDMPY RFYIKDNIFV SKK // ID 3MGH_FRATH Reviewed; 193 AA. AC Q2A3P9; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 1. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=FTL_0940; OS Francisella tularensis subsp. holarctica (strain LVS). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=376619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S., RA Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R., RA Garcia E.; RT "Complete genome sequence of Francisella tularensis LVS (Live Vaccine RT Strain)."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM233362; CAJ79379.1; -; Genomic_DNA. DR GenomeReviews; AM233362_GR; FTL_0940. DR KEGG; ftl:FTL_0940; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 193 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265020. SQ SEQUENCE 193 AA; 21894 MW; B669A55BB9A301B7 CRC64; MNNLEAILRL KTIDAAKKLL GHFLVSKYNN KILIGKIVET EAYLYNDPAC HSYSNRTKRN SMMYAQAGTS YVYFTYGMHY CFNVVTADVG IGEAILIRAL EPIAGIEQMQ LNRSKTKLID LCSGPAKLTQ ALNINLKDNG INLLDKDSSI LLRYNNDLIN EIDIVQTQRI GISKAKDMPY RFYIKDNIFV SKK // ID 3MGH_FRATO Reviewed; 193 AA. AC Q0BM56; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 12-DEC-2006, entry version 4. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=FTH_0919; OS Francisella tularensis subsp. holarctica (strain OSU18). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=393011; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16980500; DOI=10.1128/JB.00506-06; RA Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S., RA Liu Y., Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A., RA Fox G.E., Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D., RA Weinstock G.M.; RT "Chromosome rearrangement and diversification of Francisella RT tularensis revealed by the type B (OSU18) genome sequence."; RL J. Bacteriol. 188:6977-6985(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000437; ABI82828.1; -; Genomic_DNA. DR GenomeReviews; CP000437_GR; FTH_0919. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 193 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265021. SQ SEQUENCE 193 AA; 21894 MW; B669A55BB9A301B7 CRC64; MNNLEAILRL KTIDAAKKLL GHFLVSKYNN KILIGKIVET EAYLYNDPAC HSYSNRTKRN SMMYAQAGTS YVYFTYGMHY CFNVVTADVG IGEAILIRAL EPIAGIEQMQ LNRSKTKLID LCSGPAKLTQ ALNINLKDNG INLLDKDSSI LLRYNNDLIN EIDIVQTQRI GISKAKDMPY RFYIKDNIFV SKK // ID 3MGH_FRATT Reviewed; 193 AA. AC Q5NH09; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 12-DEC-2006, entry version 14. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=FTT0666c; OS Francisella tularensis subsp. tularensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=119856; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCHU S4 / Schu 4; RX PubMed=15640799; DOI=10.1038/ng1499; RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., RA Fuxelius H.-H., Garcia E., Haelltorp G., Johansson D., Isherwood K.E., RA Karp P.D., Larsson E., Liu Y., Michell S., Prior J., Prior R., RA Malfatti S., Sjoestedt A., Svensson K., Thompson N., Vergez L., RA Wagg J.K., Wren B.W., Lindler L.E., Andersson S.G.E., Forsman M., RA Titball R.W.; RT "The complete genome sequence of Francisella tularensis, the causative RT agent of tularemia."; RL Nat. Genet. 37:153-159(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ749949; CAG45299.1; -; Genomic_DNA. DR GenomeReviews; AJ749949_GR; FTT0666c. DR KEGG; ftu:FTT0666c; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 193 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265022. SQ SEQUENCE 193 AA; 21912 MW; B669A04AADA610A3 CRC64; MNNLEAILRL KTIDAAKKLL GHFLVSKYNN KILIGKIVET EAYLYNDPAC HSYSNRTKRN SMMYAQAGTS YVYFTYGMHY CFNVVTADVG IGEAILIRAL EPIAGIEQMQ LNRSKTKLMD LCSGPAKLTQ ALNINLKDNG INLLDKDSSI LLRYNNDLIN EIDIVQTQRI GISKAKDMPY RFYIKDNIFV SKK // ID 3MGH_GLOVI Reviewed; 214 AA. AC Q7NHP4; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 28-NOV-2006, entry version 23. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=gll2491; OS Gloeobacter violaceus. OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacter. OX NCBI_TaxID=33072; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7421; RX MEDLINE=22977040; PubMed=14621292; DOI=10.1093/dnares/10.4.137; RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a RT cyanobacterium that lacks thylakoids."; RL DNA Res. 10:137-145(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000045; BAC90432.1; -; Genomic_DNA. DR GenomeReviews; BA000045_GR; gll2491. DR KEGG; gvi:gll2491; -. DR BioCyc; GVIO251221:GLL2491-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 214 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100087. SQ SEQUENCE 214 AA; 23868 MW; A4B8FCB4F25A251D CRC64; MRVHHPYHEI PVETLNVDFF NLSPLSVARR LIGCAVVRVL AGERLSGRIV ETEAYGGLRD PSCYVVRRDE RIWSLLSGPP GVLYLHRAYR HWLLNITCDA VGEPACVLIR ALEPTGGEER MRQLRRGARD LTNGPARLVE ALAIDSAWEA SALPRAEFWL EAGEPVPEEQ VLNTVRIGLT RGKDLPWRFA VRDSPWVSRS VEAVLSEASL SAGL // ID 3MGH_GRABC Reviewed; 211 AA. AC Q0BR48; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 23-JAN-2007, entry version 6. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=GbCGDNIH1_1806; OS Granulobacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Granulibacter. OX NCBI_TaxID=391165; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Greenberg D.E., Porcella S.F., Zelazny A.M., Stock F., Dorward D.W., RA Murray P.R., Holland S.M.; RT "Genome sequence analysis of a novel human pathogenic acetic acid RT bacterium Granulobacter bethesdensis."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000394; ABI62704.1; -; Genomic_DNA. DR GenomeReviews; CP000394_GR; GbCGDNIH1_1806. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 211 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265025. SQ SEQUENCE 211 AA; 22898 MW; 5882EEAC69C6D945 CRC64; MKDCPDSLPV TSTGVPDGFW TRPVTEIARD LVGMTLLVDG CGGVIVETEA YDRDDPASHS FSGLTRRNAS MFGLPGHAYV YRSYGIHWCF NIVCGPVPGG AVLIRALHPM FGLEAMQLRR GAIRLRDLCR GPGRLCQALG ITDGMDGLSL CRPPFDLQPC HKTGEASDLI AAGPRIGITR AIETPWRFYQ AESVFVSGSR SSRFLINKAG K // ID 3MGH_LACAC Reviewed; 210 AA. AC Q5FMR0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 12-DEC-2006, entry version 13. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=LBA0113; OS Lactobacillus acidophilus. OC Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1579; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCFM; RX PubMed=15671160; DOI=10.1073/pnas.0409188102; RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., RA Buck B.L., McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., RA Lick S., Hamrick A., Cano R., Klaenhammer T.R.; RT "Complete genome sequence of the probiotic lactic acid bacterium RT Lactobacillus acidophilus NCFM."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000033; AAV42014.1; -; Genomic_DNA. DR GenomeReviews; CP000033_GR; LBA0113. DR KEGG; lac:LBA0113; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 210 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265026. SQ SEQUENCE 210 AA; 23844 MW; 76871B8EC3D46B5C CRC64; MNYAEYFTNR STDEITRDLI GRPLTFNDGQ EKLGGYIVEA EAYMGKLDRA AHSYGGHRSP ANEGLYRTGG TIYIYAQRQY FFFDVACQEE NEPQGVLVRA IDPAWGIDSM IKNRNGKSGV LITNGPAKMM QAFGIHDKNW NLHFLSDSPF TIDLADNHKR IAQEIIADKR VGINQSDPIW ANKKLRYYVA GNPYVSDMKK RDYASNNGWT // ID 3MGH_LACDA Reviewed; 208 AA. AC Q1G7S0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 1. DT 12-DEC-2006, entry version 7. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Ldb0170; OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM OS 20081). OC Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=390333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16754859; DOI=10.1073/pnas.0603024103; RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., RA Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., RA Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., RA Gibrat J.-F., Bessieres P., Weissenbach J., Ehrlich S.D., Maguin E.; RT "The complete genome sequence of Lactobacillus bulgaricus reveals RT extensive and ongoing reductive evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR954253; CAI97010.1; -; Genomic_DNA. DR GenomeReviews; CR954253_GR; Ldb0170. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 208 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265027. SQ SEQUENCE 208 AA; 23295 MW; C2C1A1CD252E2F13 CRC64; MDYRNFFTGR PTSEICRDLI GRPFYYQAGG EKIGGYIVES EAYLGIYDRA AHSYGGRRSH ANEGLWRAGG TIYIYSQRQY VFFDIACQEE GNPQGVLIRA IEPVWGLDQM LKNRGGKDGV LLTNGPAKLM QAMGIKSRNW DLAPLADSPF VIDLTEKKPA KEIVASPRIG IVQADPAWAQ APLRYYVAGN PYVSGMKKRD WADDHGWL // ID 3MGH_LACJO Reviewed; 208 AA. AC Q74LU5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 12-DEC-2006, entry version 16. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=LJ_0088; OS Lactobacillus johnsonii. OC Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=33959; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCC 533; RX PubMed=14983040; DOI=10.1073/pnas.0307327101; RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.; RT "The genome sequence of the probiotic intestinal bacterium RT Lactobacillus johnsonii NCC 533."; RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017198; AAS08070.1; -; Genomic_DNA. DR GenomeReviews; AE017198_GR; LJ_0088. DR KEGG; ljo:LJ0088; -. DR BioCyc; LJOH257314:LJ0088-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 208 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265028. SQ SEQUENCE 208 AA; 23353 MW; 9DF496A47F8C772D CRC64; MNYTEFFTNR STSEISKDLL GRTLSYNNGE EILSGTIVEA EAYVGVKDRA AHSYGGRRSP ANEGLYRPGG SLYIYSQRQY FFFDVSCQEE GEPQGVLIRA IDPLTGIDTM IKNRSGKTGP LLTNGPGKMM QALGITSRKW DLVDLNDSPF DIDIDHKREI EEIVALPRVG INQSDPEWAQ KKLRFIVSGN PYVSDIKKKD IKKNHGFI // ID 3MGH_LACPL Reviewed; 209 AA. AC Q88VP8; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 28-NOV-2006, entry version 23. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=lp_1991; OS Lactobacillus plantarum. OC Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1590; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX MEDLINE=22480296; PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., RA De Vos W.M., Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL935257; CAD64373.1; -; Genomic_DNA. DR HSSP; P29372; 1EWN. DR GenomeReviews; AL935263_GR; lp_1991. DR KEGG; lpl:lp_1991; -. DR BioCyc; LPLA220668:LP_1991-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 209 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100088. SQ SEQUENCE 209 AA; 23153 MW; 80A65B45F099E6C4 CRC64; MTAIERFLST CTTPEIAVSL LGKQLRLQTS SGVLTAWITE TEAYLGARDA GAHAYQNHQT PRNHALWQSA GTIYIYQMRA WCLLNIVTQA AGTPECVLIR GIEPDAGLER MQQQRPVPIA NLTNGPGKLM QALGLDKTLN GQALQPATLS LDLSHYRQPE QVVATPRIGI VNKGEWTTAP LRYFVAGNPF VSKISRRTID HEHHGWMTR // ID 3MGH_LACSS Reviewed; 213 AA. AC Q38Y85; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=LSA0543; OS Lactobacillus sakei subsp. sakei (strain 23K). OC Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=314315; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16273110; DOI=10.1038/nbt1160; RA Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M., RA Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., RA Loux V., Zagorec M.; RT "The complete genome sequence of the meat-borne lactic acid bacterium RT Lactobacillus sakei 23K."; RL Nat. Biotechnol. 23:1527-1533(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR936503; CAI54843.1; -; Genomic_DNA. DR GenomeReviews; CR936503_GR; LSA0543. DR KEGG; lsa:LSA0543; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 213 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265029. SQ SEQUENCE 213 AA; 23710 MW; CDA821C0E6D5EABD CRC64; MTTIQPAPMA FFTNRPTTEI ARDLLGTHLL YTSHQGTLGG LIVETEAYMG AQDTAAHAYN GRRTPFSEPL YHEPGTIYIY QLRSFFLFDI VTQAVDQPQG VLIRAIEPTH GLAQMQRNRP NKPSVNLTNG PGKLMGALGI HDKQLTFKNV ATAPLTIDLA NRRQPRHITT APRIGVNAKA ASGQLPYRYF ITGNPYVSGT LKKDWDREQH GWL // ID 3MGH_LEGPA Reviewed; 183 AA. AC Q5X6N6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 12-DEC-2006, entry version 14. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=lpp0929; OS Legionella pneumophila (strain Paris). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=297246; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15467720; DOI=10.1038/ng1447; RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., RA Etienne J., Glaser P., Buchrieser C.; RT "Evidence in the Legionella pneumophila genome for exploitation of RT host cell functions and high genome plasticity."; RL Nat. Genet. 36:1165-1173(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR628336; CAH12080.1; -; Genomic_DNA. DR GenomeReviews; CR628336_GR; lpp0929. DR KEGG; lpp:lpp0929; -. DR LegioList; lpp0929; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 183 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265031. SQ SEQUENCE 183 AA; 21028 MW; 8AEF075016AA2EE0 CRC64; MRKLLRPFYE RDTVLVAKEL LGKYLVHHDG LEEKIGRIVE VEAYLGQHDL ACHSSKGLTK RTKVMFGPAG YAYVYLIYGM YYCMNVVTEK EGIGSAVLIR ALEPIKNIQD RTQGPGLLSK AMRIDSKLNH RDLLSNDFYI AEPNSPTDFT IIEKPRIGVH YAKEWANELL RFYIKDNPYI SKT // ID 3MGH_LEGPH Reviewed; 183 AA. AC Q5ZX66; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 12-DEC-2006, entry version 13. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=lpg0866; OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / OS ATCC 33152 / DSM 7513). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=272624; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15448271; DOI=10.1126/science.1099776; RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., RA Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., RA Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R., RA Pampou S., Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E., RA Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G., RA Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J., RA Ju J., Kalachikov S., Shuman H.A., Russo J.J.; RT "The genomic sequence of the accidental pathogen Legionella RT pneumophila."; RL Science 305:1966-1968(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017354; AAU26954.1; -; Genomic_DNA. DR GenomeReviews; AE017354_GR; lpg0866. DR KEGG; lpn:lpg0866; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 183 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265032. SQ SEQUENCE 183 AA; 21028 MW; 8AEF075016AA2EE0 CRC64; MRKLLRPFYE RDTVLVAKEL LGKYLVHHDG LEEKIGRIVE VEAYLGQHDL ACHSSKGLTK RTKVMFGPAG YAYVYLIYGM YYCMNVVTEK EGIGSAVLIR ALEPIKNIQD RTQGPGLLSK AMRIDSKLNH RDLLSNDFYI AEPNSPTDFT IIEKPRIGVH YAKEWANELL RFYIKDNPYI SKT // ID 3MGH_LEGPL Reviewed; 183 AA. AC Q5WY41; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 12-DEC-2006, entry version 14. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=lpl0898; OS Legionella pneumophila (strain Lens). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=297245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15467720; DOI=10.1038/ng1447; RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., RA Etienne J., Glaser P., Buchrieser C.; RT "Evidence in the Legionella pneumophila genome for exploitation of RT host cell functions and high genome plasticity."; RL Nat. Genet. 36:1165-1173(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR628337; CAH15132.1; -; Genomic_DNA. DR GenomeReviews; CR628337_GR; lpl0898. DR KEGG; lpf:lpl0898; -. DR LegioList; lpl0898; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 183 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265030. SQ SEQUENCE 183 AA; 20960 MW; 56404BFF011281ED CRC64; MRKLPRPFYE RDTVLVAKEL LGKYLVHHDG LEEKIGRIVE VEAYLGQHDL ACHSSKGLTK RTKVMFGPAG YAYVYLIYGM YYCMNVVTEK EGVGSAVLIR ALEPIKNIQD RTQGPGLLSK AMRIDSKLNH RDLLSNDFYI AEPYGPTDFT IIEKPRIGVH YAKEWADALL RFYIKDNPYI SKT // ID 3MGH_LEIXX Reviewed; 213 AA. AC Q6AGC6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 12-DEC-2006, entry version 14. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Lxx06100; OS Leifsonia xyli subsp. xyli. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Microbacteriaceae; Leifsonia. OX NCBI_TaxID=59736; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CTCB07; RX PubMed=15305603; RA Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., RA Kitajima J.P., Truffi D., do Amaral A.M., Harakava R., RA de Oliveira J.C.F., Wood D., de Oliveira M.C., Miyaki C.Y., RA Takita M.A., da Silva A.C.R., Furlan L.R., Carraro D.M., Camarotte G., RA Almeida N.F. Jr., Carrer H., Coutinho L.L., El-Dorry H.A., RA Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S., RA Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M., RA Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F., RA Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A., RA Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.; RT "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia RT xyli subsp. xyli."; RL Mol. Plant Microbe Interact. 17:827-836(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016822; AAT88569.1; -; Genomic_DNA. DR GenomeReviews; AE016822_GR; Lxx06100. DR KEGG; lxx:Lxx06100; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR InterPro; IPR005829; Sug_transporter. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 213 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265033. SQ SEQUENCE 213 AA; 22210 MW; 4FC302E436EA2116 CRC64; MSSDVTLAQP GRDAFLASSL EVAPRLLGAV LRHESAEGPV ALRITEVEAY TGEGLDPGSH AFRGPTRRNA AMYGEPGRLY AYFTYGMHVC ANVVCSPAGE ASAVLLRGAE IVEGLALAER RRAGASGRRI PQRDLARGPA RLVVAAGIGL ADDGADLLAP PFGLLLPSVQ PEYATGPRTG VSGAGGGAAF PWRYWLPGEP SVSPYKRHPA SHG // ID 3MGH_LISIN Reviewed; 207 AA. AC Q92D89; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 28-NOV-2006, entry version 29. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=lin0928; OS Listeria innocua. OC Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1642; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIP 11262 / Serovar 6a; RX MEDLINE=21537279; PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL596166; CAC96160.1; -; Genomic_DNA. DR PIR; AH1548; AH1548. DR HSSP; P29372; 1F6O. DR GenomeReviews; AL592022_GR; lin0928. DR KEGG; lin:lin0928; -. DR ListiList; LIN00928; -. DR BioCyc; LINN1642:LIN0928-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 207 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100089. SQ SEQUENCE 207 AA; 23563 MW; 308A36A348EF7822 CRC64; MNAKITPTFF ENRTTIELAR DIIGMRLVHE IGNYTLSGYI VETEAYLGAT DMAAHSFKNL RTKRTEVMFG TPGTIYTYQM HQQVLLNFIT MREGIPEAVL IRALEPTKES IEQMEQNRFL KTGFELTNGP GKLTQALGLS MQDYGKTLFD SNIWLERAKV PHIIEATNRI GVPNKGIATH YPLRFTAKGS PYISAQRKRQ ISAYIWE // ID 3MGH_LISMF Reviewed; 207 AA. AC Q721N6; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-NOV-2006, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=LMOf2365_0949; OS Listeria monocytogenes serotype 4b (strain F2365). OC Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=265669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15115801; DOI=10.1093/nar/gkh562; RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., RA Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., RA Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., RA Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., RA Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., RA Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., RA Bayles D.O., Luchansky J.B., Fraser C.M.; RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food- RT borne pathogen Listeria monocytogenes reveal new insights into the RT core genome components of this species."; RL Nucleic Acids Res. 32:2386-2395(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017262; AAT03728.1; -; Genomic_DNA. DR GenomeReviews; AE017262_GR; LMOf2365_0949. DR KEGG; lmf:LMOf2365_0949; -. DR TIGR; LMOf2365_0949; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 207 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100090. SQ SEQUENCE 207 AA; 23491 MW; 21A9EE5336FE8390 CRC64; MEAIITKEFF EDKTTIELAR DILGMRLVHQ TDEGILSGLI VETEAYLGAT DMAAHSFQNL RTKRTEVMFS SPGRIYMYQM HRQVLLNFIT MPKGIPEAIL IRAIEPDEQA KQQMVQNRHG KTGYELTNGP GKLTQALGLS MQDYGKTLFD SNIWLEEAKL PHLIEATNRI GVPNKGIATH FPLRFTVKGS PYISAQRKSR ILTDIWK // ID 3MGH_LISMO Reviewed; 207 AA. AC P58621; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 1. DT 28-NOV-2006, entry version 30. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=lmo0928; OS Listeria monocytogenes. OC Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1639; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-679 / EGD-e / Serovar 1/2a; RX MEDLINE=21537279; PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL591977; CAC99006.1; -; Genomic_DNA. DR PIR; AH1190; AH1190. DR HSSP; P29372; 1F6O. DR GenomeReviews; AL591824_GR; lmo0928. DR KEGG; lmo:lmo0928; -. DR ListiList; LMO00928; -. DR BioCyc; LMON169963:LMO0928-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 207 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100091. SQ SEQUENCE 207 AA; 23372 MW; 8D66CCF4A5E1807D CRC64; MEAMITKEFF ESKTTIELAR DILGMRLVHQ TNEGLLSGLI VETEAYLGAT DMAAHSFQNL RTKRTEVMFS SPGTIYMYQM HRQVLLNFIT MPKGIPEAIL IRAIEPDEQA KQQMTQNRHG KTGYELTNGP GKLTQALGLS MQDYGKTLFD SNIWLEEAKL PHLIEATNRI GVPNKGIATH YPLRFTVKGS PYISGQRKNS IRTGIWK // ID 3MGH_MESSB Reviewed; 181 AA. AC Q11IE7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 23-JAN-2007, entry version 6. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Meso_1432; OS Mesorhizobium sp. (strain BNC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=266779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P.; RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000390; ABG62828.1; -; Genomic_DNA. DR GenomeReviews; CP000390_GR; Meso_1432. DR KEGG; mes:Meso_1432; -. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 181 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265034. SQ SEQUENCE 181 AA; 19753 MW; 68F3892E69E702E2 CRC64; MSLTAFFSRP SVVVAKDLIG ANFFVGSAGG IIVETEAYDR EEPASHSFRG PTARNRSMFG PPAHAYVYRS YGIHWCLNFV CLPGSGVLIR ALEPTAGIEL MQERRRTISL KQLCSGPGRV GEALGIDRSL DGRGLDQPPF RLDLSNAKAC AISGTRIGIT RAAELEWRFG LEGSIYVSRK F // ID 3MGH_MYCBO Reviewed; 203 AA. AC P65413; O33190; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 28-NOV-2006, entry version 15. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Mb1714; OS Mycobacterium bovis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1765; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX MEDLINE=22709107; PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., RA Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., RA Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., RA Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX248339; CAD96382.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR GenomeReviews; BX248333_GR; Mb1714. DR KEGG; mbo:Mb1714; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 203 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100095. SQ SEQUENCE 203 AA; 21340 MW; 9DFE3035819504B0 CRC64; MNAEELAIDP VAAAHRLLGA TIAGRGVRAM VVEVEAYGGV PDGPWPDAAA HSYRGRNGRN DVMFGPPGRL YTYRSHGIHV CANVACGPDG TAAAVLLRAA AIEDGAELAT SRRGQTVRAV ALARGPGNLC AALGITMADN GIDLFDPSSP VRLRLNDTHR ARSGPRVGVS QAADRPWRLW LTGRPEVSAY RRSSRAPARG ASD // ID 3MGH_MYCFO Reviewed; 194 AA. AC Q9EUU9; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 28-NOV-2006, entry version 27. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-) (3-mag) DE (Fragment). OS Mycobacterium fortuitum. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1766; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 6841 / DSM 46621 / IFO 13159 / NBRC 13159 / NCTC 10394; RA Menendez C.; RT "Characterization of an rRNA operon (rrnB) of Mycobacterium fortuitum RT and other mycobacterial species; implications for the classification RT of mycobacteria."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ296160; CAC18747.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW DNA damage; DNA repair; Hydrolase. FT CHAIN <1 194 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100092. FT NON_TER 1 1 SQ SEQUENCE 194 AA; 20023 MW; 7102DAB3370DCF98 CRC64; PLLAARRLLG AELIGRGVTA AIVEVEAYGG PADGPWPDAA SHSFRGAGGR NLVMFGPPGH LYTYRSHGIH VCANVVCGFD GVAGAVLLRA AVVRTGADVA GRRRGPAILP AALARGPGNL CSALGITMED NGIDLFDADS PVRLTLGEPV PSVDGPRVGV SKAADRRWRL WLADSSEVSA YRRSPRAPAP GASD // ID 3MGH_MYCLE Reviewed; 214 AA. AC O05678; Q9CC32; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 28-NOV-2006, entry version 44. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=ML1351; ORFNames=MLC1351.17c; OS Mycobacterium leprae. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1769; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN; RX MEDLINE=21128732; PubMed=11234002; DOI=10.1038/35059006; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z95117; CAB08290.1; ALT_INIT; Genomic_DNA. DR EMBL; AL583921; CAC31732.1; -; Genomic_DNA. DR PIR; A87078; A87078. DR HSSP; P29372; 1F6O. DR GenomeReviews; AL450380_GR; ML1351. DR KEGG; mle:ML1351; -. DR Leproma; ML1351; -. DR BioCyc; MLEP1769:ML1351-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 214 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100093. SQ SEQUENCE 214 AA; 22313 MW; 6F97A6F363468528 CRC64; MRSPRRCKIC AVSADQLVVD PVVAAHRLLG ATITGRGVCA IVVEVEAYGG VPDGPWPDAA AHSYHGRNDR NAVMFGPPGR LYTYCSHGIH VCANVSCGPD GTAAAVLIRA GALENGADVA RSRRGASVRT VALARGPGNL CSALGITMDD NGIDVFAADS PVTLVLNEAQ EAMSGPRVGI SHAADRPWRL WLPGRPEVST YRRSPRAPAP GASD // ID 3MGH_MYCPA Reviewed; 205 AA. AC Q740F6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 12-DEC-2006, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=MAP_1395; OS Mycobacterium paratuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=1770; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10; RX PubMed=16116077; DOI=10.1073/pnas.0505662102; RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., RA Banerji N., Kanjilal S., Kapur V.; RT "The complete genome sequence of Mycobacterium avium subspecies RT paratuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016958; AAS03712.1; -; Genomic_DNA. DR GenomeReviews; AE016958_GR; MAP_1395. DR KEGG; mpa:MAP1395; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265035. SQ SEQUENCE 205 AA; 21538 MW; 5E66BDFC6C6A1FC7 CRC64; MRDAAEQLLV DPVEAARRLL GATLTGRGVS GVIVEVEAYG GVPDGPWPDA AAHSYKGLRA RNFVMFGPPG RLYTYRSHGI HVCANVSCGP DGTAAAVLLR AAALEDGTDV ARGRRGELVH TAALARGPGN LCAAMGITMA DNGIDLFDPD SPVTLRLHEP LTAVCGPRVG VSQAADRPWR LWLPGRPEVS AYRRSPRAPA PGTSD // ID 3MGH_MYCSS Reviewed; 204 AA. AC Q1B7S1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 12-DEC-2006, entry version 6. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Mmcs_2956; OS Mycobacterium sp. (strain MCS). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=164756; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Miller C.D., Hughes J.E., Anderson A.J., RA Sims R.C., Richardson P.; RT "Complete sequence of chromosome of Mycobacterium sp. MCS."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000384; ABG09063.1; -; Genomic_DNA. DR GenomeReviews; CP000384_GR; Mmcs_2956. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 204 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265036. SQ SEQUENCE 204 AA; 21481 MW; BBA364C031D244A5 CRC64; MVSVELLRVD PLTAARRLLG AVLTCRGVSA TVVEVEAYGG PPDGPWPDAA AHSYRGPGPR NQVMFGPAGR LYTYRSHGIH VCANVACADD GVAAAVLLRA AVIESGHDVV QRRRGEAVRE SAFARGPGNL CSALGITMAD NGIDVFAEDS PVHLRLGEEQ PCIAGPRVGV SKAADRPWRL WLAGRPEVSA YRRSPRAPAP GGSD // ID 3MGH_MYCTU Reviewed; 203 AA. AC P65412; O33190; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 28-NOV-2006, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Rv1688, MT1727.1; ORFNames=MTCI125.10; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX842577; CAB10945.1; -; Genomic_DNA. DR EMBL; AE000516; AAK45996.1; -; Genomic_DNA. DR PIR; G70501; G70501. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE000516_GR; MT1727.1. DR GenomeReviews; AL123456_GR; Rv1688. DR KEGG; mtc:MT1727.1; -. DR KEGG; mtu:Rv1688; -. DR TIGR; MT1727.1; -. DR TubercuList; Rv1688; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 203 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100094. SQ SEQUENCE 203 AA; 21340 MW; 9DFE3035819504B0 CRC64; MNAEELAIDP VAAAHRLLGA TIAGRGVRAM VVEVEAYGGV PDGPWPDAAA HSYRGRNGRN DVMFGPPGRL YTYRSHGIHV CANVACGPDG TAAAVLLRAA AIEDGAELAT SRRGQTVRAV ALARGPGNLC AALGITMADN GIDLFDPSSP VRLRLNDTHR ARSGPRVGVS QAADRPWRLW LTGRPEVSAY RRSSRAPARG ASD // ID 3MGH_MYXXD Reviewed; 194 AA. AC Q1CYD8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 23-JAN-2007, entry version 8. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=MXAN_6462; OS Myxococcus xanthus (strain DK 1622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Myxococcus. OX NCBI_TaxID=246197; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17015832; DOI=10.1073/pnas.0607335103; RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., RA Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R., RA Kaplan H.B.; RT "Evolution of sensory complexity recorded in a myxobacterial genome."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000113; ABF91760.1; -; Genomic_DNA. DR GenomeReviews; CP000113_GR; MXAN_6462. DR KEGG; mxa:MXAN_6462; -. DR TIGR; MXAN_6462; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 194 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265037. SQ SEQUENCE 194 AA; 20857 MW; C3CE9852D6C92ACB CRC64; MNWLPESFYA RPALVVAREL LGALLVVEEG GQRRVGRIVE TEAYIGEHDL ACHAAKGLTP RTEVMFGPAG VAYVYLIYGM HHCFNVVTDA TGAGAAVLVR AVEPVEGLPP GTRTDGPGRL CKALGLTRAH NRRGLCTPVL HLRPGTPVPE SAVSRGPRIG VDYAGTWAAE PFRLWVRDSQ HVSKGPPPGR RKPA // ID 3MGH_NITHX Reviewed; 206 AA. AC Q1QMA3; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 23-JAN-2007, entry version 7. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Nham_1830; OS Nitrobacter hamburgensis (strain X14 / DSM 10229). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323097; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Ward B., RA Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., RA Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.; RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000319; ABE62644.1; -; Genomic_DNA. DR GenomeReviews; CP000319_GR; Nham_1830. DR KEGG; nha:Nham_1830; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 206 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265038. SQ SEQUENCE 206 AA; 22385 MW; E3D2A5A14A4D044D CRC64; MTPNTQSDIP DPPALGKPLT RSFFGRSVHD VAPDLIGATL LVDGVGGIIV EVEAYHHTEP AAHSHRGPTP RNMVMFGPPG FTYVYRSYGI HWCMNFVCEK DGCAAAVLIR ALQPTHGIPA MRRRRRLHEE RLLCSGPGKL CAALGISIAH NALPLDAPPI AVYQRTGKVD VVTGVRIGIT KAADLPWRYG LKGSRFLSKP FRSAES // ID 3MGH_NITMU Reviewed; 193 AA. AC Q2Y9K4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 12-DEC-2006, entry version 11. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Nmul_A1264; OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosospira. OX NCBI_TaxID=323848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC RT 25196."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000103; ABB74567.1; -; Genomic_DNA. DR GenomeReviews; CP000103_GR; Nmul_A1264. DR KEGG; nmu:Nmul_A1264; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 193 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265041. SQ SEQUENCE 193 AA; 20918 MW; E721C4E7E1E26144 CRC64; MSMSQPSIDF SASSVDVARS LIGATLLVNG VGGRIVETEA YDHDDPASHS FSGPTRRNQV MFGPPCHAYI YRSYGIHWCL NFVCRPAGHG AGVLIRAIEP LVGLDIMRKR RGLSDERLLC SGPGRVCEAL GITQEYSGMS IDTPPFQLTP PLDPVPVVTG PRIGISKAKD VPWRFGLAGS PFLSRPFRQP DIV // ID 3MGH_NITOC Reviewed; 201 AA. AC Q3JEY0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Noc_0079; OS Nitrosococcus oceani (strain ATCC 19707 / NCIMB 11848). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=323261; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16957257; DOI=10.1128/AEM.00463-06; RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., RA Poret-Peterson A.T., Vergez L.M., Ward B.B.; RT "Complete genome sequence of the marine, chemolithoautotrophic, RT ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."; RL Appl. Environ. Microbiol. 72:6299-6315(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000127; ABA56616.1; -; Genomic_DNA. DR GenomeReviews; CP000127_GR; Noc_0079. DR KEGG; noc:Noc_0079; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 201 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265040. SQ SEQUENCE 201 AA; 22255 MW; 86E094633E779C9A CRC64; MTDLLPPRFY ARDALEVAAD LLGASLCREQ VVLRITEVEA YRWPEDTANH GRHGQTLRNE PLWGPPGRVY LYLCYGIHHL LNLVTGEEGQ AAAVLIRACE PVAGLDLIQR RRRGKIKPGL LTGPGKVGAA LGLDLSWNHH PLYEPGGLEV RRGTPVAALL AGPRVGIAYA HPEHRDAPWR LAIPDNPWVS CRSQLQPRQQ N // ID 3MGH_NITWN Reviewed; 208 AA. AC Q3SSP2; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 12-DEC-2006, entry version 11. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Nwi_1438; OS Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323098; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006; RA Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., RA Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., RA Arp D.J., Hickey W.J.; RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing RT bacterium Nitrobacter winogradskyi Nb-255."; RL Appl. Environ. Microbiol. 72:2050-2063(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000115; ABA04699.1; -; Genomic_DNA. DR GenomeReviews; CP000115_GR; Nwi_1438. DR KEGG; nwi:Nwi_1438; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 208 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265039. SQ SEQUENCE 208 AA; 22512 MW; C2C405CD4F74801C CRC64; MKLTQDLTSD GPDPPVLGKP LTRAFFGRSV HDVAPDLIGA TLLVDGVGGI IVEVEAYHHT EPAAHSHRGP TPRNMVMFGP PGFAYVYRSY GIHWCVNFVC EMDGSAAAVL IRALQPTHGI PAMRRRRGLH EERLLCSGPG RLCQALGISI AHNALPLDAP PIAVFRRTEK ADVVAGVRIG ITKAADLPWR YGLKGSKFLS KPFRSAGY // ID 3MGH_NOCFA Reviewed; 212 AA. AC Q5YYA5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 12-DEC-2006, entry version 13. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=nfa19900; OS Nocardia farcinica. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Nocardia. OX NCBI_TaxID=37329; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 10152; RX PubMed=15466710; DOI=10.1073/pnas.0406410101; RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., RA Shiba T., Hattori M.; RT "The complete genomic sequence of Nocardia farcinica IFM 10152."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006618; BAD56836.1; -; Genomic_DNA. DR GenomeReviews; AP006618_GR; nfa19900. DR KEGG; nfa:nfa19900; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 212 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265042. SQ SEQUENCE 212 AA; 22185 MW; 9A99A837B347EDE1 CRC64; MAVVSVEELV VDPPTAARRL LGATLRSGQV AVRLVEVEAY GGDAEGPWPD PASHSGRGRT KRNAVMFGPA GYLYVYLSYG MHTCVNVTTG PDGTAGAVLL RAGEVVDGLD VVRGRRPTAR TDADLARGPG NFGTALGIAL DDYGTALFDP AAPIRLELAD PLPAALIADG PRVGVSSEAD RPWRFWLPSS PAVSAYRRSP RAPGAATVRA PR // ID 3MGH_OCEIH Reviewed; 198 AA. AC Q8ETG4; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 28-NOV-2006, entry version 23. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=OB0297; OS Oceanobacillus iheyensis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus. OX NCBI_TaxID=182710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831; RX MEDLINE=22220767; PubMed=12235376; DOI=10.1093/nar/gkf526; RA Takami H., Takaki Y., Uchiyama I.; RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya RT Ridge and its unexpected adaptive capabilities to extreme RT environments."; RL Nucleic Acids Res. 30:3927-3935(2002). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000028; BAC12253.1; -; Genomic_DNA. DR GenomeReviews; BA000028_GR; OB0297. DR KEGG; oih:OB0297; -. DR BioCyc; OIHE182710:OB0297-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 198 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100096. SQ SEQUENCE 198 AA; 22150 MW; 9AABACE6BDF91306 CRC64; MDQQQNFQPL AESFYQVPTL ELAKNLLGCI LVKQTEEGTS SGVIVETEAY LGNTDRAAHG YGNRRTKRTE ILYSKPGYAY VHLIHNHRLI NVVSSMEGDP ESVLIRAVEP FSGIDEMLMR RPVKKFQNLT SGPGKLTQAM GIYMEDYGHF MLAPPLFISE GKSPASVKTG SRIGIDNTGE AKDYPYRFWV DGNPFVSR // ID 3MGH_PELLD Reviewed; 196 AA. AC Q3B622; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Plut_0321; OS Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM OS 273)). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=319225; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelodictyon luteolum DSM 273."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000096; ABB23209.1; -; Genomic_DNA. DR GenomeReviews; CP000096_GR; Plut_0321. DR KEGG; plt:Plut_0321; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 196 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265043. SQ SEQUENCE 196 AA; 21756 MW; 7C93584A9BDF761D CRC64; MTRLGKQFFT APTLALTERL LGKIFVRITP SGTVLKGRIV ETEAYLGHND EACHAWRKKT ERNRVMFEAP GTLYVYFSYG CHHLLNIVTE PEGTAGAVLI RAMEPVEGIP CMQERRQTTV ETALMSGPAK LTSALGVERS SSGRDLFGNE FFLLDAPSPQ PSMICTSTRV GISRSRELPW RKYLADSPHV SKGRPS // ID 3MGH_PROAC Reviewed; 191 AA. AC Q6A5L3; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 12-DEC-2006, entry version 13. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=PPA2247; OS Propionibacterium acnes. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1747; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KPA171202 / DSM 16379; RX PubMed=15286373; DOI=10.1126/science.1100330; RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.; RT "The complete genome sequence of Propionibacterium acnes, a commensal RT of human skin."; RL Science 305:671-673(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017283; AAT83950.1; -; Genomic_DNA. DR GenomeReviews; AE017283_GR; PPA2247. DR KEGG; pac:PPA2247; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 191 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265044. SQ SEQUENCE 191 AA; 20411 MW; 15DA37C7E9867E26 CRC64; MIDLSAPAIE VAPLLLGATI WRGPVGIRLT EVEAYMGLDD PASHAFRGPT PRARVMFGPP SHIYVYLSYG MHRCVNLVCS PDGEASAVLL RGGQVIAGHD DARRRRGNVA ENRLACGPGN MGSALGASLE ESGNPVSIIG NGAISALGWR LEPAPEIAEF RQGPRVGISR NIDAPWRWWI PQDPTVSGPR T // ID 3MGH_PSEAE Reviewed; 239 AA. AC Q9HX17; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 28-NOV-2006, entry version 31. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=PA4010; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004091; AAG07397.1; -; Genomic_DNA. DR PIR; G83143; G83143. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE004091_GR; PA4010. DR KEGG; pae:PA4010; -. DR BioCyc; PAER287:PA4010-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 239 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100097. SQ SEQUENCE 239 AA; 26950 MW; 802F0365A74D95D8 CRC64; MSRDPILSLP WPDARPLPDT FFDRDALLVA RELLGKVIRH RQGNLWLAAR IIETEAYYLE EKGSHASLGY TEKRKALFLD GGHIYMYYAR GGDSLNFSAG GPGNAVLIKS GHPWLDRISD HTALERMQSL NPDSQGRPRE IGRLCAGQTL LCKAMGLKVP EWDAQRFDPQ RLFVDDVGER PSQVIQAARL GIPKGRDEHL PYRFVDAAFA AFCTRNPLRR GQVAGRDYHL LGHQDPHLQ // ID 3MGH_PSYCK Reviewed; 212 AA. AC Q1QEF7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Pcryo_0162; OS Psychrobacter cryohalolentis (strain K5). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=335284; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.; RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000323; ABE73946.1; -; Genomic_DNA. DR GenomeReviews; CP000323_GR; Pcryo_0162. DR KEGG; pcr:Pcryo_0162; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 212 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265045. SQ SEQUENCE 212 AA; 23511 MW; 6520D8662E8A6C90 CRC64; MLASQVVSSV VKPSWFARPT CVVAADLIGK VLCRELTDSD GQQKILRMRI SETEAYIGEG DAACHAHAGT RTPRTEIMYH IGGVFYVYLT YGIHHMLNLV SGPTESPEAV LIRAGFLIEG SARLMNEQLL DVNRQLNHIK QLAGPGKLTK GLQIDRTLYG KPITPASKVW VEDDGCQPLV SLRPRIGIDY AGDAKEWLLR YIWTDHPSLS KK // ID 3MGH_RHIEC Reviewed; 199 AA. AC Q2K4W8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RHE_CH03355; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16505379; DOI=10.1073/pnas.0508502103; RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., RA Jimenez-Jacinto V., Collado-Vides J., Davila G.; RT "The partitioned Rhizobium etli genome: genetic and metabolic RT redundancy in seven interacting replicons."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000133; ABC92118.1; -; Genomic_DNA. DR GenomeReviews; CP000133_GR; RHE_CH03355. DR KEGG; ret:RHE_CH03355; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 199 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265046. SQ SEQUENCE 199 AA; 21543 MW; 97D871B69E3D51F2 CRC64; MTDGGMTKDA IGAGALAGEG LRAFFERDAI TVARDLLGCH LTVDGAGGRI TETEAYFPDD EASHSFRGPT KRNGAMFGRP GNVYIYRIYG MYWCLNFVCH PGSAVLIRAL EPETGIAAMM ERRGTDMLTA LCSGPGKLCQ ALGIDIEIND RLLDLPPYAL TPSTPVPIVA GKRIGITRNA EAPWRFGIQG SRYLSKPFR // ID 3MGH_RHIL3 Reviewed; 198 AA. AC Q1MCQ8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 12-DEC-2006, entry version 8. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RL3782; OS Rhizobium leguminosarum bv. viciae (strain 3841). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=216596; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34; RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., RA Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D., RA Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C., RA Arrowsmith C., Cherevach I., Chillingworth T., Clarke K., Cronin A., RA Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S., RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., RA Whitehead S., Parkhill J.; RT "The genome of Rhizobium leguminosarum has recognizable core and RT accessory components."; RL Genome Biol. 7:RESEARCH34.1-RESEARCH34.20(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM236080; CAK09272.1; -; Genomic_DNA. DR GenomeReviews; AM236080_GR; RL3782. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 198 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265047. SQ SEQUENCE 198 AA; 21515 MW; 74C1964E60011B5B CRC64; MTDATTNGAI GAGTLTGESL RKFFERDAIT VSRDLLGCHL TVDGVGGRIT ETEAYFPDDE ASHSFRGPTK RNGAMYGKPG NVYIYRIYGV YWCLNFVCHP GSAALIRALE PETGIPRMME RRGTDMLTSL CSGPGKLCQA LGIDIAINDR LLDRAPYAIA PSAPVPIVSG KRIGITKNAE APWRFGIQGS RFLSKPFR // ID 3MGH_RHILO Reviewed; 208 AA. AC Q98DR6; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 28-NOV-2006, entry version 26. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=mll4583; OS Rhizobium loti (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=381; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF303099; RX MEDLINE=21082930; PubMed=11214968; DOI=10.1093/dnares/7.6.331; RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium RT Mesorhizobium loti."; RL DNA Res. 7:331-338(2000). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000012; BAB51204.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR GenomeReviews; BA000012_GR; mll4583. DR KEGG; mlo:mll4583; -. DR BioCyc; MLOT381:MLL4583-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 208 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100098. SQ SEQUENCE 208 AA; 22771 MW; 9972F5784111E85E CRC64; MGRAHTVSRG EDHPPIARSE LPDDTAALAR YLIGKLVVRD LPEGMVSGRI VETEAYVVGD AAGHGFRGMT PRNRSLFLER GHAYVYLAYG VSMMLNVSSE VPGIGTGVLI RALEPLDGIE IMRRNRGVER LRDLARGPGR LAAALRIDRS LDGLDLCRKG PLWLAKDNQK PGEIGQSTRI GITKDAARLL RFYVRGSLFV SGPRSLQE // ID 3MGH_RHIME Reviewed; 185 AA. AC Q92TT1; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 23-JAN-2007, entry version 31. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RB1416; ORFNames=SMb20709; OS Rhizobium meliloti (Sinorhizobium meliloti). OG Plasmid pSymB (megaplasmid 2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=382; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX MEDLINE=21396508; PubMed=11481431; DOI=10.1073/pnas.161294698; RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., RA Vorhoelter F.J., Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., RA Golding B., Puehler A.; RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2- RT fixing endosymbiont Sinorhizobium meliloti."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL591985; CAC49816.1; -; Genomic_DNA. DR PIR; H96018; H96018. DR HSSP; P29372; 1F6O. DR GenomeReviews; AL591985_GR; RB1416. DR KEGG; sme:SMb20709; -. DR BioCyc; SMEL382:SMB20709-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase; Plasmid. FT CHAIN 1 185 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100099. SQ SEQUENCE 185 AA; 19974 MW; 7DE6283605FA4A11 CRC64; MHRLTSDVDF FARSAVQVAA DLIGADFTVS GVGGTIVETE AYLPDDAASH SFAGTTARNR AMFGPPAHAY IYLSYGLHWC LNFVCLPGSA VLIRAIEPRW GIDTMRARRG VREERLLCSG PGRVGQALAI SRELDGLPLG EDPFRLTLPS TKPPLAAGIR VGITKAVEQP WRFGLAGSSF VSRKF // ID 3MGH_RHOBA Reviewed; 233 AA. AC Q7UG12; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 23-JAN-2007, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN Name=mpg; OrderedLocusNames=RB8205; OS Rhodopirellula baltica. OC Bacteria; Planctomycetes; Planctomycetacia; Planctomycetales; OC Planctomycetaceae; Pirellula. OX NCBI_TaxID=117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1; RX MEDLINE=22735913; PubMed=12835416; DOI=10.1073/pnas.1431443100; RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., RA Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., RA Schlesner H., Amann R., Reinhardt R.; RT "Complete genome sequence of the marine planctomycete Pirellula sp. RT strain 1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX294147; CAD78517.1; -; Genomic_DNA. DR GenomeReviews; BX119912_GR; RB8205. DR KEGG; rba:RB8205; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 233 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100100. SQ SEQUENCE 233 AA; 26091 MW; 92997F15CE584430 CRC64; MMNDAKRNQF REDDEEDRLI DWGSTQSLQS QFFDRRPAVV ARQLLGCGFA RRIEGVWVGG WIVETEAYLS SRDAASHSAR GEKPGNASMF GRPSTLYVYP IHAKHCVNLV TESVGCGSAV LIRALQPVWG IDRMFQHRGL HRSETTDGRA LTTGPGRLCQ SLAIDRTCDG VDPIRDPNWC VFSGPKLPSS RVTTTPRIGI SQAAELPLRF FVDGNRYVSG LVRHHRRPRR DSL // ID 3MGH_RHOP2 Reviewed; 201 AA. AC Q2IW19; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RPB_2889; OS Rhodopseudomonas palustris (strain HaA2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316058; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A., RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris HaA2."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000250; ABD07591.1; -; Genomic_DNA. DR GenomeReviews; CP000250_GR; RPB_2889. DR KEGG; rpb:RPB_2889; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 201 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265053. SQ SEQUENCE 201 AA; 21389 MW; 797C17D945F3C2E3 CRC64; MMSSRVSAPA PGALGPPLRR RFFARSVHEV APELIGATLL VEGVGGVIVE VEAYHHTDPA AHSYGGQTAR NAVMFGPPGF AYVYRSYGIH WCVNVVCEAE GSASAVLIRA LQPTHGVEAM RARRGLDDAR SLCSGPGKLA QALGISIAHN GLPLDAPPFA IHRRIGEPDI VTGPRIGITK AADYPWRFGL KGSRFVSVPF K // ID 3MGH_RHOPA Reviewed; 206 AA. AC Q6N6M8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 12-DEC-2006, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RPA2586; OS Rhodopseudomonas palustris. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=1076; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-98 / CGA009; RX PubMed=14704707; DOI=10.1038/nbt923; RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., RA Harrison F.H., Gibson J., Harwood C.S.; RT "Complete genome sequence of the metabolically versatile RT photosynthetic bacterium Rhodopseudomonas palustris."; RL Nat. Biotechnol. 22:55-61(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX572601; CAE28027.1; ALT_INIT; Genomic_DNA. DR GenomeReviews; BX571963_GR; RPA2586. DR KEGG; rpa:RPA2586; -. DR BioCyc; RPAL258594:RPA2586-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 206 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265050. SQ SEQUENCE 206 AA; 22171 MW; D7E1DF9416630E00 CRC64; MTKSRAPKPP SDGTHPALGP LLTRWFFARS VHEVAPELIG ATLLFGGAGG IIVEVEAYHH TDPAAHSYGG PTPRNQVMFG PPGFAYVYRS YGIHWCVNVV CEPEGSASAV LIRALEPTHG LAAMRKRRGL DEPRSLCSGP GKLAQALGIT IADNGLPLDA APFAIHRRTT TPEIVAGPRI GITKAADYPW RFGLKDSRFL SKPFPR // ID 3MGH_RHOPB Reviewed; 200 AA. AC Q214R5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RPC_2571; OS Rhodopseudomonas palustris (strain BisB18). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., RA Anderson I., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB18."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000301; ABD88121.1; ALT_INIT; Genomic_DNA. DR GenomeReviews; CP000301_GR; RPC_2571. DR KEGG; rpc:RPC_2571; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 200 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265051. SQ SEQUENCE 200 AA; 21251 MW; D5B6914F43165E1B CRC64; MVDLRIPAAL KLGPKLKRSF FARSVHEVAP DLIGATLLVE GSGGVIVEVE AYHHTDPAAH SFGGQTPRNA VMFGPPGVAY VYRSYGIHWC LNVVCEEAGS ASAVLIRALV PTDGLALMRR RRGVEDERAL CSGPGKLAQA LGVTIAHNGL KLDAPPFALH GRLAAPEIVA GPRIGISKAA ELPWRYGLRG SKFVSKPFAE // ID 3MGH_RHOPS Reviewed; 202 AA. AC Q137C7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 12-DEC-2006, entry version 3. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RPD_2583; OS Rhodopseudomonas palustris (strain BisB5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., RA Lykidis A., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB5."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000283; ABE39812.1; -; Genomic_DNA. DR GenomeReviews; CP000283_GR; RPD_2583. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265052. SQ SEQUENCE 202 AA; 21806 MW; 39567F26725DA2BD CRC64; MARSRVPAAA SPAKLGPLLS RRFFARSVHE VAPELIGATL LVAGVGGLIV EVEAYHHTDP AAHSYGGETP RNRVMFGPPG FAYVYRSYGI HWCVNFVCEA EGSASAVLIR ALAPTHGLGV MRKHRGLDDE RSLCSGPGKL TQALGITIAH NGAPLDIEPF AIHRRTVEPD IGTGPRIGIS KAIELPWRYG LRRSRLVSKP FK // ID 3MGH_RHOS4 Reviewed; 197 AA. AC Q3J3U4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RHOS4_09720; ORFNames=RSP_2381; OS Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM OS 158). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272943; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., RA Kaplan S.; RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000143; ABA78540.1; ALT_INIT; Genomic_DNA. DR GenomeReviews; CP000143_GR; RHOS4_09720. DR KEGG; rsp:RSP_2381; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 197 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265048. SQ SEQUENCE 197 AA; 20698 MW; 9E03DA298F543CEC CRC64; MSHRRQTAQE GGQMEGQAAC FAREAPAVAV DLLGAHLQVR GVGGRIVETE AYTPDDPASH SFRGPTPRNA AMFGPPGCAY VYLSYGIHLC LNVVCAPGHA VLIRALEPTE GLAQMAARRG TDVARLLCSG PGRIGQALGL TLADDGTAFG TRGFAVRWGA PVAAGEILCG PRIGISRAAD MPWRFGLRGS PCLSRRF // ID 3MGH_RHOSR Reviewed; 223 AA. AC Q0SI65; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 23-JAN-2007, entry version 6. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RHA1_ro00943; OS Rhodococcus sp. (strain RHA1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=101510; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA McLeod M.P., Warren R.L., Araki N., Hsiao W.W.L., Myhre M., RA Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., RA Dosanjh M., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., RA Shin H., Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., RA Eltis L.D.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000431; ABG92771.1; -; Genomic_DNA. DR GenomeReviews; CP000431_GR; RHA1_ro00943. DR KEGG; rha:RHA1_ro00943; -. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 223 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265049. SQ SEQUENCE 223 AA; 23925 MW; B2966512E59C42E8 CRC64; MNYATAGVAA STVVENRDVT IERLHRAEPV DAARIVLGST LVVGDVRIRI VEVEAYGGEK DGPWPDPASH SYRGRTPRNE VMFGPAGHLY VYRSYGMHFC MNVSYGPVGV AGGVLLRAGE VLDGCATVQA RRPRVTRPAE WARGPGNLGS ATGVTLAENG AALFESDSPV RLEVAESDGW VSGPRVGVST AADRPWRFWI PESPAVSAYR RSPRAMSADE QMG // ID 3MGH_RICBR Reviewed; 220 AA. AC Q1RJJ3; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RBE_0390; OS Rickettsia bellii (strain RML369-C). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=336407; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076; RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., RA Fournier P.-E., Claverie J.-M., Raoult D.; RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae RT in gene exchanges between intracellular pathogens."; RL PLoS Genet. 2:E76-E76(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000087; ABE04471.1; -; Genomic_DNA. DR GenomeReviews; CP000087_GR; RBE_0390. DR KEGG; rbe:RBE_0390; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 220 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265054. SQ SEQUENCE 220 AA; 24854 MW; 55CF6218D1CAC8B4 CRC64; MNNKLIPLSR EFFARDTNIV SQELLGKVLY FQGKTAIITE TESYIGQDDP ACHAARGRTK RTDIMFGPAG FSYVYLIYGM YYCLNFVTET DGFPAATLIR GAYIISTKDL YTADTSKVGS QISGETARRI LIREHRRIPK FDVPNLEVSK VDGPGKLCKY LGINISHNKI DLINNNEFFV SDINLKLPYS TTTRIGITKG IDKLWRYVVT NPIDLTKISF // ID 3MGH_RICCN Reviewed; 183 AA. AC Q92IE0; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 23-JAN-2007, entry version 28. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RC0480; OS Rickettsia conorii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=781; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX MEDLINE=21442074; PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., RA Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008611; AAL03018.1; -; Genomic_DNA. DR PIR; H97759; H97759. DR HSSP; P29372; 1F4R. DR GenomeReviews; AE006914_GR; RC0480. DR KEGG; rco:RC0480; -. DR BioCyc; RCON781:RC0480-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 183 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100101. SQ SEQUENCE 183 AA; 20502 MW; 5FE0475B9C0E9EEA CRC64; MNKLIPVPRE FFARDTNVVS TELIGKALYF QGKTAIITET ESYIGQNDPA CHAARGRTKR TDIMFGPAGF SYVYLIYGMY YCLNFVTEAK GFPAATLIRG VHVILPENLY LNGPGKLCKY LGINISHNKC DLINNNEFFV GDIGLKLPYS TTARIGITKG TDKLWRYVVT DITNLISQYN VQP // ID 3MGH_RICFE Reviewed; 177 AA. AC Q4UM12; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 12-DEC-2006, entry version 11. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RF_0560; OS Rickettsia felis (Rickettsia azadi). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=42862; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:E248-E248(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000053; AAY61411.1; -; Genomic_DNA. DR GenomeReviews; CP000053_GR; RF_0560. DR KEGG; rfe:RF_0560; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 177 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265055. SQ SEQUENCE 177 AA; 19932 MW; E2D06F077B35F3C8 CRC64; MNKLILLPRE FFARDTNLVS TELIGKVLYF QGKTAIITET ESYIGQDDPA CHAARGRTKR TDIMFGPAGF SYVYLIYGMY YCLNFVTETE GFPAATLIRG VHVISPENLY LNGPGKLCKY LGINISHNKC DLINNNEFFV SDIGLKLPYS TTTRIGITKG TDKLWRYVVT DIIRLPA // ID 3MGH_RICPR Reviewed; 217 AA. AC Q9ZDH7; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 23-JAN-2007, entry version 36. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RP351; OS Rickettsia prowazekii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=782; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX MEDLINE=99039499; PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., RA Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., RA Eriksson A.-S., Winkler H.H., Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC -!- SIMILARITY: Contains 1 RPE2 insert 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; AJ235271; CAA14811.1; -; Genomic_DNA. DR PIR; A71692; A71692. DR HSSP; P29372; 1F6O. DR GenomeReviews; AJ235269_GR; RP351. DR KEGG; rpr:RP351; -. DR BioCyc; RPRO782:RP351-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 217 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100102. FT DOMAIN 105 145 RPE2 insert. SQ SEQUENCE 217 AA; 24809 MW; 0B5A4DBE000A7942 CRC64; MNKLIPLPRE FFARDTNLVS TELIGKVLYF QGTTAIITET ESYIGEDDPA CHAARGRTKR TDVMFGPAGF SYVYLIYGMY YCLNFVTEDE GFPAATLIRG VYVISHNNVY TIDTAKIKSQ ITDEKTQSII IRKNRRIMKF YIPNLKASNL YLNGPGKLCK YLGINTSYNK CDLINNKDFF VSDIGLNLPY YSTTRIGITK GTDKLWRYIV TDPKMLY // ID 3MGH_RICTY Reviewed; 223 AA. AC Q68X22; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 20-FEB-2007, entry version 14. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=RT0340; OS Rickettsia typhi. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=785; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-144 / Wilmington; RX PubMed=15317790; DOI=10.1128/JB.186.17.5842-5855.2004; RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., RA Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., RA Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., RA Gibbs R.A., Hong C., Yu X.-J., Walker D.H., Weinstock G.M.; RT "Complete genome sequence of Rickettsia typhi and comparison with RT sequences of other Rickettsiae."; RL J. Bacteriol. 186:5842-5855(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017197; AAU03820.1; -; Genomic_DNA. DR GenomeReviews; AE017197_GR; RT0340. DR KEGG; rty:RT0340; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 2. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 223 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265056. SQ SEQUENCE 223 AA; 25246 MW; 33075B6B3AA6C0CA CRC64; MNKLIPLPRE FFARDTNLVS TELIGKVLYF QGTTAIITET ESYIGNDDPA CHAARGRTKR TDVMFGPAGF SYVYLIYGMY HCLNFVTEDE GFPAATLIRG VYVISHNDLY TIYTAKVKSQ ITDEKTQSII ISEDRRSTKF DIPNLEESNL YLNGPGKLCK YLGINTTHNK CDLINNKDFF VSDIGLNLPY STTKRIGITK GTDKLWRYIV TDNKNALLNI NIL // ID 3MGH_RUBXD Reviewed; 190 AA. AC Q1AWF5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 23-JAN-2007, entry version 7. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Rxyl_1309; OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129). OC Bacteria; Actinobacteria; Rubrobacteridae; Rubrobacterales; OC Rubrobacterineae; Rubrobacteraceae; Rubrobacter. OX NCBI_TaxID=266117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., RA Battista J.R., Richardson P.; RT "Complete sequence of Rubrobacter xylanophilus DSM 9941."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000386; ABG04273.1; -; Genomic_DNA. DR GenomeReviews; CP000386_GR; Rxyl_1309. DR KEGG; rxy:Rxyl_1309; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 190 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265057. SQ SEQUENCE 190 AA; 20386 MW; D46831BEF9EC62B1 CRC64; MDLLGCVLVS ETPEGTCSGV IVETEAYRPE DPACHAYRGP SMRNRTLFGG PGLAYVYLSY GMHRLLNAVC EGEGVGSAVL IRSLAPLEGV PLMRRRRGRA ADLCNGPGRL AESLGVGLSL DGHDLTLGEG LYIAPGPPPR GEIVSTTRIG VSRGAELPWR YLVLGERVSV PPRRISGRGL RRAWNVREPA // ID 3MGH_SALRD Reviewed; 206 AA. AC Q2S2B5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 20-FEB-2007, entry version 14. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SRU_1545; OS Salinibacter ruber (strain DSM 13855). OC Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales; OC Sphingobacteriales genera incertae sedis; Salinibacter. OX NCBI_TaxID=309807; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., RA Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., RA Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., RA Charlebois R.L., Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000159; ABC44247.1; -; Genomic_DNA. DR GenomeReviews; CP000159_GR; SRU_1545. DR KEGG; sru:SRU_1545; -. DR TIGR; SRU_1545; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 206 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265058. SQ SEQUENCE 206 AA; 22404 MW; 9265686AA453FD4B CRC64; MEPLPASFFN RPTVSVARDL LGARLVHEAP TGTRLVGRIV ETEAYTEDDP ACHASHLSRD PETGEVVGQG RGQDLFAAPG TAYVYLIYGV HWLLNVVTEP EGTAGAVLVR AVEPEEGLQD MRTERGVDRR VDLTNGPGKL AEAFGIDGEF HQTRLTARPL FFADGDSVDD EQVARSSRIG ISKGVERSWR WYVAANRFVS PASPSG // ID 3MGH_SODGL Reviewed; 170 AA. AC Q4LBY8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN ORFNames=pSG1.74; OS Sodalis glossinidius. OG Plasmid pSG1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Sodalis. OX NCBI_TaxID=63612; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC PLASMID=pSG1; RX PubMed=15995217; DOI=10.1128/JB.187.14.5003-5007.2005; RA Darby A.C., Lagnel J., Matthew C.Z., Bourtzis K., Maudlin I., RA Welburn S.C.; RT "Extrachromosomal DNA of the symbiont Sodalis glossinidius."; RL J. Bacteriol. 187:5003-5007(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ868434; CAI59516.1; -; Genomic_DNA. DR EMBL; AJ868433; CAI59343.1; -; Genomic_DNA. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW DNA damage; DNA repair; Hydrolase; Plasmid. FT CHAIN 1 170 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265059. SQ SEQUENCE 170 AA; 19040 MW; 45863FFB81DFCC36 CRC64; MLSNTILSRS FYKRDTLCVA KDLLGKVLKF ADYYGVINEV EAYIGQDDPA CHAARGYTPR TAAMFGAAGF SYVYLIYGMY HCLNIVTERE GFPAAVLIRG IDLYKPTVLS LNGPGKLCKK LNITKNNNKI DLTQSHGFCV YNTTARPEYM ATPRIGIKVG TDKLWRFKSM // ID 3MGH_STAA3 Reviewed; 202 AA. AC Q2FEF3; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SAUSA300_2290; OS Staphylococcus aureus (strain USA300). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000255; ABD21114.1; -; Genomic_DNA. DR GenomeReviews; CP000255_GR; SAUSA300_2290. DR KEGG; saa:SAUSA300_2290; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265062. SQ SEQUENCE 202 AA; 22771 MW; 231650C02B31F4E1 CRC64; MDFVNNDTRQ IAKNLLGVKV IYQDTTQTYT GYIVETEAYL GLNDRAAHGY GGKITPKVTS LYKRGGTIYA HVMHTHLLIN FVTKSEGIPE GVLIRAIEPE EGLSAMFRNR GKKGYEVTNG PGKWTKAFNI PRAIDGATLN DCRLSIDTKN RKYPKDIIAS PRIGIPNKGD WTHKSLRYTV KGNPFVSRMR KSDCMFPEDT WK // ID 3MGH_STAA8 Reviewed; 202 AA. AC Q2FVS1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 12-DEC-2006, entry version 9. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SAOUHSC_02621; OS Staphylococcus aureus (strain NCTC 8325). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=93061; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., RA Iandolo J.J.; RT "The Staphylococcus aureus NCTC8325 genome."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000253; ABD31630.1; -; Genomic_DNA. DR GenomeReviews; CP000253_GR; SAOUHSC_02621. DR KEGG; sao:SAOUHSC_02621; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265061. SQ SEQUENCE 202 AA; 22771 MW; 231650C02B31F4E1 CRC64; MDFVNNDTRQ IAKNLLGVKV IYQDTTQTYT GYIVETEAYL GLNDRAAHGY GGKITPKVTS LYKRGGTIYA HVMHTHLLIN FVTKSEGIPE GVLIRAIEPE EGLSAMFRNR GKKGYEVTNG PGKWTKAFNI PRAIDGATLN DCRLSIDTKN RKYPKDIIAS PRIGIPNKGD WTHKSLRYTV KGNPFVSRMR KSDCMFPEDT WK // ID 3MGH_STAAB Reviewed; 202 AA. AC Q2YYZ2; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 12-DEC-2006, entry version 11. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SAB2222; OS Staphylococcus aureus (strain bovine RF122). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=273036; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Herron-Olson L., Musser J.M., Kapur V.; RT "Whole-genome sequencing and comparative analysis of bovine mastitis- RT associated Staphylococcus aureus."; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ938182; CAI81911.1; -; Genomic_DNA. DR GenomeReviews; AJ938182_GR; SAB2222. DR KEGG; sab:SAB2222; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265060. SQ SEQUENCE 202 AA; 22757 MW; C25344903E305E50 CRC64; MDFVNNDTRQ IAKNLLGVKV IYQDTTQTYT GYIVETEAYL GLNDRAAHGY GGKITPKVTS LYKRGGTIYA HVMHTHLLIN FVTKSEGIPE GVLIRAIEPE DGLSAMFRNR GKKGYEVTNG PGKWTKAFNI PRAIDGATLN DCRLSIDTKN RKYPKDIIAS PRIGIPNKGD WTHKSLRYTV KGNPFVSRMR KSDCMFPEDT WK // ID 3MGH_STAAC Reviewed; 202 AA. AC Q5HDL2; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 23-JAN-2007, entry version 15. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SACOL2339; OS Staphylococcus aureus (strain COL). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=93062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000046; AAW37167.1; -; Genomic_DNA. DR GenomeReviews; CP000046_GR; SACOL2339. DR KEGG; sac:SACOL2339; -. DR TIGR; SACOL2339; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100103. SQ SEQUENCE 202 AA; 22771 MW; 231650C02B31F4E1 CRC64; MDFVNNDTRQ IAKNLLGVKV IYQDTTQTYT GYIVETEAYL GLNDRAAHGY GGKITPKVTS LYKRGGTIYA HVMHTHLLIN FVTKSEGIPE GVLIRAIEPE EGLSAMFRNR GKKGYEVTNG PGKWTKAFNI PRAIDGATLN DCRLSIDTKN RKYPKDIIAS PRIGIPNKGD WTHKSLRYTV KGNPFVSRMR KSDCMFPEDT WK // ID 3MGH_STAAM Reviewed; 202 AA. AC P65414; Q99RS9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 23-JAN-2007, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SAV2344; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., RA Ogasawara N., Hayashi H., Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus RT aureus."; RL Lancet 357:1225-1240(2001). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000017; BAB58506.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR GenomeReviews; BA000017_GR; SAV2344. DR KEGG; sav:SAV2344; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100104. SQ SEQUENCE 202 AA; 22771 MW; 231650C02B31F4E1 CRC64; MDFVNNDTRQ IAKNLLGVKV IYQDTTQTYT GYIVETEAYL GLNDRAAHGY GGKITPKVTS LYKRGGTIYA HVMHTHLLIN FVTKSEGIPE GVLIRAIEPE EGLSAMFRNR GKKGYEVTNG PGKWTKAFNI PRAIDGATLN DCRLSIDTKN RKYPKDIIAS PRIGIPNKGD WTHKSLRYTV KGNPFVSRMR KSDCMFPEDT WK // ID 3MGH_STAAN Reviewed; 202 AA. AC P65415; Q99RS9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 23-JAN-2007, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SA2134; OS Staphylococcus aureus (strain N315). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=158879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., RA Ogasawara N., Hayashi H., Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus RT aureus."; RL Lancet 357:1225-1240(2001). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000018; BAB43436.1; -; Genomic_DNA. DR PIR; C90034; C90034. DR HSSP; P29372; 1F6O. DR GenomeReviews; BA000018_GR; SA2134. DR KEGG; sau:SA2134; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100105. SQ SEQUENCE 202 AA; 22771 MW; 231650C02B31F4E1 CRC64; MDFVNNDTRQ IAKNLLGVKV IYQDTTQTYT GYIVETEAYL GLNDRAAHGY GGKITPKVTS LYKRGGTIYA HVMHTHLLIN FVTKSEGIPE GVLIRAIEPE EGLSAMFRNR GKKGYEVTNG PGKWTKAFNI PRAIDGATLN DCRLSIDTKN RKYPKDIIAS PRIGIPNKGD WTHKSLRYTV KGNPFVSRMR KSDCMFPEDT WK // ID 3MGH_STAAR Reviewed; 202 AA. AC Q6GE90; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 16. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SAR2429; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571856; CAG41411.1; -; Genomic_DNA. DR GenomeReviews; BX571856_GR; SAR2429. DR KEGG; sar:SAR2429; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100106. SQ SEQUENCE 202 AA; 22812 MW; C7F6E4959B905E50 CRC64; MDFVNNDTRQ IAKNLLGVKV IYQDTTQTYT GYIVETEAYL GLNDRAAHGY GGKITPKVTS LYKRGGTIYA HVMHTHLLIN FVTKSEGIPE GVLIRAIEPE DGLSAMFRNR GKKGYEVTNG PGKWTKAFNI PRAIDGARLN DCRLSIDTKN RKYPKDIIAS PRIGIPNKGD WTHKSLRYTV KGNPFVSRMR KSDCMFPEDT WK // ID 3MGH_STAAS Reviewed; 202 AA. AC Q6G6X6; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 16. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SAS2235; OS Staphylococcus aureus (strain MSSA476). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571857; CAG44048.1; -; Genomic_DNA. DR GenomeReviews; BX571857_GR; SAS2235. DR KEGG; sas:SAS2235; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100107. SQ SEQUENCE 202 AA; 22771 MW; 231650C02B31F4E1 CRC64; MDFVNNDTRQ IAKNLLGVKV IYQDTTQTYT GYIVETEAYL GLNDRAAHGY GGKITPKVTS LYKRGGTIYA HVMHTHLLIN FVTKSEGIPE GVLIRAIEPE EGLSAMFRNR GKKGYEVTNG PGKWTKAFNI PRAIDGATLN DCRLSIDTKN RKYPKDIIAS PRIGIPNKGD WTHKSLRYTV KGNPFVSRMR KSDCMFPEDT WK // ID 3MGH_STAAW Reviewed; 202 AA. AC P65416; Q99RS9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 23-JAN-2007, entry version 17. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=MW2265; OS Staphylococcus aureus (strain MW2). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=196620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5; RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., RA Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., RA Yamamoto K., Hiramatsu K.; RT "Genome and virulence determinants of high virulence community- RT acquired MRSA."; RL Lancet 359:1819-1827(2002). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000033; BAB96130.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR GenomeReviews; BA000033_GR; MW2265. DR KEGG; sam:MW2265; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100108. SQ SEQUENCE 202 AA; 22771 MW; 231650C02B31F4E1 CRC64; MDFVNNDTRQ IAKNLLGVKV IYQDTTQTYT GYIVETEAYL GLNDRAAHGY GGKITPKVTS LYKRGGTIYA HVMHTHLLIN FVTKSEGIPE GVLIRAIEPE EGLSAMFRNR GKKGYEVTNG PGKWTKAFNI PRAIDGATLN DCRLSIDTKN RKYPKDIIAS PRIGIPNKGD WTHKSLRYTV KGNPFVSRMR KSDCMFPEDT WK // ID 3MGH_STAEQ Reviewed; 205 AA. AC Q5HLQ3; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 23-JAN-2007, entry version 15. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SERP1931; OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=176279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000029; AAW55279.1; -; Genomic_DNA. DR GenomeReviews; CP000029_GR; SERP1931. DR KEGG; ser:SERP1931; -. DR TIGR; SERP1931; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100110. SQ SEQUENCE 205 AA; 23016 MW; 0D20E0DA3975257C CRC64; MIYLDFINQQ TTQTAKALLG VKIIYQDDYQ TYTGYIVETE AYLGIQDKAA HGFGGKITPK VTSLYKKGGT IYAHVMHTHL LINFVTRTEG IPEGVLIRAI EPDEGIGAMN VNRGKSGYEL TNGPGKWTKA FNIPRSIDGS TLNDCKLSID TNHRKYPKTI IESGRIGIPN KGEWTNKPLR FTVKGNPYVS RMRKSDFQNP DDTWK // ID 3MGH_STAES Reviewed; 205 AA. AC Q8CRC1; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 23-JAN-2007, entry version 29. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SE_1919; OS Staphylococcus epidermidis (strain ATCC 12228). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22832016; PubMed=12950922; RX DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., RA Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., RA Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015929; AAO05560.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE015929_GR; SE_1919. DR KEGG; sep:SE1919; -. DR BioCyc; SEPI176280:SE1919-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 205 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100109. SQ SEQUENCE 205 AA; 23016 MW; 0D20E0DA3975257C CRC64; MIYLDFINQQ TTQTAKALLG VKIIYQDDYQ TYTGYIVETE AYLGIQDKAA HGFGGKITPK VTSLYKKGGT IYAHVMHTHL LINFVTRTEG IPEGVLIRAI EPDEGIGAMN VNRGKSGYEL TNGPGKWTKA FNIPRSIDGS TLNDCKLSID TNHRKYPKTI IESGRIGIPN KGEWTNKPLR FTVKGNPYVS RMRKSDFQNP DDTWK // ID 3MGH_STAHJ Reviewed; 202 AA. AC Q4L8K2; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 23-JAN-2007, entry version 13. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SH0714; OS Staphylococcus haemolyticus (strain JCSC1435). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=279808; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005; RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., RA Lee J.C., Hiramatsu K.; RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the RT extreme plasticity of its genome and the evolution of human-colonizing RT staphylococcal species."; RL J. Bacteriol. 187:7292-7308(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006716; BAE04023.1; -; Genomic_DNA. DR GenomeReviews; AP006716_GR; SH0714. DR KEGG; sha:SH0714; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 202 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100111. SQ SEQUENCE 202 AA; 22757 MW; 99EF88F6BE66683F CRC64; MDFVSRPTTE TAKALLGVKV IYEDEFQTYS GYIVETEAYL GFTDRAAHGF GGKQTPKVTS LYKRGGTIYG HVMHTHLLVN FVTQNEGVPE GVLIRAIEPL DGIEMMKHNR NKSGYELTNG PGKWTKAFNI PRAIDGATLN DCRLSIDTKH RKYPRDIVES ARIGIPNKGD WTNKPLRYTV KGNPFVSHIR KSDCLNPDET WK // ID 3MGH_STAS1 Reviewed; 203 AA. AC Q49ZR8; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 23-JAN-2007, entry version 14. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SSP0561; OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / OS DSM 20229). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=342451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16135568; DOI=10.1073/pnas.0502950102; RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., RA Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., RA Hattori M., Ohta T.; RT "Whole genome sequence of Staphylococcus saprophyticus reveals the RT pathogenesis of uncomplicated urinary tract infection."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008934; BAE17706.1; -; Genomic_DNA. DR GenomeReviews; AP008934_GR; SSP0561. DR KEGG; ssp:SSP0561; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 203 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100112. SQ SEQUENCE 203 AA; 23267 MW; 0A9BC479821C7AAA CRC64; MDFLQRDTVT IAKDLLGVRI IYHDELQTFT GYIVETEAYI GTKDRAAHGY NGKRTPKVES LYKQGGTIYA HVMHTHLLIN FVTQLEGQPE GVLIRAIEPE EGIELMAINR GKNGFELTNG PGKWTKAFNI PRHLDGSKLN EGRLKIDTKN RKYPKEIEAS GRIGIPNKGE WTHKPLRFTV KGNPYISRMK KSDMRQPEYT WRI // ID 3MGH_STRAW Reviewed; 213 AA. AC Q829C5; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 23-JAN-2007, entry version 21. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SAV6486; OS Streptomyces avermitilis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=33903; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165; RX MEDLINE=21477403; PubMed=11572948; DOI=10.1073/pnas.211433198; RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., RA Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., RA Kikuchi H., Shiba T., Sakaki Y., Hattori M.; RT "Genome sequence of an industrial microorganism Streptomyces RT avermitilis: deducing the ability of producing secondary RT metabolites."; RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165; RX MEDLINE=22608306; PubMed=12692562; DOI=10.1038/nbt820; RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M., Omura S.; RT "Complete genome sequence and comparative analysis of the industrial RT microorganism Streptomyces avermitilis."; RL Nat. Biotechnol. 21:526-531(2003). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000030; BAC74197.1; -; Genomic_DNA. DR GenomeReviews; BA000030_GR; SAV6486. DR KEGG; sma:SAV6486; -. DR BioCyc; SAVE-XXX-01:SAVE-XXX-01-006584-MONOMER; -. DR BioCyc; SAVE227882:SAV6486-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 213 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100113. SQ SEQUENCE 213 AA; 23159 MW; 20E37E5AB2BE4BBC CRC64; MIAAPDRTPL TREFFARPVL DVAPDLLGRV LVRTTPDGPI ELRVTEVEAY DGPSDPGSHA YRGRTARNGV MFGPPGHVYV YFTYGMWHCM NLVCGPEGRA SAVLLRAGEI IEGAELARTR RLSARNDKEL AKGPARLATA LEVDRALDGT DACAPEGGPL TLLSGTPVPP DQVRNGPRTG VSGDGGVHPW RFWIDNDPTV SPYRAHTPRR RRT // ID 3MGH_STRCO Reviewed; 213 AA. AC Q9S208; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 23-JAN-2007, entry version 38. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=SCO1792; ORFNames=SCI51.32c; OS Streptomyces coelicolor. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1902; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX MEDLINE=21996410; PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., RA Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces RT coelicolor A3(2)."; RL Nature 417:141-147(2002). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL939110; CAB52856.1; -; Genomic_DNA. DR PIR; T36895; T36895. DR HSSP; P29372; 1EWN. DR GenomeReviews; AL645882_GR; SCO1792. DR KEGG; sco:SCO1792; -. DR BioCyc; SCOE1902:SCO1792-MONOMER; -. DR LinkHub; Q9S208; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 213 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100114. SQ SEQUENCE 213 AA; 23358 MW; 4F99FBC60E0648C0 CRC64; MIASPDRTPL PREFFDRPVL EVAPDLLGRI LVRTGPDGPI TLRLTEVEAY DGQNDPGSHA YRGRTPRNEV MFGPPGHVYV YFTYGMWFCM NLVCGPEGRS SAVLLRAGEI IDGAELARTR RLSARNDKEL AKGPARLATA LGVDRALNGT DACTSQETPL RILTGTPVPG DQVRNGPRTG VAGEGGVHPW RYWVADDPTV SPYRAHVPRK RRS // ID 3MGH_SYNJA Reviewed; 195 AA. AC Q2JXG4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CYA_0301; OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium OS Yellowstone A-Prime). OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. OX NCBI_TaxID=321327; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Heidelberg J.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000239; ABC98522.1; -; Genomic_DNA. DR GenomeReviews; CP000239_GR; CYA_0301. DR KEGG; cya:CYA_0301; -. DR TIGR; CYA_0301; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 195 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265066. SQ SEQUENCE 195 AA; 21701 MW; 7CD8D9FBEBF83460 CRC64; MAAWEWLSKP APLVAPTLLG MVLVRQFADG LQVRAQIVET EAYTAGDPAC HAYRRKTRRN QVMFGPPGHL YVYRIYGLYH CLNIVTEAEG IASAVLIRAA QLDCLPEWIP ANKRLKPARV AAGPGLLCQA LRIDGSHNGW RLEPVAAGQE GIWLEGSPAW EAQFPIVQTT RIGITRGVEL PWRWYIKGHP AVSHY // ID 3MGH_SYNJB Reviewed; 192 AA. AC Q2JI31; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 12-DEC-2006, entry version 11. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=CYB_2817; OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium OS Yellowstone B-Prime). OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. OX NCBI_TaxID=321332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Heidelberg J.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000240; ABD03740.1; -; Genomic_DNA. DR GenomeReviews; CP000240_GR; CYB_2817. DR KEGG; cyb:CYB_2817; -. DR TIGR; CYB_2817; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 192 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265065. SQ SEQUENCE 192 AA; 21330 MW; 71CAF20F5D810045 CRC64; MEWLSQPAPL VAPALLGMVL VRQFADGLQV RAQIVETEAY TAGDPACHAY RRKTQRNQVM FGPPGHLYIY RIYGLYHCLN IVTEPEGIPA AVLIRAAQLD RLPDWIPANK QNQPARAAAG PGLLCQALRI DGSHNGWRLE RAEAGQEGIW LEGSPSWQTQ LSIVQTTRIG ITQGAEIPWR WYIGGHPAVS RY // ID 3MGH_SYNP6 Reviewed; 199 AA. AC Q5N3S0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 12-DEC-2006, entry version 12. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=syc0860_c; OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) OS (Anacystis nidulans). OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. OX NCBI_TaxID=269084; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Sugita M.; RT "Complete genome structure of the unicellular cyanobacterium Anacystis RT nidulans 6301 (Synechococcus sp. PCC6301)."; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008231; BAD79050.1; -; Genomic_DNA. DR GenomeReviews; AP008231_GR; syc0860_c. DR KEGG; syc:syc0860_c; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 199 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265063. SQ SEQUENCE 199 AA; 21927 MW; 1DB04C802F5867A2 CRC64; MTTAALLESP WHPLLSQPAT EAAIALLGCW LVRRFADGRV IRGRIVETEA YEAGDPACHG YRRQTARNRS MFGPPGQVYV YQIYGRYHCI NLATEAADLA SAVLIRALEF PDTEAIAGAG PGRLCRFLAI DRQLDGSWLG PTSPLDLEAA DYPLGTLIQT TRIGLTRGVD LPWRWYLAES PAVSRRDRRA EAEQMGVSV // ID 3MGH_SYNP7 Reviewed; 194 AA. AC Q31QG8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Synpcc7942_0669; OS Synechococcus sp. (strain PCC 7942) (Anacystis nidulans R2). OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC RT 7942."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000100; ABB56701.1; -; Genomic_DNA. DR GenomeReviews; CP000100_GR; Synpcc7942_0669. DR KEGG; syf:Synpcc7942_0669; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 194 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265067. SQ SEQUENCE 194 AA; 21469 MW; 074E36B3F2AA0A28 CRC64; MLESPWHPLL SQPATEAAIA LLGCWLVRRF ADGRVIRGRI VETEAYEAGD PACHGYRRQT ARNRSMFGPP GQVYVYQIYG RYHCINLATE AADLASAVLI RALEFPDTEA IAGAGPGRLC RFLAIDRQLD GSWLGPTSPL DLEAADYPLG TLIQTTRIGL TRGVDLPWRW YLAESPAVSR RDRRAEAEQM GVSV // ID 3MGH_SYNS3 Reviewed; 212 AA. AC Q0ID97; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 12-DEC-2006, entry version 5. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=sync_0342; OS Synechococcus sp. (strain CC9311). OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. OX NCBI_TaxID=64471; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16938853; DOI=10.1073/pnas.0602963103; RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., RA Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., RA Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., RA Halpin R., Paulsen I.T.; RT "Genome sequence of Synechococcus CC9311: insights into adaptation to RT a coastal environment."; RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000435; ABI45185.1; -; Genomic_DNA. DR GenomeReviews; CP000435_GR; sync_0342. DR TIGR; sync_0342; -. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 212 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265064. SQ SEQUENCE 212 AA; 23918 MW; 1776D48F11B9601B CRC64; MSHPAHPRRF SALPQAFFCR PAEVVGPELI GCFLVKRQND GSLLWGVIVE TEAYSQDDPA CHGYRRRSPQ NETLFGEPGR FYVYVSYGIH HCVNVVTDRS DWANGVLLRA VAMPGEPERV AAGPGLLARR FGLNRTHDSQ AVCGENEFWL ASRPSVLNVP ELVTTTRIGI SQAQDLPWRW YLQDSRSVSR RARGDRMPAL SQAFIPTLEW KR // ID 3MGH_TRIEI Reviewed; 201 AA. AC Q113S1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 12-DEC-2006, entry version 5. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Tery_2004; OS Trichodesmium erythraeum (strain IMS101). OC Bacteria; Cyanobacteria; Oscillatoriales; Trichodesmium. OX NCBI_TaxID=203124; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Richardson P.; RT "Complete sequence of Trichodesmium erythraeum IMS101."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000393; ABG51253.1; -; Genomic_DNA. DR GenomeReviews; CP000393_GR; Tery_2004. DR HAMAP; MF_00527; -; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 201 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265068. SQ SEQUENCE 201 AA; 22750 MW; E3DE16D1D1675136 CRC64; MANNEVIENT WLERPSPEVA PELIGCTLVR RISEEKIIRS TIVETEAYAP GDPACHAYRK RTPRNTVMFG PPGISYVFLI YGMYHCLNVV TDIDGIPSVV LIRALQLESV PNWLWEHIPK QKSKPKVSRL AAGPGKLCRL LNIDLNLNGS RLRAGQPMWL EQRSPSFEKN LQIVQTTRIG ITKGTNLLWR WYLANCDAVS K // ID 3MGH_WOLPM Reviewed; 180 AA. AC Q73G53; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 20-FEB-2007, entry version 21. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=WD_1110; OS Wolbachia pipientis wMel. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=66077; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069; RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., RA Brownlie J.C., McGraw E.A., Martin W., Esser C., Ahmadinejad N., RA Wiegand C., Madupu R., Beanan M.J., Brinkac L.M., Daugherty S.C., RA Durkin A.S., Kolonay J.F., Nelson W.C., Mohamoud Y., Lee P., RA Berry K.J., Young M.B., Utterback T.R., Weidman J.F., Nierman W.C., RA Paulsen I.T., Nelson K.E., Tettelin H., O'Neill S.L., Eisen J.A.; RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: RT a streamlined genome overrun by mobile genetic elements."; RL PLoS Biol. 2:327-341(2004). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017196; AAS14764.1; ALT_INIT; Genomic_DNA. DR GenomeReviews; AE017196_GR; WD1110. DR KEGG; wol:WD1110; -. DR TIGR; WD_1110; -. DR BioCyc; WPIP955:WD1110-MONOMER; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 180 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265069. SQ SEQUENCE 180 AA; 20313 MW; 5487DFE175986202 CRC64; MMSNTILPRN FYERPTLVVA GELLGKMLKF SNFSGIITEV EAYIGMSDPA CHAAKGYTNR TSVMFGMPGF SYVYFIYGMY YCLNIVTEAE GFPAAVLIRG LKLIEPLEAN LGGPGILCKR LNITKEHNKQ DLTISHEFCV YESHLKPDYV CTPRIGISKG QEKFWRFKNL RSCVDYLPIG // ID 3MGH_WOLTR Reviewed; 169 AA. AC Q5GT31; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 12-DEC-2006, entry version 13. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=Wbm0254; OS Wolbachia sp. subsp. Brugia malayi (strain TRS). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=292805; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15780005; DOI=10.1371/journal.pbio.0030121; RA Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N., RA Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., RA Ingram J., Moran L., Lapidus A., Omelchenko M., Kyrpides N., RA Ghedin E., Wang S., Goltsman E., Joukov V., Ostrovskaya O., RA Tsukerman K., Mazur M., Comb D., Koonin E., Slatko B.; RT "The Wolbachia genome of Brugia malayi: endosymbiont evolution within RT a human pathogenic nematode."; RL PLoS Biol. 3:599-614(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017321; AAW70843.1; ALT_INIT; Genomic_DNA. DR GenomeReviews; AE017321_GR; Wbm0254. DR KEGG; wbm:Wbm0254; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 169 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265070. SQ SEQUENCE 169 AA; 19246 MW; EDE51B975823F208 CRC64; MNNEILPRNF YERPTLVVAG ELLGKILKFS NFSGVITEVE AYIGMDDPAC HAARGYTDRT SVMFGIPGFS YVYFIYGMYY CLNIVTETEG FPAAVLIRGL KLIEPLKANL SGPGILCKRL NITREHNKLD LTISHEFCVY ESHINLDYVC TPRIGISKGK EKFWRFKIF // ID 3MGH_XANAC Reviewed; 206 AA. AC Q8PJT1; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 1. DT 23-JAN-2007, entry version 28. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=XAC2449; OS Xanthomonas axonopodis pv. citri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=92829; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE011882; AAM37300.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE008923_GR; XAC2449. DR KEGG; xac:XAC2449; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 206 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100115. SQ SEQUENCE 206 AA; 21981 MW; ECCD0A3E32430B55 CRC64; MPAKPLPRTF YAHDARQVAP RLLNKVLVSA DGRCGRITEV EAYCGSDDPA AHSFRGMTPR TRVMFGAPGH LYVYFIYGMH WAINVVCGGA PGHAVLIRAL EPLDGIDRMQ AARGAAPFTA LTTGPGRLAQ AFGVTAADNG LDLSTAAARL WIEDDGAPPP SNPVATPRIG IRKAVDAPWR WVVADSRYLS RPLPRVTGKG TVLAGD // ID 3MGH_XANC5 Reviewed; 206 AA. AC Q3BSA6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 12-DEC-2006, entry version 11. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=XCV2626; OS Xanthomonas campestris pv. vesicatoria (strain 85-10). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=316273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005; RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., RA Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., RA Bonas U., Bartels D., Kaiser O.; RT "Insights into genome plasticity and pathogenicity of the plant RT pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed RT by the complete genome sequence."; RL J. Bacteriol. 187:7254-7266(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM039952; CAJ24303.1; -; Genomic_DNA. DR GenomeReviews; AM039952_GR; XCV2626. DR KEGG; xcv:XCV2626; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 206 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265072. SQ SEQUENCE 206 AA; 21888 MW; D4871931091E6599 CRC64; MPAKPLPRTF YAHDARHVAP QLLNKVLVSA DGRRGRITEV EAYCGSDDPA AHSFRGMTPR TRVMFGAPGH LYVYFIYGMH WAINAVCGGA PGHAVLIRAL EPLAGIDRMQ AARGAAPVTA LTTGPGRLAQ AFGVTAADNG LDLSTAAARL WIEDDGVPPP SHPVATPRIG IRKAVDAPWR WVVADSRYVS RPLPRVTGKG TAPAGD // ID 3MGH_XANC8 Reviewed; 207 AA. AC Q4UVR0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 12-DEC-2006, entry version 10. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=XC_1800; OS Xanthomonas campestris pv. campestris (strain 8004). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=314565; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15899963; DOI=10.1101/gr.3378705; RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., RA Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., RA Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.; RT "Comparative and functional genomic analyses of the pathogenicity of RT phytopathogen Xanthomonas campestris pv. campestris."; RL Genome Res. 15:757-767(2005). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000050; AAY48863.1; -; Genomic_DNA. DR GenomeReviews; CP000050_GR; XC_1800. DR KEGG; xcb:XC_1800; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 207 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000265071. SQ SEQUENCE 207 AA; 21755 MW; 8D9026EE54BD1A71 CRC64; MSLHSPLPRA FYAADARTVA PLLLNKVLVS ADGRRGRITE VEAYCGSEDA AAHSFRGMTP RTQVMFGAPG HLYVYFIYGM HWAINAVCGG APGHAVLIRA LEPLAGCDAM HAARGAAPFK SLTTGPGRLA QAFGVSAVDN GLDLTTGVAR LWIEDDGTPS PAAPLAGPRI GIRKAVELPW RWVVPGSAYL SRPLPRVSGA RASVTGD // ID 3MGH_XANCP Reviewed; 207 AA. AC Q8P8C7; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 1. DT 23-JAN-2007, entry version 28. DE Putative 3-methyladenine DNA glycosylase (EC 3.2.2.-). GN OrderedLocusNames=XCC2316; OS Xanthomonas campestris pv. campestris. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=340; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / NCPPB 528 / LMG 568; RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE012339; AAM41594.1; -; Genomic_DNA. DR HSSP; P29372; 1F6O. DR GenomeReviews; AE008922_GR; XCC2316. DR KEGG; xcc:XCC2316; -. DR HAMAP; MF_00527; -; 1. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase. FT CHAIN 1 207 Putative 3-methyladenine DNA glycosylase. FT /FTId=PRO_0000100116. SQ SEQUENCE 207 AA; 21765 MW; 16FD927E54BD1A72 CRC64; MSLHSPLPRA FYAADARTVA PLLLNKVLVS ADGRRGRITE VEAYCGSEDA AAHSFRGMTP RTQVMFGAPG HLYVYFIYGM HWAINAVCGG APGHAVLIRA LEPLAGCDAM HAARGAAPFK SLTTGPGRLA QAFGVSAVDN GLDLTTGVAR LWIEDDGTPP PAAPLAGPRI GIRKAVELPW RWVVPGSAYL SRPLPRVSGA RASVTGD // ID 3MG_ARATH Reviewed; 254 AA. AC Q39147; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 49. DE DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-methyladenine DNA DE glycosidase). GN Name=MAG; OrderedLocusNames=At3g12040; GN ORFNames=T21B14.14, MEC18.17, T21B14_115; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; TISSUE=Aerial part; RX MEDLINE=94181568; PubMed=8134381; RA Santerre A., Britt A.B.; RT "Cloning of a 3-methyladenine-DNA glycosylase from Arabidopsis RT thaliana."; RL Proc. Natl. Acad. Sci. U.S.A. 91:2240-2244(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20363099; PubMed=10907853; DOI=10.1093/dnares/7.3.217; RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. RT Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC RT and BAC clones."; RL DNA Res. 7:217-221(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine, and 7-methylguanine from the damaged DNA CC polymer formed by alkylation lesions (By similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine, 3-methylguanine, 7-methylguanine and 7- CC methyladenine. CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X76169; CAA53763.1; -; mRNA. DR EMBL; AP002040; BAB03116.1; -; Genomic_DNA. DR EMBL; AC069473; AAG51039.1; -; Genomic_DNA. DR UniGene; At.5389; -. DR HSSP; P29372; 1F4R. DR GenomeReviews; BA000014_GR; AT3G12040. DR KEGG; ath:At3g12040; -. DR TAIR; At3g12040; -. DR ArrayExpress; Q39147; -. DR GermOnline; AT3G12040; Arabidopsis thaliana. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW DNA damage; DNA repair; Hydrolase; Nuclear protein. FT CHAIN 1 254 DNA-3-methyladenine glycosylase. FT /FTId=PRO_0000100068. SQ SEQUENCE 254 AA; 28133 MW; 0BC880710D1BE1C5 CRC64; MKTPARRSKR VNQEESETNV TTRVVLRTRK TNCSKTRAAR VRPDYPLTRT TSESEMKLMP PEFFQIDALD LAPRLLGKFM RRDNVVLRIT EVEAYRPNDS ACHGRFGVTP RTAPVFGPGG HAYVYLCYGL HMMLNIVADK EGVGAAVLIR SCSPVSGMET IQERRGLKTD KPVLLNGPGK VGQALGLSTE WSHHPLYSPG GLELLDGGED VEKVMVGPRV GIDYALPEHV NALWRFAVAD TPWISAPKNT LKPL // ID 3MG_ENCCU Reviewed; 208 AA. AC Q8SQI1; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 23-JAN-2007, entry version 23. DE Probable DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3- DE methyladenine DNA glycosidase). GN OrderedLocusNames=ECU05_1590; GN and GN OrderedLocusNames=ECU11_0140; OS Encephalitozoon cuniculi. OC Eukaryota; Fungi; Microsporidia; Unikaryonidae; Encephalitozoon. OX NCBI_TaxID=6035; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-M1; RX MEDLINE=21576510; PubMed=11719806; DOI=10.1038/35106579; RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., RA Weissenbach J., Vivares C.P.; RT "Genome sequence and gene compaction of the eukaryote parasite RT Encephalitozoon cuniculi."; RL Nature 414:450-453(2001). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine, and 7-methylguanine from the damaged DNA CC polymer formed by alkylation lesions (By similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine, 3-methylguanine, 7-methylguanine and 7- CC methyladenine. CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL590445; CAD26679.1; -; Genomic_DNA. DR EMBL; AL590450; CAD25924.1; -; Genomic_DNA. DR HSSP; P29372; 1EWN. DR GenomeReviews; AL590445_GR; ECU05_1590. DR GenomeReviews; AL590450_GR; ECU11_0140. DR KEGG; ecu:ECU05_1590; -. DR KEGG; ecu:ECU11_0140; -. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW Complete proteome; DNA damage; DNA repair; Hydrolase; Nuclear protein. FT CHAIN 1 208 Probable DNA-3-methyladenine glycosylase. FT /FTId=PRO_0000100069. SQ SEQUENCE 208 AA; 23773 MW; A4A22F1DAD5B443F CRC64; MDMGIPCSQL ARRLLGKMLC RRIEGRTTKG MIVETEAYLG KEDKACHSYG GRRTERNSAM YMKAGTCYVY RIYGRYECFN ISSVEAGAGV LVRALEPLCG VSEMRERRGG RVKDRDIANG PSKLCIAMGI TRREIDKEWI AGSEKIWLEE GREVADPEIV AGRRIGIRNC GEWEEKKLRF YIRDNEFVSC IRRRELGNRK HGSVQQLP // ID 3MG_HUMAN Reviewed; 298 AA. AC P29372; Q13770; Q15275; Q15961; Q96BZ6; Q96S33; Q9NNX5; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 20-FEB-2007, entry version 81. DE DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-methyladenine DNA DE glycosidase) (ADPG) (3-alkyladenine DNA glycosylase) (N-methylpurine- DE DNA glycosylase). GN Name=MPG; Synonyms=AAG, ANPG, MID1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX MEDLINE=92021003; PubMed=1924375; RA Samson L., Derfler B., Boosalis M., Call K.; RT "Cloning and characterization of a 3-methyladenine DNA glycosylase RT cDNA from human cells whose gene maps to chromosome 16."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9127-9131(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX MEDLINE=93234512; PubMed=8475094; RA Vickers M.A., Vyas P., Harris P.C., Simmons D.L., Higgs D.R.; RT "Structure of the human 3-methyladenine DNA glycosylase gene and RT localization close to the 16p telomere."; RL Proc. Natl. Acad. Sci. U.S.A. 90:3437-3441(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21096910; PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., RA Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 RT Mb of the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-22; HIS-71; RP VAL-258 AND SER-298. RA Rieder M.J., Braun A.C., Montoya M.A., Chung M.-W., Nguyen C.P., RA Nguyen D.A., Livingston R.J., Poel C.L., Robertson P.D., RA Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.; RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 NUCLEOTIDE SEQUENCE [MRNA] OF 28-298. RX MEDLINE=91340707; PubMed=1874728; RA Chakravarti D., Ibeanu G.C., Tano K., Mitra S.; RT "Cloning and expression in Escherichia coli of a human cDNA encoding RT the DNA repair protein N-methylpurine-DNA glycosylase."; RL J. Biol. Chem. 266:15710-15715(1991). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-298. RX MEDLINE=91248199; PubMed=1645538; RA O'Connor T.R., Laval J.; RT "Human cDNA expressing a functional DNA glycosylase excising 3- RT methyladenine and 7-methylguanine."; RL Biochem. Biophys. Res. Commun. 176:1170-1177(1991). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 230-298. RX MEDLINE=93305988; PubMed=8318735; RA Kielman M., Smits R., Devi T., Fodde R., Bernini L.F.; RT "Homology of a 130-kb region enclosing the alpha-globin gene cluster, RT the alpha-locus controlling region, and two non-globin genes in human RT and mouse."; RL Mamm. Genome 4:314-323(1993). RN [10] RP INTERACTION WITH MBD1. RX PubMed=14555760; DOI=10.1073/pnas.2131819100; RA Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I., RA Shirakawa M., Kawasuji M., Nakao M.; RT "Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link RT transcriptional repression and DNA repair in chromatin."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS RP SPECTROMETRY. RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 80-199. RX MEDLINE=99005192; PubMed=9790531; DOI=10.1016/S0092-8674(00)81755-9; RA Lau A.Y., Scharer O.D., Samson L., Verdine G.L., Ellenberger T.; RT "Crystal structure of a human alkylbase-DNA repair enzyme complexed to RT DNA: mechanisms for nucleotide flipping and base excision."; RL Cell 95:249-258(1998). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine, and 7-methylguanine from the damaged DNA CC polymer formed by alkylation lesions. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine, 3-methylguanine, 7-methylguanine and 7- CC methyladenine. CC -!- SUBUNIT: Binds MBD1. CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1; CC IsoId=P29372-1; Sequence=Displayed; CC Name=2; CC IsoId=P29372-2; Sequence=VSP_003249; CC Name=3; CC IsoId=P29372-3; Sequence=VSP_003250; CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M74905; AAA58627.1; -; mRNA. DR EMBL; L10752; AAF77073.1; -; mRNA. DR EMBL; AE006462; AAK61213.1; -; Genomic_DNA. DR EMBL; AF499437; AAM14628.1; -; Genomic_DNA. DR EMBL; Z69720; CAA93540.1; -; Genomic_DNA. DR EMBL; BC014991; AAH14991.1; -; mRNA. DR EMBL; S51033; AAB19537.1; -; mRNA. DR EMBL; X56528; CAA39875.1; -; mRNA. DR EMBL; M71215; AAA58369.1; -; mRNA. DR EMBL; M99626; AAB46421.1; -; mRNA. DR PIR; A40798; A40798. DR PIR; A41230; A41230. DR PIR; A47471; A47471. DR PIR; JN0062; JN0062. DR UniGene; Hs.459596; -. DR PDB; 1BNK; X-ray; A=80-295. DR PDB; 1EWN; X-ray; A=80-298. DR PDB; 1F4R; X-ray; A=80-298. DR PDB; 1F6O; X-ray; A=80-298. DR Ensembl; ENSG00000103152; Homo sapiens. DR KEGG; hsa:4350; -. DR H-InvDB; HIX0012638; -. DR HGNC; HGNC:7211; MPG. DR MIM; 156565; gene. DR Reactome; REACT_216.1; DNA Repair. DR ArrayExpress; P29372; -. DR GermOnline; ENSG00000103152; Homo sapiens. DR RZPD-ProtExp; IOH12177; -. DR RZPD-ProtExp; RZPDo839G0465; -. DR RZPD-ProtExp; T1811; -. DR RZPD-ProtExp; V1179; -. DR GO; GO:0005654; C:nucleoplasm; TAS:ProtInc. DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc. DR GO; GO:0006284; P:base-excision repair; TAS:ProtInc. DR GO; GO:0006307; P:DNA dealkylation; TAS:ProtInc. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW 3D-structure; Alternative splicing; DNA damage; DNA repair; Hydrolase; KW Nuclear protein; Phosphorylation; Polymorphism. FT CHAIN 1 298 DNA-3-methyladenine glycosylase. FT /FTId=PRO_0000100065. FT MOD_RES 252 252 Phosphoserine. FT VAR_SEQ 1 12 MVTPALQMKKPK -> MPARSGA (in isoform 2). FT /FTId=VSP_003249. FT VAR_SEQ 195 196 HV -> QL (in isoform 3). FT /FTId=VSP_003250. FT VARIANT 22 22 K -> Q. FT /FTId=VAR_019138. FT VARIANT 64 64 P -> L (in dbSNP:rs2308315). FT /FTId=VAR_014831. FT VARIANT 71 71 Y -> H. FT /FTId=VAR_014832. FT VARIANT 120 120 R -> C (in dbSNP:rs2308313). FT /FTId=VAR_014833. FT VARIANT 141 141 R -> Q (in dbSNP:rs2308312). FT /FTId=VAR_014834. FT VARIANT 258 258 A -> V (in dbSNP:rs769193). FT /FTId=VAR_014835. FT VARIANT 298 298 A -> S (in dbSNP:rs2234949). FT /FTId=VAR_014836. FT CONFLICT 13 13 Q -> QV (in Ref. 3). FT CONFLICT 29 31 GQP -> ARA (in Ref. 7). FT CONFLICT 44 44 Q -> R (in Ref. 7). FT CONFLICT 69 71 GPY -> SKD (in Ref. 8). FT CONFLICT 82 82 H -> L (in Ref. 8). FT CONFLICT 134 134 A -> P (in Ref. 1). FT CONFLICT 287 287 V -> E (in Ref. 8). FT TURN 83 84 FT HELIX 88 91 FT HELIX 95 102 FT TURN 103 104 FT STRAND 106 110 FT TURN 112 113 FT STRAND 116 127 FT TURN 130 131 FT TURN 133 134 FT TURN 136 137 FT HELIX 138 140 FT STRAND 144 146 FT HELIX 147 150 FT TURN 153 154 FT STRAND 155 161 FT TURN 162 164 FT STRAND 165 171 FT TURN 175 176 FT STRAND 178 188 FT HELIX 190 196 FT TURN 197 198 FT HELIX 211 213 FT STRAND 214 217 FT HELIX 218 224 FT TURN 225 226 FT HELIX 229 231 FT TURN 232 233 FT TURN 236 237 FT STRAND 240 245 FT STRAND 256 259 FT TURN 262 263 FT HELIX 269 272 FT STRAND 276 279 FT TURN 280 281 FT TURN 283 284 FT HELIX 290 293 FT TURN 294 294 SQ SEQUENCE 298 AA; 32864 MW; 5067F838F70EAE96 CRC64; MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD AAQAPCPRER CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR AFLGQVLVRR LPNGTELRGR IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYI IYGMYFCMNI SSQGDGACVL LRALEPLEGL ETMRHVRSTL RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE AVWLERGPLE PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQA // ID 3MG_MOUSE Reviewed; 333 AA. AC Q04841; Q64182; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 20-FEB-2007, entry version 57. DE DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-methyladenine DNA DE glycosidase) (ADPG) (3-alkyladenine DNA glycosylase) (N-methylpurine- DE DNA glycosylase). GN Name=Mpg; Synonyms=Mid1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=FEB/N; TISSUE=Spleen; RX MEDLINE=95134354; PubMed=7832991; RA Tatsuka M., Ibeanu G.C., Izumi T., Narayan S., Ramana C.V., Kim N.K., RA Kang W., Roy G., Mitra S.; RT "Structural organization of the mouse DNA repair gene, N-methylpurine- RT DNA glycosylase."; RL DNA Cell Biol. 14:37-45(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93169718; PubMed=8435858; DOI=10.1093/carcin/14.2.175; RA Engelward B.P., Boosalis M.S., Chen B.J., Deng Z., Siciliano M.J., RA Samson L.D.; RT "Cloning and characterization of a mouse 3-methyladenine/7-methyl- RT guanine/3-methylguanine DNA glycosylase cDNA whose gene maps to RT chromosome 11."; RL Carcinogenesis 14:175-181(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96014285; PubMed=8589517; RA Kielman M.F., Smits R., Bernini L.F.; RT "Structure of the mouse 3-methyladenine DNA glycosylase gene and exact RT localization upstream of the alpha-globin gene cluster on chromosome RT 11."; RL Mamm. Genome 6:499-504(1995). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 250-324. RX MEDLINE=93305988; PubMed=8318735; RA Kielman M., Smits R., Devi T., Fodde R., Bernini L.F.; RT "Homology of a 130-kb region enclosing the alpha-globin gene cluster, RT the alpha-locus controlling region, and two non-globin genes in human RT and mouse."; RL Mamm. Genome 4:314-323(1993). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine, and 7-methylguanine from the damaged DNA CC polymer formed by alkylation lesions. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine, 3-methylguanine, 7-methylguanine and 7- CC methyladenine. CC -!- SUBUNIT: Binds MBD1 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X74509; CAA52615.1; -; Genomic_DNA. DR EMBL; X75038; CAA52615.1; JOINED; Genomic_DNA. DR EMBL; X75039; CAA52615.1; JOINED; Genomic_DNA. DR EMBL; X75040; CAA52615.1; JOINED; Genomic_DNA. DR EMBL; U10420; AAA19487.1; -; mRNA. DR EMBL; S81162; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; S81120; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; S81133; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; S81134; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014754; AAH14754.1; -; mRNA. DR EMBL; M99625; AAA02577.1; -; mRNA. DR PIR; A49003; A49003. DR PIR; I62129; I62129. DR UniGene; Mm.263161; -. DR UniGene; Mm.435524; -. DR HSSP; P29372; 1EWN. DR SMR; Q04841; 102-315. DR Ensembl; ENSMUSG00000020287; Mus musculus. DR KEGG; mmu:268395; -. DR MGI; MGI:97073; Mpg. DR ArrayExpress; Q04841; -. DR GermOnline; ENSMUSG00000020287; Mus musculus. DR GO; GO:0003905; F:alkylbase DNA N-glycosylase activity; IDA:MGI. DR GO; GO:0006284; P:base-excision repair; IMP:MGI. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR PANTHER; PTHR10429; PurDNA_glycsylse; 2. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW DNA damage; DNA repair; Hydrolase; Nuclear protein; Phosphorylation. FT CHAIN 1 333 DNA-3-methyladenine glycosylase. FT /FTId=PRO_0000100066. FT MOD_RES 272 272 Phosphoserine (By similarity). FT CONFLICT 14 14 S -> A (in Ref. 3). FT CONFLICT 319 324 PQQTAC -> LANSLL (in Ref. 5). SQ SEQUENCE 333 AA; 36488 MW; 453F707E7EA00BC6 CRC64; MPARGGSARP GRGSLKPVSV TLLPDTEQPP FLGRARRPGN ARAGSLVTGY HEVGQMPAPL SRKIGQKKQR LADSEQQQTP KERLLSTPGL RRSIYFSSPE DHSGRLGPEF FDQPAVTLAR AFLGQVLVRR LADGTELRGR IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYL IYGMYFCLNV SSQGAGACVL LRALEPLEGL ETMRQLRNSL RKSTVGRSLK DRELCSGPSK LCQALAIDKS FDQRDLAQDD AVWLEHGPLE SSSPAVVVAA ARIGIGHAGE WTQKPLRFYV QGSPWVSVVD RVAEQMDQPQ QTACSEGLLI VQK // ID 3MG_RAT Reviewed; 317 AA. AC P23571; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 20-FEB-2007, entry version 57. DE DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-methyladenine DNA DE glycosidase) (ADPG) (3-alkyladenine DNA glycosylase) (N-methylpurine- DE DNA glycosylase) (Fragment). GN Name=Mpg; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91006029; PubMed=1698614; RA O'Connor T.R., Laval F.; RT "Isolation and structure of a cDNA expressing a mammalian 3- RT methyladenine-DNA glycosylase."; RL EMBO J. 9:3337-3342(1990). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine, and 7-methylguanine from the damaged DNA CC polymer formed by alkylation lesions. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine, 3-methylguanine, 7-methylguanine and 7- CC methyladenine. CC -!- SUBUNIT: Binds MBD1 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC -!- CAUTION: Ref.1 sequence differs from that shown due to several CC frameshifts. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X56420; CAA39814.1; ALT_FRAME; mRNA. DR PIR; S12059; S12059. DR UniGene; Rn.11241; -. DR HSSP; P29372; 1EWN. DR SMR; P23571; 91-299. DR Ensembl; ENSRNOG00000020571; Rattus norvegicus. DR KEGG; rno:24561; -. DR RGD; 3106; Mpg. DR ArrayExpress; P23571; -. DR GermOnline; ENSRNOG00000020571; Rattus norvegicus. DR InterPro; IPR011034; FMT_C_like. DR InterPro; IPR003180; PurDNA_glycsylse. DR Gene3D; G3DSA:3.10.300.10; PurDNA_glycsylse; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR ProDom; PD009649; PurDNA_glycsylse; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. KW DNA damage; DNA repair; Hydrolase; Nuclear protein; Phosphorylation. FT CHAIN <1 317 DNA-3-methyladenine glycosylase. FT /FTId=PRO_0000100067. FT MOD_RES 258 258 Phosphoserine (By similarity). FT NON_TER 1 1 SQ SEQUENCE 317 AA; 34814 MW; 613849E4ADEF1BDB CRC64; SKEPVSVVLP DAEHPAFPGR TRRPGNARAG SQVTGSREVG QMPAPLSRKI GQKKQQLAQS EQQQTPKEKL SSTPGLLRSI YFSSPEDRPA RLGPEYFDQP AVTLARAFLG QVLVRRLADG TELRGRIVET EAYLGPEDEA AHSRGGRQTP RNRGMFMKPG TLYVYLIYGM YFCLNVSSQG AGACVLLRAL EPLEGLETMR QLRNSLRKST VGRSLKDREL CNGPSKLCQA LARSKSFDQR DLAQDEAVWL EHGPLESSSP AVVAAAAGIG HAGEWTQKPL RFYVQGSPWV SVVDRVAEQM YQPQQTACSD XALIVQK // ID 3O1D_COMTE Reviewed; 573 AA. AC Q06401; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 28-NOV-2006, entry version 28. DE 3-oxosteroid 1-dehydrogenase (EC 1.3.99.4). OS Comamonas testosteroni (Pseudomonas testosteroni). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=285; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 17410; RX MEDLINE=92041619; PubMed=1657885; RA Plesiat P., Grandguillot M., Harayama S., Vragar S., Michel-Briand Y.; RT "Cloning, sequencing, and expression of the Pseudomonas testosteroni RT gene encoding 3-oxosteroid delta 1-dehydrogenase."; RL J. Bacteriol. 173:7219-7227(1991). CC -!- FUNCTION: Dehydrogenates steroids by introducing a double bond in CC steroid ring A. CC -!- CATALYTIC ACTIVITY: A 3-oxosteroid + acceptor = a 3-oxo-Delta(1)- CC steroid + reduced acceptor. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Steroid catabolism; first step. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; peripheral membrane CC protein. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M68488; AAA25679.1; -; Genomic_DNA. DR PIR; A41319; A41319. DR GO; GO:0047571; F:3-oxosteroid 1-dehydrogenase activity; IEA:EC. DR InterPro; IPR003953; FAD_bind2_N. DR InterPro; IPR001100; Pyr_redox. DR Pfam; PF00890; FAD_binding_2; 1. DR PRINTS; PR00411; PNDRDTASEI. KW FAD; Flavoprotein; Inner membrane; Lipid metabolism; Membrane; KW Oxidoreductase; Steroid metabolism. FT CHAIN 1 573 3-oxosteroid 1-dehydrogenase. FT /FTId=PRO_0000064376. FT NP_BIND 7 36 FAD (By similarity). SQ SEQUENCE 573 AA; 62673 MW; 8E941AF569897734 CRC64; MAEQEYDLIV VGSGAGACWA PIRAQEQGLK TLVVEKTELF GGTSALSGGG IWIPLNYDQK TAGIKDDLET AFGYMKRCVR GMATDDRVLA YVETASKMAE YLRQIGIPYR AMAKYADYYP HIEGSRPGGR TMDPVDFNAA RLRVTALETM RPGPPGNQLF GRMSISAFEA HSMLSRELKS RFTILGIMLK YFLDYPWRNK TRRDRRMTGG QALVAGLLTA ANKARVEMWC NSPLKELVQD ASGRVTGVIV ERNGQRQQIN ARRGVLLGAG GFERNQEMRD QYLNKPTRLV DGNPCGRQYG DAHRAGQAWA HTGADGLVLG RAHHGCSQGA GLSRHFRGTL AAGVHGGQRQ GAALPQRVRP VSGIPAAMLA ENAKGNGGVP AWIVFDASFR AQNPMGPLMP GSAVPDSKVR KSWLNNVYWK GRRWKIWRAD RRGRAGLQVS ARRMTEYARA GKDLDFDRGG NVFDRYYGDP RLKNPNLGPI EKGPFYAMRL WPGEIGTKGG LLTDREGRVL DTQGRIIEGL YCVGNNSASV MAPAYAGAGS TLGPAMTFAF RAVADMVGKP LPLENPHLLG KTV // ID 3O1D_RHOOP Reviewed; 507 AA. AC Q04616; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 36. DE 3-oxosteroid 1-dehydrogenase (EC 1.3.99.4). OS Rhodococcus opacus (Nocardia opaca). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=37919; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=IMET 7030; RA Drobnic K.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, AND PROTEIN SEQUENCE OF RP 2-15. RX MEDLINE=93151836; PubMed=7916596; RA Drobnic K., Krizaj I., Gubensek F., Komel R.; RT "Improved purification of steroid 1:2-dehydrogenase from Nocardia RT opaca and partial characterization of its cloned gene sequence."; RL Biochem. Biophys. Res. Commun. 190:509-515(1993). CC -!- FUNCTION: Dehydrogenates steroids by introducing a double bond in CC steroid ring A. CC -!- CATALYTIC ACTIVITY: A 3-oxosteroid + acceptor = a 3-oxo-Delta(1)- CC steroid + reduced acceptor. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Steroid catabolism; first step. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; peripheral membrane CC protein. CC -!- INDUCTION: By steroids. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U59422; AAB02831.1; -; Genomic_DNA. DR PIR; PC1242; PC1242. DR GO; GO:0047571; F:3-oxosteroid 1-dehydrogenase activity; IEA:EC. DR InterPro; IPR003953; FAD_bind2_N. DR Pfam; PF00890; FAD_binding_2; 1. KW Direct protein sequencing; FAD; Flavoprotein; Inner membrane; KW Lipid metabolism; Membrane; Oxidoreductase; Steroid metabolism. FT INIT_MET 1 1 Removed. FT CHAIN 2 507 3-oxosteroid 1-dehydrogenase. FT /FTId=PRO_0000064377. FT NP_BIND 9 38 FAD (By similarity). SQ SEQUENCE 507 AA; 54005 MW; 067F865E9E7ED984 CRC64; MQDWTSECDL LVVGSGGGAL TGAYTAAAQG LTTIVLEKTD RFGGTSAYSG ASIWLPGTQV QERAGLPDST ENARSYLRAL LGDAESERQD AYVETAPAVV ALLEQNPNIE FEFRAFPDYY KAEGRMDTGR SINPLDLDPA DIGDLAGRCV RNCTKTDRMD HAPGRMIGGR ALIAVSAAVQ STARQNFAPE SVLTSLIVED GRVVGGLRSN PRYRQRIKAN RGVLMHAGGG FEGNAEMREQ AGTPGKAIWS MGPSGPTPAT RSPPELAGRR RNSLARSGVV LPRGRAARRR RLHGRVRGGL VVDSPGSVPQ RVASVRPVRT SHGCSPDDNG SAVPSFMIFD SREVTDCPPS ASRTRPPPST SKPEPGSVPT LSKNSLPRPD YRPERIAQHC RKVQRCRKLG VDEEFHRGED PYDAFFCPPN GGANAALTAI ENGPFYAARD RLSDLGTKGG LVTDVNGRVL RADGSAIDGL YAAGNTSASV APFYPGPGVP LGTAMVFSYR AAQDMAK // ID 3SHD_NEUCR Reviewed; 359 AA. AC P07046; Q7RVA2; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 23-JAN-2007, entry version 45. DE 3-dehydroshikimate dehydratase (EC 4.2.1.-) (DHS dehydratase) DE (DHSase). GN Name=qa-4; ORFNames=NCU06024; OS Neurospora crassa. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=5141; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX MEDLINE=89293848; PubMed=2525625; RA Geever R.F., Huiet L., Baum J.A., Tyler B.M., Patel V.B., RA Rutledge B.J., Case M.E., Giles N.H.; RT "DNA sequence, organization and regulation of the qa gene cluster of RT Neurospora crassa."; RL J. Mol. Biol. 207:15-34(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=85155494; PubMed=6241580; DOI=10.1016/0378-1119(84)90003-9; RA Rutledge B.J.; RT "Molecular characterization of the qa-4 gene of Neurospora crassa."; RL Gene 32:275-287(1984). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554; RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., RA Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., RA Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., RA Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., RA Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., RA Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., RA Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., RA Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., RA Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.; RT "The genome sequence of the filamentous fungus Neurospora crassa."; RL Nature 422:859-868(2003). CC -!- FUNCTION: Converts dehydroshikimate to protocatechuate. CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate CC biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 2 CC [final step]. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14603; CAA32750.1; -; Genomic_DNA. DR EMBL; M10139; AAA33613.1; -; Genomic_DNA. DR EMBL; AABX01000367; EAA30378.1; -; Genomic_DNA. DR PIR; A22421; A22421. DR BioCyc; NCRA-XX3-01:NCRA-XX3-01-009772-MONOMER; -. DR InterPro; IPR012307; Xylisom_TIMbarrl. DR Pfam; PF01261; AP_endonuc_2; 1. KW Lyase; Quinate metabolism. FT CHAIN 1 359 3-dehydroshikimate dehydratase. FT /FTId=PRO_0000064378. SQ SEQUENCE 359 AA; 40493 MW; AF3111E617320F12 CRC64; MPSKLAISSM SLGRCFAGHS LDSKLDAAQR YGYLGIELFY EDLVDVAEHL SNERPSPEGP FVEAQIAAAR HILQMCQARG LEVVCLQPFM HYDGLNDRAE HERRLEKLAL WIELAHELHT DIIQIPANFL PANQVSDNLD LIVSDLCKVA DIGAQALPPI RFAYESLCWS TRVDLWERCW DIVQRVDRPN FGICLDTFNI LGRIYADPTS PSGRTPNAKE AVRKSIANLV SRVDVSKVFY VQVVDAERLS KPLLPGHPYY NPEQPARMSW SRNCRLFYGE TEYGAYLPVK EVARALFHGI GFEGWVSLEL FNRRMSEEGP EVPEELAMRG AISWAKLVQD LRIPVEGPLV TMPRVSASL // ID 41KD_LACHE Reviewed; 353 AA. AC P17212; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 31-OCT-2006, entry version 26. DE 41 kDa protein. OS Lactobacillus helveticus. OG Plasmid pLJ1. OC Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1587; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Subsp. jugurti; RX MEDLINE=89350187; PubMed=2764571; RA Takiguchi R., Hashiba H., Aoyama K., Ishii S.; RT "Complete nucleotide sequence and characterization of a cryptic RT plasmid from Lactobacillus helveticus subsp. jugurti."; RL Appl. Environ. Microbiol. 55:1653-1655(1989). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J04240; AAB52500.1; -; Genomic_DNA. DR PIR; A43633; A43633. DR InterPro; IPR010724; RepA_N. DR Pfam; PF06970; RepA_N; 1. KW Plasmid. FT CHAIN 1 353 41 kDa protein. FT /FTId=PRO_0000068345. SQ SEQUENCE 353 AA; 41157 MW; 4CC885F9321996B9 CRC64; MEVFFMRRYS ATQINAELFW KFPKFLSINK KYVGLTNDDR MAYMLIKDRY RYSLSNNWID KDKNVYVYFT IDDLKELLHV GKNKVTRIKQ HLIDYGLLEI VKQGFDPQNK KNYPDRIYLL QPEYDPTDLI SQSSHASALE QSGIPKMGTR YQNEGNLDNK GKSDSENCNK DTSALEQSGI PKMGANKDNN SSDTIKDTIK DTDQWNFSTN NYTPEQVTAQ NQDLLSHLGE TLTGDKEAPM FLNKDSINLI AKWFRTPEGA SECISTILNA ANDSRKNAES QIGHHELYFE DYNNELKRMI TNRLRRYFNK MRTAKDGKIK NPKNYLYVSM RNMFDKWQND VLMAEKDKAN NKD // ID 41_BOVIN Reviewed; 617 AA. AC Q9N179; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 28-NOV-2006, entry version 34. DE Protein 4.1 (Band 4.1) (P4.1) (4.1R). GN Name=EPB41; Synonyms=E41P; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Japanese black; TISSUE=Bone marrow; RA Saito D., Inaba M., Koshino I., Matsumoto M., Ono K.; RT "The interaction of bovine red blood cell protein 4.1 with red blood RT cell membranes."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes (By similarity). CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin and DLG1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions (By similarity). CC -!- PTM: Phosphorylation on Tyr-413 reduces the ability of 4.1 to CC promote the assembly of the spectrin/actin/4.1 ternary complex (By CC similarity). CC -!- SIMILARITY: Contains 1 FERM 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; AF222767; AAF61703.1; -; mRNA. DR UniGene; Bt.33189; -. DR HSSP; P11171; 1GG3. DR SMR; Q9N179; 1-279. DR KEGG; bta:281753; -. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Gene3D; G3DSA:1.20.80.40; FERM; 1. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Cytoskeleton; Nuclear protein; Phosphorylation; KW Structural protein. FT CHAIN 1 617 Protein 4.1. FT /FTId=PRO_0000219388. FT DOMAIN 1 282 FERM. FT REGION 401 466 Spectrin--actin-binding. FT REGION 467 617 Carboxyl-terminal (CTD). FT MOD_RES 413 413 Phosphotyrosine (by EGFR) (By FT similarity). FT MOD_RES 465 465 Phosphoserine (by CDC2) (By similarity). SQ SEQUENCE 617 AA; 69258 MW; 5B49D5008AD900FB CRC64; MHCKVSLLDD TVYECVVEKH AKGQDLLKRV CEHLNLLEED YFGLAIWDNA TSKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVSGRLP CSFATLALLG SYTIQSELGD YDPELHGADY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG LLVYKEKLRI NRFPWPKVLK ISYKRSSFFI KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTIPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAV EPADRTPRPT SAPAIAPSPA AEGGVPGAPV KKAQKETVQV EVKQEEAPPE DAEPEPSEAW KKKRERLDGE NIYIRHSNLM LEDLDKSQEE IKKHHASISE LKKNFMESVP EPRPSEWDKR LSTHSPFRTL NINGQIPTGE GPPLVKTQTV TISDTANAVK SEIPTKDVPI VHTETKTITY EAAQTDDSNG DLDPGVLLTA QTITSETTSS TTTTQITKTV KGGISETRIE KRIVITGDAD IDHDQVLVQA IKEAKEQHPD MSVTKVVVHQ ETEISEE // ID 41_CANFA Reviewed; 810 AA. AC Q6Q7P4; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-NOV-2006, entry version 19. DE Protein 4.1 (Band 4.1) (P4.1) (4.1R). GN Name=EPB41; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Cocker spaniel; TISSUE=Kidney; RX PubMed=15525677; DOI=10.1091/mbc.E04-05-0426; RA Huang S.-C., Liu E.S., Chan S.-H., Munagala I.D., Cho H.T., RA Jagadeeswaran R., Benz E.J. Jr.; RT "Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 RT kinase."; RL Mol. Biol. Cell 16:117-127(2005). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes (By similarity). CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin and DLG1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in CC the C-terminal domain (By similarity). CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions (By similarity). CC -!- SIMILARITY: Contains 1 FERM 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; AY553843; AAS59144.1; -; mRNA. DR UniGene; Cfa.3914; -. DR SMR; Q6Q7P4; 211-489. DR Ensembl; ENSCAFG00000011677; Canis familiaris. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Gene3D; G3DSA:1.20.80.40; FERM; 1. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Cytoskeleton; Glycoprotein; Nuclear protein; KW Phosphorylation; Structural protein. FT CHAIN 1 810 Protein 4.1. FT /FTId=PRO_0000219389. FT DOMAIN 211 492 FERM. FT REGION 615 659 Spectrin--actin-binding. FT REGION 660 810 Carboxyl-terminal (CTD). FT COMPBIAS 680 752 Thr-rich. FT MOD_RES 61 61 Phosphothreonine (By similarity). FT MOD_RES 658 658 Phosphoserine (By similarity). SQ SEQUENCE 810 AA; 90688 MW; 8F033CCA3C157602 CRC64; MTTEKSLVAE AENSQHQQQK EEGEGVTNSG QQETQLEELS QEAAEGDNHC EQKLKTSNGD TPTHEDLTKN KERTSENRGL SRLFSSFLKR PKSQVSEEEG KDVESAKEKC EGGQKEIEFG TSLDEEIILK APIAAPEPEL KTDPSLDLHS LSSAETQPAQ EEHREDPDFE TKEGGGLEEC SKIEVKEESP ESKAERELKA SQKSIRRHRN MHCKVSLLDD TVYECVVEKH AKGQDLLKRV CEHLNLLEED YFGLAIWDNG ASKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVSGRLP CSFATLALLG SYTIQSELGD YDPELHGAEY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTLPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAV DSDRSPRPTS APAIAQSQDA EGTVPGAPVK KTVVSKAQKE TVKDEEKKEE GPPDQAEPEP TEVWKDLDKS QEEIKKHHAS ISELKKNFME SVPEPRPSEW DKRLSTHSPF RTLNINGQLP TGEGPPLVKT QTVTISDTAN SVKSEIPTKD VPIVHTETKT ITYEAAQTDD SNGDLDPGVL LTAQTITSET TSSTTTTQIT KTVKGGISET RIEKRIVITG DADIDHDQVL VQAIKEAKEQ HPDMSVTKVV VHQETEISEE // ID 41_CHICK Reviewed; 90 AA. AC P12264; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 20-FEB-2007, entry version 49. DE Erythroid protein 4.1 (Band 4.1) (Fragment). GN Name=EPB41; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RX MEDLINE=87260822; PubMed=3474611; RA Ngai J., Stack J.H., Moon R.T., Lazarides E.; RT "Regulated expression of multiple chicken erythroid membrane skeletal RT protein 4.1 variants is governed by differential RNA processing and RT translational control."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4432-4436(1987). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes (By similarity). CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin and DLG1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced; CC Name=1; CC IsoId=P12264-1; Sequence=Displayed; CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions. CC -!- SIMILARITY: Contains 1 FERM 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; M16962; AAA48762.1; -; mRNA. DR PIR; A27056; A27056. DR UniGene; Gga.2886; -. DR HSSP; P11171; 1GG3. DR SMR; P12264; 1-90. DR Ensembl; ENSGALG00000001326; Gallus gallus. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR011993; PH_type. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF00373; Band_41; 1. DR PROSITE; PS00660; FERM_1; PARTIAL. DR PROSITE; PS00661; FERM_2; PARTIAL. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Alternative splicing; Cytoskeleton; Nuclear protein; KW Phosphorylation; Structural protein. FT CHAIN <1 >90 Erythroid protein 4.1. FT /FTId=PRO_0000219392. FT DOMAIN <1 >90 FERM. FT NON_TER 1 1 FT NON_TER 90 90 SQ SEQUENCE 90 AA; 10395 MW; 8938A0C88816604A CRC64; EFLENAKKLS MYGVDLHHAK DLEGVDITLG VCSSGLLVYK DKLRINRFPW PKVLKISYKR SSFFIKIRPG EQEQYESTIG FKLPSYRAAK // ID 41_DROME Reviewed; 1698 AA. AC Q9V8R9; Q24440; Q24441; Q24442; Q9V8R8; Q9V8S0; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 06-FEB-2007, entry version 51. DE Protein 4.1 homolog (Protein coracle). GN Name=cora; ORFNames=CG11949; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND FUNCTION. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94215495; PubMed=8162854; RA Fehon R.G., Dawson I.A., Artavanis-Tsakonas S.; RT "A Drosophila homologue of membrane-skeleton protein 4.1 is associated RT with septate junctions and is encoded by the coracle gene."; RL Development 120:545-557(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 3 AND 4). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: An integral component of the septate junction. May play CC a role in cell-cell interactions that are necessary for proper CC development. Vital for embryonic development. CC -!- INTERACTION: CC Q9VHU9-1:CG9636; NbExp=1; IntAct=EBI-219149, EBI-219164; CC -!- SUBCELLULAR LOCATION: Cell junction; septate junction. CC Note=Septate junction in the apical-lateral domain of epithelial CC cells during embryonic and imaginal disk development. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1; CC IsoId=Q9V8R9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9V8R9-2; Sequence=VSP_000476, VSP_000477, VSP_000479, CC VSP_000480, VSP_000481; CC Name=3; CC IsoId=Q9V8R9-3; Sequence=VSP_000475, VSP_000478, VSP_000479; CC Name=4; CC IsoId=Q9V8R9-4; Sequence=VSP_000476, VSP_000477, VSP_000479; CC Name=5; CC IsoId=Q9V8R9-5; Sequence=VSP_000474, VSP_000478; CC -!- TISSUE SPECIFICITY: At onset of germ band retraction, expression CC is seen in epidermis, hindgut and foregut. During retraction, CC expression extends to tracheal branches and salivary glands. CC -!- DEVELOPMENTAL STAGE: Expressed weakly in 4-8 hours embryos, more CC abundant expression in 8-12 hours and remains throughout later CC embryonic and larval stages. CC -!- SIMILARITY: Contains 1 FERM 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; L27467; AAB59187.1; -; mRNA. DR EMBL; L27468; AAA28742.1; -; mRNA. DR EMBL; L27469; AAA28743.1; -; mRNA. DR EMBL; AE003796; AAF57591.1; -; Genomic_DNA. DR EMBL; AE003796; AAF57592.1; -; Genomic_DNA. DR EMBL; AE003796; AAF57593.1; -; Genomic_DNA. DR EMBL; AY070992; AAL48614.1; -; mRNA. DR PIR; T13800; T13800. DR UniGene; Dm.4694; -. DR HSSP; P11171; 1GG3. DR DIP; DIP:20283N; -. DR IntAct; Q9V8R9; -. DR Ensembl; CG11949; Drosophila melanogaster. DR KEGG; dme:Dmel_CG11949; -. DR FlyBase; FBgn0010434; cora. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-005495-MONOMER; -. DR GermOnline; CG11949; Drosophila melanogaster. DR GO; GO:0005918; C:septate junction; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase. DR GO; GO:0008362; P:embryonic cuticle biosynthetic process (sen...; TAS:FlyBase. DR GO; GO:0007163; P:establishment and/or maintenance of cell po...; NAS:FlyBase. DR GO; GO:0035321; P:maintenance of wing hair orientation; IMP:FlyBase. DR GO; GO:0006612; P:protein targeting to membrane; TAS:FlyBase. DR GO; GO:0035151; P:regulation of tracheal tube size; IMP:FlyBase. DR GO; GO:0007435; P:salivary gland morphogenesis; TAS:FlyBase. DR GO; GO:0019991; P:septate junction assembly; TAS:FlyBase. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR Gene3D; G3DSA:1.20.80.40; FERM; 1. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; FALSE_NEG. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Alternative splicing; Complete proteome; Developmental protein; KW Membrane. FT CHAIN 1 1698 Protein 4.1 homolog. FT /FTId=PRO_0000219394. FT DOMAIN 32 314 FERM. FT REGION 317 434 Hydrophilic. FT REGION 1286 1698 Carboxyl-terminal (CTD). FT COMPBIAS 404 449 Lys-rich. FT COMPBIAS 731 775 Ala-rich. FT COMPBIAS 1437 1643 Thr-rich. FT VAR_SEQ 1 312 Missing (in isoform 5). FT /FTId=VSP_000474. FT VAR_SEQ 409 409 K -> KSSTGTASASSQSSLEGDYETNLEIEAIEAEPPVQ FT (in isoform 2 and isoform 4). FT /FTId=VSP_000476. FT VAR_SEQ 409 409 K -> KLMRQSSTGTASASSQSSLEGDYETNLEIEAIEAEP FT PVQ (in isoform 3). FT /FTId=VSP_000475. FT VAR_SEQ 482 1480 Missing (in isoform 3 and isoform 5). FT /FTId=VSP_000478. FT VAR_SEQ 482 1290 Missing (in isoform 2 and isoform 4). FT /FTId=VSP_000477. FT VAR_SEQ 1554 1587 Missing (in isoform 2, isoform 3 and FT isoform 4). FT /FTId=VSP_000479. FT VAR_SEQ 1629 1635 VSSKTRT -> GGGGGGI (in isoform 2). FT /FTId=VSP_000480. FT VAR_SEQ 1636 1698 Missing (in isoform 2). FT /FTId=VSP_000481. FT CONFLICT 970 970 I -> V (in Ref. 1; AAB59187). SQ SEQUENCE 1698 AA; 184168 MW; 93940FC4F1ACEB83 CRC64; MPAEIKPSAP AEPETPTKSK PKSSSSSHGK PALARVTLLD GSLLDVSIDR KAIGRDVINS ICAGLNLIEK DYFGLTYETP TDPRTWLDLE KPVSKFFRTD TWPLTFAVKF YPPEPSQLKE DITRYHLCLQ VRNDILEGRL PCTFVTHALL GSYLVQSEMG DYDAEEMPTR AYLKDFKIAP NQTAELEDKV MDLHKTHKGQ SPAEAELHYL ENAKKLAMYG VDLHPAKDSE GVDIMLGVCA SGLLVYRDKL RINRFAWPKI LKISYKRHHF YIKIRPGEFE QYESTIGFKL ANHRAAKKLW KSCVEHHTFF RLMTPEPVSK SKMFPVFGST YRYKGRTQAE STNTPVDRTP PKFNRTLSGA RLTSRSMDAL ALAEKEKVAR KSSTLDHRGD RNADGDAHSR SPIKNKKEKD ADKEAKLREK KQKEKEEKER KEREKRELEE KKKAEKAAKA ALAAGAAAGA AVNGNDELND SNKSDKSSGR RGVGIFSSGR KSKSGSPSKD GKDKSGKDKD KEVGRLGLVV TSGLGDNQQD QNLDEAARNA AKNRGSTTPG VTRQYEYAVD NDGNTSPTRK SYTPGGFRYD QDPNSRKSGA DGQEQLSPTS QQKKIGLAFN YAPGNENALK ETAEKLKAGQ LSPRTQDKLN RGQLSPKSRA KLLQDPLLSP TTRAKLQGSA VDAAAVPLSD SQKRSYSPTK GPQGYSSGAP GSYKPISDPT ADFLESQRYN KEPGYVGPSK ADVAAGLAGA AGSKKPGSPT KTGKGAPGAA AAAAAGAAGA AAAAAKPKKR RVKIMVITSK FDPSTKRIDA ENGSIEHSTG ILDPATGLID TKYGVIDPKK GTLEALNTKT GKKEVFQGDV DGKTGNLHLV SGVADPKTGR LDDTLGQIVC ITPQDNPVVE LTVITSRIDP ATGKIDTVNG DVERSLGVLN LDTGLLDTKY GEINTRTGEL KAIDPKSGKI VVSKNVKVDP GTGQITILGI VDPKTNKIDP NQGRLIEVGQ QIDPIVEVTS LAGKFDSKRN IIDPKTAQVE TSGGQFDPKA GKIDTKYGQI DLVKHTITFN DPKSGKTVTR DIKIEPTTGQ IVLKNQVNPK NNKPDKDYAR IISLRIVQQR VDPATKAPIT EVSASKDKDI VVDPKSNQIW VPTGATDPAT KEQQYISSSV DPKTGYVITI YGYLDPKTNE IKKQTKLDPN TIKIEPTSGK IYTATGEVDQ ATGEPLYAAT QVDPESGEVY TKLARVDPKT GKIVIVRILL ISKTDERGRP EEIDPSTCEI DPVSGRVLKF FNKTVYVYNM IDPVTGEIVQ VDPNDPRFAG ARTTVTHTMT LTGEIDPVTG RIKSEYGDID PNTGDIDPAT AVTDPVTGKL ILNYAQIDPS HFGKQAQVQT TTETVPITRQ QFFDGVKHIS KGALRRDSEG SSDDDMTAQY GADQVNEILI GSPAGQAGGK LGKPVSTPTV VKTTTKQVLT KNIDGVTHNV EEEVRNLGTG EVTYSTQEHK ADATPTDLSG AYVTATAVTT RTATTHEDLG KNAKTEQLEE KTVATTRTHD PNKQQQRVVT QEVKTTATVT SGDQYQRRDS VSSTSSGDSG TPIDGPYDGA SVVRTDNQKS PLFTTSATTG PHVESTRVVL GEDTPGFSGH GEIISTQTVS SKTRTVETIT YKTERDGIVE TRVEQKITIQ SDGDPIDHDK ALAEAIQEAT AMNPDMTVEK IEIQQQTQ // ID 41_HUMAN Reviewed; 864 AA. AC P11171; P11176; Q14245; Q5TB35; Q5VXN8; Q8IXV9; Q9Y578; Q9Y579; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 4. DT 20-FEB-2007, entry version 89. DE Protein 4.1 (Band 4.1) (P4.1) (EPB4.1) (4.1R). GN Name=EPB41; Synonyms=E41P; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND PROTEIN SEQUENCE OF RP 378-393. RC TISSUE=Reticulocyte; RX MEDLINE=87092279; PubMed=3467321; RA Conboy J.G., Kan Y.W., Shohet S.B., Mohandas N.; RT "Molecular cloning of protein 4.1, a major structural element of the RT human erythrocyte membrane skeleton."; RL Proc. Natl. Acad. Sci. U.S.A. 83:9512-9516(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6). RX MEDLINE=89132003; PubMed=3223413; RA Tang T.K., Leto T.L., Marchesi V.T., Benz E.J. Jr.; RT "Expression of specific isoforms of protein 4.1 in erythroid and non- RT erythroid tissues."; RL Adv. Exp. Med. Biol. 241:81-95(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6). RX MEDLINE=88234496; PubMed=3375238; RA Tang T.K., Leto T.L., Correas I., Alonso M.A., Marchesi V.T., RA Benz E.J. Jr.; RT "Selective expression of an erythroid-specific isoform of protein RT 4.1."; RL Proc. Natl. Acad. Sci. U.S.A. 85:3713-3717(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX MEDLINE=91217063; PubMed=2022644; RA Conboy J.G., Chan J.Y.C., Chasis J.A., Kan Y.W., Mohandas N.; RT "Tissue- and development-specific alternative RNA splicing regulates RT expression of multiple isoforms of erythroid membrane protein 4.1."; RL J. Biol. Chem. 266:8273-8280(1991). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Huang S.C., Wang C., Lichtenauer U., Vortmeyer A., Zhuang Z.; RT "Sequence of protein 4.1 from a human neuroblastoma cell line: LAN5."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., RA Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 157-227, AND VARIANT ILE-214. RA Lichtenauer U., Huang S.C., Vortmeyer A., Zhuang Z.; RT "Valine to isoleucine polymorphism in exon 4 of human protein 4.1."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE OF 669-864 (ISOFORM 4), AND ALTERNATIVE SPLICING. RX MEDLINE=89057876; PubMed=3194408; RA Conboy J.G., Chan J., Mohandas N., Kan Y.W.; RT "Multiple protein 4.1 isoforms produced by alternative splicing in RT human erythroid cells."; RL Proc. Natl. Acad. Sci. U.S.A. 85:9062-9065(1988). RN [10] RP PROTEIN SEQUENCE OF 534-541; 693-701 AND 793-794, AND PHOSPHORYLATION RP AT SERINE RESIDUES. RX MEDLINE=91027920; PubMed=2171679; DOI=10.1016/0167-4889(90)90095-U; RA Horne W.C., Prinz W.C., Tang E.K.; RT "Identification of two cAMP-dependent phosphorylation sites on RT erythrocyte protein 4.1."; RL Biochim. Biophys. Acta 1055:87-92(1990). RN [11] RP PROTEIN SEQUENCE OF 648-714. RX MEDLINE=87008553; PubMed=3531202; RA Correas I., Speicher D.W., Marchesi V.T.; RT "Structure of the spectrin-actin binding site of erythrocyte protein RT 4.1."; RL J. Biol. Chem. 261:13362-13366(1986). RN [12] RP STRUCTURE OF CARBOHYDRATES. RX MEDLINE=90036892; PubMed=2808371; RA Inaba M., Maede Y.; RT "O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple RT protein 4.1 isoforms regulated by alternative pathways."; RL J. Biol. Chem. 264:18149-18155(1989). RN [13] RP PHOSPHORYLATION AT TYR-660. RX MEDLINE=91271361; PubMed=1647028; RA Subrahmanyan G., Bertics P.J., Anderson R.A.; RT "Phosphorylation of protein 4.1 on tyrosine-418 modulates its function RT in vitro."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5222-5226(1991). RN [14] RP INTERACTION WITH DLG1. RX MEDLINE=95024052; PubMed=7937897; RA Lue R.A., Marfatia S.M., Branton D., Chishti A.H.; RT "Cloning and characterization of hdlg: the human homologue of the RT Drosophila discs large tumor suppressor binds to protein 4.1."; RL Proc. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994). RN [15] RP INTERACTION WITH CALMODULIN. RX MEDLINE=20158947; PubMed=10692436; DOI=10.1074/jbc.275.9.6360; RA Nunomura W., Takakuwa Y., Parra M., Conboy J.G., Mohandas N.; RT "Ca(2+)-dependent and Ca(2+)-independent calmodulin binding sites in RT erythrocyte protein 4.1. Implications for regulation of protein 4.1 RT interactions with transmembrane proteins."; RL J. Biol. Chem. 275:6360-6367(2000). RN [16] RP INTERACTION WITH CENPJ. RX MEDLINE=20459281; PubMed=11003675; RX DOI=10.1128/MCB.20.20.7813-7825.2000; RA Hung L.-Y., Tang C.J., Tang T.K.; RT "Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) RT which is associated with the gamma-tubulin complex."; RL Mol. Cell. Biol. 20:7813-7825(2000). RN [17] RP CHARACTERIZATION OF C-TERMINAL DOMAIN. RX MEDLINE=21325946; PubMed=11432737; RA Scott C., Phillips G.W., Baines A.J.; RT "Properties of the C-terminal domain of 4.1 proteins."; RL Eur. J. Biochem. 268:3709-3717(2001). RN [18] RP SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22421379; PubMed=12427749; DOI=10.1074/jbc.M201521200; RA Luque C.M., Perez-Ferreiro C.M., Perez-Gonzalez A., Englmeier L., RA Koffa M.D., Correas I.; RT "An alternative domain containing a leucine-rich sequence regulates RT nuclear cytoplasmic localization of protein 4.1R."; RL J. Biol. Chem. 278:2686-2691(2003). RN [19] RP MUTAGENESIS OF THR-60 AND SER-712, AND PHOSPHORYLATION AT THR-60 AND RP SER-712. RX PubMed=15525677; DOI=10.1091/mbc.E04-05-0426; RA Huang S.-C., Liu E.S., Chan S.-H., Munagala I.D., Cho H.T., RA Jagadeeswaran R., Benz E.J. Jr.; RT "Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 RT kinase."; RL Mol. Biol. Cell 16:117-127(2005). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 210-488. RX MEDLINE=20473226; PubMed=11017195; DOI=10.1038/82819; RA Han B.-G., Nunomura W., Takakuwa Y., Mohandas N., Jap B.K.; RT "Protein 4.1R core domain structure and insights into regulation of RT cytoskeletal organization."; RL Nat. Struct. Biol. 7:871-875(2000). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes. CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin, CENPJ and DLG1. Also found to CC associate with contractile apparatus and tight junctions. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; CC IsoId=P11171-1; Sequence=Displayed; CC Name=2; CC IsoId=P11171-2; Sequence=VSP_000470; CC Name=3; CC IsoId=P11171-3; Sequence=VSP_000468, VSP_000471; CC Name=4; Synonyms=Erythroid; CC IsoId=P11171-4; Sequence=VSP_000468, VSP_000470, VSP_000473; CC Name=5; Synonyms=Non-erythroid A; CC IsoId=P11171-5; Sequence=VSP_000469, VSP_000470, VSP_000472; CC Name=6; Synonyms=Non-erythroid B; CC IsoId=P11171-6; Sequence=VSP_000468, VSP_000469, VSP_000470, CC VSP_000472; CC Name=7; CC IsoId=P11171-7; Sequence=VSP_000471, VSP_012872, VSP_012873; CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions. CC -!- PTM: Phosphorylation on Tyr-660 reduces the ability of 4.1 to CC promote the assembly of the spectrin/actin/4.1 ternary complex. CC -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in CC the C-terminal domain. CC -!- DISEASE: Defects in EPB41 are the cause of elliptocytosis 1 (EL1) CC [MIM:130500]. EL1 is a rhesus-linked form of hereditary CC elliptocytosis. Elliptocytosis (also known as ovalocytosis) is a CC genetically heterogeneous, autosomal dominant hematologic CC disorder. It is characterized by variable hemolytic anemia and CC elliptical or oval red cell shape. CC -!- DISEASE: Defects in EPB41 are a cause of hereditary CC pyropoikilocytosis (HPP) [MIM:266140]. HPP is an autosomal CC recessive hematologic disorder characterized by hemolytic anemia, CC microspherocytosis, poikilocytosis, and an unusual thermal CC sensitivity of red cells. CC -!- SIMILARITY: Contains 1 FERM 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; M14993; AAA35795.1; -; mRNA. DR EMBL; J03796; AAA35793.1; -; mRNA. DR EMBL; J03796; AAA35794.1; -; mRNA. DR EMBL; M61733; AAA35797.1; -; mRNA. DR EMBL; AF156225; AAD42222.1; -; mRNA. DR EMBL; AL138785; CAI21967.1; -; Genomic_DNA. DR EMBL; AL357500; CAI21967.1; JOINED; Genomic_DNA. DR EMBL; AL138785; CAI21968.1; -; Genomic_DNA. DR EMBL; AL138785; CAI21970.1; -; Genomic_DNA. DR EMBL; AL357500; CAI21970.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71636.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71636.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71637.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71637.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71638.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71638.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71639.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71639.1; JOINED; Genomic_DNA. DR EMBL; BC039079; AAH39079.1; -; mRNA. DR EMBL; AF156226; AAD42223.1; -; Genomic_DNA. DR PIR; A39810; MMHUE4. DR UniGene; Hs.175437; -. DR UniGene; Hs.644412; -. DR PDB; 1GG3; X-ray; A/B/C=210-488. DR DIP; DIP:17032N; -. DR GlycoSuiteDB; P11171; -. DR Ensembl; ENSG00000159023; Homo sapiens. DR KEGG; hsa:2035; -. DR HGNC; HGNC:3377; EPB41. DR MIM; 130500; gene+phenotype. DR MIM; 266140; phenotype. DR ArrayExpress; P11171; -. DR GermOnline; ENSG00000159023; Homo sapiens. DR RZPD-ProtExp; D0003; -. DR RZPD-ProtExp; E0753; -. DR RZPD-ProtExp; IOH27460; -. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0043234; C:protein complex; IDA:UniProtKB. DR GO; GO:0008091; C:spectrin; TAS:ProtInc. DR GO; GO:0005545; F:phosphatidylinositol binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc. DR GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; NAS:UniProtKB. DR GO; GO:0008015; P:circulation; TAS:ProtInc. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Gene3D; G3DSA:1.20.80.40; FERM; 1. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW 3D-structure; Actin-binding; Alternative splicing; Cytoskeleton; KW Direct protein sequencing; Elliptocytosis; Glycoprotein; KW Hereditary hemolytic anemia; Nuclear protein; Phosphorylation; KW Polymorphism; Pyropoikilocytosis; Structural protein. FT CHAIN 1 864 Protein 4.1. FT /FTId=PRO_0000219390. FT DOMAIN 210 491 FERM. FT REGION 494 614 Hydrophilic. FT REGION 615 713 Spectrin--actin-binding. FT REGION 714 864 Carboxyl-terminal (CTD). FT MOD_RES 60 60 Phosphothreonine (by CDC2). FT MOD_RES 660 660 Phosphotyrosine (by EGFR). FT MOD_RES 712 712 Phosphoserine (by CDC2). FT VAR_SEQ 1 209 Missing (in isoform 3, isoform 4 and FT isoform 6). FT /FTId=VSP_000468. FT VAR_SEQ 228 262 Missing (in isoform 5 and isoform 6). FT /FTId=VSP_000469. FT VAR_SEQ 616 648 Missing (in isoform 2, isoform 4, isoform FT 5 and isoform 6). FT /FTId=VSP_000470. FT VAR_SEQ 635 648 Missing (in isoform 3 and isoform 7). FT /FTId=VSP_000471. FT VAR_SEQ 649 669 Missing (in isoform 5 and isoform 6). FT /FTId=VSP_000472. FT VAR_SEQ 729 733 PPLVK -> VSTLS (in isoform 7). FT /FTId=VSP_012872. FT VAR_SEQ 734 864 Missing (in isoform 7). FT /FTId=VSP_012873. FT VAR_SEQ 772 805 Missing (in isoform 4). FT /FTId=VSP_000473. FT VARIANT 214 214 V -> I. FT /FTId=VAR_009122. FT MUTAGEN 60 60 T->A: Loss of CDC2-mediated FT phosphorylation. Abolishes targeting onto FT the mitotic spindle; when associated with FT A-712. FT MUTAGEN 712 712 S->A: Loss of CDC2-mediated FT phosphorylation. Abolishes targeting onto FT the mitotic spindle; when associated with FT A-60. FT CONFLICT 51 51 Q -> H (in Ref. 5). FT CONFLICT 76 76 S -> N (in Ref. 5). FT CONFLICT 168 168 F -> S (in Ref. 8). FT CONFLICT 259 259 A -> T (in Ref. 5). FT CONFLICT 665 665 N -> S (in Ref. 5). FT CONFLICT 669 669 E -> K (in Ref. 9). FT CONFLICT 679 679 K -> E (in Ref. 5). FT CONFLICT 802 802 Q -> K (in Ref. 2, 3, 7 and 9). FT CONFLICT 852 852 K -> L (in Ref. 9). FT CONFLICT 863 863 D -> E (in Ref. 9). FT STRAND 211 215 FT TURN 217 218 FT STRAND 221 225 FT TURN 228 229 FT HELIX 232 243 FT TURN 244 245 FT STRAND 250 252 FT STRAND 254 256 FT STRAND 259 261 FT TURN 267 268 FT HELIX 271 274 FT TURN 275 277 FT STRAND 280 285 FT HELIX 293 295 FT HELIX 299 314 FT TURN 315 316 FT HELIX 322 337 FT TURN 342 343 FT HELIX 350 352 FT HELIX 361 373 FT HELIX 379 392 FT TURN 394 397 FT STRAND 399 402 FT TURN 406 407 FT STRAND 412 426 FT STRAND 430 433 FT HELIX 434 436 FT STRAND 439 443 FT TURN 444 445 FT STRAND 446 450 FT STRAND 454 458 FT STRAND 462 466 FT HELIX 470 486 SQ SEQUENCE 864 AA; 97017 MW; B466E7A9D7FBF12B CRC64; MTTEKSLVTE AENSQHQQKE EGEEAINSGQ QEPQQEESCQ TAAEGDNWCE QKLKASNGDT PTHEDLTKNK ERTSESRGLS RLFSSFLKRP KSQVSEEEGK EVESDKEKGE GGQKEIEFGT SLDEEIILKA PIAAPEPELK TDPSLDLHSL SSAETQPAQE ELREDPDFEI KEGEGLEECS KIEVKEESPQ SKAETELKAS QKPIRKHRNM HCKVSLLDDT VYECVVEKHA KGQDLLKRVC EHLNLLEEDY FGLAIWDNAT SKTWLDSAKE IKKQVRGVPW NFTFNVKFYP PDPAQLTEDI TRYYLCLQLR QDIVAGRLPC SFATLALLGS YTIQSELGDY DPELHGVDYV SDFKLAPNQT KELEEKVMEL HKSYRSMTPA QADLEFLENA KKLSMYGVDL HKAKDLEGVD IILGVCSSGL LVYKDKLRIN RFPWPKVLKI SYKRSSFFIK IRPGEQEQYE STIGFKLPSY RAAKKLWKVC VEHHTFFRLT STDTIPKSKF LALGSKFRYS GRTQAQTRQA SALIDRPAPH FERTASKRAS RSLDGAAAVD SADRSPRPTS APAITQGQVA EGGVLDASAK KTVVPKAQKE TVKAEVKKED EPPEQAEPEP TEAWKVEKTH IEVTVPTSNG DQTQKLAEKT EDLIRMRKKK RERLDGENIY IRHSNLMLED LDKSQEEIKK HHASISELKK NFMESVPEPR PSEWDKRLST HSPFRTLNIN GQIPTGEGPP LVKTQTVTIS DNANAVKSEI PTKDVPIVHT ETKTITYEAA QTDDNSGDLD PGVLLTAQTI TSETPSSTTT TQITKTVKGG ISETRIEKRI VITGDADIDH DQVLVQAIKE AKEQHPDMSV TKVVVHQETE IADE // ID 41_MOUSE Reviewed; 858 AA. AC P48193; Q68FF1; Q6NVF5; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 20-FEB-2007, entry version 55. DE Protein 4.1 (Band 4.1) (P4.1) (4.1R). GN Name=Epb41; Synonyms=Epb4.1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING. RC STRAIN=BALB/c; RX MEDLINE=93155238; PubMed=8429050; RA Huang J.-P., Tang C.-J.C., Kou G.-H., Marchesi V.T., Benz E.J. Jr., RA Tang T.K.; RT "Genomic structure of the locus encoding protein 4.1. Structural basis RT for complex combinational patterns of tissue-specific alternative RNA RT splicing."; RL J. Biol. Chem. 268:3758-3766(1993). 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 PROTEIN SEQUENCE OF 709-713, MASS SPECTROMETRY, AND CHARACTERIZATION RP OF CARBOXY-TERMINAL DOMAIN. RX MEDLINE=21325946; PubMed=11432737; RA Scott C., Phillips G.W., Baines A.J.; RT "Properties of the C-terminal domain of 4.1 proteins."; RL Eur. J. Biochem. 268:3709-3717(2001). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes (By similarity). CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin and DLG1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=A number of isoforms are produced; CC Name=1; CC IsoId=P48193-1; Sequence=Displayed; CC Name=2; CC IsoId=P48193-2; Sequence=VSP_012874; CC Note=No experimental confirmation available; CC -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in CC the C-terminal domain (By similarity). CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions. CC -!- PTM: Phosphorylation on Tyr-654 reduces the ability of 4.1 to CC promote the assembly of the spectrin/actin/4.1 ternary complex. CC -!- SIMILARITY: Contains 1 FERM 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; L00919; AAA37122.1; -; mRNA. DR EMBL; L00919; AAA37123.1; -; mRNA. DR EMBL; BC068138; AAH68138.1; -; mRNA. DR EMBL; BC079875; AAH79875.1; -; mRNA. DR PIR; A46613; A46613. DR UniGene; Mm.30038; -. DR UniGene; Mm.432474; -. DR HSSP; P11171; 1GG3. DR SMR; P48193; 211-489. DR Ensembl; ENSMUSG00000028906; Mus musculus. DR MGI; MGI:95401; Epb4.1. DR ArrayExpress; P48193; -. DR GermOnline; ENSMUSG00000028906; Mus musculus. DR RZPD-ProtExp; IOM18602; -. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Gene3D; G3DSA:1.20.80.40; FERM; 1. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Alternative splicing; Cytoskeleton; KW Direct protein sequencing; Glycoprotein; Nuclear protein; KW Phosphorylation; Structural protein. FT CHAIN 1 858 Protein 4.1. FT /FTId=PRO_0000219391. FT DOMAIN 211 492 FERM. FT REGION 495 608 Hydrophilic. FT REGION 609 707 Spectrin--actin-binding. FT REGION 710 858 Carboxyl-terminal (CTD). FT MOD_RES 62 62 Phosphothreonine (By similarity). FT MOD_RES 654 654 Phosphotyrosine (By similarity). FT MOD_RES 706 706 Phosphoserine (By similarity). FT VAR_SEQ 610 663 Missing (in isoform 2). FT /FTId=VSP_012874. FT CONFLICT 1 3 MTT -> EPLKGREPRRARTRPGPARPGPCQVPVLCSP FT (in Ref. 2). FT CONFLICT 8 8 V -> A (in Ref. 2). FT CONFLICT 232 233 NL -> KG (in Ref. 2). FT CONFLICT 443 443 S -> Y (in Ref. 2). FT CONFLICT 576 576 R -> A (in Ref. 2). SQ SEQUENCE 858 AA; 95990 MW; 5F2FEF077946134E CRC64; MTTEKSLVAE AENSQHQQQK EEGEGATNSG QQETQLEEAS QAAAAEGSDQ GEQKLKASNG DTPTHEDLTK NKERTSESRG LSRLLSSFLK RPKSQVSEEE GREVESEKEK GEGGQKEIEL GNSLDEDIIL KAPIAAPEPE LKTDPSLDLH SLSSIETQPA QEEHREDPDS ETKEGEGIEE CSGTEVKEDP ESRAEREPEA SQKPVRRHRN MHCKVSLLDD TVYECVVEKH ANLQDLLKRV CEHLNLLEED YFGLALWDSA TSKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVAGRLP CSFATLALLG SYTIQSELGD YDPELHGMDY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG LLVYKDKLRI NRFPWPKVLK ISSKRSSFFI KIRPGEQEHY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTIPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAA ESTDRSPRPT SAPAIAQSQV TEGPGRPIKK TPKEAVKVEE KRGEEPAEPA EPEPTEAWKV EKTHTEVTVP TSNGDQTQKL AGKGEDLIRM RKKKRERLDG ENIYIRHSNL MLEDLDKSQE EIKKHHASIS ELKKNFMESV PEPRPSEWDK RLSTHSPFRT LNINGQVPTG DGPPLVKTQT VTISDTANAV KSEIPTKDVP IVHTETKTIT YEAAQTEDSN GDLDPGVLLT AQTITSETTS STTTTQITKT VKGGISETRI EKRIVITGDA DIDHDQVLVQ AIKEAKEQHP DMSVTKVVVH QETEISEE // ID 41_XENLA Reviewed; 801 AA. AC P11434; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 20-FEB-2007, entry version 59. DE Cytoskeletal protein 4.1 (Band 4.1). GN Name=epb41; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90249600; PubMed=2186944; RA Spencer M., Giebelhaus D.H., Kelly G.M., Bicknell J., Florio S.K., RA Bunt-Milam A., Moon R.T.; RT "Membrane skeleton protein 4.1 in developing Xenopus: expression in RT postmitotic cells of the retina."; RL Dev. Biol. 139:279-291(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-550. RX MEDLINE=88223353; PubMed=2453290; RA Giebelhaus D.H., Eib D.W., Moon R.T.; RT "Antisense RNA inhibits expression of membrane skeleton protein 4.1 RT during embryonic development of Xenopus."; RL Cell 53:601-615(1988). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- TISSUE SPECIFICITY: Found exclusively in photoreceptors following CC the terminal mitosis of retinal neurons. When retinal CC synaptogenesis is complete, protein 4.1 is also expressed in the CC inner retina. In adult amphibian retinas, protein 4.1 is detected CC in photoreceptors, bipolar cells, and ganglion cell axons. CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions. CC -!- SIMILARITY: Contains 1 FERM 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; M20621; AAA49695.1; -; mRNA. DR PIR; A37353; A37353. DR UniGene; Xl.12931; -. DR HSSP; P11171; 1GG3. DR SMR; P11434; 193-471. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Gene3D; G3DSA:1.20.80.40; FERM; 1. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Cytoskeleton; Nuclear protein; Phosphorylation; KW Structural protein. FT CHAIN 1 801 Cytoskeletal protein 4.1. FT /FTId=PRO_0000219393. FT DOMAIN 193 474 FERM. FT REGION 477 587 Hydrophilic. FT REGION 588 651 Spectrin--actin-binding. FT REGION 653 801 Carboxyl-terminal (CTD). SQ SEQUENCE 801 AA; 89429 MW; 07FA508552359A0F CRC64; MTTEKGLLAE AESPPQDQKQ EGEEEVESCT TQPVVGSGDK DPETEQSQES PSTTSPSTRK SKDRHSQGKG LSRLFSSFLK RPKSQVSSDE KEVELLGEKG QDQKDVDEGL GEQLEDDVFL KAPIAAPEPE LRTDPSLDLH SLSSAETQPA QEEQKEDQDP EADCEDVEGK EPIKKPEGES KASHKVVRRS PNMRCKVTLL DDTVYECDLE KHAKGQDIFK KVCSHLNIVE EDYFGLAIWE SPTCKVWLDP LKDIRKQVHG GPCEFTSNVK FYPPDPAQLS EDITRYYLCL QLRKDIFSGR LPCSFATLAL LGSYTVQSEV GDYEEDLHGV DYVSEFKLSP NQTKDLEEKV GELHKSYRSM TPAQADLEFL ENAKKLTMYG VDIHQAKDLE GVDIKLGVCS GGLMVFKDNL RINRFPWPKV LKISYKRSSF FIKIRPGEQE QYESTIGFKL PSYKAAKKLW KVCVEHHTFF RLTSTESIPK HRFLSLGSTF RYSGRTQAQT RHASALIDRP APHFVRTGSK RASRSLDGAA VATPEASRTH RPVSAPVFPP EFPAVQRKTP GPRVEEMPKK TEEKPKEGMP NQRESPKDVK ATQQDSPSPT VNGDKVKDLE KTQDEIIRHH ASIRELKKSF MESVPAPRPS EWDKRLSTHS PFRTLSFNGQ VQTGTDGPPL VKTQTVTISN ATNGEKGEIP TKEVPLVHTE TKTITYEAAR SDDVNTDQEP GILLTAHTIT SETTSSTTTT QITKTVKGGI SETLIEKRIV ITGDGDLDHD QVLVQAIKEA KEQHPDMSVT KGVVHQETEI A // ID 45C1_ANCSP Reviewed; 47 AA. AC P84028; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 31-OCT-2006, entry version 7. DE Neurotoxin ANC45C1. OS Ancylometes sp. (South American fishing spider). OC Eukaryota; Metazoa; Arthropoda; Chelicerata; Arachnida; Araneae; OC Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Ancylometes. OX NCBI_TaxID=280265; RN [1] RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS RP SPECTROMETRY. RC TISSUE=Venom; RA Richardson M., Pimenta A.M.C., Bemquerer M.P., Santoro M.M., RA Figueiredo S.G., Cordeiro M.N.; RT "Protein ANC45C1 from venom of South American fishing spider RT (Ancylometes spp.) has sequence similarities to Na channel antagonists RT from venoms of Phoneutria spiders."; RL Submitted (JUN-2004) to Swiss-Prot. CC -!- FUNCTION: Blocks voltage-gated sodium channels (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- MASS SPECTROMETRY: MW=4979.3; METHOD=Electrospray; RANGE=1-47; CC NOTE=Ref.1. CC -!- SIMILARITY: Belongs to the spider toxin Tx2 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Direct protein sequencing; Ionic channel inhibitor; Neurotoxin; KW Sodium channel inhibitor; Toxin. FT CHAIN 1 47 Neurotoxin ANC45C1. FT /FTId=PRO_0000087631. SQ SEQUENCE 47 AA; 4988 MW; 2C0D79834CF613C5 CRC64; ATCAGQDKPC KVNCDCCGER GECVCGGPCI CRQGNVFIAW SKLMTCK // ID 45KD_TAEOV Reviewed; 240 AA. AC P19617; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 28-NOV-2006, entry version 33. DE 45 kDa antigen (45W antigen) (Fragment). OS Taenia ovis (Sheep tapeworm). OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Taeniidae; Taenia. OX NCBI_TaxID=6203; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89181957; PubMed=2648160; DOI=10.1038/338585a0; RA Johnson K.S., Harrison G.B.L., Lightowlers M.W., O'Hoy K.L., RA Cougle W.G., Dempster R.P., Lawrence S.B., Vinton J.G., Heath D.D., RA Rickard M.D.; RT "Vaccination against ovine cysticercosis using a defined recombinant RT antigen."; RL Nature 338:585-587(1989). CC -!- SIMILARITY: Contains at least 2 fibronectin type-III 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; X15228; CAA33300.1; -; mRNA. DR InterPro; IPR003961; FN_III. DR InterPro; IPR008957; FN_III-like. DR Gene3D; G3DSA:2.60.40.30; FN_III-like; 1. DR SMART; SM00060; FN3; 2. DR PROSITE; PS50853; FN3; FALSE_NEG. KW Repeat. FT CHAIN <1 240 45 kDa antigen. FT /FTId=PRO_0000064379. FT DOMAIN <1 109 Fibronectin type-III 1. FT DOMAIN 110 210 Fibronectin type-III 2. FT NON_TER 1 1 SQ SEQUENCE 240 AA; 26127 MW; F58E468CCDE1E69B CRC64; EFPDYEQPIE RTVVEYPSLR DIFAWEPPTS NSIGLTWQRH AFPGVEREVL TLKAVPTSEP NNTKTAYAKL GSGKVTLDGL KPNATYLVTA TANISGDTIL VLSNTFHTLA NGTNIINNIF HWGPVTNQSI QVRWDQIKPE ETSALIVTLT AEMASDPGVE RSESALFGKG KVTVDGLESD TLYIATVMVF RNGRQYFNST RDIRTLKSGH KEVTVVTTSG SGIASTILGL LLTCVALVLA // ID 48KD_BACCE Reviewed; 15 AA. AC P80173; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 31-OCT-2006, entry version 19. DE 48 kDa protein (Fragment). OS Bacillus cereus. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1396; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=1230-88; RX MEDLINE=93307641; PubMed=8319899; DOI=10.1016/0378-1097(93)90248-Z; RA Granum P.E., Nissen H.; RT "Sphingomyelinase is part of the 'enterotoxin complex' produced by RT Bacillus cereus."; RL FEMS Microbiol. Lett. 110:97-100(1993). CC -!- FUNCTION: Not known, part of the enterotoxin complex. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Direct protein sequencing. FT CHAIN 1 >15 48 kDa protein. FT /FTId=PRO_0000064380. FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1646 MW; 88442960B4B0FB62 CRC64; XTQQEGMDIS SSLXK // ID 4CL1_ARATH Reviewed; 561 AA. AC Q42524; Q8RY63; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 49. DE 4-coumarate--CoA ligase 1 (EC 6.2.1.12) (4CL 1) (At4CL1) (4-coumaroyl- DE CoA synthase 1). GN Name=4CL1; OrderedLocusNames=At1g51680; ORFNames=F19C24.11; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX MEDLINE=95367648; PubMed=7640359; RA Lee D., Ellard M., Wanner L.A., Davis K.R., Douglas C.J.; RT "The Arabidopsis thaliana 4-coumarate:CoA ligase (4CL) gene: stress RT and developmentally regulated expression and nucleotide sequence of RT its cDNA."; RL Plant Mol. Biol. 28:871-884(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX MEDLINE=99348176; PubMed=10417722; RA Ehlting J., Buettner D., Wang Q., Douglas C.J., Somssich I.E., RA Kombrink E.; RT "Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana RT represent two evolutionarily divergent classes in angiosperms."; RL Plant J. 19:9-20(1999). RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RA Lawrence P.K.; RT "Functional classification of Arabidopsis thaliana 4-coumarate CoA RT ligase genes."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q42524-1; Sequence=Displayed; CC Name=2; CC IsoId=Q42524-2; Sequence=VSP_008911; CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; U18675; AAA82888.1; -; mRNA. DR EMBL; AF106084; AAD47191.1; -; Genomic_DNA. DR EMBL; AY376729; AAQ86588.1; -; mRNA. DR EMBL; AC025294; AAG50881.1; -; Genomic_DNA. DR EMBL; AY075622; AAL91633.1; -; mRNA. DR EMBL; AY099747; AAM20598.1; -; mRNA. DR EMBL; AY133582; AAM91412.1; -; mRNA. DR PIR; S57784; S57784. DR UniGene; At.21694; -. DR HSSP; P08659; 1LCI. DR GenomeReviews; CT485782_GR; AT1G51680. DR KEGG; ath:At1g51680; -. DR TAIR; At1g51680; -. DR ArrayExpress; Q42524; -. DR GermOnline; AT1G51680; Arabidopsis thaliana. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Alternative splicing; Ligase; Phenylpropanoid metabolism. FT CHAIN 1 561 4-coumarate--CoA ligase 1. FT /FTId=PRO_0000193027. FT VAR_SEQ 491 561 Missing (in isoform 2). FT /FTId=VSP_008911. SQ SEQUENCE 561 AA; 61053 MW; 5A9E20816D0C0D07 CRC64; MAPQEQAVSQ VMEKQSNNNN SDVIFRSKLP DIYIPNHLSL HDYIFQNISE FATKPCLING PTGHVYTYSD VHVISRQIAA NFHKLGVNQN DVVMLLLPNC PEFVLSFLAA SFRGATATAA NPFFTPAEIA KQAKASNTKL IITEARYVDK IKPLQNDDGV VIVCIDDNES VPIPEGCLRF TELTQSTTEA SEVIDSVEIS PDDVVALPYS SGTTGLPKGV MLTHKGLVTS VAQQVDGENP NLYFHSDDVI LCVLPMFHIY ALNSIMLCGL RVGAAILIMP KFEINLLLEL IQRCKVTVAP MVPPIVLAIA KSSETEKYDL SSIRVVKSGA APLGKELEDA VNAKFPNAKL GQGYGMTEAG PVLAMSLGFA KEPFPVKSGA CGTVVRNAEM KIVDPDTGDS LSRNQPGEIC IRGHQIMKGY LNNPAATAET IDKDGWLHTG DIGLIDDDDE LFIVDRLKEL IKYKGFQVAP AELEALLIGH PDITDVAVVA MKEEAAGEVP VAFVVKSKDS ELSEDDVKQF VSKQVVFYKR INKVFFTESI PKAPSGKILR KDLRAKLANG L // ID 4CL1_ORYSA Reviewed; 564 AA. AC P17814; Q6ZKV9; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 20-FEB-2007, entry version 44. DE 4-coumarate--CoA ligase 1 (EC 6.2.1.12) (4CL 1) (4-coumaroyl-CoA DE synthase 1). GN Name=4CL1; Synonyms=4CL; GN OrderedLocusNames=Os08g0245200, LOC_Os08g14760; GN ORFNames=OJ1033_B09.16; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Japonica; RX MEDLINE=91045096; PubMed=2235510; DOI=10.1093/nar/18.20.6144; RA Zhao Y., Kung S.D., Dube S.K.; RT "Nucleotide sequence of rice 4-coumarate:CoA ligase gene, 4-CL.1."; RL Nucleic Acids Res. 18:6144-6144(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RG The international rice genome sequencing project (IRGSP) consortium; RT "Oryza sativa nipponbare chromosome 8 genomic DNA sequence."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=22752273; PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- INDUCTION: By fungal elicitor and UV irradiation. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme CC family. CC -!- CAUTION: Ref.1 (CAA36850) sequence differs from that shown due to CC a frameshift in position 496. CC -!- CAUTION: Ref.1 (CAA36850) sequence differs from that shown due to CC 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; X52623; CAA36850.1; ALT_SEQ; Genomic_DNA. DR EMBL; AP003859; BAD05189.1; ALT_INIT; Genomic_DNA. DR EMBL; AK069932; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; JU0311; JU0311. DR HSSP; P08659; 1LCI. DR Gramene; P17814; -. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 564 4-coumarate--CoA ligase 1. FT /FTId=PRO_0000193031. FT CONFLICT 405 405 P -> R (in Ref. 1). FT CONFLICT 477 477 I -> N (in Ref. 1). SQ SEQUENCE 564 AA; 60902 MW; 9725A4B4A72F8C6E CRC64; MGSMEQQQPE SAAPATEASP EIIFRSKLQD IAITNTLPLH RYCFERLPEV AARPCLIDGA TGGVLTYADV DRLSRRLAAA LRRAPLGLRR GGVVMSLLRN SPEFVLSFFA ASRVGAAVTT ANPMSTPHEI ESQLAAAGAT VVITESMAAD KLPSHSHGAL TVVLIDERRD GCLHFWDDLM SEDEASPLAG DEDDEKVFDP DDVVALPYSS GTTGLPKGVM LTHRSLSTSV AQQVDGENPN IGLHAGDVIL CALPMFHIYS LNTIMMCGLR VGAAIVVMRR FDLAAMMDLV ERHRVTIAPL VPPIVVAVAK SEAAAARDLS SVRMVLSGAA PMGKDIEDAF MAKLPGAVLG QGYGMTEAGP VLSMCLAFAK EPFKVKSGAC GTVVRNAELK IIDPDTGKSL GRNLPGEICI RGQQIMKGYL NNPEATKNTI DAEGWLHTGD IGYVDDDDEI FIVDRLKEII KYRGFQVAPA ELEALLITHP SIADAAVVGK QIEPEIGEIP VAFVAKTEGS ELSEDDVKQF VAKEVIYYKK IREVFFVDKI PKAPSGKILR KELRKQLQHL QQEA // ID 4CL1_PETCR Reviewed; 544 AA. AC P14912; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 12-DEC-2006, entry version 43. DE 4-coumarate--CoA ligase 1 (EC 6.2.1.12) (4CL 1) (4-coumaroyl-CoA DE synthase 1). GN Name=4CL1; Synonyms=4CL-1; OS Petroselinum crispum (Parsley) (Petroselinum hortense). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; campanulids; Apiales; Apiaceae; Apioideae; OC apioid superclade; Apium clade; Petroselinum. OX NCBI_TaxID=4043; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=89005119; PubMed=3169018; RA Lozoya E., Hoffmann H., Douglas C., Schulz W., Scheel D., RA Hahlbrock K.; RT "Primary structures and catalytic properties of isoenzymes encoded by RT the two 4-coumarate:CoA ligase genes in parsley."; RL Eur. J. Biochem. 176:661-667(1988). RN [2] RP NUCLEOTIDE SEQUENCE OF 1-8. RA Douglas C., Hoffmann H., Schulz W., Hahlbrock K.; RT "Structure and elicitor or U.V.-light-stimulated expression of two 4- RT coumarate:CoA ligase genes in parsley."; RL EMBO J. 6:1189-1195(1987). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- INDUCTION: By fungal elicitor and UV irradiation. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; X13324; CAA31696.1; -; mRNA. DR EMBL; X05350; CAA28959.1; -; Genomic_DNA. DR PIR; S01667; S01667. DR HSSP; P08659; 1LCI. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 544 4-coumarate--CoA ligase 1. FT /FTId=PRO_0000193033. SQ SEQUENCE 544 AA; 59825 MW; 22BBAD78F255D0C8 CRC64; MGDCVAPKED LIFRSKLPDI YIPKHLPLHT YCFENISKVG DKSCLINGAT GETFTYSQVE LLSRKVASGL NKLGIQQGDT IMLLLPNSPE YFFAFLGASY RGAISTMANP FFTSAEVIKQ LKASQAKLII TQACYVDKVK DYAAEKNIQI ICIDDAPQDC LHFSKLMEAD ESEMPEVVIN SDDVVALPYS SGTTGLPKGV MLTHKGLVTS VAQQVDGDNP NLYMHSEDVM ICILPLFHIY SLNAVLCCGL RAGVTILIMQ KFDIVPFLEL IQKYKVTIGP FVPPIVLAIA KSPVVDKYDL SSVRTVMSGA APLGKELEDA VRAKFPNAKL GQGYGMTEAG PVLAMCLAFA KEPYEIKSGA CGTVVRNAEM KIVDPETNAS LPRNQRGEIC IRGDQIMKGY LNDPESTRTT IDEEGWLHTG DIGFIDDDDE LFIVDRLKEI IKYKGFQVAP AELEALLLTH PTISDAAVVP MIDEKAGEVP VAFVVRTNGF TTTEEEIKQF VSKQVVFYKR IFRVFFVDAI PKSPSGKILR KDLRARIASG DLPK // ID 4CL1_SOLTU Reviewed; 545 AA. AC P31684; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 12-DEC-2006, entry version 33. DE 4-coumarate--CoA ligase 1 (EC 6.2.1.12) (4CL 1) (4-coumaroyl-CoA DE synthase 1). GN Name=4CL1; Synonyms=4CL-1; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91217100; PubMed=2022667; RA Becker-Andre M., Schulze-Lefert P., Hahlbrock K.; RT "Structural comparison, modes of expression, and putative cis-acting RT elements of the two 4-coumarate: CoA ligase genes in potato."; RL J. Biol. Chem. 266:8551-8559(1991). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; M62755; AAA33842.1; -; Genomic_DNA. DR PIR; A39827; A39827. DR HSSP; P08659; 1LCI. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 545 4-coumarate--CoA ligase 1. FT /FTId=PRO_0000193036. SQ SEQUENCE 545 AA; 59619 MW; DE183683B774BA71 CRC64; MPMDTETKQS GDLIFRSKLP DIYIPKHLPL HSYCFENLSE FNSRPCLIDG ANDRIYTYAE VELTSRKVAV GLNKLGIQQK DTIMILLPNC PEFVFAFIGA SYLGAISTMA NPLFTPAEVV KQAKASSAKI VITQACFAGK VKDYAIENDL KVICVDSVPE GCVHFSELIQ SDEHEIPDVK IQPDDVVALP YSSGTTGLPK GVMLTHKGLV TSVAQQVDGE NANLYMHSDD VLMCVLPLFH IYSLNSVLLC ALRVGAAILI MQKFDIAQFL ELIPKHKVTI GPFVPPIVLA IAKSPLVDNY DLSSVRTVMS GAAPLGKELE DAVRAKFPNA KLGQGYGMTE AGPVLAMCLA FAKEPFDIKS GACGTVVRNA EMKIVDPDTG CSLPRNQPGE ICIRGDQIMK GYLNDPEATA RTIEKEGWLH TGDIGFIDDD DELFIVDRLK ELIKYKGFQV APAELEALLI NHPDISDAAV VPMIDEQAGE VPVAFVVRSN GSTITEDEVK DFISKQVIFY KRIKRVFFVE TVPKSPSGKI LRKDLRARLA AGISN // ID 4CL1_SOYBN Reviewed; 293 AA. AC P31686; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 12-DEC-2006, entry version 33. DE 4-coumarate--CoA ligase 1 (EC 6.2.1.12) (4CL 1) (4-coumaroyl-CoA DE synthase 1) (Clone 4CL14) (Fragment). OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Harosoy 63; RX MEDLINE=94105342; PubMed=8278545; DOI=10.1104/pp.102.4.1147; RA Uhlmann A., Ebel J.; RT "Molecular cloning and expression of 4-coumarate:coenzyme A ligase, an RT enzyme involved in the resistance response of soybean (Glycine max L.) RT against pathogen attack."; RL Plant Physiol. 102:1147-1156(1993). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; X69954; CAA49575.1; -; mRNA. DR PIR; S31705; S31705. DR HSSP; P08659; 1LCI. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PROSITE; PS00455; AMP_BINDING; PARTIAL. KW Ligase; Phenylpropanoid metabolism. FT CHAIN <1 293 4-coumarate--CoA ligase 1. FT /FTId=PRO_0000193038. FT NON_TER 1 1 SQ SEQUENCE 293 AA; 32027 MW; 25868497FCC022EC CRC64; AKATILLMPK FDINSLLALI HKHKVTIAPV VPPIVLAISK SPDLHKYDLS SIRVLKSGGA PLGKELEDTL RAKFPNAKLG QGYGMTEAGP VLTMSLAFAK EPIDVKPGAC GTVVRNAEMK IVDPETGHSL PRNQSGEICI RGDQIMKGYL NDGEATERTI DKDGWLHTGD IGYIDDDDEL FIVDRLKELI KYKGFQVAPA ELEALLLTHP KISDAAVVPM KDEAAGEVPV AFVVISNGYT DTTEDEIKQF ISKQVVFYKR INRVFFIDAI PKSPSGKILR KDLRAKIAAS VPK // ID 4CL1_TOBAC Reviewed; 547 AA. AC O24145; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 12-DEC-2006, entry version 33. DE 4-coumarate--CoA ligase 1 (EC 6.2.1.12) (4CL 1) (4-coumaroyl-CoA DE synthase 1). GN Name=4CL1; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96416441; PubMed=8819324; DOI=10.1104/pp.112.1.193; RA Lee D., Douglas C.J.; RT "Two divergent members of a tobacco 4-coumarate:coenzyme A ligase RT (4CL) gene family. cDNA structure, gene inheritance and expression, RT and properties of recombinant proteins."; RL Plant Physiol. 112:193-205(1996). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; U50845; AAB18637.1; -; mRNA. DR HSSP; P08659; 1LCI. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 547 4-coumarate--CoA ligase 1. FT /FTId=PRO_0000193040. SQ SEQUENCE 547 AA; 59842 MW; 154DF6D684E3F51B CRC64; MPMETTTETK QSGDLIFRSK LPDIYIPKHL PLHSYCFENI SEFSSRPCLI NGANDQIYTY AEVELTCRKV AVGLNKLGIQ QKDTIMILLP NSPEFVFAFM GASYLGAIST MANPLFTPAE VVKQAKASSA KIIITQSCFV GKVKDYASEN DVKVICIDSA PEGCLHFSEL TQSDEHEIPE VKIQPDDVVA LPYSSGTTGL PKGVMLTHKG LVTSVAQQVD GENANLYMHS EDVLMCVLPL FHIYSLNSIL LCGLRVGAAI LIMQKFDIAP FLELIQKYKV SIGPFVPPIV LAIAKSPIVD SYDLSSVRTV MSGAAPLGKE LEDAVRTKFP NAKLGQGYGM TEAGPVLAMC LAFAKEPFDI KSGACGTVVR NAEMKIVDPD TGCSLPRNQP GEICIRGDQI MKGYLNDPEA TTRTIDKEGW LHTGDIGFID EDDELFIVDR LKELIKYKGF QVAPAEIEAL LLNHPNISDA AVVPMKDEQA GEVPVAFVVR SNGSAITEDE VKDFISKQVI FYKRVKRVFF VETVPKSPSG KILRKDLRAR LAAGVPN // ID 4CL2_ARATH Reviewed; 556 AA. AC Q9S725; Q9LU35; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 20-FEB-2007, entry version 37. DE 4-coumarate--CoA ligase 2 (EC 6.2.1.12) (4CL 2) (At4Cl2) (4-coumaroyl- DE CoA synthase 2). GN Name=4CL2; OrderedLocusNames=At3g21240; ORFNames=MXL8.10; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=99348176; PubMed=10417722; RA Ehlting J., Buettner D., Wang Q., Douglas C.J., Somssich I.E., RA Kombrink E.; RT "Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana RT represent two evolutionarily divergent classes in angiosperms."; RL Plant J. 19:9-20(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20277480; PubMed=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; AF106085; AAD47192.1; -; Genomic_DNA. DR EMBL; AF106086; AAD47193.1; -; mRNA. DR EMBL; AB023045; BAB01716.1; -; Genomic_DNA. DR UniGene; At.57587; -. DR HSSP; P08659; 1LCI. DR GenomeReviews; BA000014_GR; AT3G21240. DR TAIR; At3g21240; -. DR ArrayExpress; Q9S725; -. DR GermOnline; AT3G21240; Arabidopsis thaliana. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 556 4-coumarate--CoA ligase 2. FT /FTId=PRO_0000193028. FT CONFLICT 247 247 W -> L (in Ref. 2). FT CONFLICT 265 265 I -> V (in Ref. 2). SQ SEQUENCE 556 AA; 60929 MW; E3C2EADE77529EED CRC64; MTTQDVIVND QNDQKQCSND VIFRSRLPDI YIPNHLPLHD YIFENISEFA AKPCLINGPT GEVYTYADVH VTSRKLAAGL HNLGVKQHDV VMILLPNSPE VVLTFLAASF IGAITTSANP FFTPAEISKQ AKASAAKLIV TQSRYVDKIK NLQNDGVLIV TTDSDAIPEN CLRFSELTQS EEPRVDSIPE KISPEDVVAL PFSSGTTGLP KGVMLTHKGL VTSVAQQVDG ENPNLYFNRD DVILCVWPMF HIYALNSIML CSLRIGATIL IMPKFEITLL LEQIQRCKVT VAMVVPPIVL AIAKSPETEK YDLSSVRMVK SGAAPLGKEL EDAISAKFPN AKLGQGYGMT EAGPVLAMSL GFAKEPFPVK SGACGTVVRN AEMKILDPDT GDSLPRNKPG EICIRGNQIM KGYLNDPLAT ASTIDKDGWL HTGDVGFIDD DDELFIVDRL KELIKYKGFQ VAPAELESLL IGHPEINDVA VVAMKEEDAG EVPVAFVVRS KDSNISEDEI KQFVSKQVVF YKRINKVFFT DSIPKAPSGK ILRKDLRARL ANGLMN // ID 4CL2_ORYSA Reviewed; 569 AA. AC Q42982; Q6YUH6; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 20-FEB-2007, entry version 37. DE 4-coumarate--CoA ligase 2 (EC 6.2.1.12) (4CL 2) (4-coumaroyl-CoA DE synthase 2). GN Name=4CL2; Synonyms=4CL.2; GN OrderedLocusNames=Os02g0697400, LOC_Os02g46970; GN ORFNames=P0666E12.12-1, P0459B01.4-1; OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zhao Y., Kung S.D., Bottino P.J.; RT "4-coumarate:CoA ligase genes in rice: divergent structure and RT differential regulation."; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Japonica / Nipponbare; RG The international rice genome sequencing project (IRGSP) consortium; RT "Oryza sativa nipponbare chromosome 2 genomic DNA sequence."; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=22752273; PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; L43362; AAA69580.1; -; mRNA. DR EMBL; AP004778; BAD07859.1; -; Genomic_DNA. DR EMBL; AP005868; BAD08175.1; -; Genomic_DNA. DR EMBL; AK105636; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; T03390; T03390. DR UniGene; Os.4377; -. DR HSSP; P08659; 1LCI. DR Gramene; Q42982; -. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 569 4-coumarate--CoA ligase 2. FT /FTId=PRO_0000193032. FT CONFLICT 138 138 A -> G (in Ref. 1). FT CONFLICT 186 187 EG -> KA (in Ref. 1). FT CONFLICT 226 226 P -> A (in Ref. 1). FT CONFLICT 242 243 QQ -> HE (in Ref. 1). FT CONFLICT 277 283 CAVRAGA -> SRVRPAP (in Ref. 1). FT CONFLICT 308 308 A -> G (in Ref. 1). FT CONFLICT 316 316 L -> V (in Ref. 1). FT CONFLICT 450 450 D -> N (in Ref. 1). FT CONFLICT 493 493 A -> R (in Ref. 1). SQ SEQUENCE 569 AA; 60815 MW; 2A1A1FF3CF7FEC91 CRC64; MITVAAPEAQ PQVAAAVDEA PPEAVTVFRS KLPDIDIPSH LPLHEYCFAR AAELPDAPCL IAAATGRTYT FAETRLLCRR AAAALHRLGV GHGDRVMVLL QNCVEFAVAF FAASFLGAVT TAANPFCTPQ EIHKQFKASG VKLILTQSVY VDKLRQHEAF PRIDACTVGD DTLTVITIDD DEATPEGCLP FWDLIADADE GSVPEVAISP DDPVALPFSS GTTGLPKGVV LTHRSVVSGV AQQVDGENPN LHMGAGDVAL CVLPLFHIFS LNSVLLCAVR AGAAVALMPR FEMGAMLGAI ERWRVTVAAV VPPLVLALAK NPFVERHDLS SIRIVLSGAA PLGKELEDAL RARLPQAIFG QGYGMTEAGP VLSMCPAFAK EPTPAKSGSC GTVVRNAELK VVDPDTGFSL GRNLPGEICI RGPQIMKGYL NDPEATAATI DVEGWLHTGD IGYVDDDDEV FIVDRVKELI KFKGFQVPPA ELESLLIAHP SIADAAVVPQ KDDVAGEVPV AFVVRAADSD ITEESIKEFI SKQVVFYKRL HKVHFIHAIP KSASGKILRR ELRAKLAAC // ID 4CL2_PETCR Reviewed; 544 AA. AC P14913; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 12-DEC-2006, entry version 43. DE 4-coumarate--CoA ligase 1 (EC 6.2.1.12) (4CL 1) (4-coumaroyl-CoA DE synthase 1). GN Name=4CL2; Synonyms=4CL-2; OS Petroselinum crispum (Parsley) (Petroselinum hortense). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; campanulids; Apiales; Apiaceae; Apioideae; OC apioid superclade; Apium clade; Petroselinum. OX NCBI_TaxID=4043; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=89005119; PubMed=3169018; RA Lozoya E., Hoffmann H., Douglas C., Schulz W., Scheel D., RA Hahlbrock K.; RT "Primary structures and catalytic properties of isoenzymes encoded by RT the two 4-coumarate:CoA ligase genes in parsley."; RL Eur. J. Biochem. 176:661-667(1988). RN [2] RP NUCLEOTIDE SEQUENCE OF 1-8. RA Douglas C., Hoffmann H., Schulz W., Hahlbrock K.; RT "Structure and elicitor or U.V.-light-stimulated expression of two 4- RT coumarate:CoA ligase genes in parsley."; RL EMBO J. 6:1189-1195(1987). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- INDUCTION: By fungal elicitor and UV irradiation. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; X13325; CAA31697.1; -; mRNA. DR EMBL; X05351; CAA28960.1; -; Genomic_DNA. DR PIR; S15695; S15695. DR HSSP; P08659; 1LCI. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 544 4-coumarate--CoA ligase 1. FT /FTId=PRO_0000193034. SQ SEQUENCE 544 AA; 59783 MW; B477965C68F8C534 CRC64; MGDCVAPKED LIFRSKLPDI YIPKHLPLHT YCFENISKVG DKSCLINGAT GETFTYSQVE LLSRKVASGL NKLGIQQGDT IMLLLPNSPE YFFAFLGASY RGAISTMANP FFTSAEVIKQ LKASLAKLII TQACYVDKVK DYAAEKNIQI ICIDDAPQDC LHFSKLMEAD ESEMPEVVID SDDVVALPYS SGTTGLPKGV MLTHKGLVTS VAQQVDGDNP NLYMHSEDVM ICILPLFHIY SLNAVLCCGL RAGVTILIMQ KFDIVPFLEL IQKYKVTIGP FVPPIVLAIA KSPVVDKYDL SSVRTVMSGA APLGKELEDA VRAKFPNAKL GQGYGMTEAG PVLAMCLAFA KEPYEIKSGA CGTVVRNAEM KIVDPETNAS LPRNQRGEIC IRGDQIMKGY LNDPESTRTT IDEEGWLHTG DIGFIDDDDE LFIVDRLKEI IKYKGFQVAP AELEALLLTH PTISDAAVVP MIDEKAGEVP VAFVVRTNGF TTTEEEIKQF VSKQVVFYKR IFRVFFVDAI PKSPSGKILR KDLRAKIASG DLPK // ID 4CL2_SOLTU Reviewed; 545 AA. AC P31685; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 12-DEC-2006, entry version 31. DE 4-coumarate--CoA ligase 2 (EC 6.2.1.12) (4CL 2) (4-coumaroyl-CoA DE synthase 2). GN Name=4CL2; Synonyms=4CL-2; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=91217100; PubMed=2022667; RA Becker-Andre M., Schulze-Lefert P., Hahlbrock K.; RT "Structural comparison, modes of expression, and putative cis-acting RT elements of the two 4-coumarate: CoA ligase genes in potato."; RL J. Biol. Chem. 266:8551-8559(1991). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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 PIR; B39827; B39827. DR HSSP; P08659; 1LCI. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 545 4-coumarate--CoA ligase 2. FT /FTId=PRO_0000193037. SQ SEQUENCE 545 AA; 59625 MW; 5481F0B0AFEA39E0 CRC64; MPMDIETKQS GDLIFRSKLP DIYIPKHLPL HSYCFENLSE FNSRPCLIDG ANDRIYTYAE VELTSRKVAV GLNKLGIQQK DTIMILLPNC PEFVFAFIGA SYLGAISTMA NPLFTPAEVV KQAKASSAKI VITQACFAGK VKDYAIENDL KVICVDSAPE GCVHFSELIQ SDEHEIPDVK IQPDDVVALP YSSGTTGLPK GVMLTHKGLV TSVAQQVDGE NANLYMHSDD VLMCVLPLFH IYSLNSVLLC ALRVGAAILI MQKFDIAQFL ELIPKHKVTI GPFVPPIVLA IAKSPLVHNY DLSSVRTVMS GAAPLGKELE DAVRAKFPNA KLGQGYGMTE AGPVLAMCLA FAKEPFDIKS GACGTVVRNA EMKIVDPDTG CSLPRNQPGE ICIRGDQIMK GYLNDPEATA RTIEKEGWLH TGDIGFIDDD DELFIVDRLK ELIKYKGFQV APAELEALLI NHPDISDAAV VPMIDEQAGE VPVAFVVRSN GSTITEDEVK DFISKQVIFY KRIKRVFFVE TVPKSPSGKI LRKDLRARLA AGISN // ID 4CL2_SOYBN Reviewed; 562 AA. AC P31687; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 2. DT 20-FEB-2007, entry version 39. DE 4-coumarate--CoA ligase 2 (EC 6.2.1.12) (4CL 2) (4-coumaroyl-CoA DE synthase 2) (Clone 4CL16). OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Lindermayr C.; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 140-562. RC STRAIN=cv. Harosoy 63; RX MEDLINE=94105342; PubMed=8278545; DOI=10.1104/pp.102.4.1147; RA Uhlmann A., Ebel J.; RT "Molecular cloning and expression of 4-coumarate:coenzyme A ligase, an RT enzyme involved in the resistance response of soybean (Glycine max L.) RT against pathogen attack."; RL Plant Physiol. 102:1147-1156(1993). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; X69955; CAC36095.1; -; mRNA. DR PIR; PQ0772; PQ0772. DR UniGene; Gma.8472; -. DR HSSP; P08659; 1LCI. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 562 4-coumarate--CoA ligase 2. FT /FTId=PRO_0000193039. SQ SEQUENCE 562 AA; 60963 MW; 2AB4652DDA5160B2 CRC64; MITLAPSLDT PKTDQNQVSD PQTSHVFKSK LPDIPISNHL PLHSYCFQNL SQFAHRPCLI VGPASKTFTY ADTHLISSKI AAGLSNLGIL KGDVVMILLQ NSADFVFSFL AISMIGAVAT TANPFYTAPE IFKQFTVSKA KLIITQAMYV DKLRNHDGAK LGEDFKVVTV DDPPENCLHF SVLSEANESD VPEVEIHPDD AVAMPFSSGT TGLPKGVILT HKSLTTSVAQ QVDGENPNLY LTTEDVLLCV LPLFHIFSLN SVLLCALRAG SAVLLMQKFE IGTLLELIQR HRVSVAMVVP PLVLALAKNP MVADFDLSSI RLVLSGAAPL GKELEEALRN RMPQAVLGQG YGMTEAGPVL SMCLGFAKQP FQTKSGSCGT VVRNAELKVV DPETGRSLGY NQPGEICIRG QQIMKGYLND EAATASTIDS EGWLHTGDVG YVDDDDEIFI VDRVKELIKY KGFQVPPAEL EGLLVSHPSI ADAAVVPQKD VAAGEVPVAF VVRSNGFDLT EEAVKEFIAK QVVFYKRLHK VYFVHAIPKS PSGKILRKDL RAKLETAATQ TP // ID 4CL2_TOBAC Reviewed; 542 AA. AC O24146; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 12-DEC-2006, entry version 35. DE 4-coumarate--CoA ligase 2 (EC 6.2.1.12) (4CL 2) (4-coumaroyl-CoA DE synthase 2). GN Name=4CL2; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96416441; PubMed=8819324; DOI=10.1104/pp.112.1.193; RA Lee D., Douglas C.J.; RT "Two divergent members of a tobacco 4-coumarate:coenzyme A ligase RT (4CL) gene family. cDNA structure, gene inheritance and expression, RT and properties of recombinant proteins."; RL Plant Physiol. 112:193-205(1996). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; U50846; AAB18638.1; -; mRNA. DR PIR; T03789; T03789. DR HSSP; P08659; 1LCI. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 542 4-coumarate--CoA ligase 2. FT /FTId=PRO_0000193041. SQ SEQUENCE 542 AA; 59480 MW; CB5579AEDFCFC003 CRC64; MEKDTKQVDI IFRSKLPDIY IPNHLPLHSY CFENISEFSS RPCLINGANK QIYTYADVEL NSRKVAAGLH KQGIQPKDTI MILLPNSPEF VFAFIGASYL GAISTMANPL FTPAEVVKQA KASSAKIIVT QACHVNKVKD YAFENDVKII CIDSAPEGCL HFSVLTQANE HDIPEVEIQP DDVVALPYSS GTTGLPKGVM LTHKGLVTSV AQQVDGENPN LYIHSEDVML CVLPLFHIYS LNSVLLCGLR VGAAILIMQK FDIVSFLELI QRYKVTIGPF VPPIVLAIAK SPMVDDYDLS SVRTVMSGAA PLGKELEDTV RAKFPNAKLG QGYGMTEAGP VLAMCLAFAK EPFEIKSGAC GTVVRNAEMK IVDPKTGNSL PRNQSGEICI RGDQIMKGYL NDPEATARTI DKEGWLYTGD IGYIDDDDEL FIVDRLKELI KYKGFQVAPA ELEALLLNHP NISDAAVVPM KDEQAGEVPV AFVVRSNGST ITEDEVKDFI SKQVIFYKRI KRVFFVDAIP KSPSGKILRK DLRAKLAAGL PN // ID 4CL3_ARATH Reviewed; 561 AA. AC Q9S777; Q93Z69; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 20-FEB-2007, entry version 43. DE 4-coumarate--CoA ligase 3 (EC 6.2.1.12) (4CL 3) (At4CL3) (4-coumaroyl- DE CoA synthase 3). GN Name=4CL3; OrderedLocusNames=At1g65060; ORFNames=F16G16.6; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=99348176; PubMed=10417722; RA Ehlting J., Buettner D., Wang Q., Douglas C.J., Somssich I.E., RA Kombrink E.; RT "Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana RT represent two evolutionarily divergent classes in angiosperms."; RL Plant J. 19:9-20(1999). RN [2] RP NUCLEOTIDE SEQUENCE. RA Lawrence P.K.; RT "Functional classification of Arabidopsis thaliana 4-coumarate CoA RT ligase genes."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-561. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences; CC Name=1; CC IsoId=Q9S777-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; AF106087; AAD47194.1; -; Genomic_DNA. DR EMBL; AF106088; AAD47195.1; -; mRNA. DR EMBL; AY376730; AAQ86589.1; -; mRNA. DR EMBL; AC009360; AAF06039.1; -; Genomic_DNA. DR EMBL; AY058083; AAL24191.1; ALT_INIT; mRNA. DR EMBL; AY090306; AAL90967.1; -; mRNA. DR PIR; D96674; D96674. DR UniGene; At.11514; -. DR HSSP; P08659; 1LCI. DR GenomeReviews; CT485782_GR; AT1G65060. DR KEGG; ath:At1g65060; -. DR TAIR; At1g65060; -. DR ArrayExpress; Q9S777; -. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Alternative splicing; Ligase; Phenylpropanoid metabolism. FT CHAIN 1 561 4-coumarate--CoA ligase 3. FT /FTId=PRO_0000193029. SQ SEQUENCE 561 AA; 61311 MW; C2EFF1C36B33F6DC CRC64; MITAALHEPQ IHKPTDTSVV SDDVLPHSPP TPRIFRSKLP DIDIPNHLPL HTYCFEKLSS VSDKPCLIVG STGKSYTYGE THLICRRVAS GLYKLGIRKG DVIMILLQNS AEFVFSFMGA SMIGAVSTTA NPFYTSQELY KQLKSSGAKL IITHSQYVDK LKNLGENLTL ITTDEPTPEN CLPFSTLITD DETNPFQETV DIGGDDAAAL PFSSGTTGLP KGVVLTHKSL ITSVAQQVDG DNPNLYLKSN DVILCVLPLF HIYSLNSVLL NSLRSGATVL LMHKFEIGAL LDLIQRHRVT IAALVPPLVI ALAKNPTVNS YDLSSVRFVL SGAAPLGKEL QDSLRRRLPQ AILGQGYGMT EAGPVLSMSL GFAKEPIPTK SGSCGTVVRN AELKVVHLET RLSLGYNQPG EICIRGQQIM KEYLNDPEAT SATIDEEGWL HTGDIGYVDE DDEIFIVDRL KEVIKFKGFQ VPPAELESLL INHHSIADAA VVPQNDEVAG EVPVAFVVRS NGNDITEEDV KEYVAKQVVF YKRLHKVFFV ASIPKSPSGK ILRKDLKAKL C // ID 4CL4_ARATH Reviewed; 570 AA. AC Q9LU36; Q84P22; Q8LPN8; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 23-JAN-2007, entry version 26. DE 4-coumarate--CoA ligase 4 (EC 6.2.1.12) (4CL 4) (At4CL4) (4-coumaroyl- DE CoA synthase 4) (4-coumarate CoA ligase isoform 5). GN Name=4CL4; OrderedLocusNames=At3g21230; ORFNames=MXL8_9; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Wassilewskija; RX MEDLINE=22690213; PubMed=12805634; DOI=10.1104/pp.103.020552; RA Shockey J.M., Fulda M.S., Browse J.; RT "Arabidopsis contains a large superfamily of acyl-activating enzymes. RT Phylogenetic and biochemical analysis reveals a new class of acyl- RT coenzyme a synthetases."; RL Plant Physiol. 132:1065-1076(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Lawrence P.K.; RT "Functional classification of Arabidopsis thaliana 4-coumarate CoA RT ligase genes."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20277480; PubMed=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-570. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP FUNCTION, AND CHARACTERIZATION. RX PubMed=14769935; DOI=10.1073/pnas.0307307101; RA Hamberger B., Hahlbrock K.; RT "The 4-coumarate:CoA ligase gene family in Arabidopsis thaliana RT comprises one rare, sinapate-activating and three commonly occurring RT isoenzymes."; RL Proc. Natl. Acad. Sci. U.S.A. 101:2209-2214(2004). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=432 uM for 4-coumarate; CC KM=186 uM for caffeate; CC KM=26 uM for ferulate; CC KM=20 uM for sinapate; CC Vmax=100 nmol/sec/mg enzyme with 4-coumarate as substrate; CC Vmax=187 nmol/sec/mg enzyme with caffeate as substrate; CC Vmax=153 nmol/sec/mg enzyme with ferulate as substrate; CC Vmax=105 nmol/sec/mg enzyme with sinapate as substrate; CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- MISCELLANEOUS: Activates efficiently sinapate, besides the usual CC 4CL substrates (4-coumarate, caffeate, and ferulate). CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; AY250837; AAP03020.1; -; mRNA. DR EMBL; AY376732; AAQ86591.1; -; mRNA. DR EMBL; AB023045; BAB01715.1; -; Genomic_DNA. DR EMBL; AY095992; AAM19949.1; ALT_INIT; mRNA. DR EMBL; BT000614; AAN18181.1; -; mRNA. DR UniGene; At.38095; -. DR HSSP; P08659; 1LCI. DR GenomeReviews; BA000014_GR; AT3G21230. DR KEGG; ath:At3g21230; -. DR TAIR; At3g21230; -. DR ArrayExpress; Q9LU36; -. DR GermOnline; AT3G21230; Arabidopsis thaliana. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 570 4-coumarate--CoA ligase 4. FT /FTId=PRO_0000193030. FT CONFLICT 81 81 T -> I (in Ref. 1). FT CONFLICT 88 88 A -> T (in Ref. 1). SQ SEQUENCE 570 AA; 62559 MW; 2C2CB71BD5F5860A CRC64; MVLQQQTHFL TKKIDQEDEE EEPSHDFIFR SKLPDIFIPN HLPLTDYVFQ RFSGDGDGDS STTCIIDGAT GRILTYADVQ TNMRRIAAGI HRLGIRHGDV VMLLLPNSPE FALSFLAVAY LGAVSTTANP FYTQPEIAKQ AKASAAKMII TKKCLVDKLT NLKNDGVLIV CLDDDGDNGV VSSSDDGCVS FTELTQADET ELLKPKISPE DTVAMPYSSG TTGLPKGVMI THKGLVTSIA QKVDGENPNL NFTANDVILC FLPMFHIYAL DALMLSAMRT GAALLIVPRF ELNLVMELIQ RYKVTVVPVA PPVVLAFIKS PETERYDLSS VRIMLSGAAT LKKELEDAVR LKFPNAIFGQ GYGMTESGTV AKSLAFAKNP FKTKSGACGT VIRNAEMKVV DTETGISLPR NKSGEICVRG HQLMKGYLND PEATARTIDK DGWLHTGDIG FVDDDDEIFI VDRLKELIKF KGYQVAPAEL EALLISHPSI DDAAVVAMKD EVADEVPVAF VARSQGSQLT EDDVKSYVNK QVVHYKRIKM VFFIEVIPKA VSGKILRKDL RAKLETMCSK // ID 4CL_PINTA Reviewed; 537 AA. AC P41636; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 12-DEC-2006, entry version 26. DE 4-coumarate--CoA ligase (EC 6.2.1.12) (4CL) (4-coumaroyl-CoA DE synthase). GN Name=4CL; OS Pinus taeda (Loblolly pine). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Coniferopsida; Coniferales; Pinaceae; Pinus; Pinus. OX NCBI_TaxID=3352; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L.; TISSUE=Xylem; RA Voo K.S.; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Needle; RX MEDLINE=97161117; PubMed=9008388; DOI=10.1104/pp.113.1.65; RA Zhang X.H., Chiang V.L.; RT "Molecular cloning of 4-coumarate:coenzyme A ligase in loblolly pine RT and the roles of this enzyme in the biosynthesis of lignin in RT compression wood."; RL Plant Physiol. 113:65-74(1997). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; U12012; AAA92668.1; -; mRNA. DR EMBL; U12013; AAA92669.1; -; mRNA. DR EMBL; U39404; AAB42382.1; -; Genomic_DNA. DR EMBL; U39405; AAB42383.1; -; Genomic_DNA. DR PIR; T09710; T09710. DR PIR; T09755; T09755. DR HSSP; P08659; 1LCI. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 537 4-coumarate--CoA ligase. FT /FTId=PRO_0000193035. FT VARIANT 422 422 E -> G. SQ SEQUENCE 537 AA; 58591 MW; 6686EB2E84C7DC43 CRC64; MANGIKKVEH LYRSKLPDIE ISDHLPLHSY CFERVAEFAD RPCLIDGATD RTYCFSEVEL ISRKVAAGLA KLGLQQGQVV MLLLPNCIEF AFVFMGASVR GAIVTTANPF YKPGEIAKQA KAAGARIIVT LAAYVEKLAD LQSHDVLVIT IDDAPKEGCQ HISVLTEADE TQCPAVKIHP DDVVALPYSS GTTGLPKGVM LTHKGLVSSV AQQVDGENPN LYFHSDDVIL CVLPLFHIYS LNSVLLCALR AGAATLIMQK FNLTTCLELI QKYKVTVAPI VPPIVLDITK SPIVSQYDVS SVRIIMSGAA PLGKELEDAL RERFPKAIFG QGYGMTEAGP VLAMNLAFAK NPFPVKSGSC GTVVRNAQIK ILDTETGESL PHNQAGEICI RGPEIMKGYI NDPESTAATI DEEGWLHTGD VEYIDDDEEI FIVDRVKEII KYKGFQVAPA ELEALLVAHP SIADAAVVPQ KHEEAGEVPV AFVVKSSEIS EQEIKEFVAK QVIFYKKIHR VYFVDAIPKS PSGKILRKDL RSRLAAK // ID 4CL_VANPL Reviewed; 553 AA. AC O24540; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 12-DEC-2006, entry version 27. DE 4-coumarate--CoA ligase (EC 6.2.1.12) (4CL) (4-coumaroyl-CoA DE synthase). GN Name=4CL; OS Vanilla planifolia (Vanilla). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Orchidaceae; OC Vanilloid clade; Vanillinae; Vanilla. OX NCBI_TaxID=51239; RN [1] RP NUCLEOTIDE SEQUENCE. RA Brodelius P., Xue Z.T.; RT "Isolation and characterization of a cDNA from cell suspension RT cultures of Vanilla planifolia encoding 4-coumarate: coenzyme A RT ligase."; RL Plant Physiol. Biochem. 35:497-506(1997). CC -!- CATALYTIC ACTIVITY: ATP + 4-coumarate + CoA = AMP + diphosphate + CC 4-coumaroyl-CoA. CC -!- PATHWAY: Secondary metabolite metabolism; stilbene, coumarine and CC lignin biosynthesis. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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 HSSP; P08659; 1LCI. DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:EC. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PRINTS; PR00154; AMPBINDING. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Phenylpropanoid metabolism. FT CHAIN 1 553 4-coumarate--CoA ligase. FT /FTId=PRO_0000193042. SQ SEQUENCE 553 AA; 60096 MW; 9A2D250BC84EA1CB CRC64; MAAAVAIEEQ KKDIIFRSKL PDIYIPKNLP LHSYCFENIS KFSSRPCLIN GATDEIFTYA DVELISRRVG SGLSKLGIKQ GDTIMILLPN SPEFVFAFLG ASFIGSISTM ANPFFTSTEV IKQAKASNAK LIITQGCYVD KVKDYACENG VKIISIDTTT TADDAANILH FSELTGADEN EMPKVEISPD GVVALPYSSG TTGLPKGVML THKGLVTSVA QQVDGENPNL YMHSDDVLLC VLPLFHIYSL NSVLLCGLRA GSGILIMQKF EIVPFLELIQ KYKVTIGPFV PPIVLAIAKS TVVDNYDLSS VRTVMSGAAP LGKELEDAVR AKFPNAKLGQ GYGMTEAGPV LAMCLAFAKE PFDIKSGACG TVVRNAEMKI VDPETGSSLP RNHPGEICIR GDQIMKGYLN DPEATARTID KEGWLHTGDI GYIDDDDELF IVDRLKELIK YKGFQVAPAE LEALLLTHPC ISDAAVVPMK DEAAGEVPVA FVVKSNGHNI TEDEIKQFIS KQVIFYKRIN RVFFVEAIPK APSGKILRKD LRARLAAAAL PTN // ID 4EBP1_HUMAN Reviewed; 118 AA. AC Q13541; Q6IBN3; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 56. DE Eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) DE (eIF4E-binding protein 1) (Phosphorylated heat- and acid-stable DE protein regulated by insulin 1) (PHAS-I). GN Name=EIF4EBP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EIF4E, AND RP PHOSPHORYLATION. RC TISSUE=Placenta; RX MEDLINE=95021760; PubMed=7935836; DOI=10.1038/371762a0; RA Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A., RA Lawrence J.C. Jr., Sonenberg N.; RT "Insulin-dependent stimulation of protein synthesis by phosphorylation RT of a regulator of 5'-cap function."; RL Nature 371:762-767(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., RA Itoh K.; RT "Identification of multiple genes and immunogenic epitopes of RT pancreatic cancer cells."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 2-13, AND ACETYLATION AT SER-2. RC TISSUE=Platelet; RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP INTERACTION WITH EIF4E AND EIF4G. RX MEDLINE=96091142; PubMed=8521827; RA Haghighat A., Mader S., Pause A., Sonenberg N.; RT "Repression of cap-dependent translation by 4E-binding protein 1: RT competition with p220 for binding to eukaryotic initiation factor- RT 4E."; RL EMBO J. 14:5701-5709(1995). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS RP SPECTROMETRY. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). CC -!- FUNCTION: Regulates eIF4E activity by preventing its assembly into CC the eIF4F complex. Mediates the regulation of protein translation CC by hormones, growth factors and other stimuli that signal through CC the MAP kinase pathway. CC -!- SUBUNIT: Nonphosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to CC interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and CC MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the CC complex allowing EIF4G1/EIF4G3 to bind and consequent initiation CC of translation. Rapamycin can attenuate insulin stimulation, CC mediated by FKBPs. CC -!- INTERACTION: CC P06730:EIF4E; NbExp=3; IntAct=EBI-74090, EBI-73440; CC Q80ZJ3:Eif4e2 (xeno); NbExp=1; IntAct=EBI-74090, EBI-934970; CC O60573:EIF4EL3; NbExp=1; IntAct=EBI-74090, EBI-398610; CC -!- PTM: Phosphorylated on serine and threonine residues in response CC to insulin, EGF and PDGF. CC -!- SIMILARITY: Belongs to the eIF4E-binding protein family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L36055; AAA62269.1; -; mRNA. DR EMBL; AB044548; BAB18650.1; -; mRNA. DR EMBL; BT007162; AAP35826.1; -; mRNA. DR EMBL; CR456769; CAG33050.1; -; mRNA. DR EMBL; BC004459; AAH04459.1; -; mRNA. DR EMBL; BC058073; AAH58073.1; -; mRNA. DR PIR; S50866; S50866. DR UniGene; Hs.411641; -. DR PDB; 1WKW; X-ray; B=47-66. DR IntAct; Q13541; -. DR Ensembl; ENSG00000187840; Homo sapiens. DR KEGG; hsa:1978; -. DR HGNC; HGNC:3288; EIF4EBP1. DR HPA; CAB005032; -. DR MIM; 602223; gene. DR Reactome; REACT_498.3; Insulin receptor mediated signaling. DR Reactome; REACT_71.1; Gene Expression. DR LinkHub; Q13541; -. DR ArrayExpress; Q13541; -. DR GermOnline; ENSG00000187840; Homo sapiens. DR RZPD-ProtExp; RZPDo834D124; -. DR RZPD-ProtExp; U0186; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR008606; EIF4EBP. DR Pfam; PF05456; eIF_4EBP; 1. KW 3D-structure; Acetylation; Direct protein sequencing; Phosphorylation; KW Protein synthesis inhibitor; Translation regulation. FT INIT_MET 1 1 Removed. FT CHAIN 2 118 Eukaryotic translation initiation factor FT 4E-binding protein 1. FT /FTId=PRO_0000190513. FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 65 65 Phosphoserine (by MAPK1 and MAPK3) (By FT similarity). FT HELIX 56 61 FT TURN 62 62 SQ SEQUENCE 118 AA; 12580 MW; 1682A6BA74132966 CRC64; MSGGSSCSQT PSRAIPATRR VVLGDGVQLP PGDYSTTPGG TLFSTTPGGT RIIYDRKFLM ECRNSPVTKT PPRDLPTIPG VTSPSSDEPP MEASQSHLRN SPEDKRAGGE ESQFEMDI // ID 4EBP1_MOUSE Reviewed; 117 AA. AC Q60876; Q3TDS8; Q9CZ40; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 49. DE Eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) DE (eIF4E-binding protein 1) (Phosphorylated heat- and acid-stable DE protein regulated by insulin 1) (PHAS-I). GN Name=Eif4ebp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, RP PHOSPHORYLATION, AND INTERACTION WITH EIF4E. RX MEDLINE=95355483; PubMed=7629182; DOI=10.1074/jbc.270.31.18531; RA Lin T.-A., Kong X., Saltiel A.R., Blackshear P.J., Lawrence J.C. Jr.; RT "Control of PHAS-I by insulin in 3T3-L1 adipocytes. Synthesis, RT degradation, and phosphorylation by a rapamycin-sensitive and mitogen- RT activated protein kinase-independent pathway."; RL J. Biol. Chem. 270:18531-18538(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; 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/6; 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: Regulates eIF4E activity by preventing its assembly into CC the eIF4F complex. Mediates the regulation of protein translation CC by hormones, growth factors and other stimuli that signal through CC the MAP kinase pathway. CC -!- SUBUNIT: Nonphosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to CC interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and CC MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the CC complex allowing EIF4G1/EIF4G3 to bind and consequent initiation CC of translation. Rapamycin can attenuate insulin stimulation, CC mediated by FKBPs. CC -!- TISSUE SPECIFICITY: Highest expression in fat cells. CC -!- PTM: Phosphorylated on serine and threonine residues in response CC to insulin, EGF and PDGF. CC -!- SIMILARITY: Belongs to the eIF4E-binding protein family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U28656; AAA88818.1; -; mRNA. DR EMBL; AK013033; BAB28612.1; -; mRNA. DR EMBL; AK169979; BAE41494.1; -; mRNA. DR EMBL; AK170031; BAE41521.1; -; mRNA. DR EMBL; BC002045; AAH02045.1; -; mRNA. DR PIR; A57396; A57396. DR UniGene; Mm.6700; -. DR Ensembl; ENSMUSG00000031490; Mus musculus. DR KEGG; mmu:13685; -. DR MGI; MGI:103267; Eif4ebp1. DR ArrayExpress; Q60876; -. DR GermOnline; ENSMUSG00000031490; Mus musculus. DR RZPD-ProtExp; IOM15454; -. DR GO; GO:0005737; C:cytoplasm; IC:MGI. DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IPI:MGI. DR GO; GO:0030371; F:translation repressor activity; TAS:MGI. DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI. DR GO; GO:0045947; P:negative regulation of translational initia...; IDA:MGI. DR InterPro; IPR008606; EIF4EBP. DR Pfam; PF05456; eIF_4EBP; 1. KW Acetylation; Phosphorylation; Protein synthesis inhibitor; KW Translation regulation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 117 Eukaryotic translation initiation factor FT 4E-binding protein 1. FT /FTId=PRO_0000190514. FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 64 64 Phosphoserine (by MAPK1 and MAPK3) (By FT similarity). FT CONFLICT 93 93 S -> N (in Ref. 2; BAB28612). SQ SEQUENCE 117 AA; 12325 MW; 3458D5687468A7EA CRC64; MSAGSSCSQT PSRAIPTRRV ALGDGVQLPP GDYSTTPGGT LFSTTPGGTR IIYDRKFLME CRNSPVAKTP PKDLPAIPGV TSPTSDEPPM QASQSQLPSS PEDKRAGGEE SQFEMDI // ID 4EBP1_RAT Reviewed; 117 AA. AC Q62622; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-FEB-2007, entry version 38. DE Eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) DE (eIF4E-binding protein 1) (Phosphorylated heat- and acid-stable DE protein regulated by insulin 1) (PHAS-I). GN Name=Eif4ebp1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-33; 43-53; 62-80 RP AND 98-117, PHOSPHORYLATION, AND TISSUE SPECIFICITY. RC STRAIN=Sprague-Dawley; TISSUE=Adipocyte, and Skeletal muscle; RX MEDLINE=94224815; PubMed=8170978; RA Hu C., Pang S., Kong X., Velleca M., Lawrence J.C. Jr.; RT "Molecular cloning and tissue distribution of PHAS-I, an intracellular RT target for insulin and growth factors."; RL Proc. Natl. Acad. Sci. U.S.A. 91:3730-3734(1994). RN [2] RP FUNCTION, INTERACTION WITH EIF4E, PHOSPHORYLATION AT SER-64 BY MAPK1 RP AND MAPK3, AND MUTAGENESIS OF SER-64. RX MEDLINE=95025978; PubMed=7939721; RA Lin T.-A., Kong X., Haystead T.A.J., Pause A., Belsham G.J., RA Sonenberg N., Lawrence J.C. Jr.; RT "PHAS-I as a link between mitogen-activated protein kinase and RT translation initiation."; RL Science 266:653-656(1994). CC -!- FUNCTION: Regulates eIF4E activity by preventing its assembly into CC the eIF4F complex. Mediates the regulation of protein translation CC by hormones, growth factors and other stimuli that signal through CC the MAP kinase pathway. CC -!- SUBUNIT: Nonphosphorylated EIF4EBP1 competes with EIF4G1/EIFG3 to CC interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and CC MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the CC complex allowing EIF4G to bind and consequent initiation of CC translation. Rapamycin can attenuate insulin stimulation, mediated CC by FKBPs. CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined; highest CC levels in fat and skeletal tissue, lowest levels in kidney. CC -!- PTM: Phosphorylated on serine and threonine residues in response CC to insulin, EGF and PDGF. CC -!- SIMILARITY: Belongs to the eIF4E-binding protein family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U05014; AAA86938.1; -; mRNA. DR PIR; A55258; A55258. DR UniGene; Rn.11161; -. DR DIP; DIP:267N; -. DR Ensembl; ENSRNOG00000012582; Rattus norvegicus. DR KEGG; rno:116636; -. DR RGD; 620259; Eif4ebp1. DR ArrayExpress; Q62622; -. DR GermOnline; ENSRNOG00000012582; Rattus norvegicus. DR InterPro; IPR008606; EIF4EBP. DR Pfam; PF05456; eIF_4EBP; 1. KW Acetylation; Direct protein sequencing; Phosphorylation; KW Protein synthesis inhibitor; Translation regulation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 117 Eukaryotic translation initiation factor FT 4E-binding protein 1. FT /FTId=PRO_0000190515. FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 64 64 Phosphoserine (by MAPK1 and MAPK3). FT MUTAGEN 64 64 S->A: Decreases phosphorylation by MAPK1 FT and MAPK3. FT CONFLICT 19 19 R -> N (in Ref. 1; AA sequence). FT CONFLICT 69 69 T -> P (in Ref. 1; AA sequence). FT CONFLICT 75 75 P -> L (in Ref. 1; AA sequence). SQ SEQUENCE 117 AA; 12404 MW; 3449D57B09FA101A CRC64; MSAGSSCSQT PSRAIPTRRV ALGDGVQLPP GDYSTTPGGT LFSTTPGGTR IIYDRKFLME CRNSPVAKTP PKDLPTIPGV TSPTSDEPPM QASQSHLHSS PEDKRAGGEE SQFEMDI // ID 4EBP2_HUMAN Reviewed; 120 AA. AC Q13542; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 49. DE Eukaryotic translation initiation factor 4E-binding protein 2 (4E-BP2) DE (eIF4E-binding protein 2). GN Name=EIF4EBP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH EIF4E. RC TISSUE=Placenta; RX MEDLINE=95021760; PubMed=7935836; DOI=10.1038/371762a0; RA Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A., RA Lawrence J.C. Jr., Sonenberg N.; RT "Insulin-dependent stimulation of protein synthesis by phosphorylation RT of a regulator of 5'-cap function."; RL Nature 371:762-767(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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 eIF4E activity by preventing its assembly into CC the eIF4F complex. Mediates the regulation of protein translation CC by hormones, growth factors and other stimuli that signal through CC the MAP kinase pathway. CC -!- SUBUNIT: Nonphosphorylated EIF4EBP2 interacts with EIF4E. CC -!- INTERACTION: CC P06730:EIF4E; NbExp=1; IntAct=EBI-935137, EBI-73440; CC Q80ZJ3:Eif4e2 (xeno); NbExp=1; IntAct=EBI-935137, EBI-934970; CC -!- PTM: Phosphorylated on serine and threonine residues in response CC to insulin, EGF and PDGF. CC -!- SIMILARITY: Belongs to the eIF4E-binding protein family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L36056; AAA62270.1; -; mRNA. DR EMBL; BT007317; AAP35981.1; -; mRNA. DR EMBL; BC005057; AAH05057.1; -; mRNA. DR EMBL; BC050633; AAH50633.1; -; mRNA. DR PIR; S50867; S50867. DR UniGene; Hs.621200; -. DR UniGene; Hs.643279; -. DR IntAct; Q13542; -. DR Ensembl; ENSG00000148730; Homo sapiens. DR KEGG; hsa:1979; -. DR H-InvDB; HIX0008896; -. DR HGNC; HGNC:3289; EIF4EBP2. DR MIM; 602224; gene. DR LinkHub; Q13542; -. DR ArrayExpress; Q13542; -. DR GermOnline; ENSG00000148730; Homo sapiens. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006412; P:translation; TAS:ProtInc. DR InterPro; IPR008606; EIF4EBP. DR PANTHER; PTHR12669; EIF4EBP; 1. DR Pfam; PF05456; eIF_4EBP; 1. KW Phosphorylation; Protein synthesis inhibitor; Translation regulation. FT CHAIN 1 120 Eukaryotic translation initiation factor FT 4E-binding protein 2. FT /FTId=PRO_0000190516. FT MOD_RES 65 65 Phosphoserine (by MAPK1 and MAPK3) (By FT similarity). SQ SEQUENCE 120 AA; 12939 MW; B8F109261A504193 CRC64; MSSSAGSGHQ PSQSRAIPTR TVAISDAAQL PHDYCTTPGG TLFSTTPGGT RIIYDRKFLL DRRNSPMAQT PPCHLPNIPG VTSPGTLIED SKVEVNNLNN LNNHDRKHAV GDDAQFEMDI // ID 4EBP2_MOUSE Reviewed; 120 AA. AC P70445; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 23-JAN-2007, entry version 40. DE Eukaryotic translation initiation factor 4E-binding protein 2 (4E-BP2) DE (eIF4E-binding protein 2) (Phosphorylated heat- and acid-stable DE protein regulated by insulin 2) (PHAS-II). GN Name=Eif4ebp2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97094737; PubMed=8939971; DOI=10.1074/jbc.271.47.30199; RA Lin T.A., Lawrence J.C. Jr.; RT "Control of the translational regulators PHAS-I and PHAS-II by insulin RT and cAMP in 3T3-L1 adipocytes."; RL J. Biol. Chem. 271:30199-30204(1996). 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: Regulates eIF4E activity by preventing its assembly into CC the eIF4F complex. Mediates the regulation of protein translation CC by hormones, growth factors and other stimuli that signal through CC the MAP kinase pathway (By similarity). CC -!- SUBUNIT: Nonphosphorylated EIF4EBP2 interacts with EIF4E (By CC similarity). CC -!- PTM: Phosphorylated on serine and threonine residues in response CC to insulin, EGF and PDGF (By similarity). CC -!- SIMILARITY: Belongs to the eIF4E-binding protein family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U75530; AAC52899.1; -; mRNA. DR EMBL; BC015082; AAH15082.1; -; mRNA. DR UniGene; Mm.259516; -. DR Ensembl; ENSMUSG00000020091; Mus musculus. DR MGI; MGI:109198; Eif4ebp2. DR ArrayExpress; P70445; -. DR GermOnline; ENSMUSG00000020091; Mus musculus. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR GO; GO:0019933; P:cAMP-mediated signaling; IDA:MGI. DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI. DR GO; GO:0006446; P:regulation of translational initiation; TAS:MGI. DR InterPro; IPR008606; EIF4EBP. DR PANTHER; PTHR12669; EIF4EBP; 1. DR Pfam; PF05456; eIF_4EBP; 1. KW Phosphorylation; Protein synthesis inhibitor; Translation regulation. FT CHAIN 1 120 Eukaryotic translation initiation factor FT 4E-binding protein 2. FT /FTId=PRO_0000190517. FT MOD_RES 65 65 Phosphoserine (by MAPK1 and MAPK3) (By FT similarity). SQ SEQUENCE 120 AA; 12898 MW; 0A1ACC082583F769 CRC64; MSASAGGSHQ PSQSRAIPTR TVAISDAAQL PQDYCTTPGG TLFSTTPGGT RIIYDRKFLL DRRNSPMAQT PPCHLPNIPG VTSPGALIED SKVEVNNLNN LNNHDRKHAV GDEAQFEMDI // ID 4EBP3_HUMAN Reviewed; 100 AA. AC O60516; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 20-FEB-2007, entry version 45. DE Eukaryotic translation initiation factor 4E-binding protein 3 (4E-BP3) DE (eIF4E-binding protein 3). GN Name=EIF4EBP3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EIF4E, MUTAGENESIS OF RP TYR-40 AND LEU-45, AND TISSUE SPECIFICITY. RX MEDLINE=98256334; PubMed=9593750; DOI=10.1074/jbc.273.22.14002; RA Poulin F., Gingras A.-C., Olsen H., Chevalier S., Sonenberg N.; RT "4E-BP3, a new member of the eukaryotic initiation factor 4E-binding RT protein family."; RL J. Biol. Chem. 273:14002-14007(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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 eIF4E activity by preventing its assembly into CC the eIF4F complex. CC -!- SUBUNIT: EIF4EBP3 interacts with EIF4E. CC -!- INTERACTION: CC P06730:EIF4E; NbExp=2; IntAct=EBI-746950, EBI-73440; CC Q80ZJ3:Eif4e2 (xeno); NbExp=2; IntAct=EBI-746950, EBI-934970; CC -!- TISSUE SPECIFICITY: Expression is highest in skeletal muscle, CC heart, kidney, and pancreas, whereas there is very little CC expression in brain and thymus. CC -!- PTM: Phosphorylated. CC -!- SIMILARITY: Belongs to the eIF4E-binding protein family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF038869; AAC39761.1; -; mRNA. DR EMBL; BC010881; AAH10881.1; -; mRNA. DR EMBL; BC069293; AAH69293.1; -; mRNA. DR EMBL; BC073751; AAH73751.1; -; mRNA. DR UniGene; Hs.434219; -. DR IntAct; O60516; -. DR Ensembl; ENSG00000131503; Homo sapiens. DR KEGG; hsa:8637; -. DR HGNC; HGNC:3290; EIF4EBP3. DR MIM; 603483; gene. DR ArrayExpress; O60516; -. DR GermOnline; ENSG00000131503; Homo sapiens. DR RZPD-ProtExp; W0996; -. DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F...; NAS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0030371; F:translation repressor activity; NAS:UniProtKB. DR GO; GO:0045947; P:negative regulation of translational initia...; NAS:UniProtKB. DR InterPro; IPR008606; EIF4EBP. DR PANTHER; PTHR12669; EIF4EBP; 1. DR Pfam; PF05456; eIF_4EBP; 1. KW Phosphorylation; Protein synthesis inhibitor; Translation regulation. FT CHAIN 1 100 Eukaryotic translation initiation factor FT 4E-binding protein 3. FT /FTId=PRO_0000190518. FT MUTAGEN 40 40 Y->A: Loss of interaction with EIF4E. FT MUTAGEN 45 45 L->A: Loss of interaction with EIF4E. SQ SEQUENCE 100 AA; 10873 MW; FD29A7F3829E546E CRC64; MSTSTSCPIP GGRDQLPDCY STTPGGTLYA TTPGGTRIIY DRKFLLECKN SPIARTPPCC LPQIPGVTTP PTAPLSKLEE LKEQETEEEI PDDAQFEMDI // ID 4EBP3_MOUSE Reviewed; 101 AA. AC Q80VV3; Q2TA53; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 20-FEB-2007, entry version 29. DE Eukaryotic translation initiation factor 4E-binding protein 3 (4E-BP3) DE (eIF4E-binding protein 3). GN Name=Eif4ebp3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RA Poulin F., Sonenberg N.; RT "Two overlapping reading frames in the second exon of the RT translational inhibitor 4E-BP3."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. 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: Regulates eIF4E activity by preventing its assembly into CC the eIF4F complex (By similarity). CC -!- SUBUNIT: EIF4EBP3 interacts with EIF4E (By similarity). CC -!- PTM: Phosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the eIF4E-binding protein family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY226182; AAO73448.1; -; mRNA. DR EMBL; BC061242; AAH61242.1; -; mRNA. DR EMBL; BC111107; AAI11108.1; -; mRNA. DR UniGene; Mm.24790; -. DR Ensembl; ENSMUSG00000033775; Mus musculus. DR MGI; MGI:1270847; Eif4ebp3. DR GermOnline; ENSMUSG00000073595; Mus musculus. DR InterPro; IPR008606; EIF4EBP. DR PANTHER; PTHR12669; EIF4EBP; 1. DR Pfam; PF05456; eIF_4EBP; 1. KW Phosphorylation; Protein synthesis inhibitor; Translation regulation. FT CHAIN 1 101 Eukaryotic translation initiation factor FT 4E-binding protein 3. FT /FTId=PRO_0000190519. SQ SEQUENCE 101 AA; 11019 MW; 78F82052696A9BD7 CRC64; MSSSTSCPIP GCRDQLPDGY STTPGGTLYA TTPGGTRIIY DRKFLLECKN SPIARTPPCC LPQIPGVTTL PAVPPSKLEL LKEQKQTEVE ITDDEQFEMD M // ID 4EBP_BRARE Reviewed; 112 AA. AC Q98TT6; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 20-FEB-2007, entry version 24. DE Eukaryotic translation initiation factor 4E-1A-binding protein (eIF4E- DE 1A-binding protein) (4E-BP). GN ORFNames=zgc:56330; OS Brachydanio rerio (Zebrafish) (Danio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH EIF4E1A. RX PubMed=14701818; DOI=10.1074/jbc.M313688200; RA Robalino J., Joshi B., Fahrenkrug S.C., Jagus R.; RT "Two zebrafish eIF4E family members are differentially expressed and RT functionally divergent."; RL J. Biol. Chem. 279:10532-10541(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Regulates eif4e1a activity by preventing its assembly CC into the eIF4F complex (By similarity). CC -!- SUBUNIT: Interacts with eif4e1a. CC -!- SIMILARITY: Belongs to the eIF4E-binding protein family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF332983; AAG50053.1; -; mRNA. DR EMBL; BC046079; AAH46079.1; -; mRNA. DR UniGene; Dr.78024; -. DR Ensembl; ENSDARG00000023315; Danio rerio. DR ZFIN; ZDB-GENE-030131-3211; zgc:56330. DR ArrayExpress; Q98TT6; -. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB. DR GO; GO:0045947; P:negative regulation of translational initia...; ISS:UniProtKB. DR InterPro; IPR008606; EIF4EBP. DR PANTHER; PTHR12669; EIF4EBP; 1. DR Pfam; PF05456; eIF_4EBP; 1. KW Protein synthesis inhibitor; Translation regulation. FT CHAIN 1 112 Eukaryotic translation initiation factor FT 4E-1A-binding protein. FT /FTId=PRO_0000190520. SQ SEQUENCE 112 AA; 12531 MW; F71BEA295722826E CRC64; MSTNTQQSKS CPIPTRVLHL KDWSQLPDCY SQTPGGTLFS TTPGGTRIIY DRKFLLDCRN SPIARTPPCC LPQIPGVTIP SLHPVSKLQE LKEELEEEKE LAADDSQFEM DI // ID 4ET_HUMAN Reviewed; 985 AA. AC Q9NRA8; Q8NCF2; Q9H708; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2002, sequence version 2. DT 20-FEB-2007, entry version 48. DE Eukaryotic translation initiation factor 4E transporter (eIF4E DE transporter) (4E-T) (Eukaryotic translation initiation factor 4E DE nuclear import factor 1). GN Name=EIF4ENIF1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, RP PHOSPHORYLATION, AND MUTAGENESIS OF TYR-30 AND 195-ARG-ARG-196. RC TISSUE=Fetal brain; RX MEDLINE=20315895; PubMed=10856257; DOI=10.1093/emboj/19.12.3142; RA Dostie J., Ferraiuolo M., Pause A., Adam S.A., Sonenberg N.; RT "A novel shuttling protein, 4E-T, mediates the nuclear import of the RT mRNA 5' cap-binding protein, eIF4E."; RL EMBO J. 19:3142-3156(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 351-985. RC TISSUE=Colon, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). CC -!- FUNCTION: Nucleoplasmic shuttling protein. Mediates the nuclear CC import of EIF4E by a piggy-back mechanism. CC -!- SUBUNIT: Interacts with EIF4E. Interacts with importin beta only CC in presence of importin alpha, suggesting a direct interaction CC with importin alpha. CC -!- INTERACTION: CC P06730:EIF4E; NbExp=1; IntAct=EBI-301024, EBI-73440; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly CC cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CC CRM1-dependent manner. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NRA8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NRA8-2; Sequence=VSP_003783, VSP_003784; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- PTM: Phosphorylated. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF240775; AAF81693.1; -; mRNA. DR EMBL; CR456386; CAG30272.1; -; mRNA. DR EMBL; BC032941; AAH32941.1; -; mRNA. DR EMBL; BC033028; AAH33028.1; -; mRNA. DR EMBL; AK025254; BAB15092.1; ALT_INIT; mRNA. DR EMBL; AK074768; BAC11194.1; ALT_INIT; mRNA. DR UniGene; Hs.517559; -. DR IntAct; Q9NRA8; -. DR Ensembl; ENSG00000184708; Homo sapiens. DR KEGG; hsa:56478; -. DR H-InvDB; HIX0016395; -. DR HGNC; HGNC:16687; EIF4ENIF1. DR HPA; HPA001619; -. DR HPA; HPA002078; -. DR MIM; 607445; gene. DR ArrayExpress; Q9NRA8; -. DR GermOnline; ENSG00000184708; Homo sapiens. DR RZPD-ProtExp; IOH22443; -. DR RZPD-ProtExp; IOH27165; -. DR RZPD-ProtExp; RZPDo839H0561; -. DR RZPD-ProtExp; RZPDo839H0571; -. DR RZPD-ProtExp; V1281; -. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0008565; F:protein transporter activity; TAS:ProtInc. KW Alternative splicing; Nuclear protein; Phosphorylation; KW Protein transport; Transport. FT CHAIN 1 985 Eukaryotic translation initiation factor FT 4E transporter. FT /FTId=PRO_0000064381. FT REGION 30 36 EIF4E-binding. FT MOTIF 195 211 Nuclear localization signal. FT MOTIF 438 447 Nuclear export signal. FT MOTIF 613 638 Nuclear export signal. FT COMPBIAS 148 210 Arg-rich. FT MOD_RES 587 587 Phosphoserine (By similarity). FT VAR_SEQ 100 262 Missing (in isoform 2). FT /FTId=VSP_003783. FT VAR_SEQ 493 504 Missing (in isoform 2). FT /FTId=VSP_003784. FT MUTAGEN 30 30 Y->A: Abolishes interaction with EIF4E. FT MUTAGEN 195 196 RR->NS: Abolishes the nuclear FT localization. FT CONFLICT 114 114 L -> F (in Ref. 1). FT CONFLICT 616 616 Q -> QQ (in Ref. 3; AAH32941 and 4). FT CONFLICT 825 825 Q -> R (in Ref. 3). SQ SEQUENCE 985 AA; 108201 MW; 4C898E0488903C04 CRC64; MDRRSMGETE SGDAFLDLKK PPASKCPHRY TKEELLDIKE LPHSKQRPSC LSEKYDSDGV WDPEKWHASL YPASGRSSPV ESLKKELDTD RPSLVRRIVD PRERVKEDDL DVVLSPQRRS FGGGCHVTAA VSSRRSGSPL EKDSDGLRLL GGRRIGSGRI ISARTFEKDH RLSDKDLRDL RDRDRERDFK DKRFRREFGD SKRVFGERRR NDSYTEEEPE WFSAGPTSQS ETIELTGFDD KILEEDHKGR KRTRRRTASV KEGIVECNGG VAEEDEVEVI LAQEPAADQE VPRDAVLPEQ SPGDFDFNEF FNLDKVPCLA SMIEDVLGEG SVSASRFSRW FSNPSRSGSR SSSLGSTPHE ELERLAGLEQ AILSPGQNSG NYFAPIPLED HAENKVDILE MLQKAKVDLK PLLSSLSANK EKLKESSHSG VVLSVEEVEA GLKGLKVDQQ VKNSTPFMAE HLEETLSAVT NNRQLKKDGD MTAFNKLVST MKASGTLPSQ PKVSRNLESH LMSPAEIPGQ PVPKNILQEL LGQPVQRPAS SNLLSGLMGS LEPTTSLLGQ RAPSPPLSQV FQTRAASADY LRPRIPSPIG FTPGPQQLLG DPFQGMRKPM SPITAQMSQL ELQQAALEGL ALPHDLAVQA ANFYQPGFGK PQVDRTRDGF RNRQQRVTKS PAPVHRGNSS SPAPAASITS MLSPSFTPTS VIRKMYESKE KSKEEPASGK AALGDSKEDT QKASEENLLS SSSVPSADRD SSPTTNSKLS ALQRSSCSTP LSQANRYTKE QDYRPKATGR KTPTLASPVP TTPFLRPVHQ VPLVPHVPMV RPAHQLHPGL VQRMLAQGVH PQHLPSLLQT GVLPPGMDLS HLQGISGPIL GQPFYPLPAA SHPLLNPRPG TPLHLAMVQQ QLQRSVLHPP GSGSHAAAVS VQTTPQNVPS RSGLPHMHSQ LEHRPSQRSS SPVGLAKWFG SDVLQQPLPS MPAKVISVDE LEYRQ // ID 4ET_MOUSE Reviewed; 983 AA. AC Q9EST3; Q9CSS3; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 23-JAN-2007, entry version 35. DE Eukaryotic translation initiation factor 4E transporter (eIF4E DE transporter) (4E-T) (Eukaryotic translation initiation factor 4E DE nuclear import factor 1). GN Name=Eif4enif1; Synonyms=Clast4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA O-Wang J.; RT "Cloning and characterization of a novel CD40-activated gene."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 428-983 (ISOFORM 2). 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND MASS RP SPECTROMETRY. 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). CC -!- FUNCTION: Nucleoplasmic shuttling protein. Mediates the nuclear CC import of EIF4E by a piggy-back mechanism (By similarity). CC -!- SUBUNIT: Interacts with EIF4E. Interacts with importin beta only CC in presence of importin alpha, suggesting a direct interaction CC with importin alpha (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). Note=Shuttles between the nucleus and cytoplasm in a CC CRM1-dependent manner. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9EST3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9EST3-2; Sequence=VSP_003785; CC Note=No experimental confirmation available; CC -!- PTM: Phosphorylated (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; AB031388; BAB11963.1; -; mRNA. DR EMBL; AK012082; BAB28016.1; -; mRNA. DR UniGene; Mm.255649; -. DR Ensembl; ENSMUSG00000020454; Mus musculus. DR KEGG; mmu:74203; -. DR MGI; MGI:1921453; Eif4enif1. DR ArrayExpress; Q9EST3; -. DR GermOnline; ENSMUSG00000020454; Mus musculus. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005515; F:protein binding; IPI:MGI. KW Alternative splicing; Nuclear protein; Phosphorylation; KW Protein transport; Transport. FT CHAIN 1 983 Eukaryotic translation initiation factor FT 4E transporter. FT /FTId=PRO_0000064382. FT REGION 29 35 EIF4E-binding (By similarity). FT MOTIF 194 210 Nuclear localization signal (By FT similarity). FT MOTIF 437 446 Nuclear export signal (By similarity). FT MOTIF 612 637 Nuclear export signal (By similarity). FT COMPBIAS 147 209 Arg-rich. FT MOD_RES 586 586 Phosphoserine. FT VAR_SEQ 504 527 Missing (in isoform 2). FT /FTId=VSP_003785. FT CONFLICT 773 773 N -> S (in Ref. 2). SQ SEQUENCE 983 AA; 107985 MW; 0EDC6500589CA4F4 CRC64; MEKSVAETEN GDAFLELKKL PTSKSPHRYT KEELLDIKER PYSKQRPSCL SEKYDSDGVW DPEKWHASLY PASGRSSPVE SLKKESESDR PSLVRRIADP RERVKEDDLD VVLSPQRRSF GGGCHVTAAV SSRRSGSPLE KDSDGLRLLG GRRIGSGRII SARAFEKDHR LSDKDLRDLR DRDRERDYKD KRFRREFGDS KRVFGERRRN DSYTEEEPEW FSAGPTSQSE TIELTGFDDK ILEEDHKGRK RTRRRTASVK EGIVECNGGV AEEDEVEVIL AQEPSADQEV PRDVILPEQS PGEFDFNEFF NLDKVPCLAS MIEDVLGEGS VSASRFSRWF SNPSQSGSRS SSLGSTPHEE LERLAGLEQA VLSPGQNSGN YFAPIPSEDH AENKVDILEM LQKAKVDLKP LLSSLSANKE KLKESSHSGV VLSVEEVEAG LKGLKVDQQM KNSTPFMAEH LEETLSAASS NRQLKKDGDM TAFNKLVNTM KASGTLPTQP KVSRNVESHL LAPAEIPGQP VSKNILQELL GQPVQRPASS NLLSGLMGSL EATASLLSQR APSPPMSQVF RTQAASADYL HPRIPSPIGF PSGPQQLLGD PFQGMRKPMS PVSAQMSQLE LQQAALEGLA LPHDLAVQTA PFYQPGFSKP QVDRTRDGLR NRQQRMSKSP APMHGGNSSS PAPAASITSM LSPSFTPTSV IRKMYESREK TKEEMAPGMV VPGDGKEDTQ KTSEENLLSS NPIPNTDQDS STTNPKLSTL QRSSCSTPLS QTNRYTKEQD YRPKTAGRKT PTLASPVPGT PFLRPTHQVP LVPHVPIVRP AHQLHPGLVQ RLIAQGVHPQ HLPSLLQAGV LPPGIDMAPL QGLSGPLLGQ PLYPLVSAAS HPLLNPRPGT PLHLAVMQQQ LQRSVLHPPG SSSQAAAISV QTPQNVPSRS GMPHMHSQLE HRTSQRSSSP VGLAKWFGSD VLQQPLPSMP TKVISVDELE YRQ // ID 4F2_HUMAN Reviewed; 529 AA. AC P08195; Q13543; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 2. DT 20-FEB-2007, entry version 83. DE 4F2 cell-surface antigen heavy chain (4F2hc) (Lymphocyte activation DE antigen 4F2 large subunit) (4F2 heavy chain antigen) (CD98 antigen). GN Name=SLC3A2; Synonyms=MDU1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87317685; PubMed=3476959; RA Quackenbush E., Clabby M., Gottesdiener K.M., Barbosa J., Jones N.H., RA Strominger J.L., Speck S., Leiden J.M.; RT "Molecular cloning of complementary DNAs encoding the heavy chain of RT the human 4F2 cell-surface antigen: a type II membrane glycoprotein RT involved in normal and neoplastic cell growth."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6526-6530(1987). RN [2] RP ERRATUM, AND SEQUENCE REVISION. RA Quackenbush E., Clabby M., Gottesdiener K.M., Barbosa J., Jones N.H., RA Strominger J.L., Speck S., Leiden J.M.; RL Proc. Natl. Acad. Sci. U.S.A. 84:8618-8618(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87250620; PubMed=3036867; RA Teixeira S., di Grandi S., Kuehn L.C.; RT "Primary structure of the human 4F2 antigen heavy chain predicts a RT transmembrane protein with a cytoplasmic NH2 terminus."; RL J. Biol. Chem. 262:9574-9580(1987). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88097456; PubMed=3480538; RA Lumadue J.A., Glick A.B., Ruddle F.H.; RT "Cloning, sequence analysis, and expression of the large subunit of RT the human lymphocyte activation antigen 4F2."; RL Proc. Natl. Acad. Sci. U.S.A. 84:9204-9208(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89127222; PubMed=3265470; RA Gottesdiener K.M., Karpinski B.A., Lindsten T., Strominger J.L., RA Jones N.H., Thompson C.B., Leiden J.M.; RT "Isolation and structural characterization of the human 4F2 heavy- RT chain gene, an inducible gene involved in T-lymphocyte activation."; RL Mol. Cell. Biol. 8:3809-3819(1988). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RA Yanagida O., Segawa H., Miyamoto K., Takeda E., Goya T., Endou H., RA Kanai Y.; RT "Cloning and characterization of a human system L amino acid RT transporter."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 11-21; 47-59; 126-144; 147-154; 187-197; 203-212; RP 339-350; 410-423 AND 492-524, AND MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Unpublished observations (MAR-2005). RN [9] RP GLYCOSYLATION AT ASN-264; ASN-280 AND ASN-323. RX MEDLINE=22660472; PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [10] RP MASS SPECTROMETRY. RC TISSUE=Mammary cancer; RX MEDLINE=21829512; PubMed=11840567; RX DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H; RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., RA Zvelebil M.J.; RT "Cluster analysis of an extensive human breast cancer cell line RT protein expression map database."; RL Proteomics 2:212-223(2002). RN [11] RP INTERACTION WITH CT120. RX MEDLINE=22230983; PubMed=12270127; DOI=10.1016/S0006-291X(02)02227-1; RA He X.H., Di Y., Li J., Xie Y., Tang Y., Zhang F., Wei L., Zhang Y., RA Qin W.X., Huo K., Li Y., Wan D.F., Gu J.R.; RT "Molecular cloning and characterization of CT120, a novel membrane- RT associated gene involved in amino acid transport and glutathione RT metabolism."; RL Biochem. Biophys. Res. Commun. 297:528-536(2002). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-280 AND ASN-323, AND MASS RP SPECTROMETRY. RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-5, AND MASS RP SPECTROMETRY. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [14] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). CC -!- FUNCTION: Involved in sodium-independent, high-affinity transport CC of large neutral amino acids (By similarity). Required for normal CC and neoplastic cell growth. CC -!- SUBUNIT: Disulfide-linked heterodimer of a glycosylated heavy CC chain and a nonglycosylated light chain (SLC7A5 or SLC7A8). CC Interacts with FAM57A. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type II membrane CC protein. Melanosome. Note=Identified by mass spectrometry in CC melanosome fractions from stage I to stage IV. CC -!- MASS SPECTROMETRY: MW=57944.93; METHOD=MALDI; RANGE=1-529; CC NOTE=Ref.10. CC -!- SIMILARITY: Belongs to the SLC3A transporter family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J02939; AAA52497.1; -; mRNA. DR EMBL; J02769; AAA51540.1; -; mRNA. DR EMBL; J03569; AAA35536.1; -; mRNA. DR EMBL; M21904; AAA35489.1; -; Genomic_DNA. DR EMBL; M21898; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; M21899; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; M21900; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; M21901; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; M21902; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; M21903; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; AB018010; BAA84649.1; -; mRNA. DR EMBL; BC001061; AAH01061.2; -; mRNA. DR EMBL; BC003000; AAH03000.2; ALT_INIT; mRNA. DR PIR; A28455; SAHU4F. DR UniGene; Hs.502769; -. DR IntAct; P08195; -. DR Ensembl; ENSG00000168003; Homo sapiens. DR KEGG; hsa:6520; -. DR H-InvDB; HIX0018301; -. DR HGNC; HGNC:11026; SLC3A2. DR MIM; 158070; gene. DR ArrayExpress; P08195; -. DR RZPD-ProtExp; G0009; -. DR RZPD-ProtExp; IOH4673; -. DR GO; GO:0009986; C:cell surface; IEP:UniProtKB. DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB. DR GO; GO:0005432; F:calcium:sodium antiporter activity; TAS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0006816; P:calcium ion transport; NAS:UniProtKB. DR GO; GO:0016049; P:cell growth; NAS:UniProtKB. DR GO; GO:0015827; P:tryptophan transport; ISS:UniProtKB. DR InterPro; IPR013780; Glyco_hydro_13_b. DR InterPro; IPR006047; Glyco_hydro_13_cat. DR InterPro; IPR013781; Glyco_hydro_cat. DR Pfam; PF00128; Alpha-amylase; 1. KW Amino-acid transport; Direct protein sequencing; Glycoprotein; KW Membrane; Phosphorylation; Signal-anchor; Transmembrane; Transport. FT CHAIN 1 529 4F2 cell-surface antigen heavy chain. FT /FTId=PRO_0000064383. FT TOPO_DOM 1 81 Cytoplasmic (Potential). FT TRANSMEM 82 104 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 105 529 Extracellular (Potential). FT MOD_RES 2 2 Phosphoserine. FT MOD_RES 5 5 Phosphothreonine. FT CARBOHYD 264 264 N-linked (GlcNAc...). FT CARBOHYD 280 280 N-linked (GlcNAc...). FT CARBOHYD 323 323 N-linked (GlcNAc...). FT CARBOHYD 405 405 N-linked (GlcNAc...) (Potential). FT DISULFID 109 109 Interchain (with light chain) (Probable). FT DISULFID 330 330 Interchain (with light chain) (Probable). FT CONFLICT 36 36 G -> E (in Ref. 4). FT CONFLICT 57 57 A -> P (in Ref. 3). FT CONFLICT 122 122 A -> P (in Ref. 4). FT CONFLICT 214 214 E -> D (in Ref. 4). FT CONFLICT 219 219 S -> F (in Ref. 5). FT CONFLICT 271 271 E -> G (in Ref. 4). FT CONFLICT 311 312 GE -> PQ (in Ref. 4). FT CONFLICT 364 364 V -> L (in Ref. 4). FT CONFLICT 380 380 G -> P (in Ref. 4). FT CONFLICT 448 448 G -> E (in Ref. 5). FT CONFLICT 508 508 L -> P (in Ref. 4). FT CONFLICT 511 511 E -> G (in Ref. 4). SQ SEQUENCE 529 AA; 57945 MW; 82F26856737E8F31 CRC64; MSQDTEVDMK EVELNELEPE KQPMNAASGA AMSLAGAEKN GLVKIKVAED EAEAAAAAKF TGLSKEELLK VAGSPGWVRT RWALLLLFWL GWLGMLAGAV VIIVRAPRCR ELPAQKWWHT GALYRIGDLQ AFQGHGAGNL AGLKGRLDYL SSLKVKGLVL GPIHKNQKDD VAQTDLLQID PNFGSKEDFD SLLQSAKKKS IRVILDLTPN YRGENSWFST QVDTVATKVK DALEFWLQAG VDGFQVRDIE NLKDASSFLA EWQNITKGFS EDRLLIAGTN SSDLQQILSL LESNKDLLLT SSYLSDSGST GEHTKSLVTQ YLNATGNRWC SWSLSQARLL TSFLPAQLLR LYQLMLFTLP GTPVFSYGDE IGLDAAALPG QPMEAPVMLW DESSFPDIPG AVSANMTVKG QSEDPGSLLS LFRRLSDQRS KERSLLHGDF HAFSAGPGLF SYIRHWDQNE RFLVVLNFGD VGLSAGLQAS DLPASASLPA KADLLLSTQP GREEGSPLEL ERLKLEPHEG LLLRFPYAA // ID 4F2_MOUSE Reviewed; 526 AA. AC P10852; Q54AH5; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 20-FEB-2007, entry version 63. DE 4F2 cell-surface antigen heavy chain (4F2hc). GN Name=Slc3a2; Synonyms=Mdu1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X DBA/2, and ICR; RX MEDLINE=89183602; PubMed=2928113; DOI=10.1093/nar/17.5.1915; RA Parmacek M.S., Karpinski B.A., Gottsdiener K.M., Thompson C.B., RA Leiden J.M.; RT "Structure, expression and regulation of the murine 4F2 heavy chain."; RL Nucleic Acids Res. 17:1915-1931(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR; TISSUE=Brain; RA Kanai Y., Watanabe M., Endou H.; RT "Localization of expression of system L neutral amino acid transporter RT LAT1 in brain."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney, 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]. 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: Involved in sodium-independent, high-affinity transport CC of large neutral amino acids (By similarity). Required for normal CC and neoplastic cell growth. CC -!- SUBUNIT: Disulfide-linked heterodimer of a glycosylated heavy CC chain and a nonglycosylated light chain (SLC7A5 or SLC7A8). CC Interacts with FAM57A (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type II membrane CC protein. Melanosome (By similarity). CC -!- SIMILARITY: Belongs to the SLC3A transporter family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14309; CAA32490.1; -; mRNA. DR EMBL; AB023408; BAA90555.1; -; mRNA. DR EMBL; AK161280; BAE36291.1; -; mRNA. DR EMBL; AK165417; BAE38172.1; -; mRNA. DR EMBL; BC065173; AAH65173.1; -; mRNA. DR PIR; S03600; S03600. DR UniGene; Mm.4114; -. DR Ensembl; ENSMUSG00000010095; Mus musculus. DR KEGG; mmu:17254; -. DR MGI; MGI:96955; Slc3a2. DR ArrayExpress; P10852; -. DR GermOnline; ENSMUSG00000010095; Mus musculus. DR GO; GO:0016021; C:integral to membrane; ISS:UniProtKB. DR GO; GO:0005515; F:protein binding; ISS:UniProtKB. DR GO; GO:0015827; P:tryptophan transport; ISS:UniProtKB. DR InterPro; IPR013780; Glyco_hydro_13_b. DR InterPro; IPR006047; Glyco_hydro_13_cat. DR InterPro; IPR013781; Glyco_hydro_cat. DR Pfam; PF00128; Alpha-amylase; 1. KW Amino-acid transport; Glycoprotein; Membrane; Phosphorylation; KW Signal-anchor; Transmembrane; Transport. FT CHAIN 1 526 4F2 cell-surface antigen heavy chain. FT /FTId=PRO_0000064384. FT TOPO_DOM 1 75 Cytoplasmic (Potential). FT TRANSMEM 76 99 Signal-anchor for type II membrane FT protein. FT TOPO_DOM 100 526 Extracellular (Potential). FT MOD_RES 2 2 Phosphoserine (By similarity). FT MOD_RES 5 5 Phosphothreonine (By similarity). FT CARBOHYD 166 166 N-linked (GlcNAc...) (Potential). FT CARBOHYD 259 259 N-linked (GlcNAc...) (Potential). FT CARBOHYD 263 263 N-linked (GlcNAc...) (Potential). FT CARBOHYD 301 301 N-linked (GlcNAc...) (Potential). FT CARBOHYD 318 318 N-linked (GlcNAc...) (Potential). FT CARBOHYD 385 385 N-linked (GlcNAc...) (Potential). FT CARBOHYD 399 399 N-linked (GlcNAc...) (Potential). FT CARBOHYD 509 509 N-linked (GlcNAc...) (Potential). FT DISULFID 103 103 Interchain (with light chain) (Probable). FT DISULFID 325 325 Interchain (with light chain) (Probable). SQ SEQUENCE 526 AA; 58337 MW; AE6261F11C7D9468 CRC64; MSQDTEVDMK DVELNELEPE KQPMNAADGA AAGEKNGLVK IKVAEDETEA GVKFTGLSKE ELLKVAGSPG WVRTRWALLL LFWLGWLGML AGAVVIIVRA PRCRELPVQR WWHKGALYRI GDLQAFVGRD AGGIAGLKSH LEYLSTLKVK GLVLGPIHKN QKDEINETDL KQINPTLGSQ EDFKDLLQSA KKKSIHIILD LTPNYQGQNA WFLPAQADIV ATKMKEALSS WLQDGVDGFQ FRDVGKLMNA PLYLAEWQNI TKNLSEDRLL IAGTESSDLQ QIVNILESTS DLLLTSSYLS NSTFTGERTE SLVTRFLNAT GSQWCSWSVS QAGLLADFIP DHLLRLYQLL LFTLPGTPVF SYGDELGLQG ALPGQPAKAP LMPWNESSIF HIPRPVSLNM TVKGQNEDPG SLLTQFRRLS DLRGKERSLL HGDFHALSSS PDLFSYIRHW DQNERYLVVL NFRDSGRSAR LGASNLPAGI SLPASAKLLL STDSARQSRE EDTSLKLENL SLNPYEGLLL QFPFVA // ID 4F2_RABIT Reviewed; 529 AA. AC Q7YQK3; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 2. DT 20-FEB-2007, entry version 21. DE 4F2 cell-surface antigen heavy chain (4F2hc). GN Name=SLC3A2; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT. RC TISSUE=Brain capillary; RX MEDLINE=22503151; PubMed=12614332; RX DOI=10.1046/j.1471-4159.2003.01622.x; RA Boado R.J., Li J.Y., Pardridge W.M.; RT "Site-directed mutagenesis of rabbit LAT1 at amino acids 219 and RT 234."; RL J. Neurochem. 84:1322-1331(2003). RN [2] RP MUTAGENESIS OF CYS-110 AND CYS-332. RX PubMed=16125134; DOI=10.1016/j.bbamem.2005.07.007; RA Boado R.J., Li J.Y., Chu C., Ogoshi F., Wise P., Pardridge W.M.; RT "Site-directed mutagenesis of cysteine residues of large neutral amino RT acid transporter LAT1."; RL Biochim. Biophys. Acta 1715:104-110(2005). CC -!- FUNCTION: Involved in sodium-independent, high-affinity transport CC of large neutral amino acids. Required for normal and neoplastic CC cell growth. CC -!- SUBUNIT: Disulfide-linked heterodimer of a glycosylated heavy CC chain and a nonglycosylated light chain (SLC7A5 or SLC7A8). CC Interacts with FAM57A. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type II membrane CC protein. Melanosome (By similarity). CC -!- SIMILARITY: Belongs to the SLC3A transporter family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF515773; AAP47190.1; ALT_INIT; mRNA. DR GO; GO:0016021; C:integral to membrane; IC:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0015827; P:tryptophan transport; IDA:UniProtKB. DR InterPro; IPR013780; Glyco_hydro_13_b. DR InterPro; IPR006047; Glyco_hydro_13_cat. DR InterPro; IPR013781; Glyco_hydro_cat. DR Gene3D; G3DSA:2.60.40.1180; Glyco_hydro_13_b; 1. DR Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1. DR Pfam; PF00128; Alpha-amylase; 1. KW Amino-acid transport; Glycoprotein; Membrane; Phosphorylation; KW Signal-anchor; Transmembrane; Transport. FT CHAIN 1 529 4F2 cell-surface antigen heavy chain. FT /FTId=PRO_0000252235. FT TOPO_DOM 1 84 Cytoplasmic (Potential). FT TRANSMEM 85 105 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 106 529 Extracellular (Potential). FT MOD_RES 2 2 Phosphoserine (By similarity). FT MOD_RES 5 5 Phosphothreonine (By similarity). FT CARBOHYD 325 325 N-linked (GlcNAc...) (Potential). FT DISULFID 110 110 Interchain (with light chain) (By FT similarity). FT DISULFID 332 332 Interchain (with light chain) (By FT similarity). FT MUTAGEN 110 110 C->S: No effect on phenylalanine FT transport. FT MUTAGEN 332 332 C->S: No effect on phenylalanine FT transport. SQ SEQUENCE 529 AA; 57795 MW; 9ACBEA22D818BF6E CRC64; MSQDTEVDMK EVELNELEPE KQPMNAASEA AVAMAVAGGA EKNGLVKIKV AEDEAEAAAK FTGLSKEELL KVAGSPGWVR TRWALLLLFW LGWIGMLAGA VVIIVRAPRC RELPVQRWWH KGALYRVGDL QAFQARDSGD LAGLKGHLDY LSTLKVKGLV LGPIHKNQED DVAGTNLQEI NPAVGSKEEF DSFLQSAKKK SIRVILDLTP NYLGQNSWFL PTQVDLVATK VKDALNFWLQ AGVDGFQVRD VGNLTNAALH LAEWRNITKS FSEDRLLIAG TESSDLHQIL SLLESTKDLL LTSSYLSASG VSGENMKFLV TQYLNATDSH WCSWSLSQAG LLTSFVPAQL LRLYQLLLFT LPGTPVFSYG DEIGLQAAAL PGEPAKAPVM LWDESSLPSA SVSANMTVKG QDEDSGSLLS LFRRLSDQRG KERSLLHGDF HALSTGSNLF SYVRHWDQNE RFLVVLNFGD ESLSARLGAS SLPAGASLPA RADLLLSTHP GREEGTSLAL EHLNLEPHEG LLLHFPYVA // ID 4F2_RAT Reviewed; 527 AA. AC Q794F9; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 25. DE 4F2 cell-surface antigen heavy chain (4F2hc). GN Name=Slc3a2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC STRAIN=Sprague-Dawley; TISSUE=Jejunal epithelium; RX MEDLINE=98149747; PubMed=9480885; RA Yao S.Y.M., Muzyka W.R., Elliott J.F., Cheeseman C.I., Young J.D.; RT "Cloning and functional expression of a cDNA from rat jejunal RT epithelium encoding a protein (4F2hc) with system y+L amino acid RT transport activity."; RL Biochem. J. 330:745-752(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT. RC TISSUE=Glial tumor; RX MEDLINE=98395066; PubMed=9726963; DOI=10.1074/jbc.273.37.23629; RA Kanai Y., Segawa H., Miyamoto K., Uchino H., Takeda E., Endou H.; RT "Expression cloning and characterization of a transporter for large RT neutral amino acids activated by the heavy chain of 4F2 antigen RT (CD98)."; RL J. Biol. Chem. 273:23629-23632(1998). 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: Involved in sodium-independent, high-affinity transport CC of large neutral amino acids. Required for normal and neoplastic CC cell growth. CC -!- SUBUNIT: Disulfide-linked heterodimer of a glycosylated heavy CC chain and a nonglycosylated light chain (SLC7A5 or SLC7A8). CC Interacts with FAM57A. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type II membrane CC protein. Melanosome (By similarity). CC -!- SIMILARITY: Belongs to the SLC3A transporter family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U59324; AAC53560.1; -; mRNA. DR EMBL; AB015433; BAA33036.1; -; mRNA. DR EMBL; BC061989; AAH61989.1; -; mRNA. DR UniGene; Rn.5801; -. DR IntAct; Q794F9; -. DR Ensembl; ENSRNOG00000018487; Rattus norvegicus. DR RGD; 3073; Slc3a2. DR GermOnline; ENSRNOG00000018487; Rattus norvegicus. DR GO; GO:0016021; C:integral to membrane; ISS:UniProtKB. DR GO; GO:0005515; F:protein binding; ISS:UniProtKB. DR GO; GO:0015827; P:tryptophan transport; ISS:UniProtKB. DR InterPro; IPR013780; Glyco_hydro_13_b. DR InterPro; IPR006047; Glyco_hydro_13_cat. DR InterPro; IPR013781; Glyco_hydro_cat. DR Pfam; PF00128; Alpha-amylase; 1. KW Amino-acid transport; Glycoprotein; Membrane; Phosphorylation; KW Signal-anchor; Transmembrane; Transport. FT CHAIN 1 527 4F2 cell-surface antigen heavy chain. FT /FTId=PRO_0000252236. FT TOPO_DOM 1 75 Cytoplasmic (Potential). FT TRANSMEM 76 98 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 99 527 Extracellular (Potential). FT MOD_RES 2 2 Phosphoserine (By similarity). FT MOD_RES 5 5 Phosphothreonine (By similarity). FT CARBOHYD 166 166 N-linked (GlcNAc...) (Potential). FT CARBOHYD 259 259 N-linked (GlcNAc...) (Potential). FT CARBOHYD 263 263 N-linked (GlcNAc...) (Potential). FT CARBOHYD 318 318 N-linked (GlcNAc...) (Potential). FT CARBOHYD 386 386 N-linked (GlcNAc...) (Potential). FT CARBOHYD 400 400 N-linked (GlcNAc...) (Potential). FT CARBOHYD 510 510 N-linked (GlcNAc...) (Potential). FT DISULFID 103 103 Interchain (with light chain) (By FT similarity). FT DISULFID 325 325 Interchain (with light chain) (By FT similarity). SQ SEQUENCE 527 AA; 58072 MW; CBA92D830893672B CRC64; MSQDTEVDMK DVELNELEPE KQPMNAADGA AAGEKNGLVK IKVAEDEAEA GVKFTGLSKE ELLKVAGSPG WVRTRWALLL LFWLGWLGML AGAVVIIVRA PRCRELPVQR WWHKGALYRI GDLQAFVGPE ARGIAGLKNH LEYLSTLKVK GLVLGPIHKN QKDEVNETDL KQIDPDLGSQ EDFKDLLQSA KKKSIHIILD LTPNYKGQNA WFLPPQADIV ATKMKEALSS WLQDGVDGFQ VRDVGKLANA SLYLAEWQNI TKNFSEDRLL IAGTASSDLQ QIVNILESTS DLLLTSSYLS QPVFTGEHAE LLVIKYLNAT GSRWCSWSVS QAGLLTSFIP AQFLRLYQLL LFTLPGTPVF SYGDELGLQA VALPGQPMEA PFMLWNESSN SQTSSPVSLN MTVKGQNEDP GSLLTQFRRL SDLRGKERSL LHGDFDALSS SSGLFSYVRH WDQNERYLVV LNFQDVGLSA RVGASNLPAG ISLPASANLL LSTDSTRLSR EEGTSLSLEN LSLNPYEGLL LQFPFVA // ID 4HBT_PSEUC Reviewed; 141 AA. AC P56653; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 1. DT 12-DEC-2006, entry version 33. DE 4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23). OS Pseudomonas sp. (strain CBS-3). OC Bacteria; Proteobacteria. OX NCBI_TaxID=72586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92304934; PubMed=1351742; DOI=10.1021/bi00139a024; RA Babbitt P.C., Kenyon G.L., Martin B.M., Charest H., Slyvestre M., RA Scholten J.D., Chang K.H., Liang P.H., Dunaway-Mariano D.; RT "Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid RT sequence identities among families of acyl:adenyl ligases, enoyl-CoA RT hydratases/isomerases, and acyl-CoA thioesterases."; RL Biochemistry 31:5594-5604(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=99057924; PubMed=9837940; DOI=10.1074/jbc.273.50.33572; RA Benning M.M., Wesenberg G., Liu R., Taylor K.L., Dunaway-Mariano D., RA Holden H.M.; RT "The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase RT from Pseudomonas sp. strain CBS-3."; RL J. Biol. Chem. 273:33572-33579(1998). CC -!- CATALYTIC ACTIVITY: 4-hydroxybenzoyl-CoA + H(2)O = 4- CC hydroxybenzoate + CoA. CC -!- PATHWAY: Xenobiotic degradation; 2,4-Dichlorobenzoate degradation. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase 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 PDB; 1BVQ; X-ray; A=1-141. DR PDB; 1LO7; X-ray; A=1-141. DR PDB; 1LO8; X-ray; A=1-141. DR PDB; 1LO9; X-ray; A=1-141. DR GO; GO:0018739; F:4-hydroxybenzoyl-CoA thioesterase activity; IEA:EC. DR InterPro; IPR008272; HB-CoA_thioesterase_AS. DR InterPro; IPR006683; Thioestr_supf. DR Pfam; PF03061; 4HBT; 1. DR PROSITE; PS01328; 4HBCOA_THIOESTERASE; 1. KW 3D-structure; Hydrolase. FT CHAIN 1 141 4-hydroxybenzoyl-CoA thioesterase. FT /FTId=PRO_0000087760. FT ACT_SITE 17 17 FT STRAND 4 10 FT HELIX 13 15 FT TURN 18 19 FT STRAND 20 22 FT TURN 24 24 FT HELIX 25 42 FT TURN 43 43 FT HELIX 47 53 FT TURN 54 54 FT STRAND 56 58 FT STRAND 61 68 FT TURN 74 75 FT STRAND 77 87 FT STRAND 92 101 FT TURN 103 104 FT STRAND 107 117 FT STRAND 119 123 FT TURN 124 125 FT STRAND 126 130 FT HELIX 134 139 SQ SEQUENCE 141 AA; 16105 MW; 410896EA5CC49F22 CRC64; MARSITMQQR IEFGDCDPAG IVWFPNYHRW LDAASRNYFI KCGLPPWRQT VVERGIVGTP IVSCNASFVC TASYDDVLTI ETCIKEWRRK SFVQRHSVSR TTPGGDVQLV MRADEIRVFA MNDGERLRAI EVPADYIELC S // ID 4HDB_CLOKL Reviewed; 371 AA. AC P38945; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 31-OCT-2006, entry version 27. DE NAD-dependent 4-hydroxybutyrate dehydrogenase (EC 1.1.1.61) (4HBD). GN Name=4hbD; OS Clostridium kluyveri. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1534; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 8527 / DSM 555 / IFO 12016 / NCIMB 10680; RX MEDLINE=96146540; PubMed=8550525; RA Soehling B., Gottschalk G.; RT "Molecular analysis of the anaerobic succinate degradation pathway in RT Clostridium kluyveri."; RL J. Bacteriol. 178:871-880(1996). CC -!- CATALYTIC ACTIVITY: 4-hydroxybutanoate + NAD(+) = succinate CC semialdehyde + NADH. CC -!- COFACTOR: Divalent cations. CC -!- SIMILARITY: Belongs to the iron-containing alcohol 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; L21902; AAA92348.1; -; Genomic_DNA. DR GO; GO:0047577; F:4-hydroxybutyrate dehydrogenase activity; IEA:EC. DR InterPro; IPR001670; Fe_ADH. DR Pfam; PF00465; Fe-ADH; 1. DR PROSITE; PS00913; ADH_IRON_1; FALSE_NEG. DR PROSITE; PS00060; ADH_IRON_2; 1. KW NAD; Oxidoreductase. FT CHAIN 1 371 NAD-dependent 4-hydroxybutyrate FT dehydrogenase. FT /FTId=PRO_0000087840. SQ SEQUENCE 371 AA; 41756 MW; 8D4A8DCD94E252C4 CRC64; MKLLKLAPDV YKFDTAEEFM KYFKVGKGDF ILTNEFLYKP FLEKFNDGAD AVFQEKYGLG EPSDEMINNI IKDIGDKQYN RIIAVGGGSV IDIAKILSLK YTDDSLDLFE GKVPLVKNKE LIIVPTTCGT GSEVTNVSVA ELKRRHTKKG IASDELYATY AVLVPEFIKG LPYKFFVTSS VDALIHATEA YVSPNANPYT DMFSVKAMEL ILNGYMQMVE KGNDYRVEII EDFVIGSNYA GIAFGNAGVG AVHALSYPIG GNYHVPHGEA NYLFFTEIFK TYYEKNPNGK IKDVNKLLAG ILKCDESEAY DSLSQLLDKL LSRKPLREYG MKEEEIETFA DSVIEGQQRL LVNNYEPFSR EDIVNTYKKL Y // ID 4OMT_COPJA Reviewed; 350 AA. AC Q9LEL5; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-JAN-2007, entry version 33. DE 3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase DE (EC 2.1.1.116) (S-adenosyl-L-methionine:3'-hydroxy-N-methylcoclaurine DE 4'-O-methyltransferase) (4'-OMT). OS Coptis japonica (Japanese goldthread). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Ranunculales; OC Ranunculaceae; Coptis. OX NCBI_TaxID=3442; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RX MEDLINE=20390108; PubMed=10811648; DOI=10.1074/jbc.M002439200; RA Morishige T., Tsujita T., Yamada Y., Sato F.; RT "Molecular characterization of the S-adenosyl-L-methionine: 3'- RT hydroxy-N-methylcoclaurine 4'O-methyltransferase involved in RT isoquinoline alkaloid biosynthesis in Coptis japonica."; RL J. Biol. Chem. 275:23398-23405(2000). CC -!- FUNCTION: Catalyzes the transfer of the methyl group to the 4'- CC hydroxyl group of 3'-hydroxy-N-methylcoclaurine to form CC reticuline. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 3'-hydroxy-N-methyl- CC (S)-coclaurine = S-adenosyl-L-homocysteine + (S)-reticuline. CC -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)- CC reticuline from (S)-norcoclaurine: step 4 [final step]. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D29812; BAB08005.1; -; mRNA. DR HSSP; P93324; 1FP1. DR GO; GO:0030784; F:3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-met...; IEA:EC. DR InterPro; IPR012967; Dimerisation. DR InterPro; IPR001077; O_Met_trans2. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF08100; Dimerisation; 1. DR Pfam; PF00891; Methyltransf_2; 1. KW Methyltransferase; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 350 3'-hydroxy-N-methyl-(S)-coclaurine 4'-O- FT methyltransferase. FT /FTId=PRO_0000204430. FT ACT_SITE 257 257 Proton acceptor (By similarity). FT BINDING 196 196 S-adenosyl-L-methionine; via carbonyl FT oxygen (By similarity). FT BINDING 219 219 S-adenosyl-L-methionine (By similarity). FT BINDING 239 239 S-adenosyl-L-methionine (By similarity). FT BINDING 240 240 S-adenosyl-L-methionine; via amide FT nitrogen (By similarity). FT BINDING 253 253 S-adenosyl-L-methionine (By similarity). SQ SEQUENCE 350 AA; 38776 MW; 547835EBCDEF9182 CRC64; MAFHGKDDVL DIKAQAHVWK IIYGFADSLV LRCAVELGIV DIIDNNNQPM ALADLASKLP VSDVNCDNLY RILRYLVKME ILRVEKSDDG QKKYALEPIA TLLSRNAKRS MVPMILGMTQ KDFMTPWHSM KDGLSDNGTA FEKAMGMTIW EYLEGHPDQS QLFNEGMAGE TRLLTSSLIS GSRDMFQGID SLVDVGGGNG TTVKAISDAF PHIKCTLFDL PHVIANSYDL PNIERIGGDM FKSVPSAQAI ILKLILHDWN DEDSIKILKQ CRNAVPKDGG KVIIVDVALD EESDHELSST RLILDIDMLV NTGGKERTKE VWEKIVKSAG FSGCKIRHIA AIQSVIEVFP // ID 4OT1_PSEPU Reviewed; 63 AA. AC Q01468; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 51. DE 4-oxalocrotonate tautomerase (EC 5.3.2.-) (4-OT). GN Name=xylH; OS Pseudomonas putida. OG Plasmid TOL pWW0. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-34. RC STRAIN=ATCC 33015 / mt-2 / JCM 6156; RX MEDLINE=92388122; PubMed=1339435; RA Chen L.H., Kenyon G.L., Curtin F., Harayama S., Bembenek M.E., RA Hajipour G., Whitman C.P.; RT "4-oxalocrotonate tautomerase, an enzyme composed of 62 amino acid RT residues per monomer."; RL J. Biol. Chem. 267:17716-17721(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33015 / mt-2 / JCM 6156; RX MEDLINE=93288011; PubMed=8510667; RA Harayama S., Rekik M.; RT "Comparison of the nucleotide sequences of the meta-cleavage pathway RT genes of TOL plasmid pWW0 from Pseudomonas putida with other meta- RT cleavage genes suggests that both single and multiple nucleotide RT substitutions contribute to enzyme evolution."; RL Mol. Gen. Genet. 239:81-89(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=22423065; PubMed=12534468; RX DOI=10.1046/j.1462-2920.2002.00305.x; RA Greated A., Lambertsen L., Williams P.A., Thomas C.M.; RT "Complete sequence of the IncP-9 TOL plasmid pWW0 from Pseudomonas RT putida."; RL Environ. Microbiol. 4:856-871(2002). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX MEDLINE=96146412; PubMed=8547259; DOI=10.1021/bi951732k; RA Subramanya H.S., Roper D.I., Dauter Z., Dodson E.J., Davies G.J., RA Wilson K.S., Wigley D.B.; RT "Enzymatic ketonization of 2-hydroxymuconate: specificity and RT mechanism investigated by the crystal structures of two isomerases."; RL Biochemistry 35:792-802(1996). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RC STRAIN=ATCC 33015 / mt-2 / JCM 6156; RX MEDLINE=98453316; PubMed=9778344; DOI=10.1021/bi981607j; RA Taylor A.B., Czerwinski R.M., Johnson W.H. Jr., Whitman C.P., RA Hackert M.L.; RT "Crystal structure of 4-oxalocrotonate tautomerase inactivated by 2- RT oxo-3-pentynoate at 2.4-A resolution: analysis and implications for RT the mechanism of inactivation and catalysis."; RL Biochemistry 37:14692-14700(1998). RN [6] RP STRUCTURE BY NMR, AND ACTIVE SITE. RX MEDLINE=96146413; PubMed=8547260; DOI=10.1021/bi951077g; RA Stivers J.T., Abeygunawardana C., Mildvan A.S., Hajipour G., RA Whitman C.P., Chen L.H.; RT "Catalytic role of the amino-terminal proline in 4-oxalocrotonate RT tautomerase: affinity labeling and heteronuclear NMR studies."; RL Biochemistry 35:803-813(1996). CC -!- FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate CC stereoselectively to yield 2-oxo-3-hexenedioate. CC -!- PATHWAY: Benzoate/toluates meta-cleavage pathway. CC -!- PATHWAY: Toluene/xylenes degradation. CC -!- SUBUNIT: Homohexamer. CC -!- SIMILARITY: Belongs to the tautomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M95650; AAA26046.1; -; Genomic_DNA. DR EMBL; M94186; AAA25694.1; -; Genomic_DNA. DR EMBL; AJ344068; CAC86799.1; -; Genomic_DNA. DR PIR; A43397; A43397. DR PDB; 1BJP; X-ray; A/B/C/D/E=1-63. DR PDB; 4OTA; X-ray; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q=1-63. DR PDB; 4OTB; X-ray; A/B/C/D/E/F/G/H/I/J/K/L=1-63. DR PDB; 4OTC; X-ray; A/B/C/D/E/F/G/H/I=1-63. DR InterPro; IPR004370; Taut. DR Pfam; PF01361; Tautomerase; 1. DR ProDom; PD404143; Taut; 1. DR TIGRFAMs; TIGR00013; taut; 1. KW 3D-structure; Aromatic hydrocarbons catabolism; KW Direct protein sequencing; Isomerase; Plasmid. FT INIT_MET 1 1 Removed. FT CHAIN 2 63 4-oxalocrotonate tautomerase. FT /FTId=PRO_0000209514. FT ACT_SITE 2 2 Proton acceptor; via imino nitrogen. FT STRAND 3 9 FT TURN 10 11 FT HELIX 14 32 FT TURN 33 33 FT HELIX 36 38 FT STRAND 40 46 FT TURN 48 49 FT STRAND 50 53 FT TURN 54 55 FT HELIX 58 61 SQ SEQUENCE 63 AA; 6942 MW; 23804AB94A126802 CRC64; MPIAQIHILE GRSDEQKETL IREVSEAISR SLDAPLTSVR VIITEMAKGH FGIGGELASK VRR // ID 4OT2_PSEPU Reviewed; 63 AA. AC Q8RQD2; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 23. DE 4-oxalocrotonate tautomerase (EC 5.3.2.-) (4-OT). GN Name=xylH; OS Pseudomonas putida. OG Plasmid TOL pDK1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=PaW630; RA Wessler H.G., Hares D.R., Poulter M.D., Voss J.A., Khedairy H.S., RA Baker R.F., Azadpour E.E., Luo X., Benjamin R.C.; RT "Sequence of the lower (meta-cleavage) xyl operon of the Pseudomonas RT putida TOL plasmid pDK1."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate CC stereoselectively to yield 2-oxo-3-hexenedioate. CC -!- PATHWAY: Benzoate/toluates meta-cleavage pathway. CC -!- PATHWAY: Toluene/xylenes degradation. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SIMILARITY: Belongs to the tautomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF134348; AAL83667.1; -; Genomic_DNA. DR HSSP; Q01468; 1BJP. DR SMR; Q8RQD2; 2-63. DR InterPro; IPR004370; Taut. DR Pfam; PF01361; Tautomerase; 1. DR ProDom; PD404143; Taut; 1. DR TIGRFAMs; TIGR00013; taut; 1. KW Aromatic hydrocarbons catabolism; Isomerase; Plasmid. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 63 4-oxalocrotonate tautomerase. FT /FTId=PRO_0000209515. FT ACT_SITE 2 2 Proton acceptor; via imino nitrogen (By FT similarity). SQ SEQUENCE 63 AA; 6969 MW; 23805E3F916B5802 CRC64; MPIAQIHILE GRNDEQKETL IREVSEAISR SLDAPLTSVR VIITEMAKGH FGIGGELASK VRR // ID 4OT3_PSEPU Reviewed; 63 AA. AC Q9Z431; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 31. DE 4-oxalocrotonate tautomerase (EC 5.3.2.-) (4-OT). GN Name=nahJ; OS Pseudomonas putida. OG Plasmid NAH7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 17485 / DSM 50208 / Stanier 111 / JCM 6158 / Biotype A; RX MEDLINE=99255564; PubMed=10322041; RA Grimm A.C., Harwood C.S.; RT "NahY, a catabolic plasmid-encoded receptor required for chemotaxis of RT Pseudomonas putida to the aromatic hydrocarbon naphthalene."; RL J. Bacteriol. 181:3310-3316(1999). CC -!- FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate CC stereoselectively to yield 2-oxo-3-hexenedioate. CC -!- PATHWAY: Salicylate meta-cleavage pathway. CC -!- PATHWAY: Naphthalene degradation. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SIMILARITY: Belongs to the tautomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF100302; AAD13221.1; -; Genomic_DNA. DR HSSP; P49172; 1OTF. DR SMR; Q9Z431; 2-60. DR InterPro; IPR004370; Taut. DR Pfam; PF01361; Tautomerase; 1. DR ProDom; PD404143; Taut; 1. DR TIGRFAMs; TIGR00013; taut; 1. KW Aromatic hydrocarbons catabolism; Isomerase; Plasmid. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 63 4-oxalocrotonate tautomerase. FT /FTId=PRO_0000209516. FT ACT_SITE 2 2 Proton acceptor; via imino nitrogen (By FT similarity). SQ SEQUENCE 63 AA; 7122 MW; 2EE96A4BA328B32F CRC64; MPIAQLYILE GRSDEQKETL IREVSEAMSR SLDAPIERVR VIITEMPKNH FGIGGEPASK LNR // ID 4OT4_PSEPU Reviewed; 63 AA. AC Q93JW0; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 24. DE 4-oxalocrotonate tautomerase (EC 5.3.2.-) (4-OT). GN Name=tdnL; OS Pseudomonas putida. OG Plasmid pTDN1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=UCC22; RA Fukumori F.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate CC stereoselectively to yield 2-oxo-3-hexenedioate. CC -!- PATHWAY: Meta-cleavage pathway. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SIMILARITY: Belongs to the tautomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D85415; BAB62059.1; -; Genomic_DNA. DR HSSP; P49172; 1OTF. DR InterPro; IPR004370; Taut. DR Pfam; PF01361; Tautomerase; 1. DR ProDom; PD404143; Taut; 1. DR TIGRFAMs; TIGR00013; taut; 1. KW Aromatic hydrocarbons catabolism; Isomerase; Plasmid. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 63 4-oxalocrotonate tautomerase. FT /FTId=PRO_0000209517. FT ACT_SITE 2 2 Proton acceptor; via imino nitrogen (By FT similarity). SQ SEQUENCE 63 AA; 6927 MW; 97ED473A49AED63B CRC64; MPFAQIYMIE GRTEAQKKAV IEKVSQALVE ATGAPMANVR VWIQEVPKEN WGIAGVSAKE LGR // ID 4OT_COMTE Reviewed; 63 AA. AC Q9RHM8; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 27. DE 4-oxalocrotonate tautomerase (EC 5.3.2.-) (4-OT). GN Name=aphI; OS Comamonas testosteroni (Pseudomonas testosteroni). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=285; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=TA441; RX MEDLINE=20340973; PubMed=10878134; RA Arai H., Ohishi T., Chang M.Y., Kudo T.; RT "Arrangement and regulation of the genes for meta-pathway enzymes RT required for degradation of phenol in Comamonas testosteroni TA441."; RL Microbiology 146:1707-1715(2000). CC -!- FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate CC stereoselectively to yield 2-oxo-3-hexenedioate. CC -!- PATHWAY: 2-hydroxymuconic semialdehyde meta-cleavage pathway. CC -!- PATHWAY: Phenol degradation. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SIMILARITY: Belongs to the tautomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB029044; BAA88507.1; -; Genomic_DNA. DR HSSP; Q01468; 1BJP. DR InterPro; IPR004370; Taut. DR Pfam; PF01361; Tautomerase; 1. DR ProDom; PD404143; Taut; 1. DR TIGRFAMs; TIGR00013; taut; 1. KW Aromatic hydrocarbons catabolism; Isomerase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 63 4-oxalocrotonate tautomerase. FT /FTId=PRO_0000209511. FT ACT_SITE 2 2 Proton acceptor; via imino nitrogen (By FT similarity). SQ SEQUENCE 63 AA; 6962 MW; 92AD4B0DAFA7799A CRC64; MPFAQIYMLE GRSEEQKKAV IEKVTRALVE AVGAPSANVR VWIHDVPKEN WGIAGVSAKE LGR // ID 4OT_PSEFL Reviewed; 63 AA. AC Q8KRR5; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 22. DE 4-oxalocrotonate tautomerase (EC 5.3.2.-) (4-OT). GN Name=nahJ; OS Pseudomonas fluorescens. OG Plasmid pLP6a. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=294; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LP6a; RA McFarlane D.M., Foght J.M.; RT "Nucleotide sequence from the lower pathway of naphthalene degradation RT in Pseudomonas fluorescens LP6a."; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate CC stereoselectively to yield 2-oxo-3-hexenedioate. CC -!- PATHWAY: Salicylate meta-cleavage pathway. CC -!- PATHWAY: Naphthalene degradation. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SIMILARITY: Belongs to the tautomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF525494; AAM88237.1; -; Genomic_DNA. DR HSSP; P49172; 1OTF. DR SMR; Q8KRR5; 2-60. DR InterPro; IPR004370; Taut. DR Pfam; PF01361; Tautomerase; 1. DR ProDom; PD404143; Taut; 1. DR TIGRFAMs; TIGR00013; taut; 1. KW Aromatic hydrocarbons catabolism; Isomerase; Plasmid. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 63 4-oxalocrotonate tautomerase. FT /FTId=PRO_0000209512. FT ACT_SITE 2 2 Proton acceptor; via imino nitrogen (By FT similarity). SQ SEQUENCE 63 AA; 7107 MW; 7FE5D126184975F4 CRC64; MPIAQLYILD GRSNEQKETL IREVSEAMSR SLDAPIERVR VIITEMPKNH FGIGGEPASK LNR // ID 4OT_PSEST Reviewed; 63 AA. AC Q9ZI54; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 30. DE 4-oxalocrotonate tautomerase (EC 5.3.2.-) (4-OT). GN Name=nahJ; OS Pseudomonas stutzeri (Pseudomonas perfectomarina). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=316; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=AN10; RX MEDLINE=20179685; PubMed=10713446; DOI=10.1016/S0378-1119(00)00038-X; RA Bosch R., Garcia-Valdes E., Moore E.R.B.; RT "Complete nucleotide sequence and evolutionary significance of a RT chromosomally encoded naphthalene-degradation lower pathway from RT Pseudomonas stutzeri AN10."; RL Gene 245:65-74(2000). CC -!- FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate CC stereoselectively to yield 2-oxo-3-hexenedioate. CC -!- PATHWAY: Salicylate meta-cleavage pathway. CC -!- PATHWAY: Naphthalene degradation. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SIMILARITY: Belongs to the tautomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF039534; AAD02155.1; -; Genomic_DNA. DR HSSP; Q01468; 1BJP. DR SMR; Q9ZI54; 2-63. DR InterPro; IPR004370; Taut. DR Pfam; PF01361; Tautomerase; 1. DR ProDom; PD404143; Taut; 1. DR TIGRFAMs; TIGR00013; taut; 1. KW Aromatic hydrocarbons catabolism; Isomerase; Plasmid. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 63 4-oxalocrotonate tautomerase. FT /FTId=PRO_0000209518. FT ACT_SITE 2 2 Proton acceptor; via imino nitrogen (By FT similarity). SQ SEQUENCE 63 AA; 6883 MW; 3FF05827BC926F87 CRC64; MPIAQIHILE GRSDEQKETL IREVSEAISR SLDAPLTSVR VIITEMPKVH FGIGGESAKA IGR // ID 4OT_PSEUF Reviewed; 63 AA. AC P49172; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 44. DE 4-oxalocrotonate tautomerase (EC 5.3.2.-) (4-OT). GN Name=dmpI; OS Pseudomonas sp. (strain CF600). OG Plasmid pVI150. OC Bacteria; Proteobacteria. OX NCBI_TaxID=79676; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92121108; PubMed=1732207; RA Shingler V., Marklund U., Powlowski J.; RT "Nucleotide sequence and functional analysis of the complete RT phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain RT CF600."; RL J. Bacteriol. 174:711-724(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX MEDLINE=96146412; PubMed=8547259; DOI=10.1021/bi951732k; RA Subramanya H.S., Roper D.I., Dauter Z., Dodson E.J., Davies G.J., RA Wilson K.S., Wigley D.B.; RT "Enzymatic ketonization of 2-hydroxymuconate: specificity and RT mechanism investigated by the crystal structures of two isomerases."; RL Biochemistry 35:792-802(1996). CC -!- FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate CC stereoselectively to yield 2-oxo-3-hexenedioate. CC -!- PATHWAY: Xenobiotic degradation; toluene and xylene degradation. CC -!- SUBUNIT: Homohexamer. CC -!- SIMILARITY: Belongs to the tautomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X60835; CAA43229.1; -; Genomic_DNA. DR PDB; 1OTF; X-ray; A/B/C/D/E/F=1-63. DR LinkHub; P49172; -. DR InterPro; IPR004370; Taut. DR Pfam; PF01361; Tautomerase; 1. DR ProDom; PD404143; Taut; 1. DR TIGRFAMs; TIGR00013; taut; 1. KW 3D-structure; Aromatic hydrocarbons catabolism; Isomerase; Plasmid. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 63 4-oxalocrotonate tautomerase. FT /FTId=PRO_0000209513. FT ACT_SITE 2 2 Proton acceptor; via imino nitrogen (By FT similarity). FT STRAND 3 10 FT HELIX 14 24 FT HELIX 27 30 FT HELIX 36 38 FT STRAND 40 46 FT HELIX 48 50 FT TURN 54 55 SQ SEQUENCE 63 AA; 7105 MW; CEBC26092D1E5342 CRC64; MPIAQLYIIE GRTDEQKETL IRQVSEAMAN SLDAPLERVR VLITEMPKNH FGIGGEPASK VRR // ID 53DR_BACSU Reviewed; 172 AA. AC P68522; O31895; O64153; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 31-OCT-2006, entry version 9. DE Putative SPBc2 prophage-derived 5'(3')-deoxyribonucleotidase DE (EC 3.1.3.-). GN Name=yorS; OrderedLocusNames=BSU20270; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z99114; CAB13919.1; -; Genomic_DNA. DR PIR; T12904; T12904. DR GenomeReviews; AL009126_GR; BSU20270. DR SubtiList; BG13703; yorS. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 172 Putative SPBc2 prophage-derived 5'(3')- FT deoxyribonucleotidase. FT /FTId=PRO_0000164373. SQ SEQUENCE 172 AA; 20417 MW; CA89B7BA30226EE8 CRC64; MKKVIAIDMD QVLADLLSDW VAYINTYDDP FLKEKDILCW DIKKYTNTNN NVYRHLDYDL FRNLNVIEGS QRVTKELMKK YEVYVVTTAT NHPDSLKAKL EWLTEYFPFI PHSNVVLCGN KNIIKADIMI DDGIHNLESF EGMKILFDAP HNRNENRFIR VMNWEEIERK LL // ID 53DR_BORBR Reviewed; 186 AA. AC Q7WQA0; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 31-OCT-2006, entry version 16. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=BB0433; OS Bordetella bronchiseptica (Alcaligenes bronchisepticus). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=518; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RB50 / ATCC BAA-588 / NCTC 13252; RX MEDLINE=22827954; PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640438; CAE30931.1; -; Genomic_DNA. DR GenomeReviews; BX470250_GR; BB0433. DR KEGG; bbr:BB0433; -. DR BioCyc; BBRO518:BB0433-MONOMER; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 186 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164375. SQ SEQUENCE 186 AA; 21692 MW; 04E00247D271C079 CRC64; MLILLDQDGV LADFEHAFID AWRKRHPDIE PVAFKDRKSF HIREDYAPEL RGLAEAIYTA PGFIRDLPPV PGAIEAFREL LALGMDVRIC SSPLMQFENC VAEKYLWVER HLGREATQRL ILTRDKTLVQ GDLLIDDRPV ITGAARPRWR HIIYDAPYNR DQTDRPRLDW RNWRNVLAGE LYRSDA // ID 53DR_BORPA Reviewed; 186 AA. AC Q7WC96; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 31-OCT-2006, entry version 16. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=BPP0431; OS Bordetella parapertussis. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=519; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253; RX MEDLINE=22827954; PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640424; CAE36015.1; -; Genomic_DNA. DR GenomeReviews; BX470249_GR; BPP0431. DR KEGG; bpa:BPP0431; -. DR BioCyc; BPAR519:BPP0431-MONOMER; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 186 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164376. SQ SEQUENCE 186 AA; 21752 MW; 2D217F09027537E2 CRC64; MLILLDQNGV LADFEHAFID AWRKRHPDIE PVAFEDRKSF HIREDYAPEL RGLAEAIYTA PGFIRDLPPV PGAIEAFREL LALGMDVRIC SSPLMQFENY VAEKYLWVER HLGREATQRL ILTRDKTLVQ GDLLIDDRPV ITGAARPRWR HIIYDAPYNR DQTDRPRLDW RNWRNVLAGE LYRSDA // ID 53DR_BORPE Reviewed; 186 AA. AC Q7W066; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 31-OCT-2006, entry version 15. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=BP0294; OS Bordetella pertussis. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=520; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251; RX MEDLINE=22827954; PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640411; CAE40672.1; -; Genomic_DNA. DR GenomeReviews; BX470248_GR; BP0294. DR KEGG; bpe:BP0294; -. DR BioCyc; BPER520:BP0294-MONOMER; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 186 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164377. SQ SEQUENCE 186 AA; 21679 MW; 9073B436FBD9FD28 CRC64; MLILLDQDGV LADFEHAFID AWRKRHPDIE PVAFEERKSF HIREDYAPEL RGLAEAIYTA PGFIRDLPPV PGAVEAFREL LALGMDVRIC SSPLMQFENC VAEKYLWVER HLGRDATQRL ILTRDKTLVQ GDLLIDDRPV ITGAARPRWR HIIYDAPYNR DQTDRPRLDW RNWRNVLAGE LYRSDA // ID 53DR_BPKV4 Reviewed; 170 AA. AC P59935; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2003, sequence version 1. DT 31-OCT-2006, entry version 13. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN Name=KVP40.0071; OS Bacteriophage KVP40. OC Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae; OC T4-like viruses. OX NCBI_TaxID=75320; OH NCBI_TaxID=662; Vibrio. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=22803260; PubMed=12923095; RX DOI=10.1128/JB.185.17.5220-5233.2003; RA Miller E., Heidelberg J., Eisen J., Nelson W., Durkin A., Ciecko A., RA Feldblyum T., White O., Paulsen I., Nierman W., Lee J., RA Szczypinski B., Fraser C.; RT "Complete genome sequence of the broad-host-range vibriophage KVP40: RT comparative genomics of a T4-related bacteriophage."; RL J. Bacteriol. 185:5220-5233(2003). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY283928; AAQ64142.1; -; Genomic_DNA. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Hydrolase; Hypothetical protein. FT CHAIN 1 170 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164388. SQ SEQUENCE 170 AA; 19766 MW; AA26FABD620DF1E1 CRC64; MKLMNVVKLM IRAIARAKKT DKPIVYIDMD NVLVDFQSGI DSLSIWEKNQ YEGRYDECPG IFAHMKPMKG AIAAFEVLNK HFDCYILSTA PWDNPGSWQD KRLWVERYLG KGAYKRLILS HHKQLNFGHY LIDDRTKNGA GEFMGEHIHF GTDEFPDWFS VVTYLTSENK // ID 53DR_BPSPC Reviewed; 172 AA. AC P68523; O31895; O64153; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 31-OCT-2006, entry version 9. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN Name=yorS; OS Bacteriophage SPBc2. OC Viruses; dsDNA viruses, no RNA stage; Caudovirales; Siphoviridae. OX NCBI_TaxID=66797; OH NCBI_TaxID=1423; Bacillus subtilis. RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=99303314; PubMed=10376821; RA Lazarevic V., Duesterhoeft A., Soldo B., Hilbert H., Mauel C., RA Karamata D.; RT "Nucleotide sequence of the Bacillus subtilis temperate bacteriophage RT SPbetac2."; RL Microbiology 145:1055-1067(1999). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF020713; AAC13113.1; -; Genomic_DNA. DR PIR; T12904; T12904. KW Hydrolase; Hypothetical protein. FT CHAIN 1 172 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164374. SQ SEQUENCE 172 AA; 20417 MW; CA89B7BA30226EE8 CRC64; MKKVIAIDMD QVLADLLSDW VAYINTYDDP FLKEKDILCW DIKKYTNTNN NVYRHLDYDL FRNLNVIEGS QRVTKELMKK YEVYVVTTAT NHPDSLKAKL EWLTEYFPFI PHSNVVLCGN KNIIKADIMI DDGIHNLESF EGMKILFDAP HNRNENRFIR VMNWEEIERK LL // ID 53DR_CHLTE Reviewed; 202 AA. AC Q8KD41; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 31-OCT-2006, entry version 16. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=CT1214; OS Chlorobium tepidum. OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=1097; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / TLS; RX MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., RA Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., RA Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., RA Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., RA Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., RA Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a RT photosynthetic, anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006470; AAM72446.1; -; Genomic_DNA. DR GenomeReviews; AE006470_GR; CT1214. DR KEGG; cte:CT1214; -. DR TIGR; CT1214; -. DR BioCyc; CTEP194439:CT1214-MONOMER; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 202 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164379. SQ SEQUENCE 202 AA; 23422 MW; 8AB18B5B9EA348D0 CRC64; MGTRWFAKNT TMSKNSIVIG VDLDGVCADF YGRMRQIASE WFERPIDELP EEVSWGLSEW GITNPSQYDS LHRFAVTQRE LFSSMEAIPG ARKYLRQLSD EGFRIRIITH RLFIHYFHAT AVQQTVNWLD SHGIPYWDLC FVKEKTQVGA DIYIEDSPEN VAQLRGRGLF TICFGNSTNR HIEELRAASW QDVYDMIKAF VT // ID 53DR_CLOAB Reviewed; 180 AA. AC Q97JQ5; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 31-OCT-2006, entry version 21. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=CA_C1218; OS Clostridium acetobutylicum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX MEDLINE=21359325; PubMed=11466286; RX DOI=10.1128/JB.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., RA Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., RA Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., RA Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001437; AAK79190.1; -; Genomic_DNA. DR PIR; C97050; C97050. DR GenomeReviews; AE001437_GR; CA_C1218. DR KEGG; cac:CAC1218; -. DR BioCyc; CACE1488:CAC1218-MONOMER; -. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 180 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164378. SQ SEQUENCE 180 AA; 21274 MW; 1AC58D7A55370CF8 CRC64; MNKPTLGIDL DTTLNTLDRE WVKRYNEIYK DKLLPSDIKG WDIENYVKPE CGKKIYDILK EPHFFRNLGV QPFAETALEE LTSIFNIYIV SATHYKVCED KGNWIKEKFP FISYQNIIFC HNKGLVHLDI LIDDNPLNLE NFKGNKILFD AHHNKSENRF VRARDWYEAK ALCESLKDFL // ID 53DR_MIMIV Reviewed; 221 AA. AC Q5UQH3; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 31-OCT-2006, entry version 11. DE Putative 5'(3')-deoxyribonucleotidase R824 (EC 3.1.3.-). GN OrderedLocusNames=MIMI_R824; OS Mimivirus. OC Viruses; dsDNA viruses, no RNA stage; Mimivirus. OX NCBI_TaxID=212035; OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rowbotham-Bradford; RX PubMed=15486256; DOI=10.1126/science.1101485; RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., RA La Scola B., Susan M., Claverie J.-M.; RT "The 1.2-megabase genome sequence of Mimivirus."; RL Science 306:1344-1350(2004). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- COFACTOR: Magnesium (By similarity). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY653733; AAV51084.1; -; Genomic_DNA. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; KW Nucleotide-binding. FT CHAIN 1 221 Putative 5'(3')-deoxyribonucleotidase FT R824. FT /FTId=PRO_0000253214. FT ACT_SITE 18 18 Nucleophile (By similarity). FT METAL 16 16 Magnesium (By similarity). FT METAL 18 18 Magnesium (via carbonyl oxygen) (By FT similarity). FT METAL 149 149 Magnesium (By similarity). FT BINDING 18 18 Phosphate (By similarity). FT BINDING 103 103 Phosphate (By similarity). FT BINDING 138 138 Phosphate (By similarity). SQ SEQUENCE 221 AA; 25469 MW; 2042E2A942C53F3D CRC64; MDNCELVGSR IRLGLDMDGV LFDFDSKIMD KFAEMGIQFT DVKEMSSAVE FDKSIKQRHR EIYHVPGFFA NLPPIKGAVN AYKYLKSLTD INNNKIFEIF IVSTPSFRNQ TCCIDKINDL NKYFGPELLE KVFFCRDKTL VNLDILIDDK PEIRGFNGSS ECLSDSNSVT NKMSFQHIRF HSDMYKYSDD VPIINNWIDG TYIDVVKNVC VDKNLLREVV V // ID 53DR_STAAC Reviewed; 180 AA. AC Q5HHU8; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 23-JAN-2007, entry version 12. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=SACOL0785; OS Staphylococcus aureus (strain COL). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=93062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000046; AAW37841.1; -; Genomic_DNA. DR GenomeReviews; CP000046_GR; SACOL0785. DR KEGG; sac:SACOL0785; -. DR TIGR; SACOL0785; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 180 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164380. SQ SEQUENCE 180 AA; 20987 MW; 11ED077D3C734330 CRC64; MTRKSIAIDM DEVLADTLGE IIDAVNFRAD LGIKMEALNG QKLKHVIPEH DGLITEVLRE PGFFRHLKVM PYAQEVVKKL TEHYDVYIAT AAMDVPTSFS DKYEWLLEFF PFLDPQHFVF CGRKNIVKAD YLIDDNPRQL EIFTGTPIMF TAVHNINDDR FERVNSWKDV EQYFLDNIEK // ID 53DR_STAAM Reviewed; 180 AA. AC P66840; Q99VP8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 23-JAN-2007, entry version 10. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=SAV0725; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., RA Ogasawara N., Hayashi H., Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus RT aureus."; RL Lancet 357:1225-1240(2001). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000017; BAB56887.1; -; Genomic_DNA. DR HSSP; Q9NPB1; 1MH9. DR GenomeReviews; BA000017_GR; SAV0725. DR KEGG; sav:SAV0725; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 180 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164381. SQ SEQUENCE 180 AA; 20961 MW; 0C5BC1A658221275 CRC64; MTRKSIAIDM DEVLADTLGE IIDAVNFRAD LGIKMEALNG QKLKHVIPEH DGLITEVLRE PGFFRHLKVM PHAQEVVKKL TEHYDVYIAT AAMDVPTSFS DKYEWLLEFF PFLDPQHFVF CGRKNIVKAD YLIDDNPRQL EIFTGTPIMF TAVHNINDDR FERVNSWKDV EQYFLDNIEK // ID 53DR_STAAN Reviewed; 180 AA. AC P66841; Q99VP8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 23-JAN-2007, entry version 10. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=SA0680; OS Staphylococcus aureus (strain N315). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=158879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., RA Ogasawara N., Hayashi H., Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus RT aureus."; RL Lancet 357:1225-1240(2001). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000018; BAB41913.1; -; Genomic_DNA. DR PIR; F89844; F89844. DR HSSP; Q9NPB1; 1MH9. DR GenomeReviews; BA000018_GR; SA0680. DR KEGG; sau:SA0680; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 180 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164382. SQ SEQUENCE 180 AA; 20961 MW; 0C5BC1A658221275 CRC64; MTRKSIAIDM DEVLADTLGE IIDAVNFRAD LGIKMEALNG QKLKHVIPEH DGLITEVLRE PGFFRHLKVM PHAQEVVKKL TEHYDVYIAT AAMDVPTSFS DKYEWLLEFF PFLDPQHFVF CGRKNIVKAD YLIDDNPRQL EIFTGTPIMF TAVHNINDDR FERVNSWKDV EQYFLDNIEK // ID 53DR_STAAR Reviewed; 180 AA. AC Q6GIR7; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 11. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=SAR0778; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571856; CAG39788.1; -; Genomic_DNA. DR GenomeReviews; BX571856_GR; SAR0778. DR KEGG; sar:SAR0778; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 180 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164383. SQ SEQUENCE 180 AA; 20961 MW; 0C5BC1A658221275 CRC64; MTRKSIAIDM DEVLADTLGE IIDAVNFRAD LGIKMEALNG QKLKHVIPEH DGLITEVLRE PGFFRHLKVM PHAQEVVKKL TEHYDVYIAT AAMDVPTSFS DKYEWLLEFF PFLDPQHFVF CGRKNIVKAD YLIDDNPRQL EIFTGTPIMF TAVHNINDDR FERVNSWKDV EQYFLDNIEK // ID 53DR_STAAS Reviewed; 180 AA. AC Q6GBA5; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 11. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=SAS0690; OS Staphylococcus aureus (strain MSSA476). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571857; CAG42466.1; -; Genomic_DNA. DR GenomeReviews; BX571857_GR; SAS0690. DR KEGG; sas:SAS0690; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 180 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164384. SQ SEQUENCE 180 AA; 20987 MW; 11ED077D3C734330 CRC64; MTRKSIAIDM DEVLADTLGE IIDAVNFRAD LGIKMEALNG QKLKHVIPEH DGLITEVLRE PGFFRHLKVM PYAQEVVKKL TEHYDVYIAT AAMDVPTSFS DKYEWLLEFF PFLDPQHFVF CGRKNIVKAD YLIDDNPRQL EIFTGTPIMF TAVHNINDDR FERVNSWKDV EQYFLDNIEK // ID 53DR_STAAW Reviewed; 180 AA. AC Q8NXN2; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 23-JAN-2007, entry version 17. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=MW0687; OS Staphylococcus aureus (strain MW2). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=196620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5; RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., RA Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., RA Yamamoto K., Hiramatsu K.; RT "Genome and virulence determinants of high virulence community- RT acquired MRSA."; RL Lancet 359:1819-1827(2002). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000033; BAB94552.1; -; Genomic_DNA. DR HSSP; Q9NPB1; 1MH9. DR GenomeReviews; BA000033_GR; MW0687. DR KEGG; sam:MW0687; -. DR BioCyc; SAUR196620:MW0687-MONOMER; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 180 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164385. SQ SEQUENCE 180 AA; 20987 MW; 11ED077D3C734330 CRC64; MTRKSIAIDM DEVLADTLGE IIDAVNFRAD LGIKMEALNG QKLKHVIPEH DGLITEVLRE PGFFRHLKVM PYAQEVVKKL TEHYDVYIAT AAMDVPTSFS DKYEWLLEFF PFLDPQHFVF CGRKNIVKAD YLIDDNPRQL EIFTGTPIMF TAVHNINDDR FERVNSWKDV EQYFLDNIEK // ID 53DR_STAEQ Reviewed; 179 AA. AC Q5HR07; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 23-JAN-2007, entry version 12. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=SERP0388; OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=176279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000029; AAW53769.1; -; Genomic_DNA. DR GenomeReviews; CP000029_GR; SERP0388. DR KEGG; ser:SERP0388; -. DR TIGR; SERP0388; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 179 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164387. SQ SEQUENCE 179 AA; 20944 MW; ED5BA6437DE442DD CRC64; MTRQRIAIDM DEVLADTLGA VVKAVNERAD LNIKMESLNG KKLKHMIPEH EGLVMDILKE PGFFRNLDVM PHAQEVVKQL NEHYDIYIAT AAMDVPTSFH DKYEWLLEYF PFLDPQHFVF CGRKNIILAD YLIDDNPKQL EIFEGKSIMF TASHNVNEHR FERVSGWRDV KNYFNSIEK // ID 53DR_STAES Reviewed; 179 AA. AC Q8CTG7; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 23-JAN-2007, entry version 20. DE Putative 5'(3')-deoxyribonucleotidase (EC 3.1.3.-). GN OrderedLocusNames=SE_0505; OS Staphylococcus epidermidis (strain ATCC 12228). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22832016; PubMed=12950922; RX DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., RA Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., RA Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides (Potential). CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015929; AAO04102.1; -; Genomic_DNA. DR GenomeReviews; AE015929_GR; SE_0505. DR KEGG; sep:SE0505; -. DR BioCyc; SEPI176280:SE0505-MONOMER; -. DR InterPro; IPR010708; NT5C. DR Pfam; PF06941; NT5C; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 179 Putative 5'(3')-deoxyribonucleotidase. FT /FTId=PRO_0000164386. SQ SEQUENCE 179 AA; 20993 MW; 9A5BA6437DE45A6A CRC64; MTRQRIAIDM DEVLADTLGA VVKAVNERAD LNIKMESLNG KKLKHMIPEH EGLVMDILKE PGFFRNLDVM PHAQEVVKQL NEHYDIYIAT AAMDVPTSFH DKYEWLLEYF PFLDPQHFVF CGRKNIILAD YLIDDNPKQL EIFEGKSIMF TASHNVYEHR FERVSGWRDV KNYFNSIEK // ID 5E5_RAT Reviewed; 825 AA. AC Q63003; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 29. DE 5E5 antigen. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Brain; RX MEDLINE=96015159; PubMed=8537300; RA Suzuki E., Kojima N., Yoshimura K., Uyemura K., Obata K., Akagawa K.; RT "Cloning and sequence analysis of cDNA for a possible DNA-binding RT protein 5E5 in the nervous system."; RL J. Biochem. 118:122-128(1995). CC -!- FUNCTION: Might have DNA-binding ability. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in neurons. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D37934; BAA07153.1; -; mRNA. DR PIR; JC4163; JC4163. DR UniGene; Rn.59887; -. DR Ensembl; ENSRNOG00000021048; Rattus norvegicus. DR InterPro; IPR000637; AT_hook_DNA_bd. DR PRINTS; PR00929; ATHOOK. KW DNA-binding; Nuclear protein. FT CHAIN 1 825 5E5 antigen. FT /FTId=PRO_0000064385. SQ SEQUENCE 825 AA; 86831 MW; AF667FE2FD555BDF CRC64; MFLEVADLKD GLWVWKVVFL QVCIEASGWG AEVRDSCGCG DSSSHQTDDP ATALALHVAC HSFKGQLVQQ TLLLGTRPRV WVNNIPQEGP SLPLRQWLLP QCPSLNRSGS AMGTGWGLSG LSPTALSRDG YETETPFSPE GAFPGGGPAE EEGVPRPRAP PEPPDPGAPR PPPDPGPLPL PGSQEKPTFV VQVSTEQLLM STGGCDKEPP RGQGVDTRGD RTQEGGEKPR EQREGPRPEQ GPDIPGQQEE SPQQEPSSER GDSVGEREAR SPGHEGEGGG EWPGISGERR ESPGEWGADV PRGRGEGAGE WGSDVPKDRG EGGREWGPEA AQEHGEAARD WTSESPRTLG EDARDWGSSS RDAAGSSPCA LRGSLAPERL GDGPWPAWPS PQEREPGPRD RVESPREWGG TESPRGWEAG PREWGPSPGG RGDGPRRRPR KRRGRKGRMG RQLETTATSA SATGGPAEEA GASAPEGQAG GGPRGRARGP RQQARRRHGP QRRRGPPQAG EEGPGDATLV LGLGTTSGEQ RADQSQTLPA LAGAPTAHAH AVPGPGPAAA TLGGRGRRGS WRGGRRGGGA GASGGGRGGR GRGRGGRRGS GLSGTREDAG SPSARRGEQR RRGHGPPAAG AAQVSTRGRR ARGQRTGEEA QDGLLPRGRD RLPLRPGDSN QRVERPGHPR GGHGAINAPS APDASPPHHP RRWVSQQRQR LWRQFRVGGG FPPPPPTRPP PVLLPLLRLT CAGDPGASRP GSRRPARRPR GELTPQRPSP FAPQEEGLRA ESCVDDGAIA PDTDTASGEV PEAGPSLSST MCQMGRPRPS PKSPR // ID 5EAS_TOBAC Reviewed; 548 AA. AC Q40577; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 31-OCT-2006, entry version 55. DE Aristolochene synthase (EC 4.2.3.9) (5-epi-aristolochene synthase) DE (EAS). OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 56-73. RC STRAIN=cv. NK326; RX MEDLINE=93066390; PubMed=1438319; RA Facchini P.J., Chappell J.; RT "Gene family for an elicitor-induced sesquiterpene cyclase in RT tobacco."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11088-11092(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND SEQUENCE REVISION. RX MEDLINE=97442533; PubMed=9295271; DOI=10.1126/science.277.5333.1815; RA Starks C.M., Back K., Chappell J., Noel J.P.; RT "Structural basis for cyclic terpene biosynthesis by tobacco 5-epi- RT aristolochene synthase."; RL Science 277:1815-1820(1997). CC -!- FUNCTION: Catalyzes the cyclization of trans,trans-farnesyl CC diphosphate (FPP) to the bicyclic intermediate 5-epi- CC aristolochene, initial step in the conversion of FPP to the CC sesquiterpenoid antifungal phytoalexin capsidiol. CC -!- CATALYTIC ACTIVITY: 2-trans,6-trans-farnesyl diphosphate = CC aristolochene + diphosphate. CC -!- CATALYTIC ACTIVITY: 2-trans,6-trans-farnesyl diphosphate = (+)- CC (10R)-germacrene A + diphosphate. CC -!- COFACTOR: Binds 3 magnesium ions per subunit. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: By fungal elicitor. CC -!- SIMILARITY: Belongs to the terpene synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L04680; AAA19216.1; -; Unassigned_RNA. DR PIR; T03714; T03714. DR PDB; 1HX9; X-ray; A=1-548. DR PDB; 1HXA; X-ray; A=1-548. DR PDB; 1HXC; X-ray; A=1-548. DR PDB; 1HXG; X-ray; A=1-548. DR PDB; 5EAS; X-ray; @=1-548. DR PDB; 5EAT; X-ray; @=1-548. DR PDB; 5EAU; X-ray; @=1-548. DR BioCyc; MetaCyc:EAS-MONOMER; -. DR LinkHub; Q40577; -. DR GO; GO:0045483; F:aristolochene synthase activity; IEA:EC. DR InterPro; IPR008930; Terp_cyc_toroid. DR InterPro; IPR001906; Terp_synth-like. DR InterPro; IPR008949; Terpenoid_synth. DR InterPro; IPR005630; Tps_metal_bd. DR Pfam; PF01397; Terpene_synth; 1. DR Pfam; PF03936; Terpene_synth_C; 1. KW 3D-structure; Direct protein sequencing; Lyase; Magnesium; KW Metal-binding. FT CHAIN 1 548 Aristolochene synthase. FT /FTId=PRO_0000186438. FT ACT_SITE 273 273 Proton acceptor. FT ACT_SITE 444 444 FT ACT_SITE 520 520 FT ACT_SITE 525 525 FT METAL 305 305 Magnesium 1. FT METAL 305 305 Magnesium 3. FT METAL 379 379 Magnesium 1. FT METAL 444 444 Magnesium 2. FT METAL 448 448 Magnesium 2. FT METAL 452 452 Magnesium 2. FT CONFLICT 42 42 Y -> YIY (in Ref. 1). FT CONFLICT 44 44 K -> Q (in Ref. 1). FT CONFLICT 55 55 N -> S (in Ref. 1). FT CONFLICT 62 62 M -> R (in Ref. 1). FT CONFLICT 73 73 T -> I (in Ref. 1). FT CONFLICT 89 89 D -> E (in Ref. 1). FT CONFLICT 388 388 T -> M (in Ref. 1). FT TURN 26 30 FT HELIX 36 57 FT TURN 58 58 FT TURN 60 61 FT HELIX 64 76 FT TURN 77 78 FT HELIX 80 82 FT HELIX 84 95 FT TURN 96 97 FT HELIX 104 116 FT TURN 117 118 FT HELIX 123 129 FT TURN 132 133 FT STRAND 134 136 FT HELIX 138 140 FT TURN 141 142 FT HELIX 144 154 FT TURN 155 156 FT TURN 159 160 FT HELIX 162 164 FT TURN 165 166 FT HELIX 167 178 FT HELIX 179 181 FT TURN 184 185 FT HELIX 186 195 FT TURN 199 200 FT HELIX 203 213 FT TURN 214 214 FT HELIX 215 217 FT TURN 219 220 FT HELIX 223 254 FT TURN 255 255 FT HELIX 256 259 FT TURN 261 262 FT HELIX 267 277 FT HELIX 281 283 FT HELIX 284 305 FT TURN 306 307 FT HELIX 310 322 FT HELIX 325 330 FT HELIX 333 354 FT TURN 355 357 FT HELIX 359 361 FT HELIX 362 385 FT TURN 386 386 FT HELIX 391 398 FT TURN 399 399 FT HELIX 400 402 FT HELIX 404 412 FT TURN 413 414 FT TURN 416 417 FT HELIX 420 427 FT TURN 428 428 FT HELIX 431 453 FT TURN 454 456 FT TURN 458 459 FT HELIX 461 469 FT TURN 470 470 FT HELIX 473 494 FT TURN 495 495 FT STRAND 496 498 FT HELIX 503 505 FT TURN 506 506 FT HELIX 507 519 FT TURN 520 520 FT HELIX 521 523 FT TURN 526 528 FT HELIX 530 542 FT TURN 543 543 SQ SEQUENCE 548 AA; 62974 MW; 9FE1C59CF1A68BF1 CRC64; MASAAVANYE EEIVRPVADF SPSLWGDQFL SFSIDNQVAE KYAKEIEALK EQTRNMLLAT GMKLADTLNL IDTIERLGIS YHFEKEIDDI LDQIYNQNSN CNDLCTSALQ FRLLRQHGFN ISPEIFSKFQ DENGKFKESL ASDVLGLLNL YEASHVRTHA DDILEDALAF STIHLESAAP HLKSPLREQV THALEQCLHK GVPRVETRFF ISSIYDKEQS KNNVLLRFAK LDFNLLQMLH KQELAQVSRW WKDLDFVTTL PYARDRVVEC YFWALGVYFE PQYSQARVML VKTISMISIV DDTFDAYGTV KELEAYTDAI QRWDINEIDR LPDYMKISYK AILDLYKDYE KELSSAGRSH IVCHAIERMK EVVRNYNVES TWFIEGYTPP VSEYLSNALA TTTYYYLATT SYLGMKSATE QDFEWLSKNP KILEASVIIC RVIDDTATYE VEKSRGQIAT GIECCMRDYG ISTKEAMAKF QNMAETAWKD INEGLLRPTP VSTEFLTPIL NLARIVEVTY IHNLDGYTHP EKVLKPHIIN LLVDSIKI // ID 5HT1A_CANFA Reviewed; 423 AA. AC Q6XXX9; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 06-FEB-2007, entry version 22. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A). GN Name=HTR1A; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15220384; DOI=10.1093/jhered/esh033; RA Kukekova A.V., Trut L.N., Oskina I.N., Kharlamova A.V., RA Shikhevich S.G., Kirkness E.F., Aguirre G.D., Acland G.M.; RT "A marker set for construction of a genetic map of the silver fox RT (Vulpes vulpes)."; RL J. Hered. 95:185-194(2004). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY204570; AAP12467.1; -; Genomic_DNA. DR UniGene; Cfa.23472; -. DR Ensembl; ENSCAFG00000007276; Canis familiaris. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane; Ubl conjugation. FT CHAIN 1 423 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000068901. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 62 1 (Potential). FT TOPO_DOM 63 73 Cytoplasmic (Potential). FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 178 4 (Potential). FT TOPO_DOM 179 191 Extracellular (Potential). FT TRANSMEM 192 217 5 (Potential). FT TOPO_DOM 218 345 Cytoplasmic (Potential). FT TRANSMEM 346 367 6 (Potential). FT TOPO_DOM 368 378 Extracellular (Potential). FT TRANSMEM 379 403 7 (Potential). FT TOPO_DOM 404 423 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. FT CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). SQ SEQUENCE 423 AA; 46356 MW; 0E397FD4AE673269 CRC64; MEGLSPRQGN NTTSSEGPFG TLGNATGISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKAERKGADA RSGVSPAPQP RKSVNGEPGG REWRQGPGSQ AGGPLCTNGA VRRGDDGAAL EVIEVHRVGS SKEHLPLPCE AGAIPCAPAS FEKKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIVRCKFC RRR // ID 5HT1A_FUGRU Reviewed; 423 AA. AC O42385; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 31-OCT-2006, entry version 41. DE 5-hydroxytryptamine 1A-alpha receptor (5-HT-1A-alpha) (Serotonin DE receptor 1A-alpha) (5-HT1A-alpha) (F1A). OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=97361762; PubMed=9218723; DOI=10.1016/S0378-1119(97)00064-4; RA Yamaguchi F., Brenner S.; RT "Molecular cloning of 5-hydroxytryptamine (5-HT) type 1 receptor genes RT from the Japanese puffer fish, Fugu rubripes."; RL Gene 191:219-223(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X95936; CAA65175.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR Ensembl; SINFRUG00000145569; Fugu rubripes. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 423 5-hydroxytryptamine 1A-alpha receptor. FT /FTId=PRO_0000068909. FT TOPO_DOM 1 45 Extracellular (Potential). FT TRANSMEM 46 71 1 (Potential). FT TOPO_DOM 72 82 Cytoplasmic (Potential). FT TRANSMEM 83 107 2 (Potential). FT TOPO_DOM 108 118 Extracellular (Potential). FT TRANSMEM 119 141 3 (Potential). FT TOPO_DOM 142 161 Cytoplasmic (Potential). FT TRANSMEM 162 186 4 (Potential). FT TOPO_DOM 187 200 Extracellular (Potential). FT TRANSMEM 201 226 5 (Potential). FT TOPO_DOM 227 346 Cytoplasmic (Potential). FT TRANSMEM 347 368 6 (Potential). FT TOPO_DOM 369 379 Extracellular (Potential). FT TRANSMEM 380 404 7 (Potential). FT TOPO_DOM 405 423 Cytoplasmic (Potential). FT CARBOHYD 9 9 N-linked (GlcNAc...) (Potential). FT CARBOHYD 12 12 N-linked (GlcNAc...) (Potential). FT CARBOHYD 30 30 N-linked (GlcNAc...) (Potential). FT DISULFID 118 196 By similarity. SQ SEQUENCE 423 AA; 47001 MW; 7B1308626B40190F CRC64; MDLRATSSND SNATSGYSDT AAVDWDEGEN ATGSGSLPDP ELSYQIITSL FLGALILCSI FGNSCVVAAI ALERSLQNVA NYLIGSLAVT DLMVSVLVLP MAALYQVLNK WTLGQDICDL FIALDVLCCT SSILHLCAIA LDRYWAITDP IDYVNKRTPR RAAVLISVTW LIGFSISIPP MLGWRSAEDR ANPDACIISQ DPGYTIYSTF GAFYIPLILM LVLYGRIFKA ARFRIRKTVK KTEKAKASDM CLTLSPAVFH KRANGDAVSA EWKRGYKFKP SSPCANGAVR HGEEMESLEI IEVNSNSKTH LPLPNTPQSS SHENINEKTT GTRRKIALAR ERKTVKTLGI IMGTFIFCWL PFFIVALVLP FCAENCYMPE WLGAVINWLG YSNSLLNPII YAYFNKDFQS AFKKILRCKF HRH // ID 5HT1A_GORGO Reviewed; 422 AA. AC Q9N297; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 06-FEB-2007, entry version 31. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A). GN Name=HTR1A; OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041405; BAA94490.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane; Ubl conjugation. FT CHAIN 1 422 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000068902. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 62 1 (Potential). FT TOPO_DOM 63 73 Cytoplasmic (Potential). FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 178 4 (Potential). FT TOPO_DOM 179 191 Extracellular (Potential). FT TRANSMEM 192 217 5 (Potential). FT TOPO_DOM 218 345 Cytoplasmic (Potential). FT TRANSMEM 346 367 6 (Potential). FT TOPO_DOM 368 378 Extracellular (Potential). FT TRANSMEM 379 403 7 (Potential). FT TOPO_DOM 404 422 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. FT CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). SQ SEQUENCE 422 AA; 46155 MW; 012335E0403F1B90 CRC64; MDVLSPGQGN NTTSPPAPFE TGGNTTGISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKTGADT RHGASPAPQP KKSVNGESGS RNWRLGVESK AGGALCANGA VRQGDDGAAL EVIEVHRVGN SKEHLPLPSE AGPTPCAPAS FERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC RQ // ID 5HT1A_HORSE Reviewed; 422 AA. AC Q0EAB6; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 06-FEB-2007, entry version 4. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A). GN Name=HTR1A; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Momozawa Y., Takeuchi Y., Mori Y.; RT "Equus caballus 5-hydroxytryptamine (serotonin) receptor 1A (HTR1A), RT mRNA."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB264325; BAF32952.1; -; mRNA. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane; Ubl conjugation. FT CHAIN 1 422 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000271442. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 62 1 (Potential). FT TOPO_DOM 63 73 Cytoplasmic (Potential). FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 178 4 (Potential). FT TOPO_DOM 179 191 Extracellular (Potential). FT TRANSMEM 192 217 5 (Potential). FT TOPO_DOM 218 345 Cytoplasmic (Potential). FT TRANSMEM 346 367 6 (Potential). FT TOPO_DOM 368 378 Extracellular (Potential). FT TRANSMEM 379 403 7 (Potential). FT TOPO_DOM 404 422 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. FT CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). SQ SEQUENCE 422 AA; 46339 MW; 5429727F7B32C6F8 CRC64; MDVLGPGQGN NTTSSEGPFG TRANATGISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLVGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKKGADS RLGASPAPQR KKSANGELGS REWRQGVENK AGGVLCANGA VRQGDDGAAL EVIEVHRMGN SKEHLPLPSE AGAIPCAPAF FEKKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKILKCKFC RR // ID 5HT1A_HUMAN Reviewed; 422 AA. AC P08908; Q6LAE7; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 3. DT 20-FEB-2007, entry version 77. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A) (G-21). GN Name=HTR1A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87315369; PubMed=3041227; DOI=10.1038/329075a0; RA Kobilka B.K., Frielle T., Collins S., Yang-Feng T.L., Kobilka T.S., RA Francke U., Lefkowitz R.J., Caron M.G.; RT "An intronless gene encoding a potential member of the family of RT receptors coupled to guanine nucleotide regulatory proteins."; RL Nature 329:75-79(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Saltzman A.G., Morse B., Felder S.; RL Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. 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 OF 1-9. RX MEDLINE=92115564; PubMed=1766875; DOI=10.1093/nar/19.25.7155; RA Parks C.L., Chang L.S., Shenk T.; RT "A polymerase chain reaction mediated by a single primer: cloning of RT genomic sequences adjacent to a serotonin receptor protein coding RT region."; RL Nucleic Acids Res. 19:7155-7160(1991). RN [7] RP NUCLEOTIDE SEQUENCE OF 200-365. RX MEDLINE=93329096; PubMed=8393041; RA Aune T.M., McGrath K.M., Sarr T., Bombara M.P., Kelley K.A.; RT "Expression of 5HT1a receptors on activated human T cells. Regulation RT of cyclic AMP levels and T cell proliferation by 5- RT hydroxytryptamine."; RL J. Immunol. 151:1175-1183(1993). RN [8] RP FUNCTION. RX MEDLINE=88334700; PubMed=3138543; DOI=10.1038/335358a0; RA Fargin A., Raymond J.R., Lohse M.L., Kobilka B.K., Caron M.G., RA Lefkowitz R.J.; RT "The genomic clone G-21 which resembles a beta-adrenergic receptor RT sequence encodes the 5-HT1A receptor."; RL Nature 335:358-360(1988). RN [9] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-334, AND MASS RP SPECTROMETRY. RX PubMed=17203973; DOI=10.1021/pr060438j; RA Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., RA Haines D.S., Figeys D.; RT "The proteomic reactor facilitates the analysis of affinity-purified RT proteins by mass spectrometry: application for identifying RT ubiquitinated proteins in human cells."; RL J. Proteome Res. 6:298-305(2007). RN [10] RP VARIANTS SER-22 AND VAL-28. RX MEDLINE=95275307; PubMed=7755630; RA Nakhai B., Nielsen D.A., Linnoila M., Goldman D.; RT "Two naturally occurring amino acid substitutions in the human 5-HT1A RT receptor: glycine 22 to serine 22 and isoleucine 28 to valine 28."; RL Biochem. Biophys. Res. Commun. 210:530-536(1995). RN [11] RP VARIANTS LEU-16 AND ASP-273. RX MEDLINE=98425601; PubMed=9754630; RX DOI=10.1002/(SICI)1096-8628(19980907)81:5<434::AID-AJMG13>3.0.CO;2-D; RA Kawanishi Y., Harada S., Tachikawa H., Okubo T., Shiraishi H.; RT "Novel mutations in the promoter and coding region of the human 5-HT1A RT receptor gene and association analysis in schizophrenia."; RL Am. J. Med. Genet. 81:434-439(1998). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M28269; AAA36440.1; -; Genomic_DNA. DR EMBL; X13556; CAA31908.1; -; Genomic_DNA. DR EMBL; X57829; CAA40962.1; -; Genomic_DNA. DR EMBL; M83181; AAA66493.1; -; Genomic_DNA. DR EMBL; AB041403; BAA94488.1; -; Genomic_DNA. DR EMBL; BC069159; AAH69159.1; -; mRNA. DR EMBL; AF498978; AAM21125.1; -; mRNA. DR EMBL; Z11168; CAA77560.1; -; Genomic_DNA. DR PIR; I38209; I38209. DR UniGene; Hs.247940; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000178394; Homo sapiens. DR KEGG; hsa:3350; -. DR HGNC; HGNC:5286; HTR1A. DR MIM; 109760; gene. DR DrugBank; APRD00638; Aripiprazole. DR DrugBank; APRD00222; Buspirone. DR DrugBank; APRD00945; Eletriptan. DR DrugBank; APRD00711; Ergoloid mesylate. DR DrugBank; APRD00096; Tegaserod. DR DrugBank; APRD00540; Ziprasidone. DR ArrayExpress; P08908; -. DR GermOnline; ENSG00000178394; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004993; F:serotonin receptor activity; TAS:ProtInc. DR GO; GO:0007610; P:behavior; TAS:ProtInc. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS:ProtInc. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism; KW Receptor; Transducer; Transmembrane; Ubl conjugation. FT CHAIN 1 422 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000068903. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 62 1 (Potential). FT TOPO_DOM 63 73 Cytoplasmic (Potential). FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 178 4 (Potential). FT TOPO_DOM 179 191 Extracellular (Potential). FT TRANSMEM 192 217 5 (Potential). FT TOPO_DOM 218 345 Cytoplasmic (Potential). FT TRANSMEM 346 367 6 (Potential). FT TOPO_DOM 368 378 Extracellular (Potential). FT TRANSMEM 379 403 7 (Potential). FT TOPO_DOM 404 422 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. FT CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VARIANT 16 16 P -> L (in dbSNP:rs1800041). FT /FTId=VAR_003446. FT VARIANT 22 22 G -> S (in dbSNP:rs1799920). FT /FTId=VAR_011826. FT VARIANT 28 28 I -> V (in dbSNP:rs1799921). FT /FTId=VAR_011827. FT VARIANT 184 184 P -> L (in dbSNP:rs1800043). FT /FTId=VAR_011828. FT VARIANT 220 220 R -> L (in dbSNP:rs1800044). FT /FTId=VAR_011829. FT VARIANT 273 273 G -> D (in dbSNP:rs1800042). FT /FTId=VAR_011830. FT CONFLICT 152 154 RAA -> PR (in Ref. 1). FT CONFLICT 172 172 M -> I (in Ref. 1). FT CONFLICT 200 202 TFG -> RPR (in Ref. 7). FT CONFLICT 228 228 K -> R (in Ref. 7). FT CONFLICT 244 244 A -> AA (in Ref. 7). FT CONFLICT 355 355 I -> T (in Ref. 7). FT CONFLICT 363 365 IVA -> MRP (in Ref. 7). FT CONFLICT 418 418 K -> N (in Ref. 1). SQ SEQUENCE 422 AA; 46107 MW; 762664FCF62CFD8F CRC64; MDVLSPGQGN NTTSPPAPFE TGGNTTGISD VTVSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKTGADT RHGASPAPQP KKSVNGESGS RNWRLGVESK AGGALCANGA VRQGDDGAAL EVIEVHRVGN SKEHLPLPSE AGPTPCAPAS FERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC RQ // ID 5HT1A_MOUSE Reviewed; 421 AA. AC Q64264; Q60956; Q61617; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-FEB-2007, entry version 62. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A). GN Name=Htr1a; Synonyms=Gpcr18; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=NIH Swiss; TISSUE=Brain; RX MEDLINE=94076019; PubMed=8254366; RA Charest A., Wainer B.H., Albert P.R.; RT "Cloning and differentiation-induced expression of a murine serotonin RT 1A receptor in a septal cell line."; RL J. Neurosci. 13:5164-5171(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23. RC STRAIN=C3H/An; RX MEDLINE=96224025; PubMed=8626793; DOI=10.1074/jbc.271.8.4417; RA Parks C.L., Shenk T.; RT "The serotonin 1a receptor gene contains a TATA-less promoter that RT responds to MAZ and Sp1."; RL J. Biol. Chem. 271:4417-4430(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 136-353. RC TISSUE=Testis; RX MEDLINE=94116980; PubMed=8288218; RA Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I., RA Copeland N.G., Jenkins N.A.; RT "Identification, chromosomal location, and genome organization of RT mammalian G-protein-coupled receptors."; RL Genomics 18:175-184(1993). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Most abundantly expressed in midbrain and CC cortex. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U39391; AAA81519.1; -; mRNA. DR EMBL; U33820; AAC52572.1; -; Genomic_DNA. DR EMBL; L20339; AAA16850.1; -; mRNA. DR PIR; I49375; I49375. DR UniGene; Mm.4716; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSMUSG00000021721; Mus musculus. DR KEGG; mmu:15550; -. DR MGI; MGI:96273; Htr1a. DR ArrayExpress; Q64264; -. DR GermOnline; ENSMUSG00000021721; Mus musculus. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane; Ubl conjugation. FT CHAIN 1 421 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000068904. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 62 1 (Potential). FT TOPO_DOM 63 73 Cytoplasmic (Potential). FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 178 4 (Potential). FT TOPO_DOM 179 191 Extracellular (Potential). FT TRANSMEM 192 217 5 (Potential). FT TOPO_DOM 218 345 Cytoplasmic (Potential). FT TRANSMEM 346 367 6 (Potential). FT TOPO_DOM 368 378 Extracellular (Potential). FT TRANSMEM 379 403 7 (Potential). FT TOPO_DOM 404 421 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 30 30 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. FT CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VARIANT 17 19 EPF -> DHL (in strain: C3H/An). FT CONFLICT 177 177 A -> T (in Ref. 3). FT CONFLICT 242 242 F -> L (in Ref. 3). FT CONFLICT 247 247 A -> V (in Ref. 3). FT CONFLICT 263 263 C -> W (in Ref. 3). FT CONFLICT 304 304 D -> H (in Ref. 3). SQ SEQUENCE 421 AA; 46124 MW; CD8519D37A1F499B CRC64; MDMFSLGQGN NTTTSLEPFG TGGNDTGLSN VTFSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRAPED RSNPNECTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKKGAGT SFGTSSAPPP KKSLNGQPGS GDCRRSAENR AVGTPCANGA VRQGEDDATL EVIEVHRVGN SKGDLPLPSE SGATSYVPAC LERKNERTAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPEL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC R // ID 5HT1A_PANTR Reviewed; 422 AA. AC Q9N298; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 06-FEB-2007, entry version 38. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A). GN Name=HTR1A; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041404; BAA94489.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR KEGG; ptr:471533; -. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane; Ubl conjugation. FT CHAIN 1 422 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000068905. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 62 1 (Potential). FT TOPO_DOM 63 73 Cytoplasmic (Potential). FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 178 4 (Potential). FT TOPO_DOM 179 191 Extracellular (Potential). FT TRANSMEM 192 217 5 (Potential). FT TOPO_DOM 218 345 Cytoplasmic (Potential). FT TRANSMEM 346 367 6 (Potential). FT TOPO_DOM 368 378 Extracellular (Potential). FT TRANSMEM 379 403 7 (Potential). FT TOPO_DOM 404 422 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. FT CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). SQ SEQUENCE 422 AA; 46172 MW; FCD989BD0313A1A0 CRC64; MDVLSPGQGN NTTSPPAPFE TGGNTSGISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKTGADT RHGASPAQQP KKSVNGESGS RNWRLGVESK AGGALCANGA VRQGDDGAAL EVIEVHRVGN SKEHLPLPSE AGPTPCAPAS FERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC RQ // ID 5HT1A_PONPY Reviewed; 422 AA. AC Q9N296; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 06-FEB-2007, entry version 33. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A). GN Name=HTR1A; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Isolate oran-Po13; RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041406; BAA94491.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane; Ubl conjugation. FT CHAIN 1 422 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000068906. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 62 1 (Potential). FT TOPO_DOM 63 73 Cytoplasmic (Potential). FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 178 4 (Potential). FT TOPO_DOM 179 191 Extracellular (Potential). FT TRANSMEM 192 217 5 (Potential). FT TOPO_DOM 218 345 Cytoplasmic (Potential). FT TRANSMEM 346 367 6 (Potential). FT TOPO_DOM 368 378 Extracellular (Potential). FT TRANSMEM 379 403 7 (Potential). FT TOPO_DOM 404 422 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. FT CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). SQ SEQUENCE 422 AA; 46122 MW; C2CCC9803E8F8F9B CRC64; MDVLSPGQGN NTTSPPAPFE TGGNTTGISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKTGADT HHGASPAPQP KKSVNGESGS RNWRLGVESK AGGGLCANGA VRQGDDGAAL EVIEVHRVGN SKEHLPLPSE AGPTPCAPAS FERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC RQ // ID 5HT1A_RAT Reviewed; 422 AA. AC P19327; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 20-FEB-2007, entry version 59. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A). GN Name=Htr1a; Synonyms=5ht1a; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=90202832; PubMed=2156831; RA Albert P.R., Zhou Q.-Y., van Tol H.H.M., Bunzow J.R., Civelli O.; RT "Cloning, functional expression, and mRNA tissue distribution of the RT rat 5-hydroxytryptamine1A receptor gene."; RL J. Biol. Chem. 265:5825-5832(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=90355775; PubMed=2167416; DOI=10.1016/0024-3205(90)90225-G; RA Fujiwara Y., Nelson D.L., Kashihara K., Varga E., Roeske W.R., RA Yamamura H.I.; RT "Role of cytochrome P450 in the control of the production of RT erythropoietin."; RL Life Sci. 47:127-132(1990). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J05276; AAA40612.1; -; Genomic_DNA. DR PIR; JH0315; JH0315. DR UniGene; Rn.44486; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSRNOG00000010254; Rattus norvegicus. DR KEGG; rno:24473; -. DR RGD; 2845; Htr1a. DR ArrayExpress; P19327; -. DR GermOnline; ENSRNOG00000010254; Rattus norvegicus. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane; Ubl conjugation. FT CHAIN 1 422 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000068907. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 62 1 (Potential). FT TOPO_DOM 63 73 Cytoplasmic (Potential). FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 178 4 (Potential). FT TOPO_DOM 179 191 Extracellular (Potential). FT TRANSMEM 192 217 5 (Potential). FT TOPO_DOM 218 345 Cytoplasmic (Potential). FT TRANSMEM 346 367 6 (Potential). FT TOPO_DOM 368 378 Extracellular (Potential). FT TRANSMEM 379 403 7 (Potential). FT TOPO_DOM 404 422 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. FT CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT CONFLICT 373 373 S -> N (in Ref. 2). SQ SEQUENCE 422 AA; 46429 MW; 19C2731834C4BBC9 CRC64; MDVFSFGQGN NTTASQEPFG TGGNVTSISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV RKVEKKGAGT SLGTSSAPPP KKSLNGQPGS GDWRRCAENR AVGTPCTNGA VRQGDDEATL EVIEVHRVGN SKEHLPLPSE SGSNSYAPAC LERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPAL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC RR // ID 5HT1A_VULVU Reviewed; 423 AA. AC Q6XXY0; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 06-FEB-2007, entry version 21. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A). GN Name=HTR1A; OS Vulpes vulpes (Red fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Vulpes. OX NCBI_TaxID=9627; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Silver; RX PubMed=15220384; DOI=10.1093/jhered/esh033; RA Kukekova A.V., Trut L.N., Oskina I.N., Kharlamova A.V., RA Shikhevich S.G., Kirkness E.F., Aguirre G.D., Acland G.M.; RT "A marker set for construction of a genetic map of the silver fox RT (Vulpes vulpes)."; RL J. Hered. 95:185-194(2004). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY204569; AAP12466.1; -; Genomic_DNA. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane; Ubl conjugation. FT CHAIN 1 423 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000068908. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 62 1 (Potential). FT TOPO_DOM 63 73 Cytoplasmic (Potential). FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 178 4 (Potential). FT TOPO_DOM 179 191 Extracellular (Potential). FT TRANSMEM 192 217 5 (Potential). FT TOPO_DOM 218 345 Cytoplasmic (Potential). FT TRANSMEM 346 367 6 (Potential). FT TOPO_DOM 368 378 Extracellular (Potential). FT TRANSMEM 379 403 7 (Potential). FT TOPO_DOM 404 423 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. FT CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). SQ SEQUENCE 423 AA; 46284 MW; FBA56507BD8CF0FF CRC64; MEGLSPGQGN NTTSSEGPFG TRGNATGISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKAERKGADA RSGVSPAPQP RKSVNGEPGG REWRQGPGSK AGGPLCTNGA VRRGDDGAAL EVIEVHRVGS SKEHLPLPSE AGAIPCAPAS FEKKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIVRCKFC RRR // ID 5HT1A_XENLA Reviewed; 408 AA. AC Q98998; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-FEB-2007, entry version 41. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A) (X5-HT1A). GN Name=htr1a; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX MEDLINE=97364954; PubMed=9221903; DOI=10.1016/S0169-328X(97)00052-1; RA Marracci S., Cini D., Nardi I.; RT "Cloning and developmental expression of 5-HT1A receptor gene in RT Xenopus laevis."; RL Brain Res. Mol. Brain Res. 47:67-77(1997). RN [2] RP FUNCTION. RX PubMed=9878840; DOI=10.1016/S0169-328X(98)00305-2; RA Cappellini C., Malatesta P., Costa B., Marracci S., Nardi I., RA Martini C.; RT "Characterization of a cloned Xenopus laevis serotonin 5-HT1A receptor RT expressed in the NIH-3T3 cell line."; RL Brain Res. Mol. Brain Res. 63:380-383(1999). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. Activation of the receptor may play a role in CC the exit from G0 phase and in promoting DNA synthesis. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: First expressed in the rostral part of the CC brain stem at stage 22. At later stages of development, expression CC is localized to serotonergic neurons. The expression pattern CC changes in the tadpole of stage 41 where, in addition to CC serotonergic neurons, expression is also localized to the inner CC nuclear layer (INL) of the developing retina. This expression CC pattern continues through to the start of metamorphosis (stage CC 46). In adults, expressed in the brain, in particular the CC telencephalon, diencephalon and mesencephalon. In the CC telencephalic region, expression is localized to the lateral, CC dorsal and medial pallium, and in the striatum, septum and CC amygdala. In the mesencephalic region, expression is strongest in CC the optic tectum and torus semicircularis with moderate levels of CC expression in tegmental nuclei. In diencephalon, localized to the CC dorsal and ventral thalamus and the preoptic area of the CC hypothalamus. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y07901; CAA69208.1; -; mRNA. DR UniGene; Xl.1104; -. DR HSSP; P08913; 1HLL. DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB. DR GO; GO:0004993; F:serotonin receptor activity; ISS:UniProtKB. DR GO; GO:0008283; P:cell proliferation; IDA:UniProtKB. DR GO; GO:0006260; P:DNA replication; IDA:UniProtKB. DR GO; GO:0007210; P:serotonin receptor signaling pathway; ISS:UniProtKB. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 408 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000245784. FT TOPO_DOM 1 34 Extracellular (Potential). FT TRANSMEM 35 55 1 (Potential). FT TOPO_DOM 56 67 Cytoplasmic (Potential). FT TRANSMEM 68 88 2 (Potential). FT TOPO_DOM 89 104 Extracellular (Potential). FT TRANSMEM 105 125 3 (Potential). FT TOPO_DOM 126 148 Cytoplasmic (Potential). FT TRANSMEM 149 169 4 (Potential). FT TOPO_DOM 170 187 Extracellular (Potential). FT TRANSMEM 188 208 5 (Potential). FT TOPO_DOM 209 333 Cytoplasmic (Potential). FT TRANSMEM 334 354 6 (Potential). FT TOPO_DOM 355 365 Extracellular (Potential). FT TRANSMEM 366 386 7 (Potential). FT TOPO_DOM 387 408 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 6 6 N-linked (GlcNAc...) (Potential). FT DISULFID 103 181 By similarity. SQ SEQUENCE 408 AA; 45788 MW; 2CB6156F7D53B1B5 CRC64; MDASNNTTSW NILQRGRMGP SWRRCPVSYQ IIASLFLGRS FSAGIFGNAC VIAAIALERS LQNVANYLIG SLAVTDLMVS VLVLPMAAQN QVLNKWTLGQ VTCDIFISLD VLCCTSSILH LCAIALDRYW AITDPIDYVN KRTPRRAAVL ISITWIVGFS ISIPPMLGWR TPEDRSDPNA CRISEDPGYT IYSTFGAFYI PLILMLVLYG KIFKAARFRI RKTVKKAEKK KVADTCLSVS QQSPKEKQRG AQQELEEVGG AQAQRCVNGA IRHGEEGAVL EIIEVHHYVN SKCHLHCKPV PPPEQLPPAL KNDRATEAKR KVALARERKT VKTLGIIMGT FILCWLPFFI VALVLPFCET CHMPHLLFDI ITWLGYSNSL LNPIIYAYFN KDFQSAFKKI IKCKFCRQ // ID 5HT1B_CANFA Reviewed; 389 AA. AC P79250; Q6VVV0; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 2. DT 31-OCT-2006, entry version 42. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B) (5-HTR1B) (5-HT1D subtype beta). GN Name=HTR1B; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=14729271; DOI=10.1016/j.gene.2003.10.028; RA van den Berg L., Imholz S., Versteeg S.A., Leegwater P.A.J., RA Zijlstra C., Bosma A.A., van Oost B.A.; RT "Isolation and characterization of the canine serotonin receptor 1B RT gene (htr1B)."; RL Gene 326:131-139(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Beagle; RX PubMed=15353848; DOI=10.1292/jvms.66.965; RA Masuda K., Hashizume C., Ogata N., Kikusui T., Takeuchi Y., Mori Y.; RT "Sequencing of canine 5-hydroxytriptamine receptor (5-HTR) 1B, 2A, 2C RT genes and identification of polymorphisms in the 5-HTR1B gene."; RL J. Vet. Med. Sci. 66:965-972(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15220384; DOI=10.1093/jhered/esh033; RA Kukekova A.V., Trut L.N., Oskina I.N., Kharlamova A.V., RA Shikhevich S.G., Kirkness E.F., Aguirre G.D., Acland G.M.; RT "A marker set for construction of a genetic map of the silver fox RT (Vulpes vulpes)."; RL J. Hered. 95:185-194(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 192-352. RC STRAIN=Alsatian, and Beagle; TISSUE=Artery; RX MEDLINE=96296365; PubMed=8763409; DOI=10.1016/0008-6363(96)00014-4; RA Sgard F., Faure C., Graham D.; RT "Evidence for 5-HT1D beta but not 5-HT1D alpha receptor subtype RT expression in canine large coronary arteries and saphenous vein."; RL Cardiovasc. Res. 31:793-799(1996). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY323909; AAQ89935.1; -; Genomic_DNA. DR EMBL; AB193090; BAD60920.1; -; mRNA. DR EMBL; AY204572; AAP12469.1; -; Genomic_DNA. DR EMBL; S82461; AAB37488.2; -; mRNA. DR UniGene; Cfa.3604; -. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 389 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068910. FT TOPO_DOM 1 50 Extracellular (Potential). FT TRANSMEM 51 74 1 (Potential). FT TOPO_DOM 75 85 Cytoplasmic (Potential). FT TRANSMEM 86 112 2 (Potential). FT TOPO_DOM 113 122 Extracellular (Potential). FT TRANSMEM 123 144 3 (Potential). FT TOPO_DOM 145 166 Cytoplasmic (Potential). FT TRANSMEM 167 186 4 (Potential). FT TOPO_DOM 187 207 Extracellular (Potential). FT TRANSMEM 208 227 5 (Potential). FT TOPO_DOM 228 314 Cytoplasmic (Potential). FT TRANSMEM 315 335 6 (Potential). FT TOPO_DOM 336 349 Extracellular (Potential). FT TRANSMEM 350 372 7 (Potential). FT TOPO_DOM 373 389 Cytoplasmic (Potential). FT LIPID 387 387 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 31 31 N-linked (GlcNAc...) (Potential). FT DISULFID 121 198 By similarity. SQ SEQUENCE 389 AA; 42930 MW; 4CCB4CCB5792936D CRC64; MEAAGAPCAP PPPAGSQTGA PPANLSSAPH NCSAEGYIYQ DSVALPWKVL LVILLALITL ATTLSNAFVI ATVYRTRKLH TPANYLIASL AVTDLLVSIL VMPISTMYTV TGRWTLGQVV CDLWLSSDIT CCTASILHLC VIALDRYWAI TDAVEYSAKR TPKRAAVMIA LVWVFSISIS LPPFFWRQAK AEEEVSDCVV NTDHILYTVY STVGAFYFPT LLLIALYGRI YVEARSRILK QTPNRTGKRL TRAQLITDSP GSTSSVTSVN SRAPDVPSES GSPVYVNQVK VRVSDALLEK KKLMAARERK ATKTLGIILG AFIVCWLPFF IISLVMPICK DACWFHLAIF DFFTWLGYLN SLINPIIYTM SNEDFKQAFH KLIRFKCAG // ID 5HT1B_CAVPO Reviewed; 389 AA. AC O08892; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 31-OCT-2006, entry version 38. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B). GN Name=HTR1B; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX MEDLINE=97368662; PubMed=9225276; DOI=10.1016/S0028-3908(97)00023-3; RA Zgombick J.M., Bard J.A., Kucharewicz S.A., Urquhart D.A., RA Weinshank R.L., Branchek T.A.; RT "Molecular cloning and pharmacological characterization of guinea pig RT 5-HT1B and 5-HT1D receptors."; RL Neuropharmacology 36:513-524(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U82175; AAB58500.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 389 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068911. FT TOPO_DOM 1 50 Extracellular (Potential). FT TRANSMEM 51 74 1 (Potential). FT TOPO_DOM 75 85 Cytoplasmic (Potential). FT TRANSMEM 86 112 2 (Potential). FT TOPO_DOM 113 122 Extracellular (Potential). FT TRANSMEM 123 144 3 (Potential). FT TOPO_DOM 145 166 Cytoplasmic (Potential). FT TRANSMEM 167 186 4 (Potential). FT TOPO_DOM 187 207 Extracellular (Potential). FT TRANSMEM 208 227 5 (Potential). FT TOPO_DOM 228 314 Cytoplasmic (Potential). FT TRANSMEM 315 335 6 (Potential). FT TOPO_DOM 336 349 Extracellular (Potential). FT TRANSMEM 350 372 7 (Potential). FT TOPO_DOM 373 389 Cytoplasmic (Potential). FT LIPID 387 387 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 31 31 N-linked (GlcNAc...) (Potential). FT DISULFID 121 198 By similarity. SQ SEQUENCE 389 AA; 43111 MW; C057CAB0A7FEE3C6 CRC64; MGNPEASCTP PAVLGSQTGL PHANVSAPPN NCSAPSHIYQ DSIALPWKVL LVVLLALITL ATTLSNAFVI ATVYRTRKLH TPANYLIASL AFTDLLVSIL VMPISTMYTV TGRWTLGQAL CDFWLSSDIT CCTASIMHLC VIALDRYWAI TDAVGYSAKR TPRRAAGMIA LVWVFSICIS LPPFFWRQAK AEEEVLDCLV NTDHVLYTVY STGGAFYLPT LLLIALYGRI YVEARSRILK QTPNKTGKRL TRAQLITDSP GSTSSVTSIN SRAPEVPCDS GSPVYVNQVK VRVSDALLEK KKLMAARERK ATKTLGVILG AFIVCWLPFF IISLVMPICK DACWFHMAIF DFFTWLGYLN SLINPIIYTM SNEDFKQAFH KLIRFKCTT // ID 5HT1B_CRIGR Reviewed; 386 AA. AC P46636; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 31-OCT-2006, entry version 41. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B). GN Name=HTR1B; OS Cricetulus griseus (Chinese hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung fibroblast; RA Wurch T., Palmier C., Colpaert F.C., Pauwels P.J.; RT "Molecular cloning and expression of a Chinese hamster lung fibroblast RT cDNA encoding a 5-HT1B receptor."; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X86458; CAA60175.1; -; mRNA. DR PIR; S54153; S54153. DR HSSP; P08913; 1HLL. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 386 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068912. FT TOPO_DOM 1 47 Extracellular (Potential). FT TRANSMEM 48 71 1 (Potential). FT TOPO_DOM 72 82 Cytoplasmic (Potential). FT TRANSMEM 83 109 2 (Potential). FT TOPO_DOM 110 119 Extracellular (Potential). FT TRANSMEM 120 141 3 (Potential). FT TOPO_DOM 142 163 Cytoplasmic (Potential). FT TRANSMEM 164 183 4 (Potential). FT TOPO_DOM 184 204 Extracellular (Potential). FT TRANSMEM 205 224 5 (Potential). FT TOPO_DOM 225 311 Cytoplasmic (Potential). FT TRANSMEM 312 332 6 (Potential). FT TOPO_DOM 333 346 Extracellular (Potential). FT TRANSMEM 347 369 7 (Potential). FT TOPO_DOM 370 386 Cytoplasmic (Potential). FT LIPID 384 384 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 28 28 N-linked (GlcNAc...) (Potential). FT DISULFID 118 195 By similarity. SQ SEQUENCE 386 AA; 42896 MW; B0DC6211C2B6DECE CRC64; MEEQGIQCAP PPPAASQTGV PLVNLSHNCS AESHIYQDSI ALPWKVLLVA LLALITLATT LSNAFVIATV YRTRKLHTPA NYLIASLAVT DLLVSILVMP VSTMYTVTGR WTLGQVVCDF WLSSDITCCT ASIMHLCVIA LDRYWAITDA VEYAAKRTPK RAAIMIALVW VFSISISLPP FFWRQAKAEE EVLTCLVNTD HVLYTVYSTG GAFYLPTLLL IALYGRIYVE ARSRILKQTP NKTGKRLTRA QLITDSPGST TSVTSINSRA PDLPSESGSP VYVNQVKVRV SDALLEKKKL MAARERKATK TLGIILGAFI VCWLPFFIIS LVMPICKDAC WFHMATLDFF NWLGYLNSLI NPIIYTMSNE DFKQAFHKLI RFKCAG // ID 5HT1B_DIDMA Reviewed; 388 AA. AC P35404; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 31-OCT-2006, entry version 38. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B). GN Name=HTR1B; OS Didelphis marsupialis virginiana (North American opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Didelphis. OX NCBI_TaxID=9267; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RX MEDLINE=94134056; PubMed=8302276; RA Cerutis D., Hass N.A., Iversen L.J., Bylund D.B.; RT "The cloning and expression of an OK cell cDNA encoding a 5- RT hydroxytryptamine1B receptor."; RL Mol. Pharmacol. 45:20-28(1994). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U04311; AAA17567.1; -; mRNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 388 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068913. FT TOPO_DOM 1 48 Extracellular (Potential). FT TRANSMEM 49 74 1 (Potential). FT TOPO_DOM 75 85 Cytoplasmic (Potential). FT TRANSMEM 86 112 2 (Potential). FT TOPO_DOM 113 122 Extracellular (Potential). FT TRANSMEM 123 144 3 (Potential). FT TOPO_DOM 145 166 Cytoplasmic (Potential). FT TRANSMEM 167 186 4 (Potential). FT TOPO_DOM 187 207 Extracellular (Potential). FT TRANSMEM 208 227 5 (Potential). FT TOPO_DOM 228 313 Cytoplasmic (Potential). FT TRANSMEM 314 335 6 (Potential). FT TOPO_DOM 336 348 Extracellular (Potential). FT TRANSMEM 349 371 7 (Potential). FT TOPO_DOM 372 388 Cytoplasmic (Potential). FT CARBOHYD 22 22 N-linked (GlcNAc...) (Potential). FT CARBOHYD 30 30 N-linked (GlcNAc...) (Potential). FT DISULFID 121 197 By similarity. SQ SEQUENCE 388 AA; 43111 MW; DB5E8A033325615A CRC64; MEQPSRLCSP PASGSLTSSQ TNHSTFPNPN CSAPDLEPYQ DSIALPWKVL LATFLGLITL GTTLSNAFVI ATVSRTRKLH TPANYLIASL AVTDLLVSIL VMPISTMYTV TGRWTLGQVV CDFWLSSDIT CCTASILHLC VIALDRYWAI TDAVEYSAKR TPKRAAGMII MVWVFSVSIS MPPLFWRQAK AEEVADCSVN TDHILYTVYS TVGAFYFPTL LLIALYGRIY VEARSRILKQ TPNRTGKRLT RAQLITDSPG SSSSGTSINS RAPEGPSESG SPVYVNQVKV KVSDALLEKK KLMAARERKA TRTLGIILGA FIVCWLPFFI ISLALPICDD ACWFHLAIFD FFNWLGYLNS LINPIIYTKS NDDFKQAFQK LMRFRRTS // ID 5HT1B_FELCA Reviewed; 389 AA. AC Q588Y6; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 31-OCT-2006, entry version 13. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B). GN Name=HTR1B; OS Felis silvestris catus (Cat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Asahi D., Mori Y.; RT "Felis catus 5-hydroxytryptamine (serotonin) receptor 1B (Htr1b), RT mRNA."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB190344; BAD93295.1; -; mRNA. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 389 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068914. FT TOPO_DOM 1 48 Extracellular (Potential). FT TRANSMEM 49 72 1 (Potential). FT TOPO_DOM 73 85 Cytoplasmic (Potential). FT TRANSMEM 86 108 2 (Potential). FT TOPO_DOM 109 118 Extracellular (Potential). FT TRANSMEM 119 144 3 (Potential). FT TOPO_DOM 145 164 Cytoplasmic (Potential). FT TRANSMEM 165 186 4 (Potential). FT TOPO_DOM 187 204 Extracellular (Potential). FT TRANSMEM 205 228 5 (Potential). FT TOPO_DOM 229 314 Cytoplasmic (Potential). FT TRANSMEM 315 339 6 (Potential). FT TOPO_DOM 340 346 Extracellular (Potential). FT TRANSMEM 347 372 7 (Potential). FT TOPO_DOM 373 389 Cytoplasmic (Potential). FT LIPID 387 387 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 31 31 N-linked (GlcNAc...) (Potential). FT DISULFID 121 198 By similarity. SQ SEQUENCE 389 AA; 43372 MW; 7FEFA1C2DB097CCC CRC64; MEETNTHCAP PPPAGSQTGV SQANLSSAPP NCSTEGYIYQ DSIALPWKVL LILVLALFTL ATTLSNAFVI ATVYRTRKLH TPANYLIASL AVTDLLVSIL VMPISTMYTV TGRWTLGQVV CDFWLSSDIT CCTASILHLC VIALDRYWAI TDAVEYSAKR TPKRAAVMIA LVWVFSISIS LPPFFWRQAK AEEEVSDCRV NTDHMLYTVY STVGAFYFPT LLLIALYGRI YVEARSRILK QTPNRTGKRL TRAQLITDSP GSTSSVTSVN SRAPDVPSES GSPVYVNQVK VRVSDALLEK KKLMAARERK ATKTLGIILG AFIVCWLPFF IISLVMPICK DACWFHLAIF DFFTWLGYLN SLINPIIYTM SNEDFKQAFH KLIRFKCTG // ID 5HT1B_FUGRU Reviewed; 416 AA. AC O42384; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 31-OCT-2006, entry version 42. DE 5-hydroxytryptamine 1A-beta receptor (5-HT-1A-beta) (Serotonin DE receptor 1A-beta) (5-HT1A-beta) (F1B). OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=97361762; PubMed=9218723; DOI=10.1016/S0378-1119(97)00064-4; RA Yamaguchi F., Brenner S.; RT "Molecular cloning of 5-hydroxytryptamine (5-HT) type 1 receptor genes RT from the Japanese puffer fish, Fugu rubripes."; RL Gene 191:219-223(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X95937; CAA65176.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR Ensembl; SINFRUG00000129352; Fugu rubripes. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 416 5-hydroxytryptamine 1A-beta receptor. FT /FTId=PRO_0000068924. FT TOPO_DOM 1 33 Extracellular (Potential). FT TRANSMEM 34 59 1 (Potential). FT TOPO_DOM 60 70 Cytoplasmic (Potential). FT TRANSMEM 71 95 2 (Potential). FT TOPO_DOM 96 106 Extracellular (Potential). FT TRANSMEM 107 129 3 (Potential). FT TOPO_DOM 130 149 Cytoplasmic (Potential). FT TRANSMEM 150 170 4 (Potential). FT TOPO_DOM 171 193 Extracellular (Potential). FT TRANSMEM 194 219 5 (Potential). FT TOPO_DOM 220 339 Cytoplasmic (Potential). FT TRANSMEM 340 361 6 (Potential). FT TOPO_DOM 362 372 Extracellular (Potential). FT TRANSMEM 373 397 7 (Potential). FT TOPO_DOM 398 416 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 6 6 N-linked (GlcNAc...) (Potential). FT CARBOHYD 18 18 N-linked (GlcNAc...) (Potential). FT DISULFID 106 189 By similarity. SQ SEQUENCE 416 AA; 47031 MW; 9B4CC415BEC750FE CRC64; MEGTNNTTGW THFDSTSNRT SKSFDEEVKL SYQVVTSFLL GALILCSIFG NACVVAAIAL ERSLQNVANY LIGSLAVTDL MVSVLVLPMA ALYQVLNRWT LGQIPCDIFI SLDMLCCTSS ILHLCVIALD RYWAITEPID YMKKRTPRRA AVLISVTWLV GFSISIPPML IMRSQPSSMA EDRANSKQCK ITQDPWYTIY STFGAFYIPL TLMLVLYGRI FKAARFRIRR TVRKTEKKKV SDTCLALSPA MFHRKTPGDA HGKSWKRSVE PRPLPNVNGA VKHAGEGESL DIIEVQSNSR CNLPLPNTPG TVPLFENRHE KATETKRKIA LARERKTVKT LGIIMGTFIL CWLPFFIVAL VMPFCQESCF MPHWLKDVIN WLGYSNSLLN PIIYAYFNKD FQSAFKKIIK CHFCRA // ID 5HT1B_GORGO Reviewed; 390 AA. AC Q9N2B7; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 31-OCT-2006, entry version 29. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B). GN Name=HTR1B; OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041372; BAA94457.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 390 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068915. FT TOPO_DOM 1 49 Extracellular (Potential). FT TRANSMEM 50 73 1 (Potential). FT TOPO_DOM 74 86 Cytoplasmic (Potential). FT TRANSMEM 87 109 2 (Potential). FT TOPO_DOM 110 119 Extracellular (Potential). FT TRANSMEM 120 145 3 (Potential). FT TOPO_DOM 146 165 Cytoplasmic (Potential). FT TRANSMEM 166 187 4 (Potential). FT TOPO_DOM 188 205 Extracellular (Potential). FT TRANSMEM 206 229 5 (Potential). FT TOPO_DOM 230 315 Cytoplasmic (Potential). FT TRANSMEM 316 340 6 (Potential). FT TOPO_DOM 341 347 Extracellular (Potential). FT TRANSMEM 348 373 7 (Potential). FT TOPO_DOM 374 390 Cytoplasmic (Potential). FT LIPID 388 388 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 32 32 N-linked (GlcNAc...) (Potential). FT DISULFID 122 199 By similarity. SQ SEQUENCE 390 AA; 43566 MW; 37D54B95E3277FC3 CRC64; MEEPGAQCAP PXPAGSETWV PQANLSSAPS QNCSAKDYIY QDSIALPWKV LLVMLLALIT LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV VCDFWLSSDI TCCTASILHL CVIALDRYWA ITDAVEYSAK RTPKRAAVMI ALVWVFSISI SLPPFFWRQA KAEEEVSECV VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL KQTPNRTGKR LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI FDFFTWLGYL NSLINPIIYT MSNEDFKQAF HKLIRFKCTS // ID 5HT1B_HORSE Reviewed; 390 AA. AC Q0EAB5; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 09-JAN-2007, entry version 3. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B). GN Name=HTR1B; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Momozawa Y., Takeuchi Y., Mori Y.; RT "Equus caballus 5-hydroxytryptamine (serotonin) receptor 1B (HTR1B), RT mRNA."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB264326; BAF32953.1; -; mRNA. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 390 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000271765. FT TOPO_DOM 1 49 Extracellular (Potential). FT TRANSMEM 50 73 1 (Potential). FT TOPO_DOM 74 86 Cytoplasmic (Potential). FT TRANSMEM 87 109 2 (Potential). FT TOPO_DOM 110 119 Extracellular (Potential). FT TRANSMEM 120 145 3 (Potential). FT TOPO_DOM 146 165 Cytoplasmic (Potential). FT TRANSMEM 166 187 4 (Potential). FT TOPO_DOM 188 205 Extracellular (Potential). FT TRANSMEM 206 229 5 (Potential). FT TOPO_DOM 230 315 Cytoplasmic (Potential). FT TRANSMEM 316 340 6 (Potential). FT TOPO_DOM 341 347 Extracellular (Potential). FT TRANSMEM 348 373 7 (Potential). FT TOPO_DOM 374 390 Cytoplasmic (Potential). FT LIPID 388 388 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 32 32 N-linked (GlcNAc...) (Potential). FT DISULFID 122 199 By similarity. SQ SEQUENCE 390 AA; 43350 MW; 8643A26FDE000B0F CRC64; MEETGAQCAP PPPAGSQTGV SQVNLSAAPS HNCSTEGYVY QDSVALPWKV LLVVLLALIT LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYV VTGRWTLGQV VCDFWLSSDI TCCTASILHL CVIALDRYWA ITDAVEYSAK RTPKRAAVMI ALVWVFSISI SLPPFFWRQA KAEEEVLDCL VNTDHILYTV YSTVGAFYFP TLLLIALYSR IYVEARSRIL KQTPNRTGKR LTRAQLMTDS PGSTSSVTSI NSRAPDVPSE SGSPVYVNQV KVRVSDALVE KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI FDFFTWLGYL NSLINPIIYT MSNEDFKQAF HKLIRFKCAS // ID 5HT1B_HUMAN Reviewed; 390 AA. AC P28222; Q4VAY7; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 23-JAN-2007, entry version 66. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B) (5-HT-1D-beta) (Serotonin 1D beta receptor) (S12). GN Name=HTR1B; Synonyms=HTR1DB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX MEDLINE=92228840; PubMed=1565658; RA Weinshank R.L., Zgombick J.M., Macchi M.J., Branchek T.A., RA Hartig P.R.; RT "Human serotonin 1D receptor is encoded by a subfamily of two distinct RT genes: 5-HT1D alpha and 5-HT1D beta."; RL Proc. Natl. Acad. Sci. U.S.A. 89:3630-3634(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92302275; PubMed=1351684; RA Demchyshyn L., Sunahara R.K., Miller K., Teitler M., Hoffman B.J., RA Kennedy J.L., Seeman P., van Tol H.H.M., Niznik H.B.; RT "A human serotonin 1D receptor variant (5HT1D beta) encoded by an RT intronless gene on chromosome 6."; RL Proc. Natl. Acad. Sci. U.S.A. 89:5522-5526(1992). RN [3] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=92304270; PubMed=1610347; RA Mochizuki D., Yuyama Y., Tsujita R., Komaki H., Sagai H.; RT "Cloning and expression of the human 5-HT1B-type receptor gene."; RL Biochem. Biophys. Res. Commun. 185:517-523(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92246962; PubMed=1315531; RA Hamblin M.W., Metcalf M.A., McGuffin R.W., Karpells S.; RT "Molecular cloning and functional characterization of a human 5-HT1B RT serotonin receptor: a homologue of the rat 5-HT1B receptor with 5- RT HT1D-like pharmacological specificity."; RL Biochem. Biophys. Res. Commun. 184:752-759(1992). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92218412; PubMed=1559993; RA Levy F.O., Gudermann T., Perez-Reyes E., Birnbaumer M., Kaumann A.J., RA Birnbaumer L.; RT "Molecular cloning of a human serotonin receptor (S12) with a RT pharmacological profile resembling that of the 5-HT1D subtype."; RL J. Biol. Chem. 267:7553-7562(1992). RN [6] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=93024334; PubMed=1328844; RA Veldman S.A., Bienkowski M.J.; RT "Cloning and pharmacological characterization of a novel human 5- RT hydroxytryptamine1D receptor subtype."; RL Mol. Pharmacol. 42:439-444(1992). RN [7] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=92210526; PubMed=1348246; RA Jin H., Oksenberg D., Ashkenazi A., Peroutka S.J., Duncan A.M.V., RA Rozmahel R., Yang Y., Mengod G., Palacios J.M., O'Dowd B.F.; RT "Characterization of the human 5-hydroxytryptamine1B receptor."; RL J. Biol. Chem. 267:5735-5738(1992). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kopatz S.A., Aronstam R.S., Sharma S.V.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [11] 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 [12] RP PALMITOYLATION, AND PHOSPHORYLATION. RX MEDLINE=94032297; PubMed=8218242; DOI=10.1021/bi00094a032; RA Ng G.Y.K., George S.R., Zastawny R.L., Caron M., Bouvier M., RA Dennis M., O'Dowd B.F.; RT "Human serotonin1B receptor expression in Sf9 cells: phosphorylation, RT palmitoylation, and adenylyl cyclase inhibition."; RL Biochemistry 32:11727-11733(1993). RN [13] RP VARIANT CYS-124. RX MEDLINE=95100945; PubMed=7802650; RA Nothen M.M., Erdmann J., Shimron-Abarbanell D., Propping P.; RT "Identification of genetic variation in the human serotonin 1D beta RT receptor gene."; RL Biochem. Biophys. Res. Commun. 205:1194-1200(1994). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated. Desensitization of the receptor may be CC mediated by its phosphorylation. CC -!- PTM: Palmitoylated. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D10995; BAA01763.1; -; Genomic_DNA. DR EMBL; M81590; AAA60316.1; -; mRNA. DR EMBL; M75128; AAA58675.1; -; Genomic_DNA. DR EMBL; M89478; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L09732; AAA36030.1; -; Genomic_DNA. DR EMBL; M83180; AAA36029.1; -; Genomic_DNA. DR EMBL; AB041370; BAA94455.1; -; Genomic_DNA. DR EMBL; AY225227; AAO67712.1; -; Genomic_DNA. DR EMBL; AL049595; CAB51537.1; -; Genomic_DNA. DR EMBL; BC069065; AAH69065.1; -; mRNA. DR EMBL; BC096206; AAH96206.1; -; mRNA. DR EMBL; BC096207; AAH96207.1; -; mRNA. DR EMBL; BC096208; AAH96208.1; -; mRNA. DR PIR; JN0268; JN0268. DR UniGene; Hs.123016; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000135312; Homo sapiens. DR KEGG; hsa:3351; -. DR HGNC; HGNC:5287; HTR1B. DR MIM; 182131; gene. DR DrugBank; APRD00476; Dihydroergotamine. DR DrugBank; APRD00945; Eletriptan. DR DrugBank; APRD00677; Ergotamine. DR DrugBank; APRD00270; Frovatriptan. DR DrugBank; APRD00220; Naratriptan. DR DrugBank; APRD00008; Rizatriptan. DR DrugBank; APRD00379; Sumatriptan. DR DrugBank; APRD00376; Zolmitriptan. DR ArrayExpress; P28222; -. DR GermOnline; ENSG00000135312; Homo sapiens. DR RZPD-ProtExp; A0434; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004993; F:serotonin receptor activity; TAS:ProtInc. DR GO; GO:0007187; P:G-protein signaling, coupled to cyclic nucl...; TAS:ProtInc. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Polymorphism; Receptor; Transducer; KW Transmembrane. FT CHAIN 1 390 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068916. FT TOPO_DOM 1 49 Extracellular (Potential). FT TRANSMEM 50 73 1 (Potential). FT TOPO_DOM 74 86 Cytoplasmic (Potential). FT TRANSMEM 87 109 2 (Potential). FT TOPO_DOM 110 119 Extracellular (Potential). FT TRANSMEM 120 145 3 (Potential). FT TOPO_DOM 146 165 Cytoplasmic (Potential). FT TRANSMEM 166 187 4 (Potential). FT TOPO_DOM 188 205 Extracellular (Potential). FT TRANSMEM 206 229 5 (Potential). FT TOPO_DOM 230 315 Cytoplasmic (Potential). FT TRANSMEM 316 340 6 (Potential). FT TOPO_DOM 341 347 Extracellular (Potential). FT TRANSMEM 348 373 7 (Potential). FT TOPO_DOM 374 390 Cytoplasmic (Potential). FT LIPID 388 388 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 32 32 N-linked (GlcNAc...) (Potential). FT DISULFID 122 199 By similarity. FT VARIANT 124 124 F -> C (in dbSNP:rs130060). FT /FTId=VAR_011715. FT VARIANT 219 219 F -> L (in dbSNP:rs130061). FT /FTId=VAR_011831. FT VARIANT 367 367 I -> V (in dbSNP:rs130063). FT /FTId=VAR_011832. FT VARIANT 374 374 E -> K (in dbSNP:rs130064). FT /FTId=VAR_011833. SQ SEQUENCE 390 AA; 43568 MW; CD874DC7EB44CF12 CRC64; MEEPGAQCAP PPPAGSETWV PQANLSSAPS QNCSAKDYIY QDSISLPWKV LLVMLLALIT LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV VCDFWLSSDI TCCTASILHL CVIALDRYWA ITDAVEYSAK RTPKRAAVMI ALVWVFSISI SLPPFFWRQA KAEEEVSECV VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL KQTPNRTGKR LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI FDFFTWLGYL NSLINPIIYT MSNEDFKQAF HKLIRFKCTS // ID 5HT1B_MOUSE Reviewed; 386 AA. AC P28334; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 23-JAN-2007, entry version 54. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B). GN Name=Htr1b; Synonyms=5ht1b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92212959; PubMed=1557407; RA Maroteaux L., Saudou F., Amlaiky N., Boschert U., Plassat J.-L., RA Hen R.; RT "Mouse 5HT1B serotonin receptor: cloning, functional expression, and RT localization in motor control centers."; RL Proc. Natl. Acad. Sci. U.S.A. 89:3020-3024(1992). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Predominantly expressed in striatum and CC Purkinje cells. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11597; CAA77678.1; -; Genomic_DNA. DR EMBL; M85151; AAA83221.1; -; Genomic_DNA. DR PIR; A42688; A42688. DR UniGene; Mm.246494; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSMUSG00000049511; Mus musculus. DR KEGG; mmu:15551; -. DR MGI; MGI:96274; Htr1b. DR ArrayExpress; P28334; -. DR GermOnline; ENSMUSG00000049511; Mus musculus. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 386 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068917. FT TOPO_DOM 1 47 Extracellular (Potential). FT TRANSMEM 48 71 1 (Potential). FT TOPO_DOM 72 82 Cytoplasmic (Potential). FT TRANSMEM 83 109 2 (Potential). FT TOPO_DOM 110 119 Extracellular (Potential). FT TRANSMEM 120 141 3 (Potential). FT TOPO_DOM 142 163 Cytoplasmic (Potential). FT TRANSMEM 164 183 4 (Potential). FT TOPO_DOM 184 204 Extracellular (Potential). FT TRANSMEM 205 224 5 (Potential). FT TOPO_DOM 225 311 Cytoplasmic (Potential). FT TRANSMEM 312 332 6 (Potential). FT TOPO_DOM 333 346 Extracellular (Potential). FT TRANSMEM 347 369 7 (Potential). FT TOPO_DOM 370 386 Cytoplasmic (Potential). FT LIPID 384 384 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 28 28 N-linked (GlcNAc...) (Potential). FT DISULFID 118 195 By similarity. SQ SEQUENCE 386 AA; 43079 MW; 58F70FBEA770C0B3 CRC64; MEEQGIQCAP PPPAASQTGV PLTNLSHNCS ADGYIYQDSI ALPWKVLLVA LLALITLATT LSNAFVIATV YRTRKLHTPA NYLIASLAVT DLLVSILVMP ISTMYTVTGR WTLGQVVCDF WLSSDITCCT ASIMHLCVIA LDRYWAITDA VEYSAKRTPK RAAIMIVLVW VFSISISLPP FFWRQAKAEE EMLDCFVNTD HVLYTVYSTV GAFYLPTLLL IALYGRIYVE ARSRILKQTP NKTGKRLTRA QLITDSPGST SSVTSINSRA PDVPSESGSP VYVNQVKVRV SDALLEKKKL MAARERKATK TLGIILGAFI VCWLPFFIIS LVMPICKDAC WFHMAIFDFF NWLGYLNSLI NPIIYTMSNE DFKQAFHKLI RFKCAG // ID 5HT1B_PANTR Reviewed; 390 AA. AC P60020; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 21-NOV-2003, sequence version 1. DT 31-OCT-2006, entry version 27. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B). GN Name=HTR1B; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041371; BAA94456.1; -; Genomic_DNA. DR KEGG; ptr:462833; -. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 390 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068918. FT TOPO_DOM 1 49 Extracellular (Potential). FT TRANSMEM 50 73 1 (Potential). FT TOPO_DOM 74 86 Cytoplasmic (Potential). FT TRANSMEM 87 109 2 (Potential). FT TOPO_DOM 110 119 Extracellular (Potential). FT TRANSMEM 120 145 3 (Potential). FT TOPO_DOM 146 165 Cytoplasmic (Potential). FT TRANSMEM 166 187 4 (Potential). FT TOPO_DOM 188 205 Extracellular (Potential). FT TRANSMEM 206 229 5 (Potential). FT TOPO_DOM 230 315 Cytoplasmic (Potential). FT TRANSMEM 316 340 6 (Potential). FT TOPO_DOM 341 347 Extracellular (Potential). FT TRANSMEM 348 373 7 (Potential). FT TOPO_DOM 374 390 Cytoplasmic (Potential). FT LIPID 388 388 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 32 32 N-linked (GlcNAc...) (Potential). FT DISULFID 122 199 By similarity. SQ SEQUENCE 390 AA; 43568 MW; CD874DC7EB44CF12 CRC64; MEEPGAQCAP PPPAGSETWV PQANLSSAPS QNCSAKDYIY QDSISLPWKV LLVMLLALIT LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV VCDFWLSSDI TCCTASILHL CVIALDRYWA ITDAVEYSAK RTPKRAAVMI ALVWVFSISI SLPPFFWRQA KAEEEVSECV VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL KQTPNRTGKR LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI FDFFTWLGYL NSLINPIIYT MSNEDFKQAF HKLIRFKCTS // ID 5HT1B_PIG Reviewed; 150 AA. AC P79399; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 31-OCT-2006, entry version 33. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B) (Fragment). GN Name=HTR1B; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain cortex; RA Wurch T., Lestienne F., Colpaert F.C., Pauwels P.J.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y11867; CAA72615.1; -; mRNA. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Lipoprotein; Membrane; Palmitate; KW Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN <1 >150 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068919. FT TOPO_DOM <1 83 Cytoplasmic (Potential). FT TRANSMEM 84 107 6 (Potential). FT TOPO_DOM 108 116 Extracellular (Potential). FT TRANSMEM 117 141 7 (Potential). FT TOPO_DOM 142 >150 Cytoplasmic (Potential). FT NON_TER 1 1 FT NON_TER 150 150 SQ SEQUENCE 150 AA; 16941 MW; 084EDF34A349555A CRC64; VEARSRILKQ TPNRTGKRLT RAQLITDSPG STSSVTSINS RAPDLPSESG SPVYVNQVKV RVSDALLEKK KLMAARERKA TKTLGIILGA FIVCWLPFFI ISLAMPICKD ACWFHLAIFD FFTWLGYLNS LINPIIYTMF NEDFKQAFHK // ID 5HT1B_RABIT Reviewed; 390 AA. AC P49144; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 31-OCT-2006, entry version 41. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B) (5-HT-1D-beta). GN Name=HTR1B; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX MEDLINE=96130324; PubMed=8543023; DOI=10.1016/0014-5793(95)01308-3; RA Harwood G.S., Lockyer M., Giles H., Fairweather N.; RT "Cloning and characterisation of the rabbit 5-HT1D alpha and 5-HT1D RT beta receptors."; RL FEBS Lett. 377:73-76(1995). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=New Zealand white; TISSUE=Saphenous vein; RA Wurch T., Cathala C., Palmer C., Valentin J.P., John G., RA Colpaert F.C., Pauwels P.J.; RT "Molecular cloning and identification of a rabbit saphenous vein 5-HT RT 1DB receptor gene."; RL Neurosci. Res. Commun. 18:155-162(1996). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=New Zealand white; RX MEDLINE=97032156; PubMed=8878052; DOI=10.1007/BF00171053; RA Bard J.A., Kucharewicz S.A., Zgombick J.M., Weinshank R.L., RA Branchek T.A., Cohen M.L.; RT "Differences in ligand binding profiles between cloned rabbit and RT human 5-HT1D alpha and 5-HT1D beta receptors: ketanserin and RT methiothepin distinguish rabbit 5-HT1D receptor subtypes."; RL Naunyn Schmiedebergs Arch. Pharmacol. 354:237-244(1996). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z50163; CAA90531.1; -; Genomic_DNA. DR EMBL; X89731; CAA61883.1; -; mRNA. DR EMBL; U60826; AAB58467.1; -; Genomic_DNA. DR PIR; S58126; S58126. DR PIR; S68422; S68422. DR HSSP; P08913; 1HLL. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 390 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068920. FT TOPO_DOM 1 49 Extracellular (Potential). FT TRANSMEM 50 73 1 (Potential). FT TOPO_DOM 74 86 Cytoplasmic (Potential). FT TRANSMEM 87 109 2 (Potential). FT TOPO_DOM 110 119 Extracellular (Potential). FT TRANSMEM 120 145 3 (Potential). FT TOPO_DOM 146 165 Cytoplasmic (Potential). FT TRANSMEM 166 187 4 (Potential). FT TOPO_DOM 188 205 Extracellular (Potential). FT TRANSMEM 206 229 5 (Potential). FT TOPO_DOM 230 315 Cytoplasmic (Potential). FT TRANSMEM 316 340 6 (Potential). FT TOPO_DOM 341 347 Extracellular (Potential). FT TRANSMEM 348 373 7 (Potential). FT TOPO_DOM 374 390 Cytoplasmic (Potential). FT LIPID 388 388 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 32 32 N-linked (GlcNAc...) (Potential). FT DISULFID 122 199 By similarity. FT CONFLICT 5 5 G -> S (in Ref. 1 and 3). FT CONFLICT 7 7 Q -> R (in Ref. 1 and 3). FT CONFLICT 14 14 Missing (in Ref. 1 and 3). FT CONFLICT 171 171 R -> A (in Ref. 1 and 3). SQ SEQUENCE 390 AA; 43496 MW; C22EBC077C6C897D CRC64; MEEPGAQCAP PLAAGSQIAV PQANLSAAHS HNCSAEGYIY QDSIALPWKV LLVLLLALFT LATTLSNAFV VATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV VCDLWLSSDI TCCTASIMHL CVIALDRYWA ITDAVEYSAK RTPKRAAIMI RLVWVFSICI SLPPFFWRQA KAEEEVSECL VNTDHVLYTV YSTVGAFYLP TLLLIALYGR IYVEARSRIL KQTPNRTGKR LTRAQLITDS PGSTTSVTSI NSRAPDVPSE SGSPVYVNQV KVRVSDALLE KKKLMAARER KATKTLGIIL GVFIVCWLPF FIISLVMPIC KDACWFHQAI FDFFTWLGYV NSLINPIIYT MSNEDFKQAF HKLIRFKCTS // ID 5HT1B_RAT Reviewed; 386 AA. AC P28564; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 20-FEB-2007, entry version 50. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B). GN Name=Htr1b; Synonyms=5ht1b; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE. RA Hamblin M.W., McGuffin R.W., Metcalf M.A., Dorsa D.M., Merchant K.M.; RT "Distinct 5-HT1B and 5-HT1D serotonin receptors in rat: structural and RT pharmacological comparison of the two cloned receptors."; RL Mol. Cell. Neurosci. 3:578-587(1992). RN [2] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain; RX MEDLINE=92097519; PubMed=1836757; RA Voigt M.M., Laurie D.J., Seeburg P.H., Bach A.; RT "Molecular cloning and characterization of a rat brain cDNA encoding a RT 5-hydroxytryptamine1B receptor."; RL EMBO J. 10:4017-4023(1991). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M89954; AAA40613.1; -; Genomic_DNA. DR EMBL; X62944; CAA44716.1; -; mRNA. DR PIR; S18637; S18637. DR UniGene; Rn.138109; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSRNOG00000013042; Rattus norvegicus. DR KEGG; rno:25075; -. DR RGD; 2846; Htr1b. DR ArrayExpress; P28564; -. DR GermOnline; ENSRNOG00000013042; Rattus norvegicus. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 386 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068921. FT TOPO_DOM 1 47 Extracellular (Potential). FT TRANSMEM 48 71 1 (Potential). FT TOPO_DOM 72 82 Cytoplasmic (Potential). FT TRANSMEM 83 109 2 (Potential). FT TOPO_DOM 110 119 Extracellular (Potential). FT TRANSMEM 120 141 3 (Potential). FT TOPO_DOM 142 163 Cytoplasmic (Potential). FT TRANSMEM 164 183 4 (Potential). FT TOPO_DOM 184 204 Extracellular (Potential). FT TRANSMEM 205 224 5 (Potential). FT TOPO_DOM 225 310 Cytoplasmic (Potential). FT TRANSMEM 311 332 6 (Potential). FT TOPO_DOM 333 346 Extracellular (Potential). FT TRANSMEM 347 369 7 (Potential). FT TOPO_DOM 370 386 Cytoplasmic (Potential). FT LIPID 384 384 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 28 28 N-linked (GlcNAc...) (Potential). FT DISULFID 118 195 By similarity. SQ SEQUENCE 386 AA; 43163 MW; 4F4E9AC1C9AED214 CRC64; MEEQGIQCAP PPPATSQTGV PLANLSHNCS ADDYIYQDSI ALPWKVLLVA LLALITLATT LSNAFVIATV YRTRKLHTPA NYLIASLAVT DLLVSILVMP ISTMYTVTGR WTLGQVVCDF WLSSDITCCT ASIMHLCVIA LDRYWAITDA VDYSAKRTPK RAAIMIVLVW VFSISISLPP FFWRQAKAEE EVLDCFVNTD HVLYTVYSTV GAFYLPTLLL IALYGRIYVE ARSRILKQTP NKTGKRLTRA QLITDSPGST SSVTSINSRV PEVPSESGSP VYVNQVKVRV SDALLEKKKL MAARERKATK TLGIILGAFI VCWLPFFIIS LVMPICKDAC WFHMAIFDFF NWLGYLNSLI NPIIYTMSNE DFKQAFHKLI RFKCTG // ID 5HT1B_SPAEH Reviewed; 386 AA. AC P56496; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 31-OCT-2006, entry version 36. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B). GN Name=HTR1B; Synonyms=5HT1B; OS Spalax leucodon ehrenbergi (Ehrenberg's mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Spalacidae; Spalacinae; Nannospalax. OX NCBI_TaxID=30637; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Devor E.J., Nevo E.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF027184; AAB82748.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 386 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068922. FT TOPO_DOM 1 47 Extracellular (Potential). FT TRANSMEM 48 71 1 (Potential). FT TOPO_DOM 72 82 Cytoplasmic (Potential). FT TRANSMEM 83 109 2 (Potential). FT TOPO_DOM 110 119 Extracellular (Potential). FT TRANSMEM 120 141 3 (Potential). FT TOPO_DOM 142 163 Cytoplasmic (Potential). FT TRANSMEM 164 183 4 (Potential). FT TOPO_DOM 184 204 Extracellular (Potential). FT TRANSMEM 205 224 5 (Potential). FT TOPO_DOM 225 311 Cytoplasmic (Potential). FT TRANSMEM 312 332 6 (Potential). FT TOPO_DOM 333 346 Extracellular (Potential). FT TRANSMEM 347 369 7 (Potential). FT TOPO_DOM 370 386 Cytoplasmic (Potential). FT LIPID 384 384 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 28 28 N-linked (GlcNAc...) (Potential). FT DISULFID 118 195 By similarity. SQ SEQUENCE 386 AA; 43102 MW; 7A006E021A44B7F4 CRC64; MEEPGARCAP PPPAGSQTQT PSSNLSHNCS ADSYIYQDSI ALPWKVLLVA LLALITLATT LSNAFVIATV YRTRKLHTPA NYLIASLAVT DLLVSILVMP ISTMYTVTGR WTLGQVVCDF WLSSDITCCT ASIMHLCVIA LDRYWAITDA VEYSAKRTPR RAAVMIALVW VFSISISLPR FFWRQAKAEE EVLDCLVNTD HVLYTVYSTV GAFYLPTLLL IALYGRIYVE ARSRILKQTP NKTGKRLSRA QLISDSPGST SSVTSINSRV PDVPSESGSP VYVNQVKVRV SDALLEKKKL MAARERKATK TLGIILGAFI VCWLPFFIIS LVMPICKDAC WFHMAIFDFF NWLGYLNSLI NPIIYTMPNE DFKQAFHKLI RFKCTG // ID 5HT1B_VULVU Reviewed; 389 AA. AC Q6XXX8; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 31-OCT-2006, entry version 19. DE 5-hydroxytryptamine 1B receptor (5-HT-1B) (Serotonin receptor 1B) (5- DE HT1B) (5-HTR1B). GN Name=HTR1B; OS Vulpes vulpes (Red fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Vulpes. OX NCBI_TaxID=9627; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Silver; RX PubMed=15220384; DOI=10.1093/jhered/esh033; RA Kukekova A.V., Trut L.N., Oskina I.N., Kharlamova A.V., RA Shikhevich S.G., Kirkness E.F., Aguirre G.D., Acland G.M.; RT "A marker set for construction of a genetic map of the silver fox RT (Vulpes vulpes)."; RL J. Hered. 95:185-194(2004). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated (By similarity). CC -!- PTM: Palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY204571; AAP12468.1; -; Genomic_DNA. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 389 5-hydroxytryptamine 1B receptor. FT /FTId=PRO_0000068923. FT TOPO_DOM 1 50 Extracellular (Potential). FT TRANSMEM 51 74 1 (Potential). FT TOPO_DOM 75 85 Cytoplasmic (Potential). FT TRANSMEM 86 112 2 (Potential). FT TOPO_DOM 113 122 Extracellular (Potential). FT TRANSMEM 123 144 3 (Potential). FT TOPO_DOM 145 166 Cytoplasmic (Potential). FT TRANSMEM 167 186 4 (Potential). FT TOPO_DOM 187 207 Extracellular (Potential). FT TRANSMEM 208 227 5 (Potential). FT TOPO_DOM 228 314 Cytoplasmic (Potential). FT TRANSMEM 315 335 6 (Potential). FT TOPO_DOM 336 349 Extracellular (Potential). FT TRANSMEM 350 372 7 (Potential). FT TOPO_DOM 373 389 Cytoplasmic (Potential). FT LIPID 387 387 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 31 31 N-linked (GlcNAc...) (Potential). FT DISULFID 121 198 By similarity. SQ SEQUENCE 389 AA; 42990 MW; 43080C597CCB39E4 CRC64; MEDAGTPCAP PPPAGSQTGA PPANLSSAPH NCSAEGYIYQ DSIALPWKVL LAILLALLTL ATTLSNAFVI ATVYRTRKLH TPANYLIASL AVTDLLVSIL VMPISTMYAV TGRWTLGQVV CDLWLSSDIT CCTASILHLC VIALDRYWAI TDAVEYSAKR TPKRAAVMIA LVWVFSISIS LPPFFWRQAK AEEEVSDCVV NTDHILYTVY STVGAFYFPT LLLIALYGRI YVEARSRILK QTPNRTGKRL TRAQLITDSP GSTSSVTSVN SRAPDVPSES GSPVYVNQVK VRVSDALLEK KKLMAARERK ATKTLGIILG AFIVCWLPFF IISLVMPICK DACWFHLAIF DFFTWLGYLN SLINPIIYTM SNEDFKQAFH KLIRFKCAS // ID 5HT1D_CANFA Reviewed; 377 AA. AC P11614; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 20-FEB-2007, entry version 56. DE 5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D). GN Name=HTR1D; Synonyms=RDC4; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Thyroid; RX MEDLINE=89242119; PubMed=2541503; RA Libert F., Parmentier M., Lefort A., Dinsart C., van Sande J., RA Maenhaut C., Simons M.-J., Dumont J.E., Vassart G.; RT "Selective amplification and cloning of four new members of the G RT protein-coupled receptor family."; RL Science 244:569-572(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Thyroid; RX MEDLINE=90245610; PubMed=2159630; DOI=10.1093/nar/18.7.1916; RA Libert F., Parmentier M., Lefort A., Dumont J.E., Vassart G.; RT "Complete nucleotide sequence of a putative G protein coupled RT receptor: RDC4."; RL Nucleic Acids Res. 18:1916-1916(1990). RN [3] RP FUNCTION. RX MEDLINE=92062181; PubMed=1659418; RA Maenhaut C., van Sande J., Massart C., Dinsart C., Libert F., RA Monferini E., Giraldo E., Ladinsky H., Vassart G., Dumont J.E.; RT "The orphan receptor cDNA RDC4 encodes a 5-HT1D serotonin receptor."; RL Biochem. Biophys. Res. Commun. 180:1460-1468(1991). RN [4] RP FUNCTION. RX MEDLINE=92100052; PubMed=1758439; RA Zgombick J.M., Weinshank R.L., Macchi M., Schechter L.E., RA Branchek T.A., Hartig P.R.; RT "Expression and pharmacological characterization of a canine 5- RT hydroxytryptamine1D receptor subtype."; RL Mol. Pharmacol. 40:1036-1042(1991). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14049; CAA32207.1; -; mRNA. DR PIR; B30341; B30341. DR UniGene; Cfa.3821; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSCAFG00000013326; Canis familiaris. DR InterPro; IPR000505; 5HT1D_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00514; 5HT1DRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 377 5-hydroxytryptamine 1D receptor. FT /FTId=PRO_0000068925. FT TOPO_DOM 1 38 Extracellular (Potential). FT TRANSMEM 39 62 1 (Potential). FT TOPO_DOM 63 75 Cytoplasmic (Potential). FT TRANSMEM 76 98 2 (Potential). FT TOPO_DOM 99 108 Extracellular (Potential). FT TRANSMEM 109 134 3 (Potential). FT TOPO_DOM 135 154 Cytoplasmic (Potential). FT TRANSMEM 155 176 4 (Potential). FT TOPO_DOM 177 194 Extracellular (Potential). FT TRANSMEM 195 218 5 (Potential). FT TOPO_DOM 219 302 Cytoplasmic (Potential). FT TRANSMEM 303 326 6 (Potential). FT TOPO_DOM 327 335 Extracellular (Potential). FT TRANSMEM 336 360 7 (Potential). FT TOPO_DOM 361 377 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 111 188 By similarity. SQ SEQUENCE 377 AA; 41883 MW; 8E6406DCE2123EE4 CRC64; MSPPNQSLEG LLQEASNRSL NATETPEAWG PETLQALKIS LALLLSIITM ATALSNAFVL TTIFLTRKLH TPANYLIGSL AMTDLLVSIL VMPISIAYTT TRTWSFGQIL CDIWLSSDIT CCTASILHLC VIALDRYWAI TDALEYSKRR TAGRAAVMIA TVWVISICIS IPPLFWRQAK AQEDMSDCQV NTSQISYTIY STCGAFYIPS VLLIILYGRI YVAARNRILN PPSLYGKRFT TAQLITGSAG SSLCSLSPSL QEERSHAAGP PLFFNHVQVK LAEGVLERKR ISAARERKAT KTLGIILGAF IVCWLPFFVA SLVLPICRAS CWLHPALFDF FTWLGYLNSL INPIIYTVFN EEFRQAFQRV VHVRKAS // ID 5HT1D_CAVPO Reviewed; 376 AA. AC Q60484; O08891; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 31-OCT-2006, entry version 38. DE 5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D). GN Name=HTR1D; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Hartley; TISSUE=Brain; RX MEDLINE=97133356; PubMed=8978753; RA Wurch T., Palmier C., Colpaert F.C., Pauwels P.J.; RT "Sequence and functional analysis of cloned guinea pig and rat RT serotonin 5-HT1D receptors: common pharmacological features within the RT 5-HT1D receptor subfamily."; RL J. Neurochem. 68:410-418(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX MEDLINE=97368662; PubMed=9225276; DOI=10.1016/S0028-3908(97)00023-3; RA Zgombick J.M., Bard J.A., Kucharewicz S.A., Urquhart D.A., RA Weinshank R.L., Branchek T.A.; RT "Molecular cloning and pharmacological characterization of guinea pig RT 5-HT1B and 5-HT1D receptors."; RL Neuropharmacology 36:513-524(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X94436; CAA64210.1; -; Genomic_DNA. DR EMBL; U82174; AAB58499.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR000505; 5HT1D_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00514; 5HT1DRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 376 5-hydroxytryptamine 1D receptor. FT /FTId=PRO_0000068926. FT TOPO_DOM 1 38 Extracellular (Potential). FT TRANSMEM 39 62 1 (Potential). FT TOPO_DOM 63 75 Cytoplasmic (Potential). FT TRANSMEM 76 98 2 (Potential). FT TOPO_DOM 99 108 Extracellular (Potential). FT TRANSMEM 109 134 3 (Potential). FT TOPO_DOM 135 154 Cytoplasmic (Potential). FT TRANSMEM 155 176 4 (Potential). FT TOPO_DOM 177 194 Extracellular (Potential). FT TRANSMEM 195 218 5 (Potential). FT TOPO_DOM 219 301 Cytoplasmic (Potential). FT TRANSMEM 302 324 6 (Potential). FT TOPO_DOM 325 334 Extracellular (Potential). FT TRANSMEM 335 359 7 (Potential). FT TOPO_DOM 360 376 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 111 188 By similarity. FT CONFLICT 222 222 R -> A (in Ref. 2). SQ SEQUENCE 376 AA; 41769 MW; 531D4E1C2C819035 CRC64; MSPPNQSEEG LPQEASNRSL NATETPGDWD PGLLQALKVS LVVVLSIITL ATVLSNAFVL TTILLTRKLH TPANYLIGSL ATTDLLVSIL VMPISIAYTT TRTWNFGQIL CDIWVSSDIT CCTASILHLC VIALDRYWAI TDALEYSKRR TAGHAGAMIA AVWVISICIS IPPLFWRQAQ AQEEMSDCLV NTSQISYTIY STCGAFYIPS VLLIILYSRI YRAARSRILN PPSLSGKRFT TAHLITGSAG SSLCSLNPSL HEGHMHPGSP LFFNHVRIKL ADSVLERKRI SAARERKATK TLGIILGAFI VCWLPFFVVS LVLPICRDSC WIHPALFDFF TWLGYLNSLI NPIIYTVFNE DFRQAFQKVV HFRKAS // ID 5HT1D_FUGRU Reviewed; 379 AA. AC P79748; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 31-OCT-2006, entry version 39. DE 5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D) DE (5HT1D) (F1D). OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=97361762; PubMed=9218723; DOI=10.1016/S0378-1119(97)00064-4; RA Yamaguchi F., Brenner S.; RT "Molecular cloning of 5-hydroxytryptamine (5-HT) type 1 receptor genes RT from the Japanese puffer fish, Fugu rubripes."; RL Gene 191:219-223(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X83865; CAA58745.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR Ensembl; SINFRUG00000120815; Fugu rubripes. DR InterPro; IPR000505; 5HT1D_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00514; 5HT1DRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 379 5-hydroxytryptamine 1D receptor. FT /FTId=PRO_0000068932. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 60 1 (Potential). FT TOPO_DOM 61 73 Cytoplasmic (Potential). FT TRANSMEM 74 96 2 (Potential). FT TOPO_DOM 97 106 Extracellular (Potential). FT TRANSMEM 107 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 174 4 (Potential). FT TOPO_DOM 175 192 Extracellular (Potential). FT TRANSMEM 193 216 5 (Potential). FT TOPO_DOM 217 307 Cytoplasmic (Potential). FT TRANSMEM 308 331 6 (Potential). FT TOPO_DOM 332 339 Extracellular (Potential). FT TRANSMEM 340 364 7 (Potential). FT TOPO_DOM 365 379 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 14 14 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 109 186 By similarity. SQ SEQUENCE 379 AA; 42302 MW; 99B6E2C0379EBC78 CRC64; MELDNNSLDY FSSNFTDIPS NTTVAHWTEA TLLGLQISVS VVLAIVTLAT MLSNAFVIAT IFLTRKLHTP ANFLIGSLAV TDMLVSILVM PISIVYTVSK TWSLGQIVCD IWLSSDITFC TASILHLCVI ALDRYWAITD ALEYSKRRTM RRAAVMVAVV WVISISISMP PLFWRQAKAH EELKECMVNT DQISYTLYST FGAFYVPTVL LIILYGRIYV AARSRIFKTP SYSGKRFTTA QLIQTSAGSS LCSLNSASNQ EAHLHSGAGG EGGGSPLFVN SVKVKLADNV LERKRLCAAR ERKATKTLGI ILGAFIICWL PFFVVTLVWA ICKECSFDPL LFDVFTWLGY LNSLINPVIY TVFNDEFKQA FQKLIKFRR // ID 5HT1D_HUMAN Reviewed; 377 AA. AC P28221; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 23-JAN-2007, entry version 70. DE 5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D) (5- DE HT-1D-alpha). GN Name=HTR1D; Synonyms=HTR1DA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91342595; PubMed=1652050; RA Hamblin M.W., Metcalf M.A.; RT "Primary structure and functional characterization of a human 5-HT1D- RT type serotonin receptor."; RL Mol. Pharmacol. 40:143-148(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX MEDLINE=92228840; PubMed=1565658; RA Weinshank R.L., Zgombick J.M., Macchi M.J., Branchek T.A., RA Hartig P.R.; RT "Human serotonin 1D receptor is encoded by a subfamily of two distinct RT genes: 5-HT1D alpha and 5-HT1D beta."; RL Proc. Natl. Acad. Sci. U.S.A. 89:3630-3634(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., RA Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] 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 [7] RP VARIANT LEU-265. RX MEDLINE=99318093; PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [8] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M89955; AAA35491.1; -; Genomic_DNA. DR EMBL; M81589; AAA60315.1; -; mRNA. DR EMBL; AF498979; AAM21126.1; -; mRNA. DR EMBL; BT007027; AAP35673.1; -; mRNA. DR EMBL; AL049576; CAB81617.1; -; Genomic_DNA. DR EMBL; BC007720; AAH07720.1; -; mRNA. DR PIR; A53279; A53279. DR UniGene; Hs.121482; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000179546; Homo sapiens. DR KEGG; hsa:3352; -. DR H-InvDB; HIX0000241; -. DR HGNC; HGNC:5289; HTR1D. DR MIM; 182133; gene. DR DrugBank; APRD00169; Almotriptan. DR DrugBank; APRD00476; Dihydroergotamine. DR DrugBank; APRD00945; Eletriptan. DR DrugBank; APRD00270; Frovatriptan. DR DrugBank; APRD00220; Naratriptan. DR DrugBank; APRD00008; Rizatriptan. DR DrugBank; APRD00379; Sumatriptan. DR DrugBank; APRD00096; Tegaserod. DR DrugBank; APRD00540; Ziprasidone. DR DrugBank; APRD00376; Zolmitriptan. DR LinkHub; P28221; -. DR ArrayExpress; P28221; -. DR GermOnline; ENSG00000179546; Homo sapiens. DR RZPD-ProtExp; A0435; -. DR RZPD-ProtExp; RZPDo834G0147; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004993; F:serotonin receptor activity; TAS:ProtInc. DR GO; GO:0007187; P:G-protein signaling, coupled to cyclic nucl...; TAS:ProtInc. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR InterPro; IPR000505; 5HT1D_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00514; 5HT1DRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 377 5-hydroxytryptamine 1D receptor. FT /FTId=PRO_0000068927. FT TOPO_DOM 1 38 Extracellular (Potential). FT TRANSMEM 39 62 1 (Potential). FT TOPO_DOM 63 75 Cytoplasmic (Potential). FT TRANSMEM 76 98 2 (Potential). FT TOPO_DOM 99 108 Extracellular (Potential). FT TRANSMEM 109 134 3 (Potential). FT TOPO_DOM 135 154 Cytoplasmic (Potential). FT TRANSMEM 155 176 4 (Potential). FT TOPO_DOM 177 194 Extracellular (Potential). FT TRANSMEM 195 218 5 (Potential). FT TOPO_DOM 219 302 Cytoplasmic (Potential). FT TRANSMEM 303 326 6 (Potential). FT TOPO_DOM 327 335 Extracellular (Potential). FT TRANSMEM 336 360 7 (Potential). FT TOPO_DOM 361 377 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 111 188 By similarity. FT VARIANT 265 265 S -> L (in dbSNP:rs6299). FT /FTId=VAR_011834. SQ SEQUENCE 377 AA; 41907 MW; 0A4FCF81FFE2322A CRC64; MSPLNQSAEG LPQEASNRSL NATETSEAWD PRTLQALKIS LAVVLSVITL ATVLSNAFVL TTILLTRKLH TPANYLIGSL ATTDLLVSIL VMPISIAYTI THTWNFGQIL CDIWLSSDIT CCTASILHLC VIALDRYWAI TDALEYSKRR TAGHAATMIA IVWAISICIS IPPLFWRQAK AQEEMSDCLV NTSQISYTIY STCGAFYIPS VLLIILYGRI YRAARNRILN PPSLYGKRFT TAHLITGSAG SSLCSLNSSL HEGHSHSAGS PLFFNHVKIK LADSALERKR ISAARERKAT KILGIILGAF IICWLPFFVV SLVLPICRDS CWIHPALFDF FTWLGYLNSL INPIIYTVFN EEFRQAFQKI VPFRKAS // ID 5HT1D_MOUSE Reviewed; 374 AA. AC Q61224; Q61615; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-FEB-2007, entry version 53. DE 5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D). GN Name=Htr1d; Synonyms=Gpcr14; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NMRI; TISSUE=Brain; RX MEDLINE=97133356; PubMed=8978753; RA Wurch T., Palmier C., Colpaert F.C., Pauwels P.J.; RT "Sequence and functional analysis of cloned guinea pig and rat RT serotonin 5-HT1D receptors: common pharmacological features within the RT 5-HT1D receptor subfamily."; RL J. Neurochem. 68:410-418(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 135-306. RC TISSUE=Testis; RX MEDLINE=94116980; PubMed=8288218; RA Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I., RA Copeland N.G., Jenkins N.A.; RT "Identification, chromosomal location, and genome organization of RT mammalian G-protein-coupled receptors."; RL Genomics 18:175-184(1993). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X94908; CAA64395.1; -; Genomic_DNA. DR EMBL; L20335; AAA16847.1; -; mRNA. DR PIR; F48909; F48909. DR UniGene; Mm.40573; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSMUSG00000036956; Mus musculus. DR KEGG; mmu:15552; -. DR MGI; MGI:96276; Htr1d. DR ArrayExpress; Q61224; -. DR GermOnline; ENSMUSG00000070687; Mus musculus. DR InterPro; IPR000505; 5HT1D_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00514; 5HT1DRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 374 5-hydroxytryptamine 1D receptor. FT /FTId=PRO_0000068928. FT TOPO_DOM 1 35 Extracellular (Potential). FT TRANSMEM 36 59 1 (Potential). FT TOPO_DOM 60 72 Cytoplasmic (Potential). FT TRANSMEM 73 95 2 (Potential). FT TOPO_DOM 96 105 Extracellular (Potential). FT TRANSMEM 106 131 3 (Potential). FT TOPO_DOM 132 151 Cytoplasmic (Potential). FT TRANSMEM 152 173 4 (Potential). FT TOPO_DOM 174 191 Extracellular (Potential). FT TRANSMEM 192 215 5 (Potential). FT TOPO_DOM 216 299 Cytoplasmic (Potential). FT TRANSMEM 300 323 6 (Potential). FT TOPO_DOM 324 332 Extracellular (Potential). FT TRANSMEM 333 357 7 (Potential). FT TOPO_DOM 358 374 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 108 185 By similarity. SQ SEQUENCE 374 AA; 41540 MW; 1FC6ABF901785D88 CRC64; MSLPNQSLEG LPQEASNRSL NATGAWDPEV LQALRISLVV VLSVITLATV LSNAFVLTTI LLTKKLHTPA NYLIGSLATT DLLVSILVMP ISIAYTTTRT WNFGQILCDI WVSSDITCCT ASILHLCVIA LDRYWAITDA LEYSKRRTAG HAAAMIAAVW IISICISIPP LFWRQATAHE EMSDCLVNTS QISYTIYSTC GAFYIPSILL IILYGRIYVA ARSRILNPPS LYGKRFTTAQ LITGSAGSSL CSLNPSLHES HTHTVGSPLF FNQVKIKLAD SILERKRISA ARERKATKTL GIILGAFIIC WLPFFVVSLV LPICRDSCWI HPALFDFFTW LGYLNSLINP VIYTVFNEDF RQAFQKVVHF RKAS // ID 5HT1D_PIG Reviewed; 291 AA. AC P79400; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 20-FEB-2007, entry version 40. DE 5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D) (5- DE HT1D) (Fragment). GN Name=HTR1D; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain cortex; RA Wurch T., Lestienne F., Colpaert F.C., Pauwels P.J.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y11868; CAA72616.1; -; mRNA. DR UniGene; Ssc.15993; -. DR HSSP; P08913; 1HLL. DR InterPro; IPR000505; 5HT1D_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00514; 5HT1DRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN <1 >291 5-hydroxytryptamine 1D receptor. FT /FTId=PRO_0000068929. FT TRANSMEM <1 18 2 (Potential). FT TOPO_DOM 19 28 Extracellular (Potential). FT TRANSMEM 29 54 3 (Potential). FT TOPO_DOM 55 74 Cytoplasmic (Potential). FT TRANSMEM 75 96 4 (Potential). FT TOPO_DOM 97 114 Extracellular (Potential). FT TRANSMEM 115 138 5 (Potential). FT TOPO_DOM 139 222 Cytoplasmic (Potential). FT TRANSMEM 223 246 6 (Potential). FT TOPO_DOM 247 255 Extracellular (Potential). FT TRANSMEM 256 280 7 (Potential). FT TOPO_DOM 281 >291 Cytoplasmic (Potential). FT CARBOHYD 111 111 N-linked (GlcNAc...) (Potential). FT DISULFID 31 108 By similarity. FT NON_TER 1 1 FT NON_TER 291 291 SQ SEQUENCE 291 AA; 32669 MW; 71E798F3652651CB CRC64; AMTDLLVSIL VMPISIPYTI TQTWSFGQLL CDIWLSSDIT CCTASILHLC VIALDRYWAI TDALEYSKRR TAGHAAAMIA IVWAISICIS IPPLFWRQAR AHEEISDCLV NTSQISYTIY STCGAFYIPS LLLIILYGRI YRAARNRILN PPSLYGKRFT TAHLITGSAG SSLCSLNPSL HEGHSHSAGS PLFFNHVKIK LADSVLERKR ISAARERKAT KTLGIILGAF IICWLPFFVA SLVLPICRDS CWIHPALFDF FTWLGYLNSL INPIIYTVFN EEFRQAFQKV V // ID 5HT1D_RABIT Reviewed; 377 AA. AC P49145; O02823; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 31-OCT-2006, entry version 42. DE 5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D) (5- DE HT-1D-alpha). GN Name=HTR1D; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX MEDLINE=96130324; PubMed=8543023; DOI=10.1016/0014-5793(95)01308-3; RA Harwood G.S., Lockyer M., Giles H., Fairweather N.; RT "Cloning and characterisation of the rabbit 5-HT1D alpha and 5-HT1D RT beta receptors."; RL FEBS Lett. 377:73-76(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=New Zealand white; RX MEDLINE=97032156; PubMed=8878052; DOI=10.1007/BF00171053; RA Bard J.A., Kucharewicz S.A., Zgombick J.M., Weinshank R.L., RA Branchek T.A., Cohen M.L.; RT "Differences in ligand binding profiles between cloned rabbit and RT human 5-HT1D alpha and 5-HT1D beta receptors: ketanserin and RT methiothepin distinguish rabbit 5-HT1D receptor subtypes."; RL Naunyn Schmiedebergs Arch. Pharmacol. 354:237-244(1996). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z50162; CAA90530.1; -; Genomic_DNA. DR EMBL; U60825; AAB58466.1; -; Genomic_DNA. DR PIR; S68423; S68423. DR HSSP; P08913; 1HLL. DR InterPro; IPR000505; 5HT1D_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00514; 5HT1DRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 377 5-hydroxytryptamine 1D receptor. FT /FTId=PRO_0000068930. FT TOPO_DOM 1 38 Extracellular (Potential). FT TRANSMEM 39 62 1 (Potential). FT TOPO_DOM 63 75 Cytoplasmic (Potential). FT TRANSMEM 76 98 2 (Potential). FT TOPO_DOM 99 108 Extracellular (Potential). FT TRANSMEM 109 134 3 (Potential). FT TOPO_DOM 135 154 Cytoplasmic (Potential). FT TRANSMEM 155 176 4 (Potential). FT TOPO_DOM 177 194 Extracellular (Potential). FT TRANSMEM 195 218 5 (Potential). FT TOPO_DOM 219 302 Cytoplasmic (Potential). FT TRANSMEM 303 326 6 (Potential). FT TOPO_DOM 327 335 Extracellular (Potential). FT TRANSMEM 336 360 7 (Potential). FT TOPO_DOM 361 377 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 111 188 By similarity. FT CONFLICT 28 28 A -> I (in Ref. 2). SQ SEQUENCE 377 AA; 41500 MW; FC1441678AB82B0A CRC64; MSPSNQSAEG LPQEAANRSL NATGTPEAWD PGTLQALKIS LAVVLSIITV ATVLSNTFVL TTILLTRKLH TPANYLIGSL ATTDLLVSIL VMPISIAYTI THTWNFGQVL CDIWVSSDIT CCTASILHLC VIALDRYWAI TDALEYSKRR TAGHAAAMIA VVWAISICIS IPPLFWRQAK AHEEVSDCLV NTSQISYTIY STCGAFYIPS VLLIVLYGRI YMAARNRILN PPSLYGKRFT TAHLITGSAG SSLCSLSPSL GEGHSHSAGS PLFFNPVRIK LADSVLERKR ISAARERKAT KTLGIILGAF IGCWLPFFVA SLVLPICRDS CWMPPGLFDF FTWLGYLNSL INPIIYTVFN EDFRQAFQRV IHFRKAF // ID 5HT1D_RAT Reviewed; 374 AA. AC P28565; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 23-JAN-2007, entry version 49. DE 5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D). GN Name=Htr1d; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Hamblin M.W., McGuffin R.W., Metcalf M.A., Dorsa D.M., Merchant K.M.; RT "Distinct 5-HT1B and 5-HT1D serotonin receptors in rat: structural and RT pharmacological comparison of the two cloned receptors."; RL Mol. Cell. Neurosci. 3:578-587(1992). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M89953; AAA40614.1; -; Genomic_DNA. DR PIR; I77467; I77467. DR UniGene; Rn.34834; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSRNOG00000012038; Rattus norvegicus. DR KEGG; rno:25323; -. DR RGD; 2847; Htr1d. DR ArrayExpress; P28565; -. DR GermOnline; ENSRNOG00000012038; Rattus norvegicus. DR InterPro; IPR000505; 5HT1D_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00514; 5HT1DRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 374 5-hydroxytryptamine 1D receptor. FT /FTId=PRO_0000068931. FT TOPO_DOM 1 35 Extracellular (Potential). FT TRANSMEM 36 59 1 (Potential). FT TOPO_DOM 60 72 Cytoplasmic (Potential). FT TRANSMEM 73 95 2 (Potential). FT TOPO_DOM 96 105 Extracellular (Potential). FT TRANSMEM 106 131 3 (Potential). FT TOPO_DOM 132 151 Cytoplasmic (Potential). FT TRANSMEM 152 173 4 (Potential). FT TOPO_DOM 174 191 Extracellular (Potential). FT TRANSMEM 192 215 5 (Potential). FT TOPO_DOM 216 299 Cytoplasmic (Potential). FT TRANSMEM 300 323 6 (Potential). FT TOPO_DOM 324 332 Extracellular (Potential). FT TRANSMEM 333 357 7 (Potential). FT TOPO_DOM 358 374 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 108 185 By similarity. SQ SEQUENCE 374 AA; 41540 MW; 345CBD528317DA21 CRC64; MSLPNQSLEG LPQEASNRSL NATGAWDPEV LQALRISLVV VLSIITLATV LSNAFVLTTI LLTKKLHTPA NYLIGSLATT DLLVSILVMP ISIAYTTTRT WNFGQILCDI WVSSDITCCT ASILHLCVIA LDRYWAITDA LEYSKRRTAG HAAAMIAAVW AISICISIPP LFWRQATAHE EMSDCLVNTS QISYTIYSTC GAFYIPSILL IILYGRIYVA ARSRILNPPS LYGKRFTTAQ LITGSAGSSL CSLNPSLHES HTHTVGSPLF FNQVKIKLAD SILERKRISA ARERKATKTL GIILGAFIIC WLPFFVVSLV LPICRDSCWI HPALFDFFTW LGYLNSLINP VIYTVFNEDF RQAFQRVVHF RKAS // ID 5HT1E_HUMAN Reviewed; 365 AA. AC P28566; Q9P1Y1; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 06-FEB-2007, entry version 70. DE 5-hydroxytryptamine 1E receptor (5-HT-1E) (Serotonin receptor 1E) (5- DE HT1E) (S31). GN Name=HTR1E; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=92302274; PubMed=1608964; RA McAllister G., Charlesworth A., Snodin C., Beer M.S., Noble A.J., RA Middlemiss D.N., Iversen L.L., Whiting P.; RT "Molecular cloning of a serotonin receptor from human brain (5HT1E): a RT fifth 5HT1-like subtype."; RL Proc. Natl. Acad. Sci. U.S.A. 89:5517-5521(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92128546; PubMed=1733778; DOI=10.1016/0014-5793(92)80379-U; RA Levy F.O., Gudermann T., Birnbaumer M., Kaumann A.J., Birnbaumer L.; RT "Molecular cloning of a human gene (S31) encoding a novel serotonin RT receptor mediating inhibition of adenylyl cyclase."; RL FEBS Lett. 296:201-206(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92382553; PubMed=1513320; RA Zgombick J.M., Schechter L.E., Macchi M., Hartig P.R., Branchek T.A., RA Weinshank R.L.; RT "Human gene S31 encodes the pharmacologically defined serotonin 5- RT hydroxytryptamine1E receptor."; RL Mol. Pharmacol. 42:180-185(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-363. RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP VARIANT PHE-262. RX MEDLINE=99318093; PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [9] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M91467; AAA58353.1; -; mRNA. DR EMBL; Z11166; CAA77558.1; -; Genomic_DNA. DR EMBL; M92826; AAA58355.1; -; Genomic_DNA. DR EMBL; AF498980; AAM21127.1; -; mRNA. DR EMBL; AL157777; CAC10582.1; -; Genomic_DNA. DR EMBL; BC069751; AAH69751.1; -; mRNA. DR EMBL; AB041373; BAA94458.1; -; Genomic_DNA. DR PIR; S20579; A45260. DR UniGene; Hs.1611; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000168830; Homo sapiens. DR KEGG; hsa:3354; -. DR HGNC; HGNC:5291; HTR1E. DR MIM; 182132; gene. DR DrugBank; APRD00945; Eletriptan. DR ArrayExpress; P28566; -. DR GermOnline; ENSG00000168830; Homo sapiens. DR RZPD-ProtExp; A0398; -. DR RZPD-ProtExp; RZPDo834G0446; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004993; F:serotonin receptor activity; TAS:ProtInc. DR GO; GO:0007187; P:G-protein signaling, coupled to cyclic nucl...; TAS:ProtInc. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR InterPro; IPR000450; 5HT1F_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00515; 5HT1FRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 365 5-hydroxytryptamine 1E receptor. FT /FTId=PRO_0000068933. FT TOPO_DOM 1 22 Extracellular (Potential). FT TRANSMEM 23 47 1 (Potential). FT TOPO_DOM 48 59 Cytoplasmic (Potential). FT TRANSMEM 60 81 2 (Potential). FT TOPO_DOM 82 96 Extracellular (Potential). FT TRANSMEM 97 118 3 (Potential). FT TOPO_DOM 119 138 Cytoplasmic (Potential). FT TRANSMEM 139 159 4 (Potential). FT TOPO_DOM 160 179 Extracellular (Potential). FT TRANSMEM 180 201 5 (Potential). FT TOPO_DOM 202 291 Cytoplasmic (Potential). FT TRANSMEM 292 314 6 (Potential). FT TOPO_DOM 315 324 Extracellular (Potential). FT TRANSMEM 325 347 7 (Potential). FT TOPO_DOM 348 365 Cytoplasmic (Potential). FT CARBOHYD 2 2 N-linked (GlcNAc...) (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT DISULFID 95 173 By similarity. FT VARIANT 208 208 A -> T (in dbSNP:rs3828741). FT /FTId=VAR_022061. FT VARIANT 262 262 S -> F (in dbSNP:rs6303). FT /FTId=VAR_014165. SQ SEQUENCE 365 AA; 41682 MW; 4C31DD783A3F7483 CRC64; MNITNCTTEA SMAIRPKTIT EKMLICMTLV VITTLTTLLN LAVIMAIGTT KKLHQPANYL ICSLAVTDLL VAVLVMPLSI IYIVMDRWKL GYFLCEVWLS VDMTCCTCSI LHLCVIALDR YWAITNAIEY ARKRTAKRAA LMILTVWTIS IFISMPPLFW RSHRRLSPPP SQCTIQHDHV IYTIYSTLGA FYIPLTLILI LYYRIYHAAK SLYQKRGSSR HLSNRSTDSQ NSFASCKLTQ TFCVSDFSTS DPTTEFEKFH ASIRIPPFDN DLDHPGERQQ ISSTRERKAA RILGLILGAF ILSWLPFFIK ELIVGLSIYT VSSEVADFLT WLGYVNSLIN PLLYTSFNED FKLAFKKLIR CREHT // ID 5HT1E_PANTR Reviewed; 363 AA. AC Q9N2B6; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 31-OCT-2006, entry version 34. DE 5-hydroxytryptamine 1E receptor (5-HT-1E) (Serotonin receptor 1E) DE (Fragment). GN Name=HTR1E; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Isolate 220; RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041374; BAA94459.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR KEGG; ptr:472064; -. DR InterPro; IPR000450; 5HT1F_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00515; 5HT1FRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 >363 5-hydroxytryptamine 1E receptor. FT /FTId=PRO_0000068934. FT TOPO_DOM 1 22 Extracellular (Potential). FT TRANSMEM 23 47 1 (Potential). FT TOPO_DOM 48 59 Cytoplasmic (Potential). FT TRANSMEM 60 81 2 (Potential). FT TOPO_DOM 82 96 Extracellular (Potential). FT TRANSMEM 97 118 3 (Potential). FT TOPO_DOM 119 138 Cytoplasmic (Potential). FT TRANSMEM 139 159 4 (Potential). FT TOPO_DOM 160 179 Extracellular (Potential). FT TRANSMEM 180 201 5 (Potential). FT TOPO_DOM 202 291 Cytoplasmic (Potential). FT TRANSMEM 292 314 6 (Potential). FT TOPO_DOM 315 324 Extracellular (Potential). FT TRANSMEM 325 347 7 (Potential). FT TOPO_DOM 348 >363 Cytoplasmic (Potential). FT CARBOHYD 2 2 N-linked (GlcNAc...) (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT DISULFID 95 173 By similarity. FT NON_TER 363 363 SQ SEQUENCE 363 AA; 41444 MW; 7D783A3F74832C8E CRC64; MNITNCTTEA SMAIRPKTIT EKMLICMTLV VITTLTTLLN LAVIMAIGTT KKLHQPANYL ICSLAVTDLL VAVLVMPLSI IYIVMDRWKL GYFLCEVWLS VDMTCCTCSI LHLCVIALDR YWAITNAIEY ARKRTAKRAA LMILTVWTIS IFISMPPLFW RSHRRLSPPP SQCTIQHDHV IYTIYSTLGA FYIPLTLILI LYYRIYHAAK SLYQKRGSSR HLSNRSTDSQ NSFASCKLTQ TFCVSDFSTS DPTTEFEKFH ASIRIPPFDN DLDHPGERQQ ISSTRERKAA RILGLILGAF ILSWLPFFIK ELIVGLSIYT VSSEVADFLT WLGYVNSLIN PLLYTSFNED FKLAFKKLIR CRE // ID 5HT1E_PIG Reviewed; 149 AA. AC Q29003; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 36. DE 5-hydroxytryptamine 1E receptor (5-HT-1E) (Serotonin receptor 1E) (5- DE HT1E) (Fragment). GN Name=HTR1E; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95385798; PubMed=7656980; DOI=10.1016/0014-5793(95)00828-W; RA Ullmer C., Schmuck K., Kalkman H.O., Luebbert H.; RT "Expression of serotonin receptor mRNAs in blood vessels."; RL FEBS Lett. 370:215-221(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z48151; CAA88168.1; -; Genomic_DNA. DR PIR; S66490; S66490. DR HSSP; P08913; 1HLL. DR InterPro; IPR000450; 5HT1F_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Membrane; Receptor; Transducer; KW Transmembrane. FT CHAIN <1 >149 5-hydroxytryptamine 1E receptor. FT /FTId=PRO_0000068935. FT TOPO_DOM <1 6 Cytoplasmic (Potential). FT TRANSMEM 7 28 2 (Potential). FT TOPO_DOM 29 43 Extracellular (Potential). FT TRANSMEM 44 65 3 (Potential). FT TOPO_DOM 66 85 Cytoplasmic (Potential). FT TRANSMEM 86 106 4 (Potential). FT TOPO_DOM 107 126 Extracellular (Potential). FT TRANSMEM 127 148 5 (Potential). FT TOPO_DOM 149 >149 Cytoplasmic (Potential). FT DISULFID 42 120 By similarity. FT NON_TER 1 1 FT NON_TER 149 149 SQ SEQUENCE 149 AA; 17116 MW; 67BCFEE083E41721 CRC64; HQPANYLICS LAVTDLLVAV LVMPLSIMYI VMDSWRLGYF ICEVWLSVDM TCCTCSILHL CVIALDRYWA ITNAIEYARK RTAKRAGLMI LTVWTISIFI SMPPLFWRSH RQLSPPPSQC AIQHDHVIYT IYSTLGAFYI PLTLILILY // ID 5HT1F_CAVPO Reviewed; 366 AA. AC O08890; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 31-OCT-2006, entry version 36. DE 5-hydroxytryptamine 1F receptor (5-HT-1F) (Serotonin receptor 1F) (5- DE HT1F). GN Name=HTR1F; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX MEDLINE=97368668; PubMed=9225282; DOI=10.1016/S0028-3908(97)00020-8; RA Adham N., Bard J.A., Zgombick J.M., Durkin M.M., Kucharewicz S., RA Weinshank R.L., Branchek T.A.; RT "Cloning and characterization of the guinea pig 5-HT1F receptor RT subtype: a comparison of the pharmacological profile to the human RT species homolog."; RL Neuropharmacology 36:569-576(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U80852; AAB58496.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR000450; 5HT1F_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00515; 5HT1FRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 366 5-hydroxytryptamine 1F receptor. FT /FTId=PRO_0000068936. FT TOPO_DOM 1 23 Extracellular (Potential). FT TRANSMEM 24 48 1 (Potential). FT TOPO_DOM 49 60 Cytoplasmic (Potential). FT TRANSMEM 61 83 2 (Potential). FT TOPO_DOM 84 94 Extracellular (Potential). FT TRANSMEM 95 119 3 (Potential). FT TOPO_DOM 120 139 Cytoplasmic (Potential). FT TRANSMEM 140 161 4 (Potential). FT TOPO_DOM 162 178 Extracellular (Potential). FT TRANSMEM 179 202 5 (Potential). FT TOPO_DOM 203 291 Cytoplasmic (Potential). FT TRANSMEM 292 314 6 (Potential). FT TOPO_DOM 315 327 Extracellular (Potential). FT TRANSMEM 328 351 7 (Potential). FT TOPO_DOM 352 366 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT DISULFID 96 172 By similarity. SQ SEQUENCE 366 AA; 41839 MW; FE4200E2DA26C9C3 CRC64; MDFLNSSDQN LTSEELLHRM PSKILVSLTL SGLALMTTTI NSLVIAAIIV TRKLHHPANY LICSLAVTDF LVAVLVMPFS IVYIVRESWI MGQVLCDIWL SVDIICCTCS ILHLSAIALD RYRAITDAVE YARKRTPKQA GIMITIVWII SVFISMPPLF WRHQGTSRDD ECIIKHDHIV STIYSTFGAF YIPLVLILIL YYKIYKAAKT LYHKRQASRI AKEELNGQVL LESGEKSIKM VSTTYVPEKS LSDPSTDFDK IHNTVKSPRC KLRHEKSWRR QKISGTRERK AATTLGLILG AFVICWLPFF VKELVVNVCE KCKISEEMAN FLAWLGYLNS LINPLIYTIF NEDFKKAFQK LVRCQY // ID 5HT1F_HUMAN Reviewed; 366 AA. AC P30939; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 23-JAN-2007, entry version 58. DE 5-hydroxytryptamine 1F receptor (5-HT-1F) (Serotonin receptor 1F). GN Name=HTR1F; Synonyms=HTR1EL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93211926; PubMed=8384716; RA Lovenberg T.W., Erlander M.G., Baron B.M., Racke M., Slone A.L., RA Siegel B.W., Craft C.M., Burns J.E., Danielson P.E., Sutcliffe G.J.; RT "Molecular cloning and functional expression of 5-HT1E-like rat and RT human 5-hydroxytryptamine receptor genes."; RL Proc. Natl. Acad. Sci. U.S.A. 90:2184-2188(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93133800; PubMed=8380639; RA Adham N., Kao H.-T., Schechter L.E., Bard J., Olsen M., Urquhart D., RA Durkin M., Hartig P.R., Winshank R.L., Branchek T.A.; RT "Cloning of another human serotonin receptor (5-HT1F): a fifth 5-HT1 RT receptor subtype coupled to the inhibition of adenylate cyclase."; RL Proc. Natl. Acad. Sci. U.S.A. 90:408-412(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) 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). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L05597; AAA36605.1; -; Genomic_DNA. DR EMBL; L04962; AAA36646.1; -; Genomic_DNA. DR EMBL; AF498981; AAM21128.1; -; mRNA. DR EMBL; BC069125; AAH69125.1; -; mRNA. DR PIR; A47321; A47321. DR UniGene; Hs.248136; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000179097; Homo sapiens. DR KEGG; hsa:3355; -. DR HGNC; HGNC:5292; HTR1F. DR MIM; 182134; gene. DR DrugBank; APRD00945; Eletriptan. DR ArrayExpress; P30939; -. DR GermOnline; ENSG00000179097; Homo sapiens. DR RZPD-ProtExp; A0549; -. DR RZPD-ProtExp; RZPDo834G0947; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004993; F:serotonin receptor activity; TAS:ProtInc. DR GO; GO:0007187; P:G-protein signaling, coupled to cyclic nucl...; TAS:ProtInc. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR InterPro; IPR000450; 5HT1F_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00515; 5HT1FRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 366 5-hydroxytryptamine 1F receptor. FT /FTId=PRO_0000068937. FT TOPO_DOM 1 23 Extracellular (Potential). FT TRANSMEM 24 48 1 (Potential). FT TOPO_DOM 49 60 Cytoplasmic (Potential). FT TRANSMEM 61 83 2 (Potential). FT TOPO_DOM 84 94 Extracellular (Potential). FT TRANSMEM 95 119 3 (Potential). FT TOPO_DOM 120 139 Cytoplasmic (Potential). FT TRANSMEM 140 161 4 (Potential). FT TOPO_DOM 162 178 Extracellular (Potential). FT TRANSMEM 179 202 5 (Potential). FT TOPO_DOM 203 291 Cytoplasmic (Potential). FT TRANSMEM 292 314 6 (Potential). FT TOPO_DOM 315 327 Extracellular (Potential). FT TRANSMEM 328 351 7 (Potential). FT TOPO_DOM 352 366 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT DISULFID 96 172 By similarity. SQ SEQUENCE 366 AA; 41709 MW; 16EA80344793B54F CRC64; MDFLNSSDQN LTSEELLNRM PSKILVSLTL SGLALMTTTI NSLVIAAIIV TRKLHHPANY LICSLAVTDF LVAVLVMPFS IVYIVRESWI MGQVVCDIWL SVDITCCTCS ILHLSAIALD RYRAITDAVE YARKRTPKHA GIMITIVWII SVFISMPPLF WRHQGTSRDD ECIIKHDHIV STIYSTFGAF YIPLALILIL YYKIYRAAKT LYHKRQASRI AKEEVNGQVL LESGEKSTKS VSTSYVLEKS LSDPSTDFDK IHSTVRSLRS EFKHEKSWRR QKISGTRERK AATTLGLILG AFVICWLPFF VKELVVNVCD KCKISEEMSN FLAWLGYLNS LINPLIYTIF NEDFKKAFQK LVRCRC // ID 5HT1F_MOUSE Reviewed; 366 AA. AC Q02284; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 23-JAN-2007, entry version 51. DE 5-hydroxytryptamine 1F receptor (5-HT-1F) (Serotonin receptor 1F) (5- DE HT-1E-beta). GN Name=Htr1f; Synonyms=5ht1f, Htr1eb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93015822; PubMed=1328180; RA Amlaiky N., Ramboz S., Boschert U., Plassat J.-L., Hen R.; RT "Isolation of a mouse '5HT1E-like' serotonin receptor expressed RT predominantly in hippocampus."; RL J. Biol. Chem. 267:19761-19764(1992). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z14224; CAA78593.1; -; mRNA. DR PIR; S26048; S26048. DR UniGene; Mm.5040; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSMUSG00000050783; Mus musculus. DR KEGG; mmu:15557; -. DR MGI; MGI:99842; Htr1f. DR ArrayExpress; Q02284; -. DR GermOnline; ENSMUSG00000050783; Mus musculus. DR InterPro; IPR000450; 5HT1F_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00515; 5HT1FRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 366 5-hydroxytryptamine 1F receptor. FT /FTId=PRO_0000068938. FT TOPO_DOM 1 23 Extracellular (Potential). FT TRANSMEM 24 48 1 (Potential). FT TOPO_DOM 49 60 Cytoplasmic (Potential). FT TRANSMEM 61 83 2 (Potential). FT TOPO_DOM 84 94 Extracellular (Potential). FT TRANSMEM 95 119 3 (Potential). FT TOPO_DOM 120 139 Cytoplasmic (Potential). FT TRANSMEM 140 161 4 (Potential). FT TOPO_DOM 162 178 Extracellular (Potential). FT TRANSMEM 179 202 5 (Potential). FT TOPO_DOM 203 291 Cytoplasmic (Potential). FT TRANSMEM 292 314 6 (Potential). FT TOPO_DOM 315 327 Extracellular (Potential). FT TRANSMEM 328 351 7 (Potential). FT TOPO_DOM 352 366 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT DISULFID 96 172 By similarity. SQ SEQUENCE 366 AA; 41977 MW; 69EC1CD6F22BD93F CRC64; MDFLNASDQN LTSEELLNRM PSKILVSLTL SGLALMTTTI NSLVIAAIIV TRKLHHPANY LICSLAVTDF LVAVLVMPFS IVYIVRESWI MGQVLCDIWL SVDIICCTCS ILHLSAIALD RYRAITDAVE YARKRTPRHA GIMITIVWVI SVFISMPPLF WRHQGTSRDD ECVIKHDHIV STIYSTFGAF YIPLVLILIL YYKIYRAART LYHKRQASRM IKEELNGQVF LESGEKSIKL VSTSYMLEKS LSDPSTDFDR IHSTVKSPRS ELKHEKSWRR QKISGTRERK AATTLGLILG AFVICWLPFF VKELVVNVCE KCKISEEMSN FLAWLGYLNS LINPLIYTIF NEDFKKAFQK LVRCRY // ID 5HT1F_PANTR Reviewed; 365 AA. AC Q9N2D9; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 31-OCT-2006, entry version 33. DE 5-hydroxytryptamine 1F receptor (5-HT-1F) (Serotonin receptor 1F) DE (Fragment). GN Name=HTR1F; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Isolate 220; RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB037534; BAA90454.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR KEGG; ptr:470863; -. DR InterPro; IPR000450; 5HT1F_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00515; 5HT1FRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 >365 5-hydroxytryptamine 1F receptor. FT /FTId=PRO_0000068939. FT TOPO_DOM 1 23 Extracellular (Potential). FT TRANSMEM 24 48 1 (Potential). FT TOPO_DOM 49 60 Cytoplasmic (Potential). FT TRANSMEM 61 83 2 (Potential). FT TOPO_DOM 84 94 Extracellular (Potential). FT TRANSMEM 95 119 3 (Potential). FT TOPO_DOM 120 139 Cytoplasmic (Potential). FT TRANSMEM 140 161 4 (Potential). FT TOPO_DOM 162 178 Extracellular (Potential). FT TRANSMEM 179 202 5 (Potential). FT TOPO_DOM 203 291 Cytoplasmic (Potential). FT TRANSMEM 292 314 6 (Potential). FT TOPO_DOM 315 327 Extracellular (Potential). FT TRANSMEM 328 351 7 (Potential). FT TOPO_DOM 352 >365 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT DISULFID 96 172 By similarity. FT NON_TER 365 365 SQ SEQUENCE 365 AA; 41605 MW; 86BB944230134CFE CRC64; MDFLNSSDQN LTSEELLNRM PSKILVSLTL SGLALMTTTI NSLVIAAIIV TRKLHHPANY LICSLAVTDF LVAVLVMPFS IVYIVRESWI MGQVVCDIWL SVDITCCTCS ILHLSAIALD RYRAITDAVE YARKRTPKHA GIMITIVWII SVFISMPPLF WRHQGTSRDD ECIIKHBHIV STIYSTFGAF YIPLALILIL YYKIYRAAKT LYHKRQASRI AKEEVNGQVL LESGEKSTKS VSTSYVLEKS LSDPSTDFDK IHSTVRSLRS EFKHEKSWRR QKISGTRERK AATTLGLILG AFVICWLPFF VKELVVNVCD KCKISEEMSN FLAWLGYLNS LINPLIYTIF NEDFKKAFQK LVRCR // ID 5HT1F_RAT Reviewed; 366 AA. AC P30940; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 23-JAN-2007, entry version 46. DE 5-hydroxytryptamine 1F receptor (5-HT-1F) (Serotonin receptor 1F). GN Name=Htr1f; Synonyms=5ht1f; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93211926; PubMed=8384716; RA Lovenberg T.W., Erlander M.G., Baron B.M., Racke M., Slone A.L., RA Siegel B.W., Craft C.M., Burns J.E., Danielson P.E., Sutcliffe G.J.; RT "Molecular cloning and functional expression of 5-HT1E-like rat and RT human 5-hydroxytryptamine receptor genes."; RL Proc. Natl. Acad. Sci. U.S.A. 90:2184-2188(1993). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L05596; AAA42133.1; -; Genomic_DNA. DR UniGene; Rn.44301; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSRNOG00000000716; Rattus norvegicus. DR KEGG; rno:60448; -. DR RGD; 71083; Htr1f. DR ArrayExpress; P30940; -. DR GermOnline; ENSRNOG00000000716; Rattus norvegicus. DR InterPro; IPR000450; 5HT1F_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00515; 5HT1FRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 366 5-hydroxytryptamine 1F receptor. FT /FTId=PRO_0000068940. FT TOPO_DOM 1 23 Extracellular (Potential). FT TRANSMEM 24 48 1 (Potential). FT TOPO_DOM 49 60 Cytoplasmic (Potential). FT TRANSMEM 61 83 2 (Potential). FT TOPO_DOM 84 94 Extracellular (Potential). FT TRANSMEM 95 119 3 (Potential). FT TOPO_DOM 120 139 Cytoplasmic (Potential). FT TRANSMEM 140 161 4 (Potential). FT TOPO_DOM 162 178 Extracellular (Potential). FT TRANSMEM 179 202 5 (Potential). FT TOPO_DOM 203 291 Cytoplasmic (Potential). FT TRANSMEM 292 314 6 (Potential). FT TOPO_DOM 315 327 Extracellular (Potential). FT TRANSMEM 328 351 7 (Potential). FT TOPO_DOM 352 366 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT DISULFID 96 172 By similarity. SQ SEQUENCE 366 AA; 41880 MW; 0672868A41DFDBFB CRC64; MDFLNSSDQN LTSEELLNRM PSKILVSLTL SGLALMTTTI NCLVITAIIV TRKLHHPANY LICSLAVTDF LVAVLVMPFS IVYIVRESWI MGQGLCDLWL SVDIICCTCS ILHLSAIALD RYRAITDAVE YARKRTPRHA GITITTVWVI SVFISVPPLF WRHQGNSRDD QCIIKHDHIV STIYSTFGAF YIPLVLILIL YYKIYRAART LYHKRQASRM IKEELNGQVL LESGEKSIKL VSTSYMLEKS LSDPSTDFDR IHSTVKSPRS ELKHEKSWRR QKISGTRERK AATTLGLILG AFVICWLPFF VKELVVNICE KCKISEEMSN FLAWLGYLNS LINPLIYTIF NEDFKKAFQK LVRCRN // ID 5HT1R_DROME Reviewed; 564 AA. AC P20905; Q9VA21; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 23-JAN-2007, entry version 70. DE 5-hydroxytryptamine receptor 1 (5-HT receptor) (Serotonin receptor 1) DE (5HT-dro). GN Name=5-HT7; Synonyms=5HT-R1; ORFNames=CG12073; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Oregon-R; TISSUE=Head; RX MEDLINE=91062395; PubMed=2174167; RA Witz P., Amlaiky N., Plassat J.-L., Maroteaux L., Borrelli E., Hen R.; RT "Cloning and characterization of a Drosophila serotonin receptor that RT activates adenylate cyclase."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8940-8944(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins which activate adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed predominantly in adult heads. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M55533; AAA28305.1; -; mRNA. DR EMBL; AE014297; AAF57104.1; -; Genomic_DNA. DR EMBL; AY118491; AAM49860.1; -; mRNA. DR UniGene; Dm.1903; -. DR HSSP; P08913; 1HLL. DR Ensembl; CG12073; Drosophila melanogaster. DR KEGG; dme:Dmel_CG12073; -. DR FlyBase; FBgn0004573; 5-HT7. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-014259-MONOMER; -. DR GermOnline; CG12073; Drosophila melanogaster. DR GO; GO:0004993; F:serotonin receptor activity; TAS:FlyBase. DR GO; GO:0007192; P:serotonin receptor, adenylate cyclase activ...; TAS:FlyBase. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Complete proteome; G-protein coupled receptor; Membrane; Receptor; KW Repeat; Transducer; Transmembrane. FT CHAIN 1 564 5-hydroxytryptamine receptor 1. FT /FTId=PRO_0000068941. FT TRANSMEM 29 51 0 (Potential). FT TRANSMEM 165 188 1 (Potential). FT TOPO_DOM 189 198 Cytoplasmic (Potential). FT TRANSMEM 199 222 2 (Potential). FT TOPO_DOM 223 236 Extracellular (Potential). FT TRANSMEM 237 258 3 (Potential). FT TOPO_DOM 259 278 Cytoplasmic (Potential). FT TRANSMEM 279 302 4 (Potential). FT TOPO_DOM 303 330 Extracellular (Potential). FT TRANSMEM 331 353 5 (Potential). FT TOPO_DOM 354 454 Cytoplasmic (Potential). FT TRANSMEM 455 476 6 (Potential). FT TOPO_DOM 477 487 Extracellular (Potential). FT TRANSMEM 488 510 7 (Potential). FT TOPO_DOM 511 564 Cytoplasmic (Potential). FT REPEAT 89 90 1. FT REPEAT 91 92 2. FT REPEAT 93 94 3. FT REPEAT 95 96 4. FT REPEAT 97 98 5. FT REPEAT 99 100 6. FT REPEAT 101 102 7. FT REPEAT 103 104 8. FT REPEAT 105 106 9. FT REGION 89 106 9 X 2 AA tandem repeats of G-S. FT DISULFID 235 314 By similarity. SQ SEQUENCE 564 AA; 60861 MW; 0C8B9F8DA63D8095 CRC64; MALSGQDWRR HQSHRQHRNH RTQGNHQKLI STATLTLFVL FLSSWIAYAA GKATVPAPLV EGETESATSQ DFNSSSAFLG AIASASSTGS GSGSGSGSGS GSGSGSYGLA SMNSSPIAIV SYQGITSSNL GDSNTTLVPL SDTPLLLEEF AAGEFVLPPL TSIFVSIVLL IVILGTVVGN VLVCIAVCMV RKLRRPCNYL LVSLALSDLC VALLVMPMAL LYEVLEKWNF GPLLCDIWVS FDVLCCTASI LNLCAISVDR YLAITKPLEY GVKRTPRRMM LCVGIVWLAA ACISLPPLLI LGNEHEDEEG QPICTVCQNF AYQIYATLGS FYIPLSVMLF VYYQIFRAAR RIVLEEKRAQ THLQQALNGT GSPSAPQAPP LGHTELASSG NGQRHSSVGN TSLTYSTCGG LSSGGGALAG HGSGGGVSGS TGLLGSPHHK KLRFQLAKEK KASTTLGIIM SAFTVCWLPF FILALIRPFE TMHVPASLSS LFLWLGYANS LLNPIIYATL NRDFRKPFQE ILYFRCSSLN TMMRENYYQD QYGEPPSQRV MLGDERHGAR ESFL // ID 5HT2A_BOVIN Reviewed; 470 AA. AC Q75Z89; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 12-DEC-2006, entry version 20. DE 5-hydroxytryptamine 2A receptor (5-HT-2A) (Serotonin receptor 2A) (5- DE HT-2). GN Name=HTR2A; Synonyms=5HTR2A; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Adipose tissue; RA Tahara K., Aso H., Yamasaki T., Yamaguchi T., Takano S.; RT "Expression of 5-HT2A during adipogenesis."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. This CC receptor is involved in tracheal smooth muscle contraction, CC bronchoconstriction, and control of aldosterone production (By CC similarity). CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and AIP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). Note=Localizes to the post-synaptic thickening of CC axo-dendritic synapses (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB119637; BAD12238.1; -; mRNA. DR UniGene; Bt.27990; -. DR KEGG; bta:407230; -. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 470 5-hydroxytryptamine 2A receptor. FT /FTId=PRO_0000068942. FT TOPO_DOM 1 78 Extracellular (Potential). FT TRANSMEM 79 99 Potential. FT TOPO_DOM 100 115 Cytoplasmic (Potential). FT TRANSMEM 116 136 Potential. FT TOPO_DOM 137 148 Extracellular (Potential). FT TRANSMEM 149 169 Potential. FT TOPO_DOM 170 192 Cytoplasmic (Potential). FT TRANSMEM 193 213 Potential. FT TOPO_DOM 214 233 Extracellular (Potential). FT TRANSMEM 234 254 Potential. FT TOPO_DOM 255 322 Cytoplasmic (Potential). FT TRANSMEM 323 343 Potential. FT TOPO_DOM 344 358 Extracellular (Potential). FT TRANSMEM 359 379 Potential. FT TOPO_DOM 380 470 Cytoplasmic (Potential). FT MOTIF 468 470 PDZ-binding. FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT DISULFID 148 227 By similarity. SQ SEQUENCE 470 AA; 52571 MW; 85414E50CA9A91F0 CRC64; MDILCEENTS LSSTTNSLMQ LHADTRLYST DFNSGEGNTS NAFNWTVDSE NRTNLSCEGC LSPPCFSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV STLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DENFVLIGSF VAFFIPLTIM VITYFLTIKS LQKEATLCVS DPGTRTKLAS FSFLPQSSLS SEKLFQRSIH REPGSYGRRT MQSISNEQKA CKVLGIVFFL FVVMWCPFFI TNIMAVICKE SCNRDVIEAL LNVFVWIGYL SSAVNPLVYT LFNKTYRSAF SRYIQCQYKE NKKPLQLILV NTIPALAYKS SQLQMGPKKN SKKDDKTTDN DCTMVALGKE HPEDAPADSS NTVNEKVSCV // ID 5HT2A_CANFA Reviewed; 470 AA. AC O46635; Q50DZ9; Q60F96; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 2. DT 20-FEB-2007, entry version 45. DE 5-hydroxytryptamine 2A receptor (5-HT-2A) (Serotonin receptor 2A) (5- DE HT-2) (5-hydroxytryptamine receptor). GN Name=HTR2A; Synonyms=5-HTR2A; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Beagle; RX PubMed=15353848; DOI=10.1292/jvms.66.965; RA Masuda K., Hashizume C., Ogata N., Kikusui T., Takeuchi Y., Mori Y.; RT "Sequencing of canine 5-hydroxytriptamine receptor (5-HTR) 1B, 2A, 2C RT genes and identification of polymorphisms in the 5-HTR1B gene."; RL J. Vet. Med. Sci. 66:965-972(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=15862800; DOI=10.1016/j.ejphar.2005.03.013; RA Bonaventure P., Nepomuceno D., Miller K., Chen J., Kuei C., Kamme F., RA Tran D.T., Lovenberg T.W., Liu C.; RT "Molecular and pharmacological characterization of serotonin 5-HT(2A) RT and 5-HT(2B) receptor subtypes in dog."; RL Eur. J. Pharmacol. 513:181-192(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 120-307. RC TISSUE=Femoral artery; RA Sgard F.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. This CC receptor is involved in tracheal smooth muscle contraction, CC bronchoconstriction, and control of aldosterone production (By CC similarity). CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and AIP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). Note=Localizes to the post-synaptic thickening of CC axo-dendritic synapses (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB193092; BAD60922.1; -; mRNA. DR EMBL; AY832858; AAX39385.1; -; mRNA. DR EMBL; Y16134; CAA76080.1; -; mRNA. DR UniGene; Cfa.8880; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSCAFG00000004468; Canis familiaris. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 470 5-hydroxytryptamine 2A receptor. FT /FTId=PRO_0000068943. FT TOPO_DOM 1 75 Extracellular (Potential). FT TRANSMEM 76 99 1 (Potential). FT TOPO_DOM 100 110 Cytoplasmic (Potential). FT TRANSMEM 111 132 2 (Potential). FT TOPO_DOM 133 147 Extracellular (Potential). FT TRANSMEM 148 171 3 (Potential). FT TOPO_DOM 172 191 Cytoplasmic (Potential). FT TRANSMEM 192 215 4 (Potential). FT TOPO_DOM 216 233 Extracellular (Potential). FT TRANSMEM 234 254 5 (Potential). FT TOPO_DOM 255 323 Cytoplasmic (Potential). FT TRANSMEM 324 345 6 (Potential). FT TOPO_DOM 346 361 Extracellular (Potential). FT TRANSMEM 362 383 7 (Potential). FT TOPO_DOM 384 470 Cytoplasmic (Potential). FT MOTIF 468 470 PDZ-binding. FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential). FT DISULFID 148 227 By similarity. SQ SEQUENCE 470 AA; 52378 MW; 5C654F81E88B92E3 CRC64; MDVLFEDNAP LSPTTSSLMP SNGDPRLYGN DLNAGDANTS DAFNWTVDAE NRTNLSCEGC LSPPCFSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF VSFFIPLTIM VITYFLTIKS LQKEATLCVS DPGTRAKLAS FSFLPQSSLS SEKLFQRSIH REPGSYGRRT MQSISNEQKA CKVLGIVFFL FVVMWCPFFI TNIMAVICKE SCNEDIIGAL LNVFVWIGYL SSAVNPLVYT LFNKTYRSAF SRYIQCQYKE NKKPLQLILV NTIPALAYKS SQLQMGQKKN SKKDAKSTDN DYSMVALGKQ HSEDAPTDNI NTVNEKVSCV // ID 5HT2A_CAVPO Reviewed; 247 AA. AC P35382; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 12-DEC-2006, entry version 44. DE 5-hydroxytryptamine 2A receptor (5-HT-2A) (Serotonin receptor 2A) (5- DE HT-2) (Fragment). GN Name=HTR2A; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=94157576; PubMed=8113814; RA Watts S.W., Cohen M.L., Mooney P.Q., Johnson B.G., Schoepp D.D., RA Baez M.; RT "Disruption of potential alpha-helix in the G loop of the guinea pig RT 5-hydroxytryptamine2 receptor does not prevent receptor coupling to RT phosphoinositide hydrolysis."; RL J. Neurochem. 62:934-943(1994). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. This CC receptor is involved in tracheal smooth muscle contraction, CC bronchoconstriction, and control of aldosterone production. CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and AIP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). Note=Localizes to the post-synaptic thickening of CC axo-dendritic synapses (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M85162; AAA21022.1; -; mRNA. DR PIR; I48149; I48149. DR HSSP; P08913; 1HLL. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Membrane; Receptor; Transducer; KW Transmembrane. FT CHAIN <1 >247 5-hydroxytryptamine 2A receptor. FT /FTId=PRO_0000068944. FT TOPO_DOM <1 2 Extracellular (Potential). FT TRANSMEM 3 26 3 (Potential). FT TOPO_DOM 27 46 Cytoplasmic (Potential). FT TRANSMEM 47 70 4 (Potential). FT TOPO_DOM 71 88 Extracellular (Potential). FT TRANSMEM 89 109 5 (Potential). FT TOPO_DOM 110 179 Cytoplasmic (Potential). FT TRANSMEM 180 201 6 (Potential). FT TOPO_DOM 202 217 Extracellular (Potential). FT TRANSMEM 218 239 7 (Potential). FT TOPO_DOM 240 >247 Cytoplasmic (Potential). FT DISULFID 3 82 By similarity. FT NON_TER 1 1 FT NON_TER 247 247 SQ SEQUENCE 247 AA; 27698 MW; D58C4AAB2A663EA5 CRC64; KLCAIWIYLD VLFSTASIMH LCAISLDRYV AIQNPIHHSR FNSRTKAFLK IIAVWTISVG ISMPVPVFGL QDDSKVFKEG SCLLADDNFV LIGSFVAFFI PLTIMVITYF LTIKSLQKEA TLCVSDPGTR AKLSSFSFLP QSSLSSEKLF QRSIHRETGS YAGRRTMQSI SNEQKACKVL GIVFFLFVVM WCPFFVTNIM AVICKESCNE DVIGALLNVF VWIGYLSSAV NPLVYTLFNK TYRSAFA // ID 5HT2A_CRIGR Reviewed; 471 AA. AC P18599; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 20-FEB-2007, entry version 53. DE 5-hydroxytryptamine 2A receptor (5-HT-2A) (Serotonin receptor 2A) (5- DE HT-2). GN Name=HTR2A; OS Cricetulus griseus (Chinese hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung; RX MEDLINE=90384833; PubMed=2402449; DOI=10.1093/nar/18.17.5282; RA Chambard J.-C., van Obberghen-Schilling E., Haslam R.J., Vouret V., RA Pouyssegur J.; RT "Chinese hamster serotonin (5-HT) type 2 receptor cDNA sequence."; RL Nucleic Acids Res. 18:5282-5282(1990). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. This CC receptor is involved in tracheal smooth muscle contraction, CC bronchoconstriction, and control of aldosterone production. CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and AIP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). Note=Localizes to the post-synaptic thickening of CC axo-dendritic synapses (By similarity). CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with INADL, CASK, APBA1, DLG1 and DLG4 (By CC similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X53791; CAA37800.1; -; mRNA. DR PIR; S11280; S11280. DR HSSP; P08913; 1HLL. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 471 5-hydroxytryptamine 2A receptor. FT /FTId=PRO_0000068945. FT TOPO_DOM 1 75 Extracellular (Potential). FT TRANSMEM 76 99 1 (Potential). FT TOPO_DOM 100 110 Cytoplasmic (Potential). FT TRANSMEM 111 132 2 (Potential). FT TOPO_DOM 133 147 Extracellular (Potential). FT TRANSMEM 148 171 3 (Potential). FT TOPO_DOM 172 191 Cytoplasmic (Potential). FT TRANSMEM 192 215 4 (Potential). FT TOPO_DOM 216 233 Extracellular (Potential). FT TRANSMEM 234 254 5 (Potential). FT TOPO_DOM 255 324 Cytoplasmic (Potential). FT TRANSMEM 325 346 6 (Potential). FT TOPO_DOM 347 362 Extracellular (Potential). FT TRANSMEM 363 384 7 (Potential). FT TOPO_DOM 385 471 Cytoplasmic (Potential). FT MOTIF 469 471 PDZ-binding. FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential). FT DISULFID 148 227 By similarity. SQ SEQUENCE 471 AA; 52702 MW; A05242652039B869 CRC64; MEILCEDNTS LSSIPNSLMQ VDGDSGLYRN DFNSRDANSS DASNWTIDGE NRTNLSFEGY LPPTCLSILH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGVSMPI PVFGLQDDSK VFKQGSCLLA DDNFVLIGSF VAFFIPLTIM VITYFLTIKS LQKEATLCVS DLSTRAKLAS FSFLPQSSLS SEKLFQRSIH REPGSYTGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNEHVIGA LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENRKPLQLIL VNTIPALAYK SSQLQAGQNK DSKEDAEPTD NDCSMVTLGK QQSEETCTDN INTVNEKVSC V // ID 5HT2A_DROME Reviewed; 834 AA. AC P28285; Q0E921; Q4QQC9; Q5MTE9; Q5MTF1; Q5MTF2; Q5MTF3; Q5MTF8; AC Q5MTF9; Q5MTG0; Q5MTG1; Q5MTG2; Q5MTG3; Q5MTG4; Q5MTG6; Q5MTG9; AC Q5MTH1; Q5MTH2; Q5MTH5; Q5MTH6; Q5MTH7; Q5MTH9; Q5MTI0; Q5MTI1; AC Q5MTI4; Q5MTI6; Q5MTI7; Q5MTI8; Q5MTJ0; Q5MTJ4; Q5MTJ5; Q5MTJ6; AC Q5MTJ9; Q5MTK5; Q5MTL1; Q5MTL5; Q5MTL6; Q5MTM2; Q5MTM5; Q5MTM8; AC Q5MTN6; Q5MTQ1; Q5MTQ4; Q5MTR1; Q5MTR3; Q5MTR6; Q5MTR8; Q5MTS1; AC Q5MTT8; Q5MTV6; Q5MTV7; Q5MTV9; Q5MTW8; Q5MTX2; Q5MTX7; Q5MTY3; AC Q5MTY7; Q5MTY8; Q5MTY9; Q5MTZ0; Q5MTZ6; Q5MUJ0; Q5MUK2; Q5MUK5; AC Q5MUK8; Q5MUL0; Q5MUL2; Q5MUL5; Q5MUM3; Q5MUM7; Q5MUM9; Q5MUN0; AC Q5MUN1; Q5MUN2; Q5MUP0; Q5MUP5; Q5MUP6; Q5MUP7; Q5MUP8; Q5MUQ1; AC Q5MUQ6; Q5MUQ7; Q5MUQ8; Q5MUQ9; Q5MUR1; Q5MUR2; Q5MUR3; Q5MUR4; AC Q5MUR5; Q5MUT3; Q5MUT4; Q5MUT7; Q5MUT9; Q5MUU2; Q5MUU5; Q5MUU6; AC Q5MUV4; Q5MUV5; Q5MUV8; Q5MUV9; Q5MUW3; Q5MUW4; Q5MUW7; Q5MUX4; AC Q5MUX6; Q5MUY1; Q5MUY3; Q5MV05; Q5MV06; Q5MV07; Q5MV08; Q5MV13; AC Q5MV14; Q5MV15; Q5MV26; Q5MV30; Q9V8Q9; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 2. DT 23-JAN-2007, entry version 51. DE 5-hydroxytryptamine receptor 2A (5-HT receptor) (Serotonin receptor DE 2A). GN Name=5-HT1A; Synonyms=5HT-R2A; ORFNames=CG16720; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Canton-S, and Oregon-R; TISSUE=Head; RX MEDLINE=92155185; PubMed=1310937; RA Saudou F., Boschert U., Amlaiky N., Plassat J.-L., Hen R.; RT "A family of Drosophila serotonin receptors with distinct RT intracellular signalling properties and expression patterns."; RL EMBO J. 11:7-17(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., RA Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242, AND NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 511-834. RC STRAIN=CA-001, CA-002, CA-003, CA-008, CA-009, CA-010, CA-011, CA-012, RC CA-013, CA-015, CA-017, CA-018, CA-023, CA-026, CA-027, CA-030, RC CA-031, CA-033, CA-034, CA-035, CA-037, CA-040, CA-041, CA-043, RC CA-044, CA-045, CA-046, CA-047, CA-048, CA-052, CA-055, CA-056, RC CA-057, CA-058, CA-060, CA-061, CA-062, CA-063, CA-064, CA-065, RC CA-066, CA-068, CA-069, CA-070, CA-072, CA-073, CA-075, CA-081, RC CA-083, CA-086, CA-087, CA-088, CA-089, CA-090, CA-091, CA-093, RC CA-095, CA-096, CA-100, CA-105, CA-113, CA-114, CA-115, CA-118, RC CA-120, CA-123, CA-126, CA-127, CA-128, CA-129, CA-130, CA-132, RC CA-133, CA-136, CA-137, CA-140, CA-142, CA-144, CA-145, CA-147, RC CA-148, NC-001, NC-002, NC-003, NC-004, NC-005, NC-006, NC-008, RC NC-010, NC-011, NC-012, NC-013, NC-014, NC-015, NC-017, NC-021, RC NC-022, NC-023, NC-024, NC-025, NC-026, NC-027, NC-028, NC-029, RC NC-030, NC-032, NC-033, NC-034, NC-036, NC-037, NC-038, NC-039, RC NC-040, NC-041, NC-042, NC-043, NC-044, NC-046, NC-047, NC-048, RC NC-049, NC-050, NC-051, NC-052, NC-053, NC-054, NC-057, NC-058, RC NC-059, NC-060, NC-061, NC-064, NC-066, NC-067, NC-068, NC-069, RC NC-070, NC-071, NC-072, NC-073, NC-074, NC-075, NC-077, NC-079, RC NC-080, NC-081, NC-084, NC-086, NC-087, NC-088, NC-089, NC-091, RC NC-092, NC-094, NC-095, NC-096, NC-097, NC-098, NC-100, NC-101, RC NC-103, NC-104, NC-105, NC-107, NC-108, NC-109, NC-110, NC-111, RC NC-112, NC-113, NC-114, NC-115, NC-116, NC-118, NC-119, NC-121, RC NC-123, NC-124, NC-125, NC-126, NC-127, NC-128, NC-129, NC-131, RC NC-133, NC-134, NC-135, NC-136, NC-137, NC-138, NC-139, NC-141, RC NC-142, NC-144, NC-146, NC-147, NC-148, NC-149, and NC-150; RX PubMed=15611167; DOI=10.1534/genetics.104.028712; RA Nikoh N., Duty A., Gibson G.; RT "Effects of population structure and sex on association between RT serotonin receptors and Drosophila heart rate."; RL Genetics 168:1963-1974(2004). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins which inhibit adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- CAUTION: Ref.4 sequence differs from that shown due to a stop CC codon at position 49 which was translated as Glu to extend the CC 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; Z11489; CAA77570.1; -; mRNA. DR EMBL; AE013599; AAF57603.1; -; Genomic_DNA. DR EMBL; BT023487; AAY84887.1; ALT_SEQ; mRNA. DR EMBL; AY564785; AAS73796.1; -; Genomic_DNA. DR EMBL; AY564786; AAS73797.1; -; Genomic_DNA. DR EMBL; AY564787; AAS73798.1; -; Genomic_DNA. DR EMBL; AY564788; AAS73799.1; -; Genomic_DNA. DR EMBL; AY564789; AAS73800.1; -; Genomic_DNA. DR EMBL; AY564790; AAS73801.1; -; Genomic_DNA. DR EMBL; AY564791; AAS73802.1; -; Genomic_DNA. DR EMBL; AY564792; AAS73803.1; -; Genomic_DNA. DR EMBL; AY564793; AAS73804.1; -; Genomic_DNA. DR EMBL; AY564794; AAS73805.1; -; Genomic_DNA. DR EMBL; AY564795; AAS73806.1; -; Genomic_DNA. DR EMBL; AY564796; AAS73807.1; -; Genomic_DNA. DR EMBL; AY564797; AAS73808.1; -; Genomic_DNA. DR EMBL; AY564798; AAS73809.1; -; Genomic_DNA. DR EMBL; AY564799; AAS73810.1; -; Genomic_DNA. DR EMBL; AY564800; AAS73811.1; -; Genomic_DNA. DR EMBL; AY564801; AAS73812.1; -; Genomic_DNA. DR EMBL; AY564802; AAS73813.1; -; Genomic_DNA. DR EMBL; AY564803; AAS73814.1; -; Genomic_DNA. DR EMBL; AY564804; AAS73815.1; -; Genomic_DNA. DR EMBL; AY564805; AAS73816.1; -; Genomic_DNA. DR EMBL; AY564806; AAS73817.1; -; Genomic_DNA. DR EMBL; AY564807; AAS73818.1; -; Genomic_DNA. DR EMBL; AY564808; AAS73819.1; -; Genomic_DNA. DR EMBL; AY564809; AAS73820.1; -; Genomic_DNA. DR EMBL; AY564810; AAS73821.1; -; Genomic_DNA. DR EMBL; AY564811; AAS73822.1; -; Genomic_DNA. DR EMBL; AY564812; AAS73823.1; -; Genomic_DNA. DR EMBL; AY564813; AAS73824.1; -; Genomic_DNA. DR EMBL; AY564814; AAS73825.1; -; Genomic_DNA. DR EMBL; AY564815; AAS73826.1; -; Genomic_DNA. DR EMBL; AY564816; AAS73827.1; -; Genomic_DNA. DR EMBL; AY564817; AAS73828.1; -; Genomic_DNA. DR EMBL; AY564818; AAS73829.1; -; Genomic_DNA. DR EMBL; AY564819; AAS73830.1; -; Genomic_DNA. DR EMBL; AY564820; AAS73831.1; -; Genomic_DNA. DR EMBL; AY564821; AAS73832.1; -; Genomic_DNA. DR EMBL; AY564822; AAS73833.1; -; Genomic_DNA. DR EMBL; AY564823; AAS73834.1; -; Genomic_DNA. DR EMBL; AY564824; AAS73835.1; -; Genomic_DNA. DR EMBL; AY564825; AAS73836.1; -; Genomic_DNA. DR EMBL; AY564826; AAS73837.1; -; Genomic_DNA. DR EMBL; AY564827; AAS73838.1; -; Genomic_DNA. DR EMBL; AY564828; AAS73839.1; -; Genomic_DNA. DR EMBL; AY564829; AAS73840.1; -; Genomic_DNA. DR EMBL; AY564830; AAS73841.1; -; Genomic_DNA. DR EMBL; AY564831; AAS73842.1; -; Genomic_DNA. DR EMBL; AY564832; AAS73843.1; -; Genomic_DNA. DR EMBL; AY564833; AAS73844.1; -; Genomic_DNA. DR EMBL; AY564834; AAS73845.1; -; Genomic_DNA. DR EMBL; AY564835; AAS73846.1; -; Genomic_DNA. DR EMBL; AY564836; AAS73847.1; -; Genomic_DNA. DR EMBL; AY564837; AAS73848.1; -; Genomic_DNA. DR EMBL; AY564838; AAS73849.1; -; Genomic_DNA. DR EMBL; AY564839; AAS73850.1; -; Genomic_DNA. DR EMBL; AY564840; AAS73851.1; -; Genomic_DNA. DR EMBL; AY564841; AAS73852.1; -; Genomic_DNA. DR EMBL; AY564842; AAS73853.1; -; Genomic_DNA. DR EMBL; AY564843; AAS73854.1; -; Genomic_DNA. DR EMBL; AY564844; AAS73855.1; -; Genomic_DNA. DR EMBL; AY564845; AAS73856.1; -; Genomic_DNA. DR EMBL; AY564846; AAS73857.1; -; Genomic_DNA. DR EMBL; AY564847; AAS73858.1; -; Genomic_DNA. DR EMBL; AY564848; AAS73859.1; -; Genomic_DNA. DR EMBL; AY564849; AAS73860.1; -; Genomic_DNA. DR EMBL; AY564850; AAS73861.1; -; Genomic_DNA. DR EMBL; AY564851; AAS73862.1; -; Genomic_DNA. DR EMBL; AY564852; AAS73863.1; -; Genomic_DNA. DR EMBL; AY564853; AAS73864.1; -; Genomic_DNA. DR EMBL; AY564854; AAS73865.1; -; Genomic_DNA. DR EMBL; AY564855; AAS73866.1; -; Genomic_DNA. DR EMBL; AY564856; AAS73867.1; -; Genomic_DNA. DR EMBL; AY564857; AAS73868.1; -; Genomic_DNA. DR EMBL; AY564858; AAS73869.1; -; Genomic_DNA. DR EMBL; AY564859; AAS73870.1; -; Genomic_DNA. DR EMBL; AY564860; AAS73871.1; -; Genomic_DNA. DR EMBL; AY564861; AAS73872.1; -; Genomic_DNA. DR EMBL; AY564862; AAS73873.1; -; Genomic_DNA. DR EMBL; AY564863; AAS73874.1; -; Genomic_DNA. DR EMBL; AY564864; AAS73875.1; -; Genomic_DNA. DR EMBL; AY564865; AAS73876.1; -; Genomic_DNA. DR EMBL; AY564866; AAS73877.1; -; Genomic_DNA. DR EMBL; AY564867; AAS73878.1; -; Genomic_DNA. DR EMBL; AY564868; AAS73879.1; -; Genomic_DNA. DR EMBL; AY564869; AAS73880.1; -; Genomic_DNA. DR EMBL; AY564870; AAS73881.1; -; Genomic_DNA. DR EMBL; AY564871; AAS73882.1; -; Genomic_DNA. DR EMBL; AY564872; AAS73883.1; -; Genomic_DNA. DR EMBL; AY564873; AAS73884.1; -; Genomic_DNA. DR EMBL; AY564874; AAS73885.1; -; Genomic_DNA. DR EMBL; AY564875; AAS73886.1; -; Genomic_DNA. DR EMBL; AY564876; AAS73887.1; -; Genomic_DNA. DR EMBL; AY564877; AAS73888.1; -; Genomic_DNA. DR EMBL; AY564878; AAS73889.1; -; Genomic_DNA. DR EMBL; AY564879; AAS73890.1; -; Genomic_DNA. DR EMBL; AY564880; AAS73891.1; -; Genomic_DNA. DR EMBL; AY564881; AAS73892.1; -; Genomic_DNA. DR EMBL; AY564882; AAS73893.1; -; Genomic_DNA. DR EMBL; AY564883; AAS73894.1; -; Genomic_DNA. DR EMBL; AY564884; AAS73895.1; -; Genomic_DNA. DR EMBL; AY564885; AAS73896.1; -; Genomic_DNA. DR EMBL; AY564886; AAS73897.1; -; Genomic_DNA. DR EMBL; AY564887; AAS73898.1; -; Genomic_DNA. DR EMBL; AY564888; AAS73899.1; -; Genomic_DNA. DR EMBL; AY564889; AAS73900.1; -; Genomic_DNA. DR EMBL; AY564890; AAS73901.1; -; Genomic_DNA. DR EMBL; AY564891; AAS73902.1; -; Genomic_DNA. DR EMBL; AY564892; AAS73903.1; -; Genomic_DNA. DR EMBL; AY564893; AAS73904.1; -; Genomic_DNA. DR EMBL; AY564894; AAS73905.1; -; Genomic_DNA. DR EMBL; AY564895; AAS73906.1; -; Genomic_DNA. DR EMBL; AY564896; AAS73907.1; -; Genomic_DNA. DR EMBL; AY564897; AAS73908.1; -; Genomic_DNA. DR EMBL; AY564898; AAS73909.1; -; Genomic_DNA. DR EMBL; AY564899; AAS73910.1; -; Genomic_DNA. DR EMBL; AY564900; AAS73911.1; -; Genomic_DNA. DR EMBL; AY564901; AAS73912.1; -; Genomic_DNA. DR EMBL; AY564902; AAS73913.1; -; Genomic_DNA. DR EMBL; AY564903; AAS73914.1; -; Genomic_DNA. DR EMBL; AY564904; AAS73915.1; -; Genomic_DNA. DR EMBL; AY564905; AAS73916.1; -; Genomic_DNA. DR EMBL; AY564906; AAS73917.1; -; Genomic_DNA. DR EMBL; AY564907; AAS73918.1; -; Genomic_DNA. DR EMBL; AY564908; AAS73919.1; -; Genomic_DNA. DR EMBL; AY564909; AAS73920.1; -; Genomic_DNA. DR EMBL; AY564910; AAS73921.1; -; Genomic_DNA. DR EMBL; AY564911; AAS73922.1; -; Genomic_DNA. DR EMBL; AY564912; AAS73923.1; -; Genomic_DNA. DR EMBL; AY564913; AAS73924.1; -; Genomic_DNA. DR EMBL; AY564914; AAS73925.1; -; Genomic_DNA. DR EMBL; AY564915; AAS73926.1; -; Genomic_DNA. DR EMBL; AY564916; AAS73927.1; -; Genomic_DNA. DR EMBL; AY564917; AAS73928.1; -; Genomic_DNA. DR EMBL; AY564918; AAS73929.1; -; Genomic_DNA. DR EMBL; AY564919; AAS73930.1; -; Genomic_DNA. DR EMBL; AY564920; AAS73931.1; -; Genomic_DNA. DR EMBL; AY564921; AAS73932.1; -; Genomic_DNA. DR EMBL; AY564922; AAS73933.1; -; Genomic_DNA. DR EMBL; AY564925; AAS73936.1; -; Genomic_DNA. DR EMBL; AY564926; AAS73937.1; -; Genomic_DNA. DR EMBL; AY564927; AAS73938.1; -; Genomic_DNA. DR EMBL; AY564928; AAS73939.1; -; Genomic_DNA. DR EMBL; AY564929; AAS73940.1; -; Genomic_DNA. DR EMBL; AY564930; AAS73941.1; -; Genomic_DNA. DR EMBL; AY564931; AAS73942.1; -; Genomic_DNA. DR EMBL; AY564932; AAS73943.1; -; Genomic_DNA. DR EMBL; AY564933; AAS73944.1; -; Genomic_DNA. DR EMBL; AY564934; AAS73945.1; -; Genomic_DNA. DR EMBL; AY564935; AAS73946.1; -; Genomic_DNA. DR EMBL; AY564936; AAS73947.1; -; Genomic_DNA. DR EMBL; AY564937; AAS73948.1; -; Genomic_DNA. DR EMBL; AY564938; AAS73949.1; -; Genomic_DNA. DR EMBL; AY564939; AAS73950.1; -; Genomic_DNA. DR EMBL; AY564940; AAS73951.1; -; Genomic_DNA. DR EMBL; AY564941; AAS73952.1; -; Genomic_DNA. DR EMBL; AY564942; AAS73953.1; -; Genomic_DNA. DR EMBL; AY564943; AAS73954.1; -; Genomic_DNA. DR EMBL; AY564944; AAS73955.1; -; Genomic_DNA. DR EMBL; AY564945; AAS73956.1; -; Genomic_DNA. DR EMBL; AY564946; AAS73957.1; -; Genomic_DNA. DR EMBL; AY564947; AAS73958.1; -; Genomic_DNA. DR EMBL; AY564948; AAS73959.1; -; Genomic_DNA. DR EMBL; AY564949; AAS73960.1; -; Genomic_DNA. DR EMBL; AY564950; AAS73961.1; -; Genomic_DNA. DR EMBL; AY564951; AAS73962.1; -; Genomic_DNA. DR EMBL; AY564952; AAS73963.1; -; Genomic_DNA. DR EMBL; AY564953; AAS73964.1; -; Genomic_DNA. DR EMBL; AY564954; AAS73965.1; -; Genomic_DNA. DR EMBL; AY564955; AAS73966.1; -; Genomic_DNA. DR EMBL; AY564956; AAS73967.1; -; Genomic_DNA. DR EMBL; AY564958; AAS73968.1; -; Genomic_DNA. DR EMBL; AY564959; AAS73969.1; -; Genomic_DNA. DR EMBL; AY564960; AAS73970.1; -; Genomic_DNA. DR EMBL; AY564961; AAS73971.1; -; Genomic_DNA. DR EMBL; AY564962; AAS73972.1; -; Genomic_DNA. DR EMBL; AY564963; AAS73973.1; -; Genomic_DNA. DR EMBL; AY564964; AAS73974.1; -; Genomic_DNA. DR EMBL; AY564965; AAS73975.1; -; Genomic_DNA. DR EMBL; AY564966; AAS73976.1; -; Genomic_DNA. DR EMBL; AY564967; AAS73977.1; -; Genomic_DNA. DR EMBL; AY564968; AAS73978.1; -; Genomic_DNA. DR EMBL; AY564969; AAS73979.1; -; Genomic_DNA. DR EMBL; AY564971; AAS73981.1; -; Genomic_DNA. DR EMBL; AY564972; AAS73982.1; -; Genomic_DNA. DR EMBL; AY564973; AAS73983.1; -; Genomic_DNA. DR EMBL; AY564974; AAS73984.1; -; Genomic_DNA. DR EMBL; AY564975; AAS73985.1; -; Genomic_DNA. DR EMBL; AY564976; AAS73986.1; -; Genomic_DNA. DR EMBL; AY564977; AAS73987.1; -; Genomic_DNA. DR EMBL; AY565171; AAS74181.1; -; Genomic_DNA. DR EMBL; AY565172; AAS74182.1; -; Genomic_DNA. DR EMBL; AY565173; AAS74183.1; -; Genomic_DNA. DR EMBL; AY565174; AAS74184.1; -; Genomic_DNA. DR EMBL; AY565175; AAS74185.1; -; Genomic_DNA. DR EMBL; AY565176; AAS74186.1; -; Genomic_DNA. DR EMBL; AY565177; AAS74187.1; -; Genomic_DNA. DR EMBL; AY565178; AAS74188.1; -; Genomic_DNA. DR EMBL; AY565179; AAS74189.1; -; Genomic_DNA. DR EMBL; AY565180; AAS74190.1; -; Genomic_DNA. DR EMBL; AY565181; AAS74191.1; -; Genomic_DNA. DR EMBL; AY565182; AAS74192.1; -; Genomic_DNA. DR EMBL; AY565183; AAS74193.1; -; Genomic_DNA. DR EMBL; AY565184; AAS74194.1; -; Genomic_DNA. DR EMBL; AY565185; AAS74195.1; -; Genomic_DNA. DR EMBL; AY565186; AAS74196.1; -; Genomic_DNA. DR EMBL; AY565187; AAS74197.1; -; Genomic_DNA. DR EMBL; AY565188; AAS74198.1; -; Genomic_DNA. DR EMBL; AY565189; AAS74199.1; -; Genomic_DNA. DR EMBL; AY565190; AAS74200.1; -; Genomic_DNA. DR EMBL; AY565191; AAS74201.1; -; Genomic_DNA. DR EMBL; AY565192; AAS74202.1; -; Genomic_DNA. DR EMBL; AY565193; AAS74203.1; -; Genomic_DNA. DR EMBL; AY565194; AAS74204.1; -; Genomic_DNA. DR EMBL; AY565195; AAS74205.1; -; Genomic_DNA. DR EMBL; AY565196; AAS74206.1; -; Genomic_DNA. DR EMBL; AY565197; AAS74207.1; -; Genomic_DNA. DR EMBL; AY565198; AAS74208.1; -; Genomic_DNA. DR EMBL; AY565199; AAS74209.1; -; Genomic_DNA. DR EMBL; AY565200; AAS74210.1; -; Genomic_DNA. DR EMBL; AY565201; AAS74211.1; -; Genomic_DNA. DR EMBL; AY565202; AAS74212.1; -; Genomic_DNA. DR EMBL; AY565203; AAS74213.1; -; Genomic_DNA. DR EMBL; AY565204; AAS74214.1; -; Genomic_DNA. DR EMBL; AY565205; AAS74215.1; -; Genomic_DNA. DR EMBL; AY565206; AAS74216.1; -; Genomic_DNA. DR EMBL; AY565207; AAS74217.1; -; Genomic_DNA. DR EMBL; AY565208; AAS74218.1; -; Genomic_DNA. DR EMBL; AY565209; AAS74219.1; -; Genomic_DNA. DR EMBL; AY565210; AAS74220.1; -; Genomic_DNA. DR EMBL; AY565211; AAS74221.1; -; Genomic_DNA. DR EMBL; AY565212; AAS74222.1; -; Genomic_DNA. DR EMBL; AY565213; AAS74223.1; -; Genomic_DNA. DR EMBL; AY565214; AAS74224.1; -; Genomic_DNA. DR EMBL; AY565215; AAS74225.1; -; Genomic_DNA. DR EMBL; AY565216; AAS74226.1; -; Genomic_DNA. DR EMBL; AY565217; AAS74227.1; -; Genomic_DNA. DR EMBL; AY565218; AAS74228.1; -; Genomic_DNA. DR EMBL; AY565219; AAS74229.1; -; Genomic_DNA. DR EMBL; AY565220; AAS74230.1; -; Genomic_DNA. DR EMBL; AY565221; AAS74231.1; -; Genomic_DNA. DR EMBL; AY565222; AAS74232.1; -; Genomic_DNA. DR EMBL; AY565223; AAS74233.1; -; Genomic_DNA. DR EMBL; AY565224; AAS74234.1; -; Genomic_DNA. DR EMBL; AY565225; AAS74235.1; -; Genomic_DNA. DR EMBL; AY565226; AAS74236.1; -; Genomic_DNA. DR EMBL; AY565227; AAS74237.1; -; Genomic_DNA. DR EMBL; AY565228; AAS74238.1; -; Genomic_DNA. DR EMBL; AY565229; AAS74239.1; -; Genomic_DNA. DR EMBL; AY565230; AAS74240.1; -; Genomic_DNA. DR EMBL; AY565231; AAS74241.1; -; Genomic_DNA. DR EMBL; AY565232; AAS74242.1; -; Genomic_DNA. DR EMBL; AY565233; AAS74243.1; -; Genomic_DNA. DR EMBL; AY565234; AAS74244.1; -; Genomic_DNA. DR EMBL; AY565235; AAS74245.1; -; Genomic_DNA. DR EMBL; AY565236; AAS74246.1; -; Genomic_DNA. DR EMBL; AY565237; AAS74247.1; -; Genomic_DNA. DR EMBL; AY565238; AAS74248.1; -; Genomic_DNA. DR EMBL; AY565239; AAS74249.1; -; Genomic_DNA. DR EMBL; AY565240; AAS74250.1; -; Genomic_DNA. DR EMBL; AY565241; AAS74251.1; -; Genomic_DNA. DR EMBL; AY565242; AAS74252.1; -; Genomic_DNA. DR EMBL; AY565243; AAS74253.1; -; Genomic_DNA. DR EMBL; AY565244; AAS74254.1; -; Genomic_DNA. DR EMBL; AY565245; AAS74255.1; -; Genomic_DNA. DR EMBL; AY565246; AAS74256.1; -; Genomic_DNA. DR EMBL; AY565247; AAS74257.1; -; Genomic_DNA. DR EMBL; AY565248; AAS74258.1; -; Genomic_DNA. DR EMBL; AY565249; AAS74259.1; -; Genomic_DNA. DR EMBL; AY565250; AAS74260.1; -; Genomic_DNA. DR EMBL; AY565251; AAS74261.1; -; Genomic_DNA. DR EMBL; AY565252; AAS74262.1; -; Genomic_DNA. DR EMBL; AY565253; AAS74263.1; -; Genomic_DNA. DR EMBL; AY565254; AAS74264.1; -; Genomic_DNA. DR EMBL; AY565255; AAS74265.1; -; Genomic_DNA. DR EMBL; AY565256; AAS74266.1; -; Genomic_DNA. DR EMBL; AY565257; AAS74267.1; -; Genomic_DNA. DR EMBL; AY565258; AAS74268.1; -; Genomic_DNA. DR EMBL; AY565259; AAS74269.1; -; Genomic_DNA. DR EMBL; AY565260; AAS74270.1; -; Genomic_DNA. DR EMBL; AY565261; AAS74271.1; -; Genomic_DNA. DR EMBL; AY565262; AAS74272.1; -; Genomic_DNA. DR EMBL; AY565263; AAS74273.1; -; Genomic_DNA. DR EMBL; AY565264; AAS74274.1; -; Genomic_DNA. DR EMBL; AY565265; AAS74275.1; -; Genomic_DNA. DR EMBL; AY565266; AAS74276.1; -; Genomic_DNA. DR EMBL; AY565267; AAS74277.1; -; Genomic_DNA. DR EMBL; AY565268; AAS74278.1; -; Genomic_DNA. DR EMBL; AY565269; AAS74279.1; -; Genomic_DNA. DR EMBL; AY565270; AAS74280.1; -; Genomic_DNA. DR EMBL; AY565271; AAS74281.1; -; Genomic_DNA. DR EMBL; AY565272; AAS74282.1; -; Genomic_DNA. DR EMBL; AY565273; AAS74283.1; -; Genomic_DNA. DR EMBL; AY565274; AAS74284.1; -; Genomic_DNA. DR EMBL; AY565275; AAS74285.1; -; Genomic_DNA. DR EMBL; AY565276; AAS74286.1; -; Genomic_DNA. DR EMBL; AY565277; AAS74287.1; -; Genomic_DNA. DR EMBL; AY565278; AAS74288.1; -; Genomic_DNA. DR EMBL; AY565279; AAS74289.1; -; Genomic_DNA. DR EMBL; AY565280; AAS74290.1; -; Genomic_DNA. DR EMBL; AY565281; AAS74291.1; -; Genomic_DNA. DR EMBL; AY565282; AAS74292.1; -; Genomic_DNA. DR EMBL; AY565283; AAS74293.1; -; Genomic_DNA. DR EMBL; AY565284; AAS74294.1; -; Genomic_DNA. DR EMBL; AY565285; AAS74295.1; -; Genomic_DNA. DR EMBL; AY565286; AAS74296.1; -; Genomic_DNA. DR EMBL; AY565287; AAS74297.1; -; Genomic_DNA. DR EMBL; AY565288; AAS74298.1; -; Genomic_DNA. DR EMBL; AY565289; AAS74299.1; -; Genomic_DNA. DR EMBL; AY565290; AAS74300.1; -; Genomic_DNA. DR EMBL; AY565291; AAS74301.1; -; Genomic_DNA. DR EMBL; AY565292; AAS74302.1; -; Genomic_DNA. DR EMBL; AY565293; AAS74303.1; -; Genomic_DNA. DR EMBL; AY565294; AAS74304.1; -; Genomic_DNA. DR EMBL; AY565295; AAS74305.1; -; Genomic_DNA. DR EMBL; AY565296; AAS74306.1; -; Genomic_DNA. DR EMBL; AY565297; AAS74307.1; -; Genomic_DNA. DR EMBL; AY565298; AAS74308.1; -; Genomic_DNA. DR EMBL; AY565299; AAS74309.1; -; Genomic_DNA. DR EMBL; AY565300; AAS74310.1; -; Genomic_DNA. DR EMBL; AY565301; AAS74311.1; -; Genomic_DNA. DR EMBL; AY565302; AAS74312.1; -; Genomic_DNA. DR EMBL; AY565303; AAS74313.1; -; Genomic_DNA. DR EMBL; AY565304; AAS74314.1; -; Genomic_DNA. DR EMBL; AY565305; AAS74315.1; -; Genomic_DNA. DR EMBL; AY565306; AAS74316.1; -; Genomic_DNA. DR EMBL; AY565307; AAS74317.1; -; Genomic_DNA. DR EMBL; AY565308; AAS74318.1; -; Genomic_DNA. DR EMBL; AY565309; AAS74319.1; -; Genomic_DNA. DR EMBL; AY565310; AAS74320.1; -; Genomic_DNA. DR EMBL; AY565311; AAS74321.1; -; Genomic_DNA. DR EMBL; AY565312; AAS74322.1; -; Genomic_DNA. DR EMBL; AY565313; AAS74323.1; -; Genomic_DNA. DR EMBL; AY565314; AAS74324.1; -; Genomic_DNA. DR EMBL; AY565315; AAS74325.1; -; Genomic_DNA. DR EMBL; AY565316; AAS74326.1; -; Genomic_DNA. DR EMBL; AY565317; AAS74327.1; -; Genomic_DNA. DR EMBL; AY565318; AAS74328.1; -; Genomic_DNA. DR EMBL; AY565319; AAS74329.1; -; Genomic_DNA. DR EMBL; AY565320; AAS74330.1; -; Genomic_DNA. DR EMBL; AY565321; AAS74331.1; -; Genomic_DNA. DR EMBL; AY565322; AAS74332.1; -; Genomic_DNA. DR EMBL; AY565323; AAS74333.1; -; Genomic_DNA. DR EMBL; AY565324; AAS74334.1; -; Genomic_DNA. DR EMBL; AY565325; AAS74335.1; -; Genomic_DNA. DR EMBL; AY565326; AAS74336.1; -; Genomic_DNA. DR EMBL; AY565327; AAS74337.1; -; Genomic_DNA. DR EMBL; AY565328; AAS74338.1; -; Genomic_DNA. DR EMBL; AY565329; AAS74339.1; -; Genomic_DNA. DR EMBL; AY565330; AAS74340.1; -; Genomic_DNA. DR EMBL; AY565331; AAS74341.1; -; Genomic_DNA. DR EMBL; AY565332; AAS74342.1; -; Genomic_DNA. DR EMBL; AY565333; AAS74343.1; -; Genomic_DNA. DR EMBL; AY565334; AAS74344.1; -; Genomic_DNA. DR EMBL; AY565335; AAS74345.1; -; Genomic_DNA. DR EMBL; AY565336; AAS74346.1; -; Genomic_DNA. DR EMBL; AY565337; AAS74347.1; -; Genomic_DNA. DR EMBL; AY565338; AAS74348.1; -; Genomic_DNA. DR EMBL; AY565339; AAS74349.1; -; Genomic_DNA. DR EMBL; AY565340; AAS74350.1; -; Genomic_DNA. DR EMBL; AY565341; AAS74351.1; -; Genomic_DNA. DR EMBL; AY565342; AAS74352.1; -; Genomic_DNA. DR EMBL; AY565343; AAS74353.1; -; Genomic_DNA. DR EMBL; AY565344; AAS74354.1; -; Genomic_DNA. DR EMBL; AY565345; AAS74355.1; -; Genomic_DNA. DR EMBL; AY565346; AAS74356.1; -; Genomic_DNA. DR EMBL; AY565347; AAS74357.1; -; Genomic_DNA. DR EMBL; AY565348; AAS74358.1; -; Genomic_DNA. DR EMBL; AY565349; AAS74359.1; -; Genomic_DNA. DR EMBL; AY565350; AAS74360.1; -; Genomic_DNA. DR EMBL; AY565351; AAS74361.1; -; Genomic_DNA. DR EMBL; AY565352; AAS74362.1; -; Genomic_DNA. DR EMBL; AY565353; AAS74363.1; -; Genomic_DNA. DR EMBL; AY565354; AAS74364.1; -; Genomic_DNA. DR EMBL; AY565355; AAS74365.1; -; Genomic_DNA. DR EMBL; AY565356; AAS74366.1; -; Genomic_DNA. DR EMBL; AY565357; AAS74367.1; -; Genomic_DNA. DR EMBL; AY565358; AAS74368.1; -; Genomic_DNA. DR EMBL; AY565359; AAS74369.1; -; Genomic_DNA. DR EMBL; AY565360; AAS74370.1; -; Genomic_DNA. DR EMBL; AY565361; AAS74371.1; -; Genomic_DNA. DR EMBL; AY565362; AAS74372.1; -; Genomic_DNA. DR EMBL; AY565363; AAS74373.1; -; Genomic_DNA. DR EMBL; AY565364; AAS74374.1; -; Genomic_DNA. DR EMBL; AY565365; AAS74375.1; -; Genomic_DNA. DR EMBL; AY565366; AAS74376.1; -; Genomic_DNA. DR EMBL; AY565367; AAS74377.1; -; Genomic_DNA. DR EMBL; AY565368; AAS74378.1; -; Genomic_DNA. DR PIR; S19155; S19155. DR UniGene; Dm.4703; -. DR HSSP; P08913; 1HLL. DR Ensembl; CG16720; Drosophila melanogaster. DR KEGG; dme:Dmel_CG16720; -. DR FlyBase; FBgn0004168; 5-HT1A. DR GermOnline; CG16720; Drosophila melanogaster. DR GO; GO:0001586; F:5-HT1 receptor activity; NAS:FlyBase. DR GO; GO:0007198; P:serotonin receptor, adenylate cyclase inhib...; IDA:FlyBase. DR GO; GO:0007208; P:serotonin receptor, phospholipase C activat...; IDA:FlyBase. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Complete proteome; G-protein coupled receptor; Glycoprotein; Membrane; KW Polymorphism; Receptor; Transducer; Transmembrane. FT CHAIN 1 834 5-hydroxytryptamine receptor 2A. FT /FTId=PRO_0000068962. FT TOPO_DOM 1 230 Extracellular (Potential). FT TRANSMEM 231 253 1 (Potential). FT TOPO_DOM 254 263 Cytoplasmic (Potential). FT TRANSMEM 264 285 2 (Potential). FT TOPO_DOM 286 300 Extracellular (Potential). FT TRANSMEM 301 322 3 (Potential). FT TOPO_DOM 323 341 Cytoplasmic (Potential). FT TRANSMEM 342 364 4 (Potential). FT TOPO_DOM 365 391 Extracellular (Potential). FT TRANSMEM 392 413 5 (Potential). FT TOPO_DOM 414 752 Cytoplasmic (Potential). FT TRANSMEM 753 776 6 (Potential). FT TOPO_DOM 777 785 Extracellular (Potential). FT TRANSMEM 786 808 7 (Potential). FT TOPO_DOM 809 834 Cytoplasmic (Potential). FT COMPBIAS 108 136 Ala-rich. FT COMPBIAS 707 723 Gln-rich. FT CARBOHYD 68 68 N-linked (GlcNAc...) (Potential). FT CARBOHYD 97 97 N-linked (GlcNAc...) (Potential). FT CARBOHYD 161 161 N-linked (GlcNAc...) (Potential). FT CARBOHYD 175 175 N-linked (GlcNAc...) (Potential). FT CARBOHYD 183 183 N-linked (GlcNAc...) (Potential). FT CARBOHYD 194 194 N-linked (GlcNAc...) (Potential). FT CARBOHYD 203 203 N-linked (GlcNAc...) (Potential). FT CARBOHYD 209 209 N-linked (GlcNAc...) (Potential). FT DISULFID 299 378 By similarity. FT VARIANT 29 32 Missing (in strain: CA-128). FT VARIANT 46 46 E -> Q (in strain: NC-066). FT VARIANT 49 49 E -> V (in strain: NC-036 and NC-123). FT VARIANT 51 51 D -> E (in strain: CA-002, CA-008, CA- FT 009, CA-011, CA-013, CA-015, CA-026, CA- FT 031, CA-033, CA-034, CA-035, CA-037, CA- FT 040, CA-048, CA-052, CA-055, CA-057, CA- FT 060, CA-061, CA-063, CA-064, CA-065, CA- FT 069, CA-072, CA-073, CA-075, CA-088, CA- FT 090, CA-093, CA-096, CA-100, CA-114, CA- FT 120, CA-127, CA-129, CA-132, CA-133, CA- FT 140, CA-142, CA-145, CA-147, NC-003, NC- FT 006, NC-010, NC-011, NC-014, NC-015, NC- FT 021, NC-033, NC-034, NC-036, NC-040, NC- FT 042, NC-044, NC-046, NC-047, NC-051, NC- FT 052, NC-054, NC-057, NC-066, NC-069, NC- FT 071, NC-073, NC-081, NC-084, NC-086, NC- FT 089, NC-092, NC-094, NC-096, NC-097, NC- FT 101, NC-103, NC-104, NC-107, NC-108, NC- FT 118, NC-119, NC-121, NC-123, NC-127, NC- FT 128, NC-129, NC-134, NC-136, NC-137, NC- FT 138, NC-141, NC-144 and NC-148). FT VARIANT 52 52 D -> E (in strain: NC-103 and NC-118). FT VARIANT 54 54 A -> G (in strain: NC-061). FT VARIANT 76 76 S -> T (in strain: NC-012, NC-023, NC- FT 037, NC-038, NC-039, NC-124 and NC-131). FT VARIANT 86 86 S -> T (in strain: CA-008, CA-009, CA- FT 013, CA-026, CA-031, CA-033, CA-035, CA- FT 037, CA-040, CA-048, CA-052, CA-057, CA- FT 060, CA-061, CA-063, CA-065, CA-072, CA- FT 073, CA-088, CA-093, CA-096, CA-100, CA- FT 114, CA-120, CA-129, CA-132, CA-133, CA- FT 140, CA-147, NC-011, NC-015, NC-021, NC- FT 033, NC-034, NC-040, NC-042, NC-044, NC- FT 046, NC-047, NC-051, NC-052, NC-054, NC- FT 057, NC-069, NC-084, NC-089, NC-092, NC- FT 094, NC-097, NC-103, NC-107, NC-119, NC- FT 121, NC-127, NC-128, NC-129, NC-134, NC- FT 137, NC-138, NC-141, NC-144 and NC-148). FT VARIANT 91 91 P -> Q (in strain: CA-030, CA-068, CA- FT 091, NC-008, NC-025, NC-043, NC-048, NC- FT 060, NC-075, NC-088, NC-091, NC-114, NC- FT 116 and NC-135). FT VARIANT 96 96 V -> A (in strain: CA-008, CA-009, CA- FT 011, CA-013, CA-015, CA-026, CA-031, CA- FT 033, CA-034, CA-035, CA-037, CA-040, CA- FT 048, CA-052, CA-055, CA-057, CA-060, CA- FT 061, CA-063, CA-064, CA-065, CA-069, CA- FT 072, CA-073, CA-075, CA-088, CA-090, CA- FT 093, CA-095, CA-096, CA-100, CA-114, CA- FT 120, CA-129, CA-132, CA-133, CA-140, CA- FT 147, NC-010, NC-011, NC-012, NC-014, NC- FT 015, NC-021, NC-023, NC-033, NC-034, NC- FT 036, NC-037, NC-038, NC-039, NC-040, NC- FT 042, NC-044, NC-046, NC-047, NC-051, NC- FT 052, NC-054, NC-057, NC-066, NC-069, NC- FT 073, NC-081, NC-084, NC-086, NC-089, NC- FT 092, NC-094, NC-096, NC-097, NC-101, NC- FT 103, NC-104, NC-107, NC-108, NC-118, NC- FT 119, NC-121, NC-123, NC-124, NC-127, NC- FT 128, NC-129, NC-131, NC-134, NC-136, NC- FT 137, NC-138, NC-141, NC-144, NC-148 and FT Oregon-R). FT VARIANT 143 143 A -> T (in strain: CA-064). FT VARIANT 146 146 S -> T (in strain: CA-008, CA-026, CA- FT 033, CA-035, CA-037, CA-048, CA-052, CA- FT 057, CA-060, CA-063, CA-065, CA-072, CA- FT 088, CA-090, CA-096, CA-100, CA-114, CA- FT 120, CA-132, CA-140, CA-147, NC-011, NC- FT 014, NC-033, NC-034, NC-040, NC-042, NC- FT 044, NC-046, NC-047, NC-051, NC-052, NC- FT 054, NC-057, NC-069, NC-084, NC-092, NC- FT 094, NC-096, NC-103, NC-105, NC-107, NC- FT 108, NC-118, NC-119, NC-121, NC-125, NC- FT 126, NC-127, NC-129, NC-138, NC-144 and FT NC-148). FT VARIANT 171 171 A -> V (in strain: CA-008, CA-009, CA- FT 026, CA-031, CA-033, CA-035, CA-037, CA- FT 048, CA-052, CA-057, CA-060, CA-061, CA- FT 063, CA-065, CA-072, CA-088, CA-096, CA- FT 100, CA-114, CA-120, CA-132, CA-140, CA- FT 147, NC-011, NC-034, NC-040, NC-042, NC- FT 044, NC-046, NC-047, NC-051, NC-052, NC- FT 054, NC-057, NC-069, NC-084, NC-092, NC- FT 094, NC-103, NC-107, NC-119, NC-121, NC- FT 127, NC-129, NC-138, NC-144 and NC-148). FT VARIANT 182 182 G -> D (in strain: NC-066). FT VARIANT 184 184 D -> Y (in strain: NC-086, NC-104 and NC- FT 010). FT VARIANT 196 196 S -> N (in strain: NC-114). FT VARIANT 198 198 Q -> H (in strain: CA-001, CA-009, CA- FT 011, CA-013, CA-015, CA-026, CA-030, CA- FT 031, CA-033, CA-034, CA-035, CA-037, CA- FT 040, CA-046, CA-048, CA-052, CA-055, CA- FT 057, CA-060, CA-061, CA-063, CA-065, CA- FT 066, CA-068, CA-069, CA-072, CA-073, CA- FT 075, CA-088, CA-090, CA-091, CA-093, CA- FT 095, CA-096, CA-100, CA-114, CA-120, CA- FT 132, CA-133, CA-140, CA-147, NC-008, NC- FT 011, NC-014, NC-015, NC-025, NC-034, NC- FT 040, NC-042, NC-043, NC-044, NC-046, NC- FT 047, NC-048, NC-051, NC-052, NC-054, NC- FT 057, NC-060, NC-066, NC-069, NC-073, NC- FT 075, NC-081, NC-084, NC-088, NC-091, NC- FT 092, NC-094, NC-096, NC-101, NC-103, NC- FT 107, NC-108, NC-110, NC-113, NC-114, NC- FT 115, NC-116, NC-118, NC-119, NC-121, NC- FT 123, NC-127, NC-128, NC-129, NC-135, NC- FT 136, NC-137, NC-138, NC-139, NC-142, NC- FT 144, NC-146, NC-148 and Oregon-R). FT VARIANT 213 213 S -> G (in strain: CA-015). FT VARIANT 531 531 Q -> L (in strain: NC-104). FT VARIANT 536 536 T -> A (in strain: CA-011, CA-017, CA- FT 018, CA-062, CA-130, NC-118, NC-022, NC- FT 026, NC-049 and NC-073). FT VARIANT 547 550 APSG -> GPMGPL (in strain: CA-013, CA-026 FT and CA-093). FT VARIANT 571 571 E -> V (in strain: CA-002, CA-003, CA- FT 008, CA-011, CA-012, CA-015, CA-023, CA- FT 027, CA-030, CA-031, CA-034, CA-035, CA- FT 037, CA-043, CA-044, CA-045, CA-046, CA- FT 048, CA-052, CA-055, CA-057, CA-058, CA- FT 063, CA-064, CA-065, CA-066, CA-068, CA- FT 070, CA-072, CA-073, CA-075, CA-081, CA- FT 083, CA-087, CA-088, CA-089, CA-091, CA- FT 096, CA-100, CA-105, CA-114, CA-120, CA- FT 123, CA-128, CA-129, CA-133, CA-140, CA- FT 145, CA-147, CA-148, NC-001, NC-002, NC- FT 003, NC-010, NC-011, NC-012, NC-013, NC- FT 015, NC-023, NC-024, NC-025, NC-027, NC- FT 028, NC-029, NC-030, NC-032, NC-033, NC- FT 034, NC-036, NC-040, NC-041, NC-042, NC- FT 043, NC-044, NC-046, NC-047, NC-048, NC- FT 050, NC-051, NC-052, NC-054, NC-057, NC- FT 059, NC-060, NC-061, NC-066, NC-069, NC- FT 071, NC-072, NC-074, NC-075, NC-077, NC- FT 079, NC-080, NC-081, NC-084, NC-086, NC- FT 087, NC-088, NC-089, NC-091, NC-092, NC- FT 094, NC-098, NC-101, NC-103, NC-104, NC- FT 107, NC-109, NC-110, NC-111, NC-112, NC- FT 113, NC-114, NC-115, NC-116, NC-119, NC- FT 121, NC-124, NC-127, NC-128, NC-129, NC- FT 131, NC-133, NC-134, NC-135, NC-136, NC- FT 137, NC-138, NC-144, NC-146, NC-147, NC- FT 148 and NC-149). FT VARIANT 585 585 T -> K (in strain: NC-026). FT VARIANT 588 588 T -> M (in strain: Berkeley, CA-009, CA- FT 010, CA-013, CA-026, CA-041, CA-060, CA- FT 063, CA-066, CA-086, CA-093, CA-113, CA- FT 137, CA-145, NC-006, NC-008, NC-021, NC- FT 064, NC-067, NC-123, NC-142 and NC-150). FT VARIANT 589 589 T -> R (in strain: CA-040, CA-056, CA- FT 115, CA-118, CA-126, CA-132, CA-142, NC- FT 005, NC-037, NC-038, NC-039, NC-053, NC- FT 068, NC-095, NC-100, NC-105, NC-125, NC- FT 126 and NC-139). FT VARIANT 648 648 A -> V (in strain: CA-023, CA-048, NC- FT 015, NC-110, NC-128, NC-133 and NC-137). FT VARIANT 657 657 Q -> P (in strain: CA-130). FT VARIANT 682 682 S -> W (in strain: CA-043, CA-058 and CA- FT 105). FT VARIANT 688 688 T -> I (in strain: CA-088). FT VARIANT 692 692 S -> T (in strain: NC-104). FT VARIANT 706 706 P -> T (in strain: NC-001). FT VARIANT 716 718 Missing (in strain: NC-118). FT VARIANT 716 717 Missing (in strain: CA-002, CA-009, CA- FT 010, CA-011, CA-017, CA-018, CA-023, CA- FT 030, CA-031, CA-037, CA-040, CA-041, CA- FT 044, CA-045, CA-047, CA-048, CA-052, CA- FT 056, CA-057, CA-062, CA-068, CA-070, CA- FT 075, CA-086, CA-087, CA-088, CA-089, CA- FT 091, CA-095, CA-096, CA-100, CA-113, CA- FT 114, CA-115, CA-118, CA-120, CA-126, CA- FT 127, CA-129, CA-132, CA-133, CA-136, CA- FT 140, CA-142, CA-145, CA-147, NC-001, NC- FT 003, NC-004, NC-005, NC-011, NC-015, NC- FT 017, NC-021, NC-022, NC-025, NC-033, NC- FT 034, NC-036, NC-037, NC-038, NC-039, NC- FT 040, NC-042, NC-044, NC-046, NC-048, NC- FT 049, NC-051, NC-052, NC-053, NC-054, NC- FT 057, NC-059, NC-068, NC-069, NC-070, NC- FT 071, NC-079, NC-080, NC-084, NC-086, NC- FT 087, NC-088, NC-089, NC-091, NC-092, NC- FT 094, NC-095, NC-100, NC-101, NC-104, NC- FT 105, NC-107, NC-109, NC-110, NC-111, NC- FT 112, NC-113, NC-114, NC-115, NC-116, NC- FT 119, NC-121, NC-123, NC-125, NC-126, NC- FT 128, NC-129, NC-133, NC-134, NC-135, NC- FT 136, NC-137, NC-138, NC-139, NC-142, NC- FT 144, NC-146, NC-147, NC-148, NC-149 and FT NC-150;). FT VARIANT 716 716 Q -> H (in strain: NC-032). FT VARIANT 716 716 Q -> QH (in strain: NC-047). FT VARIANT 717 719 QQQ -> H (in strain: CA-069, NC-096 and FT NC-108). FT CONFLICT 135 135 R -> W (in Ref. 1). FT CONFLICT 400 400 L -> M (in Ref. 1). FT CONFLICT 813 813 R -> Q (in Ref. 4; AAY84887). SQ SEQUENCE 834 AA; 89521 MW; D3E27389921BD04F CRC64; MAHETSFNDA LDYIYIANSM NDRAFLIAEP HPEQPNVDGQ DQDDAELEEL DDMAVTDDGQ LEDTNNNNNS KRYYSSGKRR ADFIGSLALK PPPTDVNTTT TTAGSPLATA ALAAAAASAS VAAAAARITA KAAHRALTTK QDATSSPASS PALQLIDMDN NYTNVAVGLG AMLLNDTLLL EGNDSSLFGE MLANRSGQLD LINGTGGLNV TTSKVAEDDF TQLLRMAVTS VLLGLMILVT IIGNVFVIAA IILERNLQNV ANYLVASLAV ADLFVACLVM PLGAVYEISQ GWILGPELCD IWTSCDVLCC TASILHLVAI AVDRYWAVTN IDYIHSRTSN RVFMMIFCVW TAAVIVSLAP QFGWKDPDYL QRIEQQKCMV SQDVSYQVFA TCCTFYVPLL VILALYWKIY QTARKRIHRR RPRPVDAAVN NNQPDGGAAT DTKLHRLRLR LGRFSTAKSK TGSAVGVSGP ASGGRALGLV DGNSTNTVNT VEDTEFSSSN VDSKSRAGVE APSTSGNQIA TVSHLVALAK QQGKSTAKSS AAVNGMAPSG RQEDDGQRPE HGEQEDREEL EDQDEQVGPQ PTTATSATTA AGTNESEDQC KANGVEVLED PQLQQQLEQV QQLQKSVKSG GGGGASTSNA TTITSISALS PQTPTSQGVG IAAAAAGPMT AKTSTLTSCN QSHPLCGTAN ESPSTPEPRS RQPTTPQQQP HQQAHQQQQQ QQQLSSIANP MQKVNKRKET LEAKRERKAA KTLAIITGAF VVCWLPFFVM ALTMPLCAAC QISDSVASLF LWLGYFNSTL NPVIYTIFSP EFRQAFKRIL FGGHRPVHYR SGKL // ID 5HT2A_HUMAN Reviewed; 471 AA. AC P28223; Q5T8C0; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 20-FEB-2007, entry version 75. DE 5-hydroxytryptamine 2A receptor (5-HT-2A) (Serotonin receptor 2A) (5- DE HT-2). GN Name=HTR2A; Synonyms=HTR2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain stem; RX MEDLINE=92109767; PubMed=1722404; RA Saltzman A.G., Morse B., Whitman M.M., Ivanshchenko Y., Jaye M., RA Felder S.; RT "Cloning of the human serotonin 5-HT2 and 5-HT1C receptor subtypes."; RL Biochem. Biophys. Res. Commun. 181:1469-1478(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92356792; PubMed=1323014; DOI=10.1016/0169-328X(92)90005-V; RA Chen K., Yang W., Grimsby J., Shih J.C.; RT "The human 5-HT2 receptor is encoded by a multiple intron-exon gene."; RL Brain Res. Mol. Brain Res. 14:20-26(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94308772; PubMed=8035173; RA Cook E.H. Jr., Fletcher K.E., Wainwright M., Marks N., Yan S.Y., RA Leventhal B.L.; RT "Primary structure of the human platelet serotonin 5-HT2A receptor: RT identify with frontal cortex serotonin 5-HT2A receptor."; RL J. Neurochem. 63:465-469(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T., RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R., RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 NUCLEOTIDE SEQUENCE [MRNA] OF 9-464. RC TISSUE=Brain; RA Tritch R.J., Robinson D.L., Sahagan B.G., Horlick R.A.; RT "Cloning and nucleotide sequence of the human(5HT) type 2 receptor."; RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-218. RX MEDLINE=93049882; PubMed=1330647; DOI=10.1016/0922-4106(92)90123-D; RA Stam N.J., van Huizen F., van Alebeek C., Brands J., Dijkema R., RA Tonnaer J.A., Olijve W.; RT "Genomic organization, coding sequence and functional expression of RT human 5-HT2 and 5-HT1A receptor genes."; RL Eur. J. Pharmacol. 227:153-162(1992). RN [9] RP INTERACTION WITH MPDZ. RX MEDLINE=21201137; PubMed=11150294; DOI=10.1074/jbc.M008089200; RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J., RA Luebbert H., Ullmer C.; RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with RT PDZ10 of the multi-PDZ domain protein MUPP1."; RL J. Biol. Chem. 276:12974-12982(2001). RN [10] RP INTERACTION WITH INADL; MPP3; PRDX6; DLG4; DLG1; CASK; APBA1 AND AIP1, RP AND MUTAGENESIS OF GLY-463; ASN-465; CYS-470 AND VAL-471. 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 [11] RP VARIANTS ASN-25 AND TYR-452. RX MEDLINE=96209907; PubMed=8655141; DOI=10.1007/s004390050104; RA Erdmann J., Shimron-Abarbanell D., Rietschel M., Albus M., Maier W., RA Koerner J., Bondy B., Chen K., Shih J.C., Knapp M., Propping P., RA Noethen M.M.; RT "Systematic screening for mutations in the human serotonin-2A (5-HT2A) RT receptor gene: identification of two naturally occurring receptor RT variants and association analysis in schizophrenia."; RL Hum. Genet. 97:614-619(1996). RN [12] RP VARIANTS ASN-25 AND TYR-452. RX MEDLINE=20049881; PubMed=10581480; RX DOI=10.1002/(SICI)1096-8628(19991215)88:6<621::AID-AJMG9>3.0.CO;2-H; RA Marshall S.E., Bird T.G., Hart K., Welsh K.I.; RT "Unified approach to the analysis of genetic variation in serotonergic RT pathways."; RL Am. J. Med. Genet. 88:621-627(1999). RN [13] RP VARIANTS VAL-197; VAL-447 AND TYR-452. RX MEDLINE=99318093; PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [14] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. This CC receptor is involved in tracheal smooth muscle contraction, CC bronchoconstriction, and control of aldosterone production. CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and AIP1. CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). Note=Localizes to the post-synaptic thickening of CC axo-dendritic synapses (By similarity). CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with INADL, CASK, APBA1, DLG1 and DLG4. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- WEB RESOURCE: NAME=SHMPD; CC NOTE=The Singapore human mutation and polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HTR2A". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X57830; CAA40963.1; -; mRNA. DR EMBL; S42168; AAB22791.2; -; Genomic_DNA. DR EMBL; S42165; AAB22791.2; JOINED; Genomic_DNA. DR EMBL; S42167; AAB22791.2; JOINED; Genomic_DNA. DR EMBL; S71229; AAB31320.1; -; mRNA. DR EMBL; AF498982; AAM21129.1; -; mRNA. DR EMBL; AL160397; CAI16877.1; -; Genomic_DNA. DR EMBL; AL136958; CAI16877.1; JOINED; Genomic_DNA. DR EMBL; AL136958; CAI12227.1; -; Genomic_DNA. DR EMBL; AL160397; CAI12227.1; JOINED; Genomic_DNA. DR EMBL; BC069356; AAH69356.1; -; mRNA. DR EMBL; BC069576; AAH69576.1; -; mRNA. DR EMBL; BC074848; AAH74848.1; -; mRNA. DR EMBL; BC074849; AAH74849.1; -; mRNA. DR EMBL; BC096839; AAH96839.1; -; mRNA. DR EMBL; M86841; AAA58354.1; -; mRNA. DR EMBL; S50130; AAB24166.2; -; Genomic_DNA. DR EMBL; S49737; AAB24166.2; JOINED; Genomic_DNA. DR EMBL; S50113; AAB24166.2; JOINED; Genomic_DNA. DR PIR; A43956; A43956. DR UniGene; Hs.72630; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000102468; Homo sapiens. DR KEGG; hsa:3356; -. DR HGNC; HGNC:5293; HTR2A. DR MIM; 182135; gene. DR DrugBank; APRD00638; Aripiprazole. DR DrugBank; APRD00482; Chlorpromazine. DR DrugBank; APRD00470; Clozapine. DR DrugBank; APRD00213; Cyclobenzaprine. DR DrugBank; APRD00033; Cyproheptadine. DR DrugBank; APRD00043; Epinastine. DR DrugBank; APRD00574; Loxapine. DR DrugBank; APRD00610; Mesoridazine. DR DrugBank; APRD00463; Methysergide. DR DrugBank; APRD00735; Minaprine. DR DrugBank; APRD00685; Mirtazapine. DR DrugBank; APRD00402; Nefazodone. DR DrugBank; APRD00138; Olanzapine. DR DrugBank; APRD00624; Prochlorperazine. DR DrugBank; APRD00358; Promazine. DR DrugBank; APRD00601; Promethazine. DR DrugBank; APRD00339; Propiomazine. DR DrugBank; APRD00675; Quetiapine. DR DrugBank; APRD00187; Risperidone. DR DrugBank; APRD00323; Thiethylperazine. DR DrugBank; APRD00596; Thioridazine. DR DrugBank; APRD00533; Trazodone. DR DrugBank; APRD00540; Ziprasidone. DR ArrayExpress; P28223; -. DR GermOnline; ENSG00000102468; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004993; F:serotonin receptor activity; TAS:ProtInc. DR GO; GO:0007210; P:serotonin receptor signaling pathway; TAS:ProtInc. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 471 5-hydroxytryptamine 2A receptor. FT /FTId=PRO_0000068946. FT TOPO_DOM 1 75 Extracellular (Potential). FT TRANSMEM 76 99 1 (Potential). FT TOPO_DOM 100 110 Cytoplasmic (Potential). FT TRANSMEM 111 132 2 (Potential). FT TOPO_DOM 133 147 Extracellular (Potential). FT TRANSMEM 148 171 3 (Potential). FT TOPO_DOM 172 191 Cytoplasmic (Potential). FT TRANSMEM 192 215 4 (Potential). FT TOPO_DOM 216 233 Extracellular (Potential). FT TRANSMEM 234 254 5 (Potential). FT TOPO_DOM 255 324 Cytoplasmic (Potential). FT TRANSMEM 325 346 6 (Potential). FT TOPO_DOM 347 362 Extracellular (Potential). FT TRANSMEM 363 384 7 (Potential). FT TOPO_DOM 385 471 Cytoplasmic (Potential). FT MOTIF 469 471 PDZ-binding. FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential). FT DISULFID 148 227 By similarity. FT VARIANT 25 25 T -> N (in dbSNP:rs1805055). FT /FTId=VAR_003448. FT VARIANT 197 197 I -> V (in dbSNP:rs6304). FT /FTId=VAR_013901. FT VARIANT 447 447 A -> V (in dbSNP:rs6308). FT /FTId=VAR_013902. FT VARIANT 452 452 H -> Y (in dbSNP:rs6314). FT /FTId=VAR_003449. FT MUTAGEN 463 463 G->V: Loss of interaction with INADL. FT MUTAGEN 465 465 N->S: No effect on interaction with FT INADL. Acquires the binding properties of FT HTR2C; when associated with S-470. FT MUTAGEN 470 470 C->S: No effect on interaction with FT INADL. Acquires the binding properties of FT HTR2C; when associated with S-465. FT MUTAGEN 471 471 V->A: Loss of interaction with INADL, FT CASK, APBA1, DLG1 and DLG4. SQ SEQUENCE 471 AA; 52603 MW; EF8AAC0BC5379DA2 CRC64; MDILCEENTS LSSTTNSLMQ LNDDTRLYSN DFNSGEANTS DAFNWTVDSE NRTNLSCEGC LSPSCLSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF VSFFIPLTIM VITYFLTIKS LQKEATLCVS DLGTRAKLAS FSFLPQSSLS SEKLFQRSIH REPGSYTGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNEDVIGA LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENKKPLQLIL VNTIPALAYK SSQLQMGQKK NSKQDAKTTD NDCSMVALGK QHSEEASKDN SDGVNEKVSC V // ID 5HT2A_MACMU Reviewed; 471 AA. AC P50128; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 12-DEC-2006, entry version 44. DE 5-hydroxytryptamine 2A receptor (5-HT-2A) (Serotonin receptor 2A) (5- DE HT-2). GN Name=HTR2A; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95315240; PubMed=7794950; DOI=10.1016/0005-2736(95)00073-C; RA Johnson M.P., Baez M., Kursar J.D., Nelson D.L.; RT "Species differences in 5-HT2A receptors: cloned pig and rhesus monkey RT 5-HT2A receptors reveal conserved transmembrane homology to the human RT rather than rat sequence."; RL Biochim. Biophys. Acta 1236:201-206(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. This CC receptor is involved in tracheal smooth muscle contraction, CC bronchoconstriction, and control of aldosterone production. CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and AIP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). Note=Localizes to the post-synaptic thickening of CC axo-dendritic synapses (By similarity). CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with INADL, CASK, APBA1, DLG1 and DLG4 (By CC similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S78209; AAB34691.1; -; mRNA. DR UniGene; Mmu.3400; -. DR HSSP; P08913; 1HLL. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 471 5-hydroxytryptamine 2A receptor. FT /FTId=PRO_0000068947. FT TOPO_DOM 1 75 Extracellular (Potential). FT TRANSMEM 76 99 1 (Potential). FT TOPO_DOM 100 110 Cytoplasmic (Potential). FT TRANSMEM 111 132 2 (Potential). FT TOPO_DOM 133 147 Extracellular (Potential). FT TRANSMEM 148 171 3 (Potential). FT TOPO_DOM 172 191 Cytoplasmic (Potential). FT TRANSMEM 192 215 4 (Potential). FT TOPO_DOM 216 233 Extracellular (Potential). FT TRANSMEM 234 254 5 (Potential). FT TOPO_DOM 255 324 Cytoplasmic (Potential). FT TRANSMEM 325 346 6 (Potential). FT TOPO_DOM 347 362 Extracellular (Potential). FT TRANSMEM 363 384 7 (Potential). FT TOPO_DOM 385 471 Cytoplasmic (Potential). FT MOTIF 469 471 PDZ-binding. FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential). FT DISULFID 148 227 By similarity. SQ SEQUENCE 471 AA; 52603 MW; 300FFC84DE03D462 CRC64; MDILCEENTS LSSTTNSLMQ LNEDTRLYSN DFNSGEANTS DAFNWTVESE NRTNLSCEGC LSPSCLSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF VSFFIPLTIM VITYFLTIKS LQKEATLCVS DLGTRAKLAS FSFLPQSSLS SEKLFQRSIH RDPGSYTGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNEDVIGA LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENKKPLQLIL VNTIPALAYK SSQLQMGQKK NSKQDAKTTD NDCSMVALGK QHSEDASKDN SDGVNEKVSC V // ID 5HT2A_MOUSE Reviewed; 471 AA. AC P35363; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 12-DEC-2006, entry version 50. DE 5-hydroxytryptamine 2A receptor (5-HT-2A) (Serotonin receptor 2A) (5- DE HT-2). GN Name=Htr2a; Synonyms=Htr2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=93085774; PubMed=1333538; RA Yang W., Chen K., Lan N.C., Gallaher T.K., Shih J.C.; RT "Gene structure and expression of the mouse 5-HT2 receptor."; RL J. Neurosci. Res. 33:196-204(1992). RN [2] RP SUBCELLULAR LOCATION. 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). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. This CC receptor is involved in tracheal smooth muscle contraction, CC bronchoconstriction, and control of aldosterone production. CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and AIP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein. CC Note=Localizes to the post-synaptic thickening of axo-dendritic CC synapses. CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with INADL, CASK, APBA1, DLG1 and DLG4 (By CC similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S49542; AAB24369.1; -; mRNA. DR PIR; S40689; S40689. DR UniGene; Mm.214351; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSMUSG00000034997; Mus musculus. DR KEGG; mmu:15558; -. DR MGI; MGI:109521; Htr2a. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 471 5-hydroxytryptamine 2A receptor. FT /FTId=PRO_0000068948. FT TOPO_DOM 1 75 Extracellular (Potential). FT TRANSMEM 76 99 1 (Potential). FT TOPO_DOM 100 110 Cytoplasmic (Potential). FT TRANSMEM 111 132 2 (Potential). FT TOPO_DOM 133 147 Extracellular (Potential). FT TRANSMEM 148 171 3 (Potential). FT TOPO_DOM 172 191 Cytoplasmic (Potential). FT TRANSMEM 192 215 4 (Potential). FT TOPO_DOM 216 233 Extracellular (Potential). FT TRANSMEM 234 254 5 (Potential). FT TOPO_DOM 255 324 Cytoplasmic (Potential). FT TRANSMEM 325 346 6 (Potential). FT TOPO_DOM 347 362 Extracellular (Potential). FT TRANSMEM 363 384 7 (Potential). FT TOPO_DOM 385 471 Cytoplasmic (Potential). FT MOTIF 469 471 PDZ-binding. FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential). FT DISULFID 148 227 By similarity. SQ SEQUENCE 471 AA; 52842 MW; DE763E5617EE8435 CRC64; MEILCEDNIS LSSIPNSLMQ LGDDSRLYPN DFNSRDANTS EASNWTIDAE NRTNLSCEGY LPPTCLSILH LQEKNWSALL TTVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF VAFFIPLTIM VITYFLTIKS LQKEATLCVS DLSTRAKLSS FSFLPQSSLS SEKLFQRSIH REPGSYAGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNENVIGA LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENRKPLQLIL VNTIPTLAYK SSQLQVGQKK NSQEDAEPTA NDCSMVTLGN QHSEEMCTDN IETVNEKVSC V // ID 5HT2A_PIG Reviewed; 470 AA. AC P50129; Q29004; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 12-DEC-2006, entry version 44. DE 5-hydroxytryptamine 2A receptor (5-HT-2A) (Serotonin receptor 2A) (5- DE HT-2) (5-HT2A). GN Name=HTR2A; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95315240; PubMed=7794950; DOI=10.1016/0005-2736(95)00073-C; RA Johnson M.P., Baez M., Kursar J.D., Nelson D.L.; RT "Species differences in 5-HT2A receptors: cloned pig and rhesus monkey RT 5-HT2A receptors reveal conserved transmembrane homology to the human RT rather than rat sequence."; RL Biochim. Biophys. Acta 1236:201-206(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 146-213. RC TISSUE=Pulmonary artery; RX MEDLINE=95385798; PubMed=7656980; DOI=10.1016/0014-5793(95)00828-W; RA Ullmer C., Schmuck K., Kalkman H.O., Luebbert H.; RT "Expression of serotonin receptor mRNAs in blood vessels."; RL FEBS Lett. 370:215-221(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. This CC receptor is involved in tracheal smooth muscle contraction, CC bronchoconstriction, and control of aldosterone production. CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and AIP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). Note=Localizes to the post-synaptic thickening of CC axo-dendritic synapses (By similarity). CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with INADL, CASK, APBA1, DLG1 and DLG4 (By CC similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S78208; AAB34690.1; -; mRNA. DR EMBL; Z48152; CAA88169.1; -; mRNA. DR PIR; S66489; S66489. DR UniGene; Ssc.16141; -. DR HSSP; P08913; 1HLL. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 470 5-hydroxytryptamine 2A receptor. FT /FTId=PRO_0000068949. FT TOPO_DOM 1 75 Extracellular (Potential). FT TRANSMEM 76 99 1 (Potential). FT TOPO_DOM 100 110 Cytoplasmic (Potential). FT TRANSMEM 111 132 2 (Potential). FT TOPO_DOM 133 147 Extracellular (Potential). FT TRANSMEM 148 171 3 (Potential). FT TOPO_DOM 172 191 Cytoplasmic (Potential). FT TRANSMEM 192 215 4 (Potential). FT TOPO_DOM 216 233 Extracellular (Potential). FT TRANSMEM 234 254 5 (Potential). FT TOPO_DOM 255 323 Cytoplasmic (Potential). FT TRANSMEM 324 345 6 (Potential). FT TOPO_DOM 346 361 Extracellular (Potential). FT TRANSMEM 362 383 7 (Potential). FT TOPO_DOM 384 470 Cytoplasmic (Potential). FT MOTIF 468 470 PDZ-binding. FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential). FT CARBOHYD 75 75 N-linked (GlcNAc...) (Potential). FT DISULFID 148 227 By similarity. FT CONFLICT 184 184 R -> S (in Ref. 2). FT CONFLICT 208 208 M -> K (in Ref. 2). SQ SEQUENCE 470 AA; 52676 MW; 8231AD580BEE2A8F CRC64; MDVLCEENTS LSSPTNSFMQ LNDDTRLYHN DFNSGEANTS DAFNWTVDSE NRTNLSCEGC LSPPCFSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHRRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF VSFFIPLTIM VITYFLTIKS LQKEATLCVS DLGTRAKLAS FSFLPQSSLS SEKLFQRSIH REPGSYGRRT MQSISNEQKA CKVLGIVFFL FVVMWCPFFI TNIMAVICKE SCNEDVIGAL LNVFVWIGYL SSAVNPLVYT LFNKTYRSAF SRYIQCQYKE NKKPLQLILV NTIPALAYKS SQLQTGQKEN SKQDDKATEN DCTMVALGKQ HSEDAPADNS NTVNEKVSCV // ID 5HT2A_PONPY Reviewed; 471 AA. AC Q5R4Q6; Q9N2F2; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 12-DEC-2006, entry version 15. DE 5-hydroxytryptamine 2A receptor (5-HT-2A) (Serotonin receptor 2A) (5- DE HT-2). GN Name=HTR2A; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 216-460. RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. This CC receptor is involved in tracheal smooth muscle contraction, CC bronchoconstriction, and control of aldosterone production (By CC similarity). CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and AIP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). Note=Localizes to the post-synaptic thickening of CC axo-dendritic synapses (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR861189; CAH93260.1; -; mRNA. DR EMBL; AB037516; BAA90436.1; -; Genomic_DNA. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 471 5-hydroxytryptamine 2A receptor. FT /FTId=PRO_0000068950. FT TOPO_DOM 1 78 Extracellular (Potential). FT TRANSMEM 79 99 Potential. FT TOPO_DOM 100 115 Cytoplasmic (Potential). FT TRANSMEM 116 136 Potential. FT TOPO_DOM 137 148 Extracellular (Potential). FT TRANSMEM 149 169 Potential. FT TOPO_DOM 170 192 Cytoplasmic (Potential). FT TRANSMEM 193 213 Potential. FT TOPO_DOM 214 233 Extracellular (Potential). FT TRANSMEM 234 254 Potential. FT TOPO_DOM 255 323 Cytoplasmic (Potential). FT TRANSMEM 324 344 Potential. FT TOPO_DOM 345 356 Extracellular (Potential). FT TRANSMEM 357 377 Potential. FT TOPO_DOM 378 471 Cytoplasmic (Potential). FT MOTIF 469 471 PDZ-binding. FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT DISULFID 148 227 By similarity. FT CONFLICT 330 330 S -> F (in Ref. 2). SQ SEQUENCE 471 AA; 52529 MW; EFE1DC10C48C9D02 CRC64; MDILCEENTS LSSTTNSLMQ LNDDTRLYSN DFNSGEANTS DAFNWTVDSE NRTNLSCEGC LSPSCLSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF VSFFIPLTIM VITYFLTIKS LQKEATLCVS DLGTRAKLAS FSFLPQSSLS SEKLFQRSIH REPGSYTGRR TMQSISNEQK ACKVLGIVFS LFVVMWCPFF ITNIMAVICK ESCNEDVIGA LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENKKPLQLIL VNTIPALAYK SSQLQMGQKK NSKQDAKTTD NDCSMVALGK QHSEDASKDN SDGVNEKVSC V // ID 5HT2A_RAT Reviewed; 471 AA. AC P14842; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 20-FEB-2007, entry version 61. DE 5-hydroxytryptamine 2A receptor (5-HT-2A) (Serotonin receptor 2A) (5- DE HT-2). GN Name=Htr2a; Synonyms=Htr2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90138991; PubMed=2300586; RA Julius D., Huang K.N., Livelli T.J., Axel R., Jessell T.M.; RT "The 5HT2 receptor defines a family of structurally distinct but RT functionally conserved serotonin receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 87:928-932(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89210797; PubMed=2854054; RA Pritchett D.B., Bach A.W.J., Wozny M., Taleb O., Dal-Toso R., RA Shih J.C., Seeburg P.H.; RT "Structure and functional expression of cloned rat serotonin 5HT-2 RT receptor."; RL EMBO J. 7:4135-4140(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92112222; PubMed=1765383; RA Liu J., Chen Y., Kozak C.A., Yu L.; RT "The 5-HT2 serotonin receptor gene Htr-2 is tightly linked to Es-10 on RT mouse chromosome 14."; RL Genomics 11:231-234(1991). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. This CC receptor is involved in tracheal smooth muscle contraction, CC bronchoconstriction, and control of aldosterone production. CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and AIP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). Note=Localizes to the post-synaptic thickening of CC axo-dendritic synapses (By similarity). CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with INADL, CASK, APBA1, DLG1 and DLG4 (By CC similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- CAUTION: Ref.2 (CAA32150) sequence differs from that shown due to CC a frameshift in position 37. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M30705; AAA42178.1; -; mRNA. DR EMBL; X13971; CAA32150.1; ALT_FRAME; mRNA. DR EMBL; M64867; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; A34863; A34863. DR PIR; S02011; S02011. DR UniGene; Rn.10294; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSRNOG00000010063; Rattus norvegicus. DR KEGG; rno:29595; -. DR RGD; 61800; Htr2a. DR ArrayExpress; P14842; -. DR GermOnline; ENSRNOG00000010063; Rattus norvegicus. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 471 5-hydroxytryptamine 2A receptor. FT /FTId=PRO_0000068951. FT TOPO_DOM 1 75 Extracellular (Potential). FT TRANSMEM 76 99 1 (Potential). FT TOPO_DOM 100 110 Cytoplasmic (Potential). FT TRANSMEM 111 132 2 (Potential). FT TOPO_DOM 133 147 Extracellular (Potential). FT TRANSMEM 148 171 3 (Potential). FT TOPO_DOM 172 191 Cytoplasmic (Potential). FT TRANSMEM 192 215 4 (Potential). FT TOPO_DOM 216 233 Extracellular (Potential). FT TRANSMEM 234 254 5 (Potential). FT TOPO_DOM 255 324 Cytoplasmic (Potential). FT TRANSMEM 325 346 6 (Potential). FT TOPO_DOM 347 362 Extracellular (Potential). FT TRANSMEM 363 384 7 (Potential). FT TOPO_DOM 385 471 Cytoplasmic (Potential). FT MOTIF 469 471 PDZ-binding. FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential). FT DISULFID 148 227 By similarity. SQ SEQUENCE 471 AA; 52850 MW; 3626DACE5F6C7FF4 CRC64; MEILCEDNIS LSSIPNSLMQ LGDGPRLYHN DFNSRDANTS EASNWTIDAE NRTNLSCEGY LPPTCLSILH LQEKNWSALL TTVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAI WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF VAFFIPLTIM VITYFLTIKS LQKEATLCVS DLSTRAKLAS FSFLPQSSLS SEKLFQRSIH REPGSYAGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNENVIGA LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENRKPLQLIL VNTIPALAYK SSQLQVGQKK NSQEDAEQTV DDCSMVTLGK QQSEENCTDN IETVNEKVSC V // ID 5HT2B_CAVPO Reviewed; 96 AA. AC P97267; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 31-OCT-2006, entry version 41. DE 5-hydroxytryptamine 2B receptor (5-HT-2B) (Serotonin receptor 2B) (5- DE HT2B) (Fragment). GN Name=HTR2B; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Dunkin-Hartley; TISSUE=Superior cervical ganglion; RX MEDLINE=97166356; PubMed=9116207; RA Newberry N.R., Watkins C.J., Volenec A., Flanigan T.P.; RT "5-HT2B receptor mRNA in guinea pig superior cervical ganglion."; RL NeuroReport 7:2909-2911(1996). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC -!- SUBUNIT: Interacts with MPDZ (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U69635; AAB36680.1; -; mRNA. DR InterPro; IPR000482; 5HT2B_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00651; 5HT2BRECEPTR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; PARTIAL. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN <1 >96 5-hydroxytryptamine 2B receptor. FT /FTId=PRO_0000068952. FT TOPO_DOM <1 8 Extracellular (Potential). FT TRANSMEM 9 31 7 (Potential). FT TOPO_DOM 32 >96 Cytoplasmic (Potential). FT LIPID 45 45 S-palmitoyl cysteine (Potential). FT CARBOHYD 2 2 N-linked (GlcNAc...) (Potential). FT NON_TER 1 1 FT NON_TER 96 96 SQ SEQUENCE 96 AA; 11226 MW; ED35252CD8A6D842 CRC64; CNQSTLQMLL EIFVWIGYVS SGVNPLVYTL FNKTFRDAFG RYITCNYKAT KSVKTVRKCS NKIYFRNPMT ENSKFFMKHG MRNGINSTMY QSPVRL // ID 5HT2B_DROME Reviewed; 617 AA. AC P28286; Q9V8Q3; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 3. DT 20-FEB-2007, entry version 49. DE 5-hydroxytryptamine receptor 2B (5-HT receptor) (Serotonin receptor DE 2B). GN Name=5-HT1B; Synonyms=5HT-R2B; ORFNames=CG15113; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=92155185; PubMed=1310937; RA Saudou F., Boschert U., Amlaiky N., Plassat J.-L., Hen R.; RT "A family of Drosophila serotonin receptors with distinct RT intracellular signalling properties and expression patterns."; RL EMBO J. 11:7-17(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins which inhibit adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- CAUTION: Ref.1 sequence differs from that shown because it is CC chimeric. Chimeric DNA 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; Z11490; CAA77571.1; ALT_SEQ; mRNA. DR EMBL; AE003797; AAF57610.4; -; Genomic_DNA. DR PIR; S19156; S19156. DR UniGene; Dm.2573; -. DR HSSP; P08913; 1HLL. DR Ensembl; CG15113; Drosophila melanogaster. DR KEGG; dme:Dmel_CG15113; -. DR FlyBase; FBgn0004572; 5-HT1B. DR GermOnline; CG15113; Drosophila melanogaster. DR GO; GO:0001586; F:5-HT1 receptor activity; NAS:FlyBase. DR GO; GO:0007198; P:serotonin receptor, adenylate cyclase inhib...; IDA:FlyBase. DR GO; GO:0007208; P:serotonin receptor, phospholipase C activat...; IDA:FlyBase. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Complete proteome; G-protein coupled receptor; Glycoprotein; Membrane; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 617 5-hydroxytryptamine receptor 2B. FT /FTId=PRO_0000068963. FT TOPO_DOM 1 95 Extracellular (Potential). FT TRANSMEM 96 116 1 (Potential). FT TOPO_DOM 117 128 Cytoplasmic (Potential). FT TRANSMEM 129 149 2 (Potential). FT TOPO_DOM 150 164 Extracellular (Potential). FT TRANSMEM 165 185 3 (Potential). FT TOPO_DOM 186 205 Cytoplasmic (Potential). FT TRANSMEM 206 226 4 (Potential). FT TOPO_DOM 227 256 Extracellular (Potential). FT TRANSMEM 257 277 5 (Potential). FT TOPO_DOM 278 534 Cytoplasmic (Potential). FT TRANSMEM 535 555 6 (Potential). FT TOPO_DOM 556 570 Extracellular (Potential). FT TRANSMEM 571 591 7 (Potential). FT TOPO_DOM 592 617 Cytoplasmic (Potential). FT CARBOHYD 31 31 N-linked (GlcNAc...) (Potential). FT CARBOHYD 41 41 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 58 58 N-linked (GlcNAc...) (Potential). FT DISULFID 163 242 By similarity. FT CONFLICT 61 61 I -> V (in Ref. 1). FT CONFLICT 332 332 T -> M (in Ref. 1). FT CONFLICT 424 424 L -> V (in Ref. 1). SQ SEQUENCE 617 AA; 67530 MW; DD0E1AB7706FD844 CRC64; MLKTVTTAMA AGDDDVPASI LEIELPAILL NESLFIELNG NLTQLVDTTS NLSQIVWNRS INGNGNSNTF DLVDDEQERA AVEFWLLVKM IAMAVVLGLM ILVTIIGNVF VIAAIILERN LQNVANYLVA SLAVADLFVA CLVMPLGAVY EISNGWILGP ELCDIWTSCD VLCCTASILH LVAIAADRYW TVTNIDYNNL RTPRRVFLMI FCVWFAALIV SLAPQFGWKD PDYMKRIEEQ HCMVSQDVGY QIFATCCTFY VPLLVILFLY WKIYIIARKR IQRRAQKSFN VTLTETDCDS AVRELKKERS KRRAERKRLE AGERTPVDGD GTGGQLQRRT RKRMRICFGR NTNTANVVAG SEGAVARSMA AIAVDFASLA ITREETEFST SNYDNKSHAG TELTTVSSDA DDYRTSNANE IITLSQQVAH ATQHHLIASH LNAITPLAQS IAMGGVGCLT TTTPSEKALS GAGTVAGAVA GGSGSGSGEE GAGTEGKNAG VGLGGVLASI ANPHQKLAKR RQLLEAKRER KAAQTLAIIT GAFVICWLPF FVMALTMSLC KECEIHTAVA SLFLWLGYFN STLNPVIYTI FNPEFRRAFK RILFGRKAAA RARSAKI // ID 5HT2B_HUMAN Reviewed; 481 AA. AC P41595; Q53TI1; Q62221; Q6P523; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-FEB-2007, entry version 67. DE 5-hydroxytryptamine 2B receptor (5-HT-2B) (Serotonin receptor 2B). GN Name=HTR2B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94192809; PubMed=8143856; DOI=10.1016/0014-5793(94)80590-3; RA Schmuck K., Ullmer C., Engels P., Luebbert H.; RT "Cloning and functional characterization of the human 5-HT2B serotonin RT receptor."; RL FEBS Lett. 342:85-90(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=95010749; PubMed=7926008; DOI=10.1016/0014-5793(94)00968-6; RA Choi D.S., Birraux G., Launay J.-M., Maroteaux L.; RT "The human serotonin 5-HT2B receptor: pharmacological link between 5- RT HT2 and 5-HT1D receptors."; RL FEBS Lett. 352:393-399(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Uterus; RX MEDLINE=94359485; PubMed=8078486; RA Kursar J.D., Nelson D.L., Wainscott D.B., Baez M.; RT "Molecular cloning, functional expression, and mRNA tissue RT distribution of the human 5-hydroxytryptamine2B receptor."; RL Mol. Pharmacol. 46:227-234(1994). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=20189989; PubMed=10722792; DOI=10.1006/mcpr.1999.0281; RA Kim S.J., Veenstra-VanderWeele J., Hanna G.L., Gonen D., RA Leventhal B.L., Cook E.H. Jr.; RT "Mutation screening of human 5-HT(2B) receptor gene in early-onset RT obsessive-compulsive disorder."; RL Mol. Cell. Probes 14:47-52(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 INTERACTION WITH MPDZ. RX MEDLINE=21201137; PubMed=11150294; DOI=10.1074/jbc.M008089200; RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J., RA Luebbert H., Ullmer C.; RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with RT PDZ10 of the multi-PDZ domain protein MUPP1."; RL J. Biol. Chem. 276:12974-12982(2001). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC -!- SUBUNIT: Interacts with MPDZ. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Detected in most peripheral organs. Only low CC expression levels were found in the brain. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X77307; CAA54513.1; -; mRNA. DR EMBL; Z36748; CAA85319.1; -; mRNA. DR EMBL; AF156160; AAD39259.1; -; Genomic_DNA. DR EMBL; AF156158; AAD39259.1; JOINED; Genomic_DNA. DR EMBL; AF156159; AAD39259.1; JOINED; Genomic_DNA. DR EMBL; AY136751; AAN01277.1; -; mRNA. DR EMBL; AC009407; AAX93128.1; -; Genomic_DNA. DR EMBL; BC063123; AAH63123.1; -; mRNA. DR PIR; S43687; S43687. DR UniGene; Hs.421649; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000135914; Homo sapiens. DR KEGG; hsa:3357; -. DR HGNC; HGNC:5294; HTR2B. DR MIM; 601122; gene. DR DrugBank; APRD00945; Eletriptan. DR DrugBank; APRD00735; Minaprine. DR DrugBank; APRD00675; Quetiapine. DR DrugBank; APRD00465; Triflupromazine. DR ArrayExpress; P41595; -. DR GermOnline; ENSG00000135914; Homo sapiens. DR RZPD-ProtExp; A1084; -. DR RZPD-ProtExp; RZPDo834F0845; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004993; F:serotonin receptor activity; TAS:ProtInc. DR GO; GO:0008015; P:circulation; TAS:ProtInc. DR GO; GO:0007200; P:G-protein signaling, coupled to IP3 second ...; TAS:ProtInc. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-k...; IEP:UniProtKB. DR InterPro; IPR000482; 5HT2B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00651; 5HT2BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 481 5-hydroxytryptamine 2B receptor. FT /FTId=PRO_0000068953. FT TOPO_DOM 1 56 Extracellular (Potential). FT TRANSMEM 57 79 1 (Potential). FT TOPO_DOM 80 91 Cytoplasmic (Potential). FT TRANSMEM 92 113 2 (Potential). FT TOPO_DOM 114 129 Extracellular (Potential). FT TRANSMEM 130 151 3 (Potential). FT TOPO_DOM 152 171 Cytoplasmic (Potential). FT TRANSMEM 172 192 4 (Potential). FT TOPO_DOM 193 216 Extracellular (Potential). FT TRANSMEM 217 239 5 (Potential). FT TOPO_DOM 240 324 Cytoplasmic (Potential). FT TRANSMEM 325 345 6 (Potential). FT TOPO_DOM 346 360 Extracellular (Potential). FT TRANSMEM 361 383 7 (Potential). FT TOPO_DOM 384 481 Cytoplasmic (Potential). FT MOTIF 479 481 PDZ-binding. FT LIPID 397 397 S-palmitoyl cysteine (Potential). FT CARBOHYD 30 30 N-linked (GlcNAc...) (Potential). FT DISULFID 128 207 By similarity. FT CONFLICT 452 452 T -> P (in Ref. 2). FT CONFLICT 477 477 Q -> R (in Ref. 7; AAH63123). SQ SEQUENCE 481 AA; 54298 MW; CDA4447ECDBA3B46 CRC64; MALSYRVSEL QSTIPEHILQ STFVHVISSN WSGLQTESIP EEMKQIVEEQ GNKLHWAALL ILMVIIPTIG GNTLVILAVS LEKKLQYATN YFLMSLAVAD LLVGLFVMPI ALLTIMFEAM WPLPLVLCPA WLFLDVLFST ASIMHLCAIS VDRYIAIKKP IQANQYNSRA TAFIKITVVW LISIGIAIPV PIKGIETDVD NPNNITCVLT KERFGDFMLF GSLAAFFTPL AIMIVTYFLT IHALQKKAYL VKNKPPQRLT WLTVSTVFQR DETPCSSPEK VAMLDGSRKD KALPNSGDET LMRRTSTIGK KSVQTISNEQ RASKVLGIVF FLFLLMWCPF FITNITLVLC DSCNQTTLQM LLEIFVWIGY VSSGVNPLVY TLFNKTFRDA FGRYITCNYR ATKSVKTLRK RSSKIYFRNP MAENSKFFKK HGIRNGINPA MYQSPMRLRS STIQSSSIIL LDTLLLTENE GDKTEEQVSY V // ID 5HT2B_MOUSE Reviewed; 479 AA. AC Q02152; Q8JZK5; Q9QWS2; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 20-FEB-2007, entry version 64. DE 5-hydroxytryptamine 2B receptor (5-HT-2B) (Serotonin receptor 2B) (5- DE HT-2F) (NP75 protein). GN Name=Htr2b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=93050195; PubMed=1426253; DOI=10.1016/0014-5793(92)80936-B; RA Loric S., Launay J.-M., Colas J.-F., Maroteaux L.; RT "New mouse 5-HT2-like receptor. Expression in brain, heart and RT intestine."; RL FEBS Lett. 312:203-207(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; RA Choi D.S., Maroteaux L.; RT "Genomic sequence of the 5-HT2B receptor locus."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=ILS, and ISS; RX MEDLINE=21363810; 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 [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). 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: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC -!- SUBUNIT: Interacts with MPDZ (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Intestine and heart, but also in brain and CC kidney. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- CAUTION: Ref.1 sequence differs from that shown due to a Leu codon CC in position 480 which was translated as stop codon to shorten the CC 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; Z15119; CAA78824.1; ALT_SEQ; mRNA. DR EMBL; AJ012488; CAA10051.1; -; Genomic_DNA. DR EMBL; AF498254; AAM22971.1; -; mRNA. DR EMBL; AF498255; AAM22972.1; -; mRNA. DR EMBL; AK033713; BAC28441.1; -; mRNA. DR EMBL; BC023690; AAH23690.1; -; mRNA. DR PIR; S27269; S27269. DR UniGene; Mm.435322; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSMUSG00000026228; Mus musculus. DR KEGG; mmu:15559; -. DR MGI; MGI:109323; Htr2b. DR ArrayExpress; Q02152; -. DR GermOnline; ENSMUSG00000026228; Mus musculus. DR GO; GO:0004993; F:serotonin receptor activity; TAS:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0007208; P:serotonin receptor, phospholipase C activat...; TAS:MGI. DR InterPro; IPR000482; 5HT2B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00651; 5HT2BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 479 5-hydroxytryptamine 2B receptor. FT /FTId=PRO_0000068954. FT TOPO_DOM 1 55 Extracellular (Potential). FT TRANSMEM 56 78 1 (Potential). FT TOPO_DOM 79 90 Cytoplasmic (Potential). FT TRANSMEM 91 112 2 (Potential). FT TOPO_DOM 113 128 Extracellular (Potential). FT TRANSMEM 129 150 3 (Potential). FT TOPO_DOM 151 170 Cytoplasmic (Potential). FT TRANSMEM 171 191 4 (Potential). FT TOPO_DOM 192 215 Extracellular (Potential). FT TRANSMEM 216 238 5 (Potential). FT TOPO_DOM 239 323 Cytoplasmic (Potential). FT TRANSMEM 324 344 6 (Potential). FT TOPO_DOM 345 359 Extracellular (Potential). FT TRANSMEM 360 382 7 (Potential). FT TOPO_DOM 383 479 Cytoplasmic (Potential). FT MOTIF 477 479 PDZ-binding. FT LIPID 396 396 S-palmitoyl cysteine (Potential). FT CARBOHYD 29 29 N-linked (GlcNAc...) (Potential). FT DISULFID 127 206 By similarity. FT CONFLICT 167 167 S -> T (in Ref. 1). FT CONFLICT 227 227 V -> A (in Ref. 3, 4 and 5). FT CONFLICT 449 449 S -> C (in Ref. 1). SQ SEQUENCE 479 AA; 53625 MW; FDB030D809079B6D CRC64; MASSYKMSEQ STTSEHILQK TCDHLILTNR SGLETDSVAE EMKQTVEGQG HTVHWAALLI LAVIIPTIGG NILVILAVAL EKRLQYATNY FLMSLAIADL LVGLFVMPIA LLTIMFEAIW PLPLALCPAW LFLDVLFSTA SIMHLCAISL DRYIAIKKPI QANQCNSRAT AFIKITVVWL ISIGIAIPVP IKGIETDVIN PHNVTCELTK DRFGSFMVFG SLAAFFVPLT IMVVTYFLTI HTLQKKAYLV KNKPPQRLTR WTVPTVFLRE DSSFSSPEKV AMLDGSHRDK ILPNSSDETL MRRMSSVGKR SAQTISNEQR ASKALGVVFF LFLLMWCPFF ITNLTLALCD SCNQTTLKTL LEIFVWIGYV SSGVNPLIYT LFNKTFREAF GRYITCNYRA TKSVKALRKF SSTLCFGNSM VENSKFFTKH GIRNGINPAM YQSPMRLRSS TIQSSSIILL DTLLTENDGD KAEEQVSYI // ID 5HT2B_PIG Reviewed; 60 AA. AC Q29005; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 43. DE 5-hydroxytryptamine 2B receptor (5-HT-2B) (Serotonin receptor 2B) (5- DE HT2B) (Fragment). GN Name=HTR2B; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pulmonary artery; RX MEDLINE=95385798; PubMed=7656980; DOI=10.1016/0014-5793(95)00828-W; RA Ullmer C., Schmuck K., Kalkman H.O., Luebbert H.; RT "Expression of serotonin receptor mRNAs in blood vessels."; RL FEBS Lett. 370:215-221(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC -!- SUBUNIT: Interacts with MPDZ (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z48174; CAA88197.1; -; mRNA. DR UniGene; Ssc.16145; -. DR HSSP; P08913; 1HLL. DR InterPro; IPR000482; 5HT2B_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Lipoprotein; Membrane; Palmitate; KW Receptor; Transducer; Transmembrane. FT CHAIN <1 >60 5-hydroxytryptamine 2B receptor. FT /FTId=PRO_0000068955. FT TOPO_DOM <1 4 Extracellular (Potential). FT TRANSMEM 5 26 3 (Potential). FT TOPO_DOM 27 46 Cytoplasmic (Potential). FT TRANSMEM 47 60 4 (Potential). FT NON_TER 1 1 FT NON_TER 60 60 SQ SEQUENCE 60 AA; 6725 MW; 920DCF0D76A8404B CRC64; VLCPAWLFLD VLFSTASIMH LCAISVDRYI AIKKPIQANQ YNSRATAFIK ITVVWLISIG // ID 5HT2B_RAT Reviewed; 479 AA. AC P30994; Q9QW44; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 23-JAN-2007, entry version 55. DE 5-hydroxytryptamine 2B receptor (5-HT-2B) (Serotonin receptor 2B) (5- DE HT-2F) (Stomach fundus serotonin receptor). GN Name=Htr2b; Synonyms=Srl; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=Sprague-Dawley; RX MEDLINE=92371456; PubMed=1505525; RA Foguet M., Hoyer D., Pardo L.A., Parekh A., Kluxen F.-W., RA Kalkman M.O., Stuehmer W., Luebbert H.; RT "Cloning and functional characterization of the rat stomach fundus RT serotonin receptor."; RL EMBO J. 11:3481-3487(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Gastric fundus; RX MEDLINE=93062814; PubMed=1331748; RA Kursar J.D., Nelson D.L., Wainscott D.B., Cohen M.L., Baez M.; RT "Molecular cloning, functional expression, and pharmacological RT characterization of a novel serotonin receptor (5-hydroxytryptamine2F) RT from rat stomach fundus."; RL Mol. Pharmacol. 42:549-557(1992). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC -!- SUBUNIT: Interacts with MPDZ (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Stomach fundus. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X66842; CAA47318.1; -; mRNA. DR PIR; S23562; S23562. DR UniGene; Rn.10425; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSRNOG00000017625; Rattus norvegicus. DR KEGG; rno:29581; -. DR RGD; 61801; Htr2b. DR ArrayExpress; P30994; -. DR GermOnline; ENSRNOG00000017625; Rattus norvegicus. DR InterPro; IPR000482; 5HT2B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00651; 5HT2BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 479 5-hydroxytryptamine 2B receptor. FT /FTId=PRO_0000068956. FT TOPO_DOM 1 55 Extracellular (Potential). FT TRANSMEM 56 78 1 (Potential). FT TOPO_DOM 79 90 Cytoplasmic (Potential). FT TRANSMEM 91 112 2 (Potential). FT TOPO_DOM 113 128 Extracellular (Potential). FT TRANSMEM 129 150 3 (Potential). FT TOPO_DOM 151 170 Cytoplasmic (Potential). FT TRANSMEM 171 191 4 (Potential). FT TOPO_DOM 192 215 Extracellular (Potential). FT TRANSMEM 216 238 5 (Potential). FT TOPO_DOM 239 323 Cytoplasmic (Potential). FT TRANSMEM 324 344 6 (Potential). FT TOPO_DOM 345 359 Extracellular (Potential). FT TRANSMEM 360 382 7 (Potential). FT TOPO_DOM 383 479 Cytoplasmic (Potential). FT MOTIF 477 479 PDZ-binding. FT LIPID 396 396 S-palmitoyl cysteine (Potential). FT CARBOHYD 203 203 N-linked (GlcNAc...) (Potential). FT CARBOHYD 353 353 N-linked (GlcNAc...) (Potential). FT DISULFID 127 206 By similarity. FT CONFLICT 281 281 V -> A (in Ref. 2). FT CONFLICT 296 296 T -> I (in Ref. 2). SQ SEQUENCE 479 AA; 53652 MW; 17FFC73213B42038 CRC64; MASSYKMSEQ STISEHILQK TCDHLILTDR SGLKAESAAE EMKQTAENQG NTVHWAALLI FAVIIPTIGG NILVILAVSL EKRLQYATNY FLMSLAVADL LVGLFVMPIA LLTIMFEATW PLPLALCPAW LFLDVLFSTA SIMHLCAISL DRYIAIKKPI QANQCNSRTT AFVKITVVWL ISIGIAIPVP IKGIEADVVN AHNITCELTK DRFGSFMLFG SLAAFFAPLT IMIVTYFLTI HALRKKAYLV RNRPPQRLTR WTVSTVLQRE DSSFSSPEKM VMLDGSHKDK ILPNSTDETL MRRMSSAGKK PAQTISNEQR ASKVLGIVFL FFLLMWCPFF ITNVTLALCD SCNQTTLKTL LQIFVWVGYV SSGVNPLIYT LFNKTFREAF GRYITCNYQA TKSVKVLRKC SSTLYFGNSM VENSKFFTKH GIRNGINPAM YQSPVRLRSS TIQSSSIILL NTFLTENDGD KVEDQVSYI // ID 5HT2B_TETFL Reviewed; 471 AA. AC Q8UUG8; Q8UUP7; Q8UUP8; Q8UUP9; Q8UUQ0; Q8UUQ1; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 12-DEC-2006, entry version 25. DE 5-hydroxytryptamine 2B receptor (5-HT-2B) (Serotonin receptor 2B). GN Name=HTR2B; OS Tetraodon fluviatilis (Puffer fish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Tetraodon. OX NCBI_TaxID=47145; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3 AND 4), AND RP TISSUE SPECIFICITY. RC TISSUE=Gut; RX MEDLINE=21610095; PubMed=11744166; DOI=10.1016/S0169-328X(01)00293-5; RA De Lucchini S., Marracci S., Nardi I.; RT "The serotonin 5-HT2B receptor from the puffer fish Tetraodon RT fluviatilis: cDNA cloning, genomic organization and alternatively RT spliced variants."; RL Brain Res. Mol. Brain Res. 97:89-93(2001). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8UUG8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8UUG8-2; Sequence=VSP_052051; CC Name=3; CC IsoId=Q8UUG8-3; Sequence=VSP_052052, VSP_052053; CC Name=4; CC IsoId=Q8UUG8-4; Sequence=VSP_052050; CC -!- TISSUE SPECIFICITY: Detected in brain, heart and gut. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ315179; CAC86245.1; -; Genomic_DNA. DR EMBL; AJ315180; CAC86246.1; -; mRNA. DR EMBL; AJ315181; CAC86247.1; -; mRNA. DR EMBL; AJ315182; CAC86248.1; -; mRNA. DR EMBL; AJ315183; CAC86249.1; -; mRNA. DR EMBL; AJ320211; CAC85962.1; -; mRNA. DR EMBL; AJ320212; CAC85912.1; -; mRNA. DR HSSP; P08913; 1HLL. DR GO; GO:0030285; C:integral to synaptic vesicle membrane; IC:UniProtKB. DR GO; GO:0001587; F:5-HT2 receptor activity; NAS:UniProtKB. DR GO; GO:0030594; F:neurotransmitter receptor activity; NAS:UniProtKB. DR GO; GO:0048598; P:embryonic morphogenesis; TAS:UniProtKB. DR GO; GO:0051610; P:serotonin uptake; IC:UniProtKB. DR InterPro; IPR000482; 5HT2B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00651; 5HT2BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 471 5-hydroxytryptamine 2B receptor. FT /FTId=PRO_0000239461. FT TOPO_DOM 1 28 Extracellular (Potential). FT TRANSMEM 29 49 1 (Potential). FT TOPO_DOM 50 65 Cytoplasmic (Potential). FT TRANSMEM 66 86 2 (Potential). FT TOPO_DOM 87 98 Extracellular (Potential). FT TRANSMEM 99 119 3 (Potential). FT TOPO_DOM 120 141 Cytoplasmic (Potential). FT TRANSMEM 142 162 4 (Potential). FT TOPO_DOM 163 191 Extracellular (Potential). FT TRANSMEM 192 212 5 (Potential). FT TOPO_DOM 213 308 Cytoplasmic (Potential). FT TRANSMEM 309 329 6 (Potential). FT TOPO_DOM 330 346 Extracellular (Potential). FT TRANSMEM 347 367 7 (Potential). FT TOPO_DOM 368 471 Cytoplasmic (Potential). FT MOTIF 469 471 PDZ-binding (By similarity). FT LIPID 381 381 S-palmitoyl cysteine (Potential). FT CARBOHYD 12 12 N-linked (GlcNAc...) (Potential). FT CARBOHYD 173 173 N-linked (GlcNAc...) (Potential). FT CARBOHYD 179 179 N-linked (GlcNAc...) (Potential). FT DISULFID 98 182 By similarity. FT VAR_SEQ 32 471 Missing (in isoform 4). FT /FTId=VSP_052050. FT VAR_SEQ 88 155 DSDWPLPEPLCPIWLFLDVLFSTASIMHLCAISLDRYIAIK FT KPIQHSQYKSRAKVMLKIALVWLISIC -> G (in FT isoform 2). FT /FTId=VSP_052051. FT VAR_SEQ 150 177 WLISICIAIPIPIKGLRNYPHPNNITFT -> LQSQFQLRG FT LGTTLILTTSPLPVTIHAC (in isoform 3). FT /FTId=VSP_052052. FT VAR_SEQ 178 471 Missing (in isoform 3). FT /FTId=VSP_052053. FT CONFLICT 5 5 A -> V (in Ref. 1; CAC86249). FT CONFLICT 20 20 P -> L (in Ref. 1; CAC86249). FT CONFLICT 213 213 F -> L (in Ref. 1; CAC86247). FT CONFLICT 220 220 R -> H (in Ref. 1; CAC86247). FT CONFLICT 242 242 V -> G (in Ref. 1; CAC86247). FT CONFLICT 254 254 P -> S (in Ref. 1; CAC86247). FT CONFLICT 261 261 G -> D (in Ref. 1; CAC86247). SQ SEQUENCE 471 AA; 53057 MW; 60DC34CA971E18CB CRC64; MFQAAVGPLQ TNISLPEETP GLELNWAALL IVMVIIPTIG GNILVILAVW LEKKLQNATN FFLMSLAVAD LLVGLLVMPI ALITILYDSD WPLPEPLCPI WLFLDVLFST ASIMHLCAIS LDRYIAIKKP IQHSQYKSRA KVMLKIALVW LISICIAIPI PIKGLRNYPH PNNITFTSNH TCVLKTDTFQ EFIIFGSLVA FFIPLTIMMI IYFLTVRVLR KKVYLLRSKV TQRFSYPIIS TVFQREQAAN PPQPEQPDST GNSLARIQEK TDTDGMSSPT GDEKSFRRLS TMGKKSMQTL TNEQRASKVL GIVFLLFVVM WCPFFITNIT SALCGPCDAN IIGRLMEIFS WVGYVSSGIN PLVYTLFNKT FRQAFTRYIT CNYRNFASKE QGRSFRASTV DRMLTHISPR SSVAENAKLF TKQEIKNETT DYRSPLGCLQ PSAQTSTGVV LDKILLTHTE NCKQEERVSC V // ID 5HT2C_CANFA Reviewed; 458 AA. AC Q60F97; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 31-OCT-2006, entry version 18. DE 5-hydroxytryptamine 2C receptor (5-HT-2C) (Serotonin receptor 2C) (5- DE HT2C) (5-HTR2C). GN Name=HTR2C; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Beagle; RX PubMed=15353848; DOI=10.1292/jvms.66.965; RA Masuda K., Hashizume C., Ogata N., Kikusui T., Takeuchi Y., Mori Y.; RT "Sequencing of canine 5-hydroxytriptamine receptor (5-HTR) 1B, 2A, 2C RT genes and identification of polymorphisms in the 5-HTR1B gene."; RL J. Vet. Med. Sci. 66:965-972(2004). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system (By CC similarity). CC -!- SUBUNIT: Interacts with MPDZ (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein (By CC similarity). CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with MPDZ (By similarity). CC -!- PTM: N-glycosylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB193091; BAD60921.1; -; mRNA. DR UniGene; Cfa.16240; -. DR Ensembl; ENSCAFG00000018227; Canis familiaris. DR InterPro; IPR000377; 5HT2C_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00517; 5HT2CRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 458 5-hydroxytryptamine 2C receptor. FT /FTId=PRO_0000068957. FT TOPO_DOM 1 52 Extracellular (Potential). FT TRANSMEM 53 78 1 (Potential). FT TOPO_DOM 79 89 Cytoplasmic (Potential). FT TRANSMEM 90 110 2 (Potential). FT TOPO_DOM 111 127 Extracellular (Potential). FT TRANSMEM 128 150 3 (Potential). FT TOPO_DOM 151 170 Cytoplasmic (Potential). FT TRANSMEM 171 193 4 (Potential). FT TOPO_DOM 194 213 Extracellular (Potential). FT TRANSMEM 214 235 5 (Potential). FT TOPO_DOM 236 311 Cytoplasmic (Potential). FT TRANSMEM 312 333 6 (Potential). FT TOPO_DOM 334 348 Extracellular (Potential). FT TRANSMEM 349 371 7 (Potential). FT TOPO_DOM 372 458 Cytoplasmic (Potential). FT MOTIF 456 458 PDZ-binding. FT CARBOHYD 39 39 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 203 203 N-linked (GlcNAc...) (Potential). FT CARBOHYD 204 204 N-linked (GlcNAc...) (Potential). FT DISULFID 127 207 By similarity. SQ SEQUENCE 458 AA; 51836 MW; 5A03245262B6C7BB CRC64; MVNLRKAVHS FLVHLIGLLV WQCDISVSPV AALVTDIFNT SDGGRFKFPD GVQNWPALSI VIIIILTIGG NILVIMAVSL EKKLHNATNY FLMSLAIADM LVGLLVMPLS LLAILYDYVW PLPRYLCPVW ISLDVLFSTA SIMHLCAISL DRYVAIRNPV EHSRFNSRTK AIMKIAIVWA ISIGVSVPIP VIGLRDEEKV FVNNTTCVLN DPNFVLIGSF VAFFIPLTIM VITYCLTIHV LRRQALMLLH GHVEEPPRIN LDFLKCCRRN GTEEENSANP NQDSNPRRRK KKERRPRGTM QAINNERKAS KVLGIVFFVF LVMWCPFFIT NILSVLCGKA CNQKLMEKLL NVFVWIGYVC SGINPLVYTL FNKIYRRAFS NYLRCNYKPE KKPPVRQMPR VAATALSGRE LNVNIYRHTN EPVLKKANDK EPGIEMQVEN LELPVNPSSV VSERISSV // ID 5HT2C_HUMAN Reviewed; 458 AA. AC P28335; Q5VUF8; Q9NP28; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 23-JAN-2007, entry version 78. DE 5-hydroxytryptamine 2C receptor (5-HT-2C) (Serotonin receptor 2C) (5- DE HT2C) (5-HTR2C) (5HT-1C). GN Name=HTR2C; Synonyms=HTR1C; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=92109767; PubMed=1722404; RA Saltzman A.G., Morse B., Whitman M.M., Ivanshchenko Y., Jaye M., RA Felder S.; RT "Cloning of the human serotonin 5-HT2 and 5-HT1C receptor subtypes."; RL Biochem. Biophys. Res. Commun. 181:1469-1478(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC TISSUE=Hippocampus, and Placenta; RX MEDLINE=95203331; PubMed=7895773; DOI=10.1016/0922-4106(94)90042-6; RA Stam N.J., Vanderheyden P., Van Alebeek C., Klomp J., De Boer T., RA Van Delft A.M.L., Olijve W.; RT "Genomic organisation and functional expression of the gene encoding RT the human serotonin 5-HT2C receptor."; RL Eur. J. Pharmacol. 269:339-348(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=97001158; PubMed=8812491; DOI=10.1006/geno.1996.0397; RA Xie E., Zhao L., Levine A.J., Shenk T., Chang L.-S.; RT "The human serotonin 5-HT2C receptor: complete cDNA, genomic RT structure, and alternatively spliced variant."; RL Genomics 35:551-561(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING OF POSITIONS 156; 158 AND RP 160. RC TISSUE=Brain; RX MEDLINE=99127198; PubMed=9928237; RX DOI=10.1111/j.1749-6632.1998.tb10171.x; RA Niswender C.M., Sanders-Bush E., Emeson R.B.; RT "Identification and characterization of RNA editing events within the RT 5-HT2C receptor."; RL Ann. N. Y. Acad. Sci. 861:38-48(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [7] 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 [8] RP INTERACTION WITH MPDZ, DOMAIN, MUTAGENESIS OF SER-456; SER-457 AND RP VAL-458, AND GLYCOSYLATION. RX MEDLINE=21201137; PubMed=11150294; DOI=10.1074/jbc.M008089200; RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J., RA Luebbert H., Ullmer C.; RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with RT PDZ10 of the multi-PDZ domain protein MUPP1."; RL J. Biol. Chem. 276:12974-12982(2001). RN [9] RP VARIANT SER-23. RX MEDLINE=96044432; PubMed=7557992; RA Lappalainen J., Zhang L., Dean M., Oz M., Ozaki N., Yu D., RA Virkkunen M., Weight F., Linnoila M., Goldman D.; RT "Identification, expression, and pharmacology of a Cys23-Ser23 RT substitution in the human 5-HT2c receptor gene (HTR2C)."; RL Genomics 27:274-279(1995). RN [10] RP VARIANT SER-23. RX MEDLINE=99221071; PubMed=10206230; RX DOI=10.1002/(SICI)1096-8628(19990416)88:2<126::AID-AJMG6>3.3.CO;2-D; RA Samochowiec J., Smolka M., Winterer G., Rommelspacher H., RA Schmidt L.G., Sander T.; RT "Association analysis between a Cys23Ser substitution polymorphism of RT the human 5-HT2c receptor gene and neuronal hyperexcitability."; RL Am. J. Med. Genet. 88:126-130(1999). RN [11] RP VARIANT SER-23. RX MEDLINE=20049881; PubMed=10581480; RX DOI=10.1002/(SICI)1096-8628(19991215)88:6<621::AID-AJMG9>3.0.CO;2-H; RA Marshall S.E., Bird T.G., Hart K., Welsh K.I.; RT "Unified approach to the analysis of genetic variation in serotonergic RT pathways."; RL Am. J. Med. Genet. 88:621-627(1999). RN [12] RP VARIANT SER-23. RX MEDLINE=99318093; PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [13] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC -!- SUBUNIT: Interacts with MPDZ. CC -!- INTERACTION: CC Q91YI4:Arrb2 (xeno); NbExp=1; IntAct=EBI-994141, EBI-994161; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with MPDZ. CC -!- PTM: N-glycosylated. CC -!- RNA EDITING: Modified_positions=156, 158, 160; Note=Partially CC edited. RNA editing generates receptor isoforms that differ in CC their ability to interact with the phospholipase C signaling CC cascade in a transfected cell line, suggesting that this RNA CC processing event may contribute to the modulation of serotonergic CC neurotransmission in the central nervous system. CC -!- POLYMORPHISM: Position 23 is polymorphic; the frequencies in CC unrelated Caucasians are 0.87 for Cys and 0.13 for Ser. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M81778; AAA60317.1; -; mRNA. DR EMBL; X80763; CAB59978.1; -; Genomic_DNA. DR EMBL; U49516; AAB40898.1; -; mRNA. DR EMBL; AF208053; AAF35842.1; -; mRNA. DR EMBL; AF498983; AAM21130.1; -; mRNA. DR EMBL; AC004822; AAC71658.1; -; Genomic_DNA. DR EMBL; AL355812; CAI41335.1; -; Genomic_DNA. DR EMBL; AL590097; CAI41335.1; JOINED; Genomic_DNA. DR EMBL; AC004822; CAI41335.1; JOINED; Genomic_DNA. DR EMBL; AL590097; CAH70193.1; -; Genomic_DNA. DR EMBL; AC004822; CAH70193.1; JOINED; Genomic_DNA. DR EMBL; AL355812; CAH70193.1; JOINED; Genomic_DNA. DR EMBL; BC095543; AAH95543.1; -; mRNA. DR PIR; JS0616; JS0616. DR UniGene; Hs.149037; -. DR HSSP; P08913; 1HLL. DR IntAct; P28335; -. DR Ensembl; ENSG00000147246; Homo sapiens. DR KEGG; hsa:3358; -. DR HGNC; HGNC:5295; HTR2C. DR MIM; 312861; gene. DR DrugBank; APRD00319; Fenfluramine. DR DrugBank; APRD00735; Minaprine. DR DrugBank; APRD00685; Mirtazapine. DR DrugBank; APRD00138; Olanzapine. DR DrugBank; APRD00358; Promazine. DR DrugBank; APRD00339; Propiomazine. DR DrugBank; APRD00675; Quetiapine. DR DrugBank; APRD00323; Thiethylperazine. DR DrugBank; APRD00540; Ziprasidone. DR ArrayExpress; P28335; -. DR GermOnline; ENSG00000147246; Homo sapiens. DR RZPD-ProtExp; RZPDo834A0645; -. DR RZPD-ProtExp; T0336; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007631; P:feeding behavior; TAS:ProtInc. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR InterPro; IPR000377; 5HT2C_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00517; 5HT2CRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism; KW Receptor; RNA editing; Transducer; Transmembrane. FT CHAIN 1 458 5-hydroxytryptamine 2C receptor. FT /FTId=PRO_0000068958. FT TOPO_DOM 1 52 Extracellular (Potential). FT TRANSMEM 53 78 1 (Potential). FT TOPO_DOM 79 89 Cytoplasmic (Potential). FT TRANSMEM 90 110 2 (Potential). FT TOPO_DOM 111 127 Extracellular (Potential). FT TRANSMEM 128 150 3 (Potential). FT TOPO_DOM 151 170 Cytoplasmic (Potential). FT TRANSMEM 171 193 4 (Potential). FT TOPO_DOM 194 213 Extracellular (Potential). FT TRANSMEM 214 235 5 (Potential). FT TOPO_DOM 236 311 Cytoplasmic (Potential). FT TRANSMEM 312 333 6 (Potential). FT TOPO_DOM 334 348 Extracellular (Potential). FT TRANSMEM 349 371 7 (Potential). FT TOPO_DOM 372 458 Cytoplasmic (Potential). FT MOTIF 456 458 PDZ-binding. FT CARBOHYD 39 39 N-linked (GlcNAc...) (Probable). FT DISULFID 127 207 By similarity. FT VARIANT 23 23 C -> S (in dbSNP:rs6318). FT /FTId=VAR_003450. FT VARIANT 156 156 I -> V (in RNA edited version). FT /FTId=VAR_010166. FT VARIANT 158 158 N -> S (in RNA edited version). FT /FTId=VAR_010167. FT VARIANT 160 160 I -> V (in RNA edited version). FT /FTId=VAR_010168. FT MUTAGEN 456 456 S->A: Loss of interaction with MPDZ. FT MUTAGEN 456 456 S->T: No effect on interaction with MPDZ. FT MUTAGEN 457 457 S->A: No effect on interaction with MPDZ. FT MUTAGEN 458 458 V->A: Loss of interaction with MPDZ. SQ SEQUENCE 458 AA; 51821 MW; 9E76B3FFD3E09C93 CRC64; MVNLRNAVHS FLVHLIGLLV WQCDISVSPV AAIVTDIFNT SDGGRFKFPD GVQNWPALSI VIIIIMTIGG NILVIMAVSM EKKLHNATNY FLMSLAIADM LVGLLVMPLS LLAILYDYVW PLPRYLCPVW ISLDVLFSTA SIMHLCAISL DRYVAIRNPI EHSRFNSRTK AIMKIAIVWA ISIGVSVPIP VIGLRDEEKV FVNNTTCVLN DPNFVLIGSF VAFFIPLTIM VITYCLTIYV LRRQALMLLH GHTEEPPGLS LDFLKCCKRN TAEEENSANP NQDQNARRRK KKERRPRGTM QAINNERKAS KVLGIVFFVF LIMWCPFFIT NILSVLCEKS CNQKLMEKLL NVFVWIGYVC SGINPLVYTL FNKIYRRAFS NYLRCNYKVE KKPPVRQIPR VAATALSGRE LNVNIYRHTN EPVIEKASDN EPGIEMQVEN LELPVNPSSV VSERISSV // ID 5HT2C_MOUSE Reviewed; 459 AA. AC P34968; Q5WRU6; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 20-FEB-2007, entry version 56. DE 5-hydroxytryptamine 2C receptor (5-HT-2C) (Serotonin receptor 2C) (5- DE HT2C) (5-HTR2C) (5HT-1C). GN Name=Htr2c; Synonyms=5ht1c, Htr1c; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92099829; PubMed=1661811; DOI=10.1016/0169-328X(91)90116-F; RA Yu L., Nguyen H., Le H., Bloem L.J., Kozak C.A., Hoffman B.J., RA Snutch T.P., Lester H.A., Davidson N., Luebbert H.; RT "The mouse 5-HT1C receptor contains eight hydrophobic domains and is RT X-linked."; RL Brain Res. Mol. Brain Res. 11:143-149(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92385744; PubMed=1381232; RA Foguet M., Nguyen H., Le H., Luebbert H.; RT "Structure of the mouse 5-HT1C, 5-HT2 and stomach fundus serotonin RT receptor genes."; RL NeuroReport 3:345-348(1992). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC -!- SUBUNIT: Interacts with MPDZ (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with MPDZ (By similarity). CC -!- PTM: N-glycosylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X72230; CAA51031.1; -; mRNA. DR EMBL; S44559; AAA10521.1; -; Genomic_DNA. DR EMBL; S44556; AAA10521.1; JOINED; Genomic_DNA. DR EMBL; S44557; AAA10521.1; JOINED; Genomic_DNA. DR EMBL; S44558; AAA10521.1; JOINED; Genomic_DNA. DR PIR; A43951; A43951. DR UniGene; Mm.391323; -. DR Ensembl; ENSMUSG00000041380; Mus musculus. DR KEGG; mmu:15560; -. DR MGI; MGI:96281; Htr2c. DR ArrayExpress; P34968; -. DR GermOnline; ENSMUSG00000041380; Mus musculus. DR InterPro; IPR000377; 5HT2C_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00517; 5HT2CRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 459 5-hydroxytryptamine 2C receptor. FT /FTId=PRO_0000068959. FT TOPO_DOM 1 53 Extracellular (Potential). FT TRANSMEM 54 79 1 (Potential). FT TOPO_DOM 80 90 Cytoplasmic (Potential). FT TRANSMEM 91 111 2 (Potential). FT TOPO_DOM 112 128 Extracellular (Potential). FT TRANSMEM 129 151 3 (Potential). FT TOPO_DOM 152 171 Cytoplasmic (Potential). FT TRANSMEM 172 194 4 (Potential). FT TOPO_DOM 195 214 Extracellular (Potential). FT TRANSMEM 215 236 5 (Potential). FT TOPO_DOM 237 312 Cytoplasmic (Potential). FT TRANSMEM 313 334 6 (Potential). FT TOPO_DOM 335 349 Extracellular (Potential). FT TRANSMEM 350 372 7 (Potential). FT TOPO_DOM 373 459 Cytoplasmic (Potential). FT MOTIF 457 459 PDZ-binding. FT CARBOHYD 39 39 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 204 204 N-linked (GlcNAc...) (Potential). FT CARBOHYD 205 205 N-linked (GlcNAc...) (Potential). FT DISULFID 128 208 By similarity. SQ SEQUENCE 459 AA; 51874 MW; E25A1BACCE794079 CRC64; MVNLGTAVRS LLVHLIGLLV WQFDISISPV AAIVTDTFNS SDGGRLFQFP DGVQNWPALS IVVIIIMTIG GNILVIMAVS MEKKLHNATN YFLMSLAIAD MLVGLLVMPL SLLAILYDYV WPLPRYLCPV WISLDVLFST ASIMHLCAIS LDRYVAVRSP VEHSRFNSRT KAIMKIAIVW AISIGVSVPI PVIGLRDESK VFVNNTTCVL NDPNFVLIGS FVAFFIPLTI MVITYFLTIY VLRRQTLMLL RGHTEEELRN ISLNFLKCCC KKGDEEENAP NPNPDQKPRR KKKEKRPRGT MQAINNEKKA SKVLGIVFFV FLIMWCPFFI TNILSVLCGK ACNQKLMEKL LNVFVWIGYV CSGINPLVYT LFNKIYRRAF SKYLRCDYKP DKKPPVRQIP RVAATALSGR ELNVNIYRHT NERVVRKAND TEPGIEMQVE NLELPVNPSN VVSERISSV // ID 5HT2C_PANTR Reviewed; 458 AA. AC Q5IS66; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 31-OCT-2006, entry version 15. DE 5-hydroxytryptamine 2C receptor (5-HT-2C) (Serotonin receptor 2C) (5- DE HT2C) (5-HTR2C). GN Name=HTR2C; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040; RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L., RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.; RT "Accelerated evolution of nervous system genes in the origin of Homo RT sapiens."; RL Cell 119:1027-1040(2004). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system (By CC similarity). CC -!- SUBUNIT: Interacts with MPDZ (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with MPDZ (By similarity). CC -!- PTM: N-glycosylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY665262; AAV74300.1; -; mRNA. DR KEGG; ptr:473740; -. DR InterPro; IPR000377; 5HT2C_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00517; 5HT2CRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 458 5-hydroxytryptamine 2C receptor. FT /FTId=PRO_0000068960. FT TOPO_DOM 1 52 Extracellular (Potential). FT TRANSMEM 53 78 1 (Potential). FT TOPO_DOM 79 89 Cytoplasmic (Potential). FT TRANSMEM 90 110 2 (Potential). FT TOPO_DOM 111 127 Extracellular (Potential). FT TRANSMEM 128 150 3 (Potential). FT TOPO_DOM 151 170 Cytoplasmic (Potential). FT TRANSMEM 171 193 4 (Potential). FT TOPO_DOM 194 213 Extracellular (Potential). FT TRANSMEM 214 235 5 (Potential). FT TOPO_DOM 236 311 Cytoplasmic (Potential). FT TRANSMEM 312 333 6 (Potential). FT TOPO_DOM 334 348 Extracellular (Potential). FT TRANSMEM 349 371 7 (Potential). FT TOPO_DOM 372 458 Cytoplasmic (Potential). FT MOTIF 456 458 PDZ-binding. FT CARBOHYD 39 39 N-linked (GlcNAc...) (By similarity). FT DISULFID 127 207 By similarity. SQ SEQUENCE 458 AA; 51834 MW; 3E9E05260351C6CC CRC64; MVNLRNAVHS FLVHLIGLLV WQCDISVSPV AAIVTDIFNT SDGGRFKFPD GVQNWPALSI VVIIIMTIGG NILVIMAVSM EKKLHNATNY FLMSLAIADM LVGLLVMPLS LLAILYDYVW PLPRYLCPVW ISLDVLFSTA SIMHLCAISL DRYVAIRNPI EHSRFNSRTK AIMKIAIVWA ISIGVSVPIP VIGLRDERKV FVNNTTCVLN DPNFVLIGSF VAFFIPLTIM VITYCLTIYV LRRQALMLLH GHTEEPPGLS LDFLKCCKRN TAEEENSANP NQDQNARRRK KKERRPRGTM QAINNERKAS KVLGIVFFVF LIMWCPFFIT NILSVLCEKS CNQKLMEKLL NVFVWIGYVC SGINPLVYTL FNKIYRRAFS NYLRCNYKVE KKPPVRQIPR VAATALSGRE LNVNIYRHTN EPVIEKASDN EPGIEMQVEN LELPVNPSSV VSERISSV // ID 5HT2C_RAT Reviewed; 460 AA. AC P08909; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 06-FEB-2007, entry version 68. DE 5-hydroxytryptamine 2C receptor (5-HT-2C) (Serotonin receptor 2C) (5- DE HT2C) (5-HTR2C) (5HT-1C). GN Name=Htr2c; Synonyms=5ht1c, Htr1c; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88290673; PubMed=3399891; RA Julius D., McDermott A.B., Axel R., Jessell T.M.; RT "Molecular characterization of a functional cDNA encoding the RT serotonin 1c receptor."; RL Science 241:558-564(1988). RN [2] RP INTERACTION WITH MPDZ, AND MUTAGENESIS OF SER-458 AND SER-459. RX MEDLINE=22679206; PubMed=12682077; DOI=10.1074/jbc.M210973200; RA Parker L.L., Backstrom J.R., Sanders-Bush E., Shieh B.H.; RT "Agonist-induced phosphorylation of the serotonin 5-HT2C receptor RT regulates its interaction with multiple PDZ protein 1."; RL J. Biol. Chem. 278:21576-21583(2003). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC -!- SUBUNIT: Interacts with MPDZ. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with MPDZ. CC -!- PTM: N-glycosylated (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M21410; AAA42177.1; -; Genomic_DNA. DR PIR; A32605; A32605. DR UniGene; Rn.9935; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSRNOG00000030877; Rattus norvegicus. DR KEGG; rno:25187; -. DR RGD; 2848; Htr2c. DR ArrayExpress; P08909; -. DR GermOnline; ENSRNOG00000030877; Rattus norvegicus. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0004993; F:serotonin receptor activity; IDA:MGI. DR GO; GO:0007187; P:G-protein signaling, coupled to cyclic nucl...; TAS:RGD. DR GO; GO:0048016; P:inositol phosphate-mediated signaling; IDA:MGI. DR InterPro; IPR000377; 5HT2C_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00517; 5HT2CRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 460 5-hydroxytryptamine 2C receptor. FT /FTId=PRO_0000068961. FT TOPO_DOM 1 53 Extracellular (Potential). FT TRANSMEM 54 79 1 (Potential). FT TOPO_DOM 80 90 Cytoplasmic (Potential). FT TRANSMEM 91 111 2 (Potential). FT TOPO_DOM 112 128 Extracellular (Potential). FT TRANSMEM 129 151 3 (Potential). FT TOPO_DOM 152 171 Cytoplasmic (Potential). FT TRANSMEM 172 194 4 (Potential). FT TOPO_DOM 195 214 Extracellular (Potential). FT TRANSMEM 215 236 5 (Potential). FT TOPO_DOM 237 313 Cytoplasmic (Potential). FT TRANSMEM 314 335 6 (Potential). FT TOPO_DOM 336 350 Extracellular (Potential). FT TRANSMEM 351 373 7 (Potential). FT TOPO_DOM 374 460 Cytoplasmic (Potential). FT MOTIF 458 460 PDZ-binding. FT CARBOHYD 39 39 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 204 204 N-linked (GlcNAc...) (Potential). FT CARBOHYD 205 205 N-linked (GlcNAc...) (Potential). FT DISULFID 128 208 By similarity. FT MUTAGEN 458 458 S->A,D: Loss of interaction with MPDZ. FT MUTAGEN 459 459 S->D: No effect on interaction with MPDZ. SQ SEQUENCE 460 AA; 51917 MW; D44E977D8F80047E CRC64; MVNLGNAVRS LLMHLIGLLV WQFDISISPV AAIVTDTFNS SDGGRLFQFP DGVQNWPALS IVVIIIMTIG GNILVIMAVS MEKKLHNATN YFLMSLAIAD MLVGLLVMPL SLLAILYDYV WPLPRYLCPV WISLDVLFST ASIMHLCAIS LDRYVAIRNP IEHSRFNSRT KAIMKIAIVW AISIGVSVPI PVIGLRDESK VFVNNTTCVL NDPNFVLIGS FVAFFIPLTI MVITYFLTIY VLRRQTLMLL RGHTEEELAN MSLNFLNCCC KKNGGEEENA PNPNPDQKPR RKKKEKRPRG TMQAINNEKK ASKVLGIVFF VFLIMWCPFF ITNILSVLCG KACNQKLMEK LLNVFVWIGY VCSGINPLVY TLFNKIYRRA FSKYLRCDYK PDKKPPVRQI PRVAATALSG RELNVNIYRH TNERVARKAN DPEPGIEMQV ENLELPVNPS NVVSERISSV // ID 5HT3R_CAVPO Reviewed; 490 AA. AC O70212; O70213; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 28-NOV-2006, entry version 45. DE 5-hydroxytryptamine 3 receptor precursor (5-HT-3) (Serotonin-gated ion DE channel receptor) (5-HT3R). GN Name=HTR3A; Synonyms=5HT3R, HTR3; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE RP SPECIFICITY, AND PHARMACOLOGICAL CHARACTERIZATION. RC TISSUE=Small intestine; RX MEDLINE=98130690; PubMed=9463477; RA Lankiewicz S., Lobitz N., Wetzel C.H.R., Rupprecht R., Gisselmann G., RA Hatt H.; RT "Molecular cloning, functional expression, and pharmacological RT characterization of 5-hydroxytryptamine3 receptor cDNA and its splice RT variants from guinea pig."; RL Mol. Pharmacol. 53:202-212(1998). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor is CC a ligand-gated ion channel, which when activated causes fast, CC depolarizing responses in neurons. It is a cation-specific, but CC otherwise relatively nonselective, ion channel. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=5-HT3R-L; CC IsoId=O70212-1; Sequence=Displayed; CC Name=2; Synonyms=5-HT3R-S; CC IsoId=O70212-2; Sequence=VSP_000077; CC -!- TISSUE SPECIFICITY: Expressed in cortex, intestine and liver. Not CC expressed in muscle or spleen. CC -!- SIMILARITY: Belongs to the ligand-gated ionic channel (TC 1.A.9) 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; AF006461; AAC06136.1; -; mRNA. DR EMBL; AF006462; AAC06137.1; -; mRNA. DR GO; GO:0030285; C:integral to synaptic vesicle membrane; IDA:UniProtKB. DR GO; GO:0004890; F:GABA-A receptor activity; IDA:UniProtKB. DR GO; GO:0006812; P:cation transport; IDA:UniProtKB. DR InterPro; IPR008132; 5HT3_rcpt. DR InterPro; IPR008133; 5HT3_rcpt_A. DR InterPro; IPR006029; Neu_channel_TM. DR InterPro; IPR006202; Neur_chan_lig_bd. DR InterPro; IPR006201; Neur_channel. DR Gene3D; G3DSA:3.30.1100.20; Neur_chan_lig_bd; 1. DR PANTHER; PTHR18945; Neur_channel; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR01709; 5HT3ARECEPTR. DR PRINTS; PR01708; 5HT3RECEPTOR. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Alternative splicing; Glycoprotein; Ion transport; Ionic channel; KW Membrane; Postsynaptic membrane; Receptor; Signal; Transmembrane; KW Transport. FT SIGNAL 1 19 Potential. FT CHAIN 20 490 5-hydroxytryptamine 3 receptor. FT /FTId=PRO_0000000407. FT TOPO_DOM 20 249 Extracellular (Potential). FT TRANSMEM 250 270 1 (Potential). FT TOPO_DOM 271 285 Cytoplasmic (Potential). FT TRANSMEM 286 306 2 (Potential). FT TOPO_DOM 307 312 Extracellular (Potential). FT TRANSMEM 313 333 3 (Potential). FT TOPO_DOM 334 467 Cytoplasmic (Potential). FT TRANSMEM 468 488 4 (Potential). FT TOPO_DOM 489 490 Extracellular (Potential). FT CARBOHYD 33 33 N-linked (GlcNAc...) (Potential). FT CARBOHYD 109 109 N-linked (GlcNAc...) (Potential). FT CARBOHYD 175 175 N-linked (GlcNAc...) (Potential). FT CARBOHYD 191 191 N-linked (GlcNAc...) (Potential). FT DISULFID 162 176 By similarity. FT VAR_SEQ 386 391 Missing (in isoform 2). FT /FTId=VSP_000077. SQ SEQUENCE 490 AA; 55656 MW; EDB32F8597494F61 CRC64; MVLWLQLALL ALLLPTSLAQ GEVRGKGTAQ AHNSTRPALQ RLSDHLLADY RKSVRPVRDW RKPTTVSIDA IVYAILSVDE KNQVLTTYIW YRQFWTDEFL QWNPEDFDNI TKLSIPTDSI WVPDILINEF VDVGKSPNIP YVYVRHQGEV QNYKPLQVVT ACSLDIYNFP FDVQNCSLTF TSWLHTIQDI NISLWRLPEK VKSDKSVFMN QGEWELLGVL TEFLEFSDRE SRGSFAEMKF YVVIRRRPLF YAVTLLLPSI FLMIVDIVGF YLPPDSGERV SFKITLLLGY SVFLIIVSDT LPATAIGTPL ISVYFVVCMA LLVISLAETI LIVRLVHKQD LQQPVPLWLR HLVLERIAGL LCLGEQLTSH RGPATLQATK TDDFSGSTLL PAMGNHCGPL GGPQDLEKTS RGRGSPPPPP REASLAMCGL LQELASIRHF LEKREETREV ARDWLRVGSV LDKLLFRVYL LAVLAYSITL VTLWSVWHYA // ID 5HT3R_HUMAN Reviewed; 478 AA. AC P46098; O60854; Q99918; Q9BSZ9; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-FEB-2007, entry version 72. DE 5-hydroxytryptamine 3 receptor precursor (5-HT-3) (Serotonin-gated ion DE channel receptor) (5-HT3R). GN Name=HTR3A; Synonyms=5HT3R, HTR3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Hippocampus; RX MEDLINE=96018832; PubMed=7565620; RA Miyake A., Mochizuki S., Takemoto Y., Akuzawa S.; RT "Molecular cloning of human 5-hydroxytryptamine3 receptor: RT heterogeneity in distribution and function among species."; RL Mol. Pharmacol. 48:407-416(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Amygdala; RX MEDLINE=96110993; PubMed=8848005; RA Belelli D., Balcarek J.M., Hope A.G., Peters J.A., Lambert J.J., RA Blackburn T.P.; RT "Cloning and functional expression of a human 5-hydroxytryptamine type RT 3AS receptor subunit."; RL Mol. Pharmacol. 48:1054-1062(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, and Hippocampus; RX MEDLINE=99127223; PubMed=9928262; RX DOI=10.1111/j.1749-6632.1998.tb10196.x; RA Bruess M., Goethert M., Hayer M., Bonisch H.; RT "Molecular cloning of alternatively spliced human 5HT3 receptor RT cDNAs."; RL Ann. N. Y. Acad. Sci. 861:234-235(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Blood; RX MEDLINE=20133886; PubMed=10670426; DOI=10.1016/S0028-3908(99)00116-1; RA Bruess M., Eucker T., Goethert M., Bonisch H.; RT "Exon-intron organization of the human 5-HT3A receptor gene."; RL Neuropharmacology 39:308-315(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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 is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor is CC a ligand-gated ion channel, which when activated causes fast, CC depolarizing responses in neurons. It is a cation-specific, but CC otherwise relatively nonselective, ion channel. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=5-HT3R-AS; CC IsoId=P46098-1; Sequence=Displayed; CC Name=2; Synonyms=5-HT3R-AL; CC IsoId=P46098-2; Sequence=VSP_000078; CC -!- SIMILARITY: Belongs to the ligand-gated ionic channel (TC 1.A.9) 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; D49394; BAA08387.1; -; mRNA. DR EMBL; S82612; AAB37533.2; -; mRNA. DR EMBL; AJ003078; CAA05851.1; -; mRNA. DR EMBL; AJ003079; CAA05852.1; -; mRNA. DR EMBL; AJ005205; CAA06442.3; -; Genomic_DNA. DR EMBL; AF498984; AAM21131.1; -; mRNA. DR EMBL; BC002354; AAH02354.1; -; mRNA. DR EMBL; BC004453; AAH04453.2; -; mRNA. DR UniGene; Hs.413899; -. DR Ensembl; ENSG00000166736; Homo sapiens. DR KEGG; hsa:3359; -. DR H-InvDB; HIX0010139; -. DR HGNC; HGNC:5297; HTR3A. DR MIM; 182139; gene. DR DrugBank; APRD00580; Alosetron. DR DrugBank; APRD00404; Chloroprocaine. DR DrugBank; APRD00518; Dolasetron. DR DrugBank; APRD01002; Granisetron. DR DrugBank; APRD00685; Mirtazapine. DR DrugBank; APRD00481; Ondansetron. DR DrugBank; APRD00351; Palonosetron. DR DrugBank; APRD00650; Procaine. DR ArrayExpress; P46098; -. DR GermOnline; ENSG00000166736; Homo sapiens. DR RZPD-ProtExp; A1298; -. DR RZPD-ProtExp; IOH46144; -. DR RZPD-ProtExp; T3082; -. DR RZPD-ProtExp; Z0321; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004993; F:serotonin receptor activity; NAS:UniProtKB. DR GO; GO:0005232; F:serotonin-activated cation-selective channe...; TAS:ProtInc. DR GO; GO:0007586; P:digestion; TAS:ProtInc. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR GO; GO:0006810; P:transport; NAS:UniProtKB. DR InterPro; IPR008132; 5HT3_rcpt. DR InterPro; IPR008133; 5HT3_rcpt_A. DR InterPro; IPR006029; Neu_channel_TM. DR InterPro; IPR006202; Neur_chan_lig_bd. DR InterPro; IPR006201; Neur_channel. DR Gene3D; G3DSA:3.30.1100.20; Neur_chan_lig_bd; 1. DR PANTHER; PTHR18945; Neur_channel; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR01709; 5HT3ARECEPTR. DR PRINTS; PR01708; 5HT3RECEPTOR. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Alternative splicing; Glycoprotein; Ion transport; Ionic channel; KW Membrane; Postsynaptic membrane; Receptor; Signal; Transmembrane; KW Transport. FT SIGNAL 1 23 Potential. FT CHAIN 24 478 5-hydroxytryptamine 3 receptor. FT /FTId=PRO_0000000408. FT TOPO_DOM 24 241 Extracellular (Potential). FT TRANSMEM 242 268 1 (Potential). FT TOPO_DOM 269 273 Cytoplasmic (Potential). FT TRANSMEM 274 292 2 (Potential). FT TOPO_DOM 293 302 Extracellular (Potential). FT TRANSMEM 303 321 3 (Potential). FT TOPO_DOM 322 455 Cytoplasmic (Potential). FT TRANSMEM 456 475 4 (Potential). FT TOPO_DOM 476 478 Extracellular (Potential). FT CARBOHYD 28 28 N-linked (GlcNAc...) (Potential). FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT CARBOHYD 170 170 N-linked (GlcNAc...) (Potential). FT CARBOHYD 186 186 N-linked (GlcNAc...) (Potential). FT DISULFID 157 171 By similarity. FT VAR_SEQ 306 306 G -> GKAPPGSRAQSGEKPAPSHLLHVSLASALGCTG FT (in isoform 2). FT /FTId=VSP_000078. FT CONFLICT 46 46 R -> T (in Ref. 2). FT CONFLICT 125 125 F -> L (in Ref. 2). FT CONFLICT 321 321 A -> T (in Ref. 2). FT CONFLICT 386 386 S -> T (in Ref. 2). SQ SEQUENCE 478 AA; 55280 MW; 24CA9A232286FBC9 CRC64; MLLWVQQALL ALLLPTLLAQ GEARRSRNTT RPALLRLSDY LLTNYRKGVR PVRDWRKPTT VSIDVIVYAI LNVDEKNQVL TTYIWYRQYW TDEFLQWNPE DFDNITKLSI PTDSIWVPDI LINEFVDVGK SPNIPYVYIR HQGEVQNYKP LQVVTACSLD IYNFPFDVQN CSLTFTSWLH TIQDINISLW RLPEKVKSDR SVFMNQGEWE LLGVLPYFRE FSMESSNYYA EMKFYVVIRR RPLFYVVSLL LPSIFLMVMD IVGFYLPPNS GERVSFKITL LLGYSVFLII VSDTLPATAI GTPLIGVYFV VCMALLVISL AETIFIVRLV HKQDLQQPVP AWLRHLVLER IAWLLCLREQ STSQRPPATS QATKTDDCSA MGNHCSHMGG PQDFEKSPRD RCSPPPPPRE ASLAVCGLLQ ELSSIRQFLE KRDEIREVAR DWLRVGSVLD KLLFHIYLLA VLAYSITLVM LWSIWQYA // ID 5HT3R_MOUSE Reviewed; 487 AA. AC P23979; Q61225; Q61226; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 23-JAN-2007, entry version 65. DE 5-hydroxytryptamine 3 receptor precursor (5-HT-3) (Serotonin-gated ion DE channel receptor) (5-HT3R). GN Name=Htr3a; Synonyms=5ht3, Htr3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92022603; PubMed=1718042; RA Maricq A.V., Peterson A.S., Brake A.J., Myers R.M., Julius D.; RT "Primary structure and functional expression of the 5HT3 receptor, a RT serotonin-gated ion channel."; RL Science 254:432-437(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BALB/c; TISSUE=Brain; RX MEDLINE=94156052; PubMed=8112471; DOI=10.1016/0014-5793(94)80435-4; RA Uetz P., Abdelatty F., Villarroel A., Gundrun R., Weiss B., Koenen M.; RT "Organisation of the murine 5-HT3 receptor gene and assignment to RT human chromosome 11."; RL FEBS Lett. 339:302-306(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=A/J; RX MEDLINE=93259238; PubMed=7683998; DOI=10.1016/0922-4106(93)90128-V; RA Hope A.G., Downie D.L., Sutherland L., Lambert J.J., Peters J.A., RA Burchell B.; RT "Cloning and functional expression of an apparent splice variant of RT the murine 5-HT3 receptor A subunit."; RL Eur. J. Pharmacol. 245:187-192(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RC STRAIN=129/Sv; RX MEDLINE=95157178; PubMed=7854052; DOI=10.1016/0169-328X(94)90095-7; RA Werner P., Kawashima E., Reid J., Hussy N., Lundstrom K., Buell G., RA Humbert Y., Jones K.A.; RT "Organization of the mouse 5-HT3 receptor gene and functional RT expression of two splice variants."; RL Brain Res. Mol. Brain Res. 26:233-241(1994). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor is CC a ligand-gated ion channel, which when activated causes fast, CC depolarizing responses in neurons. It is a cation-specific, but CC otherwise relatively nonselective, ion channel. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=5-HT3R-A; CC IsoId=P23979-1; Sequence=Displayed; CC Name=5-HT3R-AS; CC IsoId=P23979-2; Sequence=VSP_000079; CC -!- TISSUE SPECIFICITY: Brain, spinal cord, and heart. CC -!- SIMILARITY: Belongs to the ligand-gated ionic channel (TC 1.A.9) 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; M74425; AAA37124.1; -; mRNA. DR EMBL; Z22772; CAA80453.1; -; Genomic_DNA. DR EMBL; Z22773; CAA80453.1; JOINED; Genomic_DNA. DR EMBL; X72395; CAA51089.1; -; mRNA. DR EMBL; X79283; CAA55870.1; -; Genomic_DNA. DR EMBL; X79283; CAA55871.1; -; Genomic_DNA. DR PIR; S41757; S41757. DR UniGene; Mm.4831; -. DR Ensembl; ENSMUSG00000032269; Mus musculus. DR KEGG; mmu:15561; -. DR MGI; MGI:96282; Htr3a. DR ArrayExpress; P23979; -. DR GermOnline; ENSMUSG00000032269; Mus musculus. DR InterPro; IPR008132; 5HT3_rcpt. DR InterPro; IPR008133; 5HT3_rcpt_A. DR InterPro; IPR006029; Neu_channel_TM. DR InterPro; IPR006202; Neur_chan_lig_bd. DR InterPro; IPR006201; Neur_channel. DR Gene3D; G3DSA:3.30.1100.20; Neur_chan_lig_bd; 1. DR PANTHER; PTHR18945; Neur_channel; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR01709; 5HT3ARECEPTR. DR PRINTS; PR01708; 5HT3RECEPTOR. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Alternative splicing; Glycoprotein; Ion transport; Ionic channel; KW Membrane; Postsynaptic membrane; Receptor; Signal; Transmembrane; KW Transport. FT SIGNAL 1 23 Potential. FT CHAIN 24 487 5-hydroxytryptamine 3 receptor. FT /FTId=PRO_0000000409. FT TOPO_DOM 24 245 Extracellular (Potential). FT TRANSMEM 246 272 1 (Potential). FT TOPO_DOM 273 277 Cytoplasmic (Potential). FT TRANSMEM 278 296 2 (Potential). FT TOPO_DOM 297 305 Extracellular (Potential). FT TRANSMEM 306 324 3 (Potential). FT TOPO_DOM 325 464 Cytoplasmic (Potential). FT TRANSMEM 465 484 4 (Potential). FT TOPO_DOM 485 487 Extracellular (Potential). FT CARBOHYD 108 108 N-linked (GlcNAc...) (Potential). FT CARBOHYD 174 174 N-linked (GlcNAc...) (Potential). FT CARBOHYD 190 190 N-linked (GlcNAc...) (Potential). FT DISULFID 161 175 By similarity. FT VAR_SEQ 383 388 Missing (in isoform 5-HT3R-AS). FT /FTId=VSP_000079. FT CONFLICT 31 31 E -> AR (in Ref. 3 and 4). FT CONFLICT 74 74 I -> V (in Ref. 3). FT CONFLICT 302 302 T -> TA (in Ref. 3 and 4). FT CONFLICT 384 384 S -> SS (in Ref. 2). FT CONFLICT 393 393 H -> T (in Ref. 4). SQ SEQUENCE 487 AA; 56056 MW; D0148867C8536D66 CRC64; MRLCIPQVLL ALFLSMLTAP GEGSRRRATQ EDTTQPALLR LSDHLLANYK KGVRPVRDWR KPTTVSIDVI MYAILNVDEK NQVLTTYIWY RQYWTDEFLQ WTPEDFDNVT KLSIPTDSIW VPDILINEFV DVGKSPNIPY VYVHHRGEVQ NYKPLQLVTA CSLDIYNFPF DVQNCSLTFT SWLHTIQDIN ITLWRSPEEV RSDKSIFINQ GEWELLEVFP QFKEFSIDIS NSYAEMKFYV IIRRRPLFYA VSLLLPSIFL MVVDIVGFCL PPDSGERVSF KITLLLGYSV FLIIVSDTLP ATIGTPLIGV YFVVCMALLV ISLAETIFIV RLVHKQDLQR PVPDWLRHLV LDRIAWILCL GEQPMAHRPP ATFQANKTDD CSGSDLLPAM GNHCSHVGGP QDLEKTPRGR GSPLPPPREA SLAVRGLLQE LSSIRHFLEK RDEMREVARD WLRVGYVLDR LLFRIYLLAV LAYSITLVTL WSIWHYS // ID 5HT3R_RAT Reviewed; 483 AA. AC P35563; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 20-FEB-2007, entry version 56. DE 5-hydroxytryptamine 3 receptor precursor (5-HT-3) (Serotonin-gated ion DE channel receptor) (5-HT3R). GN Name=Htr3a; Synonyms=5ht3, Htr3; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Miyake A., Mochizuki S., Akuzawa S., Kon G.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-483. RX MEDLINE=94154206; PubMed=7509203; RA Isenberg K.E., Ukhun I.A., Holstad S.G., Jafri S., Uchida U., RA Zorumski C.F., Yang J.; RT "Partial cDNA cloning and NGF regulation of a rat 5-HT3 receptor RT subunit."; RL NeuroReport 5:121-124(1993). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor is CC a ligand-gated ion channel, which when activated causes fast, CC depolarizing responses in neurons. It is a cation-specific, but CC otherwise relatively nonselective, ion channel. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the ligand-gated ionic channel (TC 1.A.9) 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; D49395; BAA08388.1; -; mRNA. DR EMBL; U01227; AAA52182.1; -; mRNA. DR UniGene; Rn.55109; -. DR Ensembl; ENSRNOG00000006595; Rattus norvegicus. DR KEGG; rno:79246; -. DR RGD; 61818; Htr3a. DR ArrayExpress; P35563; -. DR GermOnline; ENSRNOG00000006595; Rattus norvegicus. DR GO; GO:0005887; C:integral to plasma membrane; TAS:RGD. DR GO; GO:0005232; F:serotonin-activated cation-selective channe...; IDA:RGD. DR GO; GO:0007268; P:synaptic transmission; TAS:RGD. DR InterPro; IPR008132; 5HT3_rcpt. DR InterPro; IPR008133; 5HT3_rcpt_A. DR InterPro; IPR006029; Neu_channel_TM. DR InterPro; IPR006202; Neur_chan_lig_bd. DR InterPro; IPR006201; Neur_channel. DR Gene3D; G3DSA:3.30.1100.20; Neur_chan_lig_bd; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR01709; 5HT3ARECEPTR. DR PRINTS; PR01708; 5HT3RECEPTOR. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Glycoprotein; Ion transport; Ionic channel; Membrane; KW Postsynaptic membrane; Receptor; Signal; Transmembrane; Transport. FT SIGNAL 1 23 Potential. FT CHAIN 24 483 5-hydroxytryptamine 3 receptor. FT /FTId=PRO_0000000410. FT TOPO_DOM 24 246 Extracellular (Potential). FT TRANSMEM 247 273 1 (Potential). FT TOPO_DOM 274 278 Cytoplasmic (Potential). FT TRANSMEM 279 297 2 (Potential). FT TOPO_DOM 298 307 Extracellular (Potential). FT TRANSMEM 308 326 3 (Potential). FT TOPO_DOM 327 460 Cytoplasmic (Potential). FT TRANSMEM 461 480 4 (Potential). FT TOPO_DOM 481 483 Extracellular (Potential). FT CARBOHYD 109 109 N-linked (GlcNAc...) (Potential). FT CARBOHYD 175 175 N-linked (GlcNAc...) (Potential). FT CARBOHYD 191 191 N-linked (GlcNAc...) (Potential). FT DISULFID 162 176 By similarity. FT CONFLICT 22 22 E -> K (in Ref. 2). FT CONFLICT 306 306 G -> R (in Ref. 2). SQ SEQUENCE 483 AA; 55428 MW; ED85257BBCCF28A4 CRC64; MPLCIPQVLL ALFLSVLIAQ GEGSRRRATQ AHSTTQPALL RLSDHLLANY KKGVRPVRDW RKPTLVSIDV IMYAILNVDE KNQVLTTYIW YRQFWTDEFL QWTPEDFDNV TKLSIPTDSI WVPDILINEF VDVGKSPSIP YVYVHHQGEV QNYKPLQLVT ACSLDIYNFP FDVQNCSLTF TSWLHTIQDI NISLWRTPEE VRSDKSIFIN QGEWELLGVF TKFQEFSIET SNSYAEMKFY VVIRRRPLFY AVSLLLPSIF LMVVDIVGFC LPPDSGERVS FKITLLLGYS VFLIIVSDTL PATAIGTPLI GVYFVVCMAL LVISLAETIF IVQLVHKQDL QRPVPDWLRH LVLDRIAWLL CLGEQPMAHR PPATFQANKT DDCSAMGNHC SHVGSPQDLE KTSRSRDSPL PPPREASLAV RGLLQELSSI RHSLEKRDEM REVARDWLRV GYVLDRLLFR IYLLAVLAYS ITLVTLWSIW HYS // ID 5HT4R_CAVPO Reviewed; 388 AA. AC O70528; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 31-OCT-2006, entry version 40. DE 5-hydroxytryptamine 4 receptor (5-HT-4) (Serotonin receptor 4) (5- DE HT4). GN Name=HTR4; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Van den Wyngaert I., Gommeren W., Jurzak M., Verhasselt P., Gordon R., RA Leysen J., Luyten W., Bender E.; RT "Cloning and expression of 5-HT4 receptor species and splice RT variants."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced; CC Name=1; CC IsoId=O70528-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y13585; CAA73912.1; -; mRNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR001520; 5HT4_rcpt. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01059; 5HT4RECEPTR. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 388 5-hydroxytryptamine 4 receptor. FT /FTId=PRO_0000068964. FT TOPO_DOM 1 19 Extracellular (Potential). FT TRANSMEM 20 40 1 (Potential). FT TOPO_DOM 41 58 Cytoplasmic (Potential). FT TRANSMEM 59 79 2 (Potential). FT TOPO_DOM 80 93 Extracellular (Potential). FT TRANSMEM 94 116 3 (Potential). FT TOPO_DOM 117 137 Cytoplasmic (Potential). FT TRANSMEM 138 158 4 (Potential). FT TOPO_DOM 159 192 Extracellular (Potential). FT TRANSMEM 193 213 5 (Potential). FT TOPO_DOM 214 260 Cytoplasmic (Potential). FT TRANSMEM 261 281 6 (Potential). FT TOPO_DOM 282 294 Extracellular (Potential). FT TRANSMEM 295 315 7 (Potential). FT TOPO_DOM 316 388 Cytoplasmic (Potential). FT LIPID 329 329 S-palmitoyl cysteine (By similarity). FT CARBOHYD 7 7 N-linked (GlcNAc...) (Potential). FT DISULFID 93 184 By similarity. SQ SEQUENCE 388 AA; 43726 MW; 3D45B3A37F60D02B CRC64; MDKLDANVSS KEGFGSVEKV VLLTFLSAVI LMAILGNLLV MVAVCRDRQL RKIKTNYFIV SLAFADLLVS VLVMPFGAIE LVQDIWVYGE MFCLVRTSLD VLLTTASIFH LCCISLDRYY AICCQPLVYR NKMTPLRIAL MLGGCWVIPM FISFLPIMQG WNNIGIVDLI EKRKFNQNSN STYCVFMVNK PYAITCSVVA FYIPFLLMVL AYYRIYVTAK EHARQIQVLQ RAGAPAEGRP QPADQHSTHR MRTETKAAKT LCIIMGCFCL CWAPFFVTNI VDPFIDYTVP GQLWTAFLWL GYINSGLNPF LYAFLNKSFR RAFLIILCCD DERYRRPSIL GQTVPCSTTT INGSTHVLRD TVECGGQWES QCHPAASSPL VAAQPIDT // ID 5HT4R_HUMAN Reviewed; 388 AA. AC Q13639; Q96KH9; Q96KI0; Q9H199; Q9NY73; Q9UBM6; Q9UBT4; Q9UE22; AC Q9UE23; Q9UQR6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 23-JAN-2007, entry version 66. DE 5-hydroxytryptamine 4 receptor (5-HT-4) (Serotonin receptor 4) (5- DE HT4). GN Name=HTR4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5-HT4(A); 5-HT4(B); 5-HT4(C) AND RP 5-HT4(D)). RC TISSUE=Gut; RX MEDLINE=98264328; PubMed=9603189; RA Blondel O., Gastineau M., Dahmoune Y., Langlois M., Fischmeister R.; RT "Cloning, expression, and pharmacology of four human 5- RT hydroxytryptamine 4 receptor isoforms produced by alternative splicing RT in the carboxyl terminus."; RL J. Neurochem. 70:2252-2261(1998). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORMS 5-HT4(A) AND 5HT4(B)). RC TISSUE=Brain; RA Van den Wyngaert I., Gommeren W., Jurzak M., Verhasselt P., Gordon R., RA Leysen J., Luyten W., Bender E.; RT "Cloning and expression of 5-HT4 receptor species and splice RT variants."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM 5-HT4(A)). RC TISSUE=Heart; RX MEDLINE=98012006; PubMed=9351641; RA Claeysen S., Faye P., Sebben M., Lemaire S., Bockaert J., Dumuis A.; RT "Cloning and expression of human 5-HT4S receptors. Effect of receptor RT density on their coupling to adenylyl cyclase."; RL NeuroReport 8:3189-3195(1997). RN [4] RP NUCLEOTIDE SEQUENCE (ISOFORM 5-HT4(E)). RC TISSUE=Brain; RX MEDLINE=99238795; PubMed=10220570; RA Claeysen S., Sebben M., Becamel C., Bockaert J., Dumuis A.; RT "Novel brain-specific 5-HT4 receptor splice variants show marked RT constitutive activity: role of the C-terminal intracellular domain."; RL Mol. Pharmacol. 55:910-920(1999). RN [5] RP NUCLEOTIDE SEQUENCE (ISOFORMS 5-HT4(A); 5-HT4(E) AND 5-HT4(G)). RC TISSUE=Hippocampus; RA Vilaro M.T., Domenech T., Palacios J.M., Mengod G.; RT "Cloning and characterization of multiple human 5-HT4 receptor RT variants including a novel variant that lacks the alternatively RT spliced C-terminal exon."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5-HT4(B)). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 NUCLEOTIDE SEQUENCE OF 10-388 (ISOFORM 5-HT4(F)). RX MEDLINE=20110418; PubMed=10646498; RA Bender E., Pindon A., van Oers I., Zhang Y.B., Gommeren W., RA Verhasselt P., Jurzak M., Leysen J., Luyten W.; RT "Structure of the human serotonin 5-HT4 receptor gene and cloning of a RT novel 5-HT4 splice variant."; RL J. Neurochem. 74:478-489(2000). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 112-255. RC TISSUE=Brain; RX MEDLINE=95385798; PubMed=7656980; DOI=10.1016/0014-5793(95)00828-W; RA Ullmer C., Schmuck K., Kalkman H.O., Luebbert H.; RT "Expression of serotonin receptor mRNAs in blood vessels."; RL FEBS Lett. 370:215-221(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Additional isoforms seem to exist; CC Name=5-HT4(B); CC IsoId=Q13639-1; Sequence=Displayed; CC Name=5-HT4(A); Synonyms=5-HT4S; CC IsoId=Q13639-2; Sequence=VSP_001849; CC Name=5-HT4(C); CC IsoId=Q13639-3; Sequence=VSP_001848; CC Name=5-HT4(D); CC IsoId=Q13639-4; Sequence=VSP_001847; CC Name=5-HT4(E); Synonyms=H5-HT4(g); CC IsoId=Q13639-5; Sequence=VSP_001846; CC Name=5-HT4(F); CC IsoId=Q13639-6; Sequence=VSP_001845; CC Name=5-HT4(G); CC IsoId=Q13639-7; Sequence=VSP_001850; CC -!- TISSUE SPECIFICITY: Isoform 5-HT4(A) is expressed in ileum, brain, CC and atrium, but not in the ventricle. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y12505; CAA73107.1; -; mRNA. DR EMBL; Y12506; CAA73108.1; -; mRNA. DR EMBL; Y12507; CAA73109.1; -; mRNA. DR EMBL; Y10437; CAA71462.1; -; mRNA. DR EMBL; Y08756; CAA70002.1; -; mRNA. DR EMBL; Y09586; CAA70774.1; -; mRNA. DR EMBL; Y13584; CAA73911.1; -; mRNA. DR EMBL; AJ011371; CAA09600.1; -; mRNA. DR EMBL; AJ243213; CAB71316.1; -; Genomic_DNA. DR EMBL; AJ278979; CAC22248.1; -; mRNA. DR EMBL; AJ278981; CAC22250.1; -; mRNA. DR EMBL; AJ278982; CAC22251.1; -; mRNA. DR EMBL; BC074755; AAH74755.1; -; mRNA. DR EMBL; Z48150; CAA88167.1; -; mRNA. DR PIR; S66493; S66493. DR UniGene; Hs.483773; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000164270; Homo sapiens. DR KEGG; hsa:3360; -. DR HGNC; HGNC:5299; HTR4. DR MIM; 602164; gene. DR DrugBank; APRD00454; Cisapride. DR DrugBank; APRD00096; Tegaserod. DR ArrayExpress; Q13639; -. DR GermOnline; ENSG00000164270; Homo sapiens. DR RZPD-ProtExp; RZPDo834H0945; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0005624; C:membrane fraction; IDA:MGI. DR GO; GO:0004993; F:serotonin receptor activity; IDA:MGI. DR GO; GO:0007187; P:G-protein signaling, coupled to cyclic nucl...; TAS:ProtInc. DR InterPro; IPR001520; 5HT4_rcpt. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01059; 5HT4RECEPTR. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 388 5-hydroxytryptamine 4 receptor. FT /FTId=PRO_0000068965. FT TOPO_DOM 1 19 Extracellular (Potential). FT TRANSMEM 20 40 1 (Potential). FT TOPO_DOM 41 58 Cytoplasmic (Potential). FT TRANSMEM 59 79 2 (Potential). FT TOPO_DOM 80 93 Extracellular (Potential). FT TRANSMEM 94 116 3 (Potential). FT TOPO_DOM 117 137 Cytoplasmic (Potential). FT TRANSMEM 138 158 4 (Potential). FT TOPO_DOM 159 192 Extracellular (Potential). FT TRANSMEM 193 213 5 (Potential). FT TOPO_DOM 214 260 Cytoplasmic (Potential). FT TRANSMEM 261 281 6 (Potential). FT TOPO_DOM 282 294 Extracellular (Potential). FT TRANSMEM 295 315 7 (Potential). FT TOPO_DOM 316 388 Cytoplasmic (Potential). FT LIPID 329 329 S-palmitoyl cysteine (By similarity). FT CARBOHYD 7 7 N-linked (GlcNAc...) (Potential). FT DISULFID 93 184 By similarity. FT VAR_SEQ 169 169 L -> LERSLNQGLGQDFHA (in isoform 5- FT HT4(F)). FT /FTId=VSP_001845. FT VAR_SEQ 359 388 RDAVECGGQWESQCHPPATSPLVAAQPSDT -> SSGTETD FT RRNFGIRKRRLTKPS (in isoform 5-HT4(D)). FT /FTId=VSP_001847. FT VAR_SEQ 359 388 RDAVECGGQWESQCHPPATSPLVAAQPSDT -> SGCSPVS FT SFLLLFCNRPVPV (in isoform 5-HT4(E)). FT /FTId=VSP_001846. FT VAR_SEQ 360 388 DAVECGGQWESQCHPPATSPLVAAQPSDT -> YTVLHRGH FT HQELEKLPIHNDPESLESCF (in isoform 5- FT HT4(A)). FT /FTId=VSP_001849. FT VAR_SEQ 360 388 DAVECGGQWESQCHPPATSPLVAAQPSDT -> F (in FT isoform 5-HT4(C)). FT /FTId=VSP_001848. FT VAR_SEQ 360 388 Missing (in isoform 5-HT4(G)). FT /FTId=VSP_001850. SQ SEQUENCE 388 AA; 43761 MW; 7FCFEC60E7BDF560 CRC64; MDKLDANVSS EEGFGSVEKV VLLTFLSTVI LMAILGNLLV MVAVCWDRQL RKIKTNYFIV SLAFADLLVS VLVMPFGAIE LVQDIWIYGE VFCLVRTSLD VLLTTASIFH LCCISLDRYY AICCQPLVYR NKMTPLRIAL MLGGCWVIPT FISFLPIMQG WNNIGIIDLI EKRKFNQNSN STYCVFMVNK PYAITCSVVA FYIPFLLMVL AYYRIYVTAK EHAHQIQMLQ RAGASSESRP QSADQHSTHR MRTETKAAKT LCIIMGCFCL CWAPFFVTNI VDPFIDYTVP GQVWTAFLWL GYINSGLNPF LYAFLNKSFR RAFLIILCCD DERYRRPSIL GQTVPCSTTT INGSTHVLRD AVECGGQWES QCHPPATSPL VAAQPSDT // ID 5HT4R_MOUSE Reviewed; 388 AA. AC P97288; O89003; O89004; Q9R2A4; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 20-FEB-2007, entry version 59. DE 5-hydroxytryptamine 4 receptor (5-HT-4) (Serotonin receptor 4) (5- DE HT4). GN Name=Htr4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Swiss; TISSUE=Brain; RX MEDLINE=97102706; PubMed=8946946; DOI=10.1016/S0014-5793(96)01132-5; RA Claeysen S., Sebben M., Journot L., Bockaert J., Dumuis A.; RT "Cloning, expression and pharmacology of the mouse 5-HT(4L) RT receptor."; RL FEBS Lett. 398:19-25(1996). RN [2] RP SEQUENCE REVISION TO C-TERMINUS. RA Dumuis A.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5-HT4(A) AND 5-HT4(E)). RC STRAIN=Swiss; TISSUE=Brain; RX MEDLINE=99127199; PubMed=9928238; RX DOI=10.1111/j.1749-6632.1998.tb10172.x; RA Claeysen S., Faye P., Sebben M., Taviaux S., Bockaert J., Dumuis A.; RT "5-HT4 receptors: cloning and expression of new splice variants."; RL Ann. N. Y. Acad. Sci. 861:49-56(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5-HT4(F)). RC TISSUE=Brain; RX MEDLINE=99238795; PubMed=10220570; RA Claeysen S., Sebben M., Becamel C., Bockaert J., Dumuis A.; RT "Novel brain-specific 5-HT4 receptor splice variants show marked RT constitutive activity: role of the C-terminal intracellular domain."; RL Mol. Pharmacol. 55:910-920(1999). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=P97288-1; Sequence=Displayed; CC Name=5-HT4(A); CC IsoId=P97288-2; Sequence=VSP_001851; CC Name=5-HT4(E); CC IsoId=P97288-3; Sequence=VSP_001852; CC Name=5-HT4(F); CC IsoId=P97288-4; Sequence=VSP_001853; CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y09585; CAA70773.1; -; mRNA. DR EMBL; Y09587; CAA70775.1; -; mRNA. DR EMBL; Y09588; CAA70776.1; -; mRNA. DR EMBL; AJ011369; CAA09598.1; -; mRNA. DR UniGene; Mm.20440; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSMUSG00000026322; Mus musculus. DR KEGG; mmu:15562; -. DR MGI; MGI:109246; Htr4. DR ArrayExpress; P97288; -. DR GermOnline; ENSMUSG00000026322; Mus musculus. DR InterPro; IPR001520; 5HT4_rcpt. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01059; 5HT4RECEPTR. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 388 5-hydroxytryptamine 4 receptor. FT /FTId=PRO_0000068966. FT TOPO_DOM 1 19 Extracellular (Potential). FT TRANSMEM 20 40 1 (Potential). FT TOPO_DOM 41 58 Cytoplasmic (Potential). FT TRANSMEM 59 79 2 (Potential). FT TOPO_DOM 80 93 Extracellular (Potential). FT TRANSMEM 94 116 3 (Potential). FT TOPO_DOM 117 137 Cytoplasmic (Potential). FT TRANSMEM 138 158 4 (Potential). FT TOPO_DOM 159 192 Extracellular (Potential). FT TRANSMEM 193 213 5 (Potential). FT TOPO_DOM 214 260 Cytoplasmic (Potential). FT TRANSMEM 261 281 6 (Potential). FT TOPO_DOM 282 294 Extracellular (Potential). FT TRANSMEM 295 315 7 (Potential). FT TOPO_DOM 316 388 Cytoplasmic (Potential). FT LIPID 329 329 S-palmitoyl cysteine (By similarity). FT CARBOHYD 7 7 N-linked (GlcNAc...) (Potential). FT DISULFID 93 184 By similarity. FT VAR_SEQ 359 388 RDAVECGGQWESRCHLTATSPLVAAQPSDT -> SFPLLFR FT NRPVPV (in isoform 5-HT4(E)). FT /FTId=VSP_001852. FT VAR_SEQ 360 388 DAVECGGQWESRCHLTATSPLVAAQPSDT -> YTVLHSGH FT HQELEKLPIHNDPESLESCF (in isoform 5- FT HT4(A)). FT /FTId=VSP_001851. FT VAR_SEQ 360 388 DAVECGGQWESRCHLTATSPLVAAQPSDT -> PVPV (in FT isoform 5-HT4(F)). FT /FTId=VSP_001853. SQ SEQUENCE 388 AA; 43932 MW; F84163F39BA115B0 CRC64; MDKLDANVSS NEGFRSVEKV VLLTFLAVVI LMAILGNLLV MVAVCRDRQL RKIKTNYFIV SLAFADLLVS VLVMPFGAIE LVQDIWAYGE MFCLVRTSLD VLLTTASIFH LCCISLDRYY AICCQPLVYR NKMTPLRIAL MLGGCWVLPM FISFLPIMQG WNNIGIVDVI EKRKFSHNSN STWCVFMVNK PYAITCSVVA FYIPFLLMVL AYYRIYVTAK EHAQQIQMLQ RAGATSESRP QPADQHSTHR MRTETKAAKT LCVIMGCFCF CWAPFFVTNI VDPFIDYTVP EQVWTAFLWL GYINSGLNPF LYAFLNKSFR RAFLIILCCD DERYKRPPIL GQTVPCSTTT INGSTHVLRD AVECGGQWES RCHLTATSPL VAAQPSDT // ID 5HT4R_PIG Reviewed; 137 AA. AC Q29006; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 40. DE 5-hydroxytryptamine 4 receptor (5-HT-4) (Serotonin receptor 4) (5-HT4) DE (Fragment). GN Name=HTR4; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=95385798; PubMed=7656980; DOI=10.1016/0014-5793(95)00828-W; RA Ullmer C., Schmuck K., Kalkman H.O., Luebbert H.; RT "Expression of serotonin receptor mRNAs in blood vessels."; RL FEBS Lett. 370:215-221(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z48175; CAA88198.1; -; mRNA. DR PIR; S66487; S66487. DR InterPro; IPR001520; 5HT4_rcpt. DR InterPro; IPR002110; ANK. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01059; 5HT4RECEPTR. DR PRINTS; PR01415; ANKYRIN. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; PARTIAL. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN <1 >137 5-hydroxytryptamine 4 receptor. FT /FTId=PRO_0000068967. FT TOPO_DOM <1 15 Cytoplasmic (Potential). FT TRANSMEM 16 36 4 (Potential). FT TOPO_DOM 37 70 Extracellular (Potential). FT TRANSMEM 71 91 5 (Potential). FT TOPO_DOM 92 >137 Cytoplasmic (Potential). FT CARBOHYD 58 58 N-linked (GlcNAc...) (Potential). FT NON_TER 1 1 FT NON_TER 137 137 SQ SEQUENCE 137 AA; 15622 MW; C9D60744DA4D0263 CRC64; CCQPLVYRNK MTPLRVAVLL AGCWAIPVLI SFLPIMQGWN NIGITDLIEK RKFHQNSNST YCIFMVNKPY AITCSVVAFY IPFLLMVLAY WRIYVTAKEH AHQIQMLQRA GAPAEGRPPS ADQHSTHRMR TETKAAK // ID 5HT4R_RAT Reviewed; 406 AA. AC Q62758; O89034; Q62757; Q63006; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 59. DE 5-hydroxytryptamine 4 receptor (5-HT-4) (Serotonin receptor 4) (5- DE HT4). GN Name=Htr4; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=95317299; PubMed=7796807; RA Gerald C., Adham N., Kao H.T., Olsen M.A., Laz T.M., Schechter L.E., RA Bard J.A., Vaysse P., Hartig P.R., Branchek T.A., Weinshank R.L.; RT "The 5-HT4 receptor: molecular cloning and pharmacological RT characterization of two splice variants."; RL EMBO J. 14:2806-2815(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-259. RC TISSUE=Brain; RX MEDLINE=95385798; PubMed=7656980; DOI=10.1016/0014-5793(95)00828-W; RA Ullmer C., Schmuck K., Kalkman H.O., Luebbert H.; RT "Expression of serotonin receptor mRNAs in blood vessels."; RL FEBS Lett. 370:215-221(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5-HT4(E)). RC TISSUE=Brain; RX MEDLINE=99238795; PubMed=10220570; RA Claeysen S., Sebben M., Becamel C., Bockaert J., Dumuis A.; RT "Novel brain-specific 5-HT4 receptor splice variants show marked RT constitutive activity: role of the C-terminal intracellular domain."; RL Mol. Pharmacol. 55:910-920(1999). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=5-HT4L; CC IsoId=Q62758-1; Sequence=Displayed; CC Name=5-HT4S; CC IsoId=Q62758-2; Sequence=VSP_001854; CC Name=5-HT4(E); CC IsoId=Q62758-3; Sequence=VSP_001855; CC -!- TISSUE SPECIFICITY: In brain, isoform 5-HT4S is restricted to the CC striatum, but isoform 5-HT4L is expressed throughout the brain, CC except in the cerebellum. In peripheral tissues, differential CC expression is also observed in the atrium of the heart where only CC isoform 5-HT4S is detectable. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U20907; AAC52233.1; -; mRNA. DR EMBL; U20906; AAC52232.1; -; mRNA. DR EMBL; Z48153; CAA88170.1; -; mRNA. DR EMBL; AJ011370; CAA09599.1; -; mRNA. DR PIR; S55549; S55549. DR PIR; S55550; S55550. DR UniGene; Rn.10094; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSRNOG00000019134; Rattus norvegicus. DR KEGG; rno:25324; -. DR RGD; 2850; Htr4. DR ArrayExpress; Q62758; -. DR GermOnline; ENSRNOG00000019134; Rattus norvegicus. DR InterPro; IPR001520; 5HT4_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01059; 5HT4RECEPTR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 406 5-hydroxytryptamine 4 receptor. FT /FTId=PRO_0000068968. FT TOPO_DOM 1 19 Extracellular (Potential). FT TRANSMEM 20 40 1 (Potential). FT TOPO_DOM 41 58 Cytoplasmic (Potential). FT TRANSMEM 59 79 2 (Potential). FT TOPO_DOM 80 93 Extracellular (Potential). FT TRANSMEM 94 116 3 (Potential). FT TOPO_DOM 117 137 Cytoplasmic (Potential). FT TRANSMEM 138 158 4 (Potential). FT TOPO_DOM 159 192 Extracellular (Potential). FT TRANSMEM 193 213 5 (Potential). FT TOPO_DOM 214 260 Cytoplasmic (Potential). FT TRANSMEM 261 281 6 (Potential). FT TOPO_DOM 282 294 Extracellular (Potential). FT TRANSMEM 295 315 7 (Potential). FT TOPO_DOM 316 406 Cytoplasmic (Potential). FT LIPID 329 329 S-palmitoyl cysteine (By similarity). FT CARBOHYD 7 7 N-linked (GlcNAc...) (Potential). FT DISULFID 93 184 By similarity. FT VAR_SEQ 359 406 RDTVECGGQWESRCHLTATSPLVAAQPVIRRPQDNDLEDSC FT SLKRSQS -> SFPLLFCNRPVPV (in isoform 5- FT HT4(E)). FT /FTId=VSP_001855. FT VAR_SEQ 360 406 DTVECGGQWESRCHLTATSPLVAAQPVIRRPQDNDLEDSCS FT LKRSQS -> YTVLHSGQHQELEKLPIHNDPESLESCF FT (in isoform 5-HT4S). FT /FTId=VSP_001854. FT CONFLICT 74 75 NA -> MP (in Ref. 3). SQ SEQUENCE 406 AA; 46107 MW; A1889155A08930B4 CRC64; MDRLDANVSS NEGFGSVEKV VLLTFFAMVI LMAILGNLLV MVAVCRDRQL RKIKTNYFIV SLAFADLLVS VLVNAFGAIE LVQDIWFYGE MFCLVRTSLD VLLTTASIFH LCCISLDRYY AICCQPLVYR NKMTPLRIAL MLGGCWVIPM FISFLPIMQG WNNIGIVDVI EKRKFNHNSN STFCVFMVNK PYAITCSVVA FYIPFLLMVL AYYRIYVTAK EHAQQIQMLQ RAGATSESRP QTADQHSTHR MRTETKAAKT LCVIMGCFCF CWAPFFVTNI VDPFIDYTVP EKVWTAFLWL GYINSGLNPF LYAFLNKSFR RAFLIILCCD DERYKRPPIL GQTVPCSTTT INGSTHVLRD TVECGGQWES RCHLTATSPL VAAQPVIRRP QDNDLEDSCS LKRSQS // ID 5HT5A_HUMAN Reviewed; 357 AA. AC P47898; Q2M2D2; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 20-FEB-2007, entry version 56. DE 5-hydroxytryptamine 5A receptor (5-HT-5A) (Serotonin receptor 5A) (5- DE HT-5). GN Name=HTR5A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95080386; PubMed=7988681; DOI=10.1016/0014-5793(94)01209-1; RA Rees S., den Daas I., Foord S., Goodson S., Bull D., Kilpatrick G., RA Lee M.; RT "Cloning and characterisation of the human 5-HT5A serotonin RT receptor."; RL FEBS Lett. 355:242-246(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) 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 -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X81411; CAA57168.1; -; Genomic_DNA. DR EMBL; X81412; CAA57168.1; JOINED; Genomic_DNA. DR EMBL; AF498985; AAM21132.1; -; mRNA. DR EMBL; BC112021; AAI12022.1; -; mRNA. DR PIR; I37107; I37107. DR UniGene; Hs.65791; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000157219; Homo sapiens. DR KEGG; hsa:3361; -. DR H-InvDB; HIX0007245; -. DR HGNC; HGNC:5300; HTR5A. DR MIM; 601305; gene. DR LinkHub; P47898; -. DR ArrayExpress; P47898; -. DR GermOnline; ENSG00000157219; Homo sapiens. DR RZPD-ProtExp; IOH42519; -. DR RZPD-ProtExp; RZPDo834C0245; -. DR RZPD-ProtExp; T1367; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004993; F:serotonin receptor activity; TAS:ProtInc. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS:ProtInc. DR InterPro; IPR001397; 5HT5A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00518; 5HT5ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 357 5-hydroxytryptamine 5A receptor. FT /FTId=PRO_0000068969. FT TOPO_DOM 1 40 Extracellular (Potential). FT TRANSMEM 41 63 1 (Potential). FT TOPO_DOM 64 78 Cytoplasmic (Potential). FT TRANSMEM 79 99 2 (Potential). FT TOPO_DOM 100 115 Extracellular (Potential). FT TRANSMEM 116 137 3 (Potential). FT TOPO_DOM 138 158 Cytoplasmic (Potential). FT TRANSMEM 159 181 4 (Potential). FT TOPO_DOM 182 198 Extracellular (Potential). FT TRANSMEM 199 219 5 (Potential). FT TOPO_DOM 220 282 Cytoplasmic (Potential). FT TRANSMEM 283 303 6 (Potential). FT TOPO_DOM 304 320 Extracellular (Potential). FT TRANSMEM 321 341 7 (Potential). FT TOPO_DOM 342 357 Cytoplasmic (Potential). FT CARBOHYD 6 6 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 120 192 By similarity. SQ SEQUENCE 357 AA; 40255 MW; 92F8A78C69169790 CRC64; MDLPVNLTSF SLSTPSPLET NHSLGKDDLR PSSPLLSVFG VLILTLLGFL VAATFAWNLL VLATILRVRT FHRVPHNLVA SMAVSDVLVA ALVMPLSLVH ELSGRRWQLG RRLCQLWIAC DVLCCTASIW NVTAIALDRY WSITRHMEYT LRTRKCVSNV MIALTWALSA VISLAPLLFG WGETYSEGSE ECQVSREPSY AVFSTVGAFY LPLCVVLFVY WKIYKAAKFR VGSRKTNSVS PISEAVEVKD SAKQPQMVFT VRHATVTFQP EGDTWREQKE QRAALMVGIL IGVFVLCWIP FFLTELISPL CSCDIPAIWK SIFLWLGYSN SFFNPLIYTA FNKNYNSAFK NFFSRQH // ID 5HT5A_MOUSE Reviewed; 357 AA. AC P30966; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 20-FEB-2007, entry version 54. DE 5-hydroxytryptamine 5A receptor (5-HT-5A) (Serotonin receptor 5A) (5- DE HT-5). GN Name=Htr5a; Synonyms=5ht5a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Brain; RX MEDLINE=93099851; PubMed=1464308; RA Plassat J.-L., Boschert U., Amlaiky N., Hen R.; RT "The mouse 5HT5 receptor reveals a remarkable heterogeneity within the RT 5HT1D receptor family."; RL EMBO J. 11:4779-4786(1992). RN [2] RP CHARACTERIZATION. RC TISSUE=Brain; RX MEDLINE=93196607; PubMed=8450829; RA Matthes H., Boschert U., Amlaiky N., Grailhe R., Plassat J.-L., RA Muscatelli F., Mattei M.-G., Hen R.; RT "Mouse 5-hydroxytryptamine5A and 5-hydroxytryptamine5B receptors RT define a new family of serotonin receptors: cloning, functional RT expression, and chromosomal localization."; RL Mol. Pharmacol. 43:313-319(1993). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed predominantly in the central nervous CC system; in the cerebral cortex, hippocampus, habenula, olfactory CC bulb and granular layer of the cerebellum. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z18278; CAA79155.1; -; Genomic_DNA. DR UniGene; Mm.4835; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSMUSG00000039106; Mus musculus. DR KEGG; mmu:15563; -. DR MGI; MGI:96283; Htr5a. DR ArrayExpress; P30966; -. DR GermOnline; ENSMUSG00000039106; Mus musculus. DR InterPro; IPR001397; 5HT5A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00518; 5HT5ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 357 5-hydroxytryptamine 5A receptor. FT /FTId=PRO_0000068970. FT TOPO_DOM 1 40 Extracellular (Potential). FT TRANSMEM 41 63 1 (Potential). FT TOPO_DOM 64 78 Cytoplasmic (Potential). FT TRANSMEM 79 99 2 (Potential). FT TOPO_DOM 100 115 Extracellular (Potential). FT TRANSMEM 116 137 3 (Potential). FT TOPO_DOM 138 158 Cytoplasmic (Potential). FT TRANSMEM 159 181 4 (Potential). FT TOPO_DOM 182 198 Extracellular (Potential). FT TRANSMEM 199 219 5 (Potential). FT TOPO_DOM 220 282 Cytoplasmic (Potential). FT TRANSMEM 283 303 6 (Potential). FT TOPO_DOM 304 320 Extracellular (Potential). FT TRANSMEM 321 341 7 (Potential). FT TOPO_DOM 342 357 Cytoplasmic (Potential). FT CARBOHYD 6 6 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 120 192 By similarity. SQ SEQUENCE 357 AA; 40805 MW; 5F5D856AC477BFAC CRC64; MDLPVNLTSF SLSTPSSLEP NRSLDTEVLR PSRPFLSAFR VLVLTLLGFL AAATFTWNLL VLATILKVRT FHRVPHNLVA SMAISDVLVA VLVMPLSLVH ELSGRRWQLG RRLCQLWIAC DVLCCTASIW NVTAIALDRY WSITRHLEYT LRTRKRVSNV MILLTWALST VISLAPLLFG WGETYSEPSE ECQVSREPSY TVFSTVGAFY LPLWLVLFVY WKIYRAAKFR MGSRKTNSVS PVPEAVEVKN ATQHPQMVFT ARHATVTFQT EGDTWREQKE QRAALMVGIL IGVFVLCWFP FFVTELISPL CSWDVPAIWK SIFLWLGYSN SFFNPLIYTA FNRSYSSAFK VFFSKQQ // ID 5HT5A_RAT Reviewed; 357 AA. AC P35364; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 20-FEB-2007, entry version 50. DE 5-hydroxytryptamine 5A receptor (5-HT-5A) (Serotonin receptor 5A) DE (REC17). GN Name=Htr5a; Synonyms=5ht5a; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX MEDLINE=93234515; PubMed=7682702; RA Erlander M.G., Lovenberg T.W., Baron B.M., de Lecea L., RA Danielson P.E., Racke M., Slone A.L., Siegel B.W., Foye P.E., RA Cannon K., Burns J.E., Sutcliffe G.J.; RT "Two members of a distinct subfamily of 5-hydroxytryptamine receptors RT differentially expressed in rat brain."; RL Proc. Natl. Acad. Sci. U.S.A. 90:3452-3456(1993). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Central nervous system. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L10072; AAA40615.1; -; mRNA. DR PIR; B47472; B47472. DR UniGene; Rn.10569; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSRNOG00000007066; Rattus norvegicus. DR KEGG; rno:25689; -. DR RGD; 2851; Htr5a. DR ArrayExpress; P35364; -. DR GermOnline; ENSRNOG00000007066; Rattus norvegicus. DR InterPro; IPR001397; 5HT5A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00518; 5HT5ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 357 5-hydroxytryptamine 5A receptor. FT /FTId=PRO_0000068971. FT TOPO_DOM 1 40 Extracellular (Potential). FT TRANSMEM 41 63 1 (Potential). FT TOPO_DOM 64 78 Cytoplasmic (Potential). FT TRANSMEM 79 99 2 (Potential). FT TOPO_DOM 100 115 Extracellular (Potential). FT TRANSMEM 116 137 3 (Potential). FT TOPO_DOM 138 158 Cytoplasmic (Potential). FT TRANSMEM 159 181 4 (Potential). FT TOPO_DOM 182 198 Extracellular (Potential). FT TRANSMEM 199 219 5 (Potential). FT TOPO_DOM 220 282 Cytoplasmic (Potential). FT TRANSMEM 283 303 6 (Potential). FT TOPO_DOM 304 320 Extracellular (Potential). FT TRANSMEM 321 341 7 (Potential). FT TOPO_DOM 342 357 Cytoplasmic (Potential). FT CARBOHYD 6 6 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 120 192 By similarity. SQ SEQUENCE 357 AA; 40673 MW; 8C498A50C88408B5 CRC64; MDLPINLTSF SLSTPSTLEP NRSLDTEALR TSQSFLSAFR VLVLTLLGFL AAATFTWNLL VLATILRVRT FHRVPHNLVA SMAISDVLVA VLVMPLSLVH ELSGRRWQLG RRLCQLWIAC DVLCCTASIW NVTAIALDRY WSITRHLEYT LRARKRVSNV MILLTWALSA VISLAPLLFG WGETYSELSE ECQVSREPSY TVFSTVGAFY LPLCVVLFVY WKIYKAAKFR MGSRKTNSVS PIPEAVEVKD ASQHPQMVFT VRHATVTFQT EGDTWREQKE QRAALMVGIL IGVFVLCWFP FFVTELISPL CSWDIPALWK SIFLWLGYSN SFFNPLIYTA FNRSYSSAFK VFFSKQQ // ID 5HT5B_MOUSE Reviewed; 370 AA. AC P31387; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 23-JAN-2007, entry version 53. DE 5-hydroxytryptamine 5B receptor (5-HT-5B) (Serotonin receptor 5B). GN Name=Htr5b; Synonyms=5ht5b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=93196607; PubMed=8450829; RA Matthes H., Boschert U., Amlaiky N., Grailhe R., Plassat J.-L., RA Muscatelli F., Mattei M.-G., Hen R.; RT "Mouse 5-hydroxytryptamine5A and 5-hydroxytryptamine5B receptors RT define a new family of serotonin receptors: cloning, functional RT expression, and chromosomal localization."; RL Mol. Pharmacol. 43:313-319(1993). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins. Probably involved in CC anxiety and depression. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed predominantly in the central nervous CC system; in the hippocampus, habenula, and the doral raphe. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X69867; CAA49501.1; -; mRNA. DR PIR; I48231; I48231. DR UniGene; Mm.4833; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSMUSG00000050534; Mus musculus. DR KEGG; mmu:15564; -. DR MGI; MGI:96284; Htr5b. DR LinkHub; P31387; -. DR ArrayExpress; P31387; -. DR GermOnline; ENSMUSG00000050534; Mus musculus. DR InterPro; IPR000431; 5HT5B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00519; 5HT5BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 370 5-hydroxytryptamine 5B receptor. FT /FTId=PRO_0000068972. FT TOPO_DOM 1 52 Extracellular (Potential). FT TRANSMEM 53 75 1 (Potential). FT TOPO_DOM 76 90 Cytoplasmic (Potential). FT TRANSMEM 91 111 2 (Potential). FT TOPO_DOM 112 128 Extracellular (Potential). FT TRANSMEM 129 150 3 (Potential). FT TOPO_DOM 151 171 Cytoplasmic (Potential). FT TRANSMEM 172 194 4 (Potential). FT TOPO_DOM 195 211 Extracellular (Potential). FT TRANSMEM 212 232 5 (Potential). FT TOPO_DOM 233 295 Cytoplasmic (Potential). FT TRANSMEM 296 316 6 (Potential). FT TOPO_DOM 317 333 Extracellular (Potential). FT TRANSMEM 334 354 7 (Potential). FT TOPO_DOM 355 370 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT DISULFID 127 205 By similarity. SQ SEQUENCE 370 AA; 41201 MW; 0553C62B12DAAD84 CRC64; MEVSNLSGAT PGLAFPPGPE SCSDSPSSGR SMGSTPGGLI LPGREPPFSA FTVLVVTLLV LLIAATFLWN LLVLVTILRV RAFHRVPHNL VASTAVSDVL VAVLVMPLSL VSELSAGRRW QLGRSLCHVW ISFDVLCCTA SIWNVAAIAL DRYWTITRHL QYTLRTRSRA SALMIAITWA LSALIALAPL LFGWGEAYDA RLQRCQVSQE PSYAVFSTCG AFYLPLAVVL FVYWKIYKAA KFRFGRRRRA VVPLPATTQA KEAPPESEMV FTARRRATVT FQTSGDSWRE QKEKRAAMMV GILIGVFVLC WIPFFLTELI SPLCACSLPP IWKSIFLWLG YSNSFFNPLI YTAFNKNYNN AFKSLFTKQR // ID 5HT5B_RAT Reviewed; 370 AA. AC P35365; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 23-JAN-2007, entry version 48. DE 5-hydroxytryptamine 5B receptor (5-HT-5B) (Serotonin receptor 5B) DE (MR22). GN Name=Htr5b; Synonyms=5ht5b; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX MEDLINE=93234515; PubMed=7682702; RA Erlander M.G., Lovenberg T.W., Baron B.M., de Lecea L., RA Danielson P.E., Racke M., Slone A.L., Siegel B.W., Foye P.E., RA Cannon K., Burns J.E., Sutcliffe G.J.; RT "Two members of a distinct subfamily of 5-hydroxytryptamine receptors RT differentially expressed in rat brain."; RL Proc. Natl. Acad. Sci. U.S.A. 90:3452-3456(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94039744; PubMed=8224165; DOI=10.1016/0014-5793(93)80368-5; RA Wisden W., Parker E.M., Mahle C.D., Grisel D.A., Nowak H.P., RA Yocca F.D., Felder C.C., Seeburg P.H., Voigt M.M.; RT "Cloning and characterization of the rat 5-HT5B receptor. Evidence RT that the 5-HT5B receptor couples to a G protein in mammalian cell RT membranes."; RL FEBS Lett. 333:25-31(1993). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins. Probably involved in CC anxiety and depression. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Brain; in the CA1 region of hippocampus, the CC medial habenula, and raphe nuclei. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L10073; AAA40616.1; -; mRNA. DR PIR; S38744; S38744. DR HSSP; P08913; 1HOD. DR Ensembl; ENSRNOG00000002549; Rattus norvegicus. DR RGD; 62388; Htr5b. DR ArrayExpress; P35365; -. DR GermOnline; ENSRNOG00000002549; Rattus norvegicus. DR InterPro; IPR000431; 5HT5B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00519; 5HT5BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 370 5-hydroxytryptamine 5B receptor. FT /FTId=PRO_0000068973. FT TOPO_DOM 1 52 Extracellular (Potential). FT TRANSMEM 53 75 1 (Potential). FT TOPO_DOM 76 90 Cytoplasmic (Potential). FT TRANSMEM 91 111 2 (Potential). FT TOPO_DOM 112 128 Extracellular (Potential). FT TRANSMEM 129 150 3 (Potential). FT TOPO_DOM 151 171 Cytoplasmic (Potential). FT TRANSMEM 172 194 4 (Potential). FT TOPO_DOM 195 211 Extracellular (Potential). FT TRANSMEM 212 232 5 (Potential). FT TOPO_DOM 233 295 Cytoplasmic (Potential). FT TRANSMEM 296 316 6 (Potential). FT TOPO_DOM 317 333 Extracellular (Potential). FT TRANSMEM 334 354 7 (Potential). FT TOPO_DOM 355 370 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT DISULFID 127 205 By similarity. SQ SEQUENCE 370 AA; 41122 MW; 8EC5F789BFD647E5 CRC64; MEVSNLSGAT PGIAFPPGPE SCSDSPSSGR SMGSTPGGLI LSGREPPFSA FTVLVVTLLV LLIAATFLWN LLVLVTILRV RAFHRVPHNL VASTAVSDVL VAALVMPLSL VSELSAGRRW QLGRSLCHVW ISFDVLCCTA SIWNVAAIAL DRYWTITRHL QYTLRTRRRA SALMIAITWA LSALIALAPL LFGWGEAYDA RLQRCQVSQE PSYAVFSTCG AFYVPLAVVL FVYWKIYKAA KFRFGRRRRA VVPLPATTQA KEAPQESETV FTARCRATVA FQTSGDSWRE QKEKRAAMMV GILIGVFVLC WIPFFLTELV SPLCACSLPP IWKSIFLWLG YSNSFFNPLI YTAFNKNYNN AFKSLFTKQR // ID 5HT6R_HUMAN Reviewed; 440 AA. AC P50406; Q13640; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 54. DE 5-hydroxytryptamine 6 receptor (5-HT-6) (Serotonin receptor 6). GN Name=HTR6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Corpus striatum; RX MEDLINE=96102917; PubMed=8522988; RA Kohen R., Metcalf M.A., Khan N., Druck T., Huebner K., Lachowicz J.E., RA Sibley D.R., Roth B., Hamblin M.W.; RT "Cloning, characterization, and chromosomal localization of a human 5- RT HT6 serotonin receptor."; RL J. Neurochem. 66:47-56(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Kopatz S.A., Aronstam R.S., Sharma S.V.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal 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 215-280. RC TISSUE=Corpus striatum; RX MEDLINE=95385798; PubMed=7656980; DOI=10.1016/0014-5793(95)00828-W; RA Ullmer C., Schmuck K., Kalkman H.O., Luebbert H.; RT "Expression of serotonin receptor mRNAs in blood vessels."; RL FEBS Lett. 370:215-221(1995). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-125, AND MASS RP SPECTROMETRY. RX PubMed=16094384; DOI=10.1038/nmeth776; RA Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., RA Bodenmiller B., Watts J.D., Hood L., Aebersold R.; RT "Quantitative phosphoproteome analysis using a dendrimer conjugation RT chemistry and tandem mass spectrometry."; RL Nat. Methods 2:591-598(2005). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. It has a high affinity for tricyclic psychotropic drugs. CC -!- INTERACTION: CC P06241:FYN; NbExp=7; IntAct=EBI-1182222, EBI-515315; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in several human brain regions, most CC prominently in the caudate nucleus. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L41147; AAA92622.1; -; mRNA. DR EMBL; AY429105; AAR07900.1; -; mRNA. DR EMBL; BC074995; AAH74995.1; -; mRNA. DR EMBL; BC074996; AAH74996.1; -; mRNA. DR EMBL; Z49119; CAA88929.1; -; mRNA. DR PIR; JC5520; JC5520. DR UniGene; Hs.22180; -. DR HSSP; P08913; 1HLL. DR IntAct; P50406; -. DR Ensembl; ENSG00000158748; Homo sapiens. DR KEGG; hsa:3362; -. DR HGNC; HGNC:5301; HTR6. DR MIM; 601109; gene. DR ArrayExpress; P50406; -. DR GermOnline; ENSG00000158748; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004969; F:histamine receptor activity; TAS:ProtInc. DR GO; GO:0007187; P:G-protein signaling, coupled to cyclic nucl...; TAS:ProtInc. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Membrane; Phosphorylation; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 440 5-hydroxytryptamine 6 receptor. FT /FTId=PRO_0000068974. FT TOPO_DOM 1 34 Extracellular (Potential). FT TRANSMEM 35 57 1 (Potential). FT TOPO_DOM 58 64 Cytoplasmic (Potential). FT TRANSMEM 65 85 2 (Potential). FT TOPO_DOM 86 100 Extracellular (Potential). FT TRANSMEM 101 122 3 (Potential). FT TOPO_DOM 123 144 Cytoplasmic (Potential). FT TRANSMEM 145 166 4 (Potential). FT TOPO_DOM 167 184 Extracellular (Potential). FT TRANSMEM 185 208 5 (Potential). FT TOPO_DOM 209 265 Cytoplasmic (Potential). FT TRANSMEM 266 290 6 (Potential). FT TOPO_DOM 291 295 Extracellular (Potential). FT TRANSMEM 296 320 7 (Potential). FT TOPO_DOM 321 440 Cytoplasmic (Potential). FT MOD_RES 125 125 Phosphotyrosine. FT DISULFID 99 180 By similarity. FT CONFLICT 247 247 V -> M (in Ref. 4). SQ SEQUENCE 440 AA; 46954 MW; C888F47650C1D2EF CRC64; MVPEPGPTAN STPAWGAGPP SAPGGSGWVA AALCVVIALT AAANSLLIAL ICTQPALRNT SNFFLVSLFT SDLMVGLVVM PPAMLNALYG RWVLARGLCL LWTAFDVMCC SASILNLCLI SLDRYLLILS PLRYKLRMTP LRALALVLGA WSLAALASFL PLLLGWHELG HARPPVPGQC RLLASLPFVL VASGLTFFLP SGAICFTYCR ILLAARKQAV QVASLTTGMA SQASETLQVP RTPRPGVESA DSRRLATKHS RKALKASLTL GILLGMFFVT WLPFFVANIV QAVCDCISPG LFDVLTWLGY CNSTMNPIIY PLFMRDFKRA LGRFLPCPRC PRERQASLAS PSLRTSHSGP RPGLSLQQVL PLPLPPDSDS DSDAGSGGSS GLRLTAQLLL PGEATQDPPL PTRAAAAVNF FNIDPAEPEL RPHPLGIPTN // ID 5HT6R_MOUSE Reviewed; 440 AA. AC Q9R1C8; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 20-FEB-2007, entry version 47. DE 5-hydroxytryptamine 6 receptor (5-HT-6) (Serotonin receptor 6). GN Name=Htr6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/SvJ; TISSUE=Brain; RX MEDLINE=21299097; PubMed=11406289; DOI=10.1016/S0169-328X(01)00090-0; RA Kohen R., Fashingbauer L.A., Heidmann D.E.A., Guthrie C.R., RA Hamblin M.W.; RT "Cloning of the mouse 5-HT6 serotonin receptor and mutagenesis studies RT of the third cytoplasmic loop."; RL Brain Res. Mol. Brain Res. 90:110-117(2001). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that function as CC a neurotransmitter, a hormone, and a mitogen. The activity of this CC receptor is mediated by G proteins that stimulate adenylate CC cyclase. It has a high affinity for tricyclic psychotropic drugs CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF134158; AAD46490.1; -; mRNA. DR UniGene; Mm.425211; -. DR Ensembl; ENSMUSG00000028747; Mus musculus. DR KEGG; mmu:15565; -. DR MGI; MGI:1196627; Htr6. DR ArrayExpress; Q9R1C8; -. DR GermOnline; ENSMUSG00000028747; Mus musculus. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphorylation; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 440 5-hydroxytryptamine 6 receptor. FT /FTId=PRO_0000068975. FT TOPO_DOM 1 34 Extracellular (Potential). FT TRANSMEM 35 57 1 (Potential). FT TOPO_DOM 58 64 Cytoplasmic (Potential). FT TRANSMEM 65 85 2 (Potential). FT TOPO_DOM 86 100 Extracellular (Potential). FT TRANSMEM 101 122 3 (Potential). FT TOPO_DOM 123 144 Cytoplasmic (Potential). FT TRANSMEM 145 166 4 (Potential). FT TOPO_DOM 167 184 Extracellular (Potential). FT TRANSMEM 185 208 5 (Potential). FT TOPO_DOM 209 267 Cytoplasmic (Potential). FT TRANSMEM 268 292 6 (Potential). FT TOPO_DOM 293 297 Extracellular (Potential). FT TRANSMEM 298 322 7 (Potential). FT TOPO_DOM 323 440 Cytoplasmic (Potential). FT MOD_RES 125 125 Phosphotyrosine (By similarity). FT CARBOHYD 9 9 N-linked (GlcNAc...) (Potential). FT DISULFID 99 180 By similarity. SQ SEQUENCE 440 AA; 46998 MW; 4440CDEBE01FEF0C CRC64; MVPEPGPVNS STPAWGPGPP PAPGGSGWVA AALCVVIVLT AAANSLLIAL ICTQPALRNT SNFFLVSLFT SDLMVGLVVM PPAMLNALYG RWVLARGLCL LWTAFDVMCC SASILNLCLI SLDRYLLILS PLRYKLRMTA PRALALILGA WSLAALASFL PLLLGWHELG KARTSAPGQC RLLASLPYVL VASGVTFFLP SGAICFTYCR ILLAARKQAV QVASLTTGTA TAGQALETLQ VPRTPRPGME SADSRRLTTK HSRKALKASL TLGILLSMFF VTWLPFFVAS IAQAVCDCIS PGLFDVLTWL GYCNSTMNPI IYPLFMRDFK RALGRFVPCV HCPPEHRASP ASPSMWTSHS GARPGLSLQQ VLPLPLPPNS DSDSASGGTS GLQLTAQLLL PGEATRDPPP PTRAPTVVNF FVTDSVEPEI RQHPLGSPMN // ID 5HT6R_PANTR Reviewed; 440 AA. AC Q5IS65; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 28-NOV-2006, entry version 13. DE 5-hydroxytryptamine 6 receptor (5-HT-6) (Serotonin receptor 6). GN Name=HTR6; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040; RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L., RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.; RT "Accelerated evolution of nervous system genes in the origin of Homo RT sapiens."; RL Cell 119:1027-1040(2004). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. It has a high affinity for tricyclic psychotropic drugs CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein (By CC similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY665263; AAV74301.1; -; mRNA. DR KEGG; ptr:469199; -. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Membrane; Phosphorylation; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 440 5-hydroxytryptamine 6 receptor. FT /FTId=PRO_0000068976. FT TOPO_DOM 1 34 Extracellular (Potential). FT TRANSMEM 35 57 1 (Potential). FT TOPO_DOM 58 64 Cytoplasmic (Potential). FT TRANSMEM 65 85 2 (Potential). FT TOPO_DOM 86 100 Extracellular (Potential). FT TRANSMEM 101 122 3 (Potential). FT TOPO_DOM 123 144 Cytoplasmic (Potential). FT TRANSMEM 145 166 4 (Potential). FT TOPO_DOM 167 184 Extracellular (Potential). FT TRANSMEM 185 208 5 (Potential). FT TOPO_DOM 209 265 Cytoplasmic (Potential). FT TRANSMEM 266 290 6 (Potential). FT TOPO_DOM 291 295 Extracellular (Potential). FT TRANSMEM 296 320 7 (Potential). FT TOPO_DOM 321 440 Cytoplasmic (Potential). FT MOD_RES 125 125 Phosphotyrosine (By similarity). FT DISULFID 99 180 By similarity. SQ SEQUENCE 440 AA; 46952 MW; 75CFFF4D27F126EE CRC64; MVPEPGPSAN STPAWGAGPP SAPGGSGWVA AALCVVIALT AAANSLLIAL ICTQPALRNT SNFFLVSLFT SDLMVGLVVM PPAMLNALYG RWVLARGLCL LWTAFDVMCC SASILNLCLI SLDRYLLILS PLRYKLRMTP PRALALVLGA WSLAALASFL PLLLGWHELG HARPPVPGQC RLLASLPFVL VASGLTFFLP SGAICFTYCR ILLAARKQAV QVASLTTGMA SQASETLQVP RTPRPGVESA DSRRLATKHS RKALKASLTL GILLGMFFVT WLPFFVANIV QAVCDCISPG LFDVLTWLGY CNSTMNPIIY PLFMRDFKRA LGRFLPCPRC PRERQASLAS PSLRTSHSGP RPGLSLQQVL PLPLPPDSDS DSDAGSGGSS GLRLTAQLLL PGEATRDPPL PTRAAAAVNF FNIDPAEPEL RPHPLGIPTN // ID 5HT6R_RAT Reviewed; 436 AA. AC P31388; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 23-JAN-2007, entry version 50. DE 5-hydroxytryptamine 6 receptor (5-HT-6) (Serotonin receptor 6) (ST- DE B17). GN Name=Htr6; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Corpus striatum; RX MEDLINE=93196608; PubMed=7680751; RA Monsma F.J. Jr., Shen Y., Ward R.P., Hamblin M.W., Sibley D.R.; RT "Cloning and expression of a novel serotonin receptor with high RT affinity for tricyclic psychotropic drugs."; RL Mol. Pharmacol. 43:320-327(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93277562; PubMed=8389146; RA Ruat M., Traiffort E., Arrang J.-M., Tardivel-Lacombe J., Diaz J., RA Leurs R., Schwartz J.-C.; RT "A novel rat serotonin (5-HT6) receptor: molecular cloning, RT localization and stimulation of cAMP accumulation."; RL Biochem. Biophys. Res. Commun. 193:268-276(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; RA Martial R.; RT "A novel rat serotonin (5HT6) receptor."; RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. It has a high affinity for tricyclic psychotropic drugs. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Localized exclusively in the central nervous CC system, predominantly in the corpus striatum but also in various CC limbic and cortical regions. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L03202; AAA40618.1; -; mRNA. DR EMBL; S62043; AAB26908.1; -; mRNA. DR EMBL; L19656; AAA40611.1; -; mRNA. DR PIR; I57942; I57942. DR PIR; JN0591; JN0591. DR UniGene; Rn.10552; -. DR KEGG; rno:64354; -. DR RGD; 62044; Htr6. DR GO; GO:0004993; F:serotonin receptor activity; IDA:RGD. DR GO; GO:0007187; P:G-protein signaling, coupled to cyclic nucl...; IMP:RGD. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphorylation; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 436 5-hydroxytryptamine 6 receptor. FT /FTId=PRO_0000068977. FT TOPO_DOM 1 34 Extracellular (Potential). FT TRANSMEM 35 57 1 (Potential). FT TOPO_DOM 58 64 Cytoplasmic (Potential). FT TRANSMEM 65 85 2 (Potential). FT TOPO_DOM 86 100 Extracellular (Potential). FT TRANSMEM 101 122 3 (Potential). FT TOPO_DOM 123 144 Cytoplasmic (Potential). FT TRANSMEM 145 166 4 (Potential). FT TOPO_DOM 167 184 Extracellular (Potential). FT TRANSMEM 185 208 5 (Potential). FT TOPO_DOM 209 265 Cytoplasmic (Potential). FT TRANSMEM 266 290 6 (Potential). FT TOPO_DOM 291 295 Extracellular (Potential). FT TRANSMEM 296 320 7 (Potential). FT TOPO_DOM 321 436 Cytoplasmic (Potential). FT MOD_RES 125 125 Phosphotyrosine (By similarity). FT CARBOHYD 9 9 N-linked (GlcNAc...) (Potential). FT DISULFID 99 180 By similarity. FT CONFLICT 57 57 L -> V (in Ref. 1). FT CONFLICT 336 436 PCVHCPPEHRPALPPPPCGPLTAVPDQASACSRCCLCLCRQ FT TQIQTPLQGAPRACSSQPSFCCLERPPGTPRHPPGPPLWST FT SLSQTLWSLRYGRIHSVPP -> HASTVPRSTGQPCLPLHV FT DLSQRCQTRPQLQQVLALPLPPNSDSDSASGGTSGLQLTAQ FT LLLPGEATRDPPPPTRATTVVNFFVTDSVEPEIRPHPLSSP FT VN (in Ref. 1). SQ SEQUENCE 436 AA; 46923 MW; 6BC00F6A3CBA5FB4 CRC64; MVPEPGPVNS STPAWGPGPP PAPGGSGWVA AALCVVIVLT AAANSLLIVL ICTQPALRNT SNFFLVSLFT SDLMVGLVVM PPAMLNALYG RWVLARGLCL LWTAFDVMCC SASILNLCLI SLDRYLLILS PLRYKLRMTA PRALALILGA WSLAALASFL PLLLGWHELG KARTPAPGQC RLLASLPFVL VASGVTFFLP SGAICFTYCR ILLAARKQAV QVASLTTGTA GQALETLQVP RTPRPGMESA DSRRLATKHS RKALKASLTL GILLGMFFVT WLPFFVANIA QAVCDCISPG LFDVLTWLGY CNSTMNPIIY PLFMRDFKRA LGRFLPCVHC PPEHRPALPP PPCGPLTAVP DQASACSRCC LCLCRQTQIQ TPLQGAPRAC SSQPSFCCLE RPPGTPRHPP GPPLWSTSLS QTLWSLRYGR IHSVPP // ID 5HT7R_CAVPO Reviewed; 446 AA. AC P50407; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 31-OCT-2006, entry version 40. DE 5-hydroxytryptamine 7 receptor (5-HT-7) (Serotonin receptor 7) (5-HT- DE X). GN Name=HTR7; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Hippocampus; RX MEDLINE=94308771; PubMed=7518496; RA Tsou A., Kosaka A., Bach C., Zuppan P., Yee C., Tom L., Alvarez R., RA Ramsey S., Bonhaus D.W., Stefanich E., Jakeman L., Eglen R.M., RA Chan H.W.; RT "Cloning and expression of a 5-hydroxytryptamine7 receptor positively RT coupled to adenylyl cyclase."; RL J. Neurochem. 63:456-464(1994). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U41372; AAA83015.1; -; mRNA. DR HSSP; P29274; 1MMH. DR InterPro; IPR001069; 5HT_7_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001671; Melcrt_ACTH_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00652; 5HT7RECEPTR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00534; MCRFAMILY. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 446 5-hydroxytryptamine 7 receptor. FT /FTId=PRO_0000068978. FT TOPO_DOM 1 82 Extracellular (Potential). FT TRANSMEM 83 109 1 (Potential). FT TOPO_DOM 110 119 Cytoplasmic (Potential). FT TRANSMEM 120 145 2 (Potential). FT TOPO_DOM 146 157 Extracellular (Potential). FT TRANSMEM 158 179 3 (Potential). FT TOPO_DOM 180 199 Cytoplasmic (Potential). FT TRANSMEM 200 223 4 (Potential). FT TOPO_DOM 224 238 Extracellular (Potential). FT TRANSMEM 239 261 5 (Potential). FT TOPO_DOM 262 329 Cytoplasmic (Potential). FT TRANSMEM 330 353 6 (Potential). FT TOPO_DOM 354 365 Extracellular (Potential). FT TRANSMEM 366 388 7 (Potential). FT TOPO_DOM 389 446 Cytoplasmic (Potential). FT LIPID 402 402 S-palmitoyl cysteine (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 67 67 N-linked (GlcNAc...) (Potential). FT DISULFID 156 232 By similarity. SQ SEQUENCE 446 AA; 49614 MW; B63FA73712F3B088 CRC64; MMGVNSSGRP DLYGHLHSIL LPGRGLPDWS PDGGADPGVS TWTPRLLSGV PEVAASPSPS WDGTWDNVSG CGEQINYGRA EKVVIGSILT LITLLTIAGN CLVVISVCFV KKLRQPSNYL IVSLALADLS VAVAVIPFVS VTDLIGGKWI FGHFFCNVFI AMDVMCCTAS IMTLCVISID RYLGITRPLT YPVRQNGKCM PKMILSVWLL SASITLPPLF GWAQNVNDDK VCLISQDFGY TIYSTAVAFY IPMSVMLFMY YRIYKAARKS AAKHKFPGFP RVQPESIISL NGMVKLQKEV EECANLSRLL KHERKNISIF KREQKAATTL GIIVGAFTVC WLPFFLLSTA RPFICGTACS CIPLWVERTC LWLGYANSLI NPFIYAFFNR DLRTTYRSLL QCQYRNINRK LSAAGMHEAL KLAERPERPE CVLQNSDYCR KKGHDS // ID 5HT7R_HUMAN Reviewed; 479 AA. AC P34969; P78336; P78372; P78516; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 23-JAN-2007, entry version 69. DE 5-hydroxytryptamine 7 receptor (5-HT-7) (Serotonin receptor 7) (5-HT- DE X) (5HT7). GN Name=HTR7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, AND RP TISSUE SPECIFICITY. RX MEDLINE=97238071; PubMed=9084407; RA Heidmann D.E.A., Metcalf M.A., Kohen R., Hamblin M.W.; RT "Four 5-hydroxytryptamine7 (5-HT7) receptor isoforms in human and rat RT produced by alternative splicing: species differences due to altered RT intron-exon organization."; RL J. Neurochem. 68:1372-1381(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RC TISSUE=Fetal brain, and Placenta; RX MEDLINE=94043137; PubMed=8226867; RA Bard J.A., Zgombick J.M., Adham N., Vaysse P., Branchek T.A., RA Weinshank R.L.; RT "Cloning of a novel human serotonin receptor (5-HT7) positively linked RT to adenylate cyclase."; RL J. Biol. Chem. 268:23422-23426(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC TISSUE=Brain; RA King M.M., Aronstam R.S., Sharma S.V.; RT "Isolation of cDNA coding for 5-hydroxytryptamine receptor 7, RT transcript variant b (HTR7B)."; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). 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 [5] RP VARIANTS LYS-92 AND LEU-279. RX MEDLINE=97298817; PubMed=9154233; RA Erdmann J., Nothen M.M., Shimron-Abarbanell D., Rietschel M., RA Albus M., Borrmann M., Maier W., Franzek E., Korner J., Weigelt B., RA Fimmers R., Propping P.; RT "The human serotonin 7 (5-HT7) receptor gene: genomic organization and RT systematic mutation screening in schizophrenia and bipolar affective RT disorder."; RL Mol. Psychiatry 1:392-397(1996). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Isoform A and isoform B appear to be expressed at higher CC levels; CC Name=D; CC IsoId=P34969-1; Sequence=Displayed; CC Name=A; CC IsoId=P34969-2; Sequence=VSP_001857; CC Name=B; CC IsoId=P34969-3; Sequence=VSP_001856; CC -!- TISSUE SPECIFICITY: Isoform A is the predominant isoform in CC spleen, caudate and hippocampus. Isoform B is expressed at lower CC levels, and isoform D is a minor isoform. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U68487; AAB48393.1; -; mRNA. DR EMBL; U68488; AAB48394.1; -; mRNA. DR EMBL; U68492; AAF07218.1; -; Genomic_DNA. DR EMBL; U68493; AAF07217.1; -; Genomic_DNA. DR EMBL; U68492; AAF07217.1; JOINED; Genomic_DNA. DR EMBL; U68493; AAB48397.2; -; Genomic_DNA. DR EMBL; U68492; AAB48397.2; JOINED; Genomic_DNA. DR EMBL; L21195; AAC37538.1; -; mRNA. DR EMBL; AY493988; AAR87480.1; -; mRNA. DR EMBL; BC047526; AAH47526.1; -; mRNA. DR PIR; A48881; A48881. DR UniGene; Hs.73739; -. DR Ensembl; ENSG00000148680; Homo sapiens. DR KEGG; hsa:3363; -. DR HGNC; HGNC:5302; HTR7. DR MIM; 182137; gene. DR DrugBank; APRD00945; Eletriptan. DR DrugBank; APRD00540; Ziprasidone. DR ArrayExpress; P34969; -. DR GermOnline; ENSG00000148680; Homo sapiens. DR RZPD-ProtExp; IOH45473; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004993; F:serotonin receptor activity; TAS:ProtInc. DR GO; GO:0007623; P:circadian rhythm; TAS:ProtInc. DR GO; GO:0008015; P:circulation; TAS:ProtInc. DR GO; GO:0007187; P:G-protein signaling, coupled to cyclic nucl...; TAS:ProtInc. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR InterPro; IPR001069; 5HT_7_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001671; Melcrt_ACTH_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00652; 5HT7RECEPTR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00534; MCRFAMILY. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Polymorphism; Receptor; Transducer; KW Transmembrane. FT CHAIN 1 479 5-hydroxytryptamine 7 receptor. FT /FTId=PRO_0000068979. FT TOPO_DOM 1 83 Extracellular (Potential). FT TRANSMEM 84 104 1 (Potential). FT TOPO_DOM 105 117 Cytoplasmic (Potential). FT TRANSMEM 118 138 2 (Potential). FT TOPO_DOM 139 157 Extracellular (Potential). FT TRANSMEM 158 178 3 (Potential). FT TOPO_DOM 179 201 Cytoplasmic (Potential). FT TRANSMEM 202 222 4 (Potential). FT TOPO_DOM 223 236 Extracellular (Potential). FT TRANSMEM 237 257 5 (Potential). FT TOPO_DOM 258 325 Cytoplasmic (Potential). FT TRANSMEM 326 346 6 (Potential). FT TOPO_DOM 347 367 Extracellular (Potential). FT TRANSMEM 368 388 7 (Potential). FT TOPO_DOM 389 479 Cytoplasmic (Potential). FT LIPID 401 401 S-palmitoyl cysteine (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 66 66 N-linked (GlcNAc...) (Potential). FT DISULFID 155 231 By similarity. FT VAR_SEQ 433 479 RACTRRVLLRPEKRPPVSVWVLQSPDHHNWLADKMLTTVEK FT KVMIHD -> QNADYCRKKGHDS (in isoform A). FT /FTId=VSP_001857. FT VAR_SEQ 433 479 Missing (in isoform B). FT /FTId=VSP_001856. FT VARIANT 92 92 T -> K. FT /FTId=VAR_012995. FT VARIANT 279 279 P -> L. FT /FTId=VAR_012996. SQ SEQUENCE 479 AA; 53555 MW; 1F62E985EADE1F23 CRC64; MMDVNSSGRP DLYGHLRSFL LPEVGRGLPD LSPDGGADPV AGSWAPHLLS EVTASPAPTW DAPPDNASGC GEQINYGRVE KVVIGSILTL ITLLTIAGNC LVVISVCFVK KLRQPSNYLI VSLALADLSV AVAVMPFVSV TDLIGGKWIF GHFFCNVFIA MDVMCCTASI MTLCVISIDR YLGITRPLTY PVRQNGKCMA KMILSVWLLS ASITLPPLFG WAQNVNDDKV CLISQDFGYT IYSTAVAFYI PMSVMLFMYY QIYKAARKSA AKHKFPGFPR VEPDSVIALN GIVKLQKEVE ECANLSRLLK HERKNISIFK REQKAATTLG IIVGAFTVCW LPFFLLSTAR PFICGTSCSC IPLWVERTFL WLGYANSLIN PFIYAFFNRD LRTTYRSLLQ CQYRNINRKL SAAGMHEALK LAERPERPEF VLRACTRRVL LRPEKRPPVS VWVLQSPDHH NWLADKMLTT VEKKVMIHD // ID 5HT7R_MOUSE Reviewed; 448 AA. AC P32304; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 23-JAN-2007, entry version 55. DE 5-hydroxytryptamine 7 receptor (5-HT-7) (Serotonin receptor 7) (5-HT- DE X) (5HT7). GN Name=Htr7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93360913; PubMed=8394987; RA Plassat J.-L., Amlaiky N., Hen R.; RT "Molecular cloning of a mammalian serotonin receptor that activates RT adenylate cyclase."; RL Mol. Pharmacol. 44:229-236(1993). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z23107; CAA80654.1; -; mRNA. DR PIR; I48779; S36402. DR UniGene; Mm.254266; -. DR Ensembl; ENSMUSG00000024798; Mus musculus. DR KEGG; mmu:15566; -. DR MGI; MGI:99841; Htr7. DR ArrayExpress; P32304; -. DR GermOnline; ENSMUSG00000024798; Mus musculus. DR InterPro; IPR001069; 5HT_7_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001671; Melcrt_ACTH_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00652; 5HT7RECEPTR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00534; MCRFAMILY. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 448 5-hydroxytryptamine 7 receptor. FT /FTId=PRO_0000068980. FT TOPO_DOM 1 84 Extracellular (Potential). FT TRANSMEM 85 111 1 (Potential). FT TOPO_DOM 112 121 Cytoplasmic (Potential). FT TRANSMEM 122 147 2 (Potential). FT TOPO_DOM 148 159 Extracellular (Potential). FT TRANSMEM 160 181 3 (Potential). FT TOPO_DOM 182 201 Cytoplasmic (Potential). FT TRANSMEM 202 225 4 (Potential). FT TOPO_DOM 226 240 Extracellular (Potential). FT TRANSMEM 241 263 5 (Potential). FT TOPO_DOM 264 331 Cytoplasmic (Potential). FT TRANSMEM 332 355 6 (Potential). FT TOPO_DOM 356 367 Extracellular (Potential). FT TRANSMEM 368 390 7 (Potential). FT TOPO_DOM 391 448 Cytoplasmic (Potential). FT LIPID 404 404 S-palmitoyl cysteine (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 69 69 N-linked (GlcNAc...) (Potential). FT DISULFID 158 234 By similarity. SQ SEQUENCE 448 AA; 49861 MW; 01C7380300991C30 CRC64; MMDVNSSGRP DLYGHLRSLI LPEVGRRLQD LSPDGGAHSV VSSWMPHLLS GFPEVTASPA PTWDAPPDNV SGCGEQINYG RVEKVVIGSI LTLITLLTIA GNCLVVISVC FVKNVRQPSN YLIVSLALAD LSVAVAVMPF VSVTDLIGGK WIFGHFFCNV FIAMDVMCCT ASIMTLCVIS IDRYLGITRP LTYPVRQNGK CMAKMILSVW PLSASITLPP LFGWAQNVND DKVCLISQDF GYTIYSTAVA FYIPMSVMLF MYYQIYKAAR KSAAKHKFSG FPRVQPESVI SLNGVVKLQK EVEECANLSR LLKHERKNIS SFKREQKAAT TLGIIVGAFT VCWLPFFLLS TARPFICGTS CSCIPLWVER TCLWLGYANS LINPFIYSFF NRDLRTTYRS LLQCQYRNIN RKLSAAGMHE ALKLAERPER SEFVLQNCDH CGKKGHDT // ID 5HT7R_RAT Reviewed; 448 AA. AC P32305; P97936; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 2. DT 20-FEB-2007, entry version 59. DE 5-hydroxytryptamine 7 receptor (5-HT-7) (Serotonin receptor 7) (5-HT- DE X) (5HT7) (GPRFO). GN Name=Htr7; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A). RC STRAIN=Wistar; TISSUE=Brain; RX MEDLINE=93391391; PubMed=8397408; RA Martial R., Traiffort E., Leurs R., Tardivel-Lacombe J., Diaz J., RA Arrang J.-M., Schwartz J.-C.; RT "Molecular cloning, characterization, and localization of a high- RT affinity serotonin receptor (5-HT7) activating cAMP formation."; RL Proc. Natl. Acad. Sci. U.S.A. 90:8547-8551(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RC STRAIN=Wistar; TISSUE=Brain; RX MEDLINE=93298238; PubMed=8517926; RA Meyerhof W., Obermueller F., Fehr S., Richter D.; RT "A novel rat serotonin receptor: primary structure, pharmacology, and RT expression pattern in distinct brain regions."; RL DNA Cell Biol. 12:401-409(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). RC STRAIN=Sprague-Dawley; TISSUE=Hypothalamus; RX MEDLINE=94000811; PubMed=8398139; DOI=10.1016/0896-6273(93)90149-L; RA Lovenberg T.W., Baron B.M., de Lecea L., Miller J.D., Prosser R.A., RA Rea M.A., Foye P.E., Slone A.L., Siegel B.W., Danielson P.E., RA Sutcliffe G.J., Erlander M.G.; RT "A novel adenylyl cyclase-activating serotonin receptor (5-HT7) RT implicated in the regulation of mammalian circadian rhythms."; RL Neuron 11:449-458(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A). RC STRAIN=Sprague-Dawley; RX MEDLINE=93352643; PubMed=8394362; RA Shen Y., Monsma F.J. Jr., Metcalf M.A., Jose P.A., Hamblin M.W., RA Sibley D.R.; RT "Molecular cloning and expression of a 5-hydroxytryptamine7 serotonin RT receptor subtype."; RL J. Biol. Chem. 268:18200-18204(1993). RN [5] RP NUCLEOTIDE SEQUENCE (ISOFORM B). RX MEDLINE=97238071; PubMed=9084407; RA Heidmann D.E.A., Metcalf M.A., Kohen R., Hamblin M.W.; RT "Four 5-hydroxytryptamine7 (5-HT7) receptor isoforms in human and rat RT produced by alternative splicing: species differences due to altered RT intron-exon organization."; RL J. Neurochem. 68:1372-1381(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. This receptor is implicated in the regulation of CC mammalian circadian rhythms. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=P32305-1; Sequence=Displayed; CC Name=B; CC IsoId=P32305-2; Sequence=VSP_001858; CC -!- TISSUE SPECIFICITY: Thalamus, hypothalamus, and the hippocampal CC rudiments. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L19654; AAA40617.1; -; Genomic_DNA. DR EMBL; X69663; CAA49352.1; -; mRNA. DR EMBL; L22558; AAA42132.1; -; mRNA. DR EMBL; L15228; AAA42134.1; ALT_INIT; Genomic_DNA. DR EMBL; U68489; AAB48395.1; -; mRNA. DR PIR; A47519; A47519. DR UniGene; Rn.87132; -. DR Ensembl; ENSRNOG00000018827; Rattus norvegicus. DR KEGG; rno:65032; -. DR RGD; 71034; Htr7. DR ArrayExpress; P32305; -. DR GermOnline; ENSRNOG00000018827; Rattus norvegicus. DR GO; GO:0030594; F:neurotransmitter receptor activity; IDA:RGD. DR GO; GO:0004993; F:serotonin receptor activity; IDA:RGD. DR GO; GO:0007210; P:serotonin receptor signaling pathway; IDA:RGD. DR GO; GO:0007192; P:serotonin receptor, adenylate cyclase activ...; IDA:RGD. DR InterPro; IPR001069; 5HT_7_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001671; Melcrt_ACTH_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00652; 5HT7RECEPTR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00534; MCRFAMILY. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 448 5-hydroxytryptamine 7 receptor. FT /FTId=PRO_0000068981. FT TOPO_DOM 1 84 Extracellular (Potential). FT TRANSMEM 85 111 1 (Potential). FT TOPO_DOM 112 121 Cytoplasmic (Potential). FT TRANSMEM 122 147 2 (Potential). FT TOPO_DOM 148 159 Extracellular (Potential). FT TRANSMEM 160 181 3 (Potential). FT TOPO_DOM 182 201 Cytoplasmic (Potential). FT TRANSMEM 202 225 4 (Potential). FT TOPO_DOM 226 240 Extracellular (Potential). FT TRANSMEM 241 263 5 (Potential). FT TOPO_DOM 264 331 Cytoplasmic (Potential). FT TRANSMEM 332 355 6 (Potential). FT TOPO_DOM 356 367 Extracellular (Potential). FT TRANSMEM 368 390 7 (Potential). FT TOPO_DOM 391 448 Cytoplasmic (Potential). FT LIPID 404 404 S-palmitoyl cysteine (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 69 69 N-linked (GlcNAc...) (Potential). FT DISULFID 158 234 By similarity. FT VAR_SEQ 436 448 Missing (in isoform B). FT /FTId=VSP_001858. FT CONFLICT 110 110 C -> S (in Ref. 4). FT CONFLICT 149 149 G -> D (in Ref. 2). FT CONFLICT 168 168 C -> Y (in Ref. 2). FT CONFLICT 196 196 R -> S (in Ref. 2). FT CONFLICT 199 199 G -> E (in Ref. 2). FT CONFLICT 237 237 S -> N (in Ref. 2). FT CONFLICT 348 348 L -> P (in Ref. 2). FT CONFLICT 396 396 T -> P (in Ref. 4). FT CONFLICT 398 398 Y -> S (in Ref. 4). SQ SEQUENCE 448 AA; 49837 MW; 746E69C7763B317B CRC64; MMDVNSSGRP DLYGHLRSLI LPEVGRGLQD LSPDGGAHPV VSSWMPHLLS GFLEVTASPA PTWDAPPDNV SGCGEQINYG RVEKVVIGSI LTLITLLTIA GNCLVVISVC FVKKLRQPSN YLIVSLALAD LSVAVAVMPF VSVTDLIGGK WIFGHFFCNV FIAMDVMCCT ASIMTLCVIS IDRYLGITRP LTYPVRQNGK CMAKMILSVW LLSASITLPP LFGWAQNVND DKVCLISQDF GYTIYSTAVA FYIPMSVMLF MYYQIYKAAR KSAAKHKFPG FPRVQPESVI SLNGVVKLQK EVEECANLSR LLKHERKNIS IFKREQKAAT TLGIIVGAFT VCWLPFFLLS TARPFICGTS CSCIPLWVER TCLWLGYANS LINPFIYAFF NRDLRTTYRS LLQCQYRNIN RKLSAAGMHE ALKLAERPER SEFVLQNSDH CGKKGHDT // ID 5HT7R_XENLA Reviewed; 425 AA. AC Q91559; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-FEB-2007, entry version 43. DE 5-hydroxytryptamine 7 receptor (5-HT-7) (Serotonin receptor 7). GN Name=htr7; Synonyms=5ht7; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Skin; RX MEDLINE=96172463; PubMed=8589994; RA Nelson C.S., Cone R.D., Robbins L.S., Allen C.N., Adelman J.P.; RT "Cloning and expression of a 5HT7 receptor from Xenopus laevis."; RL Recept. Channels 3:61-70(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U10161; AAA96812.1; -; mRNA. DR UniGene; Xl.1034; -. DR HSSP; P29274; 1MMH. DR InterPro; IPR001069; 5HT_7_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00652; 5HT7RECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 425 5-hydroxytryptamine 7 receptor. FT /FTId=PRO_0000068982. FT TOPO_DOM 1 70 Extracellular (Potential). FT TRANSMEM 71 97 1 (Potential). FT TOPO_DOM 98 107 Cytoplasmic (Potential). FT TRANSMEM 108 133 2 (Potential). FT TOPO_DOM 134 145 Extracellular (Potential). FT TRANSMEM 146 167 3 (Potential). FT TOPO_DOM 168 187 Cytoplasmic (Potential). FT TRANSMEM 188 211 4 (Potential). FT TOPO_DOM 212 226 Extracellular (Potential). FT TRANSMEM 227 249 5 (Potential). FT TOPO_DOM 250 324 Cytoplasmic (Potential). FT TRANSMEM 325 348 6 (Potential). FT TOPO_DOM 349 360 Extracellular (Potential). FT TRANSMEM 361 383 7 (Potential). FT TOPO_DOM 384 425 Cytoplasmic (Potential). FT LIPID 397 397 S-palmitoyl cysteine (Potential). FT CARBOHYD 14 14 N-linked (GlcNAc...) (Potential). FT CARBOHYD 41 41 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT DISULFID 144 220 By similarity. SQ SEQUENCE 425 AA; 48017 MW; C42C75ACB4A1A255 CRC64; MLIQVQPSHL TDTNLSLHSA KPSSDHQNLL PSEFMTERPL NTTEQDLTAL NHTEKPDCGK ELLLYGDTEK IVIGVVLSII TLFTIAGNAL VIISVCIVKK LRQPSNYLVV SLAAADLSVA VAVMPFVIIT DLVGGEWLFG KVFCNVFIAM DVMCCTASIM TLCVISVDRY LGITRPLTYP ARQNGKLMAK MVFIVWLLSA SITLPPLFGW AKNVNVERVC LISQDFGYTV YSTAVAFYIP MTVMLVMYQR IFVAAKISAE KHKFVNIPRL YEQEGIYCLE DKLPPKKNSK KKKAVEEFAS LSKLIRQDRK NISIFKREQK AARTLGIIVG AFTFCWLPFF LLSTARPFIC GIMCSCMPLR LERTLLWLGY TNSLINPLIY AFFNRDLRTT FWNLLRCKYT NINRRLSAAS MHEALKVTER HEGIL // ID 5HTB1_APLCA Reviewed; 453 AA. AC Q16950; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 29. DE 5-hydroxytryptamine 1 receptor (5-HTB1) (Serotonin receptor 1). GN Name=5HTB1; OS Aplysia californica (California sea hare). OC Eukaryota; Metazoa; Mollusca; Gastropoda; Orthogastropoda; OC Apogastropoda; Heterobranchia; Euthyneura; Opisthobranchia; Anaspidea; OC Aplysioidea; Aplysiidae; Aplysia. OX NCBI_TaxID=6500; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96066780; PubMed=7472509; RA Li X.C., Giot J.F., Kuhl D., Hen R., Kandel E.R.; RT "Cloning and characterization of two related serotonergic receptors RT from the brain and the reproductive system of Aplysia that activate RT phospholipase C."; RL J. Neurosci. 15:7585-7591(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin). 5-HT plays important roles in CC various behavioral and physiological processes in aplysia. These CC include feeding, locomotion, circadian rhythm, learning and CC memory, synaptic plasticity, and synaptic growth. This receptor is CC mediated by G proteins that stimulate phospholipase C. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Reproductive system. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43557; AAA93101.1; -; Genomic_DNA. DR HSSP; P29274; 1MMH. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Membrane; Receptor; Transducer; KW Transmembrane. FT CHAIN 1 453 5-hydroxytryptamine 1 receptor. FT /FTId=PRO_0000068983. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 57 1 (Potential). FT TOPO_DOM 58 74 Cytoplasmic (Potential). FT TRANSMEM 75 94 2 (Potential). FT TOPO_DOM 95 110 Extracellular (Potential). FT TRANSMEM 111 133 3 (Potential). FT TOPO_DOM 134 153 Cytoplasmic (Potential). FT TRANSMEM 154 175 4 (Potential). FT TOPO_DOM 176 223 Extracellular (Potential). FT TRANSMEM 224 244 5 (Potential). FT TOPO_DOM 245 301 Cytoplasmic (Potential). FT TRANSMEM 302 322 6 (Potential). FT TOPO_DOM 323 331 Extracellular (Potential). FT TRANSMEM 332 352 7 (Potential). FT TOPO_DOM 353 453 Cytoplasmic (Potential). FT DISULFID 110 225 By similarity. SQ SEQUENCE 453 AA; 50622 MW; 227B997840C0C820 CRC64; MKSLKSSTHD VPHPEHVVWA PPAYDEQHHL FFSHGTVLIG IVGSLIITVA VVGNVLVCLA IFTEPILSHS KSNFFIVSLA VADLLLALLV MTFALVNDMY GYWLFGETFC FIWMSADVMC ETASIFSICV ISYDRLKQVQ KPLHYEEFMT TTRALLIIAC LWICSFVLSF VPIFLEWHEL SVEEIKAIFK DNKTEKEKAL EAHNFSSALN QTLGDNQKSN AKHVCLFDVH FTYSVIYSFI CFYVPCTLML TNYLRLFLIA QTHQVRIRSL QMTNPPQLRG QGASSYRNQG TQGSKAARTL TIITGTFLAC WLPFFIINPI AAADEHLIPL ECFMVTIWLG YFNSSVNPII YGTSNSKFRA AFKRLLRCRS VKSVVGSISP VSPAYRAFSW IRPSRLDLSS SEHPSDACDT GRGKNSKGGD CATADPTKPD VSVSEEIIYA GTKVFDSDTA FSS // ID 5HTB2_APLCA Reviewed; 421 AA. AC Q16951; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 34. DE 5-hydroxytryptamine 2 receptor (5-HTB2) (Serotonin receptor 2). GN Name=5HTB2; OS Aplysia californica (California sea hare). OC Eukaryota; Metazoa; Mollusca; Gastropoda; Orthogastropoda; OC Apogastropoda; Heterobranchia; Euthyneura; Opisthobranchia; Anaspidea; OC Aplysioidea; Aplysiidae; Aplysia. OX NCBI_TaxID=6500; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96066780; PubMed=7472509; RA Li X.C., Giot J.F., Kuhl D., Hen R., Kandel E.R.; RT "Cloning and characterization of two related serotonergic receptors RT from the brain and the reproductive system of Aplysia that activate RT phospholipase C."; RL J. Neurosci. 15:7585-7591(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin). 5-HT plays important roles in CC various behavioral and physiological processes in aplysia. These CC include feeding, locomotion, circadian rhythm, learning and CC memory, synaptic plasticity, and synaptic growth. This receptor is CC mediated by G proteins that stimulate phospholipase C. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Central nervous system. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43558; AAA93102.1; -; Genomic_DNA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR000611; NPY_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01012; NRPEPTIDEYR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 421 5-hydroxytryptamine 2 receptor. FT /FTId=PRO_0000068984. FT TOPO_DOM 1 21 Extracellular (Potential). FT TRANSMEM 22 42 1 (Potential). FT TOPO_DOM 43 59 Cytoplasmic (Potential). FT TRANSMEM 60 79 2 (Potential). FT TOPO_DOM 80 95 Extracellular (Potential). FT TRANSMEM 96 118 3 (Potential). FT TOPO_DOM 119 138 Cytoplasmic (Potential). FT TRANSMEM 139 160 4 (Potential). FT TOPO_DOM 161 213 Extracellular (Potential). FT TRANSMEM 214 234 5 (Potential). FT TOPO_DOM 235 274 Cytoplasmic (Potential). FT TRANSMEM 275 295 6 (Potential). FT TOPO_DOM 296 304 Extracellular (Potential). FT TRANSMEM 305 325 7 (Potential). FT TOPO_DOM 326 421 Cytoplasmic (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT DISULFID 95 210 By similarity. SQ SEQUENCE 421 AA; 47637 MW; 88482EA81D15FED6 CRC64; MLCGRLRHTM NSTTCFFSHR TVLIGIVGSL IIAVSVVGNV LVCLAIFTEP ILSHSKSKFF IVSLAVADLL LALLVMTFAL VNSLYGYWLF GETFCFIWMS ADVMCETASI FSICVISYNR LKQVQKPLQY EEFMTTTRAL LIIASLWICS FVVSFVPFFL EWHELSMEEI KTIFKDLISD KVKTSDAHTF SFALEQTLGD NRTSNPKPEC LFDVHFIYSV IYSLFCFYIP CTLMLRNYLR LFLIAKKHHV RIKNLHRLHR NQGTQGSKAA RTLTIITGTF LACWLPFFII NPIEAVDEHL IPLECFMVTI WLGYFNSCVN PIIYGTSNSK FRAAFQRLLR CRSVKSTVSS ISPVASVYRA FSWIRPSLLD GPPSAVCDTG QDENRKGGGC VTTIPTESHV IISEEEIRAN VMLSESDTVF S // ID 5HTR_BOMMO Reviewed; 446 AA. AC Q17239; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 36. DE 5-hydroxytryptamine receptor (5-HT receptor) (Serotonin receptor). OS Bombyx mori (Silk moth). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Bombycidae; Bombyx. OX NCBI_TaxID=7091; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Antenna; RX MEDLINE=97166608; PubMed=9014328; DOI=10.1016/S0965-1748(96)00031-8; RA von Nickisch-Rosenegk E., Krieger J., Kubick S., Laage R., Strobel J., RA Strotmann J., Breer H.; RT "Cloning of biogenic amine receptors from moths (Bombyx mori and RT Heliothis virescens)."; RL Insect Biochem. Mol. Biol. 26:817-827(1996). CC -!- FUNCTION: This is a receptor for 5-hydroxytryptamine (serotonin), CC a biogenic hormone that function as a neurotransmitter, a hormone, CC and a mitogen (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X95604; CAA64862.1; -; mRNA. DR UniGene; Bmo.8; -. DR HSSP; P08913; 1HLL. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 446 5-hydroxytryptamine receptor. FT /FTId=PRO_0000068985. FT TOPO_DOM 1 65 Extracellular (Potential). FT TRANSMEM 66 88 1 (Potential). FT TOPO_DOM 89 98 Cytoplasmic (Potential). FT TRANSMEM 99 120 2 (Potential). FT TOPO_DOM 121 135 Extracellular (Potential). FT TRANSMEM 136 157 3 (Potential). FT TOPO_DOM 158 176 Cytoplasmic (Potential). FT TRANSMEM 177 199 4 (Potential). FT TOPO_DOM 200 227 Extracellular (Potential). FT TRANSMEM 228 249 5 (Potential). FT TOPO_DOM 250 367 Cytoplasmic (Potential). FT TRANSMEM 368 391 6 (Potential). FT TOPO_DOM 392 399 Extracellular (Potential). FT TRANSMEM 400 422 7 (Potential). FT TOPO_DOM 423 446 Cytoplasmic (Potential). FT CARBOHYD 23 23 N-linked (GlcNAc...) (Potential). FT CARBOHYD 27 27 N-linked (GlcNAc...) (Potential). FT CARBOHYD 36 36 N-linked (GlcNAc...) (Potential). FT CARBOHYD 42 42 N-linked (GlcNAc...) (Potential). FT DISULFID 134 214 By similarity. SQ SEQUENCE 446 AA; 48599 MW; 85D4E52C63726AA4 CRC64; MEGAEGQEEL DWEALYLRLP LQNCSWNSTG WEPNWNVTVV PNTTWWQASA PFDTPAALVR AAAKAVVLGL LILATVVGNV FVIAAILLER HLRSAANNLI LSLAVADLLV ACLVMPLGAV YEVVQRWTLG PELCDMWTSG DVLCCTASIL HLVAIALDRY WAVTNIDYIH ASTAKRVGMM IACVWTVSFF VCIAQLLGWK DPDWNQRVSE DLRCVVSQDV GYQIFATASS FYVPVLIILI LYWRIYQTAR KRIRRRRGAT ARGGVGPPPV PAGGALVAGG GSGGIAAAVV AVIGRPLPTI SETTTTGFTN VSSNNTSPEK QSCANGLEAD PPTTGYGAVA AAYYPSLVRR KPKEAADSKR ERKAAKTLAI ITGAFVACWL PFFVLAILVP TCDCEVSPVL TSLSLWLGYF NSTLNPVIYT VFSPEFRHAF QRLLCGRRVR RRRAPQ // ID 5HTR_HELVI Reviewed; 466 AA. AC Q25190; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 31-OCT-2006, entry version 34. DE 5-hydroxytryptamine receptor (5-HT receptor) (Serotonin receptor). OS Heliothis virescens (Noctuid moth) (Owlet moth). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea; OC Noctuidae; Heliothinae; Heliothis. OX NCBI_TaxID=7102; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Antenna; RX MEDLINE=97166608; PubMed=9014328; DOI=10.1016/S0965-1748(96)00031-8; RA von Nickisch-Rosenegk E., Krieger J., Kubick S., Laage R., Strobel J., RA Strotmann J., Breer H.; RT "Cloning of biogenic amine receptors from moths (Bombyx mori and RT Heliothis virescens)."; RL Insect Biochem. Mol. Biol. 26:817-827(1996). CC -!- FUNCTION: This is a receptor for 5-hydroxytryptamine (serotonin), CC a biogenic hormone that function as a neurotransmitter, a hormone, CC and a mitogen (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X95605; CAA64863.1; -; mRNA. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 466 5-hydroxytryptamine receptor. FT /FTId=PRO_0000068986. FT TOPO_DOM 1 66 Extracellular (Potential). FT TRANSMEM 67 89 1 (Potential). FT TOPO_DOM 90 99 Cytoplasmic (Potential). FT TRANSMEM 100 121 2 (Potential). FT TOPO_DOM 122 136 Extracellular (Potential). FT TRANSMEM 137 158 3 (Potential). FT TOPO_DOM 159 177 Cytoplasmic (Potential). FT TRANSMEM 178 200 4 (Potential). FT TOPO_DOM 201 228 Extracellular (Potential). FT TRANSMEM 229 250 5 (Potential). FT TOPO_DOM 251 386 Cytoplasmic (Potential). FT TRANSMEM 387 410 6 (Potential). FT TOPO_DOM 411 419 Extracellular (Potential). FT TRANSMEM 420 442 7 (Potential). FT TOPO_DOM 443 466 Cytoplasmic (Potential). FT CARBOHYD 2 2 N-linked (GlcNAc...) (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 29 29 N-linked (GlcNAc...) (Potential). FT CARBOHYD 41 41 N-linked (GlcNAc...) (Potential). FT CARBOHYD 45 45 N-linked (GlcNAc...) (Potential). FT CARBOHYD 50 50 N-linked (GlcNAc...) (Potential). FT DISULFID 135 215 By similarity. SQ SEQUENCE 466 AA; 52094 MW; AD29A38EC37106EB CRC64; MNASRLPGFN DTSQDQPYPT SSEWFDGSNC SWVDAVSWGC NVTINGTSTN ATSTDVTSFV LMAVTSVVLA LIILATIVGN VFVIAAIIIE RNLQNVANYL VASLAVADLM VACLVMPLGA VYEVSQGWIL GPELCDMWTS SDVLCSSASI LHLVAIATDR YWAVTDVDYI HIRNEKRIFT MIVLVWGAAL VVSLAPQLGW KDPDYLARIT QQQKCLVSQD LAYQIFATMS TFYVPLAVIL ILYWKIFQTA RRRIRRRRDP PPPRPTSADG ATPSGRPVQS ARDRRFVKKR FLNLKKCNQR TRAETLAAAL LLTEGQSTST VDTLDEEPRT TAFTINEKVP PSVSPEKSSS TVTNGSKPER AIVPAPTHRE KKESLEAKRE RKAAKTLAII TGAFVFCWLP FFIMALVMPI CQTCVISDYL ASFFLWLGYF NSTLNPVIYT IFSPDFRQAF ARILFGTHRR RRYKKF // ID 5HTR_LYMST Reviewed; 509 AA. AC Q25414; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 31-OCT-2006, entry version 31. DE 5-hydroxytryptamine receptor (5-HT receptor) (Serotonin receptor). OS Lymnaea stagnalis (Great pond snail). OC Eukaryota; Metazoa; Mollusca; Gastropoda; Pulmonata; Basommatophora; OC Lymnaeoidea; Lymnaeidae; Lymnaea. OX NCBI_TaxID=6523; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93126323; PubMed=8093556; RA Sugamori K.S., Sunahara R.K., Guan H.-C., Bulloch A.G., Tensen C.P., RA Seeman P., Niznik H.B., van Tol H.H.; RT "Serotonin receptor cDNA cloned from Lymnaea stagnalis."; RL Proc. Natl. Acad. Sci. U.S.A. 90:11-15(1993). CC -!- FUNCTION: This is a receptor for 5-hydroxytryptamine (serotonin), CC a biogenic hormone that function as a neurotransmitter, a hormone, CC and a mitogen. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L06803; AAA29290.1; -; mRNA. DR PIR; A47174; A47174. DR HSSP; P08913; 1HLL. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 509 5-hydroxytryptamine receptor. FT /FTId=PRO_0000068987. FT TOPO_DOM 1 99 Extracellular (Potential). FT TRANSMEM 100 122 1 (Potential). FT TOPO_DOM 123 132 Cytoplasmic (Potential). FT TRANSMEM 133 154 2 (Potential). FT TOPO_DOM 155 169 Extracellular (Potential). FT TRANSMEM 170 191 3 (Potential). FT TOPO_DOM 192 210 Cytoplasmic (Potential). FT TRANSMEM 211 233 4 (Potential). FT TOPO_DOM 234 259 Extracellular (Potential). FT TRANSMEM 260 281 5 (Potential). FT TOPO_DOM 282 432 Cytoplasmic (Potential). FT TRANSMEM 433 456 6 (Potential). FT TOPO_DOM 457 465 Extracellular (Potential). FT TRANSMEM 466 488 7 (Potential). FT TOPO_DOM 489 509 Cytoplasmic (Potential). FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). FT CARBOHYD 47 47 N-linked (GlcNAc...) (Potential). FT CARBOHYD 58 58 N-linked (GlcNAc...) (Potential). FT CARBOHYD 68 68 N-linked (GlcNAc...) (Potential). FT CARBOHYD 72 72 N-linked (GlcNAc...) (Potential). FT CARBOHYD 78 78 N-linked (GlcNAc...) (Potential). FT DISULFID 168 246 By similarity. SQ SEQUENCE 509 AA; 56902 MW; D283696C8C50B1B8 CRC64; MANFTFGDLA LDVARMGGLA STPSGLRSTG LTTPGLSPTG LVTSDFNDSY GLTGQFINGS HSSRSRDNAS ANDTSATNMT DDRYWSLTVY SHEHLVLTSV ILGLFVLCCI IGNCFVIAAV MLERSLHNVA NYLILSLAVA DLMVAVLVMP LSVVSEISKV WFLHSEVCDM WISVDVLCCT ASILHLVAIA MDRYWAVTSI DYIRRRSARR ILLMIMVVWI VALFISIPPL FGWRDPNNDP DKTGTCIISQ DKGYTIFSTV GAFYLPMLVM MIIYIRIWLV ARSRIRKDKF QMTKARLKTE ETTLVASPKT EYSVVSDCNG CNSPDSTTEK KKRRAPFKSY GCSPRPERKK NRAKKLPENA NGVNSNSSSS ERLKQIQIET AEAFANGCAE EASIAMLERQ CNNGKKISSN DTPYSRTREK LELKRERKAA RTLAIITGAF LICWLPFFII ALIGPFVDPE GIPPFARSFV LWLGYFNSLL NPIIYTIFSP EFRSAFQKIL FGKYRRGHR // ID 5NG4_PINTA Reviewed; 410 AA. AC Q6J163; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 06-FEB-2007, entry version 13. DE Auxin-induced protein 5NG4. OS Pinus taeda (Loblolly pine). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Coniferopsida; Coniferales; Pinaceae; Pinus; Pinus. OX NCBI_TaxID=3352; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INDUCTION. RC TISSUE=Shoot; RX PubMed=14722770; DOI=10.1007/s00425-003-1175-4; RA Busov V.B., Johannes E., Whetten R.W., Sederoff R.R., Spiker S.L., RA Lanz-Garcia C., Goldfarb B.; RT "An auxin-inducible gene from loblolly pine (Pinus taeda L.) is RT differentially expressed in mature and juvenile-phase shoots and RT encodes a putative transmembrane protein."; RL Planta 218:916-927(2004). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein CC (Potential). Note=Detected in the periphery of cells and punctate CC structures throughout cytoplasm. CC -!- INDUCTION: By auxin in hypocotyls, root and stems but not in CC cotyledons and needles. To a greater degree in juvenile than CC mature shoots. CC -!- SIMILARITY: Contains 1 DUF6 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; AY608411; AAT37621.1; -; mRNA. DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB. DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB. DR GO; GO:0009734; P:auxin mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0006810; P:transport; NAS:UniProtKB. DR InterPro; IPR000620; DUF6_TM. DR Pfam; PF00892; DUF6; 1. KW Glycoprotein; Membrane; Transmembrane. FT CHAIN 1 410 Auxin-induced protein 5NG4. FT /FTId=PRO_0000235823. FT TOPO_DOM 1 16 Cytoplasmic (Potential). FT TRANSMEM 17 37 Potential. FT TOPO_DOM 38 47 Extracellular (Potential). FT TRANSMEM 48 68 Potential. FT TOPO_DOM 69 74 Cytoplasmic (Potential). FT TRANSMEM 75 95 Potential. FT TOPO_DOM 96 109 Extracellular (Potential). FT TRANSMEM 110 130 Potential. FT TOPO_DOM 131 141 Cytoplasmic (Potential). FT TRANSMEM 142 162 Potential. FT TOPO_DOM 163 196 Extracellular (Potential). FT TRANSMEM 197 217 Potential. FT TOPO_DOM 218 229 Cytoplasmic (Potential). FT TRANSMEM 230 250 Potential. FT TOPO_DOM 251 264 Extracellular (Potential). FT TRANSMEM 265 285 Potential. FT TOPO_DOM 286 292 Cytoplasmic (Potential). FT TRANSMEM 293 313 Potential. FT TOPO_DOM 314 317 Extracellular (Potential). FT TRANSMEM 318 338 Potential. FT TOPO_DOM 339 410 Cytoplasmic (Potential). FT DOMAIN 209 338 DUF6. FT CARBOHYD 196 196 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 410 AA; 44975 MW; DD40B4039ADDA8C3 CRC64; MASNIMQRCN VFMSERVKLH AAMLALQFGY AGFHIVSRAA LNMGVSKVVF PVYRNILALM LIGPCAYFLE KKERPALTLS FLIQFFLLAL CGITGQSRIL SLRIVLHIPT FASAIQNSVP AITFIMAAAL RLEKVHISRR DGLAKIIGTV ACVSGATIIT LYKGPPITHI WRPNLEVTAS YFKAFQGNDL SAKSENWTLG CIYLLGNCLA WSGWIVLQAP VLKRYPARLS VTSFTCFFGV IQFLIIAAFF ETDLEHWKIH SGGELFTILY AGFVASGIAF SVQIWCIDRG GPVFVAVYQP VQTIAVAIMA SIILGEQFYL GGIFGAILII IGLYLVLWGK SEEKRLGLLQ AKSSMVPENQ PDNMDQSATL IINSSNGIKP NTSSSLTQPL LLDTSYKTVN IPSPSDEPQP // ID 5NT1A_HUMAN Reviewed; 368 AA. AC Q9BXI3; Q3SYB9; Q5TG98; Q9BWT8; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 20-FEB-2007, entry version 34. DE Cytosolic 5'-nucleotidase 1A (EC 3.1.3.5) (Cytosolic 5'-nucleotidase DE IA) (cN1A) (cN-IA) (cN-I). GN Name=NT5C1A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Heart; RX MEDLINE=21167865; PubMed=11133996; DOI=10.1074/jbc.M011218200; RA Hunsucker S.A., Spychala J., Mitchell B.S.; RT "Human cytosolic 5'-nucleotidase I: characterization and role in RT nucleoside analog resistance."; RL J. Biol. Chem. 276:10498-10504(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Heart; RA Lowenstein J.M., Huang J., Steiner A.; RT "5'-nucleotidase I from human heart."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., RA Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). 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: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides and has a broad substrate specificity. Helps CC to regulate adenosine levels in heart during ischemia and hypoxia. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Magnesium. CC -!- ENZYME REGULATION: Activated by ADP. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Detected CC at intermediate levels in heart, brain, kidney and pancreas. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase type 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; AF331801; AAK01294.1; -; mRNA. DR EMBL; AY028778; AAK30000.1; -; mRNA. DR EMBL; AL035404; CAI19573.1; -; Genomic_DNA. DR EMBL; BC103879; AAI03880.1; -; mRNA. DR EMBL; BC103880; AAI03881.1; -; mRNA. DR UniGene; Hs.307006; -. DR Ensembl; ENSG00000116981; Homo sapiens. DR KEGG; hsa:84618; -. DR HGNC; HGNC:17819; NT5C1A. DR MIM; 610525; gene. DR Reactome; REACT_1698.1; Nucleotide metabolism. DR ArrayExpress; Q9BXI3; -. DR GermOnline; ENSG00000116981; Homo sapiens. DR GO; GO:0005829; C:cytosol; NAS:UniProtKB. DR GO; GO:0008253; F:5'-nucleotidase activity; NAS:UniProtKB. DR GO; GO:0009116; P:nucleoside metabolic process; NAS:UniProtKB. DR InterPro; IPR010394; 5-nucleotidase. DR InterPro; IPR009071; HMG-box. DR Pfam; PF06189; 5-nucleotidase; 1. KW Hydrolase; Magnesium; Nucleotide metabolism; Nucleotide-binding. FT CHAIN 1 368 Cytosolic 5'-nucleotidase 1A. FT /FTId=PRO_0000144795. FT ACT_SITE 211 211 Nucleophile (By similarity). FT CONFLICT 9 11 Missing (in Ref. 2). SQ SEQUENCE 368 AA; 41021 MW; 7FB3CCEED50BA50D CRC64; MEPGQPREPQ EPREPGPGAE TAAAPVWEEA KIFYDNLAPK KKPKSPKPQN AVTIAVSSRA LFRMDEEQQI YTEQGVEEYV RYQLEHENEP FSPGPAFPFV KALEAVNRRL RELYPDSEDV FDIVLMTNNH AQVGVRLINS INHYDLFIER FCMTGGNSPI CYLKAYHTNL YLSADAEKVR EAIDEGIAAA TIFSPSRDVV VSQSQLRVAF DGDAVLFSDE SERIVKAHGL DRFFEHEKAH ENKPLAQGPL KGFLEALGRL QKKFYSKGLR LECPIRTYLV TARSAASSGA RALKTLRSWG LETDEALFLA GAPKGPLLEK IRPHIFFDDQ MFHVAGAQEM GTVAAHVPYG VAQTPRRTAP AKQAPSAQ // ID 5NT1B_HUMAN Reviewed; 610 AA. AC Q96P26; Q8N9W3; Q8NA26; Q96DU5; Q96KE6; Q96M25; Q96SA3; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 2. DT 20-FEB-2007, entry version 33. DE Cytosolic 5'-nucleotidase 1B (EC 3.1.3.5) (Cytosolic 5'-nucleotidase DE IB) (cN1B) (cN-IB) (Autoimmune infertility-related protein). GN Name=NT5C1B; Synonyms=AIRP; ORFNames=FKSG85; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Testis; RA Setiady Y.Y., Pujianto D.A., Ekowati A.L., Harahap A., Marzuki S.; RT "Isolation of a novel human testis cDNA encoding a polypeptide related RT to autoimmune infertility."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RA Ji Y., Mitchell B.S., Spychala J.; RT "Homo sapiens cytosolic nucleotidase Ib alpha mRNA."; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 312-610. RA Wang Y.-G., Gong L.; RT "Identification and characterization of FKSG85 which encodes a RT nucleotidase protein."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 325-601, AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX MEDLINE=21548829; PubMed=11690631; DOI=10.1016/S0167-4781(01)00278-0; RA Sala-Newby G.B., Newby A.C.; RT "Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene RT related to human autoimmune infertility-related protein."; RL Biochim. Biophys. Acta 1521:12-18(2001). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides. Helps to regulate adenosine levels (By CC similarity). CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Magnesium (By similarity). CC -!- ENZYME REGULATION: Activated by ADP (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=CN-Ib alpha; CC IsoId=Q96P26-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96P26-2; Sequence=VSP_010201; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q96P26-3; Sequence=VSP_010202; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q96P26-4; Sequence=VSP_010203; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in testis, placenta and CC pancreas. Detected at lower levels in heart, kidney, liver and CC lung. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase type 3 family. CC -!- CAUTION: Ref.4 (AAK83285) sequence differs from that shown due to CC a frameshift in position 320. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF356185; AAK39108.1; ALT_INIT; mRNA. DR EMBL; AF417165; AAL11910.1; -; mRNA. DR EMBL; AK093234; BAC04103.1; ALT_INIT; mRNA. DR EMBL; AK093464; BAC04174.1; -; mRNA. DR EMBL; AK057444; BAB71489.1; -; mRNA. DR EMBL; AF352326; AAK83285.1; ALT_FRAME; mRNA. DR EMBL; AJ295254; CAC44363.1; ALT_INIT; mRNA. DR UniGene; Hs.120319; -. DR Ensembl; ENSG00000185013; Homo sapiens. DR KEGG; hsa:93034; -. DR HGNC; HGNC:17818; NT5C1B. DR MIM; 610526; gene. DR Reactome; REACT_1698.1; Nucleotide metabolism. DR ArrayExpress; Q96P26; -. DR GermOnline; ENSG00000185013; Homo sapiens. DR RZPD-ProtExp; IOH12204; -. DR RZPD-ProtExp; V1279; -. DR InterPro; IPR010394; 5-nucleotidase. DR Pfam; PF06189; 5-nucleotidase; 1. KW Alternative splicing; Hydrolase; Magnesium; Nucleotide metabolism. FT CHAIN 1 610 Cytosolic 5'-nucleotidase 1B. FT /FTId=PRO_0000144796. FT COMPBIAS 102 176 Ser-rich. FT COMPBIAS 157 201 Pro-rich. FT COMPBIAS 267 271 Poly-Gln. FT ACT_SITE 467 467 Nucleophile (By similarity). FT VAR_SEQ 1 208 Missing (in isoform 3). FT /FTId=VSP_010202. FT VAR_SEQ 41 100 Missing (in isoform 2). FT /FTId=VSP_010201. FT VAR_SEQ 596 610 LGSIAAYGFNKKFSS -> KSLGWMS (in isoform FT 4). FT /FTId=VSP_010203. FT CONFLICT 173 173 G -> R (in Ref. 2). FT CONFLICT 287 287 R -> K (in Ref. 1). FT CONFLICT 297 297 S -> W (in Ref. 1). FT CONFLICT 351 351 P -> Q (in Ref. 2). FT CONFLICT 362 362 V -> I (in Ref. 3; BAC04174). FT CONFLICT 528 528 L -> P (in Ref. 5). FT CONFLICT 552 552 L -> F (in Ref. 1). SQ SEQUENCE 610 AA; 68804 MW; EEC0BE9E5498B3E9 CRC64; MSQTSLKQKK NEPGMRSSKE SLEAEKRKES DKTGVRLSNQ MRRAVNPNHS LRCCPFQGHS SCRRCLCAAE GTALGPCHTI RIYIHMCLLW EQGQQITMMR GSQESSLRKT DSRGYLVRSQ WSRISRSPST KAPSIDEPRS RNTSAKLPSS STSSRTPSTS PSLHDSSPPP LSGQPSLQPP ASPQLPRSLD SRPPTPPEPD PGSRRSTKMQ ENPEAWAQGI VREIRQTRDS QPLEYSRTSP TEWKSSSQRR GIYPASTQLD RNSLSEQQQQ QREDEDDYEA AYWASMRSFY EKNPSCSRPW PPKPKNAITI ALSSCALFNM VDGRKIYEQE GLEKYMEYQL TNENVILTPG PAFRFVKALQ YVNARLRDLY PDEQDLFDIV LMTNNHAQVG VRLINSVNHY GLLIDRFCLT GGKDPIGYLK AYLTNLYIAA DSEKVQEAIQ EGIASATMFD GAKDMAYCDT QLRVAFDGDA VLFSDESEHF TKEHGLDKFF QYDTLCESKP LAQGPLKGFL EDLGRLQKKF YAKNERLLCP IRTYLVTARS AASSGARVLK TLRRWGLEID EALFLAGAPK SPILVKIRPH IFFDDHMFHI EGAQRLGSIA AYGFNKKFSS // ID 5NT1B_MOUSE Reviewed; 573 AA. AC Q91YE9; Q91Y48; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 06-FEB-2007, entry version 32. DE Cytosolic 5'-nucleotidase 1B (EC 3.1.3.5) (Cytosolic 5'-nucleotidase DE IB) (cN1B) (cN-IB) (Autoimmune infertility-related protein). GN Name=Nt5c1b; Synonyms=Airp; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE RP SPECIFICITY. RC TISSUE=Testis; RX MEDLINE=21548829; PubMed=11690631; DOI=10.1016/S0167-4781(01)00278-0; RA Sala-Newby G.B., Newby A.C.; RT "Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene RT related to human autoimmune infertility-related protein."; RL Biochim. Biophys. Acta 1521:12-18(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=CD-1; TISSUE=Testis; RA Setiady Y.Y., Pujianto D.A., Ekowati A.L., Harahap A., Marzuki S.; RT "Isolation of a novel human testis cDNA encoding a polypeptide related RT to autoimmune infertility."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides. Helps to regulate adenosine levels. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Magnesium. CC -!- ENZYME REGULATION: Activated by ADP. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q91YE9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q91YE9-2; Sequence=VSP_010204, VSP_010205; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in testis and brain. Detected CC at lower levels in skeletal muscle, heart and kidney. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase type 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; AJ295253; CAC44364.1; -; mRNA. DR EMBL; AF356186; AAK39109.1; ALT_INIT; mRNA. DR UniGene; Mm.272843; -. DR Ensembl; ENSMUSG00000020622; Mus musculus. DR KEGG; mmu:70881; -. DR MGI; MGI:1918131; Nt5c1b. DR ArrayExpress; Q91YE9; -. DR GermOnline; ENSMUSG00000020622; Mus musculus. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:MGI. DR GO; GO:0009116; P:nucleoside metabolic process; IDA:MGI. DR InterPro; IPR010394; 5-nucleotidase. DR Pfam; PF06189; 5-nucleotidase; 1. KW Alternative splicing; Hydrolase; Magnesium; Nucleotide metabolism. FT CHAIN 1 573 Cytosolic 5'-nucleotidase 1B. FT /FTId=PRO_0000144797. FT ACT_SITE 428 428 Nucleophile (By similarity). FT VAR_SEQ 88 89 Missing (in isoform 2). FT /FTId=VSP_010204. FT VAR_SEQ 247 262 Missing (in isoform 2). FT /FTId=VSP_010205. FT CONFLICT 103 103 S -> F (in Ref. 2). FT CONFLICT 162 162 V -> A (in Ref. 2). FT CONFLICT 185 185 Q -> E (in Ref. 2). FT CONFLICT 228 228 H -> Q (in Ref. 2). SQ SEQUENCE 573 AA; 65026 MW; 9A7F3094DC8E8480 CRC64; MSQTSLKHKK KNEPGMRYSK ESLDAEKRKD SDKTGARLST QGSQELPLHN TDSRGYVVRN QWSRTSRSPS TGAPSVDEPR SRNTAIKVEA PNSSTTSRTS SASPSQHETS PPPQTSEKSS TQQTPQNRPI TQLESQPPTP PETEPNSRRT SAKMYTGSDP WVHRENREPR DLQLRDYAYS CDSRQGMPKT REYPRTPPTE WKPYAQRRLQ YGTSVDMEPE YISDGPQHRQ RQQTEEDEVD EAYWTSVSML YEKIPSCARP RPPKPKHAIT IAVSSRALFN MVDDRKIYEE EGLEKYMEYQ LTNENVILTP GPAFRFVKAL QHVNSRLRDL YPDEQDLFDI VLMTNNHAQV GVRLINSVNH YGLLIDRFCL TGGKSPIGYL KAYLTNLYLS ADSEKVQEAI KEGIASATMY AGAKDMAYCD TQLRVAFDGD AVLFSDESEH IAKDHGLDKF FQHETLFENK PLAQGPLKSF LEDLGKLQKK FYAKDERLLC PIRTYLVTAR SAASSGARVL KTLRRWGLEI DEALFLAGAP KGPILVKIRP HIFFDDQMFH IESAQKFGTI TAHVPYGIAQ KRN // ID 5NT3_CHICK Reviewed; 331 AA. AC Q5ZID6; Q802T3; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 3. DT 06-FEB-2007, entry version 18. DE Cytosolic 5'-nucleotidase III (EC 3.1.3.5) (cN-III) (Pyrimidine 5'- DE nucleotidase 1) (P5'N-1) (P5N-1) (PN-I). GN Name=NT5C3; Synonyms=PYN1; ORFNames=RCJMB04_27l2; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 46-85; RP 150-158; 220-243 AND 291-290, DEVELOPMENTAL STAGE, AND INDUCTION. RX MEDLINE=22984711; PubMed=12907448; DOI=10.1182/blood-2002-11-3388; RA Mass M., Simo E., Dragon S.; RT "Erythroid pyrimidine 5'-nucleotidase: cloning, developmental RT expression, and regulation by cAMP and in vivo hypoxia."; RL Blood 102:4198-4205(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Blood; RA Mass M., Dragon S.; RT "Cloning and gene expression of pyrimidine 5'-nucleotidase in chick RT embryonic erythrocytes."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., RA Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., RA Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005). CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; CC IsoId=Q5ZID6-3; Sequence=Displayed; CC Name=1; CC IsoId=Q5ZID6-1; Sequence=VSP_021564; CC -!- DEVELOPMENTAL STAGE: Expressed at lower until E13 and the CC expression rises transiently between E13 and E16. CC -!- INDUCTION: By norepinephrine/NE and adenosine which are released CC by the embryo under hyposic conditions. By stimulation of beta- CC adrenergic/adenosine receptors in definitive red blood cells CC (RBC). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF548635; AAQ12342.1; -; mRNA. DR EMBL; AJ496195; CAD42712.1; -; mRNA. DR EMBL; AJ720848; CAG32507.1; -; mRNA. DR UniGene; Gga.5031; -. DR SMR; Q5ZID6; 1-285. DR Ensembl; ENSGALG00000012192; Gallus gallus. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0008665; F:2'-phosphotransferase activity; ISS:UniProtKB. DR GO; GO:0008253; F:5'-nucleotidase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; ISS:UniProtKB. KW Alternative splicing; Direct protein sequencing; Hydrolase; KW Nucleotide metabolism; Nucleotide-binding. FT CHAIN 1 331 Cytosolic 5'-nucleotidase III. FT /FTId=PRO_0000064386. FT VAR_SEQ 1 46 Missing (in isoform 1). FT /FTId=VSP_021564. SQ SEQUENCE 331 AA; 37370 MW; 7AE5CFE0F280224A CRC64; MDRAAVAKMG AVASASVCAL VGGVVLAQYI FTMKKKTGRK TKIIEMMPEF QKKTVHIKDP GRVEEIICGL IKGGAAKLQI ITDFDMTLSR FSYNGKRCPT CHNIIDNSKL ITEECRKKLL QLKETYYAIE IDPALTIEEK YPYMVEWYNK SHALLIEQGL QKDKLAEVVR ESDVMLKEGY ENFFDKLSEH NIPVFIFSAG IGDILEEVIH QAGVYHSNVK VVSNFMDFDE NGILKGFKGE LIHVYNKHDG ALKNTEYFKQ LKDNSNIILL GDSQGDLSMA DGVANVEHIL KIGYLNDKVD ELLEKYMDSY DIVLVKDESL EVANSILQKI L // ID 5NT3_HUMAN Reviewed; 336 AA. AC Q9H0P0; Q6IPZ1; Q6NXS6; Q7L3G6; Q9P0P5; Q9UC42; Q9UC43; Q9UC44; AC Q9UC45; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 3. DT 20-FEB-2007, entry version 43. DE Cytosolic 5'-nucleotidase III (EC 3.1.3.5) (cN-III) (Pyrimidine 5'- DE nucleotidase 1) (P5'N-1) (P5N-1) (PN-I) (Uridine 5'-monophosphate DE hydrolase 1) (p36). GN Name=NT5C3; Synonyms=P5N1, UMPH1; ORFNames=HSPC233; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Placenta; RX MEDLINE=20400029; PubMed=10942414; RA Amici A., Emanuelli M., Raffaelli N., Ruggieri S., Saccucci F., RA Magni G.; RT "Human erythrocyte pyrimidine 5'-nucleotidase, PN-I, is identical to RT p36, a protein associated to lupus inclusion formation in response to RT alpha-interferon."; RL Blood 96:1596-1598(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND RP VARIANT P5N DEFICIENCY VAL-137. RX PubMed=11369620; DOI=10.1182/blood.V97.11.3327; RA Marinaki A.M., Escuredo E., Duley J.A., Simmonds H.A., Amici A., RA Naponelli V., Magni G., Seip M., Ben-Bassat I., Harley E.H., RA Thein S.L., Rees D.C.; RT "Genetic basis of hemolytic anemia caused by pyrimidine 5' RT nucleotidase deficiency."; RL Blood 97:3327-3332(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, VARIANTS RP P5N DEFICIENCY PRO-181 AND ARG-280, AND CHARACTERIZATION OF VARIANTS RP P5N DEFICIENCY PRO-181 AND ARG-280. RX PubMed=15238149; DOI=10.1111/j.1365-2141.2004.05029.x; RA Kanno H., Takizawa T., Miwa S., Fujii H.; RT "Molecular basis of Japanese variants of pyrimidine 5'-nucleotidase RT deficiency."; RL Br. J. Haematol. 126:265-271(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Kidney; RX MEDLINE=21154917; PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, Lung, Muscle, and Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-336 (ISOFORM 2). RC TISSUE=Umbilical cord blood; RX MEDLINE=20499367; PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). RN [8] RP PROTEIN SEQUENCE OF 83-95; 131-147; 226-240; 268-296 AND 311-329, RP INDUCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=96132854; PubMed=8557639; DOI=10.1074/jbc.271.20.11595; RA Rich S.A., Bose M., Tempst P., Rudofsky U.H.; RT "Purification, microsequencing, and immunolocalization of p36, a new RT interferon-alpha-induced protein that is associated with human lupus RT inclusions."; RL J. Biol. Chem. 271:1118-1126(1996). RN [9] RP VARIANT P5N DEFICIENCY SER-229. RX PubMed=12930399; DOI=10.1046/j.1365-2141.2003.04532.x; RA Bianchi P., Fermo E., Alfinito F., Vercellati C., Baserga M., RA Ferraro F., Guzzo I., Rotoli B., Zanella A.; RT "Molecular characterization of six unrelated Italian patients affected RT by pyrimidine 5'-nucleotidase deficiency."; RL Br. J. Haematol. 122:847-851(2003). CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Isoform 2: CC Endoplasmic reticulum. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=2; CC IsoId=Q9H0P0-4; Sequence=Displayed; CC Name=1; CC IsoId=Q9H0P0-1; Sequence=VSP_021565; CC Name=3; CC IsoId=Q9H0P0-2; Sequence=VSP_015623; CC Name=4; Synonyms=P5N-R; CC IsoId=Q9H0P0-3; Sequence=VSP_015624; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in CC reticulocytes and lymphocytes. Isoform 4 is expressed only in CC reticulocytes. CC -!- INDUCTION: Isoform 2 is induced by interferon alpha in Raji cells CC in association with lupus inclusions. CC -!- DISEASE: Defects in NT5C3 are the cause of P5N deficiency CC [MIM:266120]; also called hemolytic anemia due to P5N deficiency CC or hemolytic anemia due to UMPH1 deficiency. P5N deficiency is an CC autosomal recessive condition causing hemolytic anemia CC characterized by marked basophilic stipplig and the accumulation CC of high concentrations of pyrimidine nucleotides within the CC erythrocyte. It is implicated in the anemia of lead poisoning and CC is possibly associated with learning difficulties. CC -!- CAUTION: Ref.1 (AAG33630) sequence differs from that shown due to CC several frameshifts. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF312735; AAG33630.1; ALT_SEQ; mRNA. DR EMBL; AL136716; CAB66650.1; -; mRNA. DR EMBL; CR533518; CAG38549.1; -; mRNA. DR EMBL; BC013292; AAH13292.2; -; mRNA. DR EMBL; BC015856; AAH15856.2; -; mRNA. DR EMBL; BC066914; AAH66914.1; -; mRNA. DR EMBL; BC071652; AAH71652.2; -; mRNA. DR EMBL; AF151067; AAF36153.1; ALT_INIT; mRNA. DR UniGene; Hs.487933; -. DR PDB; 2CN1; X-ray; A=-. DR SMR; Q9H0P0; 7-297. DR Ensembl; ENSG00000122643; Homo sapiens. DR HGNC; HGNC:17820; NT5C3. DR MIM; 266120; phenotype. DR MIM; 606224; gene. DR ArrayExpress; Q9H0P0; -. DR GermOnline; ENSG00000122643; Homo sapiens. DR RZPD-ProtExp; IOH12353; -. DR RZPD-ProtExp; RZPDo834C1119; -. DR RZPD-ProtExp; RZPDo839F1075; -. DR RZPD-ProtExp; T0827; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0008665; F:2'-phosphotransferase activity; TAS:UniProtKB. DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB. DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; NAS:UniProtKB. KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disease mutation; Hydrolase; Nucleotide metabolism; KW Nucleotide-binding. FT CHAIN 1 336 Cytosolic 5'-nucleotidase III. FT /FTId=PRO_0000064387. FT VAR_SEQ 1 51 Missing (in isoform 4). FT /FTId=VSP_015624. FT VAR_SEQ 1 50 MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRK FT TGRKTKIIE -> MTNQESAVHVK (in isoform 1). FT /FTId=VSP_021565. FT VAR_SEQ 1 50 Missing (in isoform 3). FT /FTId=VSP_015623. FT VARIANT 137 137 D -> V (in P5N deficiency). FT /FTId=VAR_023511. FT VARIANT 181 181 L -> P (in P5N deficiency; markedly FT decreases activity). FT /FTId=VAR_023512. FT VARIANT 229 229 N -> S (in P5N deficiency). FT /FTId=VAR_023513. FT VARIANT 280 280 G -> R (in P5N deficiency; markedly FT decreases activity). FT /FTId=VAR_023514. FT CONFLICT 95 95 R -> K (in Ref. 8). FT CONFLICT 144 144 E -> Q (in Ref. 8). FT CONFLICT 329 329 N -> R (in Ref. 8). SQ SEQUENCE 336 AA; 37948 MW; C5D75CCF1BB61021 CRC64; MRAPSMDRAA VARVGAVASA SVCALVAGVV LAQYIFTLKR KTGRKTKIIE MMPEFQKSSV RIKNPTRVEE IICGLIKGGA AKLQIITDFD MTLSRFSYKG KRCPTCHNII DNCKLVTDEC RKKLLQLKEK YYAIEVDPVL TVEEKYPYMV EWYTKSHGLL VQQALPKAKL KEIVAESDVM LKEGYENFFD KLQQHSIPVF IFSAGIGDVL EEVIRQAGVY HPNVKVVSNF MDFDETGVLK GFKGELIHVF NKHDGALRNT EYFNQLKDNS NIILLGDSQG DLRMADGVAN VEHILKIGYL NDRVDELLEK YMDSYDIVLV QDESLEVANS ILQKIL // ID 5NT3_MOUSE Reviewed; 331 AA. AC Q9D020; Q8CI05; Q9D0D9; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 4. DT 20-FEB-2007, entry version 39. DE Cytosolic 5'-nucleotidase III (EC 3.1.3.5) (cN-III) (Pyrimidine 5'- DE nucleotidase 1) (P5'N-1) (P5N-1) (PN-I) (Lupin). GN Name=Nt5c3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=11180800; DOI=10.1007/s004270000093; RA Lu M.M., Chen F., Gitler A., Li J., Jin F., Ma X.K., Epstein J.A.; RT "Cloning and expression analysis of murine lupin, a member of a novel RT gene family that is conserved through evolution and associated with RT Lupus inclusions."; RL Dev. Genes Evol. 210:512-517(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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] (ISOFORM 1). 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 X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) (ISOFORM 1). RG Center for eukaryotic structural genomics (CESG); RT "X-ray structure of a cytosolic 5'-nucleotidase III from Mus musculus RT MM.158936."; RL Submitted (NOV-2006) to the PDB data bank. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; CC IsoId=Q9D020-3; Sequence=Displayed; CC Name=1; CC IsoId=Q9D020-1; Sequence=VSP_021566; CC -!- TISSUE SPECIFICITY: Isoform 2 is highly expressed in the brain, CC heart, spleen, kidney and blood. Isoform 2 is expressed (at CC protein level) in the spleen, skeletal muscle and gastrointestinal CC epithelia. CC -!- DEVELOPMENTAL STAGE: Isoform 2 is weakly expressed from E7.5 and CC the expression level steadily increased through gestation. At E9.5 CC and E10.5 is first detected colocalizing with embryonic blood CC cells within the region of the septum transversum and within the CC cardiac chambers and dorsal aorta. At E12.5 expression is found in CC the ventral neural tube and in the trigeminal ganglia and in the CC liver and dorsal root ganglia. Expression persisted in the liver, CC dorsal root and trigeminal ganglia at E13.5 and weaker expression CC becomes apparent in cardiac and skeletal muscle. At E16.5 CC expression is detected in liver, myocardium, tongue, bronchial CC epithelium, gastrointestinal epithelium, cartilage and forebrain CC neuroepithelium. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK011525; BAB27677.2; -; mRNA. DR EMBL; AK011894; BAB27901.2; -; mRNA. DR EMBL; BC038029; AAH38029.1; -; mRNA. DR UniGene; Mm.158936; -. DR PDB; 2BDU; X-ray; A/B=2-297. DR PDB; 2G06; X-ray; A/B=2-297. DR PDB; 2G07; X-ray; A/B=2-297. DR PDB; 2G08; X-ray; A/B=2-297. DR PDB; 2G09; X-ray; A/B=2-297. DR PDB; 2G0A; X-ray; A/B=2-297. DR Ensembl; ENSMUSG00000029780; Mus musculus. DR MGI; MGI:1927186; Nt5c3. DR ArrayExpress; Q9D020; -. DR GermOnline; ENSMUSG00000029780; Mus musculus. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0008665; F:2'-phosphotransferase activity; ISS:UniProtKB. DR GO; GO:0008253; F:5'-nucleotidase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; ISS:UniProtKB. KW 3D-structure; Alternative splicing; Hydrolase; Nucleotide metabolism; KW Nucleotide-binding. FT CHAIN 1 331 Cytosolic 5'-nucleotidase III. FT /FTId=PRO_0000064388. FT VAR_SEQ 1 45 MDRAAVARVGAVASASVCAVVAGVVLAQYIFTLKRKTGRKT FT KIIE -> MTNQESAVHLK (in isoform 1). FT /FTId=VSP_021566. FT CONFLICT 183 183 F -> L (in Ref. 2; BAB27677). FT CONFLICT 260 260 Q -> R (in Ref. 2; BAB27901). FT HELIX 10 12 FT HELIX 14 17 FT TURN 19 20 FT HELIX 26 39 FT TURN 40 40 FT HELIX 41 43 FT STRAND 44 48 FT TURN 51 53 FT STRAND 57 59 FT TURN 60 61 FT HELIX 67 72 FT TURN 73 73 FT TURN 75 76 FT HELIX 79 96 FT TURN 97 97 FT STRAND 99 101 FT HELIX 103 124 FT HELIX 128 130 FT HELIX 131 137 FT TURN 145 145 FT HELIX 146 156 FT TURN 157 157 FT STRAND 160 167 FT HELIX 168 177 FT TURN 178 179 FT TURN 183 184 FT STRAND 185 190 FT STRAND 192 194 FT TURN 196 197 FT STRAND 198 203 FT TURN 210 211 FT HELIX 213 218 FT TURN 219 220 FT HELIX 221 226 FT TURN 227 229 FT STRAND 232 240 FT HELIX 241 244 FT TURN 245 248 FT STRAND 253 261 FT HELIX 265 275 FT STRAND 276 281 FT TURN 282 282 FT HELIX 287 296 SQ SEQUENCE 331 AA; 37252 MW; 9BE4CA16863E1E0F CRC64; MDRAAVARVG AVASASVCAV VAGVVLAQYI FTLKRKTGRK TKIIEMMPEF QKSSVRIKNP TRVEEIICGL IKGGAAKLQI ITDFDMTLSR FSYNGKRCPT CHNIIDNCKL VTDECRRKLL QLKEQYYAIE VDPVLTVEEK FPYMVEWYTK SHGLLIEQGI PKAKLKEIVA DSDVMLKEGY ENFFGKLQQH GIPVFIFSAG IGDVLEEVIR QAGVYHSNVK VVSNFMDFDE NGVLKGFKGE LIHVFNKHDG ALKNTDYFSQ LKDNSNIILL GDSQGDLRMA DGVANVEHIL KIGYLNDRVD ELLEKYMDSY DIVLVKEESL EVVNSILQKT L // ID 5NTC_HUMAN Reviewed; 561 AA. AC P49902; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 06-FEB-2007, entry version 56. DE Cytosolic purine 5'-nucleotidase (EC 3.1.3.5) (5'-nucleotidase DE cytosolic II). GN Name=NT5C2; Synonyms=NT5B, NT5CP, PNT5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX MEDLINE=95091838; PubMed=7999131; RA Oka J., Matsumoto A., Hosokawa Y., Inoue S.; RT "Molecular cloning of human cytosolic purine 5'-nucleotidase."; RL Biochem. Biophys. Res. Commun. 205:917-922(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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 a critical role in the maintenance of a CC constant composition of intracellular purine/pyrimidine CC nucleotides in cooperation with other nucleotidases. CC Preferentially hydrolyzes inosine 5-prime-monophosphate (IMP) and CC other purine nucleotides. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- ENZYME REGULATION: Allosterically activated by various compounds, CC including ATP. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DISEASE: Aberration of this enzyme may be related to the urate CC production in hyperuricemia and gout. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D38524; BAA07529.1; -; mRNA. DR EMBL; BC001595; AAH01595.1; -; mRNA. DR PIR; JC2436; JC2436. DR UniGene; Hs.591920; -. DR PDB; 2J2C; X-ray; A=1-536. DR Ensembl; ENSG00000076685; Homo sapiens. DR KEGG; hsa:22978; -. DR H-InvDB; HIX0009172; -. DR HGNC; HGNC:8022; NT5C2. DR MIM; 600417; gene. DR Reactome; REACT_1698.1; Nucleotide metabolism. DR DrugBank; APRD00081; Ribavirin. DR LinkHub; P49902; -. DR ArrayExpress; P49902; -. DR GermOnline; ENSG00000076685; Homo sapiens. DR GO; GO:0008253; F:5'-nucleotidase activity; TAS:ProtInc. DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl. DR InterPro; IPR009060; UBA_like. DR PANTHER; PTHR12103; HAD-IG-Ncltidse; 1. DR Pfam; PF05761; 5_nucleotid; 1. DR TIGRFAMs; TIGR02244; HAD-IG-Ncltidse; 1. KW 3D-structure; Allosteric enzyme; Hydrolase; Polymorphism. FT CHAIN 1 561 Cytosolic purine 5'-nucleotidase. FT /FTId=PRO_0000064389. FT COMPBIAS 549 561 Asp/Glu-rich (acidic). FT VARIANT 3 3 T -> A (in dbSNP:rs10883841). FT /FTId=VAR_024244. FT VARIANT 136 136 Q -> R (in dbSNP:rs12262171). FT /FTId=VAR_030242. SQ SEQUENCE 561 AA; 64970 MW; 4C27D762575E0EA2 CRC64; MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA PQEITHCHDE DDDEEEEEEE E // ID 5NTD_BOOMI Reviewed; 580 AA. AC P52307; P90696; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 28-NOV-2006, entry version 52. DE Protein 5NUC precursor [Includes: UDP-sugar hydrolase (EC 3.6.1.45) DE (UDP-sugar diphosphatase) (UDP-sugar pyrophosphatase); 5'-nucleotidase DE (EC 3.1.3.5) (5'-NT)] (Fragment). OS Boophilus microplus (Cattle tick). OC Eukaryota; Metazoa; Arthropoda; Chelicerata; Arachnida; Acari; OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Boophilus. OX NCBI_TaxID=6941; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=99306777; PubMed=10380109; RA Liyou N., Hamilton S., Elvin C., Willadsen P.; RT "Cloning and expression of ecto 5-nucleotidase from the cattle tick RT Boophilus microplus."; RL Insect Mol. Biol. 8:257-266(1999). RN [2] RP PROTEIN SEQUENCE OF 15-40 AND 162-180. RX MEDLINE=93250870; PubMed=8387372; DOI=10.1016/0965-1748(93)90010-P; RA Willadsen P., Riding G.A., Jarmey J., Atkins A.; RT "The nucleotidase of Boophilus microplus and its relationship to RT enzymes from the rat and Escherichia coli."; RL Insect Biochem. Mol. Biol. 23:291-295(1993). CC -!- FUNCTION: Degradation of external UDP-glucose to uridine CC monophosphate and glucose-1-phosphate, which can then be used by CC the cell. CC -!- CATALYTIC ACTIVITY: UDP-sugar + H(2)O = UMP + alpha-D-aldose 1- CC phosphate. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Zinc. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor. CC -!- TISSUE SPECIFICITY: Gut, ovaries and salivary glands. CC -!- PTM: Glycosylated. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U80634; AAB38963.1; -; mRNA. DR HSSP; P07024; 2USH. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EC. DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IEA:EC. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR PANTHER; PTHR11575; 5_nucleotidase; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; FALSE_NEG. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. KW Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase; KW Lipoprotein; Membrane; Metal-binding; Nucleotide-binding; Signal; KW Zinc. FT SIGNAL <1 14 FT CHAIN 15 555 Protein 5NUC. FT /FTId=PRO_0000000021. FT PROPEP 556 580 Removed in mature form (Potential). FT /FTId=PRO_0000000022. FT REGION 502 508 Substrate binding (By similarity). FT METAL 26 26 Zinc 1 (By similarity). FT METAL 28 28 Zinc 1 (By similarity). FT METAL 79 79 Zinc 1 (By similarity). FT METAL 79 79 Zinc 2 (By similarity). FT METAL 111 111 Zinc 2 (By similarity). FT METAL 212 212 Zinc 2 (By similarity). FT METAL 235 235 Zinc 2 (By similarity). FT BINDING 415 415 Substrate (By similarity). FT SITE 112 112 Transition state stabilizer (By FT similarity). FT SITE 115 115 Transition state stabilizer (By FT similarity). FT LIPID 555 555 GPI-anchor amidated asparagine FT (Potential). FT CARBOHYD 172 172 N-linked (GlcNAc...) (Probable). FT CARBOHYD 285 285 N-linked (GlcNAc...) (Potential). FT CARBOHYD 423 423 N-linked (GlcNAc...) (Potential). FT CARBOHYD 536 536 N-linked (GlcNAc...) (Potential). FT CONFLICT 15 15 T -> K (in Ref. 2). FT CONFLICT 37 39 SGT -> HXG (in Ref. 2). FT NON_TER 1 1 SQ SEQUENCE 580 AA; 63460 MW; 588EEF2014071AB7 CRC64; GRLLACLLLP GLAATDFTAT VLHTNDVHGR FEQITASGTR CTKQAAEAQQ CVGGIARQKT VVSQAAASGA NVLFLNAGDY YQGSIWYYVL GAPIVAEAVN YLAHDAMALG NHEFDRGAEG LVPLLTESRV PIVGCNVDFS EEPTLKPLQP KPSVVVERAG IKIGLIGYTT MNTTYLSSPG KVRFTDEAEC IQREAQRLRR EEGVQVIIAV GHSGVPRDLE ICERVPEVSL VVGGHTHTFL YSGPTENGRV SGDKPQGPYP IVVDRAADSR CLVVQDFYMG KYMGNISITW NQRGEVVRWS GQPVLLDRSI PEDPDGIALL DRYRDRVAQS QASVVAESKV LLDGDKNRCR LDECNLGNLV MDAFLKKMAS LPSPQASWTR VAAVIANAGG IRASIDEQST GGRITFEDVV NVLPFGNTLV EMNVTGAQLK GLLEHGVHRH DVKGYVPPAE LVLAAGLRVV YDIQREPYDR VVEAHILCTE CRVPRYEPLE YARQYRIAAL SYIVHGGDNF DFSFVKPKDM YDTGFQDAEI VMKYMNSTSP ITTALDGRVT FLKTNQASDA CLNLASPFLV LLVLVVFYHL // ID 5NTD_BOVIN Reviewed; 574 AA. AC Q05927; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 20-FEB-2007, entry version 61. DE 5'-nucleotidase precursor (EC 3.1.3.5) (Ecto-5'-nucleotidase) (5'-NT) DE (CD73 antigen). GN Name=NT5E; Synonyms=NT5, NTE; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX MEDLINE=93340109; PubMed=8340354; RA Suzuki K., Furukawa Y., Tamura H., Ejiri N., Suematsu H., Taguchi R., RA Nakamura S., Suzuki Y., Ikezawa H.; RT "Purification and cDNA cloning of bovine liver 5'-nucleotidase, a GPI- RT anchored protein, and its expression in COS cells."; RL J. Biochem. 113:607-613(1993). CC -!- FUNCTION: Hydrolyzes extracellular nucleotides into membrane CC permeable nucleosides. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Zinc. CC -!- SUBUNIT: Homodimer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D14541; BAA03408.1; -; mRNA. DR EMBL; S64302; AAB27698.1; -; mRNA. DR PIR; JX0269; JX0269. DR UniGene; Bt.57034; -. DR HSSP; P07024; 2USH. DR KEGG; bta:281363; -. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EC. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR PANTHER; PTHR11575; 5_nucleotidase; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. KW Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase; KW Lipoprotein; Membrane; Metal-binding; Nucleotide-binding; Signal; KW Zinc. FT SIGNAL 1 26 FT CHAIN 27 549 5'-nucleotidase. FT /FTId=PRO_0000000013. FT PROPEP 550 574 Removed in mature form (By similarity). FT /FTId=PRO_0000000014. FT REGION 500 506 Substrate binding (By similarity). FT METAL 36 36 Zinc 1 (By similarity). FT METAL 38 38 Zinc 1 (By similarity). FT METAL 85 85 Zinc 1 (By similarity). FT METAL 85 85 Zinc 2 (By similarity). FT METAL 117 117 Zinc 2 (By similarity). FT METAL 220 220 Zinc 2 (By similarity). FT METAL 243 243 Zinc 2 (By similarity). FT BINDING 417 417 Substrate (By similarity). FT SITE 118 118 Transition state stabilizer (By FT similarity). FT SITE 121 121 Transition state stabilizer (By FT similarity). FT LIPID 549 549 GPI-anchor amidated serine (By FT similarity). FT CARBOHYD 53 53 N-linked (GlcNAc...) (Potential). FT CARBOHYD 311 311 N-linked (GlcNAc...) (Potential). FT CARBOHYD 333 333 N-linked (GlcNAc...) (Potential). FT CARBOHYD 403 403 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 574 AA; 63085 MW; 6DABF54A18FDB338 CRC64; MNPGAARTPA LRILPLGALL WPAARPWELT ILHTNDVHSR LEQTSEDSSK CVNASRCVGG VARLATKVHQ IRRAEPHVLL LDAGDQYQGT IWFTVYKGTE VAHFMNALGY ESMALGNHEF DNGVEGLIDP LLKEVNFPIL SANIKAKGPL ASKISGLYSP YKILTVGDEV VGIVGYTSKE TPFLSNPGTN LVFEDEITAL QPEVDKLKTL NVNKIIALGH SGFEVDKLIA QKVKGVDVVV GGHSNTFLYT GNPPSKEVPA GQYPFIVTSD DGRKVPVVQA YAFGKYLGYL KVEFDEKGNV VTSHGNPILL NSSIPEDPNI KADINKWRVK LDNYSTQELG KTIVYLDGTA QSCRFRECNM GNLICDAMIN NNLRHPDEMS WNHVSMCILN GGGIRSPIDE RNNGTITWEN LAAVLPFGGT FDLVQLKGST LKKAFDDTVH RYGQRTGEFL QVGGIHVVYD ISRNPGDRVV KLEVLCTQCR VPSYEPLRMD KVYKVILPSF LVSGGDGFQM IKDEKIKHDS GDQDINVVSG YISKMKVLYP AVEGRIQFSA GSHCCGSFSL IFLSVLAVII ILYQ // ID 5NTD_DISOM Reviewed; 577 AA. AC P29240; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 28-NOV-2006, entry version 49. DE 5'-nucleotidase precursor (EC 3.1.3.5) (Ecto-nucleotidase). OS Discopyge ommata (Electric ray). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Squalea; Hypnosqualea; Pristiorajea; Batoidea; OC Torpediniformes; Narcinoidei; Narcinidae; Discopyge. OX NCBI_TaxID=7785; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Electric lobe; RX MEDLINE=92111535; PubMed=1765099; RA Volknandt W., Vogel M., Pevsner J., Misumi Y., Ikehara Y., RA Zimmermann H.; RT "5'-nucleotidase from the electric ray electric lobe. Primary RT structure and relation to mammalian and procaryotic enzymes."; RL Eur. J. Biochem. 202:855-861(1991). CC -!- FUNCTION: Hydrolyzes extracellular nucleotides into membrane CC permeable nucleosides. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Zinc. CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X62278; CAA44168.1; -; mRNA. DR PIR; S19564; S19564. DR HSSP; P07024; 2USH. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EC. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR PANTHER; PTHR11575; 5_nucleotidase; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; KW Metal-binding; Nucleotide-binding; Signal; Zinc. FT SIGNAL 1 30 FT CHAIN 31 552 5'-nucleotidase. FT /FTId=PRO_0000000024. FT PROPEP 553 577 Removed in mature form. FT /FTId=PRO_0000000025. FT REGION 500 506 Substrate binding (By similarity). FT METAL 39 39 Zinc 1 (By similarity). FT METAL 41 41 Zinc 1 (By similarity). FT METAL 86 86 Zinc 1 (By similarity). FT METAL 86 86 Zinc 2 (By similarity). FT METAL 118 118 Zinc 2 (By similarity). FT METAL 221 221 Zinc 2 (By similarity). FT METAL 244 244 Zinc 2 (By similarity). FT BINDING 417 417 Substrate (By similarity). FT SITE 119 119 Transition state stabilizer (By FT similarity). FT SITE 122 122 Transition state stabilizer (By FT similarity). FT LIPID 552 552 GPI-anchor amidated serine (By FT similarity). FT CARBOHYD 135 135 N-linked (GlcNAc...) (Potential). FT CARBOHYD 311 311 N-linked (GlcNAc...) (Potential). FT CARBOHYD 347 347 N-linked (GlcNAc...) (Potential). FT CARBOHYD 403 403 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 577 AA; 63613 MW; 3B52535C2F70C0DB CRC64; MPRVPSASAT GSSALLSLLC AFSLGRAAPF QLTILHTNDV HARVEETNQD SGKCFTQSFA GVARRWTKIE ELRARDKNVL LLDAGDQYQG TIWFNYYKGA EAAHFIEAVG YNAMALGNHE FDNGAEGLLD PFLLNVSFPV LSANLEQGED QVPSLIGYYK PSTVLDVNGE KIGVVGYTSK ETPTLSSPGP HLIFKDEIQA VQHEVDILVS QGIDKIIALG HSGFETDKLI AQKVRGVDVV VGGHSNTFLY TGKAPSNDVP VGPYPFLVNS DDQRTIPVVQ AYAYGKYLGY LKLTFDKGEV IKREGNPILL NSSIIQDPVL LAEVNKWKES LANFGKEVIG RTVVYLNGTT EECRNRECNM GNLICDAMIQ QNIRNPDEKF WNHVSICIFQ GGGIRAPINE QNNGTIQVDS LLAVLPFGST IDLLEVYGST LRAAFDHSVR RYGQNTGEFL QVSGIQVQFN LKRPPGSRVV KIDVLCADCR VPHYQPLLDN KIYKIVTNSY IAEGGDGFTM LKNERLRYDT GSTDISVVSS YIKQMKVVYP AVEGRILFVE NSATLPIINL KIGLSLFAFL TWFLHCS // ID 5NTD_HAEIN Reviewed; 603 AA. AC P44569; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 28-NOV-2006, entry version 54. DE Probable 5'-nucleotidase precursor (EC 3.1.3.5). GN OrderedLocusNames=HI0206; OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 26-38. RX MEDLINE=20137488; PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.3.CO;2-W; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Divalent cations (By similarity). CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21874.1; -; Genomic_DNA. DR PIR; E64054; E64054. DR HSSP; P07024; 2USH. DR GenomeReviews; L42023_GR; HI0206. DR KEGG; hin:HI0206; -. DR TIGR; HI0206; -. DR BioCyc; HINF71421:HI0206-MONOMER; -. DR BioCyc; MetaCyc:MONOMER-8341; -. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR InterPro; IPR006420; NadN. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR PANTHER; PTHR11575; 5_nucleotidase; 2. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR TIGRFAMs; TIGR01530; nadN; 1. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. KW Complete proteome; Direct protein sequencing; Hydrolase; KW Metal-binding; Nucleotide-binding; Signal. FT SIGNAL 1 25 FT CHAIN 26 603 Probable 5'-nucleotidase. FT /FTId=PRO_0000000026. FT REGION 540 546 Substrate binding (By similarity). FT METAL 44 44 Divalent metal cation 1 (By similarity). FT METAL 46 46 Divalent metal cation 1 (By similarity). FT METAL 94 94 Divalent metal cation 1 (By similarity). FT METAL 94 94 Divalent metal cation 2 (By similarity). FT METAL 126 126 Divalent metal cation 2 (By similarity). FT METAL 227 227 Divalent metal cation 2 (By similarity). FT BINDING 456 456 Substrate (By similarity). FT SITE 127 127 Transition state stabilizer (By FT similarity). FT SITE 130 130 Transition state stabilizer (By FT similarity). SQ SEQUENCE 603 AA; 66245 MW; B641C32A5A2B6AEA CRC64; MLLSKKSASF ALSAFAMLFT SVALAKEAPQ AHKAVELSIL HINDHHSYLE PHETRINLNG QQTKVDIGGF SAVNAKLNKL RKKYKNPLVL HAGDAITGTL YFTLFGGSAD AAVMNAGNFH YFTLGNHEFD AGNEGLLKLL EPLKIPVLSA NVIPDKNSIL YNKWKPYDIF TVDGEKIAII GLDTVNKTVN SSSPGKDVKF YDEIATAQIM ANALKQQGIN KIILLSHAGS EKNIEIAQKV NDIDVIVTGD SHYLYGNDEL RSLKLPVIYE YPLEFKNPNG DPVFVMEGWA YSAVVGDLGV KFSPEGIASI TRKIPHVLMS SHKLQVKNAE GKWTELTGDE RKKALDTLKS MKSISLDDHD AKTDMLISKY KSEKDRLAQE IVGVITGSAM PGGSANRIPN KAGSNPEGSI ATRFIAETMY NELKTVDLTI QNAGGVRADI LPGNVTFNDA YTFLPFGNTL YTYKMEGSLV KQVLEDAMQF ALVDGSTGAF PYGAGIRYEA NETPNAEGKR LVSVEVLNKQ TQQWEPIDDN KRYLVGTNAY VAGGKDGYKT FGKLFNDPKY EGVDTYLPDA ESFIKFMKKH PHFEAYTSSN VKFNASTDAL PKK // ID 5NTD_HUMAN Reviewed; 574 AA. AC P21589; O75520; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 06-FEB-2007, entry version 77. DE 5'-nucleotidase precursor (EC 3.1.3.5) (Ecto-5'-nucleotidase) (5'-NT) DE (CD73 antigen). GN Name=NT5E; Synonyms=NT5, NTE; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND GPI-ANCHOR RP AT SER-549. RC TISSUE=Placenta; RX MEDLINE=90361037; PubMed=2129526; RA Misumi Y., Ogata S., Ohkubo K., Hirose S., Ikehara Y.; RT "Primary structure of human placental 5'-nucleotidase and RT identification of the glycolipid anchor in the mature form."; RL Eur. J. Biochem. 191:563-569(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-113. RC TISSUE=Placenta; RX MEDLINE=96144293; PubMed=8566797; DOI=10.1016/0378-1119(95)00574-9; RA Hansen K.R., Resta R., Webb C.F., Thompson L.F.; RT "Isolation and characterization of the promoter of the human 5'- RT nucleotidase (CD73)-encoding gene."; RL Gene 167:307-312(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 359-489, AND VARIANT ALA-376. RC TISSUE=Leukocyte; RA Zanoni L., Rosi F., Pagani R., Marinello E.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 27-40. RC TISSUE=Placenta; RX MEDLINE=91058583; PubMed=2173922; RA Klemens M.R., Sherman W.R., Holmberg N.J., Ruedi J.M., Low M.G., RA Thompson L.F.; RT "Characterization of soluble vs membrane-bound human placental 5'- RT nucleotidase."; RL Biochem. Biophys. Res. Commun. 172:1371-1377(1990). RN [5] RP DISEASE. RX MEDLINE=98313134; PubMed=9651114; DOI=10.1016/S0024-3205(98)00206-9; RA Rosi F., Agostinho A.B., Carlucci F., Zanoni L., Porcelli B., RA Marinello E., Galieni P., Tabucchi A.; RT "Behaviour of human lymphocytic isoenzymes of 5'-nucleotidase."; RL Life Sci. 62:2257-2266(1998). CC -!- FUNCTION: Hydrolyzes extracellular nucleotides into membrane CC permeable nucleosides. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Zinc. CC -!- SUBUNIT: Homodimer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor. CC -!- DISEASE: There is a decrease in the activity of NT5 in B-cell CC chronic lymphocytic leukemia. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X55740; CAA39271.1; -; mRNA. DR EMBL; U21730; AAA96950.1; -; Genomic_DNA. DR EMBL; AF069067; AAC98672.1; -; Genomic_DNA. DR PIR; S11032; S11032. DR UniGene; Hs.153952; -. DR HSSP; P07024; 2USH. DR Ensembl; ENSG00000135318; Homo sapiens. DR KEGG; hsa:4907; -. DR HGNC; HGNC:8021; NT5E. DR MIM; 129190; gene. DR Reactome; REACT_1698.1; Nucleotide metabolism. DR ArrayExpress; P21589; -. DR GermOnline; ENSG00000135318; Homo sapiens. DR RZPD-ProtExp; C0325; -. DR RZPD-ProtExp; IOH10119; -. DR GO; GO:0005624; C:membrane fraction; TAS:ProtInc. DR GO; GO:0008253; F:5'-nucleotidase activity; TAS:ProtInc. DR GO; GO:0006259; P:DNA metabolic process; TAS:ProtInc. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR PANTHER; PTHR11575; 5_nucleotidase; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. KW Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase; KW Lipoprotein; Membrane; Metal-binding; Nucleotide-binding; KW Polymorphism; Signal; Zinc. FT SIGNAL 1 26 FT CHAIN 27 549 5'-nucleotidase. FT /FTId=PRO_0000000015. FT PROPEP 550 574 Removed in mature form. FT /FTId=PRO_0000000016. FT REGION 500 506 Substrate binding (By similarity). FT METAL 36 36 Zinc 1 (By similarity). FT METAL 38 38 Zinc 1 (By similarity). FT METAL 85 85 Zinc 1 (By similarity). FT METAL 85 85 Zinc 2 (By similarity). FT METAL 117 117 Zinc 2 (By similarity). FT METAL 220 220 Zinc 2 (By similarity). FT METAL 243 243 Zinc 2 (By similarity). FT BINDING 417 417 Substrate (By similarity). FT SITE 118 118 Transition state stabilizer (By FT similarity). FT SITE 121 121 Transition state stabilizer (By FT similarity). FT LIPID 549 549 GPI-anchor amidated serine. FT CARBOHYD 53 53 N-linked (GlcNAc...) (Potential). FT CARBOHYD 311 311 N-linked (GlcNAc...) (Potential). FT CARBOHYD 333 333 N-linked (GlcNAc...) (Potential). FT CARBOHYD 403 403 N-linked (GlcNAc...) (Potential). FT VARIANT 376 376 T -> A (in dbSNP:rs3812138). FT /FTId=VAR_022091. SQ SEQUENCE 574 AA; 63368 MW; A99AF170AB7EAECE CRC64; MCPRAARAPA TLLLALGAVL WPAAGAWELT ILHTNDVHSR LEQTSEDSSK CVNASRCMGG VARLFTKVQQ IRRAEPNVLL LDAGDQYQGT IWFTVYKGAE VAHFMNALRY DAMALGNHEF DNGVEGLIEP LLKEAKFPIL SANIKAKGPL ASQISGLYLP YKVLPVGDEV VGIVGYTSKE TPFLSNPGTN LVFEDEITAL QPEVDKLKTL NVNKIIALGH SGFEMDKLIA QKVRGVDVVV GGHSNTFLYT GNPPSKEVPA GKYPFIVTSD DGRKVPVVQA YAFGKYLGYL KIEFDERGNV ISSHGNPILL NSSIPEDPSI KADINKWRIK LDNYSTQELG KTIVYLDGSS QSCRFRECNM GNLICDAMIN NNLRHTDEMF WNHVSMCILN GGGIRSPIDE RNNGTITWEN LAAVLPFGGT FDLVQLKGST LKKAFEHSVH RYGQSTGEFL QVGGIHVVYD LSRKPGDRVV KLDVLCTKCR VPSYDPLKMD EVYKVILPNF LANGGDGFQM IKDELLRHDS GDQDINVVST YISKMKVIYP AVEGRIKFST GSHCHGSFSL IFLSLWAVIF VLYQ // ID 5NTD_LUTLO Reviewed; 572 AA. AC Q9XZ43; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 28-NOV-2006, entry version 44. DE Protein 5NUC precursor [Includes: UDP-sugar hydrolase (EC 3.6.1.45) DE (UDP-sugar diphosphatase) (UDP-sugar pyrophosphatase); 5'-nucleotidase DE (EC 3.1.3.5) (5'-NT)]. GN Name=5NUC; OS Lutzomyia longipalpis (Sand fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; OC Psychodidae; Lutzomyia; Lutzomyia. OX NCBI_TaxID=7200; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Jacobina; TISSUE=Salivary gland; RA Charlab R., Valenzuela J.G., Rowton E.D., Ribeiro J.M.C.; RT "Toward an understanding of the biochemical and pharmacological RT complexity of the saliva of a hematophagous sand fly, Lutzomyia RT longipalpis."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP CHARACTERIZATION. RC TISSUE=Salivary gland; RX MEDLINE=20193550; PubMed=10727894; DOI=10.1016/S0965-1748(99)00123-X; RA Ribeiro J.M.C., Rowton E.D., Charlab R.; RT "The salivary 5'-nucleotidase/phosphodiesterase of the hematophagus RT sand fly corrected, Lutzomyia longipalpis."; RL Insect Biochem. Mol. Biol. 30:279-285(2000). RN [3] RP ERRATUM. RA Ribeiro J.M.C., Rowton E.D., Charlab R.; RL Insect Biochem. Mol. Biol. 30:609-609(2000). CC -!- FUNCTION: Degradation of external UDP-glucose to uridine CC monophosphate and glucose-1-phosphate, which can then be used by CC the cell (By similarity). CC -!- CATALYTIC ACTIVITY: UDP-sugar + H(2)O = UMP + alpha-D-aldose 1- CC phosphate. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Zinc (By similarity). CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF132510; AAD32190.1; -; mRNA. DR HSSP; P07024; 2USH. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EC. DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IEA:EC. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR PANTHER; PTHR11575; 5_nucleotidase; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. KW Glycoprotein; Hydrolase; Metal-binding; Nucleotide-binding; Signal; KW Zinc. FT SIGNAL 1 25 Potential. FT CHAIN 26 572 Protein 5NUC. FT /FTId=PRO_0000000023. FT REGION 512 518 Substrate binding (By similarity). FT METAL 39 39 Zinc 1 (By similarity). FT METAL 41 41 Zinc 1 (By similarity). FT METAL 93 93 Zinc 1 (By similarity). FT METAL 93 93 Zinc 2 (By similarity). FT METAL 125 125 Zinc 2 (By similarity). FT METAL 227 227 Zinc 2 (By similarity). FT METAL 250 250 Zinc 2 (By similarity). FT BINDING 427 427 Substrate (By similarity). FT SITE 126 126 Transition state stabilizer (By FT similarity). FT SITE 129 129 Transition state stabilizer (By FT similarity). FT CARBOHYD 82 82 N-linked (GlcNAc...) (Potential). FT CARBOHYD 454 454 N-linked (GlcNAc...) (Potential). FT CARBOHYD 490 490 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 572 AA; 63354 MW; 69A652338C04536D CRC64; MLFFLNFFVL VFSIELALLT ASAAAEDGSY EIIILHTNDM HARFDQTNAG SNKCQEKDKI ASKCYGGFAR VSTMVKKFRE ENGSSVLFLN AGDTYTGTPW FTLYKETIAT EMMNILRPDA ASLGNHEFDK GVEGLVPFLN GVTFPILTAN LDTSQEPTMT NAKNLKRSMI FTVSGHRVGV IGYLTPDTKF LSDVGKVNFI PEVEAINTEA QRLKKEENAE IIIVVGHSGL IKDREIAEKC PLVDIIVGGH SHTFLYTGSQ PDREVPVDVY PVVVTQSSGK KVPIVQAYCF TKYLGYFKVT INGKGNVVGW TGQPILLNNN IPQDQEVLTA LEKYRERVEN YGNRVIGVSR VILNGGHTEC RFHECNMGNL ITDAFVYANV ISTPMSTNAW TDASVVLYQS GGIRAPIDPR TAAGSITRLE LDNVLPFGNA LYVVKVPGNV LRKALEHSVH RYSNTSGWGE FPQVSGLKIR FNVNEEIGKR VKSVKVLCSN CSQPEYQPLR NKKTYNVIMD SFMKDGGDGY SMFKPLKIIK TLPLGDIETV EAYIEKMGPI FPAVEGRITV LGGLQKSDED WH // ID 5NTD_MOUSE Reviewed; 576 AA. AC Q61503; Q3U3S1; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 2. DT 23-JAN-2007, entry version 68. DE 5'-nucleotidase precursor (EC 3.1.3.5) (Ecto-5'-nucleotidase) (5'-NT) DE (CD73 antigen). GN Name=Nt5e; Synonyms=Nt5, Nte; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Kidney; RX MEDLINE=94040807; PubMed=8224905; DOI=10.1016/0378-1119(93)90635-G; RA Resta R., Hooker S.W., Hansen K.R., Laurent A.B., Park J.L., RA Blackburn M.R., Knudsen T.B., Thompson L.F.; RT "Murine ecto-5'-nucleotidase (CD73): cDNA cloning and tissue RT distribution."; RL Gene 133:171-177(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=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). CC -!- FUNCTION: Hydrolyzes extracellular nucleotides into membrane CC permeable nucleosides. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Zinc (By similarity). CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor (By CC similarity). CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L12059; AAC13542.1; -; mRNA. DR EMBL; AK028723; BAC26084.1; -; mRNA. DR EMBL; AK029979; BAC26714.1; -; mRNA. DR EMBL; AK154614; BAE32714.1; -; mRNA. DR UniGene; Mm.244235; -. DR HSSP; P07024; 2USH. DR Ensembl; ENSMUSG00000032420; Mus musculus. DR KEGG; mmu:23959; -. DR MGI; MGI:99782; Nt5e. DR ArrayExpress; Q61503; -. DR GermOnline; ENSMUSG00000032420; Mus musculus. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; KW Metal-binding; Nucleotide-binding; Signal; Zinc. FT SIGNAL 1 28 By similarity. FT CHAIN 29 551 5'-nucleotidase. FT /FTId=PRO_0000000017. FT PROPEP 552 576 Removed in mature form (By similarity). FT /FTId=PRO_0000000018. FT REGION 502 508 Substrate binding (By similarity). FT METAL 38 38 Zinc 1 (By similarity). FT METAL 40 40 Zinc 1 (By similarity). FT METAL 87 87 Zinc 1 (By similarity). FT METAL 87 87 Zinc 2 (By similarity). FT METAL 119 119 Zinc 2 (By similarity). FT METAL 222 222 Zinc 2 (By similarity). FT METAL 245 245 Zinc 2 (By similarity). FT BINDING 419 419 Substrate (By similarity). FT SITE 120 120 Transition state stabilizer (By FT similarity). FT SITE 123 123 Transition state stabilizer (By FT similarity). FT LIPID 551 551 GPI-anchor amidated serine (By FT similarity). FT CARBOHYD 55 55 N-linked (GlcNAc...) (Potential). FT CARBOHYD 313 313 N-linked (GlcNAc...) (Potential). FT CARBOHYD 335 335 N-linked (GlcNAc...) (Potential). FT CARBOHYD 405 405 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 576 AA; 63864 MW; 29D697928A5D5915 CRC64; MRPAAAKVPK WLLLALSALL PQWPAASAWE LTILHTNDVH SRLEQTSDDS TKCLNASLCV GGVARLFTKV QQIRKEEPNV LFLDAGDQYQ GTIWFTVYKG LEVAHFMNIL GYDAMALGNH EFDNGVEGLI DPLLRNVKFP ILSANIKARG PLAHQISGLF LPSKVLSVGG EVVGIVGYTS KETPFLSNPG TNLVFEDEIS ALQPEVDKLK TLNVNKIIAL GHSGFEMDKL IAQKVRGVDI VVGGHSNTFL YTGNPPSKEV PAGKYPFIVT ADDGRQVPVV QAYAFGKYLG YLKVEFDDKG NVITSYGNPI LLNSSIPEDA TIKADINQWR IKLDNYSTQE LGRTIVYLDG STQTCRFREC NMGNLICDAM INNNLRHPDE MFWNHVSMCI VNGGGIRSPI DEKNNGTITW ENLAAVLPFG GTFDLVQLKG STLKKAFEHS VHRYGQSTGE FLQVGGIHVV YDINRKPWNR VVQLEVLCTK CRVPIYEPLE MDKVYKVTLP SYLANGGDGF QMIKDELLKH DSGDQDISVV SEYISKMKVV YPAVEGRIKF SAASHYQGSF PLVILSFWAM ILILYQ // ID 5NTD_PSEAE Reviewed; 221 AA. AC Q9I767; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 31-OCT-2006, entry version 25. DE 5'-nucleotidase (EC 3.1.3.5) (Nucleoside 5'-monophosphate DE phosphohydrolase). GN OrderedLocusNames=PA0065; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). RN [2] RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15808744; DOI=10.1016/j.femsre.2004.12.006; RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.; RT "Enzyme genomics: application of general enzymatic screens to discover RT new enzymes."; RL FEMS Microbiol. Rev. 29:263-279(2005). CC -!- FUNCTION: Specifically dephosphorylates nucleoside 5'- CC monophosphates to nucleosides and inorganic phosphate. Displays CC high activity toward 5'-UMP and 5'-IMP, significant activity CC against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Divalent metal cation. Prefers manganese over magnesium. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.39 mM for 5'-UMP; CC Vmax=3.14 umol/min/mg enzyme with 5'-UMP as substrate; CC pH dependence: CC Optimum pH is 7.4; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004091; AAG03455.1; -; Genomic_DNA. DR PIR; C83636; C83636. DR GenomeReviews; AE004091_GR; PA0065. DR KEGG; pae:PA0065; -. DR BioCyc; PAER287:PA0065-MONOMER; -. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EC. DR InterPro; IPR005834; Dehalogen-like_hydro. DR Pfam; PF00702; Hydrolase; 1. KW Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding. FT CHAIN 1 221 5'-nucleotidase. FT /FTId=PRO_0000064390. FT ACT_SITE 14 14 Nucleophile (By similarity). SQ SEQUENCE 221 AA; 24951 MW; 8885AF689CC828B1 CRC64; MRDAALRYPN ILFDLDGTLT DPREGITRSV QFALARLGID EPDLARLEHF IGPPLLQCFM QTYGFDEARA WEAVNHYRER FRVTGLYENR VFDGIPELLE ALVGRGHTLY VATSKPGVFA REIARHFAFD RHFKAIYGSE LDGTRTHKEE LIRHLLDSEG LAAEHCLMIG DRMHDLLGAS RNGVACIGVG YGFGSEDELR AHQPTHYCAD LAALRQVLES H // ID 5NTD_RAT Reviewed; 576 AA. AC P21588; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 06-FEB-2007, entry version 69. DE 5'-nucleotidase precursor (EC 3.1.3.5) (Ecto-5'-nucleotidase) (5'-NT) DE (CD73 antigen). GN Name=Nt5e; Synonyms=Nt5, Nte; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX MEDLINE=90130472; PubMed=2298743; RA Misumi Y., Ogata S., Hirose S., Ikehara Y.; RT "Primary structure of rat liver 5'-nucleotidase deduced from the cDNA. RT Presence of the COOH-terminal hydrophobic domain for possible post- RT translational modification by glycophospholipid."; RL J. Biol. Chem. 265:2178-2183(1990). RN [2] RP PROTEIN SEQUENCE OF 538-551, AND GPI-ANCHOR AT SER-551. RC TISSUE=Liver; RX MEDLINE=91084455; PubMed=2148114; DOI=10.1021/bi00486a021; RA Ogata S., Hayashi Y., Misumi Y., Ikehara Y.; RT "Membrane-anchoring domain of rat liver 5'-nucleotidase: RT identification of the COOH-terminal serine-523 covalently attached RT with a glycolipid."; RL Biochemistry 29:7923-7927(1990). CC -!- FUNCTION: Hydrolyzes extracellular nucleotides into membrane CC permeable nucleosides. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Zinc. CC -!- SUBUNIT: Homodimer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J05214; AAA40621.1; -; mRNA. DR PIR; A35036; A35036. DR UniGene; Rn.40132; -. DR HSSP; P07024; 2USH. DR Ensembl; ENSRNOG00000011071; Rattus norvegicus. DR KEGG; rno:58813; -. DR RGD; 61956; Nt5e. DR ArrayExpress; P21588; -. DR GermOnline; ENSRNOG00000011071; Rattus norvegicus. DR GO; GO:0016021; C:integral to membrane; TAS:RGD. DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:RGD. DR GO; GO:0008198; F:ferrous iron binding; IDA:RGD. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:RGD. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR PANTHER; PTHR11575; 5_nucleotidase; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. KW Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase; KW Lipoprotein; Membrane; Metal-binding; Nucleotide-binding; Signal; KW Zinc. FT SIGNAL 1 28 FT CHAIN 29 551 5'-nucleotidase. FT /FTId=PRO_0000000019. FT PROPEP 552 576 Removed in mature form. FT /FTId=PRO_0000000020. FT REGION 502 508 Substrate binding (By similarity). FT METAL 38 38 Zinc 1 (By similarity). FT METAL 40 40 Zinc 1 (By similarity). FT METAL 87 87 Zinc 1 (By similarity). FT METAL 87 87 Zinc 2 (By similarity). FT METAL 119 119 Zinc 2 (By similarity). FT METAL 222 222 Zinc 2 (By similarity). FT METAL 245 245 Zinc 2 (By similarity). FT BINDING 419 419 Substrate (By similarity). FT SITE 120 120 Transition state stabilizer (By FT similarity). FT SITE 123 123 Transition state stabilizer (By FT similarity). FT LIPID 551 551 GPI-anchor amidated serine. FT CARBOHYD 55 55 N-linked (GlcNAc...) (Potential). FT CARBOHYD 313 313 N-linked (GlcNAc...) (Potential). FT CARBOHYD 335 335 N-linked (GlcNAc...) (Potential). FT CARBOHYD 349 349 N-linked (GlcNAc...) (Potential). FT CARBOHYD 405 405 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 576 AA; 63969 MW; 9EB75DD51E678AA6 CRC64; MRPAAATAPK WLLLALSALL PLWPTAKSWE LTIMHTNDVH SRLEQTSDDS TKCLNASLCV GGVARLFTKV QQIRKEEPNV LLLDAGDQYQ GTIWFTVYKG LEVAHFMNLL GYDAMALGNH EFDNGVEGLI DPLLRNVKFP ILSANIKARG PLAPQISGLY LPYKVLSVGG EVVGIVGYTS KETPFLSNPG TNLVFEDEVT ALQPEVDKLK TLNVNKIIAL GHSGFEMDKL IAQKVRGVDV VVGGHTNTFL YTGNPPSKEV PAGKYPFIVT SDDGRKVPVV QAYAFGKYLG YLKVEFDDKG NVVTSYGNPI LLNSTIREDA AIKADINQWR IKLDNYSTQE LGRTIVYLNG SAQECRFREC NMGNLICDAM INNNLRHPDE MFWNHVSMCI VNGGGIRSPI DERNNGTITW ENLAAVLPFG GTFDLVQLKG STLKKAFEHS VHRYGQSTGE FLQVGGIHVV YDISRKPWDR VVQLKVLCTK CRVPIYEPLE MDKVYKVVLP SYLVNGGDGF QMIKDELLKH DSGDQDISVV SEYISKMKVI YPAVEGRIKF SAASHYQGSF PLIILSFWAV ILVLYQ // ID 5NTD_TREPA Reviewed; 593 AA. AC O83142; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 20-FEB-2007, entry version 50. DE Probable 5'-nucleotidase precursor (EC 3.1.3.5). GN OrderedLocusNames=TP_0104; OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nichols; RX MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., RA Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., RA Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., RA Weidman J.F., Smith H.O., Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Divalent cations (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor (Potential). CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000520; AAC26552.1; -; Genomic_DNA. DR PIR; E71365; E71365. DR HSSP; P07024; 2USH. DR GenomeReviews; AE000520_GR; TP0104. DR KEGG; tpa:TP0104; -. DR TIGR; TP_0104; -. DR LinkHub; O83142; -. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR InterPro; IPR006420; NadN. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR PANTHER; PTHR11575; 5_nucleotidase; 2. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR TIGRFAMs; TIGR01530; nadN; 1. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Complete proteome; Hydrolase; Lipoprotein; Membrane; Metal-binding; KW Nucleotide-binding; Palmitate; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 593 Probable 5'-nucleotidase. FT /FTId=PRO_0000000027. FT REGION 539 545 Substrate binding (By similarity). FT METAL 41 41 Divalent metal cation 1 (By similarity). FT METAL 43 43 Divalent metal cation 1 (By similarity). FT METAL 91 91 Divalent metal cation 1 (By similarity). FT METAL 91 91 Divalent metal cation 2 (By similarity). FT METAL 123 123 Divalent metal cation 2 (By similarity). FT METAL 224 224 Divalent metal cation 2 (By similarity). FT BINDING 456 456 Substrate (By similarity). FT SITE 124 124 Transition state stabilizer (By FT similarity). FT SITE 127 127 Transition state stabilizer (By FT similarity). FT LIPID 22 22 N-palmitoyl cysteine (Probable). FT LIPID 22 22 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 593 AA; 64871 MW; 051931037DF33B40 CRC64; MKRFIPHRVI HAVCIGLALV GCRKLDSRAG DFELTIIHIN DHHSHLEPEP LELAVAGERL RAAVGGYAAL VHEIQRLRAE SKNALVLHAG DALIGTLYST LFRGRADAVL MNHAGFDFFT LGNHEFDNGN EGLKEFLHYL EVPVLSANVV PNAASTLHGL WKPSAIVERA GERIGVIGLD TVKKTVESSS PGKDINFIDE IEAVRRATVE MQQQGVNKII LLSHAGFEKN CEIAQNISGI DVIVSGDTHY LLGDESLGRL GLPVVGEYPR KIMSPAGEPV YVVEAWEYGK CLGELNVVFD RTGVITSAVG MPRFLLHTNT LQKKGADRKN YPLEEAEREA LLVALRMTPE IIFAQENDQI ISVLEEFKKE KEALGAQAIG VITGASMRGG SVHRVPDAQN PQGSVATRFV AETMLSDIQS FGAGKVDCVI QNAGGARSNI QPGEITYNDA YTLLPFSNTL VLVDVSGAEL KQIIEDALQF ALGDGSTGAF PYGAGVRYEA RQEPDEHGKR VIKLEVQKKD GAWVPVDERA PYRLGVNSYI ARGKDGYKTL GEIVSTRGAE DTYLRDAESL IKFLRAHKNF RAYTDSNVIF RLK // ID 5NTD_VIBCH Reviewed; 553 AA. AC Q9KQ30; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 23-JAN-2007, entry version 49. DE 5'-nucleotidase precursor (EC 3.1.3.5). GN Name=nutA; OrderedLocusNames=VC2174; OS Vibrio cholerae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=666; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961 / Serotype O1; RX MEDLINE=20406833; PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., RA Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., RA Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I., RA Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., RA Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., RA Mekalanos J.J., Venter J.C., Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). CC -!- FUNCTION: Degradation of extracellular 5'-nucleotides for CC nutritional needs (By similarity). CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Chloride (By similarity). CC -!- COFACTOR: Magnesium (By similarity). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor (By CC similarity). CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004289; AAF95319.1; -; Genomic_DNA. DR PIR; E82108; E82108. DR HSSP; P07024; 2USH. DR GenomeReviews; AE003852_GR; VC2174. DR KEGG; vch:VC2174; -. DR TIGR; VC2174; -. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EC. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR PANTHER; PTHR11575; 5_nucleotidase; 2. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Complete proteome; Hydrolase; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Nucleotide-binding; Outer membrane; Palmitate; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 553 5'-nucleotidase. FT /FTId=PRO_0000000028. FT REGION 501 507 Substrate binding (By similarity). FT METAL 45 45 Divalent metal cation 1 (By similarity). FT METAL 47 47 Divalent metal cation 1 (By similarity). FT METAL 88 88 Divalent metal cation 1 (By similarity). FT METAL 88 88 Divalent metal cation 2 (By similarity). FT METAL 120 120 Divalent metal cation 2 (By similarity). FT METAL 221 221 Divalent metal cation 2 (By similarity). FT METAL 256 256 Divalent metal cation 2 (By similarity). FT METAL 258 258 Divalent metal cation 1 (By similarity). FT BINDING 432 432 Substrate (By similarity). FT SITE 121 121 Transition state stabilizer (By FT similarity). FT SITE 124 124 Transition state stabilizer (By FT similarity). FT LIPID 22 22 N-palmitoyl cysteine (Probable). FT LIPID 22 22 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 553 AA; 60903 MW; 5AA621C27526B311 CRC64; MKQGLILKSV LSAAIIASLA GCATAPAQQW EADKTYKLTI LHTNDHHGRF WQNQYGEYGM AARKTLIDQL RADIEAQGGS VLLLSGGDIN TGVPESDLQD AEPDFKGMSK IGYDAMALGN HEFDNPLEVL FKQKEWANFP MLSANIYDKA TGKRLFEPYH IFDKQGIKIA VIGLTTEDTA KIGNPEYIGG IDFRDPKEEA KKVIAELKKK EKPDLIIAVT HMGHYQNGEH GVNAPGDVAL ARYLPAGELD MIVGGHSQEP VCMEGPNLVK KNFKPGDECK PDIQNGTYIV QAYEWGKYVG RADYEFRNGE LNMVSYNLIP VNLKKKVEVN GETQRVFATS EIKEDSAMLE FLRPFQEKGQ EQLSIKIAHS NGKLEGDRNV VRFEQTNLGR MIAMAHMQRA KADFAVMNSG GVRDSIQAGD ITYKDVLKVQ PFGNIVSYVD MNGQEVLDYL NVVATKPVDS GAYAQFAGIS MTVADGKVSN VVIGGKQLRL DATYRFTVPS FNAAGGDGYP KITDHPGYVN TGFVDAEVLK DYLEANSPID VNRFAPAGEI VYR // ID 5NTD_VIBPA Reviewed; 560 AA. AC P22848; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2003, sequence version 2. DT 23-JAN-2007, entry version 61. DE 5'-nucleotidase precursor (EC 3.1.3.5). GN Name=nutA; OrderedLocusNames=VP0748; OS Vibrio parahaemolyticus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=670; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=AQ3334; RX MEDLINE=91201280; PubMed=2016269; RA Tamao Y., Noguchi K., Sakai-Tomita Y., Hama H., Shimamoto T., RA Kanazawa H., Tsuda M., Tsuchiya T.; RT "Sequence analysis of nutA gene encoding membrane-bound Cl(-)- RT dependent 5'-nucleotidase of Vibrio parahaemolyticus."; RL J. Biochem. 109:24-29(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIMD 2210633 / Serotype O3:K6; RX MEDLINE=22508454; PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1; RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.; RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism RT distinct from that of V. cholerae."; RL Lancet 361:743-749(2003). CC -!- FUNCTION: Degradation of extracellular 5'-nucleotides for CC nutritional needs. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Chloride. CC -!- COFACTOR: Magnesium. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X57711; CAA40882.1; -; Genomic_DNA. DR EMBL; D00910; BAA00756.1; -; Genomic_DNA. DR EMBL; BA000031; BAC59011.1; -; Genomic_DNA. DR PIR; JX0153; JX0153. DR HSSP; P07024; 2USH. DR GenomeReviews; BA000031_GR; VP0748. DR KEGG; vpa:VP0748; -. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EC. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR PANTHER; PTHR11575; 5_nucleotidase; 2. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Complete proteome; Hydrolase; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Nucleotide-binding; Outer membrane; Palmitate; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 560 5'-nucleotidase. FT /FTId=PRO_0000000029. FT REGION 501 507 Substrate binding (By similarity). FT METAL 45 45 Divalent metal cation 1 (By similarity). FT METAL 47 47 Divalent metal cation 1 (By similarity). FT METAL 88 88 Divalent metal cation 1 (By similarity). FT METAL 88 88 Divalent metal cation 2 (By similarity). FT METAL 120 120 Divalent metal cation 2 (By similarity). FT METAL 221 221 Divalent metal cation 2 (By similarity). FT METAL 256 256 Divalent metal cation 2 (By similarity). FT METAL 258 258 Divalent metal cation 1 (By similarity). FT BINDING 432 432 Substrate (By similarity). FT SITE 121 121 Transition state stabilizer (By FT similarity). FT SITE 124 124 Transition state stabilizer (By FT similarity). FT LIPID 22 22 N-palmitoyl cysteine (Probable). FT LIPID 22 22 S-diacylglycerol cysteine (Probable). FT CONFLICT 198 198 V -> A (in Ref. 1). SQ SEQUENCE 560 AA; 62175 MW; F82E6B4095403D05 CRC64; MNQRLIIKTA LSAAILASLA GCASQPAHEW NADTTYKLTV LHTNDHHGRF WQNKHGEYGM AARKTLIDDL RDEIQAEGGS VLLLSGGDIN TGVPESDLQD AEPDFKGMSK IGYDAMALGN HEFDNPLDVL FKQQDWANFP MLSANIYDKK TGKRLFQPYA MFNKQGIKIA VIGLTTEDTA KLGNPEFIGQ VDFRDPKVEA KELIAELKKT ENPDLIFAVT HMGHYENGNR GINAPGDVAL ARYLNEGDLD MIVGGHSQEP VCMEGPNVIK KNFKPGDECQ PDQQNGTYIV QAHEWGKYVG RADYEFRNGE LSMVSYDLIP VNLKKKINVD GQSQRVFVQD EITQDKAMLD FLRPFQEKGQ SQLNVKIAES NGKLEGDRDV VRFQQTNLGR LIATAHMERA KADFAVMNSG GVRDSIEAGD ITYKDVLTVQ PFGNMVSYVD MSGQEVLDYL NIVATKPVDS GAYAQFAGIS MRIENDKVTN VFIGNKQLRL DGRYRFTVPS YNASGGDGYP KIDTHPGYVN TGFTDAEVLK DYLESHSPID VNEYAPSGEV MYQTNNVVNQ // ID 5NTD_VIBVU Reviewed; 553 AA. AC Q8DFG4; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 21-NOV-2003, sequence version 2. DT 23-JAN-2007, entry version 33. DE 5'-nucleotidase precursor (EC 3.1.3.5). GN Name=nutA; OrderedLocusNames=VV1_0248; OS Vibrio vulnificus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=672; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CMCP6; RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., RA Choy H.E.; RT "Complete genome sequence of Vibrio vulnificus CMCP6."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Degradation of extracellular 5'-nucleotides for CC nutritional needs (By similarity). CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Chloride (By similarity). CC -!- COFACTOR: Magnesium (By similarity). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; lipid-anchor CC (Probable). CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016795; AAO08784.1; ALT_INIT; Genomic_DNA. DR HSSP; P07024; 2USH. DR GenomeReviews; AE016795_GR; VV1_0248. DR KEGG; vvu:VV10248; -. DR BioCyc; VVUL216895:VV10248-MONOMER; -. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EC. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_N. DR InterPro; IPR006179; 5_nucleotidase. DR InterPro; IPR004843; M-pesterase. DR Gene3D; G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. KW Complete proteome; Hydrolase; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Nucleotide-binding; Outer membrane; Palmitate; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 553 5'-nucleotidase. FT /FTId=PRO_0000000030. FT REGION 501 507 Substrate binding (By similarity). FT METAL 45 45 Divalent metal cation 1 (By similarity). FT METAL 47 47 Divalent metal cation 1 (By similarity). FT METAL 88 88 Divalent metal cation 1 (By similarity). FT METAL 88 88 Divalent metal cation 2 (By similarity). FT METAL 120 120 Divalent metal cation 2 (By similarity). FT METAL 221 221 Divalent metal cation 2 (By similarity). FT METAL 256 256 Divalent metal cation 2 (By similarity). FT METAL 258 258 Divalent metal cation 1 (By similarity). FT BINDING 432 432 Substrate (By similarity). FT SITE 121 121 Transition state stabilizer (By FT similarity). FT SITE 124 124 Transition state stabilizer (By FT similarity). FT LIPID 22 22 N-palmitoyl cysteine (Probable). FT LIPID 22 22 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 553 AA; 61331 MW; A4A63360A44C27A6 CRC64; MKQRLIVKTA LSAAILATLA GCATQPTQEW AADTTYKLTV LHTNDHHGRF WQNKYGEYGM AARKTLIDEL RAEIQAEGGS VLLLSGGDIN TGVPESDLQD AEPDFKGMSK IGYDAMALGN HEFDNPLDVL MKQKEWANFP MLSANIYDKK TGERMFQAYE MFDKQGIKIA VIGLTTEDTA KLGNPEFIGA IDFRDPKEEA KKLIAELKET EKPDLIFAVT HMGHYEDGKR GINAPGDVAL ARYLNEGDLD MIVGGHSQEP VCMEAPNVVK KNFKPADECK PDQQNGTYIV QAHEWGKYVG RADYEFRNGE LRMVSYDLIP VNLKKKVEVD GKSQRVFIES EIKEDTALLE FLRPYQEKGQ EQLNVKIADT NGKLEGDRNV VRFQQTNLGR LIAVSHMERA KADFAVMNSG GVRDSIEAGE VTYKDVLTVQ PFANILTYTD MTGKEVLDYL NVVATKPVDS GAYAQFAGIS MTVANGKVSN VFIGGKQLRL DETYRFTVPS YNAAGGDGYP KLTGHPGYVN TGFVDAEVLK EFLEKNSPID VNKFAPNGEI VYK // ID 5S_PROFR Reviewed; 505 AA. AC Q70AC7; Q05618; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 31-OCT-2006, entry version 16. DE Methylmalonyl-CoA carboxyltransferase 5S subunit (EC 2.1.3.1) DE (Transcarboxylase 5S subunit). OS Propionibacterium freudenreichii subsp. shermanii. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1752; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 3-22; RP 67-76; 88-92; 111-124; 134-147; 305-316; 325-337; 371-393; 397-410 AND RP 431-456. RC STRAIN=St33; RX MEDLINE=93374062; PubMed=8365490; DOI=10.1016/0014-5793(93)80271-U; RA Thornton C.G., Kumar G.K., Shenoy B.C., Haase F.C., Phillips N.F.B., RA Park V.M., Magner W.J., Hejlik D.P., Wood H.G., Samols D.; RT "Primary structure of the 5 S subunit of transcarboxylase as deduced RT from the genomic DNA sequence."; RL FEBS Lett. 330:191-196(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13673 / VPI 0409 / 33; RX PubMed=14993680; DOI=10.1107/S0907444903028294; RA Hall P.R., Zheng R., Pusztai-Carey M., van den Akker F., Carey P.R., RA Yee V.C.; RT "Expression and crystallization of several forms of the RT Propionibacterium shermanii transcarboxylase 5S subunit."; RL Acta Crystallogr. D 60:521-523(2004). CC -!- FUNCTION: The 5S subunit specifically catalyzes the transfer of CC the carboxyl group from biotin of the 1.3S subunit to pyruvate to CC form oxaloacetate and 1.3S biotin. CC -!- CATALYTIC ACTIVITY: (S)-methylmalonyl-CoA + pyruvate = propanoyl- CC CoA + oxaloacetate. CC -!- SUBUNIT: Homodimer. Transcarboxylase is composed of three CC subunits: 1.3S, 5S, and 12S. The core of the enzyme is composed of CC six 12S subunits. On each side of the core there are three pairs CC of 5S subunits. Each 5S dimer is attached to the core by two 1.3S CC subunits. Thus the total number of chains is 30 (6 + 12 + 12). CC -!- SIMILARITY: Contains 1 carboxyltransferase domain. CC -!- CAUTION: Ref.1 sequence differs from that shown due to several CC frameshifts. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L06488; AAA03174.1; ALT_FRAME; Unassigned_DNA. DR EMBL; AJ606310; CAE54442.1; -; Genomic_DNA. DR PIR; S36808; S36808. DR PDB; 1RQB; X-ray; A=2-505. DR PDB; 1RQE; X-ray; A=2-505. DR PDB; 1RQH; X-ray; A=2-505. DR PDB; 1RR2; X-ray; A=2-505. DR PDB; 1S3H; X-ray; A=2-505. DR PDB; 1U5J; X-ray; A=2-505. DR GO; GO:0047154; F:methylmalonyl-CoA carboxytransferase activity; IEA:EC. DR InterPro; IPR003379; PYC_OADA. DR InterPro; IPR000891; PYR_CT. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF02436; PYC_OADA; 1. DR PROSITE; PS50991; PYR_CT; 1. KW 3D-structure; Direct protein sequencing; Transferase. FT CHAIN 1 505 Methylmalonyl-CoA carboxyltransferase 5S FT subunit. FT /FTId=PRO_0000146816. FT CONFLICT 237 239 Missing (in Ref. 1). FT CONFLICT 386 386 S -> T (in Ref. 1). FT CONFLICT 392 392 P -> PKWSVGEEHRRAITQRPADHDP (in Ref. 1). FT CONFLICT 421 421 K -> E (in Ref. 1). FT STRAND 4 8 FT STRAND 11 13 FT STRAND 15 18 FT TURN 20 22 FT HELIX 23 28 FT TURN 30 31 FT HELIX 35 37 FT TURN 38 38 FT HELIX 39 41 FT HELIX 42 47 FT TURN 48 49 FT STRAND 51 57 FT TURN 58 59 FT HELIX 60 66 FT TURN 67 67 FT HELIX 72 82 FT TURN 84 85 FT STRAND 88 92 FT HELIX 94 96 FT TURN 97 98 FT STRAND 99 101 FT HELIX 105 117 FT TURN 118 119 FT STRAND 122 125 FT TURN 128 129 FT TURN 132 132 FT HELIX 133 144 FT TURN 145 146 FT STRAND 148 154 FT TURN 159 160 FT HELIX 163 175 FT TURN 176 177 FT STRAND 179 185 FT TURN 186 187 FT HELIX 192 206 FT TURN 208 209 FT STRAND 212 217 FT TURN 219 220 FT HELIX 223 232 FT TURN 233 234 FT STRAND 236 241 FT HELIX 243 245 FT TURN 248 249 FT HELIX 254 260 FT TURN 261 263 FT STRAND 264 267 FT HELIX 272 285 FT HELIX 286 292 FT TURN 301 301 FT HELIX 302 305 FT HELIX 309 320 FT TURN 321 322 FT TURN 326 327 FT HELIX 328 341 FT TURN 342 343 FT TURN 349 350 FT HELIX 351 365 FT TURN 367 368 FT HELIX 373 379 FT TURN 380 383 FT HELIX 392 402 FT HELIX 411 414 FT HELIX 419 426 FT TURN 427 428 FT TURN 430 431 FT HELIX 436 444 FT TURN 446 448 FT HELIX 449 455 FT HELIX 456 458 FT HELIX 467 473 SQ SEQUENCE 505 AA; 55649 MW; 6DF657E231609064 CRC64; MSPREIEVSE PREVGITELV LRDAHQSLMA TRMAMEDMVG ACADIDAAGY WSVECWGGAT YDSCIRFLNE DPWERLRTFR KLMPNSRLQM LLRGQNLLGY RHYNDEVVDR FVDKSAENGM DVFRVFDAMN DPRNMAHAMA AVKKAGKHAQ GTICYTISPV HTVEGYVKLA GQLLDMGADS IALKDMAALL KPQPAYDIIK AIKDTYGQKT QINLHCHSTT GVTEVSLMKA IEAGVDVVDT AISSMSLGPG HNPTESVAEM LEGTGYTTNL DYDRLHKIRD HFKAIRPKYK KFESKTLVDT SIFKSQIPGG MLSNMESQLR AQGAEDKMDE VMAEVPRVRK AAGFPPLVTP SSQIVGTQAV FNVMMGEYKR MTGEFADIML GYYGASPADR DPKVVKLAEE QSGKKPITQR PADLLPPEWE KQSKEAATLK GFNGTDEDVL TYALFPQVAP VFFEHRAEGP HSVALTDAQL KAEAEGDEKS LAVAGPVTYN VNVGGTVREV TVQQA // ID 60A_DROME Reviewed; 455 AA. AC P27091; Q9W1I4; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 20-FEB-2007, entry version 60. DE Protein 60A precursor (Protein glass bottom boat). GN Name=gbb; Synonyms=60A, gbb-60A, TGFb-60A; ORFNames=CG5562; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE. RX MEDLINE=92021021; PubMed=1924384; RA Wharton K.A., Thomsen G.H., Gelbart W.M.; RT "Drosophila 60A gene, another transforming growth factor beta family RT member, is closely related to human bone morphogenetic proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9214-9218(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=92290120; PubMed=1601181; RA Doctor J.S., Jackson P.D., Rashka K.E., Visalli M., Hoffmann F.M.; RT "Sequence, biochemical characterization, and developmental expression RT of a new member of the TGF-beta superfamily in Drosophila RT melanogaster."; RL Dev. Biol. 151:491-505(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=9636086; RA Khalsa O., Yoon J.-W., Torres-Schumann S., Wharton K.A.; RT "TGF-beta/BMP superfamily members, Gbb-60A and Dpp, cooperate to RT provide pattern information and establish cell identity in the RT Drosophila wing."; RL Development 125:2723-2734(1998). CC -!- FUNCTION: Required for the growth of imaginal tissues and for CC patterning of the adult wing. CC -!- SUBUNIT: Homodimer; disulfide-linked. CC -!- INTERACTION: CC Q9W4X2:HLH3B; NbExp=1; IntAct=EBI-184929, EBI-181758; CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed in cells of the developing foregut CC and hindgut during germ band retraction and later embryonic CC stages. Expressed in the wing disk, mainly in the posterior CC compartment in the pteropleural and medial regions extending into CC the progenitors of the scutellum. High levels are found within the CC posterior and anterior compartments of the wing pouch and low CC levels in the hinge region. In the eye/antennal disk, expression CC is highest anterior to the morphogenetic furrow and in the medial CC regions with lower levels of expression posterior to the CC morphogenetic furrow. Expressed throughout the posterior CC compartment of the leg imaginal disks and within the ventral CC anterior compartment. CC -!- DEVELOPMENTAL STAGE: Expressed throughout development with peaks CC of transcription during early embryogenesis, in pupae, and in CC adult males. CC -!- MISCELLANEOUS: Flies lacking gbb exhibit transparent larvae, and a CC reduction of the adult wing size. CC -!- SIMILARITY: Belongs to the TGF-beta family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M77012; AAA28306.1; -; Genomic_DNA. DR EMBL; M84795; AAA28307.1; -; mRNA. DR EMBL; AE013599; AAF47075.1; -; Genomic_DNA. DR PIR; A43918; A43918. DR UniGene; Dm.4758; -. DR HSSP; P08476; 1NYS. DR DIP; DIP:19466N; -. DR IntAct; P27091; -. DR Ensembl; CG5562; Drosophila melanogaster. DR KEGG; dme:Dmel_CG5562; -. DR FlyBase; FBgn0024234; gbb. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-006308-MONOMER; -. DR GermOnline; CG5562; Drosophila melanogaster. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase. DR GO; GO:0008586; P:wing vein morphogenesis; IMP:FlyBase. DR GO; GO:0007474; P:wing vein specification; IMP:FlyBase. DR InterPro; IPR002400; GF_cysknot. DR InterPro; IPR002405; Inhibin_alpha. DR InterPro; IPR011037; PK_B_barrel_like. DR InterPro; IPR001839; TGFb. DR InterPro; IPR001111; TGFb_N. DR Gene3D; G3DSA:2.40.33.10; PK_B_barrel_like; 1. DR Pfam; PF00019; TGF_beta; 1. DR Pfam; PF00688; TGFb_propeptide; 1. DR PRINTS; PR00438; GFCYSKNOT. DR PRINTS; PR00669; INHIBINA. DR ProDom; PD000357; TGFb; 1. DR SMART; SM00204; TGFB; 1. DR PROSITE; PS00250; TGF_BETA_1; 1. KW Cleavage on pair of basic residues; Complete proteome; Cytokine; KW Developmental protein; Glycoprotein; Growth factor; Signal. FT SIGNAL 1 36 Potential. FT PROPEP 37 335 Potential. FT /FTId=PRO_0000033660. FT CHAIN 336 455 Protein 60A. FT /FTId=PRO_0000033661. FT CARBOHYD 238 238 N-linked (GlcNAc...) (Potential). FT CARBOHYD 250 250 N-linked (GlcNAc...) (Potential). FT CARBOHYD 396 396 N-linked (GlcNAc...) (Potential). FT DISULFID 354 420 By similarity. FT DISULFID 383 452 By similarity. FT DISULFID 387 454 By similarity. FT DISULFID 419 419 Interchain (By similarity). SQ SEQUENCE 455 AA; 51687 MW; C8FA795556341F94 CRC64; MSGLRNTSEA VAVLASLGLG MVLLMFVATT PPAVEATQSG IYIDNGKDQT IMHRVLSEDD KLDVSYEILE FLGIAERPTH LSSHQLSLRK SAPKFLLDVY HRITAEEGLS DQDEDDDYER GHRSRRSADL EEDEGEQQKN FITDLDKRAI DESDIIMTFL NKRHHNVDEL RHEHGRRLWF DVSNVPNDNY LVMAELRIYQ NANEGKWLTA NREFTITVYA IGTGTLGQHT MEPLSSVNTT GDYVGWLELN VTEGLHEWLV KSKDNHGIYI GAHAVNRPDR EVKLDDIGLI HRKVDDEFQP FMIGFFRGPE LIKATAHSSH HRSKRSASHP RKRKKSVSPN NVPLLEPMES TRSCQMQTLY IDFKDLGWHD WIIAPEGYGA FYCSGECNFP LNAHMNATNH AIVQTLVHLL EPKKVPKPCC APTRLGALPV LYHLNDENVN LKKYRNMIVK SCGCH // ID 60A_DROVI Reviewed; 436 AA. AC Q24735; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 31-OCT-2006, entry version 38. DE Protein 60A precursor (Protein glass bottom boat). GN Name=gbb; Synonyms=60A, TGFb-60A; OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7244; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96305349; PubMed=8688461; DOI=10.1016/0167-4781(96)00080-2; RA Du W., Doctor J.S.; RT "Isolation and sequence of the Drosophila virilis 60 A gene, a RT transforming growth factor-beta superfamily member related to RT vertebrate bone morphogenetic proteins."; RL Biochim. Biophys. Acta 1307:273-279(1996). CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- SIMILARITY: Belongs to the TGF-beta family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U48595; AAC47262.1; -; Genomic_DNA. DR HSSP; P08476; 1NYS. DR FlyBase; FBgn0015681; Dvir\gbb. DR InterPro; IPR002400; GF_cysknot. DR InterPro; IPR002405; Inhibin_alpha. DR InterPro; IPR011037; PK_B_barrel_like. DR InterPro; IPR001839; TGFb. DR InterPro; IPR001111; TGFb_N. DR Pfam; PF00019; TGF_beta; 1. DR Pfam; PF00688; TGFb_propeptide; 1. DR PRINTS; PR00438; GFCYSKNOT. DR PRINTS; PR00669; INHIBINA. DR ProDom; PD000357; TGFb; 1. DR SMART; SM00204; TGFB; 1. DR PROSITE; PS00250; TGF_BETA_1; 1. KW Cytokine; Glycoprotein; Growth factor; Signal. FT SIGNAL 1 27 Potential. FT PROPEP 28 317 Potential. FT /FTId=PRO_0000033662. FT CHAIN 318 436 Protein 60A. FT /FTId=PRO_0000033663. FT CARBOHYD 102 102 N-linked (GlcNAc...) (Potential). FT CARBOHYD 114 114 N-linked (GlcNAc...) (Potential). FT CARBOHYD 217 217 N-linked (GlcNAc...) (Potential). FT CARBOHYD 229 229 N-linked (GlcNAc...) (Potential). FT CARBOHYD 377 377 N-linked (GlcNAc...) (Potential). FT DISULFID 335 401 By similarity. FT DISULFID 364 433 By similarity. FT DISULFID 368 435 By similarity. FT DISULFID 400 400 Interchain (By similarity). SQ SEQUENCE 436 AA; 49999 MW; C744B4AE58796692 CRC64; MTASLVVLPS LWLILIIFTA PYTHCTQSGI YIDNGKDQTV MERVLTDDDK LDVSHEILEF LGIAARPLHH KSHGLSLRKS APKFLLDVYY RITAEEGLAI KNKSDHSRSK RDANESEQNF ITDLDKRAID ESDIIMTFLN KRNHNVEEMR HEHGRRLWFD VNNIPTDNYL MMAELRIYQN SNEGKWTTTN KQFTVTVYML RSGGSAPNML EPLSSVNTTG DYVGWLELNV TEALHDWRVN SNENHGIYIG AHALNKPERE IKLDDIGLIH RRTKVDDENQ PFMIGFFRGP ELIKSTSGHS TQKRTKRSTL HQRKKSKSEP VNPFIENSIE NTRSCQMQTL YIDFKDLGWH DWIIAPEGYG AFYCSGECNF PLNAHMNATN HAIVQTLVHL LEPKRVPKPC CAPTRLGALP VLYHLNDENV NLKKYRNMIV KSCGCH // ID 62KD_BACCE Reviewed; 15 AA. AC P83071; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 23-JAN-2007, entry version 13. DE 62 kDa protein (Fragment). OS Bacillus cereus. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1396; RN [1] RP PROTEIN SEQUENCE, AND INDUCTION. RC STRAIN=NCIMB 11796 / DSM 626; RX PubMed=11872115; DOI=10.1046/j.1365-2672.2002.01541.x; RA Browne N., Dowds B.C.A.; RT "Acid stress in the food pathogen Bacillus cereus."; RL J. Appl. Microbiol. 92:404-414(2002). CC -!- INDUCTION: Repressed by acid stress. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Direct protein sequencing. FT CHAIN 1 >15 62 kDa protein. FT /FTId=PRO_0000270970. FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1603 MW; 6E9E778D6E231342 CRC64; MTKDEPLEGN VGVLT // ID 65KD_ZYMMO Reviewed; 584 AA. AC P15255; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 31-OCT-2006, entry version 23. DE 65 kDa protein (ORF 1). OS Zymomonas mobilis. OG Plasmid pZM2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=542; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 10988 / NCIB 8938 / NRRL B-806 / ZM1; RA Misawa N., Nakamura K.; RT "The nucleotide sequence of the 2.7 kilobase pair plasmid of Zymomonas RT mobilis ATCC 10988."; RL J. Biotechnol. 12:63-70(1989). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14438; CAA32611.1; -; Genomic_DNA. DR PIR; S06696; S06696. DR InterPro; IPR001668; Mob_Pre. DR InterPro; IPR006171; Toprim_dom. DR InterPro; IPR006154; Toprim_sub. DR Pfam; PF01076; Mob_Pre; 1. DR Pfam; PF01751; Toprim; 1. DR SMART; SM00493; TOPRIM; 1. KW Plasmid. FT CHAIN 1 584 65 kDa protein. FT /FTId=PRO_0000064391. SQ SEQUENCE 584 AA; 65793 MW; 0402D2FB569B65A6 CRC64; MPNYAIFRFE KHKTVGTIKA ASLHMTRGRE TQNADPDRKE LNEILKGSTD PSADVKSMLN KIQKETGKPL RKNGVQAIEL FFGMSPEWSK QATPEKLEHW KTITQQWAEQ TFGENNLVSL QLHADETTPH LTGFMVPRDP DTGRLNASRW FDGRKALSAL QTDYAASMEP LGLARGVKGS KATHQRVQRH YGNINKTLQL DPKIQAPIPP SIFTNKEEWA EKERLKAQKS ALSVIQPLAD KAARYVEEKK RADRAEEALS LARRKADSMR AIPLSDVLKT LGMELDPADK KQWRDPEHRF RITIDNYKFY DHSAQKGGGG AIDLLMHTTG QDYKGALSWL ADRFGDETAR HDMLLNDLYR SKIRINEAKQ RPAFKQPEHK NEPKIREFLN SRGISFNNIP DSIRTDDRGN VAFLMYDDKD TLQGAELRGT SSGFKGLALG SSREAHFTGS INVKNDEKYD LYIAESAIDA ISVVGFLSPE KIKAGVKLLS TSGVRTSLTK TLRKIVEKAS SVHIAYDWDA VGQRAASLLV GAIKAAFPTK KVENWLPPKE QMIHGKDWND LLMVKRGLKK TVAPKQTVKR KIRF // ID 68MP_BOVIN Reviewed; 60 AA. AC P14790; Q3ZCB5; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 20-FEB-2007, entry version 38. DE 6.8 kDa mitochondrial proteolipid. GN Name=MP68; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY. RC TISSUE=Heart; RX MEDLINE=90127394; PubMed=2298292; DOI=10.1016/0014-5793(90)80082-T; RA Terzi E., Boyot P., van Dorsselaer A., Luu B., Trifilieff E.; RT "Isolation and amino acid sequence of a novel 6.8-kDa mitochondrial RT proteolipid from beef heart. Use of FAB-MS for molecular mass RT determination."; RL FEBS Lett. 260:122-126(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- TISSUE SPECIFICITY: Heart, brain and liver mitochondria. CC -!- MASS SPECTROMETRY: MW=6834.1; METHOD=FAB; RANGE=1-60; NOTE=Ref.1. CC -!- SIMILARITY: Belongs to the small mitochondrial proteolipid family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC102582; AAI02583.1; -; mRNA. DR PIR; A34138; A34138. DR UniGene; Bt.49302; -. DR LinkHub; P14790; -. DR InterPro; IPR012574; Mit_preoteolip. DR Pfam; PF08039; Mit_preoteolip; 1. KW Direct protein sequencing; Mitochondrion. FT CHAIN 1 60 6.8 kDa mitochondrial proteolipid. FT /FTId=PRO_0000064392. SQ SEQUENCE 60 AA; 6834 MW; 0D8AF6566B0AFD12 CRC64; MLQSLIKKVW IPMKPYYTQA YQEIWVGTGL MAYIVYKIRS ADKRSKALKA SSAAPAHGHH // ID 68MP_HUMAN Reviewed; 58 AA. AC P56378; Q86TT7; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 23-JAN-2007, entry version 47. DE 6.8 kDa mitochondrial proteolipid. GN Name=MP68; Synonyms=C14orf2; ORFNames=PRO1574; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Umbilical cord blood; RX MEDLINE=98318631; PubMed=9653160; DOI=10.1073/pnas.95.14.8175; RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., RA Wang Y.-X., Chen S.-J., Chen Z.; RT "Identification of genes expressed in human CD34(+) hematopoietic RT stem/progenitor cells by expressed sequence tags and efficient full- RT length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J., RA Liu M., He F.; RT "Functional prediction of the coding sequences of 121 new genes RT deduced by analysis of cDNA clones from human fetal liver."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Neuroblastoma; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the small mitochondrial proteolipid family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF054175; AAC39909.1; -; mRNA. DR EMBL; AF116639; AAF71062.1; -; mRNA. DR EMBL; BX161388; CAD61878.1; ALT_INIT; mRNA. DR EMBL; BC000429; AAH00429.1; -; mRNA. DR EMBL; BC001944; AAH01944.1; -; mRNA. DR UniGene; Hs.109052; -. DR Ensembl; ENSG00000156411; Homo sapiens. DR KEGG; hsa:9556; -. DR H-InvDB; HIX0012010; -. DR HGNC; HGNC:1188; C14orf2. DR MIM; 604573; gene. DR LinkHub; P56378; -. DR ArrayExpress; P56378; -. DR GermOnline; ENSG00000156411; Homo sapiens. DR RZPD-ProtExp; I0178; -. DR RZPD-ProtExp; IOH3428; -. DR InterPro; IPR012574; Mit_preoteolip. DR Pfam; PF08039; Mit_preoteolip; 1. KW Mitochondrion; Polymorphism. FT CHAIN 1 58 6.8 kDa mitochondrial proteolipid. FT /FTId=PRO_0000064393. FT VARIANT 9 9 I -> V (in dbSNP:rs1053419). FT /FTId=VAR_014526. SQ SEQUENCE 58 AA; 6662 MW; 1B8A63046C0383F6 CRC64; MLQSIIKNIW IPMKPYYTKV YQEIWIGMGL MGFIVYKIRA ADKRSKALKA SAPAPGHH // ID 68MP_MOUSE Reviewed; 58 AA. AC P56379; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 23-JAN-2007, entry version 40. DE 6.8 kDa mitochondrial proteolipid. GN Name=Mp68; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; 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: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the small mitochondrial proteolipid family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK008333; BAB25610.1; -; mRNA. DR EMBL; BC055712; AAH55712.1; -; mRNA. DR EMBL; BC059719; AAH59719.1; -; mRNA. DR UniGene; Mm.318; -. DR Ensembl; ENSMUSG00000021290; Mus musculus. DR KEGG; mmu:70257; -. DR MGI; MGI:1917507; 2010107E04Rik. DR LinkHub; P56379; -. DR ArrayExpress; P56379; -. DR GermOnline; ENSMUSG00000021290; Mus musculus. DR InterPro; IPR012574; Mit_preoteolip. DR Pfam; PF08039; Mit_preoteolip; 1. KW Mitochondrion. FT CHAIN 1 58 6.8 kDa mitochondrial proteolipid. FT /FTId=PRO_0000064394. SQ SEQUENCE 58 AA; 6698 MW; 29778A1393D38DCE CRC64; MFQTLIQKVW VPMKPYYTQV YQEIWVGVGL MSLIVYKIRS ADKRSKALKG PAPAHGHH // ID 6B1_AGRT4 Reviewed; 207 AA. AC P0A3T0; P04031; DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-1986, sequence version 1. DT 31-OCT-2006, entry version 9. DE Protein 6b. GN Name=6b; OS Agrobacterium tumefaciens (strain Ach5). OG Plasmid pTiAch5. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=176298; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84207942; PubMed=6327292; RA Gielen J., de Beuckeleer M., Seurinck J., Deboeck F., de Greve H., RA Lemmers M., van Montagu M., Schell J.; RT "The complete nucleotide sequence of the TL-DNA of the Agrobacterium RT tumefaciens plasmid pTiAch5."; RL EMBO J. 3:835-846(1984). CC -!- FUNCTION: Involved in tumor formation and increases auxin and CC cytokinin effects in host plants. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A04499; QQAG7T. DR InterPro; IPR006064; Glycosidase. DR Pfam; PF02027; RolB_RolC; 1. KW Crown gall tumor; Plasmid. FT CHAIN 1 207 Protein 6b. FT /FTId=PRO_0000064395. SQ SEQUENCE 207 AA; 23451 MW; 00896365CC1D065D CRC64; MTVANWQVRD LTLILRTGEM KSRLEQARTD FGALLSETVY FQPSAIRLGE FDDEYIHSRQ ELVYVYLRED IARQCALRRN LPSNSSNFGT MATAIPPWLM NARSLNRVMQ ERCDQGGLVN YYQGPHTNQF FLAIMPSNCF VRFGTDIINN ENYGFYARGG NYTEEGEDDD DEMDDEGEAG GAEPRECQIG NLINYPIIAL GSCDLSA // ID 6B1_AGRT9 Reviewed; 207 AA. AC P0A3T1; P04031; DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 31-OCT-2006, entry version 9. DE Protein 6b. GN Name=6b; OS Agrobacterium tumefaciens (strain 15955). OG Plasmid pTi15955. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=190386; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Barker R.F., Idler K.B., Thompson D.V., Kemp J.D.; RT "Nucleotide sequence of the T-DNA region from the Agrobacterium RT tumefaciens octopine Ti plasmid pTi15955."; RL Plant Mol. Biol. 2:335-350(1983). CC -!- FUNCTION: Involved in tumor formation and increases auxin and CC cytokinin effects in host plants. CC -!- CAUTION: Ref.1 sequence differs from that shown due to frameshifts CC in positions 156 and 160. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X00493; CAA25172.1; ALT_FRAME; Genomic_DNA. DR InterPro; IPR006064; Glycosidase. DR Pfam; PF02027; RolB_RolC; 1. KW Crown gall tumor; Plasmid. FT CHAIN 1 207 Protein 6b. FT /FTId=PRO_0000064396. SQ SEQUENCE 207 AA; 23448 MW; 9409637EA5568DAC CRC64; MTVANWQVRD LTLILRTGEM KSRLEQARTD FGALLSETVY FQPSAIRLGE FDDEYIHSRQ ELVYVYLRED IARQCALRRN LPSNSSNFGT MATAIPPWLM NARSLNRVMQ ERCDQGGLVN YYQGPHTNQF FLAIMPSNCF VRFGTDIINN ENYGFXARRG NTLEEGEDDD DEMDDEGEAG GAEPRECQIG NLINYPIIAL GSCDLSA // ID 6B1_AGRVI Reviewed; 206 AA. AC Q04551; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 31-OCT-2006, entry version 29. DE Protein 6b. GN Name=6b; OS Agrobacterium vitis (Rhizobium vitis). OG Plasmid pTiS4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=373; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S4; RX MEDLINE=93101133; PubMed=1465104; DOI=10.1007/BF00279373; RA Canaday J., Gerard J.-C., Crouzet P., Otten L.; RT "Organization and functional analysis of three T-DNAs from the RT vitopine Ti plasmid pTiS4."; RL Mol. Gen. Genet. 235:292-303(1992). CC -!- FUNCTION: Involved in tumor formation and increases auxin and CC cytokinin effects in host plants. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M91608; AAA25043.1; -; Genomic_DNA. DR PIR; S30108; S30108. DR InterPro; IPR006064; Glycosidase. DR Pfam; PF02027; RolB_RolC; 1. KW Crown gall tumor; Plasmid. FT CHAIN 1 206 Protein 6b. FT /FTId=PRO_0000064397. SQ SEQUENCE 206 AA; 23077 MW; 9F59C0DB7B69CE21 CRC64; MAVPRWAVRD LTQISSAREL SLRLEQARND FRATVGSICY FNASARTPGQ FDDEYIMTDQ SLTYVYADGV TAQSCAMNRL LPSSSSNFGA AATAIPPWLL DPPRLNRLLR EGTDEGGLVN YYEGPHKNAF FLAIMRSCIF VRPGADEING VSYDFFARSG NYTEQAEEEE EEEEEEEEEE VLDREFQLGN LVSYPIIAWG SCPNSA // ID 6B2_AGRVI Reviewed; 207 AA. AC P25019; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 31-OCT-2006, entry version 30. DE Protein 6b. GN Name=6b; OS Agrobacterium vitis (Rhizobium vitis). OG Plasmid pTiTM4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=373; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=TM4; RX MEDLINE=91329707; PubMed=1868204; RA Bonnard G., Vincent F., Otten L.; RT "Sequence of Agrobacterium tumefaciens biotype III auxin genes."; RL Plant Mol. Biol. 16:733-738(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CG474; RA Otten L., de Ruffray P.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in tumor formation and increases auxin and CC cytokinin effects in host plants. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X56185; CAA39648.1; -; Genomic_DNA. DR EMBL; U83987; AAB41876.1; -; Genomic_DNA. DR PIR; S15451; BWAG6B. DR InterPro; IPR006064; Glycosidase. DR Pfam; PF02027; RolB_RolC; 1. KW Crown gall tumor; Plasmid. FT CHAIN 1 207 Protein 6b. FT /FTId=PRO_0000064398. SQ SEQUENCE 207 AA; 22964 MW; 680FFD61EEEEAFE8 CRC64; MTVANWQVRD FTRILNAGEL QGRLEQARTD FGALLAEIVY FHPPGATPEE GDDEYILTGQ GLVYVYLSEQ TARQCALNRL LPSNSSNFGT VVTAIPPWLM DTQTLNLTLQ ERCDQGGIVN YYHGSRTNEF FLAIMLSNCF VRFGTDEING ASYGFYARRG NYTEEGEDDD NEIGDEGEAG GAEIRDYQFG DLVNYPIVAL GSSRLSA // ID 6DCS_SOYBN Reviewed; 315 AA. AC P26690; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 20-FEB-2007, entry version 46. DE NAD(P)H-dependent 6'-deoxychalcone synthase (EC 2.3.1.170). OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=cv. Harosoy 63; RX MEDLINE=91177016; PubMed=1840523; RA Welle R., Schroeder G., Schiltz E., Grisebach H., Schroeder J.; RT "Induced plant responses to pathogen attack. Analysis and heterologous RT expression of the key enzyme in the biosynthesis of phytoalexins in RT soybean (Glycine max L. Merr. cv. Harosoy 63)."; RL Eur. J. Biochem. 196:423-430(1991). CC -!- FUNCTION: Co-acts with chalcone synthase in formation of 4,2',4'- CC trihydroxychalcone, involved in the biosynthesis of glyceollin CC type phytoalexins. CC -!- CATALYTIC ACTIVITY: 3 malonyl-CoA + 4-coumaroyl-CoA + NADPH = 4 CC CoA + isoliquiritigenin + 3 CO(2) + NADP(+) + H(2)O. CC -!- PATHWAY: Phytoalexins biosynthesis. CC -!- SUBUNIT: Monomer. CC -!- INDUCTION: By pathogen infection. 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; X55730; CAA39261.1; -; mRNA. DR PIR; S14222; S14222. DR UniGene; Gma.11304; -. DR HSSP; P52895; 1J96. DR SMR; P26690; 6-313. DR InterPro; IPR001395; Aldo/ket_red. DR Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR ProDom; PD000288; Aldo/ket_red; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. KW Direct protein sequencing; Flavonoid biosynthesis; NADP; Transferase. FT CHAIN 1 315 NAD(P)H-dependent 6'-deoxychalcone FT synthase. FT /FTId=PRO_0000124609. FT NP_BIND 216 274 NADP (By similarity). FT ACT_SITE 59 59 Proton donor (By similarity). FT BINDING 121 121 Substrate (By similarity). FT SITE 88 88 Lowers pKa of active site Tyr (By FT similarity). SQ SEQUENCE 315 AA; 35490 MW; C3A6BE07EF330F47 CRC64; MAAAIEIPTI VFPNSSAQQR MPVVGMGSAP DFTCKKDTKE AIIEAVKQGY RHFDTAAAYG SEQALGEALK EAIHLGLVSR QDLFVTSKLW VTENHPHLVL PALRKSLKTL QLEYLDLYLI HWPLSSQPGK FSFPIEVEDL LPFDVKGVWE SMEECQKLGL TKAIGVSNFS VKKLQNLLSV ATIRPVVDQV EMNLAWQQKK LREFCKENGI IVTAFSPLRK GASRGPNEVM ENDVLKEIAE AHGKSIAQVS LRWLYEQGVT FVPKSYDKER MNQNLHIFDW ALTEQDHHKI SQISQSRLIS GPTKPQLADL WDDQI // ID 6OMT_COPJA Reviewed; 347 AA. AC Q9LEL6; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-JAN-2007, entry version 36. DE (RS)-norcoclaurine 6-O-methyltransferase (EC 2.1.1.128) (S-adenosyl-L- DE methionine:norcoclaurine 6-O-methyltransferase) (6-OMT). OS Coptis japonica (Japanese goldthread). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Ranunculales; OC Ranunculaceae; Coptis. OX NCBI_TaxID=3442; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=20390108; PubMed=10811648; DOI=10.1074/jbc.M002439200; RA Morishige T., Tsujita T., Yamada Y., Sato F.; RT "Molecular characterization of the S-adenosyl-L-methionine: 3'- RT hydroxy-N-methylcoclaurine 4'O-methyltransferase involved in RT isoquinoline alkaloid biosynthesis in Coptis japonica."; RL J. Biol. Chem. 275:23398-23405(2000). RN [2] RP PROTEIN SEQUENCE OF 88-103, AND CHARACTERIZATION. RX MEDLINE=95010097; PubMed=7925429; RA Sato F., Tsujita T., Katagiri Y., Yoshida S., Yamada Y.; RT "Purification and characterization of S-adenosyl-L-methionine: RT norcoclaurine 6-O-methyltransferase from cultured Coptis japonica RT cells."; RL Eur. J. Biochem. 225:125-131(1994). CC -!- FUNCTION: Catalyzes the transfer of the S-methyl group of S- CC adenosyl-L-methionine (AdoMet) to the 6-hydroxyl group of CC norcoclaurine to form coclaurine. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + (RS)-norcoclaurine = CC S-adenosyl-L-homocysteine + (RS)-coclaurine. CC -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)- CC reticuline from (S)-norcoclaurine: step 1. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D29811; BAB08004.1; -; mRNA. DR HSSP; O24529; 1FP2. DR GO; GO:0030786; F:(RS)-norcoclaurine 6-O-methyltransferase ac...; IEA:EC. DR InterPro; IPR012967; Dimerisation. DR InterPro; IPR001077; O_Met_trans2. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF08100; Dimerisation; 1. DR Pfam; PF00891; Methyltransf_2; 1. KW Direct protein sequencing; Methyltransferase; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 347 (RS)-norcoclaurine 6-O-methyltransferase. FT /FTId=PRO_0000204433. FT ACT_SITE 253 253 Proton acceptor (By similarity). FT BINDING 192 192 S-adenosyl-L-methionine; via carbonyl FT oxygen (By similarity). FT BINDING 215 215 S-adenosyl-L-methionine (By similarity). FT BINDING 235 235 S-adenosyl-L-methionine (By similarity). FT BINDING 236 236 S-adenosyl-L-methionine; via amide FT nitrogen (By similarity). FT BINDING 249 249 S-adenosyl-L-methionine (By similarity). SQ SEQUENCE 347 AA; 38700 MW; 2BC34B3FBE67167C CRC64; MEVKKDNLSS QAKLWNFIYG FAESLVLKCA VQLDLANIIH NSGTSMTLSE LSSRLPSQPV NEDALYRVMR YLVHMKLFTK ASIDGELRYG LAPPAKYLVK GWDKCMVGSI LAITDKDFMA PWHYLKDGLS GESGTAFEKA LGTNIWGYMA EHPEKNQLFN EAMANDSRLI MSALVKECGN IFNGITTLVD VGGGTGTAVR NIANAFPHIK CTVYDLPHVI ADSPGYSEVH CVAGDMFKFI PKADAIMMKC ILHDWDDKEC IEILKRCKEA VPVKGGKVII VDIVLNVQSE HPYTKMRLTL DLDMMLNTGG KERTEEEWKK LIHDAGYKGH KITQITAVQS VIEAYPY // ID 6P21_YEAST Reviewed; 827 AA. AC P40433; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 20-FEB-2007, entry version 67. DE 6-phosphofructo-2-kinase 1 (EC 2.7.1.105) (Phosphofructokinase 2 I) DE (6PF-2-K 1). GN Name=PFK26; OrderedLocusNames=YIL107C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92031513; PubMed=1657152; DOI=10.1021/bi00108a009; RA Kretschmer M., Fraenkel D.G.; RT "Yeast 6-phosphofructo-2-kinase: sequence and mutant."; RL Biochemistry 30:10663-10672(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313266; PubMed=9169870; RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., RA Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., RA Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N., RA Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; RL Nature 387:84-87(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RA Marsischky G., Rolfs A., Richardson A., Kane M., Baqui M., Taycher E., RA Hu Y., Vannberg F., Weger J., Kramer J., Moreira D., Kelley F., RA Zuo D., Raphael J., Hogle C., Jepson D., Williamson J., Camargo A., RA Gonzaga L., Vasconcelos A.T., Simpson A., Kolodner R., Harlow E., RA LaBaer J.; RT "Creation of the YFLEX clone resource: cloning of Saccharomyces RT cerevisiae ORFs in the Gateway recombinational cloning system."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP PARTIAL PROTEIN SEQUENCE. RX MEDLINE=91224128; PubMed=1851090; RA Kretschmer M., Tempst P., Fraenkel D.G.; RT "Identification and cloning of yeast phosphofructokinase 2."; RL Eur. J. Biochem. 197:367-372(1991). RN [5] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-644 AND SER-659, AND RP MASS SPECTROMETRY. RX PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., RA Mann M., Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone RT signaling pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). CC -!- FUNCTION: Synthesis of fructose 2,6-bisphosphate. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D- CC fructose 2,6-bisphosphate. CC -!- ENZYME REGULATION: Phosphorylation results in the activation of CC the kinase activity. CC -!- INTERACTION: CC P11484:SSB1; NbExp=1; IntAct=EBI-1956, EBI-8627; CC -!- MISCELLANEOUS: Present with 1710 molecules/cell. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z38125; CAA86273.1; -; Genomic_DNA. DR EMBL; M80801; AAA34858.1; -; Genomic_DNA. DR EMBL; AY692819; AAT92838.1; -; Genomic_DNA. DR PIR; S48465; S48465. DR HSSP; P07953; 1FBT. DR IntAct; P40433; -. DR Ensembl; YIL107C; Saccharomyces cerevisiae. DR GenomeReviews; Z47047_GR; YIL107C. DR KEGG; sce:YIL107C; -. DR CYGD; YIL107c; -. DR SGD; S000001369; PFK26. DR BioCyc; SCER-S28-01:SCER-S28-01-002966-MONOMER; -. DR LinkHub; P40433; -. DR GermOnline; YIL107C; Saccharomyces cerevisiae. DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR003094; 6Pfruct_kin. DR InterPro; IPR013079; 6Phosfructo_kin. DR InterPro; IPR013078; PG_mutase. DR Pfam; PF01591; 6PF2K; 1. DR Pfam; PF00300; PGAM; 1. DR PRINTS; PR00991; 6PFRUCTKNASE. KW ATP-binding; Complete proteome; Direct protein sequencing; Kinase; KW Nucleotide-binding; Phosphorylation; Transferase. FT CHAIN 1 827 6-phosphofructo-2-kinase 1. FT /FTId=PRO_0000179976. FT NP_BIND 190 197 ATP (Potential). FT ACT_SITE 277 277 Potential. FT ACT_SITE 309 309 Potential. FT ACT_SITE 404 404 Phosphoserine intermediate (By FT similarity). FT ACT_SITE 497 497 Potential. FT ACT_SITE 565 565 Proton donor (By similarity). FT BINDING 343 343 Fructose-6-phosphate (By similarity). FT MOD_RES 644 644 Phosphoserine. FT MOD_RES 659 659 Phosphoserine. FT CONFLICT 382 382 A -> R (in Ref. 1). FT CONFLICT 477 477 G -> E (in Ref. 4). SQ SEQUENCE 827 AA; 93417 MW; 9FA7BCBA08C9F0E3 CRC64; MFKPVDFSET SPVPPDIDLA PTQSPHHVAP SQDSSYDLLS RSSDDKIDAE KGPHDELSKH LPLFQKRPLS DTPISSNWNS PGITEENTPS DSPENSATNL KSLHRLHIND ETQLKNAKIP TNDTTDYMPP SDGANEVTRI DLKDIKSPTR HHKRRPTTID VPGLTKSKTS PDGLISKEDS GSKLVIVMVG LPATGKSFIT NKLSRFLNYS LYYCKVFNVG NTRRKFAKEH GLKDQDSKFF EPKNADSTRL RDKWAMDTLD ELLDYLLEGS GSVGIFDATN TSRERRKNVL ARIRKRSPHL KVLFLESVCS DHALVQKNIR LKLFGPDYKG KDPESSLKDF KSRLANYLKA YEPIEDDENL QYIKMIDVGK KVIAYNIQGF LASQTVYYLL NFNLADRQIW ITRSGESEDN VSGRIGGNSH LTPRGLRFAK SLPKFIARQR EIFYQNLMQQ KKNNENTDGN IYNDFFVWTS MRARTIGTAQ YFNEDDYPIK QMKMLDELSA GDYDGMTYPE IKNNFPEEFE KRQKDKLRYR YPGIGGESYM DVINRLRPVI TELERIEDNV LIITHRVVAR ALLGYFMNLS MGIIANLDVP LHCVYCLEPK PYGITWSLWE YDEASDSFSK VPQTDLNTTR VKEVGLVYNE RRYSVIPTAP PSARSSFASD FLSRKRSNPT SASSSQSELS EQPKNSVSAQ TGSNNTTLIG SNFNIKNENG DSRIPLSAPL MATNTSNNIL DGGGTSISIH RPRVVPNQNN VNPLLANNNK AASNVPNVKK SAATPRQIFE IDKVDEKLSM LKNKSFLLHG KDYPNNADNN DNEDIRAKTM NRSQSHV // ID 6P22_YEAST Reviewed; 397 AA. AC Q12471; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-FEB-2007, entry version 45. DE 6-phosphofructo-2-kinase 2 (EC 2.7.1.105) (Phosphofructokinase 2 II) DE (6PF-2-K 2). GN Name=PFK27; OrderedLocusNames=YOL136C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=WA-1A; RX MEDLINE=97014370; PubMed=8861205; RA Boles E., Goehlmann H.W.H., Zimmermann F.K.; RT "Cloning of a second gene encoding 5-phosphofructo-2-kinase in yeast, RT and characterization of mutant strains without fructose-2,6- RT bisphosphate."; RL Mol. Microbiol. 20:65-76(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97051593; PubMed=8896270; RX DOI=10.1002/(SICI)1097-0061(199609)12:10B<1053::AID-YEA993>3.3.CO;2-J; RA Aldea M., Piedrafita L., Casas C., Casamayor A., Khalid H., RA Balcells L., Arino J., Herrero E.; RT "Sequence analysis of a 12 801 bp fragment of the left arm of yeast RT chromosome XV containing a putative 6-phosphofructo-2-kinase gene, a RT gene for a possible glycophospholipid-anchored surface protein and six RT other open reading frames."; RL Yeast 12:1053-1058(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97313270; PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., RA Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., RA Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., RA Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., RA Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., RA Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., RA Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., RA Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., RA Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., RA Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., RA Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., RA Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., RA Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., RA Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., RA Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). CC -!- FUNCTION: Synthesis of fructose 2,6-bisphosphate. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D- CC fructose 2,6-bisphosphate. CC -!- INDUCTION: By glucose and fructose, but not by galactose or CC maltose. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X90861; CAA62371.1; -; Genomic_DNA. DR EMBL; Z74878; CAA99157.1; -; Genomic_DNA. DR EMBL; X95465; CAA64733.1; -; Genomic_DNA. DR PIR; S61066; S61066. DR DIP; DIP:958N; -. DR IntAct; Q12471; -. DR Ensembl; YOL136C; Saccharomyces cerevisiae. DR GenomeReviews; Y13140_GR; YOL136C. DR KEGG; sce:YOL136C; -. DR CYGD; YOL136c; -. DR SGD; S000005496; PFK27. DR BioCyc; SCER-S28-01:SCER-S28-01-005419-MONOMER; -. DR LinkHub; Q12471; -. DR GermOnline; YOL136C; Saccharomyces cerevisiae. DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IMP:SGD. DR GO; GO:0006110; P:regulation of glycolysis; IMP:SGD. DR InterPro; IPR013079; 6Phosfructo_kin. DR Pfam; PF01591; 6PF2K; 1. KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Transferase. FT CHAIN 1 397 6-phosphofructo-2-kinase 2. FT /FTId=PRO_0000179977. FT NP_BIND 103 110 ATP (Potential). FT REGION 85 305 6-phosphofructo-2-kinase. FT ACT_SITE 197 197 Potential. FT ACT_SITE 235 235 Potential. FT BINDING 269 269 Fructose-6-phosphate (By similarity). SQ SEQUENCE 397 AA; 45318 MW; F8A36E8BE135A55C CRC64; MGGSSDSDSH DGYLTSEYNS SNSLFSLNTG NSYSSASLDR ATLDCQDSVF FDNHKSSLLS TEVPRFISND PLHLPITLNY KRDNADPTYT NGKVNKFMIV LIGLPATGKS TISSHLIQCL KNNPLTNSLR CKVFNAGKIR RQISCATISK PLLLSNTSSE DLFNPKNNDK KETYARITLQ KLFHEINNDE CDVGIFDATN STIERRRFIF EEVCSFNTDE LSSFNLVPII LQVSCFNRSF IKYNIHNKSF NEDYLDKPYE LAIKDFAKRL KHYYSQFTPF SLDEFNQIHR YISQHEEIDT SLFFFNVINA GVVEPHSLNQ SHYPSTCGKQ IRDTIMVIEN FINHYSQMFG FEYIEAVKLF FESFGNSSEE TLTTLDSVVN DKFFDDLQSL IESNGFA // ID 6PGD1_YEAST Reviewed; 489 AA. AC P38720; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 20-FEB-2007, entry version 59. DE 6-phosphogluconate dehydrogenase, decarboxylating 1 (EC 1.1.1.44). GN Name=GND1; OrderedLocusNames=YHR183W; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Desouza M., Lobo Z., Maitra P.K.; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=94378003; PubMed=8091229; RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., RA Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., RA Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., RA Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., RA Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., RA Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., RA Vaudin M.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT VIII."; RL Science 265:2077-2082(1994). RN [3] RP PROTEIN SEQUENCE OF 41-47 AND 120-131. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=95203288; PubMed=7895733; RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., RA Volpe T., Warner J.R., McLaughlin C.S.; RT "Protein identifications for a Saccharomyces cerevisiae protein RT database."; RL Electrophoresis 15:1466-1486(1994). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). 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. CC -!- INTERACTION: CC P02829:HSP82; NbExp=1; IntAct=EBI-1965, EBI-8659; CC P33203:PRP40; NbExp=1; IntAct=EBI-1965, EBI-701; CC P39940:RSP5; NbExp=1; IntAct=EBI-1965, EBI-16219; CC P40318:SSM4; NbExp=1; IntAct=EBI-1965, EBI-18208; CC Q06525:YPR152C; NbExp=1; IntAct=EBI-1965, EBI-35138; CC -!- MISCELLANEOUS: Present with 101000 molecules/cell. 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; Z46631; CAA86600.1; -; Genomic_DNA. DR EMBL; U00028; AAB68452.1; -; Genomic_DNA. DR EMBL; U17155; AAA53637.1; -; Genomic_DNA. DR PIR; S46671; S46671. DR HSSP; P00349; 2PGD. DR DIP; DIP:6604N; -. DR IntAct; P38720; -. DR Ensembl; YHR183W; Saccharomyces cerevisiae. DR GenomeReviews; U00093_GR; YHR183W. DR KEGG; sce:YHR183W; -. DR CYGD; YHR183w; -. DR SGD; S000001226; GND1. DR BioCyc; SCER-S28-01:SCER-S28-01-002818-MONOMER; -. DR LinkHub; P38720; -. DR GermOnline; YHR183W; Saccharomyces cerevisiae. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IMP:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IGI:SGD. DR GO; GO:0006979; P:response to oxidative stress; IMP:SGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Direct protein sequencing; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 489 6-phosphogluconate dehydrogenase, FT decarboxylating 1. FT /FTId=PRO_0000090075. SQ SEQUENCE 489 AA; 53543 MW; 55CAE5DACDC6A00B CRC64; MSADFGLIGL AVMGQNLILN AADHGFTVCA YNRTQSKVDH FLANEAKGKS IIGATSIEDF ISKLKRPRKV MLLVKAGAPV DALINQIVPL LEKGDIIIDG GNSHFPDSNR RYEELKKKGI LFVGSGVSGG EEGARYGPSL MPGGSEEAWP HIKNIFQSIS AKSDGEPCCE WVGPAGAGHY VKMVHNGIEY GDMQLICEAY DIMKRLGGFT DKEISDVFAK WNNGVLDSFL VEITRDILKF DDVDGKPLVE KIMDTAGQKG TGKWTAINAL DLGMPVTLIG EAVFARCLSA LKNERIRASK VLPGPEVPKD AVKDREQFVD DLEQALYASK IISYAQGFML IREAAATYGW KLNNPAIALM WRGGCIIRSV FLGQITKAYR EEPDLENLLF NKFFADAVTK AQSGWRKSIA LATTYGIPTP AFSTALSFYD GYRSERLPAN LLQAQRDYFG AHTFRVLPEC ASDNLPVDKD IHINWTGHGG NVSSSTYQA // ID 6PGD2_BACSU Reviewed; 469 AA. AC P80859; P54546; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 20-FEB-2007, entry version 52. DE 6-phosphogluconate dehydrogenase, decarboxylating 2 (EC 1.1.1.44) DE (GNTZII). GN Name=yqjI; OrderedLocusNames=BSU23860; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / JH642; RX MEDLINE=97124195; PubMed=8969508; RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., RA Kobayashi Y.; RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of RT the Bacillus subtilis genome containing the skin element and many RT sporulation genes."; RL Microbiology 142:3103-3111(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [3] RP SEQUENCE REVISION. RX MEDLINE=20036940; PubMed=10568751; DOI=10.1101/gr.9.11.1116; RA Medigue C., Rose M., Viari A., Danchin A.; RT "Detecting and analyzing DNA sequencing errors: toward a higher RT quality of the Bacillus subtilis genome sequence."; RL Genome Res. 9:1116-1127(1999). RN [4] RP PROTEIN SEQUENCE OF 2-14. RC STRAIN=168 / IS58; RX MEDLINE=97443988; PubMed=9298659; RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.; RT "First steps from a two-dimensional protein index towards a response- RT regulation map for Bacillus subtilis."; RL Electrophoresis 18:1451-1463(1997). 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. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. CC -!- CAUTION: Ref.1 (BAA12615) sequence differs from that shown due to CC a frameshift in position 42. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D84432; BAA12615.1; ALT_FRAME; Genomic_DNA. DR EMBL; Z99116; CAB14318.2; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR GenomeReviews; AL009126_GR; BSU23860. DR KEGG; bsu:BG11738; -. DR SubtiList; BG11738; yqjI. DR BioCyc; MetaCyc:MONOMER-6842; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Direct protein sequencing; Gluconate utilization; KW NADP; Oxidoreductase; Pentose shunt. FT INIT_MET 1 1 Removed. FT CHAIN 2 469 6-phosphogluconate dehydrogenase, FT decarboxylating 2. FT /FTId=PRO_0000090027. FT CONFLICT 11 11 L -> W (in Ref. 4). FT CONFLICT 62 62 Q -> E (in Ref. 1). SQ SEQUENCE 469 AA; 51775 MW; D0A94E0B4F2250EF CRC64; MSKQQIGVIG LAVMGKNLAL NIESRGFSVS VYNRSSSKTE EFLQEAKGKN VVGTYSIEEF VQSLETPRKI LLMVKAGTAT DATIQSLLPH LEKDDILIDG GNTYYKDTQR RNKELAESGI HFIGTGVSGG EEGALKGPSI MPGGQKEAHE LVKPILEAIS AKVDGEPCTT YIGPDGAGHY VKMVHNGIEY GDMQLISESY FILKQVLGLS ADELHEVFAE WNKGELDSYL IEITADIFTK KDEETGKPLV DVILDKAGQK GTGKWTSQSA LDLGVPLPII TESVFARFIS AMKEERVKAS GLLSGPEVKP VTENKEELIE AVRKALFMSK ICSYAQGFAQ MKAASEEYNW DLKYGEIAMI FRGGCIIRAA FLQKIKEAYD REPELDNLLL DSYFKNIVES YQGALRQVIS LAVAQGVPVP SFSSALAYYD SYRTAVLPAN LIQAQRDYFG AHTYERTDKE GIFHTEWMK // ID 6PGD2_YEAST Reviewed; 492 AA. AC P53319; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 58. DE 6-phosphogluconate dehydrogenase, decarboxylating 2 (EC 1.1.1.44). GN Name=GND2; OrderedLocusNames=YGR256W; ORFNames=G9170; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=97279233; PubMed=9133741; RX DOI=10.1002/(SICI)1097-0061(19970330)13:4<369::AID-YEA81>3.3.CO;2-M; RA Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., RA Frontali L.; RT "Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome RT VII reveals the presence of three new open reading frames and of a RT tRNAThr gene."; RL Yeast 13:369-372(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=97313265; PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., RA Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., RA Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., RA Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., RA Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., RA Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., RA Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., RA Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., RA Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., RA Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., RA Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., RA Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., RA Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., RA Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., RA Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., RA Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., RA Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., RA Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., RA Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., RA van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., RA Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., RA Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., RA Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RA Marsischky G., Rolfs A., Richardson A., Kane M., Baqui M., Taycher E., RA Hu Y., Vannberg F., Weger J., Kramer J., Moreira D., Kelley F., RA Zuo D., Raphael J., Hogle C., Jepson D., Williamson J., Camargo A., RA Gonzaga L., Vasconcelos A.T., Simpson A., Kolodner R., Harlow E., RA LaBaer J.; RT "Creation of the YFLEX clone resource: cloning of Saccharomyces RT cerevisiae ORFs in the Gateway recombinational cloning system."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). 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. CC -!- MISCELLANEOUS: Present with 556 molecules/cell. 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; X99228; CAA67612.1; -; Genomic_DNA. DR EMBL; Z73041; CAA97285.1; -; Genomic_DNA. DR EMBL; AY692811; AAT92830.1; -; Genomic_DNA. DR PIR; S64588; S64588. DR HSSP; P00349; 2PGD. DR DIP; DIP:6605N; -. DR IntAct; P53319; -. DR Ensembl; YGR256W; Saccharomyces cerevisiae. DR GenomeReviews; Y13135_GR; YGR256W. DR KEGG; sce:YGR256W; -. DR CYGD; YGR256w; -. DR SGD; S000003488; GND2. DR BioCyc; SCER-S28-01:SCER-S28-01-002532-MONOMER; -. DR LinkHub; P53319; -. DR GermOnline; YGR256W; Saccharomyces cerevisiae. DR GO; GO:0005829; C:cytosol; TAS:SGD. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IMP:SGD. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IGI:SGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 492 6-phosphogluconate dehydrogenase, FT decarboxylating 2. FT /FTId=PRO_0000090076. SQ SEQUENCE 492 AA; 53923 MW; 3D75D53563987735 CRC64; MSKAVGDLGL VGLAVMGQNL ILNAADHGFT VVAYNRTQSK VDRFLANEAK GKSIIGATSI EDLVAKLKKP RKIMLLIKAG APVDTLIKEL VPHLDKGDII IDGGNSHFPD TNRRYEELTK QGILFVGSGV SGGEDGARFG PSLMPGGSAE AWPHIKNIFQ SIAAKSNGEP CCEWVGPAGS GHYVKMVHNG IEYGDMQLIC EAYDIMKRIG RFTDKEISEV FDKWNTGVLD SFLIEITRDI LKFDDVDGKP LVEKIMDTAG QKGTGKWTAI NALDLGMPVT LIGEAVFARC LSAIKDERKR ASKLLAGPTV PKDAIHDREQ FVYDLEQALY ASKIISYAQG FMLIREAARS YGWKLNNPAI ALMWRGGCII RSVFLAEITK AYRDDPDLEN LLFNEFFASA VTKAQSGWRR TIALAATYGI PTPAFSTALA FYDGYRSERL PANLLQAQRD YFGAHTFRIL PECASAHLPV DKDIHINWTG HGGNISSSTY QA // ID 6PGD9_ECOLI Reviewed; 468 AA. AC P37754; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 09-JAN-2007, entry version 41. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=O9:K30:H12 / E69; RX MEDLINE=94252978; PubMed=7515042; RA Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N., RA Whitfield C.; RT "Cloning and analysis of duplicated rfbM and rfbK genes involved in RT the formation of GDP-mannose in Escherichia coli O9:K30 and RT participation of rfb genes in the synthesis of the group I K30 RT capsular polysaccharide."; RL J. Bacteriol. 176:3126-3139(1994). 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. 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; L27646; AAA21136.1; -; Genomic_DNA. DR PIR; I41250; I41250. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090038. SQ SEQUENCE 468 AA; 51625 MW; C13D94CFD78BFF3A CRC64; MSKQQIGVVG MAVMGRNLAL NIESRGYTVS VFNRSREKTE EVIAENPGKK LVPYYTVQEF VESLETPRRI LLMVKAGSGT DSAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILKQIA AVAEDGEPCV TYIGADGAGH YVKMVHNGIE YGDMQLIAEA YALLKGGLTL SNEELAQTFT EWNEGELSSY LYDITKDIFT KKDEEGKYLV DVILDEAANK GTGKWTSQSS LDLGEPLSLI TESVFPRYIS SLKDQRVAAS KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASDEYNWE LNYAEIAKIF RAGCIIRAQF LQKITDAYAQ NAGIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIRVPT FSAAIAYYDS YRSAVLPANL IQAQRDYFGA HTYKRTDKEG VFHTEWLE // ID 6PGD_ACTAC Reviewed; 484 AA. AC P70718; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 23-JAN-2007, entry version 40. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OS Actinobacillus actinomycetemcomitans (Haemophilus OS actinomycetemcomitans). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=714; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43718 / FDC Y4 / Serotype b; RX MEDLINE=97148607; PubMed=9020051; DOI=10.1006/bbrc.1996.5917; RA Yoshida Y., Nakano Y., Yamashita Y., Koga T.; RT "The gnd gene encoding a novel 6-phosphogluconate dehydrogenase and RT its adjacent region of Actinobacillus actinomycetemcomitans RT chromosomal DNA."; RL Biochem. Biophys. Res. Commun. 230:220-225(1997). 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. 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; D88189; BAA13558.1; -; Genomic_DNA. DR PIR; JC5282; JC5282. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 484 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090024. SQ SEQUENCE 484 AA; 53289 MW; F7BD0B2EA3BF624D CRC64; MSVKGDIGVI GLAVMGQNLI LNMNDHGFKV VAYNRTTSKV DEFLEGAAKG TNIIGAYSLE DLANKLEKPR KVMLMVRAGE VVDHFIDALL PHLEAGDIII DGGNSNYPDT NRRVAALREK GIRFIGTGVS GGEEGARHGP SIMPGGNEEA WQFVKPVLQA ISAKTEQGEP CCDWVGKDGA GHFVKMVHNG IEYGDMQLIC EAYQFLKEGV GLSDDELQAT FNEWRNTELD SYLIDITADI LGYKDADGSR LVDKVLDTAG QKGTGKWTGI NALDFGIPLT LITESVFARC VSAFKDQRVA ASKLFHKTIG KVEGDKKVWI EAVRKALLAS KIISYAQGFM LIREASEHFN WNINYGNTAL LWREGCIIRS RFLGNIRDAY EANPDLIFLG SDSYFKGILE NAMSDWRKVV AKSIEVGIPM PCMASAITFL DGYTSARLPA NLLQAQRDYF GAHTYERTDK PRGEFFHTNW TGRGGNTAST TYDV // ID 6PGD_BACLI Reviewed; 467 AA. AC P52207; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 09-JAN-2007, entry version 40. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gntZ; OS Bacillus licheniformis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1402; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BGSC5A2; RX MEDLINE=96051988; PubMed=8535972; DOI=10.1093/dnares/1.4.157; RA Yoshida K., Seki S., Fujita Y.; RT "Nucleotide sequence and features of the Bacillus licheniformis gnt RT operon."; RL DNA Res. 1:157-162(1994). 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. 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; D31631; BAA06504.1; -; Genomic_DNA. DR PIR; JC2306; JC2306. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 467 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090025. SQ SEQUENCE 467 AA; 51642 MW; 3F14CFF0320D8E52 CRC64; MRNTIGVIGL GVMGSNIALN MASKGEQVAV YNYTRDLTDQ LVQKTGGQTV KPYYELEDFV QSLEKPRKIF LMVTAGKPVD SVIDSLVPLL EEGDVIMDGG NSHYEDTERR YDSLKAKGIG YLGIGISGGE VGALKGPSIM PGGDRDVYEK AAPILTKIAA QVEGDPCCVY IGPKGAGHFV KMVHNGIEYA DMQLIAEAYT FLREKLLLPI DEIADIFDTW NQGELKSYLI EITAEILRKK DERTGAPLID VILDKTGQKG TGKWTSLQAI DNGIPSSIIT ESLFARYLSS LKDERTAAEN VLAGPETEER PLDQNVWIDR VRQALYMGKV CAYAQGFAQY KMTSDLNGWH LPLKDIALIF RGGCIIRAQF LNLISEVYDK QPDLSNLLVA PDFAEKLKEY QSGLRKVVCE GISSGISFPC LSTALSYYDG YRTGRSNANL LQAQANYFGA HTYERTDMEG VFHTDWY // ID 6PGD_BACSU Reviewed; 468 AA. AC P12013; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 09-JAN-2007, entry version 58. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gntZ; OrderedLocusNames=BSU40080; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87008613; PubMed=3020045; RA Fujita Y., Fujita T., Miwa Y., Nihashi J., Aratani Y.; RT "Organization and transcription of the gluconate operon, gnt, of RT Bacillus subtilis."; RL J. Biol. Chem. 261:13744-13753(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / BGSC1A1; RX MEDLINE=96093926; PubMed=7584049; DOI=10.1093/dnares/2.2.61; RA Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.; RT "Cloning and sequencing of a 36-kb region of the Bacillus subtilis RT genome between the gnt and iol operons."; RL DNA Res. 2:61-69(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 460-468. RC STRAIN=168; RA Kasahara Y., Nakai S., Yoshikawa H., Ogasawara N.; RT "36kb sequence between gntZ and trnY of B. subtilis genome."; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP PROBABLE FUNCTION. RX MEDLINE=92065803; PubMed=1659648; RA Reizer A., Deutscher J., Saier M.H. Jr., Reizer J.; RT "Analysis of the gluconate (gnt) operon of Bacillus subtilis."; RL Mol. Microbiol. 5:1081-1089(1991). 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. 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; J02584; AAA56927.1; -; Genomic_DNA. DR EMBL; AB005554; BAA21576.1; -; Genomic_DNA. DR EMBL; Z99124; CAB16045.1; -; Genomic_DNA. DR EMBL; D78193; BAA11267.1; -; Genomic_DNA. DR PIR; D26190; D26190. DR HSSP; P00349; 2PGD. DR GenomeReviews; AL009126_GR; BSU40080. DR KEGG; bsu:BG10651; -. DR SubtiList; BG10651; gntZ. DR BioCyc; BSUB1423:BSU4005-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090026. SQ SEQUENCE 468 AA; 51983 MW; 56D88BEB8E553856 CRC64; MFNSIGVIGL GVMGSNIALN MANKGENVAV YNYTRDLTDQ LIQKLDGQSL SPYYELEDFV QSLEKPRKIF LMVTAGKPVD SVIQSLKPLL EEGDVIMDGG NSHYEDTERR YDELKEKGIG YLGVGISGGE VGALTGPSIM PGGDRDVYEK AAPILTKIAA QVGDDPCCVY IGPKGAGHFT KMVHNGIEYA DMQLIAEAYT FLRETLRLPL DEIASIFETW NQGELKSYLI EITAEILRKK DEKTGQPLID VILDKTGQKG TGKWTSMQAI DNGIPSTIIT ESLFARYLSS LKEERMAAQD VLAGPEAEEK HLDKDTWIEY VRQALYMGKV CAYAQGFAQY KMSSELYGWN LPLKDIALIF RGGCIIRADF LNVISEAFSE QPNLANLLIA PYFTDKLHAY QTGLRKVVCE GISTGISFPC LTTALSYYDG YRTGRSNANL LQAQRDYFGA HTYERTDMDG VFHTNWSE // ID 6PGD_BUCAI Reviewed; 468 AA. AC P57208; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 09-JAN-2007, entry version 37. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=BU107; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum OS symbiotic bacterium). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=118099; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tokyo 1998; RX MEDLINE=20445173; PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids RT Buchnera sp. APS."; RL Nature 407:81-86(2000). 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. 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; BA000003; BAB12826.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR GenomeReviews; BA000003_GR; BU107. DR KEGG; buc:BU107; -. DR BioCyc; BSP107806:BU107-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090028. SQ SEQUENCE 468 AA; 53574 MW; 3317FDDF8F3EF20A CRC64; MSRQQIGVVG MAVMGRNLAL NIESKNYSVS IFNRTRSVTE EVFNQNKKKN IVPYFSIKDF IDSLLKPRCI LLMVQSGKAT DETIKMILPY LEKEDILIDA GNTFYKDTIR RNEKLSKYEI NFIGMGVSGG ELGALNGPSI MPGGQKEAYK LVLPMLEKIS AKFKGEPCVS YIGPNGAGHY VKMVHNGIEY GDMQLISESY FLLKYLLNMS NEELSSTFSK WNKGELNSYL IEITKNIFIE KDEKGKYLID RILDVAEDKG TGKWISKSAL DLREPLSLIT ESVFARYLSS LKRQRIIASK ILQGPKIKTF IKDKNSFIEE VRRALYLGKI ISYAQGFSQL KRASEKYHWN LKYGEIAKIF RAGCIIRANF LQKITDEYTQ NKNVVNLLLT PYFSKIANEY ENSLRNIVMY AIKYGISTPT FSAAISYYDS YRALYLPANL IQAQRDYFGS HTYQRTDQTG YFHTNWSQ // ID 6PGD_BUCAP Reviewed; 473 AA. AC Q9ZHD9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2002, sequence version 2. DT 09-JAN-2007, entry version 48. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=BUsg_100; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=98440331; PubMed=9767718; DOI=10.1007/s002849900392; RA Clark M.A., Baumann L., Baumann P.; RT "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding RT enzymes of histidine biosynthesis."; RL Curr. Microbiol. 37:356-358(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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. 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; AF067228; AAC97362.1; -; Genomic_DNA. DR EMBL; AE013218; AAM67670.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR GenomeReviews; AE013218_GR; BUsg_100. DR KEGG; bas:BUsg100; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 473 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090029. FT CONFLICT 158 158 K -> N (in Ref. 1). FT CONFLICT 324 326 RRA -> TKS (in Ref. 1). FT CONFLICT 348 348 K -> I (in Ref. 1). SQ SEQUENCE 473 AA; 53805 MW; A11842A037E1E984 CRC64; MLKQQVGVIG MAVMGRNLAL NIESKKYTVS IFNRTQSVTE EVINNNKEKK IFPYFSIKDF VNSLRKPRCI LLMVKSGQPT DETIQFILPY LNKGDILIDG GNTFYKDSIR RSNDLMKCGI NFIGMGVSGG ELGALNGPSI MPGGSREAYD LVSSMLKKIS AKFKNEPCVS YIGPNGAGHY VKMIHNGIEY GDMQLISESY FILKNVLNMK NEELSNTFSQ WNKGELNSYL IEITKNIFLK KEKDGIHYLI DSILDHAEDK GTGKWISQDA LELHEPLSLI TESVFARYLS SLKDQRLIAS KILKGPILKC ISSQNKELFV EEVRRALYLG KIISYAQGFS QLKKASEKYS WNLQYGKIAK IFRAGCIIRA DFLERITDAF KSNNVTNLLL TPYFSEISNK YEKSLRYITS YAIKYGIPVP TFASAISYYD NYRTMSSSAN LIQAQRDYFG AHTYRRTDKK GYFHTNWLTK KEL // ID 6PGD_BUCBP Reviewed; 468 AA. AC Q89AX5; DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2003, sequence version 1. DT 09-JAN-2007, entry version 31. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=bbp_101; OS Buchnera aphidicola subsp. Baizongia pistaciae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=135842; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22426901; PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). 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. 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; AE016826; AAO26836.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR GenomeReviews; AE016826_GR; bbp_101. DR KEGG; bab:bbp101; -. DR BioCyc; BAPH224915:BBP101-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090030. SQ SEQUENCE 468 AA; 52646 MW; C28B8C09CCB64E11 CRC64; MAKQQIGVIG MAVMGRNLAL NMERNQYTVS IFNRSLDITE KIILNNPNKN LFPFFSIKDF VLSLIVPRCI VLMIKSGVAT DDTIKSLIPY LSKGDIIIDG GNTFYKDTIQ RGYELLKIGV NLIGAGFSGG EKGALYGPSI MPGGRQEAYN YVSPILKKIA SNSEGIPCVT YIGPDGSGHY VKMVHNGIEY GDMQLIAESY FILKTLLRLD NQSISKIFDI WNQGELNSYL IDITKDILIK KDDQNNYLID CILDEGSSKG TGTWTTKSAL DLNEPLTLIT ESVFFRYLSS LKSQRLLASK ILCGPKDFFI VLNRDDFIEK IRQALYLGKI ISYAQGFSQL NSASQKYNWN LKLGEISRIF QSGCIIRAKL LKNITQEYSS NNNFVNLLLT PYFREIANTY HSSLREIVSI SVKYGIPIPA LSSAISYFDS YRSAFLPSNL IQAQRDFFGA HTYKRIDKSG IFHTNWYS // ID 6PGD_CAEEL Reviewed; 484 AA. AC Q17761; Q22772; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 2. DT 09-JAN-2007, entry version 48. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN ORFNames=T25B9.9; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). 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. 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; Z70311; CAA94380.1; -; Genomic_DNA. DR EMBL; Z70306; CAA94380.1; JOINED; Genomic_DNA. DR EMBL; Z70306; CAA94326.1; -; Genomic_DNA. DR EMBL; Z70311; CAA94326.1; JOINED; Genomic_DNA. DR PIR; T19020; T19020. DR UniGene; Cel.6711; -. DR HSSP; P00349; 2PGD. DR Ensembl; T25B9.9; Caenorhabditis elegans. DR KEGG; cel:T25B9.9; -. DR WormBase; WBGene00012015; T25B9.9. DR WormPep; T25B9.9; CE06508. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 484 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090067. SQ SEQUENCE 484 AA; 53196 MW; D3CF6F1065F17535 CRC64; MAEADIAVIG LAVMGQNLIL NMNDHGFTVC AFNRTVKLVD DFLANEAKGT KIIGAHSIEE MCKKLKRPRR VMMLIKAGTP VDMMIDAIVP HLEEGDIIID GGNSEYTDSN RRSEQLAAKG IMFVGCGVSG GEEGARFGPS LMPGGNPKAW PHLKDIFQKI AAKSNGEPCC DWVGNAGSGH FVKMVHNGIE YGDMQLIAEA YHLLSKAVEL NHDQMAEVLD DWNKGELESF LIEITANILK YRDEQGEPIV PKIRDSAGQK GTGKWTCFAA LEYGLPVTLI GEAVFARCLS ALKDERVRAS KQLPRPQVSP DTVVQDKRVF IKQISKALYA SKIVSYAQGF MLLAEASKQF NWNLNFGAIA LMWRGGCIIR SRFLGDIEHA FQKNKQLSNL LLDDFFTKAI TEAQDSWRVV VCAAVRLGIP VPAFSSALAF YDGYTSEVVP ANLLQAQRDY FGAHTYELLA KPGTWVHTNW TGTGGRVTSN AYNA // ID 6PGD_CANAL Reviewed; 517 AA. AC O13287; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 09-JAN-2007, entry version 36. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=DOR14; OS Candida albicans (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5476; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 10259 / CBS 5796 / IFO 1060 / JCM 2078; RA Watanabe M., Ishii N., Arisawa M., Aoki Y.; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. 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. 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; AB006102; BAA21690.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 517 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090072. SQ SEQUENCE 517 AA; 56924 MW; 91E3F520FFCABF7A CRC64; MKNFNALSRL SILSKQLSFN NTNSSIARGD IGLIGLAVMG QNLILNMADH GYTVVAYNRT TAKVDRFLEN EAKGKSILGA HSIKELVDQL KRPRRIMLLV KAGAPVDEFI NQLLPYLEEG DIIIDGGNSH FPDSNRRYEE LAKKGILFVG SGVSGGEEGA RTGPSLMPGG NEKAWPHIKE IFQDVAAKSD GEPCCDWVGD AGAGHYVKMV HNGIEYGDMQ LICEAYDLMK RVGKFEDKEI GDVFATWNKG VLDSFLIEIT RDILYYNDPT DGKPLVEKIL DTAGQKGTGK WTAVNALDLG IPVTLIGEAV FSRCLSAMKA ERVEASKALK GPQVTGESPI TDKKQFIDDL EQALYASKII SYTQGFMLMN QAAKDYGWKL NNAGIALMWR GGCIIRSVFL AEITAAYRKK PDLENLLLYP FFNDAITKAQ SGWRASVGKA IQYGIPTPAF STALAFYDGL RSERLPANLL QAQRDYFGAH TFKVLPGQEN ELLKKDEWIH INWTGRGGDV SSTTYDA // ID 6PGD_CERCA Reviewed; 481 AA. AC P41570; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 40. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=Pgd; OS Ceratitis capitata (Mediterranean fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Tephritoidea; Tephritidae; Ceratitis. OX NCBI_TaxID=7213; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94093871; PubMed=8269100; RA Scott M.J., Kriticou D., Robinson A.S.; RT "Isolation of cDNAs encoding 6-phosphogluconate dehydrogenase and RT glucose-6-phosphate dehydrogenase from the mediterranean fruit fly RT Ceratitis capitata: correlating genetic and physical maps of RT chromosome 5."; RL Insect Mol. Biol. 1:213-222(1993). 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. 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; S67873; AAB29396.1; -; mRNA. DR HSSP; P00349; 2PGD. DR SMR; P41570; 3-472. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 481 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090068. SQ SEQUENCE 481 AA; 52964 MW; F0ABB506AD1B86D0 CRC64; MSAKADIALI GLAVMGQNLV LNMNDKGFVV CAYNRTVEKV NQFLKNEAKG TNVIGATSLQ DMVNKLKLPR KIMLLVKAGS AVDDFIQQLV PLLSPGDVII DGGNSEYQDT ARRCDELRAK KILYVGSGVS GGEEGARHGP SLMPGGHPEA WPLIQPIFQS ICAKADKEPC CEWVGEGGAG HFVKMVHNGI EYGDMQLICE AYQIMKALGL SQAEMATEFE KWNSEELDSF LIEITRDILN YQDDRGYLLE RIRDTAGQKG TGKWTAISAL QYGVPVTLIG EAVFSRCLSA LKDERVAASK QLKGPNVNAK VEDLPKFLNH IKHALYCSKI VSYAQGFMLM REAAKENNWN LNYGGIALMW RGGCIIRSVF LGNIKDAYTR NPQLSNLLLD DFFKKAIEVG QNSWRQVVAN AFLWGIPVPA LSTALSFYDG YRTEKLPANL LQAQRDYFGA HTYELLGAEG KFVHTNWTGT GGNVSASTYQ A // ID 6PGD_CHLMU Reviewed; 479 AA. AC Q9PKX7; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-JAN-2007, entry version 39. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=TC_0333; OS Chlamydia muridarum. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=83560; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MoPn / Nigg; RX MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., RA White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., RA Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., RA Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., RA McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia RT pneumoniae AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). 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. 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; AE002160; AAF39196.1; -; Genomic_DNA. DR PIR; A81714; A81714. DR HSSP; P00349; 2PGD. DR GenomeReviews; AE002160_GR; TC_0333. DR KEGG; cmu:TC0333; -. DR TIGR; TC_0333; -. DR BioCyc; CMUR83560:TC0333-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 479 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090031. SQ SEQUENCE 479 AA; 52689 MW; 3501DD6DAA0B8F8B CRC64; MAPADIGLIG LAVMGKNLVL NMIDHGFAVS VYNRSPEKTE EFLKEHGENI SLQGFTAIEE FVQSLKRPRK IMIMIKAGAP VDEMISSLLP FLEEGDILID GGNSYYLDSE RRYIDLKKKG ILFVGMGVSG GEEGARKGPS IMPGGNIEAW PVIAPIFQSI AAQVDGQPCC SWIGTGGAGH FVKAVHNGIE YGDIQLICET YEILKSRLDL SLEQIGNIFF EWNQTDLNSY LMGASAAVLT AKDENGVAVA STILDVAGQK GTGRWVAEDA IKAGVPMSLI IESVLARYLS AWKEVRRQAA REFPVASLLY QPSQEASVLI EDAREALYAA KIISYAQGFM LLKQISEERN WDLNLGELAL IWRGGCIIQS AFLDKIHQGF ESCPDAHSLM LQDYFKNVLL NSETGFRRAI LHAVGAGVAI PCLASALAFY DGYRTENSPL FLVQGLRDYF GAHGYERQDR PRGEFYHTDW LGSKNASRM // ID 6PGD_CHLPN Reviewed; 479 AA. AC Q9Z8I3; Q9JQC1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 09-JAN-2007, entry version 48. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=CPn_0360, CP_0398, CpB0369; OS Chlamydia pneumoniae (Chlamydophila pneumoniae). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila. OX NCBI_TaxID=83558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CWL029; RX MEDLINE=99206606; PubMed=10192388; DOI=10.1038/7716; RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.; RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis."; RL Nat. Genet. 21:385-389(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AR39; RX MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., RA White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., RA Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., RA Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., RA McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia RT pneumoniae AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J138; RX MEDLINE=20330349; PubMed=10871362; DOI=10.1093/nar/28.12.2311; RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.; RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 RT from Japan and CWL029 from USA."; RL Nucleic Acids Res. 28:2311-2314(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW-183; RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.; RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with RT other Chlamydia strains based on whole genome sequence analysis."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. 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. 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; AE001363; AAD18504.1; -; Genomic_DNA. DR EMBL; AE002161; AAF38243.1; -; Genomic_DNA. DR EMBL; BA000008; BAA98568.1; -; Genomic_DNA. DR EMBL; AE017158; AAP98300.1; -; Genomic_DNA. DR PIR; C72088; C72088. DR PIR; F86535; F86535. DR HSSP; P00349; 2PGD. DR GenomeReviews; AE002161_GR; CP_0398. DR GenomeReviews; AE009440_GR; CpB0369. DR GenomeReviews; AE001363_GR; CPn_0360. DR GenomeReviews; BA000008_GR; gnd. DR KEGG; cpa:CP0398; -. DR KEGG; cpj:CPj0360; -. DR KEGG; cpn:CPn0360; -. DR KEGG; cpt:CpB0369; -. DR TIGR; CP_0398; -. DR BioCyc; CPNE115711:CP0398-MONOMER; -. DR BioCyc; CPNE115713:CPN0360-MONOMER; -. DR BioCyc; CPNE138677:CPJ0360-MONOMER; -. DR BioCyc; CPNE182082:CPB0369-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 479 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090032. SQ SEQUENCE 479 AA; 52939 MW; 0FD301D3378E11F4 CRC64; MQTNIGLIGL AVMGKNLVLN MIDHGFSVSV YNRTPEKTRD FLKEYPNHRE LVGFESLEDF VNSLERPRKI MLMIQAGKPV DQSIHALLPF LEPGDVIIDG GNSYFKDSER RCKELQEKGI LFLGVGISGG EEGARHGPSI MPGGNPEAWP LVAPIFQSIA AKVQGRPCCS WVGTGGAGHY VKAVHNGIEY GDIQLICEAY GILRDFLKLS ATAVATILKE WNTLELESYL IRIASEVLAL KDPEGIPVID TILDVVGQKG TGKWTAIDAL NSGVPLSLII GAVLARFLSS WKEIREQAAR NYPGTPLIFE MPHDPSVFIQ DVFHALYASK IISYAQGFML LGEASKEYNW GLDLGEIALM WRGGCIIQSA FLDVIHKGFA ANPENTSLIF QEYFRGALRH AEMGWRRTVV TAIGAGLPIP CLAAAITFYD GYRTASSSMS LAQGLRDYFG AHTYERNDRP RGEFYHTDWV HTKTTERVK // ID 6PGD_CHLTR Reviewed; 480 AA. AC O84066; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 09-JAN-2007, entry version 41. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=CT_063; OS Chlamydia trachomatis. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D/UW-3/Cx; RX MEDLINE=99000809; PubMed=9784136; DOI=10.1126/science.282.5389.754; RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., RA Davis R.W.; RT "Genome sequence of an obligate intracellular pathogen of humans: RT Chlamydia trachomatis."; RL Science 282:754-759(1998). 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. 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; AE001273; AAC67654.1; -; Genomic_DNA. DR PIR; A71561; A71561. DR HSSP; P00349; 2PGD. DR GenomeReviews; AE001273_GR; CT_063. DR KEGG; ctr:CT063; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 480 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090033. SQ SEQUENCE 480 AA; 52667 MW; E2D9BFE893DCECB2 CRC64; MAPNTDIGLI GLAVMGKNLV LNMVDHGFSV SVYNRSPAKT EEFLKDHGES GALQGFTTIQ EFVQSLKRPR KIMIMIKAGA PVDEMIASLL PFLEEGDILI DGGNSYYLDS EQRYVDLKKE GILFVGMGVS GGEEGARKGP SIMPGGNIDA WPAIAPIFQS IAAQVDGRPC CSWIGTGGAG HFVKAVHNGI EYGDIQLICE TYEILKTRLN LSLEQIGNIF FEWNQTDLNS YLIGAAAAVL IAKDENGNAI ASTILDVAGQ KGTGRWVAED AIKAGVPMSL IIESVLARYL STWKEVRTKA AQEFPGIPLL CQPPQEASAF IEDVREALYA AKIISYAQGF MLLKQVSQDK GWDLNLGELA LIWRGGCIIQ SAFLDKIHQG FENSPEAHSL ILQDYFKKVL FDSETGFRRA VLHAIGSGVA IPCLSSALSF YDGYRTVDSS LFLVQGLRDY FGAHGYERRD CPRGEFYHTD WLETKKTFRV // ID 6PGD_CITAM Reviewed; 445 AA. AC P41581; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 39. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) DE (Fragment). GN Name=gnd; OS Citrobacter amalonaticus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=35703; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CT28; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; U14426; AAC43773.1; -; Genomic_DNA. DR PIR; I40629; I40629. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1 >445 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090034. FT NON_TER 1 1 FT NON_TER 445 445 SQ SEQUENCE 445 AA; 48887 MW; A3771DFC9678EEF1 CRC64; AVMGRNLALN IESRGYTVSV FNRSREKTEE VIAENPGKKL VPYYTVQEFV ESLETPRRIL LMVKAGAGTD SAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSEEGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILKQIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY GDMQLIAEAY SLLKGGLNLS NEELATTFSE WNKGELSSYL IDITKDIFTK KDEEGKYLVD VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKTQRVAASK VLTGPQAQPA GDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASDEYNWDL NYGEIAKIFR AGCIIRAQFL QKITDAYAEN PAIANLLLAP YFKQIADDYQ QALRDVVSYA VQNGIPVPTF SAAVAYYDSY RAAVLPANLI QAQRDYFGAH TYKRT // ID 6PGD_CITDI Reviewed; 445 AA. AC P41582; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 43. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) DE (Fragment). GN Name=gnd; OS Citrobacter diversus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=545; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CT19, CT27, CT4, CT42, CT45, and CT9; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; U14424; AAC43774.1; -; Genomic_DNA. DR EMBL; U14425; AAC43775.1; -; Genomic_DNA. DR EMBL; U14427; AAC43776.1; -; Genomic_DNA. DR EMBL; U14428; AAC43777.1; -; Genomic_DNA. DR EMBL; U14429; AAC43778.1; -; Genomic_DNA. DR EMBL; U14432; AAC43779.1; -; Genomic_DNA. DR PIR; I40681; I40681. DR PIR; I40682; I40682. DR PIR; I40684; I40684. DR PIR; I40685; I40685. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1 >445 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090035. FT VARIANT 31 31 V -> G (in strain: CT45). FT VARIANT 206 206 E -> D (in strain: CT42). FT VARIANT 300 300 A -> E (in strain: CT27). FT NON_TER 1 1 FT NON_TER 445 445 SQ SEQUENCE 445 AA; 48829 MW; 9DB96925EC40EDC4 CRC64; AVMGRNLALN IESRGYTVSV FNRSREKTEE VIAENPGKKL VPYYTVKEFV ESLETPRRIL LMVKAGAGTD AAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSAEGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILTKIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY GDMQLIAEAY SLLKGGLNLS NEELAETFTE WNKGELNSYL IDITKDIFTK KDEEGKYLVD VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKEQRVAASK VLSGPKAQLA GDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASDEYNWDL NYGEIAKIFR AGCIIRAQFL QKITDAYAEN AGIANLLLAP YFKKIADDYQ QALRDVVAYA VQNGIPVPTF SAAVAYYDSY RAAVLPANLI QAQRDYFGAH TYKRT // ID 6PGD_CITFR Reviewed; 445 AA. AC P41583; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 40. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) DE (Fragment). GN Name=gnd; OS Citrobacter freundii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=546; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 8090 / DSM 30039 / JCM 1657 / LMG 3246 / NCTC 9750; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; U14466; AAC43814.1; -; Genomic_DNA. DR PIR; I40709; I40709. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1 >445 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090036. FT NON_TER 1 1 FT NON_TER 445 445 SQ SEQUENCE 445 AA; 48832 MW; 717E56C3D6F3BFAC CRC64; AVMGRNLALN IESRGYTVSI FNRSREKTEE VVAENPGKKL VPYYTVKEFV ESLETPRRIL LMVKAGAGTD AAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSAEGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILTKIAA VAEDGEPCVI YIGADGAGHY VKMVHNGIEY GDMQLIAEAY SLLKGGLNLS NEELATTFTE WNEGELSSYL IDITKDIFTK KDEEGKYLVD VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKDQRVAASK VLSGPQAKLA GDKAEFVEKV RRALYLGKIV SYAQGFSQLR AASDEYNWDL NYGEIAKIFR AGCIIRAQFL QKITDAYAEN KGIANLLLAP YFKNIADEYQ QALRDVVAYA VQNGIPVPTF SAAVAYYDSY RSAVLPANLI QAQRDYFGAH TYKRT // ID 6PGD_CUNEL Reviewed; 485 AA. AC O60037; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 09-JAN-2007, entry version 38. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=6-PGD; OS Cunninghamella elegans. OC Eukaryota; Fungi; Zygomycota; Zygomycetes; Mucorales; OC Cunninghamellaceae; Cunninghamella. OX NCBI_TaxID=4853; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ATCC 36112 / DSM 8217; RX MEDLINE=99085678; PubMed=9868787; RA Wang R.F., Khan A.A., Cao W.W., Cerniglia C.E.; RT "Identification and sequencing of a cDNA encoding 6-phosphogluconate RT dehydrogenase from a fungus, Cunninghamella elegans and expression of RT the gene in Escherichia coli."; RL FEMS Microbiol. Lett. 169:397-402(1998). 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. 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; Y17297; CAA76734.1; -; mRNA. DR HSSP; P00349; 2PGD. DR SMR; O60037; 4-476. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 485 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090073. SQ SEQUENCE 485 AA; 53102 MW; F7E6DDFF3D21EFB2 CRC64; MVEAVADIGL IGLAVMGQNL ILNMNDHGFV VCAYNRTTSK VDDFLANEAK GTNVVGAHSV EELCAKLKRP RKVMLLVKAG SAVDAFIDQL LPHLEEGDII IDGGNSHFPD SIRRTKELEA KGILFVGSGV SGGEEGARYG PSLMPGGNSK AWEHIQPIFQ AIAAKAPDGA SCCEWVGETG AGHYVKMVHN GIEYGDMQLI TEVYQILHEG LGLSHDEMAD IFEEWNKGDL DSFLIEITRD ILRFKDTDGQ PLVTKIRDTA GQKGTGKWTA IDSLDRGIPV TLIGEAVYSR CLSSLKDERV RASKILQGPS SSKFTGDKKT FIAQLGQALY AAKIVSYAQG YMLMRQAAKD YEWKLNNAGI ALMWRGGCII RSVFLGKIRD AYTKNPELEN LLFDDFFKDA TAKAQDAWRN VTAQAVLMGI PTPALSTALN FYDGLRHEIL PANLLQAQRD YFGAHTYELL HTPGKWVHTN WTGRGGNVSA STYDA // ID 6PGD_DROME Reviewed; 481 AA. AC P41572; Q9W519; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 23-JAN-2007, entry version 59. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=Pgd; ORFNames=CG3724; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Canton-S; RX MEDLINE=92112041; PubMed=1765265; DOI=10.1016/0378-1119(91)90607-D; RA Scott M.J., Lucchesi J.C.; RT "Structure and expression of the Drosophila melanogaster gene encoding RT 6-phosphogluconate dehydrogenase."; RL Gene 109:177-183(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; DOI=10.1126/science.287.5461.2220; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). 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. 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; M80598; AAA28786.1; -; Genomic_DNA. DR EMBL; AE014298; AAF45732.1; -; Genomic_DNA. DR EMBL; Z98269; CAB10974.1; -; Genomic_DNA. DR EMBL; AY089447; AAL90185.1; -; mRNA. DR PIR; JH0531; JH0531. DR UniGene; Dm.27; -. DR HSSP; P00349; 2PGD. DR SMR; P41572; 3-472. DR Ensembl; CG3724; Drosophila melanogaster. DR KEGG; dme:Dmel_CG3724; -. DR FlyBase; FBgn0004654; Pgd. DR GermOnline; CG3724; Drosophila melanogaster. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; TAS:FlyBase. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 481 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090069. FT CONFLICT 206 206 K -> Q (in Ref. 2). SQ SEQUENCE 481 AA; 52491 MW; 85EB7D97547E81B4 CRC64; MSGQADIALI GLAVMGQNLI LNMDEKGFVV CAYNRTVAKV KEFLANEAKD TKVIGADSLE DMVSKLKSPR KVMLLVKAGS AVDDFIQQLV PLLSAGDVII DGGNSEYQDT SRRCDELAKL GLLFVGSGVS GGEEGARHGP SLMPGGHEAA WPLIQPIFQA ICAKADGEPC CEWVGDGGAG HFVKMVHNGI EYGDMQLICE AYHIMKSLGL SADQMADEFG KWNSAELDSF LIEITRDILK YKDGKGYLLE RIRDTAGQKG TGKWTAIAAL QYGVPVTLIG EAVFSRCLSA LKDERVQASS VLKGPSTKAQ VANLTKFLDD IKHALYCAKI VSYAQGFMLM REAARENKWR LNYGGIALMW RGGCIIRSVF LGNIKDAYTS QPELSNLLLD DFFKKAIERG QDSWREVVAN AFRWGIPVPA LSTALSFYDG YRTAKLPANL LQAQRDYFGA HTYELLGQEG QFHHTNWTGT GGNVSASTYQ A // ID 6PGD_DROSI Reviewed; 481 AA. AC P41573; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 39. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=Pgd; OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7240; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=94186040; PubMed=8138153; RA Begun D.J.; RT "Evolutionary inferences from DNA variation at the 6-phosphogluconate RT dehydrogenase locus in natural populations of Drosophila: selection RT and geographic differentiation."; RL Genetics 136:155-171(1994). 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. 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; U02288; AAA18587.1; -; Unassigned_DNA. DR HSSP; P00349; 2PGD. DR SMR; P41573; 3-472. DR FlyBase; FBgn0012849; Dsim\Pgd. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 481 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090070. SQ SEQUENCE 481 AA; 52394 MW; 49F97625D5B94822 CRC64; MSGQADIALI GLAVMGQNLI LNMDEKGFVV CAYNRTVAKV KEFLANEAKG TNVIGADSLK DMVSKLKSPR KVMLLVKGGS AVDDFIQQLV PLLSAGDVII DGGNSEYQDT SRRCDELAKL GLLYVGSGVS GGEEGARHGP SLMPGGHEAA WPLIQPIFQA ICAKADGEPC CEWVGDGGAG HFVKMVHNGI EYGDMQLICE AYHIMQSLGL SADQMADEFG KWNSAELDSF LIEITRDILK YKDGKGHLLE RIRDTAGQKG TGKWTAIAAL QYGVPVTLIG EAVFSRCLSA LKDERVQASS VLKGPSTKAE VANLTKFLDD IKHALYCAKI VSYAQGFMLM REAARENKWR LNYGGIALMW RGGCIIRSVF LGNIKDAYTS QPQLSNLLLD DFFKKAIERG QDSWREVVAN AFRWGIPVPA LSTALSFYDG YRTAKLPANL LQAQRDYFGA HTYELLGQEG QFHHTNWTGT GGNVSASTYQ A // ID 6PGD_ECOLI Reviewed; 468 AA. AC P00350; P78080; Q47571; Q59366; Q59402; Q59411; Q59412; Q59413; AC Q59414; Q59416; Q79DT3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 09-JAN-2007, entry version 68. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=b2029, JW2011; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84237540; PubMed=6329905; DOI=10.1016/0378-1119(84)90070-2; RA Nasoff M.S., Baker H.V. II, Wolf R.E. Jr.; RT "DNA sequence of the Escherichia coli gene, gnd, for 6- RT phosphogluconate dehydrogenase."; RL Gene 27:253-264(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ECOR 10; RX MEDLINE=91267957; PubMed=2050640; RA Bisercic M., Feutrier J.Y., Reeves P.R.; RT "Nucleotide sequences of the gnd genes from nine natural isolates of RT Escherichia coli: evidence of intragenic recombination as a RT contributing factor in the evolution of the polymorphic gnd locus."; RL J. Bacteriol. 173:3894-3900(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ECOR 45, ECOR 65, ECOR 67, ECOR 68, ECOR 69, and ECOR 70; RX MEDLINE=92041624; PubMed=1938920; RA Dykhuizen D.E., Green L.; RT "Recombination in Escherichia coli and the definition of biological RT species."; RL J. Bacteriol. 173:7257-7268(1991). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97251358; PubMed=9097040; DOI=10.1093/dnares/3.6.379; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., RA Yamamoto Y., Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RX MEDLINE=89126937; PubMed=2464736; RA Miller R.D., Dykhuizen D.E., Hartl D.L.; RT "Fitness effects of a deletion mutation increasing transcription of RT the 6-phosphogluconate dehydrogenase gene in Escherichia coli."; RL Mol. Biol. Evol. 5:691-703(1988). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RX MEDLINE=88086897; PubMed=3275621; RA Barcak G.J., Wolf R.E. Jr.; RT "Comparative nucleotide sequence analysis of growth-rate-regulated gnd RT alleles from natural isolates of Escherichia coli and from Salmonella RT typhimurium LT-2."; RL J. Bacteriol. 170:372-379(1988). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RC STRAIN=O7:K1 / VW187; RX MEDLINE=93106949; PubMed=7677991; RA Marolda C.L., Valvano M.A.; RT "Identification, expression, and DNA sequence of the GDP-mannose RT biosynthesis genes encoded by the O7 rfb gene cluster of strain VW187 RT (Escherichia coli O7:K1)."; RL J. Bacteriol. 175:148-158(1993). 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. CC -!- INTERACTION: CC P18843:nadE; NbExp=1; IntAct=EBI-907049, EBI-548960; 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; K02072; AAA23918.1; -; Genomic_DNA. DR EMBL; M63821; AAA24488.1; -; Genomic_DNA. DR EMBL; M64326; AAA24204.1; -; Genomic_DNA. DR EMBL; M64327; AAA24205.1; -; Genomic_DNA. DR EMBL; M64328; AAA24206.1; -; Genomic_DNA. DR EMBL; M64329; AAA24207.1; -; Genomic_DNA. DR EMBL; M64330; AAA24208.1; -; Genomic_DNA. DR EMBL; M64331; AAA24209.1; -; Genomic_DNA. DR EMBL; U00096; AAC75090.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15869.1; -; Genomic_DNA. DR EMBL; M23181; AAA23924.1; -; Genomic_DNA. DR EMBL; M18956; AAA23919.1; -; Genomic_DNA. DR EMBL; M18957; AAA23920.1; -; Genomic_DNA. DR EMBL; M18960; AAA23922.1; -; Genomic_DNA. DR EMBL; AF125322; AAC27540.1; -; Genomic_DNA. DR PIR; D64968; DEECGC. DR PIR; I62463; I62463. DR PIR; I62465; I62465. DR HSSP; P00349; 2PGD. DR IntAct; P00350; -. DR ECO2DBASE; C042.6; 6TH EDITION. DR GenomeReviews; U00096_GR; b2029. DR GenomeReviews; AP009048_GR; JW2011. DR KEGG; ecj:JW2011; -. DR KEGG; eco:b2029; -. DR EchoBASE; EB0406; -. DR EcoGene; EG10411; gnd. DR BioCyc; EcoCyc:6PGLUCONDEHYDROG-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090037. FT VARIANT 2 2 S -> L (in strain: ECOR 70). FT VARIANT 32 32 F -> Y (in strain: ECOR 70). FT VARIANT 39 39 T -> Q (in strain: O7:K1 / VW187). FT VARIANT 52 52 V -> D (in strain: ECOR 10). FT VARIANT 55 55 Y -> F (in strain: ECOR 10). FT VARIANT 102 102 N -> K (in strain: ECOR 65). FT VARIANT 117 117 A -> S (in strain: ECOR 70). FT VARIANT 123 125 IGT -> YRY (in strain: O7:K1 / VW187). FT VARIANT 170 170 V -> F (in strain: ECOR 10). FT VARIANT 175 175 A -> S (in strain: ECOR 45). FT VARIANT 209 209 N -> S (in strain: ECOR 68). FT VARIANT 211 211 T -> S (in strain: ECOR 10 and ECOR 69). FT VARIANT 216 216 A -> T (in strain: ECOR 67). FT VARIANT 294 294 D -> E (in strain: ECOR 70). FT VARIANT 308 308 A -> G (in strain: ECOR 68). FT VARIANT 313 313 D -> N (in strain: ECOR 67). FT VARIANT 315 315 A -> G (in strain: ECOR 70). FT VARIANT 325 325 L -> Q (in strain: ECOR 69). FT VARIANT 330 330 I -> S (in strain: ECOR 10). FT VARIANT 350 350 D -> A (in strain: ECOR 10 and ECOR 69). FT VARIANT 369 369 Q -> R (in strain: ECOR 10). FT VARIANT 422 422 S -> A (in strain: ECOR 10, ECOR 65, ECOR FT 68, ECOR 69 and ECOR 70). FT CONFLICT 306 306 P -> R (in Ref. 1). SQ SEQUENCE 468 AA; 51481 MW; 62A32C84DC596D86 CRC64; MSKQQIGVVG MAVMGRNLAL NIESRGYTVS IFNRSREKTE EVIAENPGKK LVPYYTVKEF VESLETPRRI LLMVKAGAGT DAAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILTKIA AVAEDGEPCV TYIGADGAGH YVKMVHNGIE YGDMQLIAEA YSLLKGGLNL TNEELAQTFT EWNNGELSSY LIDITKDIFT KKDEDGNYLV DVILDEAANK GTGKWTSQSA LDLGEPLSLI TESVFARYIS SLKDQRVAAS KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASEEYNWD LNYGEIAKIF RAGCIIRAQF LQKITDAYAE NPQIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIPVPT FSAAVAYYDS YRAAVLPANL IQAQRDYFGA HTYKRIDKEG VFHTEWLD // ID 6PGD_ESCVU Reviewed; 445 AA. AC P41574; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 38. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) DE (Fragment). GN Name=gnd; OS Escherichia vulneris. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=566; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33821 / DSM 4564 / JCM 1688 / LMG 7868 / NCTC 12130; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; U14465; AAC43815.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1 >445 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090039. FT NON_TER 1 1 FT NON_TER 445 445 SQ SEQUENCE 445 AA; 48806 MW; 0315BE126C2A45FE CRC64; AVMGRNLALN IESRGYTVSV FNRSREKTEE VVAENPGKKL VPYYTVQEFV ESLETPRRIL LMVQAGAGTD AAINSLKPYL DKGDIIIDGG NTFFHDTIRR NRELSAEGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILTKIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY GDMQLIAEAY SLLKGGLNLS NEELAQTFTE WNKGELSSYL IDITKDIFTK KDEEGKYLVD VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKEQRVAASK VLSGPQSQPA GDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASEEYNWDL NYGEIAKIFR AGCIIRAQFL QKITDAYAET PAIANLLLAP YFKQIADDYQ QALRDVVAYA VQNGIPVPTF GAAVAYYDSY RAAVLPANLI QAQRDYFGAH TYKRT // ID 6PGD_HAEDU Reviewed; 484 AA. AC Q7VMX4; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 09-JAN-2007, entry version 22. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=HD_0833; OS Haemophilus ducreyi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=35000HP / ATCC 700724; RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., RA Johnson L., Nguyen D., Wang J., Forst C., Hood L.; RT "The complete genome sequence of Haemophilus ducreyi."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. 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. 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; AE017143; AAP95728.1; -; Genomic_DNA. DR GenomeReviews; AE017143_GR; HD_0833. DR KEGG; hdu:HD0833; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 484 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090040. SQ SEQUENCE 484 AA; 53272 MW; BA23A9A770615B23 CRC64; MSIKGDIGVI GLAVMGQNLI LNMNDNGFKV VAYNRTASKV DEFLAGEAKD TNIIGAYSLE DLAAKLEKPR KIMLMVRAGE VVDQFIDALL PHLEAGDIII DGGNSNYPDT NRRTITLAEK GIRFIGTGVS GGEEGARHGP SIMPGGNEEA WPFVKPILQA ISAKTDKDEP CCDWVGKEGA GHFVKMVHNG IEYGDMQLIC EAYQFLKDGL GLNYEEMHAI FADWKNTELD SYLIDITADI LAYKDADGEP LVEKILDTAG QKGTGKWTGI NALDFGIPLT LITEAVFARC VSAFKDQRVA VSQLFNKTIT PISDDKKEWI EAVRKALLAS KIISYAQGFM LIREASENFE WNINYGATAL LWREGCIIRS AFLGNIRDAY EANPGLVFLG SDPYFQNILQ SAMADWRKVV AKSIEIGIPM PCMAAAITFL DGYSSEHLPA NLLQAQRDYF GAHTYERTDK PRCSFFHTNW TGRGGNTAST TYDV // ID 6PGD_HAEIN Reviewed; 484 AA. AC P43774; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 45. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=HI0553; OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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. 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; L42023; AAC22210.1; -; Genomic_DNA. DR PIR; C64077; C64077. DR HSSP; P00349; 2PGD. DR GenomeReviews; L42023_GR; HI0553. DR KEGG; hin:HI0553; -. DR TIGR; HI0553; -. DR BioCyc; HINF71421:HI0553-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 484 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090041. SQ SEQUENCE 484 AA; 53140 MW; 8381EEB3C704C5DA CRC64; MSVKGDIGVI GLAVMGQNLI LNMNDHGFKV VAYNRTTSKV DEFLQGAAKG TNIIGAYSLE DLAAKLEKPR KVMLMVRAGD VVDQFIEALL PHLEEGDIII DGGNSNYPDT NRRVKALAEK GIRFIGSGVS GGEEGARHGP SIMPGGNQEA WQYVKPIFQA ISAKTEQGEP CCDWVGGEGA GHFVKMVHNG IEYGDMQLIC EAYQFLKEGL GLSYEEMQAI FAEWKNTELD SYLIDITTDI LGYKDASGEP LVEKILDTAG QKGTGKWTGI NALDFGIPLT LITESVFARC VSSFKDQRVA ANQLFGKTIT PVEGDKKVWI EAVRKALLAS KIISYAQGFM LIREASEQFG WDINYGATAL LWREGCIIRS RFLGNIRDAY EANPNLVFLG SDSYFKGILE NALSDWRKVV AKSIEVGIPM PCMASAITFL DGYTSARLPA NLLQAQRDYF GAHTYERTDK PRGEFFHTNW TGRGGNTAST TYDV // ID 6PGD_HUMAN Reviewed; 483 AA. AC P52209; Q9BWD8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 66. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=PGD; Synonyms=PGDH; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Heart; RX MEDLINE=97133513; PubMed=8978909; RA Tsui S.K.W., Chan J.Y., Waye M.M.Y., Fung K.-P., Lee C.-Y.; RT "Identification of a cDNA encoding 6-phosphogluconate dehydrogenase RT from a human heart cDNA library."; RL Biochem. Genet. 34:367-373(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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: 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. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- INTERACTION: CC O95777:LSM8; NbExp=1; IntAct=EBI-372761, EBI-347779; 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; U30255; AAA75302.1; -; mRNA. DR EMBL; BC000368; AAH00368.1; -; mRNA. DR PIR; G01922; G01922. DR UniGene; Hs.464071; -. DR HSSP; P00349; 2PGD. DR SMR; P52209; 2-474. DR IntAct; P52209; -. DR Ensembl; ENSG00000142657; Homo sapiens. DR KEGG; hsa:5226; -. DR H-InvDB; HIX0000112; -. DR HGNC; HGNC:8891; PGD. DR MIM; 172200; gene. DR Reactome; REACT_1709.1; Metabolism of small molecules. DR LinkHub; P52209; -. DR ArrayExpress; P52209; -. DR GermOnline; ENSG00000142657; Homo sapiens. DR RZPD-ProtExp; C0451; -. DR RZPD-ProtExp; IOH3407; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006118; P:electron transport; IDA:UniProtKB. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IDA:UniProtKB. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW NADP; Oxidoreductase; Pentose shunt. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 483 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090063. FT CONFLICT 118 118 A -> G (in Ref. 1). FT CONFLICT 135 135 A -> P (in Ref. 1). SQ SEQUENCE 483 AA; 53140 MW; 6CEFC0077D1283E3 CRC64; MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS YNA // ID 6PGD_KLEPL Reviewed; 445 AA. AC P41575; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 40. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) DE (Fragment). GN Name=gnd; OS Klebsiella planticola (Raoultella planticola). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Raoultella. OX NCBI_TaxID=575; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33531 / DSM 3069 / IFO 14939 / JCM 7251 / V-236; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; U14464; AAC43816.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1 >445 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090042. FT NON_TER 1 1 FT NON_TER 445 445 SQ SEQUENCE 445 AA; 48829 MW; 48E581E9B9290681 CRC64; AVMGRNLALN IESRGYTVSV FNRSREKTEE VIAENPGKKL VPHYTVKEFV ESLETPRRIL LMVKAGAGTD SAIDSLKPYL NKGDIIIDGG NTFFQDTIRR NRELSAEGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILEQIAA RAEDGEPCVA YIGADGAGHY VKMVHNGIEY GDMQLIAEAY ALLKGGLALS NEELATTFTK WNEGELSSYL IDITKDIFTK KDEEGKYLVD VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKDQRVAASK VLTGPKAQPA GDKAEFVEKV RRALYLGKIV SYAQGFSQLR AASNEYNWDL NYGEIAKIFR AGCIIRAQFL QKITDAYEQN AGIANLLLAP YFKQIADEYQ QALRDVVAYA VQNGIPVPTF SAAIAYYDSY RSAVLPANLI QAQRDYFGAH TYKRT // ID 6PGD_KLEPN Reviewed; 468 AA. AC P41576; Q48461; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 09-JAN-2007, entry version 41. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OS Klebsiella pneumoniae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=573; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Chedid; RX MEDLINE=95204345; PubMed=7896702; RA Arakawa Y., Wacharotayankun R., Nagatsuka T., Ito H., Kato N., RA Ohta M.; RT "Genomic organization of the Klebsiella pneumoniae cps region RT responsible for serotype K2 capsular polysaccharide synthesis in the RT virulent strain Chedid."; RL J. Bacteriol. 177:1788-1796(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-456. RC STRAIN=CW 7380; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; D21242; BAA04786.1; -; Genomic_DNA. DR EMBL; U14471; AAC43817.1; -; Genomic_DNA. DR PIR; D56146; D56146. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090043. FT CONFLICT 316 316 G -> E (in Ref. 2). FT CONFLICT 421 421 V -> F (in Ref. 2). SQ SEQUENCE 468 AA; 51328 MW; FF1EB5E7665FDC90 CRC64; MSKQQIGVVG MAVMGRNLAL NIESRGYTVS VFNRSREKTE EVIAENTGKK LVPYYTVQEF VESLETPRRI LLMVKAGAGT DSAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILKQIA AVAEDGEPCV TYIGADGAGH YVKMVHNGIE YGDMQLIAEA YALLKGGLAL SNEELAQTFT EWNEGELSSY LIDITKDIFT KKDEEGKYLV DVILDEAANK GTGKWTSQSS LDLGEPLSLI TESVFARYIS SLKDQRVAAS KVLSGPQAQP VGDKAGFIEK VRRALYLGKI VSYAQGFSQL RAASDEYNWD LNYGEIAKIF RAGCIIRAQF LQKITDAYAQ NAGIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIPVPT VSAAIAYYDS YRSAVLPANL IQAQRDYFGA HTYKRTDKEG VFHTEWLE // ID 6PGD_KLETE Reviewed; 445 AA. AC P41577; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 39. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) DE (Fragment). GN Name=gnd; OS Klebsiella terrigena (Raoultella terrigena). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Raoultella. OX NCBI_TaxID=577; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33257 / DSM 2687 / IFO 14941 / NCTC 13038; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; U14473; AAC43819.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1 >445 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090044. FT NON_TER 1 1 FT NON_TER 445 445 SQ SEQUENCE 445 AA; 48834 MW; 2FBD0E46CDAB69A8 CRC64; AVMGRNLALN IESRGYTVSV FNRSREKTEE VIAENPGKKL VPHYTVKEFV ESLETPRRIL LMVKAGAGTD SAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSADGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILEQIAA RAEDGEPCVA YIGADGAGHY VKMVHNGIEY GDMQLIAEAY ALLKGGLALS NEELATTFTE WNQGELSSYL IDITKDIFTK KDEEGKYLVD VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKDQRVAASK VLTGPQAQPA SDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASNEYSWDL NYGEIAKIFR AGCIIRAQFL QKITDAYEEN AGIANLLLAP YFKQIADEYQ QALRDVVAYA VQNGIPVPTF SAAIAYYDSY RSAVLPANLI QAQRDYFGAH TYKRT // ID 6PGD_LACLA Reviewed; 472 AA. AC Q9CHU6; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 09-JAN-2007, entry version 35. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=LL0622; OS Lactococcus lactis subsp. lactis (Streptococcus lactis). OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Lactococcus. OX NCBI_TaxID=1360; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL1403; RX MEDLINE=21235186; PubMed=11337471; DOI=10.1101/gr.GR-1697R; RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "The complete genome sequence of the lactic acid bacterium Lactococcus RT lactis ssp. lactis IL1403."; RL Genome Res. 11:731-753(2001). 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. 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; AE006295; AAK04720.1; -; Genomic_DNA. DR PIR; F86702; F86702. DR HSSP; P00349; 2PGD. DR GenomeReviews; AE005176_GR; LL0622. DR KEGG; lla:L0046; -. DR BioCyc; LLAC1360:L0046-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 472 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090045. SQ SEQUENCE 472 AA; 52424 MW; 6EF4F504F217E55F CRC64; MAQANFGVVG MAVMGKNLAL NVESRGYTVA IYNRTTSKTE EVYKEHQDKN LVLTKTLEEF VGSLEKPRRI MLMVQAGAAT DATIKSLLPL LDKGDILIDG GNTHFPDTMR RNAELADSGI NFIGTGVSGG EKGALLGPSM MPGGQKEAYD LVAPIFEQIA AKAPQDGKPC VAYMGANGAG HYVKMVHNGI EYGDMQLIAE SYDLLKRVLG LSNAEIQAIF EEWNEGELDS YLIEITKEVL KRKDDEGEGY IVDKILDKAG NKGTGKWTSE SALDLGVPLP LITESVFARY ISTYKDERVK ASKVLSGPAV NFSGDKKEVI EKIRKALYFS KIMSYAQGFA QLRKASEEFD WDLPYGTIAQ IWRAGCIIRA EFLQNITDAF DKDSELENLL LDDYFVDITK RYQEAVRDVV SLAVQAGIPI PTFTSAISYY DSYRSENLPA NLIQAQRDYF GAHTYERTDK AGIFHYDWYT ED // ID 6PGD_LACLC Reviewed; 472 AA. AC P96789; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 2. DT 09-JAN-2007, entry version 43. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris). OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Lactococcus. OX NCBI_TaxID=1359; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MG1363; RX MEDLINE=99131986; PubMed=9931298; DOI=10.1042/0264-6021:3380055; RA Tetaud E., Hanau S., Wells J.M., Le Page R.W.F., Adams M.J., RA Arkison S., Barrett M.P.; RT "6-phosphogluconate dehydrogenase from Lactococcus lactis: a role for RT arginine residues in binding substrate and coenzyme."; RL Biochem. J. 338:55-60(1999). 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. 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; U74322; AAC12804.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 472 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090046. SQ SEQUENCE 472 AA; 52444 MW; 739958A068D63CD0 CRC64; MAQANFGVVG MAVMGKNLAL NVESRGYTVA IYNRTTSKTE EVFKEHQDKN LVFTKTLEEF VGSLEKPRRI MLMVQAGAAT DATIKSLLPL LDIGDILIDG GNTHFPDTMR RNAELADSGI NFIGTGVSGG EKGALLGPSM MPGGQKEAYD LVAPIFEQIA AKAPQDGKPC VAYMGANGAG HYVKMVHNGI EYGDMQLIAE SYDLLKRILG LSNAEIQAIF EEWNEGELDS YLIEITKEVL KRKDDEGEGY IVDKILDKAG NKGTGKWTSE SALDLGVPLP LITESVFARY ISTYKDERVK ASKVLSGPAL DFSGDKKEVI EKIRKALYFS KIMSYAQGFA QLRKASEEFD WDLPYGTIAQ IWRAGCIIRA EFLQNITDAF DKDSELENLL LDDYFVDITK RYQEAVRDVV SLAVQAGTPI PTFTSAISYY DSYRSENLPA NLIQAQRDYF GAHTYERTDK AGIFHYDWYT ED // 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 23-JAN-2007, entry version 44. DE 6-phosphogluconate dehydrogenase, decarboxylating (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. 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). 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. CC -!- SUBUNIT: Homodimer (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 UniGene; Mm.252080; -. DR HSSP; P00349; 2PGD. DR SMR; Q9DCD0; 2-474. DR Ensembl; ENSMUSG00000028961; Mus musculus. DR KEGG; mmu:110208; -. DR MGI; MGI:97553; Pgd. DR ArrayExpress; Q9DCD0; -. DR GermOnline; ENSMUSG00000028961; Mus musculus. DR RZPD-ProtExp; IOM17252; -. DR RZPD-ProtExp; IOM18539; -. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IDA:MGI. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW NADP; Oxidoreductase; Pentose shunt. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 483 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090064. 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 6PGD_PIG Reviewed; 250 AA. AC P14332; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2003, sequence version 3. DT 20-FEB-2007, entry version 51. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) DE (Fragment). GN Name=PGD; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=90299673; PubMed=2361879; RA Harbitz I., Chowdhary B., Chowdhary R., Kran S., Frengen E., RA Gustavsson I., Davies W.; RT "Isolation, characterization and chromosomal assignment of a partial RT cDNA for porcine 6-phosphogluconate dehydrogenase."; RL Hereditas 112:83-88(1990). RN [2] RP IDENTIFICATION OF PROBABLE FRAMESHIFTS. RX MEDLINE=92065803; PubMed=1659648; RA Reizer A., Deutscher J., Saier M.H. Jr., Reizer J.; RT "Analysis of the gluconate (gnt) operon of Bacillus subtilis."; RL Mol. Microbiol. 5:1081-1089(1991). 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. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. CC -!- CAUTION: Ref.1 sequence differs from that shown due to frameshifts CC in positions 226 and 249. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X16638; CAA34633.1; ALT_FRAME; mRNA. DR PIR; A48325; A48325. DR UniGene; Ssc.16347; -. DR HSSP; P00349; 2PGD. DR SMR; P14332; 1-241. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR PROSITE; PS00461; 6PGD; 1. KW NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1 250 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090065. FT NON_TER 1 1 SQ SEQUENCE 250 AA; 27806 MW; 8BBB0655D9A40C36 CRC64; IEITANILKF QDADGKHLLP KIRDSAGQKG TGKWTAISAL EYGVPVTLIG EAVFARCLSS LKDERVQASK KLKGPQKIQF SGDKKSFLED IRKALYASKI ISYTQGFMLL RQAAAEFGWS STTEHRLMWR GGCIIRSVFL GKIKDAFDRN PGLQNLLLDD FFKSAVEDCQ DSWRRAVSTG VQTGIPMPCF TTALSFYDGY RHEMLPANLI QAQRDYFGAH TYELLAKPGH FVHTNWTGHG GSVSSSSYNA // ID 6PGD_SALTY Reviewed; 468 AA. AC P14062; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 23-JAN-2007, entry version 61. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=STM2081; OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=602; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2; RX MEDLINE=89364685; PubMed=2671649; DOI=10.1007/BF00330960; RA Reeves P., Stevenson G.; RT "Cloning and nucleotide sequence of the Salmonella typhimurium LT2 gnd RT gene and its homology with the corresponding sequence of Escherichia RT coli K12."; RL Mol. Gen. Genet. 217:182-184(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2; RX MEDLINE=92041624; PubMed=1938920; RA Dykhuizen D.E., Green L.; RT "Recombination in Escherichia coli and the definition of biological RT species."; RL J. Bacteriol. 173:7257-7268(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., RA Waterston R., Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium RT LT2."; RL Nature 413:852-856(2001). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57. RC STRAIN=LT2; RX MEDLINE=91260454; PubMed=1710759; RA Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.; RT "Structure and sequence of the rfb (O antigen) gene cluster of RT Salmonella serovar typhimurium (strain LT2)."; RL Mol. Microbiol. 5:695-713(1991). 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. 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; X15651; CAA33677.1; -; Genomic_DNA. DR EMBL; M64332; AAA27137.1; -; Genomic_DNA. DR EMBL; AE008792; AAL20985.1; -; Genomic_DNA. DR EMBL; X56793; CAA40131.1; -; Genomic_DNA. DR PIR; S04397; S04397. DR HSSP; P00349; 2PGD. DR GenomeReviews; AE006468_GR; STM2081. DR KEGG; stm:STM2081; -. DR StyGene; SG10146; gnd. DR BioCyc; STYP99287:STM2081-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090047. SQ SEQUENCE 468 AA; 51395 MW; D8EBB53A2DAADBF7 CRC64; MSKQQIGVVG MAVMGRNLAL NIESRGYTVS VFNRSREKTE EVIAENPGKK LVPYYTVKEF VESLETPRRI LLMVKAGAGT DAAIDSLKPY LEKGDIIIDG GNTFFQDTIR RNRELSAEGF NFIGTGVSGG EEGALKGPSI MPGGQKDAYE LVAPILTKIA AVAEDGEPCV TYIGADGAGH YVKMVHNGIE YGDMQLIAEA YSLLKGGLNL SNEELANTFT EWNNGELSSY LIDITKDIFT KKDEDGNYLV DVILDEAANK GTGKWTSQSA LDLGEPLSLI TESVFARYIS SLKAQRVAAS KVLSGPKAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASDEYHWD LNYGEIAKIF RAGCIIRAQF LQKITDAYAE NADIANLLLA PYFKKIADEY QQALRDVVAY AVQNGIPVPT FSAAVAYYDS YRAAVLPANL IQAQRDYFGA HTYKRTDKEG IFHTEWLE // ID 6PGD_SCHPO Reviewed; 492 AA. AC P78812; Q9UQW5; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 20-FEB-2007, entry version 48. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN ORFNames=SPBC660.16; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=PR745; RX MEDLINE=98162722; PubMed=9501991; DOI=10.1093/dnares/4.6.363; RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.; RT "Identification of open reading frames in Schizosaccharomyces pombe RT cDNAs."; RL DNA Res. 4:363-369(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). 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. 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; D89161; BAA13823.1; ALT_INIT; mRNA. DR EMBL; AL034563; CAA22536.1; -; Genomic_DNA. DR PIR; T40628; T40628. DR HSSP; P00349; 2PGD. DR KEGG; spo:SPBC660.16; -. DR GeneDB_Spombe; SPBC660.16; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-003196-MONOMER; -. DR ArrayExpress; P78812; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0050661; F:NADP binding; IDA:GeneDB_SPombe. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IDA:GeneDB_SPombe. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IDA:GeneDB_SPombe. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 492 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090074. FT CONFLICT 219 220 IA -> ST (in Ref. 1). SQ SEQUENCE 492 AA; 53680 MW; F55F342957A9D3E1 CRC64; MSQKEVADFG LIGLAVMGQN LILNGADKGF TVCCYNRTTS RVDEFLANEA KGKSIVGAHS LEEFVSKLKK PRVCILLVKA GKPVDYLIEG LAPLLEKGDI IVDGGNSHYP DTTRRCEELA KKGILFVGSG VSGGEEGARY GPSLMPGGNP AAWPRIKPIF QTLAAKAGNN EPCCDWVGEQ GAGHYVKMVH NGIEYGDMQL ICETYDIMKR GLGMSCDEIA DVFEKWNTGK LDSFLIEITR DVLRYKADDG KPLVEKILDA AGQKGTGKWT AQNALEMGTP VSLITEAVFA RCLSSLKSER VRASKKLTGP NTKFTGDKKQ LIDDLEDALY ASKIISYAQG FMLMREAAKE YGWKLNNAGI ALMWRGGCII RSVFLKDITE AFREDPNLES ILFHPFFTNG VEKAQAGWRR VVAQAAMLGI PVPATSTGLS FYDGYRSAVL PANLLQAQRD YFGAHTFRVL PEAADKSLPA DKDIHINWTG HGGNISATTY DA // ID 6PGD_SHEEP Reviewed; 483 AA. AC P00349; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 23-JAN-2007, entry version 68. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=PGD; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=93111932; PubMed=1471978; RA Somers D.O., Medd S.M., Walker J.E., Adams M.J.; RT "Sheep 6-phosphogluconate dehydrogenase. Revised protein sequence RT based upon the sequences of cDNA clones obtained with the polymerase RT chain reaction."; RL Biochem. J. 288:1061-1067(1992). RN [2] RP PRELIMINARY PROTEIN SEQUENCE OF 2-483. RC TISSUE=Liver; RX MEDLINE=84032505; PubMed=6685125; RA Carne A., Walker J.E.; RT "Amino acid sequence of ovine 6-phosphogluconate dehydrogenase."; RL J. Biol. Chem. 258:12895-12906(1983). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX MEDLINE=84057760; PubMed=6641716; RA Adams M.J., Archibald I.G., Bugg C.E., Carne A., Gover S., RA Helliwell J.R., Pickersgill R.W., White S.W.; RT "The three dimensional structure of sheep liver 6-phosphogluconate RT dehydrogenase at 2.6-A resolution."; RL EMBO J. 2:1009-1014(1983). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=92172317; PubMed=1793548; DOI=10.1107/S0108768191010315; RA Adams M.J., Gover S., Leaback R., Phillips C., Somers D.O.; RT "The structure of 6-phosphogluconate dehydrogenase refined at 2.5-A RT resolution."; RL Acta Crystallogr. B 47:817-820(1991). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX MEDLINE=95006333; PubMed=7922042; RA Adams M.J., Ellis G.H., Gover S., Naylor C.E., Phillips C.; RT "Crystallographic study of coenzyme, coenzyme analogue and substrate RT binding in 6-phosphogluconate dehydrogenase: implications for NADP RT specificity and the enzyme mechanism."; RL Structure 2:651-668(1994). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=15299295; DOI=10.1107/S0907444994012229; RA Phillips C., Gover S., Adams M.J.; RT "Structure of 6-phosphogluconate dehydrogenase refined at 2-A RT resolution."; RL Acta Crystallogr. D 51:290-304(1995). 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. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. CC -!- CAUTION: Ref.2 sequence was incorrect in the order of the CNBR CC peptides. There were many other sequencing errors. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X60195; CAA42751.1; -; mRNA. DR PIR; S27359; DESHGC. DR UniGene; Oar.419; -. DR PDB; 1PGN; X-ray; @=1-483. DR PDB; 1PGO; X-ray; @=1-483. DR PDB; 1PGP; X-ray; @=1-483. DR PDB; 1PGQ; X-ray; @=1-483. DR PDB; 2PGD; X-ray; @=1-483. DR LinkHub; P00349; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase; KW Pentose shunt. FT INIT_MET 1 1 Removed. FT CHAIN 2 483 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090066. FT STRAND 4 9 FT HELIX 13 24 FT TURN 25 25 FT STRAND 29 32 FT TURN 36 36 FT HELIX 37 44 FT TURN 45 49 FT HELIX 58 64 FT STRAND 70 73 FT HELIX 79 91 FT TURN 94 95 FT STRAND 97 100 FT HELIX 106 118 FT TURN 119 120 FT STRAND 122 130 FT HELIX 131 137 FT STRAND 140 145 FT HELIX 147 149 FT HELIX 150 160 FT TURN 165 167 FT STRAND 168 170 FT TURN 177 178 FT HELIX 179 207 FT TURN 208 209 FT HELIX 213 223 FT TURN 224 228 FT HELIX 231 241 FT TURN 245 246 FT STRAND 247 250 FT HELIX 251 253 FT HELIX 263 274 FT TURN 275 275 FT HELIX 279 292 FT HELIX 294 303 FT HELIX 316 349 FT TURN 350 350 FT HELIX 355 361 FT TURN 362 363 FT STRAND 364 366 FT TURN 367 368 FT HELIX 372 382 FT TURN 384 385 FT HELIX 389 391 FT HELIX 393 416 FT TURN 417 417 FT HELIX 421 434 FT TURN 439 439 FT HELIX 440 451 FT STRAND 457 460 FT TURN 461 462 SQ SEQUENCE 483 AA; 52970 MW; F4AC5DB414385F11 CRC64; MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVLGAHSLEE MVSKLKKPRR IILLVKAGQA VDNFIEKLVP LLDIGDIIID GGNSEYRDTM RRCRDLKDKG ILFVGSGVSG GEDGARYGPS LMPGGNKEAW PHIKAIFQGI AAKVGTGEPC CDWVGDDGAG HFVKMVHNGI EYGDMQLICE AYHLMKDVLG LGHKEMAKAF EEWNKTELDS FLIEITASIL KFQDADGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA SKKLKGPQNI PFEGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPGLQNLL LDDFFKSAVE NCQDSWRRAI STGVQAGIPM PCFTTALSFY DGYRHAMLPA NLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGSVSSSS YNA // ID 6PGD_SHIBO Reviewed; 445 AA. AC P41578; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 40. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) DE (Fragment). GN Name=gnd; OS Shigella boydii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=621; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 8700 / DSM 7532 / NCTC 12985; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; U14469; AAC43820.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1 >445 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090048. FT NON_TER 1 1 FT NON_TER 445 445 SQ SEQUENCE 445 AA; 48833 MW; B90F886E7AD0CB0B CRC64; AVMGRNLALN IESRGYTVSI FNRSREKTEE VIAENPGKKL VPYYTVKEFV ESLETPRRIL LMVKAGAGTD AAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSAEGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILTKIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY GDMQLIAEAY SLLKGGLNLS NEELAQTFTE WNNGELSSYL IDITKDIFTK KDEDGNYLVD VILDEAANKG TGKWTSQSAL DLGEPLSLIT ESVFARYISS LKDQRVAASK VLSGPQAQPA GNKAEFIEKV RRALYLGKIV SYAQGFSQLR AASEEYNWDL NYGEIAKIFR AGCIIRAQFL QKITDAYAEN PQIANLLLAP YFKQIADDYQ QALRDVVAYA VQNGIPVPTF AAAVAYYDSY RAAVLPANLI QAQRDYFGAH TYKRI // ID 6PGD_SHIDY Reviewed; 445 AA. AC P41579; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 40. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) DE (Fragment). GN Name=gnd; OS Shigella dysenteriae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=622; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13313 / NCTC 4837; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; U14467; AAC43821.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1 >445 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090049. FT NON_TER 1 1 FT NON_TER 445 445 SQ SEQUENCE 445 AA; 48882 MW; 04C8E50E7AC0116E CRC64; AVMGRNLALN IESRGYTVSI FNRSREKTEE VIAENPGKKL VPYYTVKEFV ESLETPRRIL LMVKAGAGTD AAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSAEGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILTKIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY GDMQLIAEAY SLLKGGLNLS NEELAQTFTE WNNGELSSYL IDITKDIFTK KDEDGNYLVD VILDEAANKG TGKWTSQSAL DLGEPLSLIT ESVFARYISS LKDQRVAASK VLSGPQAQPA GDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASEEYNWDL NYGEIAKIFR AGCIIRAQFL QKITDAYAEN PQIANLLLAP YFKQIADDYQ QALRDVVAYA VQNGIPVPTF AAAVAYYDSY RAAFLPANLI QAQRDYFGAH TYKRI // ID 6PGD_SHIFL Reviewed; 468 AA. AC P37756; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 23-JAN-2007, entry version 55. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=SF2091, S_2212; OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=PE577 / Serotype 2a; RX MEDLINE=94131953; PubMed=7507920; RA Morona R., Mavris M., Fallarino A., Manning P.A.; RT "Characterization of the rfc region of Shigella flexneri."; RL J. Bacteriol. 176:733-747(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RX DOI=10.1128/IAI.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-456. RC STRAIN=ATCC 29903; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; X71970; CAA50781.1; -; Genomic_DNA. DR EMBL; AE005674; AAN43630.1; -; Genomic_DNA. DR EMBL; AE014073; AAP17458.1; -; Genomic_DNA. DR EMBL; U14468; AAC43834.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR GenomeReviews; AE014073_GR; S_2212. DR GenomeReviews; AE005674_GR; SF2091. DR KEGG; sfl:SF2091; -. DR KEGG; sfx:S2212; -. DR BioCyc; SFLE198214:AAN43630.1-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090050. SQ SEQUENCE 468 AA; 51344 MW; 2203A0D82120CD61 CRC64; MSKQQIGVVG MAVMGRNLAL NIESRGYTVS IFNRSREKTE EVIAENPGKK LAPYYTVKEF VESLETPRRI LLMVKAGAGT DAAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILTKIA AVAEDGEPCV TYIGADGAGH YVKMVHNGIE YGDMQLIAEA YSLLKGGLNL SNEELAQTFT EWNNGELSSY LIDITKDIFT KKDEDGNYLV DVILDEAANK GTGKWTSQSA LDLGEPLSLI TESVFARYIS SLKDQRVAAS KVLSGPQAQS AGDKAEFIEK VRSALYLGKI VSYAQGFSQL RAASEEYNWD LNYGEIAKIF RAGCIIRAQF LQKITDAYAE NPQIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIPVPT FAAAVAYYDS YRAAVLPANL IQAQRDYFGA HTYKRIDKEG VFHTEWLD // ID 6PGD_SHISO Reviewed; 445 AA. AC P41580; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JAN-2007, entry version 40. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) DE (Fragment). GN Name=gnd; OS Shigella sonnei. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=624; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29930 / DSM 5570 / NCTC 12984; RX MEDLINE=95024018; PubMed=7937867; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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. 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; U14470; AAC43835.1; -; Genomic_DNA. DR EMBL; U14440; AAC43790.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1 >445 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090051. FT NON_TER 1 1 FT NON_TER 445 445 SQ SEQUENCE 445 AA; 48824 MW; 07F8D753DBB0366E CRC64; AVMGRNLALN IESRGYTVSI FNRSREKTEE VIAENPGKKL VPYYTVKEFV ESLETPRRIL LMVKAGAGTD AAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSAEGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILTKIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY GDMQLIAEAY SLLKGGLNLS NEELAQTFTE WNNGELSSYL IDITKDIFTK KDEDGNYLVD VILDEAANKG TGKWTSQSAL DLGEPLSLIT ESVFARYISS LKDQRVAASK VLSGPQAQSA GDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASEEYNWDL NYGEIAKIFR AGCIIRAQFL QKITDAYAEN PQIANLLLAP YFKQIADDYQ QALRDVVAYA VQNGIPVPTF AAAVAYYDSY RAAVLPANLI QAQRDYFGAH TYKRI // ID 6PGD_STAAC Reviewed; 468 AA. AC Q5HFR2; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 23-JAN-2007, entry version 17. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=SACOL1554; OS Staphylococcus aureus (strain COL). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=93062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). 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. 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; CP000046; AAW36746.1; -; Genomic_DNA. DR GenomeReviews; CP000046_GR; SACOL1554. DR KEGG; sac:SACOL1554; -. DR TIGR; SACOL1554; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090052. SQ SEQUENCE 468 AA; 51803 MW; 61A5C2CAF3CCD011 CRC64; MTQQIGVIGL AVMGKNLAWN IESRGYSVSV FNRSSEKTDL MVEESKGKNI HPTYSLEEFV NSLEKPRKIL LMVQAGKATD ATIDSLLPLL DDGDILIDGG NTNYQDTIRR NKALAQSAIN FIGMGVSGGE IGALTGPSLM PGGQEEAYNK VADILDAIAA KAKDGASCVT YIGPNGAGHY VKMVHNGIEY ADMQLIAESY AMMKELLGMS HEDIAQTFKD WNAGELESYL IEITGDIFMK LDENKEALVE KILDTAGQKG TGKWTSINAL ELGIPLTIIT ESVFARFISS IKEERVNASK ELNGPKASFD GDKKDFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGDLAMIWR EGCIIRAQFL QKIKDAYDNN PGLQNLLLDP YFKNIVTEYQ DALRDVVATG VQNGVPTPGF SSSINYYDSY RAADLPANLI QAQRDYFGAH TYERKDKEGV FHTQWIEE // ID 6PGD_STAAM Reviewed; 468 AA. AC Q931R3; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 23-JAN-2007, entry version 29. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=SAV1511; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., RA Ogasawara N., Hayashi H., Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus RT aureus."; RL Lancet 357:1225-1240(2001). 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. 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; BA000017; BAB57673.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR GenomeReviews; BA000017_GR; SAV1511. DR KEGG; sav:SAV1511; -. DR BioCyc; SAUR158878:SAV1511-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090054. SQ SEQUENCE 468 AA; 51784 MW; 07205599873133D5 CRC64; MTQQIGVIGL AVMGKNLAWN IESHGYSVSV FNRSSEKTDL MVEESKGKNI HPTYSLEEFV NSLEKPRKIL LMVQAGKATD ATIDSLLPLL DDGDILIDGG NTNYQDTIRR NKALAQSAIN FIGMGVSGGE IGALTGPSLM PGGQEEAYNK VADILDAIAA KAKDGASCVT YIGPNGAGHY VKMVHNGIEY ADMQLIAESY AMMKELLGMS HEDIAQTFKD WNAGELESYL IEITGDIFMK LDENKEALVE KILDTAGQKG TGKWTSINAL ELGIPLTIIT ESVFARFISS IKEERVNASK ELNGPKASFD GDKKDFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGDLAMIWR EGCIIRAQFL QKIKDAYDNN PGLQNLLLDP YFKNIVTEYQ DALRDVVATG VQNGVPTPGF SSSINYYDSY RAADLPANLI QAQRDYFGAH TYERKDKEGV FHTQWIEE // ID 6PGD_STAAN Reviewed; 468 AA. AC P63334; Q99TY2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 23-JAN-2007, entry version 19. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=SA1342; OS Staphylococcus aureus (strain N315). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=158879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., RA Ogasawara N., Hayashi H., Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus RT aureus."; RL Lancet 357:1225-1240(2001). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017; RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., RA Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., RA Schrenzel J.; RT "Correlation of proteomic and transcriptomic profiles of RT Staphylococcus aureus during the post-exponential phase of growth."; RL J. Microbiol. Methods 60:247-257(2005). 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. 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; BA000018; BAB42604.1; -; Genomic_DNA. DR PIR; G89930; G89930. DR HSSP; P00349; 2PGD. DR SWISS-2DPAGE; P63334; STAAN. DR GenomeReviews; BA000018_GR; SA1342. DR KEGG; sau:SA1342; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090053. SQ SEQUENCE 468 AA; 51803 MW; 61A5C2CAF3CCD011 CRC64; MTQQIGVIGL AVMGKNLAWN IESRGYSVSV FNRSSEKTDL MVEESKGKNI HPTYSLEEFV NSLEKPRKIL LMVQAGKATD ATIDSLLPLL DDGDILIDGG NTNYQDTIRR NKALAQSAIN FIGMGVSGGE IGALTGPSLM PGGQEEAYNK VADILDAIAA KAKDGASCVT YIGPNGAGHY VKMVHNGIEY ADMQLIAESY AMMKELLGMS HEDIAQTFKD WNAGELESYL IEITGDIFMK LDENKEALVE KILDTAGQKG TGKWTSINAL ELGIPLTIIT ESVFARFISS IKEERVNASK ELNGPKASFD GDKKDFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGDLAMIWR EGCIIRAQFL QKIKDAYDNN PGLQNLLLDP YFKNIVTEYQ DALRDVVATG VQNGVPTPGF SSSINYYDSY RAADLPANLI QAQRDYFGAH TYERKDKEGV FHTQWIEE // ID 6PGD_STAAR Reviewed; 468 AA. AC Q6GGI7; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 18. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=SAR1589; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). 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. 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; BX571856; CAG40584.1; -; Genomic_DNA. DR GenomeReviews; BX571856_GR; SAR1589. DR KEGG; sar:SAR1589; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090055. SQ SEQUENCE 468 AA; 51803 MW; 61A5C2CAF3CCD011 CRC64; MTQQIGVIGL AVMGKNLAWN IESRGYSVSV FNRSSEKTDL MVEESKGKNI HPTYSLEEFV NSLEKPRKIL LMVQAGKATD ATIDSLLPLL DDGDILIDGG NTNYQDTIRR NKALAQSAIN FIGMGVSGGE IGALTGPSLM PGGQEEAYNK VADILDAIAA KAKDGASCVT YIGPNGAGHY VKMVHNGIEY ADMQLIAESY AMMKELLGMS HEDIAQTFKD WNAGELESYL IEITGDIFMK LDENKEALVE KILDTAGQKG TGKWTSINAL ELGIPLTIIT ESVFARFISS IKEERVNASK ELNGPKASFD GDKKDFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGDLAMIWR EGCIIRAQFL QKIKDAYDNN PGLQNLLLDP YFKNIVTEYQ DALRDVVATG VQNGVPTPGF SSSINYYDSY RAADLPANLI QAQRDYFGAH TYERKDKEGV FHTQWIEE // ID 6PGD_STAAS Reviewed; 468 AA. AC Q6G954; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 23-JAN-2007, entry version 17. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=SAS1450; OS Staphylococcus aureus (strain MSSA476). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). 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. 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; BX571857; CAG43229.1; -; Genomic_DNA. DR GenomeReviews; BX571857_GR; SAS1450. DR KEGG; sas:SAS1450; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090056. SQ SEQUENCE 468 AA; 51803 MW; 61A5C2CAF3CCD011 CRC64; MTQQIGVIGL AVMGKNLAWN IESRGYSVSV FNRSSEKTDL MVEESKGKNI HPTYSLEEFV NSLEKPRKIL LMVQAGKATD ATIDSLLPLL DDGDILIDGG NTNYQDTIRR NKALAQSAIN FIGMGVSGGE IGALTGPSLM PGGQEEAYNK VADILDAIAA KAKDGASCVT YIGPNGAGHY VKMVHNGIEY ADMQLIAESY AMMKELLGMS HEDIAQTFKD WNAGELESYL IEITGDIFMK LDENKEALVE KILDTAGQKG TGKWTSINAL ELGIPLTIIT ESVFARFISS IKEERVNASK ELNGPKASFD GDKKDFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGDLAMIWR EGCIIRAQFL QKIKDAYDNN PGLQNLLLDP YFKNIVTEYQ DALRDVVATG VQNGVPTPGF SSSINYYDSY RAADLPANLI QAQRDYFGAH TYERKDKEGV FHTQWIEE // ID 6PGD_STAAW Reviewed; 468 AA. AC P63335; Q99TY2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 23-JAN-2007, entry version 18. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=MW1464; OS Staphylococcus aureus (strain MW2). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=196620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5; RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., RA Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., RA Yamamoto K., Hiramatsu K.; RT "Genome and virulence determinants of high virulence community- RT acquired MRSA."; RL Lancet 359:1819-1827(2002). 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. 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; BA000033; BAB95329.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR GenomeReviews; BA000033_GR; MW1464. DR KEGG; sam:MW1464; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090057. SQ SEQUENCE 468 AA; 51803 MW; 61A5C2CAF3CCD011 CRC64; MTQQIGVIGL AVMGKNLAWN IESRGYSVSV FNRSSEKTDL MVEESKGKNI HPTYSLEEFV NSLEKPRKIL LMVQAGKATD ATIDSLLPLL DDGDILIDGG NTNYQDTIRR NKALAQSAIN FIGMGVSGGE IGALTGPSLM PGGQEEAYNK VADILDAIAA KAKDGASCVT YIGPNGAGHY VKMVHNGIEY ADMQLIAESY AMMKELLGMS HEDIAQTFKD WNAGELESYL IEITGDIFMK LDENKEALVE KILDTAGQKG TGKWTSINAL ELGIPLTIIT ESVFARFISS IKEERVNASK ELNGPKASFD GDKKDFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGDLAMIWR EGCIIRAQFL QKIKDAYDNN PGLQNLLLDP YFKNIVTEYQ DALRDVVATG VQNGVPTPGF SSSINYYDSY RAADLPANLI QAQRDYFGAH TYERKDKEGV FHTQWIEE // ID 6PGD_STAEQ Reviewed; 468 AA. AC Q5HP42; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 23-JAN-2007, entry version 17. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=SERP1071; OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=176279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). 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. 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; CP000029; AAW54437.1; -; Genomic_DNA. DR GenomeReviews; CP000029_GR; SERP1071. DR KEGG; ser:SERP1071; -. DR TIGR; SERP1071; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090059. SQ SEQUENCE 468 AA; 52234 MW; A4738F224237494E CRC64; MTQQIGVVGL AVMGKNLAWN IESRGYSVSV YNRSRQKTDE MVKESPGREI YPTYSLEEFV ESLEKPRKIL LMVKAGPATD ATIDGLLPLL DDDDILIDGG NTNYQDTIRR NKALAESSIN FIGMGVSGGE IGALTGPSLM PGGQKDAYNK VSDILDAIAA KAQDGASCVT YIGPNGAGHY VKMVHNGIEY ADMQLIAESY AMMKDLLGMS HKEISQTFKE WNAGELESYL IEITGDIFNK LDDDNEALVE KILDTAGQKG TGKWTSINAL ELGVPLTIIT ESVFARFISS IKEERVTASK SLKGPKAHFE GDKKTFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGELAMIWR EGCIIRAQFL QKIKDAYDNN ENLQNLLLDP YFKNIVMEYQ DALREVVATS VYNGVPTPGF SASINYYDSY RSEDLPANLI QAQRDYFGAH TYERKDREGI FHTQWVEE // ID 6PGD_STAES Reviewed; 468 AA. AC Q8CP47; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 23-JAN-2007, entry version 29. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=SE_1192; OS Staphylococcus epidermidis (strain ATCC 12228). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22832016; PubMed=12950922; RX DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., RA Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., RA Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). 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. 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; AE015929; AAO04791.1; -; Genomic_DNA. DR HSSP; P00349; 2PGD. DR GenomeReviews; AE015929_GR; SE_1192. DR KEGG; sep:SE1192; -. DR BioCyc; SEPI176280:SE1192-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090058. SQ SEQUENCE 468 AA; 52234 MW; A4738F224237494E CRC64; MTQQIGVVGL AVMGKNLAWN IESRGYSVSV YNRSRQKTDE MVKESPGREI YPTYSLEEFV ESLEKPRKIL LMVKAGPATD ATIDGLLPLL DDDDILIDGG NTNYQDTIRR NKALAESSIN FIGMGVSGGE IGALTGPSLM PGGQKDAYNK VSDILDAIAA KAQDGASCVT YIGPNGAGHY VKMVHNGIEY ADMQLIAESY AMMKDLLGMS HKEISQTFKE WNAGELESYL IEITGDIFNK LDDDNEALVE KILDTAGQKG TGKWTSINAL ELGVPLTIIT ESVFARFISS IKEERVTASK SLKGPKAHFE GDKKTFLEKI RKALYMSKIC SYAQGFAQMR KASEDNEWNL KLGELAMIWR EGCIIRAQFL QKIKDAYDNN ENLQNLLLDP YFKNIVMEYQ DALREVVATS VYNGVPTPGF SASINYYDSY RSEDLPANLI QAQRDYFGAH TYERKDREGI FHTQWVEE // ID 6PGD_SYNP7 Reviewed; 471 AA. AC P21577; Q31S98; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 4. DT 23-JAN-2007, entry version 49. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=Synpcc7942_0039; OS Synechococcus sp. (strain PCC 7942) (Anacystis nidulans R2). OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBSTRATE-BINDING SITE. RX MEDLINE=90299831; PubMed=2113917; RA Broedel S.E. Jr., Wolf R.E. Jr.; RT "Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. RT strain PCC 7942 gene (gnd) encoding 6-phosphogluconate RT dehydrogenase."; RL J. Bacteriol. 172:4023-4031(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Culler D.C., Krogmann D.W.; RT "Amino acid sequence comparisons of 6-phosphogluconate RT dehydrogenase."; RL Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC RT 7942."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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. 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; M55002; AAA27330.1; -; Genomic_DNA. DR EMBL; X58719; CAA41555.1; -; Genomic_DNA. DR EMBL; CP000100; ABB56071.1; -; Genomic_DNA. DR PIR; S14628; S14628. DR HSSP; P00349; 2PGD. DR GenomeReviews; CP000100_GR; Synpcc7942_0039. DR KEGG; syf:Synpcc7942_0039; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 471 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090060. FT CONFLICT 154 159 EPIVRS -> SRSVPT (in Ref. 1). FT CONFLICT 159 159 S -> T (in Ref. 2). FT CONFLICT 407 407 A -> R (in Ref. 2). FT CONFLICT 415 439 AAERGIPVPAFSASLDYFDSYRRDR -> RQNEEFRFRFQC FT FPGLLRQLPARS (in Ref. 2). FT CONFLICT 437 441 RDRLP -> ASPA (in Ref. 1). FT CONFLICT 450 453 DYFG -> TTC (in Ref. 1). FT CONFLICT 458 465 ERTDRSGS -> KAPIALL (in Ref. 1). FT CONFLICT 469 470 QW -> M (in Ref. 1). SQ SEQUENCE 471 AA; 51073 MW; 0C75D58209E124E7 CRC64; MALQQFGLIG LAVMGENLAL NIERNGFSLT VYNRTAEKTE AFMADRAQGK NIVPAYSLED FVASLERPRR ILVMVKAGGP VDAVVEQLKP LLDPGDLIID GGNSLFTDTE RRVKDLEALG LGFMGMGVSG GEEGALNGPS LMPGGTQAAY EAVEPIVRSI AAQVDDGPCV TYIGPGGSGH YVKMVHNGIE YGDMQLIAEA YDLLKSVAGL NASELHDVFA AWNKTPELDS FLIEITADIF TKVDDLGTGQ PLVELILDAA GQKGTGRWTV ETALEIGVAI PTIIAAVNAR ILSSIKAERQ AASEILSGPI TEPFSGDRQA FIDSVRDALY CSKICSYAQG MALLAKASQV YNYGLNLGEL ARIWKGGCII RAGFLNKIKQ AYDADPTLAN LLLAPEFRQT ILDRQLAWRR VIAIAAERGI PVPAFSASLD YFDSYRRDRL PQNLTQAQRD YFGAHTYERT DRSGSFHAQW F // ID 6PGD_SYNY3 Reviewed; 482 AA. AC P52208; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 23-JAN-2007, entry version 42. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=sll0329; OS Synechocystis sp. (strain PCC 6803). OC Bacteria; Cyanobacteria; Chroococcales; Synechocystis. OX NCBI_TaxID=1148; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=96127529; PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb RT region from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). 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. 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; BA000022; BAA10105.1; -; Genomic_DNA. DR PIR; S76127; S76127. DR HSSP; P00349; 2PGD. DR GenomeReviews; BA000022_GR; sll0329. DR KEGG; syn:sll0329; -. DR BioCyc; SSP1148:SLL0329-MONOMER; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 482 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090061. SQ SEQUENCE 482 AA; 52874 MW; E3F982A81ABE4E68 CRC64; MQFNVAIMTK RTFGVIGLAV MGENLALNVE SRGFPIAVFN RSPNKTEKFM AERAVGKDIK AAYTVEEFVQ LLERPRKILV MVKAGGPVDA VINELKPLLE EGDMIIDGGN SLYEDTERRT KDLEATGLGF VGMGVSGGEE GALLGPSLMP GGTPAAYKEL EPILTKIAAQ VEDPDNPACV TFIGPGGAGH YVKMVHNGIE YGDMQLIAEA YDILKNGLGL SNEQLHEVFG QWNQTDELNS FLIEISTDIF AKKDPETGGH LIDYILDAAG QKGTGRWTVM SGLELGVPIP TIYAAVNARV MSSLKEERVA ASGQLSGPSK TFSGDVEAWI PKVRDALYCS KMCSYAQGMA LIAKASQEFG YDVNLPEIAR IWKGGCIIRA GFLDKIKKAF KDNPQLPNLL LAPEFKQSIL DRQGPWREVL MLANEMGIAV PAFSSSLDYF DSYRRAVLPQ NLTQAQRDYF GAHTYERTDK PRGEFFHTEW LD // ID 6PGD_TREPA Reviewed; 488 AA. AC O83351; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 20-FEB-2007, entry version 41. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=gnd; OrderedLocusNames=TP_0331; OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nichols; RX MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., RA Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., RA Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., RA Weidman J.F., Smith H.O., Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). 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. 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; AE000520; AAC65319.1; -; Genomic_DNA. DR PIR; A71337; A71337. DR HSSP; P00349; 2PGD. DR GenomeReviews; AE000520_GR; TP0331. DR KEGG; tpa:TP0331; -. DR TIGR; TP_0331; -. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR012284; 6PGD_C_extension. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Gene3D; G3DSA:4.10.390.10; 6PGD_C_extension; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 488 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090062. SQ SEQUENCE 488 AA; 52767 MW; FB69CCCA98DEE6B5 CRC64; MGADIGFIGL AVMGENLVLN IERNGFSVAV FNRTTTVVDR FLAGRAHGKR ITGAHSIAEL VSLLARPRKI MLMVKAGSAV DAVIDQILPL LEKGDLVIDG GNSHYQDTIR RMHALEAAGI HFIGTGVSGG EEGALRGPSL MPGGSAQAWP LVSPIFCAIA AKADDGTPCC DWVGSDGAGH YVKMIHNGIE YGDMQIIAEG YWFMKHALGM SYEHMHHTFT RWNTGRLHSY LIEITAAILA HQDTDGTPLL EKILDAAGQK GTGRWTCVAA LEEGSPLTLI TESVMARSLS AQKQARCKAH RVFGSPVKVS KAETLSAQQR EELVSALEDA LYCAKIVSYA QGFELLSHTA KRRGWTLDFS RIASLWRGGC IIRSGFLSKI SAAFAQQHDL ENLVLAPFFA EELKRACPGW RTIVAESVRQ ALPVPALSAA LAWFDGFTGA ALPANLLQAQ RDYFGAHTYE RTDAPRGEFF HTNWTGTGGD TIAGTYSI // ID 6PGD_TRYBB Reviewed; 479 AA. AC P31072; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 09-JAN-2007, entry version 48. DE 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). GN Name=GND; OS Trypanosoma brucei brucei. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=427; RX MEDLINE=93149212; PubMed=8426618; DOI=10.1016/0166-6851(93)90247-U; RA Barrett M.P., le Page R.W.F.; RT "A 6-phosphogluconate dehydrogenase gene from Trypanosoma brucei."; RL Mol. Biochem. Parasitol. 57:89-100(1993). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX MEDLINE=98411456; PubMed=9737929; DOI=10.1006/jmbi.1998.2059; RA Phillips C., Dohnalek J., Gover S., Barrett M.P., Adams M.J.; RT "A 2.8-A resolution structure of 6-phosphogluconate dehydrogenase from RT the protozoan parasite Trypanosoma brucei: comparison with the sheep RT enzyme accounts for differences in activity with coenzyme and RT substrate analogues."; RL J. Mol. Biol. 282:667-681(1998). 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. CC -!- SUBUNIT: Homodimer. 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; X65623; CAA46577.1; -; Genomic_DNA. DR PIR; A48565; A48565. DR PDB; 1PGJ; X-ray; A/B=2-479. DR InterPro; IPR008927; 6DGDH_C_like. DR InterPro; IPR006183; 6PGD. DR InterPro; IPR006114; 6PGD_C. DR InterPro; IPR012283; 6PGD_C_core. DR InterPro; IPR006113; 6PGD_decarbox. DR InterPro; IPR006115; 6PGD_NAD_bd. DR InterPro; IPR006184; 6PGdom_BS. DR Gene3D; G3DSA:1.10.570.10; 6PGD_C_core; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. KW 3D-structure; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 479 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090071. FT STRAND 3 8 FT HELIX 12 23 FT TURN 24 25 FT STRAND 28 31 FT HELIX 35 44 FT TURN 45 47 FT TURN 49 50 FT HELIX 51 53 FT STRAND 54 56 FT HELIX 60 66 FT STRAND 72 75 FT HELIX 81 93 FT TURN 96 97 FT STRAND 99 102 FT HELIX 108 119 FT TURN 120 122 FT STRAND 124 132 FT HELIX 133 139 FT STRAND 142 147 FT HELIX 149 162 FT TURN 167 168 FT TURN 179 180 FT HELIX 181 209 FT TURN 210 211 FT HELIX 214 226 FT TURN 227 227 FT TURN 229 230 FT HELIX 233 243 FT TURN 247 248 FT STRAND 249 251 FT HELIX 252 255 FT HELIX 265 276 FT TURN 277 277 FT HELIX 281 294 FT TURN 295 295 FT HELIX 296 305 FT TURN 307 310 FT TURN 322 323 FT HELIX 325 356 FT HELIX 362 367 FT TURN 368 369 FT STRAND 370 373 FT TURN 374 375 FT TURN 378 379 FT HELIX 380 389 FT TURN 391 392 FT TURN 396 397 FT HELIX 398 400 FT HELIX 401 421 FT HELIX 427 439 FT TURN 440 440 FT TURN 445 445 FT HELIX 446 458 FT STRAND 462 471 SQ SEQUENCE 479 AA; 52154 MW; 64FED260915ABC2F CRC64; MSMDVGVVGL GVMGANLALN IAEKGFKVAV FNRTYSKSEE FMKANASAPF AGNLKAFETM EAFAASLKKP RKALILVQAG AATDSTTEQL KKVFEKGDIL VDTGNAHFKD QGRRAQQLEA AGLRFLGMGI SGGEEGARKG PAFFPGGTLS VWEEIRPIVE AAAAKADDGR PCVTMNGSGG AGSCVKMYHN SGEYAILQIW GEVFDILRAM GLNNDEVAAV LEDWKSKNFL KSYMLDISIA AARAKDKDGS YLTEHVMDRI GSKGTGLWSA QEALEIGVPA PSLNMAVVSR QFTMYKTERQ ANASNAPGIT QSPGYTLKNK SPSGPEIKQL YDSVCIAIIS CYAQMFQCLR EMDKVHNFGL NLPATIATFR AGCILQGYLL KPMTEAFEKN PNISNLMCAF QTEIRAGLQN YRDMVALITS KLEVSIPVLS ASLNYVTAMF TPTLKYGQLV SLQRDVFGRH GYERVDKDGR ESFQWPELQ // ID 6PGL_ACTAC Reviewed; 232 AA. AC P70715; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 23-JAN-2007, entry version 30. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OS Actinobacillus actinomycetemcomitans (Haemophilus OS actinomycetemcomitans). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=714; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43718 / FDC Y4 / Serotype b; RX MEDLINE=97148607; PubMed=9020051; DOI=10.1006/bbrc.1996.5917; RA Yoshida Y., Nakano Y., Yamashita Y., Koga T.; RT "The gnd gene encoding a novel 6-phosphogluconate dehydrogenase and RT its adjacent region of Actinobacillus actinomycetemcomitans RT chromosomal DNA."; RL Biochem. Biophys. Res. Commun. 230:220-225(1997). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; D88189; BAA13555.1; ALT_INIT; Genomic_DNA. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Hydrolase. FT CHAIN 1 232 6-phosphogluconolactonase. FT /FTId=PRO_0000090088. SQ SEQUENCE 232 AA; 26224 MW; 578F29F1751CC40A CRC64; MNYITFPTAQ HAVEKIAQEF VIYSQLNHPA HISLSGGSTP KLLFKTLAQS PYAEQINWRN LHFWWGDDRM VSPSDPESNY GEVQKLLFDH IQIPAENIHR IRGENEPHFE LKRFQAELSA VISDGVFDWI ILGMGADGHT SSLFPHQTNF DDENLAVIAK HPESGQIRIS KTAKLIEQAK RITYLVTGEG KAEILKEIQS TPAENLPYPA AKIYAKNGVT EWYLDKDAAK LL // ID 6PGL_ANASP Reviewed; 240 AA. AC P46016; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 09-JAN-2007, entry version 36. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=alr1602; OS Anabaena sp. (strain PCC 7120). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Bauer C.C., Scappino L., Haselkorn R.; RT "Bacterial subtracted cDNA libraries containing genes involved in the RT differentiation of vegetative cells to heterocysts allow a new twist RT on an old method of isolating developmental genes."; RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., RA Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., RA Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(2001). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- DEVELOPMENTAL STAGE: Developmentally regulated gene in heterocyst CC development. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; U14553; AAA50355.1; -; Genomic_DNA. DR EMBL; BA000019; BAB77968.1; -; Genomic_DNA. DR PIR; AD2006; AD2006. DR GenomeReviews; BA000019_GR; alr1602. DR KEGG; ana:alr1602; -. DR BioCyc; NOST-PCC-01:NOST-PCC-01-001597-MONOMER; -. DR BioCyc; NSP103690:ALR1602-MONOMER; -. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Heterocyst; Hydrolase. FT CHAIN 1 240 6-phosphogluconolactonase. FT /FTId=PRO_0000090087. FT CONFLICT 13 16 ALIA -> RSI (in Ref. 1). FT CONFLICT 99 99 N -> D (in Ref. 1). FT CONFLICT 235 237 GAE -> RRT (in Ref. 1). SQ SEQUENCE 240 AA; 26183 MW; 69DA7B9A72729F96 CRC64; MKKTVEVLPD QTALIARSLD LILTKLDTAI KQQGRFTIAL SGGSTPKPLY EAIAAQKLPW DKIHVFWGDE RYVSPDHPDS NELMARTAWL DRVDIPAENI HAVPTLDNNP AVSAAKYEQH LQTFFNSAPG EFPALDVVLL GMGDDAHTAS LFPHTEALQV RDRLITVGNK DGNPRITFTY PFINAASSVI FVVAGANKRP ALAQVFAPSA DDLAYPSRFI QPQGELLWLL DAAAGAELSV // ID 6PGL_BLOFL Reviewed; 338 AA. AC Q7VR81; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 06-FEB-2007, entry version 17. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=Bfl341; OS Blochmannia floridanus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia. OX NCBI_TaxID=203907; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22784745; PubMed=12886019; DOI=10.1073/pnas.1533499100; RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., RA van Ham R.C.H.J., Gross R., Moya A.; RT "The genome sequence of Blochmannia floridanus: comparative analysis RT of reduced genomes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; BX248585; CAD83408.1; -; Genomic_DNA. DR HSSP; P52697; 1RI6. DR GenomeReviews; BX248583_GR; Bfl341. DR KEGG; bfl:Bfl341; -. DR BioCyc; BFLO203907:BFL341-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. DR InterPro; IPR011045; N2O_reductase_N. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 338 6-phosphogluconolactonase. FT /FTId=PRO_0000171131. SQ SEQUENCE 338 AA; 38907 MW; E2BBCCA423CDF8DB CRC64; MQIFYISSPD NQKIYVWKLD NHQEKLELMQ VVSTDGCAQP TVVHPNQNFL YVGIRPDFKI DTYRISQNGL LTKIQSTKIC DSPTYLTINI YGTFIYCVSY NFNCINVIKI DKFGLLCNSI QIIKNMLGCH SANINKDRKV LWAPCLQENT IRLFDIDHLY GTLKPHNPHV INTNMQSGPR HMAFHSTDNY AYVINEYNGV IDVIQYNDSI TNLAIIQKIN ILSNHGLDTK KFWSSDIHIT PNNRWLYCAD RFCNTISLFE ILLNTKKLKF INYIYTEDQP RGFLIDSTGN FLIVAGQKSH FITLYRIHAN NGNLSVISRH ASGMGPMWIS ILSKNTIH // ID 6PGL_BORBU Reviewed; 235 AA. AC O51240; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 09-JAN-2007, entry version 39. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=BB_0222; OS Borrelia burgdorferi (Lyme disease spirochete). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia; OC Borrelia burgdorferi group. OX NCBI_TaxID=139; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680; RX MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., RA Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., RA Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., RA Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., RA Roberts K.M., Hatch B., Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia RT burgdorferi."; RL Nature 390:580-586(1997). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE000783; AAC66602.1; -; Genomic_DNA. DR PIR; F70127; F70127. DR GenomeReviews; AE000783_GR; BB_0222. DR KEGG; bbu:BB0222; -. DR TIGR; BB_0222; -. DR BioCyc; BBUR139:BB0222-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:EC. KW Complete proteome; Hydrolase. FT CHAIN 1 235 6-phosphogluconolactonase. FT /FTId=PRO_0000090089. SQ SEQUENCE 235 AA; 27198 MW; A3B16EE42D9E44F8 CRC64; MEFLYSDEEN YLKDRFFDFF NMNVDKDKYT SIGICGGRSI VNFLSVFLKQ NFSFRRSHFF LVDERCVPLN DENSNYNLLN KNFFSKMVDK NLISISKFHA FVYSEIDEAT AIHDYNIEFN SRFNIFDFII VSVGEDGHIA SLFPSRKLLF SDVEGYQYEY NSPKFPSKRI SLTPKSLFGS KAVVLLFMGV DKKCALENFL ASNSSINECP ARLLKEHPNL LVLTNIKRDE SYAGS // ID 6PGL_BUCAI Reviewed; 334 AA. AC P57380; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 06-FEB-2007, entry version 25. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=BU293; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum OS symbiotic bacterium). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=118099; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tokyo 1998; RX MEDLINE=20445173; PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids RT Buchnera sp. APS."; RL Nature 407:81-86(2000). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; BA000003; BAB13003.1; -; Genomic_DNA. DR GenomeReviews; BA000003_GR; BU293. DR KEGG; buc:BU293; -. DR BioCyc; BSP107806:BU293-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 334 6-phosphogluconolactonase. FT /FTId=PRO_0000171128. SQ SEQUENCE 334 AA; 38947 MW; 917BD56378A50908 CRC64; MKQVVYIANS ESKNIEVWNL CKSGKMNLIQ KIETDGKIQP INIIQKRNLL YAGIFPDNKI ITYSINHNGF LEKKNESNIP GKANYISFDK KKEFLFCSSY HSNFISVSPL NKFGIPQNPI QIIYNIEGCH AAKMNYKYNI LFVISLKEDC IYLYYLTDFG ILKSTEQNIL HTQKKSGPRH IIFHPNQDFI YTINELNGTI DVWKIYKKNN VIKVKNIQNI HVLKNRFLKD YWCSDIHITS CGRFLYACDR FFNIISLFHI NQNDNKLVFF KSYDTEEQPR SFNINSHNTH LIVAGEKSNT FIIYSISNST GELKKINVYS TGQRPVWILI HALC // ID 6PGL_BUCAP Reviewed; 333 AA. AC Q8K9N9; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 06-FEB-2007, entry version 25. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=BUsg_282; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; AE013218; AAM67839.1; -; Genomic_DNA. DR GenomeReviews; AE013218_GR; BUsg_282. DR KEGG; bas:BUsg282; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 333 6-phosphogluconolactonase. FT /FTId=PRO_0000171129. SQ SEQUENCE 333 AA; 38373 MW; 7D6B61FAEC29855C CRC64; MQQIIYIANA ESENIEVWIL YNNGDMKLIQ TVQTDGQVQP ISIIKNTKLL YAGIRPKNRV ITYQIDKNGL LKKKKESIVP GTPNYISFDS SEKFLFCSSY HADCISVSPL DKNGIPKDPI QIIHNIEGCH AAKFNSKYNV LFITSLKNDC IYLYYLTHFG ILKSTEQKLV FSQKNSGPRH VIFHPNQNFS YTVNELNGSV DVWKISKENK VLEVKNIQNI KLLNDLISKK YWSSDIHLTS CGNFLYVSDR YLNSISLFHV NKNDNTIIFF KQYLTEEQPR AFCIDRNNNY LIVIGQKSNK LSVYKICQKT GELKKINQYQ TGNGPLWITS FLI // ID 6PGL_BUCBP Reviewed; 331 AA. AC Q89AK3; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 06-FEB-2007, entry version 21. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=bbp_274; OS Buchnera aphidicola subsp. Baizongia pistaciae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=135842; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22426901; PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; AE016826; AAO26999.1; -; Genomic_DNA. DR GenomeReviews; AE016826_GR; bbp_274. DR KEGG; bab:bbp274; -. DR BioCyc; BAPH224915:BBP274-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 331 6-phosphogluconolactonase. FT /FTId=PRO_0000171130. SQ SEQUENCE 331 AA; 37872 MW; C65076CFA856C926 CRC64; MKQIIYITLA KNQEIEVWKL HDDFSLNLLQ RISTQGEPQP IIISKDKKYL YIGVRPKFKV YSYKIKADGT LTKHACSTLP GSPNHFEIDH TGKYLFSSSY HFNCLSITPL DTLGIPRPVT QTIKNIFGCH ASKMNCYNTC LFISALKKDC IYAYNFKKNG KLLKNTRKNF MTNVNFGPRH LDLQKCNNRL YSVNELNGSV DIWSINSFSN ELILLKNINI MSKNYCNAAW SSDLHISPCE KFLYVSDRIE NTISIIKLEK DVQNIEKIGH IKTELQPRTF SINSTGENLI VVGEKSNSFS VYKISKITGL LELKNTYSTG NRPVWISSLM L // ID 6PGL_CAEEL Reviewed; 269 AA. AC O18229; Q2EEL9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2001, sequence version 2. DT 09-JAN-2007, entry version 42. DE Putative 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN ORFNames=Y57G11C.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [2] RP SEQUENCE REVISION, AND ALTERNATIVE SPLICING. RG WormBase consortium; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; CC IsoId=O18229-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=b; CC IsoId=O18229-2; Sequence=VSP_020096; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; Z99281; CAB16505.2; -; Genomic_DNA. DR EMBL; Z99281; CAJ76962.1; -; Genomic_DNA. DR PIR; T27244; T27244. DR UniGene; Cel.11880; -. DR DIP; DIP:26505N; -. DR Ensembl; Y57G11C.3; Caenorhabditis elegans. DR KEGG; cel:Y57G11C.3; -. DR WormBase; WBGene00013301; Y57G11C.3. DR WormPep; Y57G11C.3a; CE24473. DR WormPep; Y57G11C.3b; CE14930. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Alternative splicing; Complete proteome; Hydrolase; KW Hypothetical protein. FT CHAIN 1 269 Putative 6-phosphogluconolactonase. FT /FTId=PRO_0000090080. FT VAR_SEQ 1 12 Missing (in isoform b). FT /FTId=VSP_020096. SQ SEQUENCE 269 AA; 30414 MW; 8E79075016E5071A CRC64; MCLVNEFVSN SNMKPALNVS GDEKELILQL RRYLEEKLTY LLDQNGTVSI GVSGGSMPRV FSKAILSLPQ EQLNWKRIRI FMVDERNVDL DSEESNQGEY LRLFPNELRD VFVPMQIFKD PCLTAQHYEI SLRKYLLPEQ LNNTARFDIL FLGVGPDGHT ASIFPGKERL EKITELNWVS VITDSPKPPP SRITLTLQTL QHAKNVAFII CGKQKAEIVR GICDRDQKYP AAQARPFNDK LTLFLDEDAA TGVPDRDSSD SDSPPPFDG // ID 6PGL_CAUCR Reviewed; 232 AA. AC Q9A6N1; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 09-JAN-2007, entry version 28. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; OrderedLocusNames=CC2056; OS Caulobacter crescentus (Caulobacter vibrioides). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=155892; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19089 / CB15; RX MEDLINE=21173698; PubMed=11259647; DOI=10.1073/pnas.061029298; RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., RA Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J., RA Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J., RA Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L., RA Fraser C.M.; RT "Complete genome sequence of Caulobacter crescentus."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE005879; AAK24029.1; -; Genomic_DNA. DR PIR; A87504; A87504. DR GenomeReviews; AE005673_GR; CC2056. DR KEGG; ccr:CC2056; -. DR TIGR; CC2056; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 232 6-phosphogluconolactonase. FT /FTId=PRO_0000090090. SQ SEQUENCE 232 AA; 24234 MW; 8FBEA52F720F87B6 CRC64; MPFTPIKLEA FGSREDLYDA AASVLVGALT TAVARHGRVG FAATGGTTPA PVYDRMATMT APWDKVTVTL TDERFVPATD ASSNEGLVRR HLLVGEAAKA SFAPLFFDGV SHDESARKAE AGVNAATPFG VVLLGVGPDG HFASLFPGNP MLDQGLDLAT DRSVLAVPPS DPAPDLPRLS LTLAALTRTD LIVLLVTGAA KKALLDGDVD PALPVAAILK QDRAKVRILW AE // ID 6PGL_CHLMU Reviewed; 256 AA. AC Q9PKK7; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-JAN-2007, entry version 34. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; OrderedLocusNames=TC_0458; OS Chlamydia muridarum. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=83560; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MoPn / Nigg; RX MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., RA White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., RA Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., RA Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., RA McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia RT pneumoniae AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE002160; AAF73557.1; -; Genomic_DNA. DR GenomeReviews; AE002160_GR; TC_0458. DR KEGG; cmu:TC0458; -. DR TIGR; TC_0458; -. DR BioCyc; CMUR83560:TC0458-MONOMER; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 256 6-phosphogluconolactonase. FT /FTId=PRO_0000090091. SQ SEQUENCE 256 AA; 28921 MW; 8ACC9D04059199B6 CRC64; MATLISLNDA NRMLIAESQE DFLQIACYDW ISTANKAIQK RGAFYVALSG GKTPLQIFQE IVKKRAAISD CSKIFVFWGD ERASEDTEAG SNYLKAMDIL KWLRIPDTQI FRMDTANPKG DEIYENLIRE HVPDTIFDMV MLGVGEDGHT LSLFPGTAAL EEKDRLVVFN EVPQLQTRRM TLTFPIVRQA RHLVAYIQGT AKQDLCHKLL HPLGRDTFPI ERVGTPLNPL QWVLSSDCCR AADLADIPAE CKLEMF // ID 6PGL_CHLPN Reviewed; 258 AA. AC Q9Z8U5; Q9JSH4; Q9K256; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 09-JAN-2007, entry version 46. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; GN OrderedLocusNames=CPn_0239, CP_0523, CPj0239, CpB0245; OS Chlamydia pneumoniae (Chlamydophila pneumoniae). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila. OX NCBI_TaxID=83558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CWL029; RX MEDLINE=99206606; PubMed=10192388; DOI=10.1038/7716; RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.; RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis."; RL Nat. Genet. 21:385-389(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AR39; RX MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., RA White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., RA Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., RA Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., RA McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia RT pneumoniae AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J138; RX MEDLINE=20330349; PubMed=10871362; DOI=10.1093/nar/28.12.2311; RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.; RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 RT from Japan and CWL029 from USA."; RL Nucleic Acids Res. 28:2311-2314(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW-183; RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.; RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with RT other Chlamydia strains based on whole genome sequence analysis."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase subfamily. CC -!- CAUTION: Ref.3 (BAA98449) sequence differs from that shown due to CC a stop codon at position 42 which was translated as Gly to extend CC the 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; AE001363; AAD18392.1; -; Genomic_DNA. DR EMBL; AE002161; AAF73681.1; ALT_INIT; Genomic_DNA. DR EMBL; BA000008; BAA98449.1; ALT_SEQ; Genomic_DNA. DR EMBL; AE017157; AAP98178.1; ALT_INIT; Genomic_DNA. DR PIR; D72103; D72103. DR PHCI-2DPAGE; Q9Z8U5; -. DR GenomeReviews; AE002161_GR; CP_0523. DR GenomeReviews; AE009440_GR; CpB0245. DR GenomeReviews; BA000008_GR; CPj0239. DR GenomeReviews; AE001363_GR; CPn_0239. DR KEGG; cpa:CP0523; -. DR KEGG; cpj:CPj0239; -. DR KEGG; cpn:CPn0239; -. DR KEGG; cpt:CpB0245; -. DR TIGR; CP_0523; -. DR BioCyc; CPNE115711:CP0523-MONOMER; -. DR BioCyc; CPNE115713:CPN0239-MONOMER; -. DR BioCyc; CPNE182082:CPB0245-MONOMER; -. DR LinkHub; Q9Z8U5; -. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 258 6-phosphogluconolactonase. FT /FTId=PRO_0000090092. FT CONFLICT 46 46 V -> G (in Ref. 3). SQ SEQUENCE 258 AA; 29334 MW; E49CA50014ECB797 CRC64; MATLINFNDT NKLLLTKQPS LFIDLASKDW IASANQAIKQ RGAFYVALSG GKTPLEIYKD IVINKDKLID PSKIFLFWGD ERLAPITSSE SNYGQAMSIL RDLNIPDEQI FRMETENPDG AKKYQELIEN KIPDASFDMI MLGLGEDGHT LSLFSNTSAL EEENDLVVFN SVPHLETERM TLTFPCVHKG KHVVVYVQGE NKKPILKSVF FSEGREEKLY PIERVGRDRS PLFWIISPES YDIADFDNIS SIYKMDIL // ID 6PGL_CHLTR Reviewed; 256 AA. AC O84189; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 09-JAN-2007, entry version 35. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=CT_186; OS Chlamydia trachomatis. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D/UW-3/Cx; RX MEDLINE=99000809; PubMed=9784136; DOI=10.1126/science.282.5389.754; RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., RA Davis R.W.; RT "Genome sequence of an obligate intracellular pathogen of humans: RT Chlamydia trachomatis."; RL Science 282:754-759(1998). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE001273; AAC67778.1; -; Genomic_DNA. DR PIR; C71546; C71546. DR PHCI-2DPAGE; O84189; -. DR GenomeReviews; AE001273_GR; CT_186. DR KEGG; ctr:CT186; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 256 6-phosphogluconolactonase. FT /FTId=PRO_0000090093. SQ SEQUENCE 256 AA; 29014 MW; CA1D6B5668101BF0 CRC64; MATLISLNDA NRMLIADSQE EFLQIACYDW ISTANKAIHK RGAFYVALSG GKTPLQIFQE IVKKRAAISD CSKIVVFWGD ERANEDVEAG SNYLKAMDIL KGLRIPEDQI FRMDTADPKG DEAYEALIQK YVPDAIFDMV MLGVGEDGHT LSLFPETHAL EEKERFVVFN EVPQLHTRRM TLTFPIVRQA RHLVAYVQGE NKQDLFHKLV HPLGRDTFPI ERVGTPLNPV QWVLSSDSCR KTDLADIPAD CKLEMF // ID 6PGL_DROME Reviewed; 243 AA. AC Q9VZ64; Q53XD9; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 23-JAN-2007, entry version 30. DE Putative 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN ORFNames=CG17333; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Larva, and Pupae; RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., RA Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE014298; AAF47963.1; -; Genomic_DNA. DR EMBL; BT012304; AAS77429.1; -; mRNA. DR UniGene; Dm.23623; -. DR Ensembl; CG17333; Drosophila melanogaster. DR KEGG; dme:Dmel_CG17333; -. DR FlyBase; FBgn0030239; CG17333. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-001390-MONOMER; -. DR GermOnline; CG17333; Drosophila melanogaster. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; NAS:UniProtKB. DR GO; GO:0006098; P:pentose-phosphate shunt; NAS:UniProtKB. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase; Hypothetical protein. FT CHAIN 1 243 Putative 6-phosphogluconolactonase. FT /FTId=PRO_0000090081. SQ SEQUENCE 243 AA; 26672 MW; 0E23EFDCF5FE042E CRC64; MSEKKGALKV IPSASEEQLV QALGDLLQRC SQEALAKHDK FSVGLSGGSL VQLLTKALKS CNLKTAKWVF FFCDERYVRL DDSDSTYGAY RAEWLTQLPC IQESQFVRAD TSQPLDACAA DYEAKVKSQV DRFDLLLLGM GPDGHTCSLF PEQPATLQET KRLVIPIRNS PKPPPERITF TLPLINKARN VAFVVTGAAK ASVVKSVFVD LDKKFPAAWV NPTKGQLTLI VDAGAGKEIE TLK // ID 6PGL_ECO57 Reviewed; 331 AA. AC Q8X926; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 06-FEB-2007, entry version 28. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=Z0938, ECs0795; OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; AE005174; AAG55096.1; -; Genomic_DNA. DR EMBL; BA000007; BAB34218.1; -; Genomic_DNA. DR PIR; C90728; C90728. DR SMR; Q8X926; 1-331. DR GenomeReviews; BA000007_GR; ECs0795. DR GenomeReviews; AE005174_GR; Z0938. DR KEGG; ece:Z0938; -. DR KEGG; ecs:ECs0795; -. DR BioCyc; ECOL83334-1:ECS0795-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. DR InterPro; IPR003143; Cyt_d1_haem. DR Gene3D; G3DSA:2.140.10.20; Cyt_d1_haem; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 331 6-phosphogluconolactonase. FT /FTId=PRO_0000171134. SQ SEQUENCE 331 AA; 36391 MW; BC4A7F215D231BDE CRC64; MKQTVYIASP ESQQIHVWNL NHEGALTLTQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV LAYRIAPDDG ALTFAAESAL PGSPTHISTD HQGQFVFVGS YNAGNVSVTR LEDGLPVGVV DVVEGLDGCH SANISPDNRT LWVPALKQDR ICLFTVSDDG HLVAQDPAEV TTVEGAGPRH MVFHPNEQYA YCVNELNSSV DVWELKDPHG NIECVQTLDM MPENFSDTRW AADIHITPDG RHLYACDRTA SLITVFSVSE DGSVLSKEGF QPTETQPRGF NIDHRGKYLI AAGQKSHHIS VYEIVGEQGL LHEKGRYAVG QGPMWVVVNA H // ID 6PGL_ECOL6 Reviewed; 331 AA. AC Q8FJR2; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 06-FEB-2007, entry version 22. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=c_0844; OS Escherichia coli O6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=217992; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC; RX MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; AE014075; AAN79317.1; -; Genomic_DNA. DR HSSP; P52697; 1RI6. DR SMR; Q8FJR2; 1-331. DR GenomeReviews; AE014075_GR; c_0844. DR KEGG; ecc:c0844; -. DR BioCyc; ECOL199310:C0844-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. DR InterPro; IPR003143; Cyt_d1_haem. DR Gene3D; G3DSA:2.140.10.20; Cyt_d1_haem; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 331 6-phosphogluconolactonase. FT /FTId=PRO_0000171133. SQ SEQUENCE 331 AA; 36309 MW; 7665044CFCF31A95 CRC64; MKQTVYIASP ESQQIHVWNL NHEGALTLTQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV LAYRIAPDDG ALTFAAESAL PGSPTHISTD HQGQFVFVGS YNAGNVSVTR LEDGLPVGVV DVVEGLDGCH SANISPDNRT LWVPALKQDR ICLFTVSDDG HLVAQDPAEV TTVEGAGPRH MVFHPNEQYA YCVNELNSSV DVWELKDPHG NIECVQTLDM MPENFSDTRW AADIHITPDG RHLYACDRTA SLITVFSVSE DGSVLSKEGF QPTETQPRGF NVDHSGKYLI AAGQKSHHIS VYEIVGEEGL LHEKGRYAVG QGPMWVVVNA H // ID 6PGL_ECOLI Reviewed; 331 AA. AC P52697; P75760; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 20-FEB-2007, entry version 48. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase) (Pgl). GN Name=pgl; OrderedLocusNames=b0767, JW0750; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=95394784; PubMed=7665460; RA Maupin-Furlow J.A., Rosentel J.K., Lee J.H., Deppenmeier U., RA Gunsalus R.P., Shanmugam K.T.; RT "Genetic analysis of the modABCD (molybdate transport) operon of RT Escherichia coli."; RL J. Bacteriol. 177:4851-4856(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97061202; PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., RA Yano M., Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP IDENTIFICATION. RA Rudd K.E.; RL Unpublished observations (MAR-1996). RN [6] RP FUNCTION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15576773; DOI=10.1128/JB.186.24.8248-8253.2004; RA Thomason L.C., Court D.L., Datta A.R., Khanna R., Rosner J.L.; RT "Identification of the Escherichia coli K-12 ybhE gene as pgl, RT encoding 6-phosphogluconolactonase."; RL J. Bacteriol. 186:8248-8253(2004). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RA Lima C.D., Kniewel R., Solorzano V., Wu J.; RT "Structure of a putative 7-bladed propeller isomerase."; RL Submitted (NOV-2003) to the PDB data bank. CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 2 family. CC -!- CAUTION: Ref.1 (U27192) sequence differs from that shown due to a CC frameshift in position 110. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U27192; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U00096; AAC73854.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35431.1; -; Genomic_DNA. DR PIR; G64812; G64812. DR PDB; 1RI6; X-ray; A=2-331. DR IntAct; P52697; -. DR GenomeReviews; U00096_GR; b0767. DR GenomeReviews; AP009048_GR; JW0750. DR KEGG; ecj:JW0750; -. DR KEGG; eco:b0767; -. DR EchoBASE; EB3020; -. DR EcoGene; EG13231; pgl. DR BioCyc; EcoCyc:6PGLUCONOLACT-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR HAMAP; MF_01605; -; 1. DR InterPro; IPR003143; Cyt_d1_haem. DR Gene3D; G3DSA:2.140.10.20; Cyt_d1_haem; 1. KW 3D-structure; Carbohydrate metabolism; Complete proteome; KW Glucose metabolism; Hydrolase. FT CHAIN 1 331 6-phosphogluconolactonase. FT /FTId=PRO_0000171132. FT CONFLICT 37 52 QVQPMVVSPDKRYLYV -> RCSRWWSARTNVISML (in FT Ref. 1). FT CONFLICT 319 331 VGQGPMWVVVNAH -> SGRDQCGWWLTHTKR (in Ref. FT 1). FT STRAND 2 9 FT HELIX 10 12 FT TURN 13 13 FT STRAND 14 20 FT TURN 22 23 FT STRAND 26 33 FT STRAND 41 43 FT TURN 45 46 FT STRAND 47 54 FT TURN 55 58 FT STRAND 59 65 FT TURN 67 69 FT STRAND 72 79 FT STRAND 85 89 FT TURN 91 92 FT STRAND 93 100 FT TURN 101 104 FT STRAND 105 112 FT TURN 113 114 FT STRAND 115 123 FT TURN 127 128 FT TURN 136 137 FT STRAND 138 145 FT HELIX 146 148 FT TURN 149 149 FT STRAND 150 156 FT TURN 158 159 FT STRAND 162 171 FT TURN 174 175 FT STRAND 178 183 FT TURN 185 186 FT STRAND 187 194 FT TURN 195 198 FT STRAND 199 206 FT TURN 208 209 FT STRAND 213 219 FT TURN 223 224 FT STRAND 231 236 FT TURN 238 239 FT STRAND 240 247 FT TURN 248 251 FT STRAND 252 258 FT TURN 260 261 FT STRAND 265 272 FT STRAND 274 276 FT STRAND 280 282 FT TURN 284 285 FT STRAND 286 292 FT TURN 294 296 FT STRAND 298 305 FT TURN 306 309 FT STRAND 310 318 FT STRAND 320 322 SQ SEQUENCE 331 AA; 36308 MW; D731044CFCF31A8F CRC64; MKQTVYIASP ESQQIHVWNL NHEGALTLTQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV LAYRIAPDDG ALTFAAESAL PGSPTHISTD HQGQFVFVGS YNAGNVSVTR LEDGLPVGVV DVVEGLDGCH SANISPDNRT LWVPALKQDR ICLFTVSDDG HLVAQDPAEV TTVEGAGPRH MVFHPNEQYA YCVNELNSSV DVWELKDPHG NIECVQTLDM MPENFSDTRW AADIHITPDG RHLYACDRTA SLITVFSVSE DGSVLSKEGF QPTETQPRGF NVDHSGKYLI AAGQKSHHIS VYEIVGEQGL LHEKGRYAVG QGPMWVVVNA H // ID 6PGL_ERWCT Reviewed; 332 AA. AC Q6D7C2; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 06-FEB-2007, entry version 17. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=ECA1403; OS Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=29471; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCRI 1043 / ATCC BAA-672; RX PubMed=15263089; DOI=10.1073/pnas.0402424101; RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H., RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.; RT "Genome sequence of the enterobacterial phytopathogen Erwinia RT carotovora subsp. atroseptica and characterization of virulence RT factors."; RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; BX950851; CAG74313.1; -; Genomic_DNA. DR GenomeReviews; BX950851_GR; ECA1403. DR KEGG; eca:ECA1403; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. DR InterPro; IPR011045; N2O_reductase_N. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 332 6-phosphogluconolactonase. FT /FTId=PRO_0000171135. SQ SEQUENCE 332 AA; 36134 MW; F2EEB874B1D0CE65 CRC64; MQQVVYVASP ESQQIHVWQL GAQGNLTLLQ TVEVPGQVQP MAIAPNKRHL YVGVRPDFRV LSYRIDEQGK LTEAGVASLP GSPTHLSTDN DGRFLFSASY SGACVSVSPI DADGIVGEPI QQLDGLEGCH STNIDPTNTV VWAPCLKEDR IRLYDLGSVG ELSIHRQAEM TTVSGAGPRH MAFHPNQRFA YCVNELDSSV DVYQLDAASG DVQKVQTLDA MPAGFSDTRW AADIHITPNG NFLYISDRTA SLLSVFQISE DGSTLTLTGH QPTETQPRGF NIDHTGEFLI SAGQKSQHIE VYHIDQHTGD LQPLARYAVG QGPMWVAVLA LD // ID 6PGL_HAEIN Reviewed; 232 AA. AC Q57039; P96334; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 20-FEB-2007, entry version 40. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=HI0556; OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase subfamily. CC -!- CAUTION: Ref.1 (AAC22212) sequence differs from that shown due to CC a frameshift in position 29. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22212.1; ALT_FRAME; Genomic_DNA. DR GenomeReviews; L42023_GR; HI0556. DR KEGG; hin:HI0556; -. DR TIGR; HI0556; -. DR BioCyc; HINF71421:HI0556-MONOMER; -. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 232 6-phosphogluconolactonase. FT /FTId=PRO_0000090094. SQ SEQUENCE 232 AA; 26307 MW; 4744738C62D3B11D CRC64; MNYISFPTAQ HAVDKIAQEF VIYSQLNHPV HISLSGGSTP KLLFKTLAKS PYAEQINWKN LHFWWGDDRM VPPSDPESNY GEVQKLLFDH IQIPAENIHR IRGENEPHFE LKRFEEELSA VIPNGVFDWI ILGMGIDGHT ASLFPHQTNF DDENLAVIAK HPESGQIRIS KTAKLIEQAK RITYLVTGES KADILKEIQT TPAENLPYPA AKIKAKNGVT EWYLDKAAVR LL // ID 6PGL_HELPJ Reviewed; 227 AA. AC Q9ZKB1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 09-JAN-2007, entry version 32. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=jhp_1028; OS Helicobacter pylori J99 (Campylobacter pylori J99). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=99120557; PubMed=9923682; DOI=10.1038/16495; RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., RA Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., RA Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., RA Trust T.J.; RT "Genomic sequence comparison of two unrelated isolates of the human RT gastric pathogen Helicobacter pylori."; RL Nature 397:176-180(1999). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE001439; AAD06599.1; -; Genomic_DNA. DR PIR; G71859; G71859. DR GenomeReviews; AE001439_GR; jhp_1028. DR KEGG; hpj:jhp1028; -. DR BioCyc; HPYL85963:JHP1028-MONOMER; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 227 6-phosphogluconolactonase. FT /FTId=PRO_0000090096. SQ SEQUENCE 227 AA; 25636 MW; 7BB329FBEF187E3C CRC64; MGYQLFEFEN LEDCHKALIE RFKEFFNAAL KKHHQVSVAF SGGRSPISLL QKLSVLDLKW HECLISLVDE RIIEASHEDS NAKLLHDYLL QNNALKASFT PLLPEKISGD TNELLDFANQ HFKQPHLAIL GMGTDGHTAS LFPETSAFLN EEKENIVLTK PTNAPYERLS MSINALENCE KLFLSISGVE KRGVLEKALK ENAPYSLPIA RILHSKKVTT EVFYAKN // ID 6PGL_HELPY Reviewed; 227 AA. AC O25730; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 20-FEB-2007, entry version 35. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=HP_1102; OS Helicobacter pylori (Campylobacter pylori). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=210; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., RA Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., RA Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., RA Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., RA Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., RA Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., RA Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., RA Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE000511; AAD08145.1; -; Genomic_DNA. DR PIR; F64657; F64657. DR DIP; DIP:3651N; -. DR GenomeReviews; AE000511_GR; HP1102. DR KEGG; hpy:HP1102; -. DR TIGR; HP_1102; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 227 6-phosphogluconolactonase. FT /FTId=PRO_0000090095. SQ SEQUENCE 227 AA; 25728 MW; B2592B35B63971A6 CRC64; MGYQLFEFEN LKDCHKALTE RFKEFFNTAL KKHHQISIAF SGGRSPISLL QKLSVLNLKW HECLISLVDE RIIDTSHDDS NTKLLHDYLL QNNALKASFI PLLPEKISSD TNALFNFANQ HFKQPHLAIL GMGTDGHTAS LFPETSAFLN EEKENIVLTK PINAPYERLS MSVNALENCE KLFLSISGVE KRGVLEKALK ENAPYSLPIA RILHSQKVTT EVFYAKN // ID 6PGL_HUMAN Reviewed; 258 AA. AC O95336; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 06-FEB-2007, entry version 48. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=PGLS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=99447648; PubMed=10518023; DOI=10.1016/S0014-5793(99)01247-8; RA Collard F., Collet J.-F., Gerin I., Veiga-da-Cunha M., RA van Schaftingen E.; RT "Identification of the cDNA encoding human 6-phosphogluconolactonase, RT the enzyme catalyzing the second step of the pentose phosphate RT pathway."; RL FEBS Lett. 459:223-226(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 97-242. RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.; RT "Full-insert sequence of mapped XREF EST."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AJ243972; CAB57866.1; -; mRNA. DR EMBL; BC014006; AAH14006.1; -; mRNA. DR EMBL; AF091091; AAC72960.1; ALT_INIT; mRNA. DR UniGene; Hs.466165; -. DR OGP; O95336; -. DR REPRODUCTION-2DPAGE; O95336; HUMAN. DR Ensembl; ENSG00000130313; Homo sapiens. DR KEGG; hsa:25796; -. DR H-InvDB; HIX0014894; -. DR HGNC; HGNC:8903; PGLS. DR MIM; 604951; gene. DR Reactome; REACT_1709.1; Metabolism of small molecules. DR ArrayExpress; O95336; -. DR GermOnline; ENSG00000130313; Homo sapiens. DR RZPD-ProtExp; IOH13028; -. DR RZPD-ProtExp; RZPDo839E0668; -. DR GO; GO:0006098; P:pentose-phosphate shunt; TAS:ProtInc. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Hydrolase. FT CHAIN 1 258 6-phosphogluconolactonase. FT /FTId=PRO_0000090078. SQ SEQUENCE 258 AA; 27547 MW; A753FB7E662116DD CRC64; MAAPAPGLIS VFSSSQELGA ALAQLVAQRA ACCLAGARAR FALGLSGGSL VSMLARELPA AVAPAGPASL ARWTLGFCDE RLVPFDHAES TYGLYRTHLL SRLPIPESQV ITINPELPVE EAAEDYAKKL RQAFQGDSIP VFDLLILGVG PDGHTCSLFP DHPLLQEREK IVAPISDSPK PPPQRVTLTL PVLNAARTVI FVATGEGKAA VLKRILEDQE ENPLPAALVQ PHTGKLCWFL DEAAARLLTV PFEKHSTL // ID 6PGL_MOUSE Reviewed; 257 AA. AC Q9CQ60; Q3TA62; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 06-FEB-2007, entry version 36. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=Pgls; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, 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 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: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AK003134; BAB22594.1; -; mRNA. DR EMBL; AK003985; BAB23106.1; -; mRNA. DR EMBL; AK172066; BAE42808.1; -; mRNA. DR EMBL; BC006594; AAH06594.1; -; mRNA. DR UniGene; Mm.282284; -. DR UniGene; Mm.402679; -. DR REPRODUCTION-2DPAGE; Q9CQ60; MOUSE. DR Ensembl; ENSMUSG00000031807; Mus musculus. DR KEGG; mmu:66171; -. DR MGI; MGI:1913421; Pgls. DR ArrayExpress; Q9CQ60; -. DR GermOnline; ENSMUSG00000031807; Mus musculus. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Hydrolase. FT CHAIN 1 257 6-phosphogluconolactonase. FT /FTId=PRO_0000090079. SQ SEQUENCE 257 AA; 27254 MW; C19AF8CFC21F01C5 CRC64; MAAPAPSLIS VFSSPQELGA SLAQLVAQRA ASCLEGDRGR FALGLSGGSL VSMLARDLPA AAAPAGPASF ARWTLGFCDE RLVPFDHAES TYGLYRTHLL SKLPIPDSQV LTINPALPVE DAAEDYARKL RQALQGDAVP VFDLLILGVG PDGHTCSLFP DHPLLQEREK IVAPISDSPK PPPQRVTLTL PVLNAAQSII FVATGEGKAA VLKRILEDKE GTLPAALVQP RTGALCWFLD EAAARLLSVP FEKHSTL // ID 6PGL_MYCBO Reviewed; 247 AA. AC P63339; O06814; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-JAN-2007, entry version 13. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=Mb1480c; OS Mycobacterium bovis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1765; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX MEDLINE=22709107; PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., RA Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., RA Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., RA Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; BX248339; CAD96147.1; -; Genomic_DNA. DR GenomeReviews; BX248333_GR; Mb1480c. DR KEGG; mbo:Mb1480c; -. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 247 6-phosphogluconolactonase. FT /FTId=PRO_0000090099. SQ SEQUENCE 247 AA; 25804 MW; 1639B68A595D7D2C CRC64; MSSSIEIFPD SDILVAAAGK RLVGAIGAAV AARGQALIVL TGGGNGIALL RYLSAQAQQI EWSKVHLFWG DERYVPEDDD ERNLKQARRA LLNHVDIPSN QVHPMAASDG DFGGDLDAAA LAYEQVLAAS AAPGDPAPNF DVHLLGMGPE GHINSLFPHS PAVLESTRMV VAVDDSPKPP PRRITLTLPA IQRSREVWLL VSGPGKADAV AAAIGGADPV SVPAAGAVGR QNTLWLLDRD AAAKLPS // ID 6PGL_MYCLE Reviewed; 247 AA. AC Q49700; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-JAN-2007, entry version 35. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=ML0579; GN ORFNames=B1496_F1_31; OS Mycobacterium leprae. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1769; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Smith D.R., Robison K.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN; RX MEDLINE=21128732; PubMed=11234002; DOI=10.1038/35059006; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; U00013; AAA17114.1; -; Genomic_DNA. DR EMBL; AL583919; CAC30087.1; -; Genomic_DNA. DR PIR; S72775; S72775. DR GenomeReviews; AL450380_GR; ML0579. DR KEGG; mle:ML0579; -. DR Leproma; ML0579; -. DR BioCyc; MLEP1769:ML0579-MONOMER; -. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 247 6-phosphogluconolactonase. FT /FTId=PRO_0000090100. SQ SEQUENCE 247 AA; 26161 MW; 70FECAA8728FC34E CRC64; MSASVEIFSD SKTMVGAAGK RLASTIQSAV AARERALIVL TGGSSGIGLL RDLATRGQQI DWSRVHLFWG DERYVPKDDD ERNEKQARVA LLDHIDIPPS QVHPMPAGDG EFGNDLEAAA LAYEQLLAAY AAPGYPTPNF DVHLMGMGPE GHINSLFPNT VAVRETSRMV VGVRNSPKPP PERITLTLNA IQRSREVWLM VSGTAKADAV AAAMGGAPSA SIPAAGAVGL ETTLWLLDEE AAAKIPG // ID 6PGL_MYCTU Reviewed; 247 AA. AC P63338; O06814; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-JAN-2007, entry version 15. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=Rv1445c, MT1492; GN ORFNames=MTCY493.09; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; BX842576; CAB09261.1; -; Genomic_DNA. DR EMBL; AE000516; AAK45755.1; -; Genomic_DNA. DR PIR; H70916; H70916. DR GenomeReviews; AE000516_GR; MT1492. DR GenomeReviews; AL123456_GR; Rv1445c. DR KEGG; mtc:MT1492; -. DR KEGG; mtu:Rv1445c; -. DR TIGR; MT1492; -. DR TubercuList; Rv1445c; -. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 247 6-phosphogluconolactonase. FT /FTId=PRO_0000090101. SQ SEQUENCE 247 AA; 25804 MW; 1639B68A595D7D2C CRC64; MSSSIEIFPD SDILVAAAGK RLVGAIGAAV AARGQALIVL TGGGNGIALL RYLSAQAQQI EWSKVHLFWG DERYVPEDDD ERNLKQARRA LLNHVDIPSN QVHPMAASDG DFGGDLDAAA LAYEQVLAAS AAPGDPAPNF DVHLLGMGPE GHINSLFPHS PAVLESTRMV VAVDDSPKPP PRRITLTLPA IQRSREVWLL VSGPGKADAV AAAIGGADPV SVPAAGAVGR QNTLWLLDRD AAAKLPS // ID 6PGL_NEIMA Reviewed; 231 AA. AC P63336; Q9JR64; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 20-FEB-2007, entry version 13. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; OrderedLocusNames=NMA1608; OS Neisseria meningitidis serogroup A. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=65699; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Z2491 / Serogroup A / Serotype 4A; RX MEDLINE=20222556; PubMed=10761919; DOI=10.1038/35006655; RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., RA Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., RA Jagels K., Leather S., Moule S., Mungall K.L., Quail M.A., RA Rajandream M.A., Rutherford K.M., Simmonds M., Skelton J., RA Whitehead S., Spratt B.G., Barrell B.G.; RT "Complete DNA sequence of a serogroup A strain of Neisseria RT meningitidis Z2491."; RL Nature 404:502-506(2000). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AL162756; CAB84836.1; -; Genomic_DNA. DR KEGG; nma:NMA1608; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 231 6-phosphogluconolactonase. FT /FTId=PRO_0000090097. SQ SEQUENCE 231 AA; 24980 MW; 5EF54C495553D073 CRC64; MFVWHEYENA AEAAQSLADA VADALQGALD EKGGAVLAVS GGRSPIAFFN ALSQKDLDWK NVGITLADER IVPTVHADSN TGLVREYLLK NKAEAAMWIP MVEDGKTETE LHPDAVVDYA LKHYKQPDVL VLGMGNDGHT ASIFPKAPQF QTAIDGSAGV ALVHTTPVTA PHERVSMTLD AIAHTGHVFL AIRGEEKKAV FDQAAQGENR EYPINLVLNH QGVNCHVFYA E // ID 6PGL_NEIMB Reviewed; 231 AA. AC P63337; Q9JR64; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-JAN-2007, entry version 13. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; OrderedLocusNames=NMB1391; OS Neisseria meningitidis serogroup B. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=491; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 / Serogroup B; RX MEDLINE=20175755; PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE002098; AAF41755.1; -; Genomic_DNA. DR PIR; F81089; F81089. DR GenomeReviews; AE002098_GR; NMB1391. DR KEGG; nme:NMB1391; -. DR TIGR; NMB1391; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 231 6-phosphogluconolactonase. FT /FTId=PRO_0000090098. SQ SEQUENCE 231 AA; 24980 MW; 5EF54C495553D073 CRC64; MFVWHEYENA AEAAQSLADA VADALQGALD EKGGAVLAVS GGRSPIAFFN ALSQKDLDWK NVGITLADER IVPTVHADSN TGLVREYLLK NKAEAAMWIP MVEDGKTETE LHPDAVVDYA LKHYKQPDVL VLGMGNDGHT ASIFPKAPQF QTAIDGSAGV ALVHTTPVTA PHERVSMTLD AIAHTGHVFL AIRGEEKKAV FDQAAQGENR EYPINLVLNH QGVNCHVFYA E // ID 6PGL_PHOLL Reviewed; 328 AA. AC Q7N6R1; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 06-FEB-2007, entry version 18. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=plu1480; OS Photorhabdus luminescens subsp. laumondii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Photorhabdus. OX NCBI_TaxID=141679; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TT01; RX MEDLINE=22957627; PubMed=14528314; DOI=10.1038/nbt886; RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., RA Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V., RA Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.; RT "The genome sequence of the entomopathogenic bacterium Photorhabdus RT luminescens."; RL Nat. Biotechnol. 21:1307-1313(2003). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; BX571864; CAE13773.1; -; Genomic_DNA. DR HSSP; P52697; 1RI6. DR GenomeReviews; BX470251_GR; plu1480. DR KEGG; plu:plu1480; -. DR PhotoList; plu1480; -. DR BioCyc; PLUM243265:PLU1480-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 328 6-phosphogluconolactonase. FT /FTId=PRO_0000171136. SQ SEQUENCE 328 AA; 36427 MW; 5B09687ABA289EB0 CRC64; MKQVVYTASP NSCQIHVWSL NNEGELSLIQ TVDVPGEVQP MVVSPDRKHL YVGIRPQFSI VTYQIGSRGE LAQQGISSIP GSPTHISTDK QGRFLFSASY SYNNLSVSLI DDQGIVGEPV QVIAGLQAPH SANIDWDNKQ LLVPCLKEDR VRIFEMAKEG YLTEKRAEEI TTAMGAGPRH MAFHPNQQVI YCINELDSTV DVYRKWEKYR TVQTVDSLPA DLAGVRWSAD IHITPDGRHL YTSERTSSLI SHFVISQDGS NLTLAGHYKT EIQPRGFAID HSGKYLIASG QKSDHISVSS IDKYTGKLTE LTRYPVGKGP MWVTVLAL // ID 6PGL_PSEAE Reviewed; 238 AA. AC Q9X2N2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 09-JAN-2007, entry version 31. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=PA3182; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RA Hager P.W., Dail M.B., Phibbs P.V. Jr.; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AF029673; AAD22666.1; ALT_INIT; Genomic_DNA. DR EMBL; AE004091; AAG06570.1; -; Genomic_DNA. DR PIR; H83247; H83247. DR GenomeReviews; AE004091_GR; PA3182. DR KEGG; pae:PA3182; -. DR BioCyc; PAER287:PA3182-MONOMER; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 238 6-phosphogluconolactonase. FT /FTId=PRO_0000090102. SQ SEQUENCE 238 AA; 25571 MW; EECE335BBE904F46 CRC64; MAISELKLPA GVGLQVWGSA AEQARGLAAE VAGRLRSALA EQGQALLVVS GGRSPVAFLE ALSEEPLDWS RITVSLADER WVPESHADSN AGLVRRHLLR GEAAKARFIG LYQPAASLEE AAELADHHLH ELPLPIDVLV LGMGDDGHTA SLFPNSPGLD LAMDPQGTRR CLPMWAPSVP HQRLTLPRAV LAAAKVQLLA IQGQSKLATL NAALAVEDER RMPVRAFLRA PLTIHWYP // ID 6PGL_PSEPU Reviewed; 242 AA. AC Q9EV79; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 09-JAN-2007, entry version 24. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; OS Pseudomonas putida. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=H; RA Petruschka L., Burchhardt G., Juergensen J., Adolf K., Herrmann H.; RT "Analysis of the zwf-operon in Pseudomonas putida H."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AJ279003; CAC14909.1; -; Genomic_DNA. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Hydrolase. FT CHAIN 1 242 6-phosphogluconolactonase. FT /FTId=PRO_0000090103. SQ SEQUENCE 242 AA; 25322 MW; 70F10B7CF5296AC9 CRC64; MGGRGMGISE LKLPAAVKVH ELADAKTLAA TLAHDVAERL RAAIAAKGQA CVVLSGGRSP VPFLEKLASE PLDWAKVTVS LADERWVPVE HADSNAGLLA RHLLTGAAAK ARFVGLYQQA ENLDAAALKA DQALTGLPPI DVLVLGMGDD GHTASLFPAS PNLEAGLDLA STRRCLPLLA PSVPHQRLSM TRSLLASAAF IALSVQGPGK LATLRAALAG NDLTEMPIRA FLHDPLDIYW CP // ID 6PGL_RHILO Reviewed; 238 AA. AC Q989A3; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 09-JAN-2007, entry version 23. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; OrderedLocusNames=mll6514; OS Rhizobium loti (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=381; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF303099; RX MEDLINE=21082930; PubMed=11214968; DOI=10.1093/dnares/7.6.331; RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium RT Mesorhizobium loti."; RL DNA Res. 7:331-338(2000). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; BA000012; BAB52794.1; -; Genomic_DNA. DR GenomeReviews; BA000012_GR; mll6514. DR KEGG; mlo:mll6514; -. DR BioCyc; MLOT381:MLL6514-MONOMER; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 238 6-phosphogluconolactonase. FT /FTId=PRO_0000090104. SQ SEQUENCE 238 AA; 25100 MW; D6D3E0F1D2D2908B CRC64; MAREQLNGAS YNWNAFPDRP QLAVALAGRV ADRLTRAIAE RGTAVLAVSG GTTPTKFFAA LSAMPIAWDK VIVTLVDERF VPASSPRSNA GLVAANLLQN AAKAARFVPL YHEASGIEDA AASDDAALRS LPWPLDVVVL GMGPDGHTAS FFPDADDLAE LLDPASDRII LPVHAASAGE PRLTLTLARI IDAGFIALHI EGEDKRTAFD GAVAPGPRKP IRAVLDAAPR PVEVFWAP // ID 6PGL_RHIME Reviewed; 232 AA. AC Q9Z3S1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 24-OCT-2001, sequence version 2. DT 23-JAN-2007, entry version 36. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=R00703; ORFNames=SMc03069; OS Rhizobium meliloti (Sinorhizobium meliloti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=382; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=99328961; PubMed=10400573; RA Willis L.B., Walker G.C.; RT "A novel Sinorhizobium meliloti operon encodes an alpha-glucosidase RT and a periplasmic-binding-protein-dependent transport system for RT alpha-glucosides."; RL J. Bacteriol. 181:4176-4184(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX MEDLINE=21396507; PubMed=11481430; DOI=10.1073/pnas.161294398; RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., RA Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., RA Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.; RT "Analysis of the chromosome sequence of the legume symbiont RT Sinorhizobium meliloti strain 1021."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase subfamily. CC -!- CAUTION: Seems to have a sequencing error in the C-terminal region CC when compared to orthologs, but the potentially correct sequence CC could not be inferred. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF045609; AAD12044.1; -; Genomic_DNA. DR EMBL; AL591784; CAC45275.1; -; Genomic_DNA. DR GenomeReviews; AL591688_GR; R00703. DR KEGG; sme:SMc03069; -. DR BioCyc; SMEL382:SMC03069-MONOMER; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 232 6-phosphogluconolactonase. FT /FTId=PRO_0000090105. FT CONFLICT 184 227 Missing (in Ref. 1). SQ SEQUENCE 232 AA; 24408 MW; 5A29D02A62FCEED7 CRC64; MSANMHIFEN PSALAEALAD DVGARLAAAI AARGTASLAV SGGSTPKAFF RSLSRRELDW SKVTVTLVDE RFVPPENDRS NHRLVADNLL KDGAAEARFV PLYQAAETAE AAAAIASGRT ASLGAPLDVV VLGMGTDGHT ASFFPGGTRL EEALDPTTPR GVITMEAEGA GEPRLTFTFS SLQDAGYLVL HIEGSGKKEV LAQAEASGDE AEMPIRAMLR RAASPLQIYW AP // ID 6PGL_SALPA Reviewed; 331 AA. AC Q5PG56; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 06-FEB-2007, entry version 14. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=SPA1967; OS Salmonella paratyphi-a. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=54388; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9150 / SARB42; RX PubMed=15531882; DOI=10.1038/ng1470; RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., RA Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., RA Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., RA Kohlberg S., Strong C., Du F., Carter J., Kremizki C., Layman D., RA Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., RA Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., RA Spieth J., Wilson R.K.; RT "Comparison of genome degradation in Paratyphi A and Typhi, human- RT restricted serovars of Salmonella enterica that cause typhoid."; RL Nat. Genet. 36:1268-1274(2004). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; CP000026; AAV77875.1; -; Genomic_DNA. DR SMR; Q5PG56; 1-331. DR GenomeReviews; CP000026_GR; SPA1967. DR KEGG; spt:SPA1967; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 331 6-phosphogluconolactonase. FT /FTId=PRO_0000171137. SQ SEQUENCE 331 AA; 36351 MW; 84BAF66E97012D13 CRC64; MKQTVYTASP ESQQIHVWSL NHEGTLTLVQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV LAYRIAPDDG ALTFAAESAL PGSPTHISTD HHGRFVFVGS YNAGNVSVTR LQDGLPVELV DVVEGLDGCH SANITPDNRT LWVPALKQER ICLFTLSDDG HLVAQEPAEV NTVEGAGPRH MVFHPNRQYA YCVNELNSSV DVWQLKNPHG EIECVQTLDM MPADFSDTRW AADIHITPDG RHLYACDRTA SLITVFSVSE DGSVLSVEGF QPTEAQPRGF NIDNSGKYLI AAGQKSHHIA VYEITGTQGL LTEKGRYAVG QGPMWVVVNA Y // ID 6PGL_SALTI Reviewed; 331 AA. AC Q8Z8A2; Q7C8Q6; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 06-FEB-2007, entry version 23. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=STY0818, t2102; OS Salmonella typhi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18; RX MEDLINE=21534947; PubMed=11677608; DOI=10.1038/35101607; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., RA Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J., RA Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., RA Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., RA Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., RA Whitehead S., Barrell B.G.; RT "Complete genome sequence of a multiple drug resistant Salmonella RT enterica serovar Typhi CT18."; RL Nature 413:848-852(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700931 / Ty2; RX MEDLINE=22531367; PubMed=12644504; RX DOI=10.1128/JB.185.7.2330-2337.2003; RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., RA Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.; RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 RT and CT18."; RL J. Bacteriol. 185:2330-2337(2003). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; AL627268; CAD05233.1; -; Genomic_DNA. DR EMBL; AE014613; AAO69719.1; -; Genomic_DNA. DR HSSP; P52697; 1RI6. DR SMR; Q8Z8A2; 1-331. DR GenomeReviews; AL513382_GR; STY0818. DR GenomeReviews; AE014613_GR; t2102. DR KEGG; stt:t2102; -. DR KEGG; sty:STY0818; -. DR BioCyc; SENT209261:T2102-MONOMER; -. DR BioCyc; SENT90370:STY0818-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 331 6-phosphogluconolactonase. FT /FTId=PRO_0000171138. SQ SEQUENCE 331 AA; 36436 MW; 3EBB46DF97112DD5 CRC64; MKQTVYTASP ESQQIHVWSL NHEGTLTLVQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV LAYRIAPDDG ALTFAAESAL PGSPTHISTD HHGRFVFVGS YNAGNVSVTR LQDGLPVELV DVVEGLDGCH SANITPDNRT LWVPALKQDR ICLFTLSDDG HLVAQEPAEV NTVEGAGPRH MVFHPNRQYA YCVNELNSSV DVWQLKNPHG EIECVQTLDM MPADFSDTRW AADIHITPDG RHLYACDRTA SLITVFSVSE DGSVLSVEGF QPTEAQPRGF NIDNSRKYLI AAGQKSHHIA VYEITGTQGL LTEKGRYAVG QGPMWVVVNA Y // ID 6PGL_SALTY Reviewed; 331 AA. AC Q8ZQR4; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 06-FEB-2007, entry version 19. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=STM0785; OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=602; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., RA Waterston R., Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium RT LT2."; RL Nature 413:852-856(2001). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; AE008732; AAL19723.1; -; Genomic_DNA. DR HSSP; P52697; 1RI6. DR SMR; Q8ZQR4; 1-331. DR GenomeReviews; AE006468_GR; STM0785. DR KEGG; stm:STM0785; -. DR StyGene; SG?????; pgl. DR BioCyc; STYP99287:STM0785-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 331 6-phosphogluconolactonase. FT /FTId=PRO_0000171139. SQ SEQUENCE 331 AA; 36337 MW; 240B46DF97002DD5 CRC64; MKQTVYTASP ESQQIHVWSL NHEGTLTLVQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV LAYRIAPDDG ALTFAAESAL PGSPTHISTD HHGRFVFVGS YNAGNVSVTR LQDGLPVELV DVVEGLDGCH SANITPDNRT LWVPALKQDR ICLFTLSDDG HLVAQEPAEV NTVEGAGPRH MVFHPNRQYA YCVNELNSSV DVWQLKNPHG EIECVQTLDM MPADFSDTRW AADIHITPDG RHLYACDRTA SLITVFSVSE DGSVLSVEGF QPTEAQPRGF NIDNSGKYLI AAGQKSHHIA VYEITGTQGL LTEKGRYAVG QGPMWVVVNA Y // ID 6PGL_SCHPO Reviewed; 257 AA. AC O74455; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 23-JAN-2007, entry version 31. DE Probable 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN ORFNames=SPCC16C4.10; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AL031535; CAA20749.1; -; Genomic_DNA. DR PIR; T41100; T41100. DR KEGG; spo:SPCC16C4.10; -. DR GeneDB_Spombe; SPCC16C4.10; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-002258-MONOMER; -. DR ArrayExpress; O74455; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 257 Probable 6-phosphogluconolactonase. FT /FTId=PRO_0000090086. SQ SEQUENCE 257 AA; 28351 MW; BCA71AB0BA7086DD CRC64; MSVYSFSDVS LVAKALGAFV KEKSEASIKR HGVFTLALSG GSLPKVLAEG LAQQRGIEFS KWEVFFADER IVPLDDENSN YALCKKLIFD KFEGFDPKKI HTINPELLKE NPIDPQNVAD EYEKQLVHVF ANSSTVKVPV FDLLLLGCGP DGHTCSLFPD HEVLQEDVAW VAPVTDSPKP PKDRITLTLP VVTHAQAIAF VTTGAGKKDI LPIVIEDFTS KLPSALITRN NLTRTSWFVD DEASANLERS SLKVFPQ // ID 6PGL_SHIFL Reviewed; 331 AA. AC Q83LP7; Q7UD46; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 2. DT 06-FEB-2007, entry version 24. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=SF0888, S_0935; OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RX DOI=10.1128/IAI.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; AE005674; AAN42519.2; -; Genomic_DNA. DR EMBL; AE014073; AAP16392.1; -; Genomic_DNA. DR HSSP; P52697; 1RI6. DR SMR; Q83LP7; 1-331. DR GenomeReviews; AE014073_GR; S_0935. DR GenomeReviews; AE005674_GR; SF0888. DR KEGG; sfl:SF0888; -. DR KEGG; sfx:S0935; -. DR BioCyc; SFLE198214:AAN42519.1-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. DR InterPro; IPR003143; Cyt_d1_haem. DR Gene3D; G3DSA:2.140.10.20; Cyt_d1_haem; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 331 6-phosphogluconolactonase. FT /FTId=PRO_0000171140. SQ SEQUENCE 331 AA; 36362 MW; B1C7AF3CF9781A9B CRC64; MKQTVYIASP ESQQIHVWNL NHEGALTLTQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV LAYRIAPDDG ALTFAAESVL PGSPTHISTD HQGQFVFVGS YNAGNVSVTR LEDGLPVGVV DVVEGLDGCH SANISPDNRT LWVPALKQDR ICLFTVSDDG HLVAQDPAEV TTVEGAGPRH MVFHPNEQYA YCVNELNSSV DVWELKDPHG NIECVQTLDM MPENFSDTRW AADIHITPDG RHLYACDRTA SLITVFSVSE DGSVLSKEGF QPTETQPRGF NVDYSGKYLI AAGQKSHHIS VYEIVGEQGL LHEKGRYAVG QGPMWVVVNA H // ID 6PGL_STRCO Reviewed; 261 AA. AC Q9XAB7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 23-JAN-2007, entry version 35. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=SCO1939; ORFNames=SCC22.21; OS Streptomyces coelicolor. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1902; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX MEDLINE=21996410; PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., RA Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces RT coelicolor A3(2)."; RL Nature 417:141-147(2002). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AL939110; CAB50764.1; -; Genomic_DNA. DR PIR; T36011; T36011. DR GenomeReviews; AL645882_GR; SCO1939. DR KEGG; sco:SCO1939; -. DR BioCyc; SCOE1902:SCO1939-MONOMER; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 261 6-phosphogluconolactonase. FT /FTId=PRO_0000090106. SQ SEQUENCE 261 AA; 27211 MW; 7FE7741A0295AF91 CRC64; MSDTPQLVVH RDKELMAEAA AARLITKIVD AQASRGSASV VLTGGRNGNG LLAALAGSPA RDAIDWSRLD LWWGDERFLP EGDPERNVTQ AQQALLDSVP LDPKRVHAMA ASDGPYGSDV EAAAAAYAQE LATASVPENH AAVPSFDVLL LGVGPDTHVA SLFPEHPGVR ETERTVIGVH GSPKPPPIRI SLTLPAIRAA REVWLLAAGE DKANAVAMAL SGAGEIQAPA AGARGRARTL WLLDSAAASQ LPRSLYPPAS A // ID 6PGL_SYNY3 Reviewed; 240 AA. AC P74618; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 31. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=sll1479; OS Synechocystis sp. (strain PCC 6803). OC Bacteria; Cyanobacteria; Chroococcales; Synechocystis. OX NCBI_TaxID=1148; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [2] RP PROTEIN SEQUENCE OF 2-20. RX MEDLINE=97443974; PubMed=9298645; RA Sazuka T., Ohara O.; RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain RT PCC6803: linking 130 protein spots with their respective genes."; RL Electrophoresis 18:1252-1258(1997). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; BA000022; BAA18726.1; ALT_INIT; Genomic_DNA. DR GenomeReviews; BA000022_GR; sll1479. DR KEGG; syn:sll1479; -. DR BioCyc; SSP1148:SLL1479-MONOMER; -. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Direct protein sequencing; Hydrolase. FT INIT_MET 1 1 Removed. FT CHAIN 2 240 6-phosphogluconolactonase. FT /FTId=PRO_0000090107. SQ SEQUENCE 240 AA; 26482 MW; F8F6E9B3F4E934B6 CRC64; MAPQVDVLIN KQILIERALV CVTTRITKAI AERGQGTIAL SGGNTPKPLY EALARQALPW EKIHVFWGDE RYVSVDHPDS NQRMARLAWL DQVDIPEANI HPMPTAAADP EQDAQTYENE LATFFQVEAG HFPAFDLILL GLGDDGHTAS LFPHTPALTV GDRLITVGNK DGQPRLTFTI PLINRARSVV FLVAGASKQH ALGEIFAPEA DPQQYPARFI QPQGELIWLL DQQAGENLRP // ID 6PGL_THEMA Reviewed; 220 AA. AC Q9X0N8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 20-FEB-2007, entry version 39. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=TM_1154; OS Thermotoga maritima. OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=2336; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX MEDLINE=99287316; PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE000512; AAD36230.1; -; Genomic_DNA. DR PIR; F72289; F72289. DR PDB; 1PBT; X-ray; A=1-220. DR PDB; 1VL1; X-ray; A=1-220. DR GenomeReviews; AE000512_GR; TM1154. DR KEGG; tma:TM1154; -. DR TIGR; TM_1154; -. DR BioCyc; TMAR2336:TM1154-MONOMER; -. DR InterPro; IPR006148; Gluc_gal_isom. DR InterPro; IPR005900; Phosphogluconlac. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. KW 3D-structure; Complete proteome; Hydrolase. FT CHAIN 1 220 6-phosphogluconolactonase. FT /FTId=PRO_0000090108. FT STRAND 3 11 FT HELIX 13 31 FT STRAND 35 39 FT TURN 43 44 FT HELIX 45 52 FT TURN 53 54 FT HELIX 59 61 FT STRAND 62 72 FT TURN 74 75 FT TURN 77 78 FT HELIX 80 87 FT TURN 88 91 FT HELIX 96 98 FT TURN 104 105 FT HELIX 108 122 FT STRAND 127 131 FT TURN 135 136 FT TURN 140 141 FT HELIX 145 148 FT TURN 149 149 FT STRAND 151 156 FT STRAND 158 160 FT TURN 161 164 FT STRAND 167 170 FT HELIX 172 175 FT TURN 176 177 FT STRAND 179 187 FT HELIX 188 198 FT TURN 199 200 FT HELIX 204 207 FT STRAND 211 219 SQ SEQUENCE 220 AA; 25325 MW; 9B0FD07EE01E60C3 CRC64; MEKTVIYLLE DGYVDFVVEK IRTKMEKLLE EKDKIFVVLA GGRTPLPVYE KLAEQKFPWN RIHFFLSDER YVPLDSDQSN FRNINEVLFS RAKIPSGNVH YVDTSLPIEK ACEKYEREIR SATDQFDLAI LGMGPDGHVA SIFDLETGNK DNLVTFTDPS GDPKVPRVTL TFRALNTSLY VLFLIRGKEK INRLTEILKD TPLPAYFVRG KEKTVWFVGK // ID 6PGL_TREPA Reviewed; 241 AA. AC O83490; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 20-FEB-2007, entry version 35. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; Synonyms=devB; OrderedLocusNames=TP_0477; OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nichols; RX MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., RA Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., RA Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., RA Weidman J.F., Smith H.O., Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE000520; AAC65464.1; -; Genomic_DNA. DR PIR; C71319; C71319. DR GenomeReviews; AE000520_GR; TP0477. DR KEGG; tpa:TP0477; -. DR TIGR; TP_0477; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 241 6-phosphogluconolactonase. FT /FTId=PRO_0000090109. SQ SEQUENCE 241 AA; 27272 MW; 148FBDA12324FEF9 CRC64; MKKHIFEDAR AIAAFLVSVF DSRLKTQEIL WLALSGGSTP REIFRTWAHE FRHHLDWKRL RFFWSDERCV PPTDAQSNFN MTHSALLEPL EINPDAVFRV RGEDAPESAC AAYSQEIEAR LPRQRGVPCF DIILLGMGAD GHTASIFPHE IELWDHSGCC VVATHPDTGQ KRVSFTGHLI NNAHEIYVVV TGREKQDMLA SVASDPHASV PLHAWTLPKR SGCWIPLLRG LYPRKQCKPT V // ID 6PGL_XENNE Reviewed; 275 AA. AC Q9RMP7; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 06-FEB-2007, entry version 20. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase) DE (Fragment). GN Name=pgl; OS Xenorhabdus nematophilus (Achromobacter nematophilus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Xenorhabdus. OX NCBI_TaxID=628; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 19061 / AN6 / DSM 3370 / LMG 1036 / NCIB 9965; RX MEDLINE=20208870; PubMed=10742251; RX DOI=10.1128/AEM.66.4.1622-1628.2000; RA Volgyi A., Fodor A., Forst S.; RT "Inactivation of a novel gene produces a phenotypic variant cell and RT affects the symbiotic behavior of Xenorhabdus nematophilus."; RL Appl. Environ. Microbiol. 66:1622-1628(2000). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; AF191556; AAF04393.1; -; Genomic_DNA. DR HSSP; P52697; 1RI6. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. DR InterPro; IPR011045; N2O_reductase_N. KW Carbohydrate metabolism; Glucose metabolism; Hydrolase. FT CHAIN <1 275 6-phosphogluconolactonase. FT /FTId=PRO_0000171141. FT NON_TER 1 1 SQ SEQUENCE 275 AA; 30624 MW; AD57759CD652AA1B CRC64; IRPQFSIVTY AIGKNGSLEQ KSIAPLPGSP THISTDRAGR FLFSASYSFN NLSVHPIDDQ GNVKAPIQIV ENLQAPHSAN IDRENRQLLV PCLKEDHIRI FNMDNQGYLV ESHADAITTE TGAGPRHMAF HPKKQAIYCI NELDSTVDVL RKWEKYRIVQ SVDSLPADFS SVRCSADIHM TPDGRHLYTS ERSESLISHF RVSEGGYHLT LTGHYLTETN PVALPLIHSG HFLIASGQKS DHISVSRIDK FSGELTQLAR YPVGKSPMWV TILAL // ID 6PGL_XYLFA Reviewed; 239 AA. AC Q9PEG5; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 23-JAN-2007, entry version 26. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; OrderedLocusNames=Xf1063; OS Xylella fastidiosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=2371; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c; RX MEDLINE=20365717; PubMed=10910347; DOI=10.1038/35018003; RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., RA Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., RA Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., RA Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., RA Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., RA Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., RA Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., RA Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., RA Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., RA Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., RA Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., RA Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., RA Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., RA de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., RA da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., RA da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., RA de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., RA Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., RA Zago M.A., Zatz M., Meidanis J., Setubal J.C.; RT "The genome sequence of the plant pathogen Xylella fastidiosa."; RL Nature 406:151-159(2000). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE003849; AAF83873.1; -; Genomic_DNA. DR PIR; D82727; D82727. DR GenomeReviews; AE003849_GR; Xf1063. DR KEGG; xfa:XF1063; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 239 6-phosphogluconolactonase. FT /FTId=PRO_0000090110. SQ SEQUENCE 239 AA; 26281 MW; 2A975549EABC8BCE CRC64; MTPPNDARIT LMNYDDPLEW AQSVTRELEN ILLQEITQRG RASLLLSGGT TPARVYETLA TRPLDWSKID IGLVDERWLS PQDKDSNAWL VRHTLLEHAK HATFLPLIRP GKTLNQCVHD ANLQITHSPP PCAAVLGMGN DGHTASLFPG SLDLPKAIST LQPYVALDAT GCPGAGVWPL RITLTPAGLS NIPHRLLLLC GKQKMQVLET ALSCKDALDY PIRTAIDLPN ARLRVHWCA // ID 6PGL_XYLFT Reviewed; 239 AA. AC Q87EG7; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 1. DT 23-JAN-2007, entry version 19. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6PGL). GN Name=pgl; OrderedLocusNames=PD_0344; OS Xylella fastidiosa (strain Temecula1 / ATCC 700964). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=183190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22421331; PubMed=12533478; RX DOI=10.1128/JB.185.3.1018-1026.2003; RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., RA Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., RA Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., RA Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., RA Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., RA Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., RA Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., RA Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., RA da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., RA Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., RA de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., RA Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., RA Kitajima J.P.; RT "Comparative analyses of the complete genome sequences of Pierce's RT disease and citrus variegated chlorosis strains of Xylella RT fastidiosa."; RL J. Bacteriol. 185:1018-1026(2003). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase 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; AE009442; AAO28224.1; -; Genomic_DNA. DR GenomeReviews; AE009442_GR; PD_0344. DR KEGG; xft:PD0344; -. DR BioCyc; XFAS183190:PD0344-MONOMER; -. DR InterPro; IPR005900; Phosphogluconlac. DR TIGRFAMs; TIGR01198; pgl; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 239 6-phosphogluconolactonase. FT /FTId=PRO_0000090111. SQ SEQUENCE 239 AA; 26367 MW; AE3E8F72B4F1A91E CRC64; MIPTNDAHIT LMNYDDPLEW AQSVTRELEN ILLQEITQRG RASLLLSGGT TPALVYETLA TRPLDWSKID IGLVDERWLS PQDKDSNAWL VRHTLLEHAK HATFLPLIRP GKTLNQCVHD ANLQITHSPP PCAVVLGMGN DGHTASLFPG SLDLQKAINT PQPYVALDAT GCPGAGVWPL RITLTPAGLN NIPHRLLLLR GKQKLKVLET ALSCKDALDY PIRTAIDLPN ARLRVHWCA // ID 6PGL_YERPE Reviewed; 334 AA. AC Q8ZGX4; Q74W78; Q7CH64; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 06-FEB-2007, entry version 25. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=YPO1149, y3033, YP1011; OS Yersinia pestis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-92 / Biovar Orientalis; RX MEDLINE=21470413; PubMed=11586360; DOI=10.1038/35097083; RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., RA Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., RA Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., RA Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.; RT "Genome sequence of Yersinia pestis, the causative agent of plague."; RL Nature 413:523-527(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIM5 / Biovar Mediaevalis; RX MEDLINE=22137863; PubMed=12142430; RX DOI=10.1128/JB.184.16.4601-4611.2002; RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., RA Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., RA Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R., RA Perry R.D.; RT "Genome sequence of Yersinia pestis KIM."; RL J. Bacteriol. 184:4601-4611(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=91001 / Biovar Mediaevalis; RX PubMed=15368893; DOI=10.1093/dnares/11.3.179; RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., RA Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., RA Yang H., Wang J., Huang P., Yang R.; RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate RT avirulent to humans."; RL DNA Res. 11:179-197(2004). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; AJ414146; CAC89990.1; -; Genomic_DNA. DR EMBL; AE009952; AAM86584.1; -; Genomic_DNA. DR EMBL; AE017130; AAS61262.1; -; Genomic_DNA. DR PIR; AC0141; AC0141. DR HSSP; P52697; 1RI6. DR GenomeReviews; AE009952_GR; y3033. DR GenomeReviews; AE017042_GR; YP1011. DR KEGG; ype:YPO1149; -. DR KEGG; ypk:y3033; -. DR KEGG; ypm:YP_1011; -. DR BioCyc; YPES187410:Y3033-MONOMER; -. DR BioCyc; YPES229193:YP1011-MONOMER; -. DR BioCyc; YPES632:YPO1149-MONOMER; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 334 6-phosphogluconolactonase. FT /FTId=PRO_0000171142. SQ SEQUENCE 334 AA; 36446 MW; 4BDAC511EF8E0F06 CRC64; MKQAVYVASP DSQQIHVWQL DSAGELTLLQ TVDVPGQVQP MAISPNQRHL YVGVRPDFGI VSYHIADDGT LTAAGMAPLP GSPTHIDTDR QGRFLFSASY SFNCVSISPI DTHGVVQAPI QQLDDLPAPH SANIDPTNQI LLVPCLKEDK VRLFDLSAEG QLTPHAQADI TVAAGAGPRH MAFHPNHQVA YCVNELNSSV DVYQISNNGQ EYHLVQSLDA MPADFTGTRW AADIHITPNG RYLYISDRTA NLLGIFTVSE DGRVISLVGH HLTEAQPRGF NIDHSGNFLI ASGQKSDHIE VYRIDQNTGE LTTLKRYPVG KGPMWVSIRG AQNS // ID 6PGL_YERPS Reviewed; 334 AA. AC Q66D69; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 06-FEB-2007, entry version 16. DE 6-phosphogluconolactonase (EC 3.1.1.31) (6-P-gluconolactonase). GN Name=pgl; OrderedLocusNames=YPTB1180; OS Yersinia pseudotuberculosis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=633; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP32953 / Serotype I; RX PubMed=15358858; DOI=10.1073/pnas.0404012101; RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M., RA Derbise A., Hauser L.J., Garcia E.; RT "Insights into the evolution of Yersinia pestis through whole-genome RT comparison with Yersinia pseudotuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to CC 6-phosphogluconate (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2. CC -!- SIMILARITY: Belongs to the cycloisomerase 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; BX936398; CAH20420.1; -; Genomic_DNA. DR GenomeReviews; BX936398_GR; YPTB1180. DR KEGG; yps:YPTB1180; -. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:HAMAP. DR HAMAP; MF_01605; -; 1. DR InterPro; IPR011045; N2O_reductase_N. DR InterPro; IPR011044; Quino_amine_DH_b. KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Hydrolase. FT CHAIN 1 334 6-phosphogluconolactonase. FT /FTId=PRO_0000171143. SQ SEQUENCE 334 AA; 36445 MW; 4BDAC8AA5983B4B0 CRC64; MKQAVYVASP DSQQIHVWQL DSAGELTLLQ TVDVPGQVQP MAISPNQRHL YVGVRPDFGI VSYHIADDGT LTAAGMAPLP GSPTHIDTDR QGRFLFSASY SFNCVSISPI DTHGVVQAPI QQLDDLPAPH SANIDPTNQI LLVPCLKEDK VRLFDLSAEG QLTPHAQADI TVAAGAGPRH MAFHPNHQVA YCVNELNSSV DVYQISNNGQ EYHLVQSLDA MPADFTGTRW AADIHITPNG RYLYISDRTA NLLGIFTVSK DGRVISLVGH HLTEAQPRGF NIDHSGNFLI ASGQKSDHIE VYRIDQNTGE LTTLKRYPVG KGPMWVSIRG AQNS // ID 7B2_HUMAN Reviewed; 212 AA. AC P05408; P01164; Q9BS38; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 2. DT 20-FEB-2007, entry version 70. DE Neuroendocrine protein 7B2 precursor (Secretogranin-5) (Secretogranin DE V) (Secretory granule endocrine protein I) (Pituitary polypeptide) DE [Contains: N-terminal peptide; C-terminal peptide]. GN Name=SCG5; Synonyms=SGNE1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Pituitary; RX MEDLINE=88271601; PubMed=3134253; DOI=10.1016/0014-5793(88)81324-3; RA Martens G.J.M.; RT "Cloning and sequence analysis of human pituitary cDNA encoding the RT novel polypeptide 7B2."; RL FEBS Lett. 234:160-164(1988). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), AND PROTEIN SEQUENCE OF RP 125-140 (ISOFORM 1) AND 126-132 (ISOFORM 2). RC TISSUE=Pituitary; RX MEDLINE=91113188; PubMed=1989596; RA Paquet L., Lazure C., Seidah N.G., Chretien M., Mbikay M.; RT "The production by alternate splicing of two mRNAs differing by one RT codon could be an intrinsic property of neuroendocrine protein 7B2 RT gene expression in man."; RL Biochem. Biophys. Res. Commun. 174:156-162(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Jackson R.S.; RT "Human neuroendocrine protein 7B2 genomic organization."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 61-92. RX MEDLINE=96184880; PubMed=8617287; RA Braks J.A., Broers C.A., Danger J.M., Martens G.J.; RT "Structural organization of the gene encoding the neuroendocrine RT chaperone 7B2."; RL Eur. J. Biochem. 236:60-67(1996). RN [6] RP PROTEIN SEQUENCE OF 27-103. RX MEDLINE=84022554; PubMed=6625600; RA Seidah N.G., Hsi K.L., de Serres G., Rochemont J., Hamelin J., RA Antakly T., Cantin M., Chretien M.; RT "Isolation and NH2-terminal sequence of a highly conserved human and RT porcine pituitary protein belonging to a new superfamily. RT Immunocytochemical localization in pars distalis and pars nervosa of RT the pituitary and in the supraoptic nucleus of the hypothalamus."; RL Arch. Biochem. Biophys. 225:525-534(1983). RN [7] RP FUNCTION, AND INTERACTION WITH PCSK2. RX MEDLINE=94320138; PubMed=7913882; DOI=10.1016/0092-8674(94)90296-8; RA Braks J.A., Martens G.J.; RT "7B2 is a neuroendocrine chaperone that transiently interacts with RT prohormone convertase PC2 in the secretory pathway."; RL Cell 78:263-273(1994). RN [8] RP REVIEW. RX MEDLINE=21332545; PubMed=11439082; DOI=10.1042/0264-6021:3570329; RA Mbikay M., Seidah N.G., Chretien M.; RT "Neuroendocrine secretory protein 7B2: structure, expression and RT functions."; RL Biochem. J. 357:329-342(2001). CC -!- FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing CC its premature activation in the regulated secretory pathway. Binds CC to inactive PCSK2 in the endoplasmic reticulum and facilitates its CC transport from there to later compartments of the secretory CC pathway where it is proteolytically matured and activated. Also CC required for cleavage of PCSK2 but does not appear to be involved CC in its folding. Plays a role in regulating pituitary hormone CC secretion. The C-terminal peptide inhibits PCSK2 in vitro. CC -!- SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway. CC Dissociation occurs at later stages. CC -!- SUBCELLULAR LOCATION: Note=Neuroendocrine and endocrine secretory CC granules. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P05408-1; Sequence=Displayed; CC Name=2; CC IsoId=P05408-2; Sequence=VSP_011754; CC -!- PTM: Proteolytically cleaved in the Golgi by a furin-like CC convertase to generate bioactive peptides (By similarity). CC -!- PTM: Sulfated on tyrosine residues (By similarity). CC -!- SIMILARITY: Belongs to the 7B2 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y00757; CAA68726.1; -; mRNA. DR EMBL; AJ290438; CAB90397.1; -; Genomic_DNA. DR EMBL; AJ290439; CAB90397.1; JOINED; Genomic_DNA. DR EMBL; AJ290440; CAB90397.1; JOINED; Genomic_DNA. DR EMBL; AJ290441; CAB90397.1; JOINED; Genomic_DNA. DR EMBL; AJ290442; CAB90397.1; JOINED; Genomic_DNA. DR EMBL; BC005349; AAH05349.1; -; mRNA. DR PIR; S01008; PUHU. DR UniGene; Hs.156540; -. DR MEROPS; I21.001; -. DR Ensembl; ENSG00000166922; Homo sapiens. DR KEGG; hsa:6447; -. DR H-InvDB; HIX0012074; -. DR HGNC; HGNC:10816; SCG5. DR MIM; 173120; gene. DR ArrayExpress; P05408; -. DR GermOnline; ENSG00000166922; Homo sapiens. DR RZPD-ProtExp; G0168; -. DR RZPD-ProtExp; IOH7305; -. DR RZPD-ProtExp; RZPDo834B0432; -. DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB. DR GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; TAS:ProtInc. DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB. DR GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB. DR GO; GO:0046883; P:regulation of hormone secretion; ISS:UniProtKB. DR InterPro; IPR007945; Secretogranin_V. DR Pfam; PF05281; Secretogranin_V; 1. KW Alternative splicing; Chaperone; Cleavage on pair of basic residues; KW Direct protein sequencing; Neuropeptide; Phosphorylation; Signal; KW Sulfation; Transport. FT SIGNAL 1 26 FT CHAIN 27 212 Neuroendocrine protein 7B2. FT /FTId=PRO_0000000041. FT CHAIN 27 176 N-terminal peptide (By similarity). FT /FTId=PRO_0000000042. FT PEPTIDE 200 212 C-terminal peptide (By similarity). FT /FTId=PRO_0000000043. FT MOD_RES 205 205 Phosphoserine (By similarity). FT DISULFID 120 130 By similarity. FT VAR_SEQ 126 126 Missing (in isoform 2). FT /FTId=VSP_011754. FT CONFLICT 151 151 F -> S (in Ref. 4). SQ SEQUENCE 212 AA; 23730 MW; A459702055C0FE84 CRC64; MVSRMVSTML SGLLFWLASG WTPAFAYSPR TPDRVSEADI QRLLHGVMEQ LGIARPRVEY PAHQAMNLVG PQSIEGGAHE GLQHLGPFGN IPNIVAELTG DNIPKDFSED QGYPDPPNPC PVGKTADDGC LENTPDTAEF SREFQLHQHL FDPEHDYPGL GKWNKKLLYE KMKGGERRKR RSVNPYLQGQ RLDNVVAKKS VPHFSDEDKD PE // ID 7B2_MOUSE Reviewed; 212 AA. AC P12961; Q8CCZ3; Q9CYP0; Q9D2P6; Q9DB14; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 20-FEB-2007, entry version 65. DE Neuroendocrine protein 7B2 precursor (Secretogranin-5) (Secretogranin DE V) (Secretory granule endocrine protein I) [Contains: N-terminal DE peptide; C-terminal peptide]. GN Name=Scg5; Synonyms=Sgne-1, Sgne1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=BALB/c; TISSUE=Pancreas; RX MEDLINE=89254271; PubMed=2542174; RA Mbikay M., Grant S.G.N., Sirois F., Tadros H., Skowronski J., RA Lazure C., Seidah N.G., Hanahan D., Chretien M.; RT "cDNA sequence of neuroendocrine protein 7B2 expressed in beta cell RT tumors of transgenic mice."; RL Int. J. Pept. Protein Res. 33:39-45(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Cerebellum, Embryo, Hippocampus, 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 [3] 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 [4] RP FUNCTION, AND NULL MUTANT. RX MEDLINE=98012196; PubMed=9348280; DOI=10.1083/jcb.139.3.625; RA Muller L., Zhu X., Lindberg I.; RT "Mechanism of the facilitation of PC2 maturation by 7B2: involvement RT in ProPC2 transport and activation but not folding."; RL J. Cell Biol. 139:625-638(1997). RN [5] RP FUNCTION. RX MEDLINE=99189754; PubMed=10089884; DOI=10.1016/S0092-8674(00)80579-6; RA Westphal C.H., Muller L., Zhou A., Zhu X., Bonner-Weir S., RA Schambelan M., Steiner D.F., Lindberg I., Leder P.; RT "The neuroendocrine protein 7B2 is required for peptide hormone RT processing in vivo and provides a novel mechanism for pituitary RT Cushing's disease."; RL Cell 96:689-700(1999). RN [6] RP INHIBITION OF PCSK2 BY C-TERMINAL PEPTIDE. RX MEDLINE=94286522; PubMed=8016065; RA Martens G.J., Braks J.A., Eib D.W., Zhou Y., Lindberg I.; RT "The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of RT prohormone convertase PC2."; RL Proc. Natl. Acad. Sci. U.S.A. 91:5784-5787(1994). RN [7] RP SULFATION, CLEAVAGE BY FURIN-LIKE CONVERTASE, AND MUTAGENESIS OF RP ARG-177 AND ARG-178. RX MEDLINE=94308204; PubMed=8034690; RA Paquet L., Bergeron F., Boudreault A., Seidah N.G., Chretien M., RA Mbikay M., Lazure C.; RT "The neuroendocrine precursor 7B2 is a sulfated protein RT proteolytically processed by a ubiquitous furin-like convertase."; RL J. Biol. Chem. 269:19279-19285(1994). RN [8] RP REVIEW. RX MEDLINE=21332545; PubMed=11439082; DOI=10.1042/0264-6021:3570329; RA Mbikay M., Seidah N.G., Chretien M.; RT "Neuroendocrine secretory protein 7B2: structure, expression and RT functions."; RL Biochem. J. 357:329-342(2001). CC -!- FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing CC its premature activation in the regulated secretory pathway. Binds CC to inactive PCSK2 in the endoplasmic reticulum and facilitates its CC transport from there to later compartments of the secretory CC pathway where it is proteolytically matured and activated. Also CC required for cleavage of PCSK2 but does not appear to be involved CC in its folding. Plays a role in regulating pituitary hormone CC secretion. The C-terminal peptide inhibits PCSK2 in vitro. CC -!- SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway. CC Dissociation occurs at later stages (By similarity). CC -!- SUBCELLULAR LOCATION: Note=Neuroendocrine and endocrine secretory CC granules. CC -!- PTM: Proteolytically cleaved in the Golgi by a furin-like CC convertase to generate bioactive peptides. CC -!- PTM: Sulfated on tyrosine residues. CC -!- MISCELLANEOUS: Mice lacking Scg5 have no demonstrable Pcsk2/Pc2 CC activity, are deficient in processing islet hormones, and display CC hypoglycemia, hyperproinsulinemia and hypoglucagonemia, similar to CC Pcsk2 null mice. In contrast to Pcsk2 null mice, they develop CC Cushing's disease due to excessive secretion of corticotropin from CC the pituitary and die before 9 weeks, indicating a role for Sgne1 CC in control of peptide secretion from the pituitary. CC -!- SIMILARITY: Belongs to the 7B2 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X15830; CAA33835.1; -; mRNA. DR EMBL; AK005331; BAB23956.1; -; mRNA. DR EMBL; AK011938; BAB27927.1; -; mRNA. DR EMBL; AK017481; BAB30765.1; -; mRNA. DR EMBL; AK019337; BAB31669.1; -; mRNA. DR EMBL; AK031856; BAC27581.1; -; mRNA. DR EMBL; BC029021; AAH29021.1; -; mRNA. DR PIR; S12477; S12477. DR UniGene; Mm.4836; -. DR MEROPS; I21.001; -. DR Ensembl; ENSMUSG00000023236; Mus musculus. DR KEGG; mmu:20394; -. DR MGI; MGI:98289; Scg5. DR ArrayExpress; P12961; -. DR GermOnline; ENSMUSG00000023236; Mus musculus. DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB. DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB. DR GO; GO:0016486; P:peptide hormone processing; IDA:UniProtKB. DR GO; GO:0046883; P:regulation of hormone secretion; IDA:UniProtKB. DR InterPro; IPR007945; Secretogranin_V. DR PANTHER; PTHR12738; Secretogranin_V; 1. DR Pfam; PF05281; Secretogranin_V; 1. KW Chaperone; Cleavage on pair of basic residues; KW Direct protein sequencing; Neuropeptide; Phosphorylation; Signal; KW Sulfation; Transport. FT SIGNAL 1 26 FT CHAIN 27 212 Neuroendocrine protein 7B2. FT /FTId=PRO_0000000044. FT CHAIN 27 176 N-terminal peptide (By similarity). FT /FTId=PRO_0000000045. FT PEPTIDE 200 212 C-terminal peptide (By similarity). FT /FTId=PRO_0000000046. FT MOD_RES 205 205 Phosphoserine (By similarity). FT DISULFID 120 130 By similarity. FT MUTAGEN 177 177 R->A: No effect on proteolytic FT processing. Abolishes proteolytic FT processing; when associated with G-178. FT MUTAGEN 178 178 R->G: Abolishes proteolytic processing; FT when associated with A-177. FT CONFLICT 6 6 V -> G (in Ref. 2; BAB23956). FT CONFLICT 119 119 P -> H (in Ref. 2; BAB30765). FT CONFLICT 145 145 Q -> R (in Ref. 2; BAB31669). FT CONFLICT 153 153 P -> T (in Ref. 2; BAC27581). SQ SEQUENCE 212 AA; 23866 MW; 6D8CD046532F9609 CRC64; MASRLVSAML SGLLFWLMFE WNPAFAYSPR TPDRVSETDI QRLLHGVMEQ LGIARPRVEY PAHQAMNLVG PQSIEGGAHE GLQHLGPFGN IPNIVAELTG DNIPKDFSED QGYPDPPNPC PLGKTADDGC LENAPDTAEF SREFQLDQHL FDPEHDYPGL GKWNKKLLYE KMKGGQRRKR RSVNPYLQGK RLDNVVAKKS VPHFSEEEKE AE // ID 7B2_PIG Reviewed; 207 AA. AC P01165; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 2. DT 20-FEB-2007, entry version 48. DE Neuroendocrine protein 7B2 precursor (Secretogranin-5) (Secretogranin DE V) (Secretory granule endocrine protein I) [Contains: N-terminal DE peptide; C-terminal peptide]. GN Name=SCG5; Synonyms=SGNE1; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89170118; PubMed=3234177; RA Brayton K.A., Aimi J., Qiu H., Yazdanparast R., Ghatei M.A., RA Polak J.M., Bloom S.R., Dixon J.E.; RT "Cloning, characterization, and sequence of a porcine cDNA encoding a RT secreted neuronal and endocrine protein."; RL DNA 7:713-719(1988). RN [2] RP PROTEIN SEQUENCE OF 23-171. RC TISSUE=Pituitary; RX PubMed=1797712; RA Lazure C., Benjannet S., Seidah N.G., Chretien M.; RT "Processed forms of neuroendocrine proteins 7B2 and secretogranin II RT are found in porcine pituitary extracts."; RL Int. J. Pept. Protein Res. 38:392-400(1991). RN [3] RP PROTEIN SEQUENCE OF 23-103. RX MEDLINE=84022554; PubMed=6625600; RA Seidah N.G., Hsi K.L., de Serres G., Rochemont J., Hamelin J., RA Antakly T., Cantin M., Chretien M.; RT "Isolation and NH2-terminal sequence of a highly conserved human and RT porcine pituitary protein belonging to a new superfamily. RT Immunocytochemical localization in pars distalis and pars nervosa of RT the pituitary and in the supraoptic nucleus of the hypothalamus."; RL Arch. Biochem. Biophys. 225:525-534(1983). RN [4] RP PROTEIN SEQUENCE OF 23-72. RX MEDLINE=83079722; PubMed=6816630; DOI=10.1016/0014-5793(82)81055-7; RA Hsi K.L., Seidah N.G., de Serres G., Chretien M.; RT "Isolation and NH2-terminal sequence of a novel porcine anterior RT pituitary polypeptide. Homology to proinsulin, secretin and Rous RT sarcoma virus transforming protein TVFV60."; RL FEBS Lett. 147:261-266(1982). RN [5] RP SUBCELLULAR LOCATION. RX MEDLINE=85086609; PubMed=6514132; RA Iguchi H., Chan J.S., Seidah N.G., Chretien M.; RT "Tissue distribution and molecular forms of a novel pituitary protein RT in the rat."; RL Neuroendocrinology 39:453-458(1984). RN [6] RP REVIEW. RX MEDLINE=21332545; PubMed=11439082; DOI=10.1042/0264-6021:3570329; RA Mbikay M., Seidah N.G., Chretien M.; RT "Neuroendocrine secretory protein 7B2: structure, expression and RT functions."; RL Biochem. J. 357:329-342(2001). CC -!- FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing CC its premature activation in the regulated secretory pathway. Binds CC to inactive PCSK2 in the endoplasmic reticulum and facilitates its CC transport from there to later compartments of the secretory CC pathway where it is proteolytically matured and activated. Also CC required for cleavage of PCSK2 but does not appear to be involved CC in its folding. Plays a role in regulating pituitary hormone CC secretion. The C-terminal peptide inhibits PCSK2 in vitro. CC -!- SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway. CC Dissociation occurs at later stages (By similarity). CC -!- SUBCELLULAR LOCATION: Note=Neuroendocrine and endocrine secretory CC granules. CC -!- PTM: Proteolytically cleaved in the Golgi by a furin-like CC convertase to generate bioactive peptides (By similarity). CC -!- PTM: Sulfated on tyrosine residues (By similarity). CC -!- SIMILARITY: Belongs to the 7B2 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M23654; AAA50416.1; -; mRNA. DR PIR; A31600; PUPG. DR UniGene; Ssc.155; -. DR MEROPS; I21.001; -. DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB. DR GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB. DR GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB. DR GO; GO:0046883; P:regulation of hormone secretion; ISS:UniProtKB. DR InterPro; IPR007945; Secretogranin_V. DR Pfam; PF05281; Secretogranin_V; 1. KW Chaperone; Cleavage on pair of basic residues; KW Direct protein sequencing; Neuropeptide; Phosphorylation; Signal; KW Sulfation; Transport. FT SIGNAL 1 22 FT CHAIN 23 207 Neuroendocrine protein 7B2. FT /FTId=PRO_0000000047. FT CHAIN 23 171 N-terminal peptide. FT /FTId=PRO_0000000048. FT PEPTIDE 195 207 C-terminal peptide. FT /FTId=PRO_0000000049. FT MOD_RES 200 200 Phosphoserine (By similarity). FT DISULFID 116 125 By similarity. SQ SEQUENCE 207 AA; 23224 MW; 20077D0E1EB6D0AC CRC64; MVSTMLSGLV LWLTFGWTPA LAYSPRTPDR VSETDIQRLL HGVMEQLGIA RPRVEYPAHQ AMNLVGPQSI EGGAHEGLQH LGPFGNIPNI VAELTGDNTP KDFSEDQGYP DPPNPCPIGK TDDGCLENTP DTAEFSREFQ LHQHLFDPEH DYPGLGKWNK KLLYEKMKGG QRRKRRSVNP YLQGQRLDNV VAKKSVPHFS DEDKDPE // ID 7B2_RAT Reviewed; 210 AA. AC P27682; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 23-JAN-2007, entry version 47. DE Neuroendocrine protein 7B2 precursor (Secretogranin-5) (Secretogranin DE V) (Secretory granule endocrine protein I) [Contains: N-terminal DE peptide; C-terminal peptide]. GN Name=Scg5; Synonyms=Sgne1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91243670; PubMed=1709861; RA Waldbieser G.C., Aimi J., Dixon J.E.; RT "Cloning and characterization of the rat complementary RT deoxyribonucleic acid and gene encoding the neuroendocrine peptide RT 7B2."; RL Endocrinology 128:3228-3236(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary anterior lobe; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 REVIEW. RX MEDLINE=21332545; PubMed=11439082; DOI=10.1042/0264-6021:3570329; RA Mbikay M., Seidah N.G., Chretien M.; RT "Neuroendocrine secretory protein 7B2: structure, expression and RT functions."; RL Biochem. J. 357:329-342(2001). CC -!- FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing CC its premature activation in the regulated secretory pathway. Binds CC to inactive PCSK2 in the endoplasmic reticulum and facilitates its CC transport from there to later compartments of the secretory CC pathway where it is proteolytically matured and activated. Also CC required for cleavage of PCSK2 but does not appear to be involved CC in its folding. Plays a role in regulating pituitary hormone CC secretion. The C-terminal peptide inhibits PCSK2 in vitro. CC -!- SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway. CC Dissociation occurs at later stages (By similarity). CC -!- INTERACTION: CC P28841:Pcsk2; NbExp=2; IntAct=EBI-988232, EBI-988244; CC -!- SUBCELLULAR LOCATION: Note=Neuroendocrine and endocrine secretory CC granules. CC -!- PTM: Proteolytically cleaved in the Golgi by a furin-like CC convertase to generate bioactive peptides (By similarity). CC -!- PTM: Sulfated on tyrosine residues (By similarity). CC -!- SIMILARITY: Belongs to the 7B2 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M63901; AAA40626.1; -; mRNA. DR EMBL; BC061560; AAH61560.1; -; mRNA. DR PIR; A49745; A49745. DR UniGene; Rn.6173; -. DR IntAct; P27682; -. DR MEROPS; I21.001; -. DR Ensembl; ENSRNOG00000007542; Rattus norvegicus. DR KEGG; rno:25719; -. DR RGD; 3669; Sgne1. DR ArrayExpress; P27682; -. DR GermOnline; ENSRNOG00000007542; Rattus norvegicus. DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB. DR GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB. DR GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB. DR GO; GO:0046883; P:regulation of hormone secretion; ISS:UniProtKB. DR InterPro; IPR007945; Secretogranin_V. DR PANTHER; PTHR12738; Secretogranin_V; 1. DR Pfam; PF05281; Secretogranin_V; 1. KW Chaperone; Cleavage on pair of basic residues; Neuropeptide; KW Phosphorylation; Signal; Sulfation; Transport. FT SIGNAL 1 24 By similarity. FT CHAIN 25 210 Neuroendocrine protein 7B2. FT /FTId=PRO_0000000050. FT CHAIN 25 176 N-terminal peptide (By similarity). FT /FTId=PRO_0000000051. FT PEPTIDE 198 210 C-terminal peptide (By similarity). FT /FTId=PRO_0000000052. FT MOD_RES 203 203 Phosphoserine (By similarity). FT DISULFID 118 128 By similarity. SQ SEQUENCE 210 AA; 23684 MW; 14FBA7D070E79992 CRC64; MTSRMAILSG LLFWLLLEWN PAFAYSPRTP DRVSETDIQR LLHGVMEQLG IARPRVEYPA HQAMNLVGPQ SIEGGAHEGL QHLGPFGNIP NIVAELTGDN IPKDFSEDQG YPDPPNPCPL GKTADDGCLE NAPDTAEFSR EFQLDQHLFD PEHDYPGLGK WNKKLLYEKM KGGQRRKRRS VNPYLQGKRL DNVVAKKSVP HFSEEEKEPE // ID 7B2_XENLA Reviewed; 161 AA. AC P18844; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 20-FEB-2007, entry version 40. DE Neuroendocrine protein 7B2 (Secretogranin V) [Contains: N-terminal DE peptide; C-terminal peptide] (Fragment). GN Name=sgne1; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89231705; PubMed=2714283; RA Martens G.J.M., Bussemakers M.J.G., Ayoubi T.A.Y., Jenks B.G.; RT "The novel pituitary polypeptide 7B2 is a highly-conserved protein RT coexpressed with proopiomelanocortin."; RL Eur. J. Biochem. 181:75-79(1989). RN [2] RP PROTEOLYTIC PROCESSING. RX MEDLINE=90368773; PubMed=2394742; RA Ayoubi T.A.Y., van Duijnhoven H.L.P., van de Ven W.J.M., Jenks B.G., RA Roubos E.W., Martens G.J.M.; RT "The neuroendocrine polypeptide 7B2 is a precursor protein."; RL J. Biol. Chem. 265:15644-15647(1990). RN [3] RP DISULFIDE BOND. RX MEDLINE=98311224; PubMed=9648890; RA Van Horssen A.M., Van Kuppeveld F.J.M., Martens G.J.M.; RT "Manipulation of disulfide bonds differentially affects the RT intracellular transport, sorting, and processing of neuroendocrine RT secretory proteins."; RL J. Neurochem. 71:402-409(1998). RN [4] RP REVIEW. RX MEDLINE=21332545; PubMed=11439082; DOI=10.1042/0264-6021:3570329; RA Mbikay M., Seidah N.G., Chretien M.; RT "Neuroendocrine secretory protein 7B2: structure, expression and RT functions."; RL Biochem. J. 357:329-342(2001). CC -!- FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing CC its premature activation in the regulated secretory pathway. Binds CC to inactive PCSK2 in the endoplasmic reticulum and facilitates its CC transport from there to later compartments of the secretory CC pathway where it is proteolytically matured and activated. Also CC required for cleavage of PCSK2 but does not appear to be involved CC in its folding. Plays a role in regulating pituitary hormone CC secretion. The C-terminal peptide inhibits PCSK2 in vitro. CC -!- SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway. CC Dissociation occurs at later stages (By similarity). CC -!- SUBCELLULAR LOCATION: Note=Neuroendocrine and endocrine secretory CC granules. CC -!- PTM: Proteolytically cleaved in the Golgi by a furin-like CC convertase to generate bioactive peptides (By similarity). CC -!- PTM: Sulfated on tyrosine residues (By similarity). CC -!- SIMILARITY: Belongs to the 7B2 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X15608; CAA33631.1; -; mRNA. DR PIR; S03938; S03938. DR UniGene; Xl.47184; -. DR MEROPS; I21.001; -. DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB. DR GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB. DR GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB. DR GO; GO:0046883; P:regulation of hormone secretion; ISS:UniProtKB. DR InterPro; IPR007945; Secretogranin_V. DR PANTHER; PTHR12738; Secretogranin_V; 1. DR Pfam; PF05281; Secretogranin_V; 1. KW Chaperone; Cleavage on pair of basic residues; Neuropeptide; KW Phosphorylation; Sulfation; Transport. FT CHAIN <1 161 Neuroendocrine protein 7B2. FT /FTId=PRO_0000045862. FT CHAIN <1 128 N-terminal peptide (By similarity). FT /FTId=PRO_0000000053. FT PEPTIDE 152 161 C-terminal peptide (By similarity). FT /FTId=PRO_0000000054. FT MOD_RES 157 157 Phosphoserine (By similarity). FT DISULFID 73 82 FT NON_TER 1 1 SQ SEQUENCE 161 AA; 17992 MW; A6E32531A29D82FC CRC64; MEELGIARPR VEYPAHQAMN LVGPQSIEGG AHEGLQHLGP YGNIPNIVAE LTGDNIPKDF REDQGYPNPP NPCPVGKTGD GCLEDTPDTA QFSREYQLHQ NLYDPEHNYP GASTWNKKLL YEKIKGASQR QKRTVNPYLQ GQKLDKVVAK KSVPHFSDEE E // ID 7E_DICDI Reviewed; 97 AA. AC P15649; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 31-OCT-2006, entry version 33. DE Protein 7E. GN Name=7E; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=AX2; RX MEDLINE=90205618; PubMed=2157129; RA Ramji D.P., Richards A.J., Jagger P., Bleasby A., Hames B.D.; RT "Two cyclic AMP-regulated genes from Dictyostelium discoideum encode RT homologous proteins."; RL Mol. Microbiol. 4:129-135(1990). CC -!- DEVELOPMENTAL STAGE: Expressed only late in development. Its CC expression ceases upon cell disaggregation but is fully restored CC by exogenous cAMP. CC -!- DOMAIN: May form an extended coil structure. CC -!- SIMILARITY: To D.discoideum protein 2C. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X16959; CAA34832.1; -; mRNA. DR PIR; S08136; S08136. DR DictyBase; DDB0001796; 7E. DR InterPro; IPR008455; Coiled. DR Pfam; PF05710; Coiled; 1. FT CHAIN 1 97 Protein 7E. FT /FTId=PRO_0000064400. FT COMPBIAS 15 36 Ser-rich. FT COMPBIAS 82 95 Gly-rich. SQ SEQUENCE 97 AA; 9110 MW; E3C20C259858B830 CRC64; MTILASICKL GNTKSTSSSI GSSYSSAVSF GSNSVSCGEC GGDGPSFPNA SPRTGVKAGV NVDGLLGAIG KTVNGMLISP NGGGGGMGMG GGSCGCI // ID 7LESS_DROME Reviewed; 2554 AA. AC P13368; Q9TYI0; Q9U5V7; Q9VZ36; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 23-JAN-2007, entry version 82. DE Protein sevenless (EC 2.7.10.1). GN Name=sev; Synonyms=HD-265; ORFNames=CG18085; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF RP LYS-2242. RC STRAIN=Canton-S; RX MEDLINE=88282538; PubMed=2840202; DOI=10.1016/0092-8674(88)90193-6; RA Basler K., Hafen E.; RT "Control of photoreceptor cell fate by the sevenless protein requires RT a functional tyrosine kinase domain."; RL Cell 54:299-311(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Oregon-R; RX MEDLINE=88329706; PubMed=3138161; RA Bowtell D.L.L., Simon M.A., Rubin G.M.; RT "Nucleotide sequence and structure of the sevenless gene of Drosophila RT melanogaster."; RL Genes Dev. 2:620-634(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2349-2408. RX MEDLINE=98401146; PubMed=9731193; DOI=10.1006/bbrc.1998.9003; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). RN [6] RP IDENTIFICATION OF FN-III REPEATS. RX MEDLINE=90199889; PubMed=2317871; DOI=10.1016/0092-8674(90)90209-W; RA Norton P.A., Hynes R.O., Ress D.J.G.; RT "Sevenless: seven found?"; RL Cell 61:15-16(1990). RN [7] RP INTERACTION WITH DAB. RX MEDLINE=98336289; PubMed=9671493; RA Le N., Simon M.A.; RT "Disabled is a putative adaptor protein that functions during RT signaling by the sevenless receptor tyrosine kinase."; RL Mol. Cell. Biol. 18:4844-4854(1998). CC -!- FUNCTION: Receptor for an extracellular signal required to CC instruct a cell to differentiate into an R7 photoreceptor. The CC ligand for sev is the boss (bride of sevenless) protein on the CC surface of the neighboring R8 cell. CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a CC [protein]-L-tyrosine phosphate. CC -!- SUBUNIT: May form a complex with drk and Sos. Binds the CC phosphotyrosine interaction domain (PID) of Dab. CC -!- DOMAIN: It is unclear whether the potential membrane spanning CC region near the N-terminus is present as a transmembrane domain in CC the native protein or serves as a cleaved signal sequence. CC -!- SIMILARITY: Belongs to the Tyr protein kinase family. Insulin CC receptor subfamily. CC -!- SIMILARITY: Contains 7 fibronectin type-III domains. CC -!- SIMILARITY: Contains 1 protein kinase 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; J03158; AAA28882.1; -; Genomic_DNA. DR EMBL; X13666; CAA31960.1; ALT_INIT; mRNA. DR EMBL; X13666; CAB55310.1; -; mRNA. DR EMBL; AE014298; AAF47992.2; -; Genomic_DNA. DR EMBL; AJ002917; CAA05752.1; -; Genomic_DNA. DR PIR; A28912; TVFF7L. DR UniGene; Dm.2618; -. DR HSSP; P08069; 1JQH. DR Ensembl; CG18085; Drosophila melanogaster. DR KEGG; dme:Dmel_CG18085; -. DR FlyBase; FBgn0003366; sev. DR GermOnline; CG18085; Drosophila melanogaster. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004713; F:protein-tyrosine kinase activity; IDA:FlyBase. DR GO; GO:0008595; P:determination of anterior/posterior axis, e...; TAS:FlyBase. DR GO; GO:0045467; P:R7 development; NAS:FlyBase. DR GO; GO:0008293; P:torso signaling pathway; NAS:FlyBase. DR InterPro; IPR003961; FN_III. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000033; LDLR. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002011; RecepttyrkinsII. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Gene3D; G3DSA:2.60.40.30; FN_III-like; 6. DR Pfam; PF00041; fn3; 6. DR Pfam; PF07714; Pkinase_Tyr; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00060; FN3; 7. DR SMART; SM00135; LY; 2. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50853; FN3; 7. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1. KW ATP-binding; Complete proteome; Glycoprotein; Kinase; Membrane; KW Nucleotide-binding; Phosphorylation; Receptor; Repeat; KW Sensory transduction; Transferase; Transmembrane; KW Tyrosine-protein kinase; Vision. FT CHAIN 1 2554 Protein sevenless. FT /FTId=PRO_0000058928. FT TOPO_DOM 1 2123 Extracellular (Potential). FT TRANSMEM 2124 2147 Potential. FT TOPO_DOM 2148 2554 Cytoplasmic (Potential). FT DOMAIN 311 431 Fibronectin type-III 1. FT DOMAIN 436 528 Fibronectin type-III 2. FT DOMAIN 822 921 Fibronectin type-III 3. FT DOMAIN 1298 1392 Fibronectin type-III 4. FT DOMAIN 1680 1794 Fibronectin type-III 5. FT DOMAIN 1797 1897 Fibronectin type-III 6. FT DOMAIN 1898 1988 Fibronectin type-III 7. FT DOMAIN 2209 2485 Protein kinase. FT NP_BIND 2215 2223 ATP (By similarity). FT COMPBIAS 2038 2046 Poly-Arg. FT ACT_SITE 2343 2343 Proton acceptor (By similarity). FT BINDING 2242 2242 ATP (By similarity). FT MOD_RES 2380 2380 Phosphotyrosine (by autocatalysis) (By FT similarity). FT CARBOHYD 30 30 N-linked (GlcNAc...) (Potential). FT CARBOHYD 129 129 N-linked (GlcNAc...) (Potential). FT CARBOHYD 481 481 N-linked (GlcNAc...) (Potential). FT CARBOHYD 505 505 N-linked (GlcNAc...) (Potential). FT CARBOHYD 617 617 N-linked (GlcNAc...) (Potential). FT CARBOHYD 647 647 N-linked (GlcNAc...) (Potential). FT CARBOHYD 966 966 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1228 1228 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1313 1313 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1353 1353 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1550 1550 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1557 1557 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1639 1639 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1725 1725 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1756 1756 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1804 1804 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1889 1889 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1947 1947 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2073 2073 N-linked (GlcNAc...) (Potential). FT MUTAGEN 2242 2242 K->M: Inactivates the protein. FT CONFLICT 392 392 V -> M (in Ref. 1). FT CONFLICT 663 663 A -> T (in Ref. 3). FT CONFLICT 1703 1703 N -> H (in Ref. 3). FT CONFLICT 1730 1731 RG -> KE (in Ref. 3). FT CONFLICT 1741 1741 V -> M (in Ref. 3). FT CONFLICT 1823 1823 E -> Q (in Ref. 2). FT CONFLICT 2271 2271 C -> R (in Ref. 1). SQ SEQUENCE 2554 AA; 287025 MW; 09E238A0F27684F8 CRC64; MTMFWQQNVD HQSDEQDKQA KGAAPTKRLN ISFNVKIAVN VNTKMTTTHI NQQAPGTSSS SSNSQNASPS KIVVRQQSSS FDLRQQLARL GRQLASGQDG HGGISTILII NLLLLILLSI CCDVCRSHNY TVHQSPEPVS KDQMRLLRPK LDSDVVEKVA IWHKHAAAAP PSIVEGIAIS SRPQSTMAHH PDDRDRDRDP SEEQHGVDER MVLERVTRDC VQRCIVEEDL FLDEFGIQCE KADNGEKCYK TRCTKGCAQW YRALKELESC QEACLSLQFY PYDMPCIGAC EMAQRDYWHL QRLAISHLVE RTQPQLERAP RADGQSTPLT IRWAMHFPEH YLASRPFNIQ YQFVDHHGEE LDLEQEDQDA SGETGSSAWF NLADYDCDEY YVCEILEALI PYTQYRFRFE LPFGENRDEV LYSPATPAYQ TPPEGAPISA PVIEHLMGLD DSHLAVHWHP GRFTNGPIEG YRLRLSSSEG NATSEQLVPA GRGSYIFSQL QAGTNYTLAL SMINKQGEGP VAKGFVQTHS ARNEKPAKDL TESVLLVGRR AVMWQSLEPA GENSMIYQSQ EELADIAWSK REQQLWLLNV HGELRSLKFE SGQMVSPAQQ LKLDLGNISS GRWVPRRLSF DWLHHRLYFA MESPERNQSS FQIISTDLLG ESAQKVGESF DLPVEQLEVD ALNGWIFWRN EESLWRQDLH GRMIHRLLRI RQPGWFLVQP QHFIIHLMLP QEGKFLEISY DGGFKHPLPL PPPSNGAGNG PASSHWQSFA LLGRSLLLPD SGQLILVEQQ GQAASPSASW PLKNLPDCWA VILLVPESQP LTSAGGKPHS LKALLGAQAA KISWKEPERN PYQSADAARS WSYELEVLDV ASQSAFSIRN IRGPIFGLQR LQPDNLYQLR VRAINVDGEP GEWTEPLAAR TWPLGPHRLR WASRQGSVIH TNELGEGLEV QQEQLERLPG PMTMVNESVG YYVTGDGLLH CINLVHSQWG CPISEPLQHV GSVTYDWRGG RVYWTDLARN CVVRMDPWSG SRELLPVFEA NFLALDPRQG HLYYATSSQL SRHGSTPDEA VTYYRVNGLE GSIASFVLDT QQDQLFWLVK GSGALRLYRA PLTAGGDSLQ MIQQIKGVFQ AVPDSLQLLR PLGALLWLER SGRRARLVRL AAPLDVMELP TPDQASPASA LQLLDPQPLP PRDEGVIPMT VLPDSVRLDD GHWDDFHVRW QPSTSGGNHS VSYRLLLEFG QRLQTLDLST PFARLTQLPQ AQLQLKISIT PRTAWRSGDT TRVQLTTPPV APSQPRRLRV FVERLATALQ EANVSAVLRW DAPEQGQEAP MQALEYHISC WVGSELHEEL RLNQSALEAR VEHLQPDQTY HFQVEARVAA TGAAAGAASH ALHVAPEVQA VPRVLYANAE FIGELDLDTR NRRRLVHTAS PVEHLVGIEG EQRLLWVNEH VELLTHVPGS APAKLARMRA EVLALAVDWI QRIVYWAELD ATAPQAAIIY RLDLCNFEGK ILQGERVWST PRGRLLKDLV ALPQAQSLIW LEYEQGSPRN GSLRGRNLTD GSELEWATVQ PLIRLHAGSL EPGSETLNLV DNQGKLCVYD VARQLCTASA LRAQLNLLGE DSIAGQLAQD SGYLYAVKNW SIRAYGRRRQ QLEYTVELEP EEVRLLQAHN YQAYPPKNCL LLPSSGGSLL KATDCEEQRC LLNLPMITAS EDCPLPIPGV RYQLNLTLAR GPGSEEHDHG VEPLGQWLLG AGESLNLTDL LPFTRYRVSG ILSSFYQKKL ALPTLVLAPL ELLTASATPS PPRNFSVRVL SPRELEVSWL PPEQLRSESV YYTLHWQQEL DGENVQDRRE WEAHERRLET AGTHRLTGIK PGSGYSLWVQ AHATPTKSNS SERLHVRSFA ELPELQLLEL GPYSLSLTWA GTPDPLGSLQ LECRSSAEQL RRNVAGNHTK MVVEPLQPRT RYQCRLLLGY AATPGAPLYH GTAEVYETLG DAPSQPGKPQ LEHIAEEVFR VTWTAARGNG APIALYNLEA LQARSDIRRR RRRRRRNSGG SLEQLPWAEE PVVVEDQWLD FCNTTELSCI VKSLHSSRLL LFRVRARSLE HGWGPYSEES ERVAEPFVSP EKRGSLVLAI IAPAAIVSSC VLALVLVRKV QKRRLRAKKL LQQSRPSIWS NLSTLQTQQQ LMAVRNRAFS TTLSDADIAL LPQINWSQLK LLRFLGSGAF GEVYEGQLKT EDSEEPQRVA IKSLRKGASE FAELLQEAQL MSNFKHENIV CLVGICFDTE SISLIMEHME AGDLLSYLRA ARATSTQEPQ PTAGLSLSEL LAMCIDVANG CSYLEDMHFV HRDLACRNCL VTESTGSTDR RRTVKIGDFG LARDIYKSDY YRKEGEGLLP VRWMSPESLV DGLFTTQSDV WAFGVLCWEI LTLGQQPYAA RNNFEVLAHV KEGGRLQQPP MCTEKLYSLL LLCWRTDPWE RPSFRRCYNT LHAISTDLRR TQMASATADT VVSCSRPEFK VRFDGQPLEE HREHNERPED ENLTLREVPL KDKQLYANEG VSRL // ID 7LESS_DROVI Reviewed; 2594 AA. AC P20806; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 28-NOV-2006, entry version 68. DE Protein sevenless (EC 2.7.10.1). GN Name=sev; OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7244; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=90319110; PubMed=2115169; RA Michael W.M., Bowtell D.D.L., Rubin G.M.; RT "Comparison of the sevenless genes of Drosophila virilis and RT Drosophila melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 87:5351-5353(1990). CC -!- FUNCTION: Receptor for an extracellular signal required to CC instruct a cell to differentiate into a R7 photoreceptor. The CC ligand for Sev is the Boss (Bride of Sevenless) protein. CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a CC [protein]-L-tyrosine phosphate. CC -!- DOMAIN: It is unclear whether the potential membrane spanning CC region near the N-terminus is present as a transmembrane domain in CC the native protein or serves as a cleaved signal sequence. CC -!- SIMILARITY: Belongs to the Tyr protein kinase family. Insulin CC receptor subfamily. CC -!- SIMILARITY: Contains 7 fibronectin type-III domains. CC -!- SIMILARITY: Contains 1 protein kinase 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; M34545; AAA28883.1; -; Genomic_DNA. DR EMBL; M34544; AAA28883.1; JOINED; Genomic_DNA. DR EMBL; M34543; AAA28883.1; JOINED; Genomic_DNA. DR PIR; A35774; A35774. DR HSSP; Q62838; 1LUF. DR FlyBase; FBgn0013140; Dvir\sev. DR InterPro; IPR003961; FN_III. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000033; LDLR. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002011; RecepttyrkinsII. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Gene3D; G3DSA:2.60.40.30; FN_III-like; 7. DR Pfam; PF00041; fn3; 6. DR Pfam; PF07714; Pkinase_Tyr; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00060; FN3; 7. DR SMART; SM00135; LY; 3. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50853; FN3; 8. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1. KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding; KW Phosphorylation; Receptor; Repeat; Sensory transduction; Transferase; KW Transmembrane; Tyrosine-protein kinase; Vision. FT CHAIN 1 2594 Protein sevenless. FT /FTId=PRO_0000058929. FT TOPO_DOM 1 2139 Extracellular (Potential). FT TRANSMEM 2140 2163 Potential. FT TOPO_DOM 2164 2594 Cytoplasmic (Potential). FT DOMAIN 356 459 Fibronectin type-III 1. FT DOMAIN 464 555 Fibronectin type-III 2. FT DOMAIN 835 935 Fibronectin type-III 3. FT DOMAIN 1328 1421 Fibronectin type-III 4. FT DOMAIN 1706 1816 Fibronectin type-III 5. FT DOMAIN 1817 1916 Fibronectin type-III 6. FT DOMAIN 1917 2007 Fibronectin type-III 7. FT DOMAIN 2224 2495 Protein kinase. FT NP_BIND 2230 2238 ATP (By similarity). FT COMPBIAS 9 26 Poly-Gln. FT COMPBIAS 2057 2063 Poly-Arg. FT ACT_SITE 2355 2355 Proton acceptor (By similarity). FT BINDING 2257 2257 ATP (By similarity). FT MOD_RES 2391 2391 Phosphotyrosine (by autocatalysis) (By FT similarity). FT CARBOHYD 77 77 N-linked (GlcNAc...) (Potential). FT CARBOHYD 401 401 N-linked (GlcNAc...) (Potential). FT CARBOHYD 508 508 N-linked (GlcNAc...) (Potential). FT CARBOHYD 532 532 N-linked (GlcNAc...) (Potential). FT CARBOHYD 641 641 N-linked (GlcNAc...) (Potential). FT CARBOHYD 667 667 N-linked (GlcNAc...) (Potential). FT CARBOHYD 778 778 N-linked (GlcNAc...) (Potential). FT CARBOHYD 797 797 N-linked (GlcNAc...) (Potential). FT CARBOHYD 874 874 N-linked (GlcNAc...) (Potential). FT CARBOHYD 980 980 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1257 1257 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1344 1344 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1382 1382 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1577 1577 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1587 1587 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1665 1665 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1752 1752 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1776 1776 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1824 1824 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1908 1908 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1966 1966 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2088 2088 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 2594 AA; 289133 MW; 77D8A356CBAD0BBD CRC64; MFWREDAAQQ QQQQQQQQQQ QQQQQQPPHP PKRLSFSFNV KIAVNVNTKM STTHINQERS KQQTTTGSRS RSRSNSNSSV SCKGDGDRRV RRHTTRLVGL RQQLLHLGRQ LNPGQFLVTG HGGISTILIA NLLLLLLLSL CCNVCCRSHI EPDQNLTPTT TSPAAVAVVP MLLPLAQTHM RPQLDSDVVE KVAVWTKHVG AAPPSIAEGI AISSVVRMPP SIQTPTETVR RQEQQRQQQQ QQQEAAAAAA ADAAIDERIV LERVTRDCVQ RCIVEEDLFL DEFGIKCEKA DNSDKCYKTR CNKGCAQWYR ALKEIEPCQE ACASTQFYPY DMPCIGACET AQRDYWHMQR LAMARLVETT QPQLLEMTDE SSTLTIKWAM QFPENYLASR PFNIQYQQVD NQSEPEWHNL ADYDCDEYYV CEILEALVPY TRYKFRFELP FGESSEDVLY SPATPVYETP MEGAPISAPI IVALLALDEH HVFVHWRPGR YSNAPIEGYR VLLTSAGNTS REQLLPAQRT SCIFAQLQPL TNYTVALTMI NKQGEGPSTV VSIVTKSPLE PQQLQSVLLA SEHSIIWQSL EPAGETRLLY TSEPAAISDF TFSQREQRLW LLDELGQLHS QLLDETTTSA ARRLRLELPS NGSSQWTPRK LSLDWLQRRL YIAAQANSSD GAEGGFELFS SNLEGGDVQM AGVQLGLVVE QLELDALNGW LFWCDADSLW RLDLSSKQQL RLTQPAGAPG RFMLEPQRWL LHVLLPQENQ LLELSYDGGH KHALALSNDS WRGFAWSSDQ AQLLLANETQ LQLLDGQTLV PLANWSPDGG CCALLPLERR RQPLSLEPPA PRELRALLGA QGAHITWQPP AANPYQTATA AARNFSYELE VLDVASQSAY NIRNIRVPHF GLERLQADNL YQLRVRANNA AGRAGVWTAP LATRTWPLGD HRLRWATQRG SLYTTNELGG QLQPLPVQLA SSPGPLALVN ASVAYYVSGR EQSLHCVNLL QPQLSCTDER LEHVGAVAYD WRGGLLYWTD LARDCVQRLD PFSGERELLP IFGARHLALD SAQGHLYYSS SAHLARRSLS ALSTHQPELE YYHVNGLAGQ ISGFCLDLPQ RHIYWLVAGN SALHLYRTAL SAGGSQAAVP LQLLTTLPAA DALPHTLQHL APLGALLWLA ADGRGAHLLR LAAQLETDTD TMRLLPEGLV EPLSAVQLLE RSAGPPPPPP DEGVRPLAVP PDSVHIDEGG HWNDFRVRWQ PAASGGNHSV CYKLLLEHGS ERLITLELLT PFARITQLAQ APLGLRISIT PHTAWRAGST TRVQLDTPVA APTQPRRLRV FVERQAAPLQ LAPNVSALLR WDVPEEHAGS QSLQYRISCW RGSELHSELL LNQSTLEARV EHLQPEETYR FQVQAHVAAT GLAAGATSHA LHVSPEVQSV PRLLYANAEH IGELDLDTGH RKQLVHTASP VEHLVVLQGE QRLLWVNEHV ELLSHVPGKA PAKLARMRAE VLALTVDWVQ RIVYWAELDA ADGGCVIYSL DLCRFDGRIL QGERLWSTPR GQLLRDLVAL PHARQLVWLQ HDLDSRNATL QGRSLANGSA LTFEGVTLPL WRLFEGSQEP LAETLNLVDH LGRLCVYHVA RQLCTSSALR AQLNLLNDDI GQLAQDPGYL YALRNGSVRA YGRRRQQLEF LLELQPDEVR LLRAYNYQAY PSRRCLLLPT TAAALESTPS SCEETQCSLQ LPALSAAPDC PLPVPGLNYQ LNLSSSSRSA QLELRSLHSA AGLTLNISQL QPYQAYELRA QVGSYYQQQL GQEPLQLPVL TLHTAAATPS APRNFSGRAL SPSELELSWL APLELRSASV YYTLHWQLQL EDTEEQSQEQ PAQEQRVETA GVQRLTGLQP ARLYQVWLQA HATPSKYNSS GRLLIRSYAP LPPLQLIELN AYGMTLAWPG TPDALSSLTL ECQSLREQLQ FNVAGNHTQM RLAPLQPKTR YSCRLALAYA ATPGAPIYFG PSHEYETLGD APSAPGRPQL EHIAGEIFRV SWTPALDNGS PILLYNLEAL QARRTNRRRR RRRETTLSLL PWAEEPLVIE DQWLDFCNTT ELSCIVRELH TRRLLLFRVR ARNRPHGWGP YSEDSERIAE PFVSPEKRGS LVLAIIAPAA IVSSCVLALV LVRKLQKRRH RAKKLLQQSR PSIWSNLSAL QTQQQLLAAR SRTFSMSLSD ADIALLPQIN WNRLTLLRFL GSGAFGEVYE GQLQAEDEAQ PQRVAIKSLR KGASEFAELL QEAQLMSNFK HENIVCLIGI CCDTDSISLI MEHMEAGDLL SYLRAARPSS QEALSKLQLP ELLSMCLDVA NGCSYMEDMH FVHRDLACRN CLVSDGAAIG GRRIVKIGDF GLARDIYKSD YYRKEGEGLL PVRWMALESL VDGLFSTQSD VWAFGVLCWE IFTLGQQPYA ARNNFEVLAH VKEGGRLQQP ERCPEKLYAL LLQCWRSEPW ERPSFKRCLS TLQALSSDLR RTEMLATDET PLVSALCAFK PDAKVRFDDA PQRLTLHLDA KDTVSTTDAD TTGSPTTPTA PTTPTTTTST IAVVSTAPSS ENGQLYANEG ISGL // ID 7OMT6_MEDSA Reviewed; 352 AA. AC O22308; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 28-NOV-2006, entry version 41. DE Isoflavone-7-O-methyltransferase 6 (EC 2.1.1.150) (Isoflavone-O- DE methyltransferase 6) (7-IOMT-6). OS Medicago sativa (Alfalfa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Trifolieae; OC Medicago. OX NCBI_TaxID=3879; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98145455; PubMed=9484461; DOI=10.1023/A:1005938121453; RA He X.-Z., Reddy J.T., Dixon R.A.; RT "Stress responses in alfalfa (Medicago sativa L). XXII. cDNA cloning RT and characterization of an elicitor-inducible isoflavone 7-O- RT methyltransferase."; RL Plant Mol. Biol. 36:43-54(1998). CC -!- FUNCTION: Transfers a methyl group to 7-hydroxyls of the CC isoflavones daidzein, genistein and 6,7,4'-trihydroxyisoflavone. CC Can also methylate (+)6a-hydroxymaackiain with lower efficiency. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 7- CC hydroxyisoflavone = S-adenosyl-L-homocysteine + a 7- CC methoxyisoflavone. CC -!- PATHWAY: Medicarpin synthesis. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF000975; AAC49926.1; -; mRNA. DR HSSP; O24529; 1FP2. DR SMR; O22308; 8-352. DR InterPro; IPR012967; Dimerisation. DR InterPro; IPR001077; O_Met_trans2. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF08100; Dimerisation; 1. DR Pfam; PF00891; Methyltransf_2; 1. KW Methyltransferase; Transferase. FT CHAIN 1 352 Isoflavone-7-O-methyltransferase 6. FT /FTId=PRO_0000204436. FT REGION 118 127 Substrate binding (By similarity). FT ACT_SITE 257 257 Proton acceptor. FT BINDING 196 196 S-adenosyl-L-methionine; via carbonyl FT oxygen (By similarity). FT BINDING 219 219 S-adenosyl-L-methionine (By similarity). FT BINDING 239 239 S-adenosyl-L-methionine (By similarity). FT BINDING 240 240 S-adenosyl-L-methionine; via amide FT nitrogen (By similarity). FT BINDING 253 253 S-adenosyl-L-methionine (By similarity). SQ SEQUENCE 352 AA; 39605 MW; 31B95226966C1C98 CRC64; MASSINGRKP SEIFKAQALL YKHIYAFIDS MSLKWAVEMN IPNIIQNHGK PISLSNLVSI LQVPSSKIGN VRRLMRYLAH NGFFEIITKE EESYALTVAS ELLVRGSDLC LAPMVECVLD PTLSGSYHEL KKWIYEEDLT LFGVTLGSGF WDFLDKNPEY NTSFNDAMAS DSKLINLALR DCDFVFDGLE SIVDVGGGTG TTAKIICETF PKLKCIVFDR PQVVENLSGS NNLTYVGGDM FTSIPNADAV LLKYILHNWT DKDCLRILKK CKEAVTNDGK RGKVTIIDMV IDEKKDENQV TQIKLLMDVN MACLNGKERN EEEWKKLFIE AGFQHYKISP LTGFLSLIEI YP // ID 7OMT8_MEDSA Reviewed; 352 AA. AC O24529; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 28-NOV-2006, entry version 48. DE Isoflavone-7-O-methyltransferase 8 (EC 2.1.1.150) (Isoflavone-O- DE methyltransferase 8) (7-IOMT-8). OS Medicago sativa (Alfalfa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Trifolieae; OC Medicago. OX NCBI_TaxID=3879; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98145455; PubMed=9484461; DOI=10.1023/A:1005938121453; RA He X.-Z., Reddy J.T., Dixon R.A.; RT "Stress responses in alfalfa (Medicago sativa L). XXII. cDNA cloning RT and characterization of an elicitor-inducible isoflavone 7-O- RT methyltransferase."; RL Plant Mol. Biol. 36:43-54(1998). RN [2] RP PROTEIN SEQUENCE OF 23-31; 77-105 AND 327-337, AND CHARACTERIZATION. RX MEDLINE=97108721; PubMed=8951042; DOI=10.1006/abbi.1996.0539; RA He X.-Z., Dixon R.A.; RT "Affinity chromatography, substrate/product specificity, and amino RT acid sequence analysis of an isoflavone O-methyltransferase from RT alfalfa (Medicago sativa L.)."; RL Arch. Biochem. Biophys. 336:121-129(1996). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, AND RP SUBUNIT. RX MEDLINE=21127494; PubMed=11224575; DOI=10.1038/85029; RA Zubieta C., He X.-Z., Dixon R.A., Noel J.P.; RT "Structures of two natural product methyltransferases reveal the basis RT for substrate specificity in plant O-methyltransferases."; RL Nat. Struct. Biol. 8:271-279(2001). CC -!- FUNCTION: Transfers a methyl group to 7-hydroxyls of the CC isoflavones daidzein, genistein and 6,7,4'-trihydroxyisoflavone. CC Can also methylate (+)6a-hydroxymaackiain with lower efficiency. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 7- CC hydroxyisoflavone = S-adenosyl-L-homocysteine + a 7- CC methoxyisoflavone. CC -!- PATHWAY: Medicarpin synthesis. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U97125; AAC49928.1; -; mRNA. DR PIR; T09707; T09707. DR PDB; 1FP2; X-ray; A=1-352. DR PDB; 1FPX; X-ray; A=1-352. DR InterPro; IPR012967; Dimerisation. DR InterPro; IPR001077; O_Met_trans2. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF08100; Dimerisation; 1. DR Pfam; PF00891; Methyltransf_2; 1. KW 3D-structure; Direct protein sequencing; Methyltransferase; KW Transferase. FT CHAIN 1 352 Isoflavone-7-O-methyltransferase 8. FT /FTId=PRO_0000204437. FT REGION 118 127 Substrate binding. FT ACT_SITE 257 257 Proton acceptor. FT BINDING 196 196 S-adenosyl-L-methionine; via carbonyl FT oxygen. FT BINDING 219 219 S-adenosyl-L-methionine. FT BINDING 239 239 S-adenosyl-L-methionine. FT BINDING 240 240 S-adenosyl-L-methionine; via amide FT nitrogen. FT BINDING 253 253 S-adenosyl-L-methionine. FT TURN 11 11 FT HELIX 12 24 FT TURN 25 26 FT HELIX 27 38 FT TURN 39 40 FT HELIX 41 48 FT TURN 49 49 FT HELIX 54 61 FT TURN 62 62 FT HELIX 65 67 FT HELIX 68 80 FT TURN 81 82 FT STRAND 83 96 FT HELIX 98 101 FT TURN 102 103 FT TURN 105 106 FT STRAND 107 109 FT HELIX 112 118 FT TURN 119 119 FT HELIX 121 125 FT HELIX 126 129 FT HELIX 130 134 FT TURN 135 135 FT HELIX 141 146 FT HELIX 150 156 FT HELIX 158 170 FT TURN 171 171 FT HELIX 172 180 FT TURN 181 181 FT HELIX 183 186 FT TURN 187 188 FT STRAND 190 195 FT TURN 196 196 FT TURN 198 199 FT HELIX 201 209 FT TURN 211 212 FT STRAND 214 219 FT HELIX 221 224 FT TURN 225 226 FT TURN 231 232 FT STRAND 233 237 FT TURN 240 242 FT STRAND 248 254 FT HELIX 256 258 FT HELIX 261 275 FT HELIX 277 279 FT STRAND 283 288 FT TURN 293 295 FT HELIX 298 310 FT HELIX 311 314 FT TURN 315 315 FT HELIX 321 330 FT TURN 331 332 FT STRAND 335 342 FT TURN 343 344 FT STRAND 345 351 SQ SEQUENCE 352 AA; 39604 MW; 31B95228986C1296 CRC64; MASSINGRKP SEIFKAQALL YKHIYAFIDS MSLKWAVEMN IPNIIQNHGK PISLSNLVSI LQVPSSKIGN VRRLMRYLAH NGFFEIITKE EESYALTVAS ELLVRGSDLC LAPMVECVLD PTLSGSYHEL KKWIYEEDLT LFGVTLGSGF WDFLDKNPEY NTSFNDAMAS DSKLINLALR DCDFVFDGLE SIVDVGGGTG TTAKIICETF PKLKCIVFDR PQVVENLSGS NNLTYVGGDM FTSIPNADAV LLKYILHNWT DKDCLRILKK CKEAVTNDGK RGKVTIIDMV IDKKKDENQV TQIKLLMDVN MACLNGKERN EEEWKKLFIE AGFQHYKISP LTGFLSLIEI YP // ID 7OMT9_MEDSA Reviewed; 352 AA. AC O22309; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 28-NOV-2006, entry version 40. DE Isoflavone-7-O-methyltransferase 9 (EC 2.1.1.150) (Isoflavone-O- DE methyltransferase 9) (7 IOMT-9). OS Medicago sativa (Alfalfa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Trifolieae; OC Medicago. OX NCBI_TaxID=3879; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98145455; PubMed=9484461; DOI=10.1023/A:1005938121453; RA He X.-Z., Reddy J.T., Dixon R.A.; RT "Stress responses in alfalfa (Medicago sativa L). XXII. cDNA cloning RT and characterization of an elicitor-inducible isoflavone 7-O- RT methyltransferase."; RL Plant Mol. Biol. 36:43-54(1998). CC -!- FUNCTION: Transfers a methyl group to 7-hydroxyls of the CC isoflavones daidzein, genistein and 6,7,4'-trihydroxyisoflavone. CC Can also methylate (+)6a-hydroxymaackiain with lower efficiency. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 7- CC hydroxyisoflavone = S-adenosyl-L-homocysteine + a 7- CC methoxyisoflavone. CC -!- PATHWAY: Medicarpin synthesis. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF000976; AAC49927.1; -; mRNA. DR PIR; T09254; T09254. DR HSSP; O24529; 1FP2. DR SMR; O22309; 8-352. DR InterPro; IPR012967; Dimerisation. DR InterPro; IPR001077; O_Met_trans2. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF08100; Dimerisation; 1. DR Pfam; PF00891; Methyltransf_2; 1. KW Methyltransferase; Transferase. FT CHAIN 1 352 Isoflavone-7-O-methyltransferase 9. FT /FTId=PRO_0000204438. FT REGION 118 127 Substrate binding. FT ACT_SITE 257 257 Proton acceptor (By similarity). FT BINDING 196 196 S-adenosyl-L-methionine; via carbonyl FT oxygen (By similarity). FT BINDING 219 219 S-adenosyl-L-methionine (By similarity). FT BINDING 239 239 S-adenosyl-L-methionine (By similarity). FT BINDING 240 240 S-adenosyl-L-methionine; via amide FT nitrogen (By similarity). FT BINDING 253 253 S-adenosyl-L-methionine (By similarity). SQ SEQUENCE 352 AA; 39541 MW; 955683CC90B94ACD CRC64; MASSINGRKP SEIFKAQALL YKHIYAFIDS MSLKWAVGMN IPNIIHNHGK PISLSNLVSI LQVPSSKIGN VRRLMRYLAH NGFFEIITKE EESYALTVAS ELLVRGSDLC LAPMVECVLD PTLSGSYHEL KKWIYEEDLT LFGVTLGSGF WDFLDKNPEY NTSFNDAMAS DSKLINLALR DCDFVFDGLE SIVDVGGGTG TTAKIICETF PKLKCIVFDR PQVVENLSGS NNLTYVGGDM FTSIPNADAV LLKYILHNWT DKDCLRILKK CKEAVTNDGK RGKVTIIDMV INEKKDENQV TQIKLLMDVN MACLNGKERN EEEWKKLFIE AGFQHYKISP LTGFLSLIEI YP // ID 7SB1_SOYBN Reviewed; 427 AA. AC P13917; Q39901; Q43464; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 20-FEB-2007, entry version 51. DE Basic 7S globulin precursor (Bg) (SBg7S) [Contains: Basic 7S globulin DE high kDa subunit; Basic 7S globulin low kDa subunit]. GN Name=BG; Synonyms=G7S; OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=cv. Miyagishirome; TISSUE=Seed; RX MEDLINE=90067863; PubMed=2587227; DOI=10.1093/nar/17.21.8868; RA Kagawa H., Hirano H.; RT "Sequence of a cDNA encoding soybean basic 7S globulin."; RL Nucleic Acids Res. 17:8868-8868(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Miyagishirome; TISSUE=Etiolated leaf; RX MEDLINE=94336768; PubMed=8058830; DOI=10.1104/pp.105.3.1019; RA Watanabe Y., Hirano H.; RT "Nucleotide sequence of the basic 7S globulin gene from soybean."; RL Plant Physiol. 105:1019-1020(1994). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Shi-shi; TISSUE=Cotyledon; RA Shu T.F., Hsieh K.L., Hsing Y.I., Chen Z.Y., Chow T.Y.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 25-57; 135-150; 276-311 AND 383-417. RX MEDLINE=91031409; PubMed=2226413; RA Hirano H., Watanabe T.; RT "Microsequencing of proteins electrotransferred onto immobilizing RT matrices from polyacrylamide gel electrophoresis: application to an RT insoluble protein."; RL Electrophoresis 11:573-580(1990). RN [5] RP PARTIAL PROTEIN SEQUENCE. RA Kagawa H., Yamauchi F., Hirano H.; RT "Soybean basic 7S globulin represents a protein widely distributed in RT legume species."; RL FEBS Lett. 226:145-149(1987). CC -!- FUNCTION: Seed storage protein. Has a protein kinase activity. CC Binds leginsulin. CC -!- SUBUNIT: The mature protein consists of high- and low-kDa subunits CC linked by disulfide bonds. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X16469; CAA34489.1; -; mRNA. DR EMBL; U59425; AAB03390.1; -; mRNA. DR EMBL; D16107; BAA03681.1; -; Genomic_DNA. DR PIR; S06750; S06750. DR UniGene; Gma.8432; -. DR InterPro; IPR009007; Pept_Aspartc_cat. DR InterPro; IPR001461; Peptidase_A1. DR Gene3D; G3DSA:2.40.70.10; Pept_Aspartc_cat; 1. DR PANTHER; PTHR13683; Peptidase_A1; 2. KW Direct protein sequencing; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 24 FT CHAIN 25 427 Basic 7S globulin. FT /FTId=PRO_0000032198. FT CHAIN 25 275 Basic 7S globulin high kDa subunit. FT /FTId=PRO_0000032199. FT CHAIN 276 427 Basic 7S globulin low kDa subunit. FT /FTId=PRO_0000032200. FT CONFLICT 48 48 W -> S (in Ref. 3). FT CONFLICT 264 264 N -> T (in Ref. 1). FT CONFLICT 305 305 F -> C (in Ref. 1). FT CONFLICT 309 309 F -> C (in Ref. 1). SQ SEQUENCE 427 AA; 46393 MW; 66041BC0680BACCB CRC64; MASILHYFLA LSLSCSFLFF LSDSVTPTKP INLVVLPVQN DGSTGLHWAN LQKRTPLMQV PVLVDLNGNH LWVNCEQQYS SKTYQAPFCH STQCSRANTH QCLSCPAASR PGCHKNTCGL MSTNPITQQT GLGELGEDVL AIHATQGSTQ QLGPLVTVPQ FLFSCAPSFL VQKGLPRNTQ GVAGLGHAPI SLPNQLASHF GLQRQFTTCL SRYPTSKGAI IFGDAPNNMR QFQNQDIFHD LAFTPLTITL QGEYNVRVNS IRINQHSVFP LNKISSTIVG STSGGTMIST STPHMVLQQS VYQAFTQVFA QQLPKQAQVK SVAPFGLCFN SNKINAYPSV DLVMDKPNGP VWRISGEDLM VQAQPGVTCL GVMNGGMQPR AEITLGARQL EENLVVFDLA RSRVGFSTSS LHSHGVKCAD LFNFANA // ID 7SBG2_SOYBN Reviewed; 433 AA. AC Q8RVH5; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 20-FEB-2007, entry version 26. DE Basic 7S globulin 2 precursor (Bg) (SBg7S) [Contains: Basic 7S DE globulin 2 high kDa subunit; Basic 7S globulin 2 low kDa subunit]. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Seed; RA Ishizu Y., Sassa H., Hirano H.; RT "Sequence of a cDNA encoding soybean basic 7S globulin isoform."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 25-59 AND 283-311. RX PubMed=2064630; RA Barbashov S.F., Egorov T.S.A., Kochkina V.M.; RT "Isolation and characteristics of insulin-binding proteins from RT soybeans."; RL Bioorg. Khim. 17:421-423(1991). CC -!- FUNCTION: Seed storage protein. Has a protein kinase activity. CC Binds leginsulin (By similarity). CC -!- SUBUNIT: The mature protein consists of high- and low-kDa subunits CC linked by disulfide bonds. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB084260; BAB91077.1; -; mRNA. DR UniGene; Gma.18201; -. DR InterPro; IPR009007; Pept_Aspartc_cat. DR InterPro; IPR001461; Peptidase_A1. DR Gene3D; G3DSA:2.40.70.10; Pept_Aspartc_cat; 1. DR PANTHER; PTHR13683; Peptidase_A1; 2. KW Direct protein sequencing; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 24 FT CHAIN 25 433 Basic 7S globulin 2. FT /FTId=PRO_0000032201. FT CHAIN 25 282 Basic 7S globulin 2 high kDa subunit. FT /FTId=PRO_0000032202. FT CHAIN 283 433 Basic 7S globulin 2 low kDa subunit. FT /FTId=PRO_0000032203. FT CONFLICT 31 31 H -> K (in Ref. 2). FT CONFLICT 49 49 A -> G (in Ref. 2). FT CONFLICT 57 57 N -> A (in Ref. 2). FT CONFLICT 287 287 G -> C (in Ref. 2). FT CONFLICT 290 291 GG -> CC (in Ref. 2). FT CONFLICT 311 311 F -> C (in Ref. 2). SQ SEQUENCE 433 AA; 47205 MW; FA41B93D8BD3EA38 CRC64; MASILHYFLA LSLSFSFLFF LSDSVPIPQH HTNPTKPINL LVLPVQNDAS TGLHWANLQK RTPLMQVPVL VDLNGNHLWV NCEQHYSSKT YQAPFCHSTQ CSRANTHQCL SCPAASRPGC HKNTCGLMST NPITQQTGLG ELGQDVLAIH ATQGSTQQLG PLVTVPQFLF SCAPSFLLQK GLPRNIQGVA GLGHAPISLP NQLASHFGLQ HQFTTCLSRY PTSKGALIFG DAPNNMQQFH NQDIFHDLAF TPLTVTPQGE YNVRVSSIRI NQHSVFPPNK ISSTIVGSSG GTMISTSTPH MVLQQSLYQA FTQVFAQQLE KQAQVKSVAP FGLCFNSNKI NAYPSVDLVM DKPNGPVWRI SGEDLMVQAQ PGVTCLGVMN GGMQPRAEVT LGTRQLEEKL MVFDLARSRV GFSTSSLHSH GVKCGDLFNF ANA // ID 7UP1_DROME Reviewed; 543 AA. AC P16375; Q8MQJ1; Q8T8U4; Q9VGA9; Q9VGB0; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 06-FEB-2007, entry version 73. DE Steroid receptor seven-up, isoforms B/C. GN Name=svp; Synonyms=NR2F3; ORFNames=CG11502; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, AND TISSUE RP SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=90124631; PubMed=2105166; RA Mlodzik M., Hiromi Y., Weber U., Goodman C.S., Rubin G.M.; RT "The Drosophila seven-up gene, a member of the steroid receptor gene RT superfamily, controls photoreceptor cell fates."; RL Cell 60:211-224(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C). RC STRAIN=Berkeley; TISSUE=Embryo, and Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=15691762; DOI=10.1016/j.devcel.2004.12.014; RA Kanai M.I., Okabe M., Hiromi Y.; RT "Seven-up controls switching of transcription factors that specify RT temporal identities of Drosophila neuroblasts."; RL Dev. Cell 8:203-213(2005). CC -!- FUNCTION: Receptor that is required in photoreceptors R1, R3, R4 CC and R6 during eye development; generation of the ganglion mother CC cell-2 (GMC-2) fate in the nb7-3 lineage, coinciding with the CC transition in the expression of HB to KR in the neuroblasts (NBs). CC -!- INTERACTION: CC Q86BY9:rig; NbExp=1; IntAct=EBI-131834, EBI-422757; CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=B; Synonyms=Type 1; CC IsoId=P16375-1; Sequence=Displayed; CC Name=C; CC IsoId=P16375-2; Sequence=VSP_013348; CC Note=No experimental confirmation available; CC Name=A; Synonyms=Type 2; CC IsoId=P16376-1; Sequence=External; CC -!- TISSUE SPECIFICITY: Expressed in several embryonic tissues; dorsal CC vessel, oenocyte and fat body. CNS expression is dynamic and CC confined to temporally restricted subsections of the NB lineage; CC expressed in many NB and GMCs, but only a small number of neurons. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 CC subfamily. CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-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; M28863; AAA62770.1; -; mRNA. DR EMBL; AE014297; AAF54773.1; -; Genomic_DNA. DR EMBL; AE014297; AAF54774.2; -; Genomic_DNA. DR EMBL; AY075272; AAL68139.1; -; mRNA. DR EMBL; AY129452; AAM76194.1; -; mRNA. DR PIR; A32693; A32693. DR UniGene; Dm.20676; -. DR HSSP; P19793; 1BY4. DR IntAct; P16375; -. DR TRANSFAC; T02741; -. DR Ensembl; CG11502; Drosophila melanogaster. DR KEGG; dme:Dmel_CG11502; -. DR FlyBase; FBgn0003651; svp. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-011233-MONOMER; -. DR GermOnline; CG11502; Drosophila melanogaster. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS:FlyBase. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0007510; P:cardioblast cell fate determination; IEP:FlyBase. DR GO; GO:0007503; P:fat body development; TAS:FlyBase. DR GO; GO:0007270; P:nerve-nerve synaptic transmission; IMP:FlyBase. DR GO; GO:0042331; P:phototaxis; IMP:FlyBase. DR GO; GO:0007462; P:R1/R6 cell fate commitment; TAS:FlyBase. DR GO; GO:0007464; P:R3/R4 cell fate commitment; TAS:FlyBase. DR GO; GO:0007465; P:R7 cell fate commitment; TAS:FlyBase. DR GO; GO:0007419; P:ventral cord development; TAS:FlyBase. DR InterPro; IPR003068; COUP_TF. DR InterPro; IPR001628; Hrmn_rcpt_DNA_bd. DR InterPro; IPR000536; Hrmn_rcpt_lig_bd. DR InterPro; IPR008946; Nucl_rcpt_lig_bd. DR InterPro; IPR001723; Str_hrmn_rcpt. DR InterPro; IPR013629; Znf-C4_C. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR Pfam; PF08420; zf-C4_C; 1. DR PRINTS; PR01282; COUPTNFACTOR. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. KW Alternative splicing; Complete proteome; DNA-binding; Metal-binding; KW Nuclear protein; Receptor; Sensory transduction; Transcription; KW Transcription regulation; Vision; Zinc; Zinc-finger. FT CHAIN 1 543 Steroid receptor seven-up, isoforms B/C. FT /FTId=PRO_0000053610. FT DNA_BIND 197 272 Nuclear receptor. FT ZN_FING 200 220 NR C4-type. FT ZN_FING 236 260 NR C4-type. FT VAR_SEQ 1 262 Missing (in isoform C). FT /FTId=VSP_013348. FT CONFLICT 203 203 C -> Y (in Ref. 4; AAM76194). SQ SEQUENCE 543 AA; 57988 MW; 0BC189DCF1A27213 CRC64; MCASPSTAPG FFNPRPQSGA ELSAFDIGLS RSMGLGVPPH SAWHEPPASL GGHLHAASAG PGTTTGSVAT GGGGTTPSSV ASQQSAVIKQ DLSCPSLNQA GSGHHPGIKE DLSSSLPSAN GGSAGGHHSG SGSGSGSGVN PGHGSDMLPL IKGHGQDMLT SIKGQPTGCG STTPSSQANS SHSQSSNSGS QIDSKQNIEC VVCGDKSSGK HYGQFTCEGC KSFFKRSVRR NLTYSCRGSR NCPIDQHHRN QCQYCRLKKC LKMGMRREAV QRGRVPPTQP GLAGMHGQYQ IANGDPMGIA GFNGHSYLSS YISLLLRAEP YPTSRYGQCM QPNNIMGIDN ICELAARLLF SAVEWAKNIP FFPELQVTDQ VALLRLVWSE LFVLNASQCS MPLHVAPLLA AAGLHASPMA ADRVVAFMDH IRIFQEQVEK LKALHVDSAE YSCLKAIVLF TTDACGLSDV THIESLQEKS QCALEEYCRT QYPNQPTRFG KLLLRLPSLR TVSSQVIEQL FFVRLVGKTP IETLIRDMLL SGNSFSWPYL PSM // ID 7UP2_DROME Reviewed; 746 AA. AC P16376; Q8INJ0; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 3. DT 06-FEB-2007, entry version 70. DE Steroid receptor seven-up, isoform A. GN Name=svp; Synonyms=NR2F3; ORFNames=CG11502; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX MEDLINE=90124631; PubMed=2105166; RA Mlodzik M., Hiromi Y., Weber U., Goodman C.S., Rubin G.M.; RT "The Drosophila seven-up gene, a member of the steroid receptor gene RT superfamily, controls photoreceptor cell fates."; RL Cell 60:211-224(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=15691762; DOI=10.1016/j.devcel.2004.12.014; RA Kanai M.I., Okabe M., Hiromi Y.; RT "Seven-up controls switching of transcription factors that specify RT temporal identities of Drosophila neuroblasts."; RL Dev. Cell 8:203-213(2005). CC -!- FUNCTION: Receptor that is required in photoreceptors R1, R3, R4 CC and R6 during eye development; generation of the ganglion mother CC cell-2 (GMC-2) fate in the nb7-3 lineage, coinciding with the CC transition in the expression of HB to KR in the neuroblasts (NBs). CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; Synonyms=Type 2; CC IsoId=P16376-1; Sequence=Displayed; CC Name=B; Synonyms=Type 1; CC IsoId=P16375-1; Sequence=External; CC Name=C; CC IsoId=P16375-2; Sequence=External; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in several embryonic tissues; dorsal CC vessel, oenocyte and fat body. CNS expression is dynamic and CC confined to temporally restricted subsections of the NB lineage; CC expressed in many NB and GMCs, but only a small number of neurons. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 CC subfamily. CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-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; M28864; AAA03014.1; -; mRNA. DR EMBL; AE014297; AAN13541.1; -; Genomic_DNA. DR PIR; B32693; B32693. DR UniGene; Dm.20676; -. DR HSSP; P19793; 1BY4. DR KEGG; dme:Dmel_CG11502; -. DR FlyBase; FBgn0003651; svp. DR GermOnline; CG11502; Drosophila melanogaster. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS:FlyBase. DR GO; GO:0005515; F:protein binding; IPI:FlyBase. DR GO; GO:0007510; P:cardioblast cell fate determination; IEP:FlyBase. DR GO; GO:0007503; P:fat body development; TAS:FlyBase. DR GO; GO:0007270; P:nerve-nerve synaptic transmission; IMP:FlyBase. DR GO; GO:0042331; P:phototaxis; IMP:FlyBase. DR GO; GO:0007462; P:R1/R6 cell fate commitment; TAS:FlyBase. DR GO; GO:0007464; P:R3/R4 cell fate commitment; TAS:FlyBase. DR GO; GO:0007465; P:R7 cell fate commitment; TAS:FlyBase. DR GO; GO:0007419; P:ventral cord development; TAS:FlyBase. DR InterPro; IPR003068; COUP_TF. DR InterPro; IPR001628; Hrmn_rcpt_DNA_bd. DR InterPro; IPR000536; Hrmn_rcpt_lig_bd. DR InterPro; IPR008946; Nucl_rcpt_lig_bd. DR InterPro; IPR001723; Str_hrmn_rcpt. DR InterPro; IPR013629; Znf-C4_C. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR Pfam; PF08420; zf-C4_C; 1. DR PRINTS; PR01282; COUPTNFACTOR. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR ProDom; PD000035; Znf_C4steroid; 1. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. KW Alternative splicing; Complete proteome; DNA-binding; Metal-binding; KW Nuclear protein; Receptor; Sensory transduction; Transcription; KW Transcription regulation; Vision; Zinc; Zinc-finger. FT CHAIN 1 746 Steroid receptor seven-up, isoform A. FT /FTId=PRO_0000053611. FT DNA_BIND 197 272 Nuclear receptor. FT ZN_FING 200 220 NR C4-type. FT ZN_FING 236 260 NR C4-type. FT COMPBIAS 538 664 Ser-rich. FT CONFLICT 546 546 A -> S (in Ref. 1). SQ SEQUENCE 746 AA; 76814 MW; D6085838A848087B CRC64; MCASPSTAPG FFNPRPQSGA ELSAFDIGLS RSMGLGVPPH SAWHEPPASL GGHLHAASAG PGTTTGSVAT GGGGTTPSSV ASQQSAVIKQ DLSCPSLNQA GSGHHPGIKE DLSSSLPSAN GGSAGGHHSG SGSGSGSGVN PGHGSDMLPL IKGHGQDMLT SIKGQPTGCG STTPSSQANS SHSQSSNSGS QIDSKQNIEC VVCGDKSSGK HYGQFTCEGC KSFFKRSVRR NLTYSCRGSR NCPIDQHHRN QCQYCRLKKC LKMGMRREAV QRGRVPPTQP GLAGMHGQYQ IANGDPMGIA GFNGHSYLSS YISLLLRAEP YPTSRYGQCM QPNNIMGIDN ICELAARLLF SAVEWAKNIP FFPELQVTDQ VALLRLVWSE LFVLNASQCS MPLHVAPLLA AAGLHASPMA ADRVVAFMDH IRIFQEQVEK LKALHVDSAE YSCLKAIVLF TTGKLLDILY KDVPALLTKV SALLGKGSTA SNDDVLAVVR DHLDELNRQE QESQAQQQAP LHLAAFMNCV AGVEAAVQQA EQAQVPTSSA SASVSAPLVP SAGSAFSSCQ AKSAGSEMDL LASLYAQAQA TPPSSGGGDA SGHNNSSGLG ASLPTQSQSG SSSRNLTASP LSTSLATAPA PASASAPAPV PTSSVAQVPV PAPVPVTSSA SSSSLGGGAY QTPSAAAAAA AMFHYQTPPR AAFGSAFDMF HHSTPFGVGV GHAHALAHSS GSGSASFGSP SYRYSPYSLA GSRWQL // ID 8511_TRYCR Reviewed; 752 AA. AC P18269; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 28-NOV-2006, entry version 50. DE Sialidase 85-1.1 precursor (EC 3.2.1.18) (Neuraminidase) (NA) (Major DE 85 kDa surface antigen) (SA85-1.1 protein). GN Name=SA85-1.1; OS Trypanosoma cruzi. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma; OC Schizotrypanum. OX NCBI_TaxID=5693; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CL; RX MEDLINE=91239592; PubMed=2034687; RA Kahn S., Colbert T.G., Wallace J.C., Hoagland N.A., Eisen H.; RT "The major 85-kDa surface antigen of the mammalian-stage forms of RT Trypanosoma cruzi is a family of sialidases."; RL Proc. Natl. Acad. Sci. U.S.A. 88:4481-4485(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 520-752. RC STRAIN=CL; RX MEDLINE=90324879; PubMed=1695668; DOI=10.1084/jem.172.2.589; RA Kahn S., van Voorhis W., Eisen H.; RT "The major 85-kD surface antigen of the mammalian form of Trypanosoma RT cruzi is encoded by a large heterogeneous family of simultaneously RT expressed genes."; RL J. Exp. Med. 172:589-597(1990). CC -!- FUNCTION: Developmentally regulated neuraminidase implicated in CC parasite invasion of cells. May contribute to the pathology during CC T.cruzi infection by cleaving sialic acid from cells of the immune CC system. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, CC alpha-(2->8)- glycosidic linkages of terminal sialic residues in CC oligosaccharides, glycoproteins, glycolipids, colominic acid and CC synthetic substrates. CC -!- DEVELOPMENTAL STAGE: Mammalian stage of parasite. CC -!- MISCELLANEOUS: The parasite mammalian stage surface antigen CC exhibits extensive antigenic diversity. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. CC -!- SIMILARITY: Contains 2 BNR 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; M62735; AAA30245.1; -; mRNA. DR EMBL; X53545; CAA37617.1; -; mRNA. DR PIR; A39378; A39378. DR PIR; S11292; S11292. DR HSSP; O44049; 1MZ5. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR013320; ConA_like_subgrp. DR InterPro; IPR002860; Glyco_hydro_BNR. DR InterPro; IPR011040; Neuramndase. DR InterPro; IPR008377; Sialidase_trypan. DR Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1. DR Pfam; PF02012; BNR; 2. DR PRINTS; PR01803; TCSIALIDASE. KW Glycosidase; Hydrolase; Repeat; Signal. FT SIGNAL 1 23 Potential. FT CHAIN 24 752 Sialidase 85-1.1. FT /FTId=PRO_0000012039. FT REPEAT 274 285 BNR 1. FT REPEAT 319 330 BNR 2. SQ SEQUENCE 752 AA; 80847 MW; BDC33F3EF2DC6859 CRC64; MSRRVFASAV LLLIVVTMCC GGAATAQVGS NADASTPGSA LTGAIAGEGS SSGGVEGLQR VDLFVPQKTQ VLPKKGPDSS RRDSFFSPSL VSAGGVIAAF AEGHINTKNP HNESAKPFSD VVAGYIDSAW EWPTLVEKVS ESTWQAHTVL GKAEGKKSLD VVLRPTTTTK GNKVFLLAGS TDLSYVNWSW REGSLELKLV VGDVTKPTSS EPTERIKWGE IKSLLNESTI AAQKGKLTEF LASGGSGVVM EDGTIVFSLM AVNEKKDGVF SLIIYSKDNG STWSLSEGIS PAKCGAPRIT EWEGSLLMIV DCENDQRVYV SRDMGTTWTE AIGTLSGVGS THNWETIGRR LAVEALITVT IEGRKVMLYT QRGYALGETE TTSPLYLWVT DNNRSFFVGP VGMDNAVKGE LAGALLYSDG GLHLLQRRDS GEDSVMSLSR LTEELKEIKS VLSTWSQKDV FFSSLSIPTV GLVAVLSDAA GDGRWYDEYL CLNATVTNAT KVKDGFQLTE PDSRAVWSVN IPDGNVRHIS LSHNFTLVAS VIIEEAPSGN TPLLTAVLVD AGPEYFMRLS YTADNKWMTM LKDEKKPTTE SRPWEAGKEH QVALMLQGNK ASVYVDGELL GEEEVPLTGE KPLEIFAFCF GACKIDGDEE ESSPKEIGKK PRVTVTNVFL YNRPLNSTEM RAIKDRIPVP TRAPEPQVKI APKPAAPAAP AGNEETARET GDGGANGDAV SAYGRVLLPL LFLLGLWGLA TA // ID 8512_TRYCR Reviewed; 240 AA. AC P18270; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 31-OCT-2006, entry version 38. DE Sialidase 85-1.2 (EC 3.2.1.18) (Neuraminidase) (NA) (Major 85 kDa DE surface antigen) (SA85-1.2 protein) (Fragment). GN Name=SA85-1.2; OS Trypanosoma cruzi. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma; OC Schizotrypanum. OX NCBI_TaxID=5693; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CL; RX MEDLINE=90324879; PubMed=1695668; DOI=10.1084/jem.172.2.589; RA Kahn S., van Voorhis W., Eisen H.; RT "The major 85-kD surface antigen of the mammalian form of Trypanosoma RT cruzi is encoded by a large heterogeneous family of simultaneously RT expressed genes."; RL J. Exp. Med. 172:589-597(1990). CC -!- FUNCTION: Developmentally regulated neuraminidase implicated in CC parasite invasion of cells. May contribute to the pathology during CC T.cruzi infection by cleaving sialic acid from cells of the immune CC system. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, CC alpha-(2->8)- glycosidic linkages of terminal sialic residues in CC oligosaccharides, glycoproteins, glycolipids, colominic acid and CC synthetic substrates. CC -!- DEVELOPMENTAL STAGE: Mammalian stage of parasite. CC -!- MISCELLANEOUS: The parasite mammalian stage surface antigen CC exhibits extensive antigenic diversity. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X53546; CAA37618.1; -; mRNA. DR PIR; S11293; S11293. DR HSSP; O44049; 1MZ5. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR008377; Sialidase_trypan. DR PRINTS; PR01803; TCSIALIDASE. KW Glycosidase; Hydrolase; Repeat. FT CHAIN <1 240 Sialidase 85-1.2. FT /FTId=PRO_0000208911. FT NON_TER 1 1 SQ SEQUENCE 240 AA; 26601 MW; 8B73A9F7EE19ED9C CRC64; EHSGDNVRHV FLNHNFTLVA SVTIEEAPSE KTPLLTALLG DAEPPYFMRL SYTADNKWET ISKGDKKLTT ESRPWVPKKE HQVALMLQGN KASVYIDGES LGEEAPLTVE TPLEPFGFCF GACDFDDDDD GGDDDDEEDS QEESSPKESS PEKIGKKPHV TVTNVFLYNR PLNPTEMRAI KDRIPVSTRA PEPQVKIAPK PVAPAAPGSL RCLAHGKYQQ HRGGQLWGEP PIPNMRQRDA // ID 8513_TRYCR Reviewed; 175 AA. AC P18271; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 28-NOV-2006, entry version 40. DE Sialidase 85-1.3 (EC 3.2.1.18) (Neuraminidase) (NA) (Major 85 kDa DE surface antigen) (SA85-1.3 protein) (Fragment). GN Name=SA85-1.3; OS Trypanosoma cruzi. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma; OC Schizotrypanum. OX NCBI_TaxID=5693; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CL; RX MEDLINE=90324879; PubMed=1695668; DOI=10.1084/jem.172.2.589; RA Kahn S., van Voorhis W., Eisen H.; RT "The major 85-kD surface antigen of the mammalian form of Trypanosoma RT cruzi is encoded by a large heterogeneous family of simultaneously RT expressed genes."; RL J. Exp. Med. 172:589-597(1990). CC -!- FUNCTION: Developmentally regulated neuraminidase implicated in CC parasite invasion of cells. May contribute to the pathology during CC T.cruzi infection by cleaving sialic acid from cells of the immune CC system. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, CC alpha-(2->8)- glycosidic linkages of terminal sialic residues in CC oligosaccharides, glycoproteins, glycolipids, colominic acid and CC synthetic substrates. CC -!- DEVELOPMENTAL STAGE: Mammalian stage of parasite. CC -!- MISCELLANEOUS: The parasite mammalian stage surface antigen CC exhibits extensive antigenic diversity. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X53547; CAA37619.1; -; mRNA. DR PIR; S11294; S11294. DR HSSP; Q26966; 1MR5. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR013320; ConA_like_subgrp. DR InterPro; IPR008377; Sialidase_trypan. DR Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1. DR PRINTS; PR01803; TCSIALIDASE. KW Glycosidase; Hydrolase; Repeat. FT CHAIN <1 175 Sialidase 85-1.3. FT /FTId=PRO_0000208912. FT NON_TER 1 1 SQ SEQUENCE 175 AA; 19552 MW; E90DD13274B75B8F CRC64; LCLNATVRNA TKVKDGFQLT EPDSGVMWPV NIPDYNKRHV FLNHNFTLVA SVTIEEAPSG NTPLLIAVLA NTEPTHTMRI LYTADNKWMT MLKDEKKPTT ESGTWEPKKE HQVALMLQGN KASVYVDGEL LGEEEVPLTG EKPLELFAFC FGACGEENPS QESHVTVTNV FLYNR // ID 88KD_BACCE Reviewed; 5 AA. AC P83073; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 23-JAN-2007, entry version 12. DE 88 kDa protein (Fragment). OS Bacillus cereus. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1396; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=NCIMB 11796 / DSM 626; RX PubMed=11872115; DOI=10.1046/j.1365-2672.2002.01541.x; RA Browne N., Dowds B.C.A.; RT "Acid stress in the food pathogen Bacillus cereus."; RL J. Appl. Microbiol. 92:404-414(2002). CC -!- MISCELLANEOUS: Under acid-stress, this protein is expressed at a CC higher level in wild type B.cereus than in the acid-sensitive CC mutant strain NB1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Direct protein sequencing. FT CHAIN 1 >5 88 kDa protein. FT /FTId=PRO_0000270971. FT NON_TER 5 5 SQ SEQUENCE 5 AA; 623 MW; 6B01AAA336F00000 CRC64; MKDTE // ID 8ODP_HUMAN Reviewed; 197 AA. AC P36639; Q6P0Y6; Q9UBM0; Q9UBM9; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2002, sequence version 2. DT 20-FEB-2007, entry version 66. DE 7,8-dihydro-8-oxoguanine triphosphatase (EC 3.1.6.-) (8-oxo-dGTPase) DE (Nucleoside diphosphate-linked moiety X motif 1) (Nudix motif 1). GN Name=NUDT1; Synonyms=MTH1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), AND PARTIAL PROTEIN RP SEQUENCE. RX MEDLINE=94043152; PubMed=8226881; RA Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., RA Sekiguchi M.; RT "Cloning and expression of cDNA for a human enzyme that hydrolyzes 8- RT oxo-dGTP, a mutagenic substrate for DNA synthesis."; RL J. Biol. Chem. 268:23524-23530(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95229148; PubMed=7713500; RA Furuichi M., Yoshida M.C., Oda H., Tajiri T., Nakabeppu Y., RA Tsuzuki T., Sekiguchi M.; RT "Genomic structure and chromosome location of the human mutT homologue RT gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G RT transversion."; RL Genomics 24:485-490(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX MEDLINE=97362283; PubMed=9211940; DOI=10.1074/jbc.272.28.17843; RA Oda H., Nakabeppu Y., Furuichi M., Sekiguchi M.; RT "Regulation of expression of the human MTH1 gene encoding 8-oxo- RT dGTPase. Alternative splicing of transcription products."; RL J. Biol. Chem. 272:17843-17850(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE INITIATION, AND VARIANT RP VAL-124. RX MEDLINE=20007875; PubMed=10536140; DOI=10.1093/nar/27.22.4335; RA Oda H., Taketomi A., Maruyama R., Itoh R., Nishioka K., Yakushiji H., RA Suzuki T., Sekiguchi M., Nakabeppu Y.; RT "Multi-forms of human MTH1 polypeptides produced by alternative RT translation initiation and single nucleotide polymorphism."; RL Nucleic Acids Res. 27:4335-4343(1999). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-124. RA Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., RA Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., RA Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., RA Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.; RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P22), AND VARIANT RP VAL-124. RC TISSUE=Lymph, and Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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: Antimutagenic. Responsible for preventing CC misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G CC transversions. CC -!- CATALYTIC ACTIVITY: 8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=4; CC Name=p26; CC IsoId=P36639-1; Sequence=Displayed; CC Note=Derived from a B-type mRNA with a polymorphic alteration CC (GU-->GC) at the beginning of exon 2c that converts an in-frame CC UGA to CGA yielding another in-frame AUG further upstream; CC Name=p22; CC IsoId=P36639-2; Sequence=VSP_018812; CC Name=p21; CC IsoId=P36639-3; Sequence=VSP_018813; CC Name=p18; CC IsoId=P36639-4; Sequence=VSP_018814; CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in CC thymus, testis, embryo and proliferating blood lymphocytes. CC -!- DEVELOPMENTAL STAGE: In peripheral blood lymphocytes, expressed at CC much higher levels in proliferating cells than in resting cells. CC -!- PTM: The N-terminus is blocked. CC -!- POLYMORPHISM: A polymorphism between Met-1 and Met-19 removes a CC stop codon before the initiation codon for isoform p22 and gives CC rise to the production of isoform p26. The allele frequency of CC isoform p26 is about 20%. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D16581; BAA04013.1; -; mRNA. DR EMBL; D38594; BAA07601.1; -; Genomic_DNA. DR EMBL; AB025233; BAA83791.1; -; mRNA. DR EMBL; AB025234; BAA83792.1; -; mRNA. DR EMBL; AB025235; BAA83793.1; -; mRNA. DR EMBL; AB025236; BAA83794.1; -; mRNA. DR EMBL; AB025237; BAA83795.1; -; mRNA. DR EMBL; AB025238; BAA83796.1; -; mRNA. DR EMBL; AB025239; BAA83797.1; -; mRNA. DR EMBL; AB025240; BAA83798.1; -; mRNA. DR EMBL; AB025241; BAA83799.1; -; mRNA. DR EMBL; AB025242; BAA83800.1; -; mRNA. DR EMBL; DQ230907; ABB02181.1; -; Genomic_DNA. DR EMBL; BC014618; AAH14618.1; -; mRNA. DR EMBL; BC065367; AAH65367.1; -; mRNA. DR UniGene; Hs.534331; -. DR PDB; 1IRY; NMR; A=42-197. DR Ensembl; ENSG00000106268; Homo sapiens. DR KEGG; hsa:4521; -. DR H-InvDB; HIX0006427; -. DR HGNC; HGNC:8048; NUDT1. DR MIM; 600312; gene. DR ArrayExpress; P36639; -. DR GermOnline; ENSG00000106268; Homo sapiens. DR RZPD-ProtExp; I0269; -. DR RZPD-ProtExp; IOH40684; -. DR RZPD-ProtExp; IOH45904; -. DR RZPD-ProtExp; RZPDo834F026; -. DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc. DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc. DR InterPro; IPR003563; 8Ox_triPHTase. DR InterPro; IPR000086; NUDIX_hydrolase. DR Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR01403; 8OXTPHPHTASE. DR PRINTS; PR00502; NUDIXFAMILY. DR PROSITE; PS00893; NUDIX; 1. KW 3D-structure; Alternative initiation; Direct protein sequencing; KW Hydrolase; Polymorphism. FT CHAIN 1 197 7,8-dihydro-8-oxoguanine triphosphatase. FT /FTId=PRO_0000019944. FT MOTIF 78 99 Nudix box. FT VAR_SEQ 1 41 Missing (in isoform p18). FT /FTId=VSP_018814. FT VAR_SEQ 1 26 Missing (in isoform p21). FT /FTId=VSP_018813. FT VAR_SEQ 1 18 Missing (in isoform p22). FT /FTId=VSP_018812. FT VARIANT 124 124 M -> V (in dbSNP:rs4866). FT /FTId=VAR_013757. FT STRAND 46 51 FT STRAND 56 70 FT TURN 71 71 FT TURN 82 83 FT HELIX 86 98 FT STRAND 107 115 FT TURN 116 117 FT STRAND 121 127 FT STRAND 140 148 FT TURN 149 150 FT TURN 155 157 FT HELIX 161 170 FT TURN 171 171 FT STRAND 173 184 FT STRAND 186 194 SQ SEQUENCE 197 AA; 22552 MW; 82B25F56D382CE57 CRC64; MYWSNQITRR LGERVQGFMS GISPQQMGEP EGSWSGKNPG TMGASRLYTL VLVLQPQRVL LGMKKRGFGA GRWNGFGGKV QEGETIEDGA RRELQEESGL TVDALHKVGQ IVFEFVGEPE LMDMHVFCTD SIQGTPVESD EMRPCWFQLD QIPFKDMWPD DSYWFPLLLQ KKKFHGYFKF QGQDTILDYT LREVDTV // ID 8ODP_MOUSE Reviewed; 156 AA. AC P53368; P97795; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 06-FEB-2007, entry version 47. DE 7,8-dihydro-8-oxoguanine triphosphatase (EC 3.1.6.-) (8-oxo-dGTPase) DE (Nucleoside diphosphate-linked moiety X motif 1) (Nudix motif 1). GN Name=Nudt1; Synonyms=Mth1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/Sv; RX MEDLINE=96029697; PubMed=7592783; DOI=10.1074/jbc.270.43.25942; RA Kakuma T., Nishida J., Tsuzuki T., Sekiguchi M.; RT "Mouse MTH1 protein with 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'- RT triphosphatase activity that prevents transversion mutation. cDNA RT cloning and tissue distribution."; RL J. Biol. Chem. 270:25942-25948(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; RX MEDLINE=97166235; PubMed=9013634; DOI=10.1074/jbc.272.6.3766; RA Igarashi H., Tsuzuki T., Kakuma T., Tominaga Y., Sekiguchi M.; RT "Organization and expression of the mouse MTH1 gene for preventing RT transversion mutation."; RL J. Biol. Chem. 272:3766-3772(1997). CC -!- FUNCTION: Antimutagenic. Responsible for preventing CC misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G CC transversions. CC -!- CATALYTIC ACTIVITY: 8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D49956; BAA08711.1; -; mRNA. DR EMBL; D88356; BAA19866.1; -; Genomic_DNA. DR PIR; I49446; I49446. DR UniGene; Mm.118846; -. DR SMR; P53368; 1-155. DR Ensembl; ENSMUSG00000036639; Mus musculus. DR KEGG; mmu:17766; -. DR MGI; MGI:109280; Nudt1. DR ArrayExpress; P53368; -. DR GermOnline; ENSMUSG00000036639; Mus musculus. DR RZPD-ProtExp; IOM14971; -. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanine triphosphatase act...; IDA:MGI. DR GO; GO:0006203; P:dGTP catabolic process; IDA:MGI. DR InterPro; IPR003563; 8Ox_triPHTase. DR InterPro; IPR000086; NUDIX_hydrolase. DR Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR01403; 8OXTPHPHTASE. DR PRINTS; PR00502; NUDIXFAMILY. DR PROSITE; PS00893; NUDIX; 1. KW Hydrolase. FT CHAIN 1 156 7,8-dihydro-8-oxoguanine triphosphatase. FT /FTId=PRO_0000057100. FT MOTIF 37 58 Nudix box. SQ SEQUENCE 156 AA; 17908 MW; 9E6C12EC2A6DE4B7 CRC64; MSTSRLYTLV LVLQPQRVLL GMKKRGFGAG RWNGFGGKVQ EGETIEDGAK RELLEESGLS VDTLHKVGHI SFEFVGSPEL MDVHIFSADH VHGTPTESEE MRPQWFQLDQ IPFADLWPDD SYWFPLLLQK KKFCGHFKFQ DQDTILSYSL REVDSF // ID 8ODP_RAT Reviewed; 156 AA. AC P53369; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-FEB-2007, entry version 38. DE 7,8-dihydro-8-oxoguanine triphosphatase (EC 3.1.6.-) (8-oxo-dGTPase) DE (Nucleoside diphosphate-linked moiety X motif 1) (Nudix motif 1). GN Name=Nudt1; Synonyms=Mth1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=Donryu; TISSUE=Spleen; RX MEDLINE=96033912; PubMed=7586133; DOI=10.1093/carcin/16.10.2343; RA Cai J.P., Kakuma T., Tsuzuki T., Sekiguchi M.; RT "cDNA and genomic sequences for rat 8-oxo-dGTPase that prevents RT occurrence of spontaneous mutations due to oxidation of guanine RT nucleotides."; RL Carcinogenesis 16:2343-2350(1995). CC -!- FUNCTION: Antimutagenic. Responsible for preventing CC misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G CC transversions. CC -!- CATALYTIC ACTIVITY: 8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D49977; BAA08726.1; -; mRNA. DR EMBL; D49980; BAA08727.1; -; Genomic_DNA. DR UniGene; Rn.10669; -. DR SMR; P53369; 1-154. DR Ensembl; ENSRNOG00000001260; Rattus norvegicus. DR KEGG; rno:117260; -. DR RGD; 621080; Nudt1. DR ArrayExpress; P53369; -. DR GermOnline; ENSRNOG00000001260; Rattus norvegicus. DR InterPro; IPR003563; 8Ox_triPHTase. DR InterPro; IPR000086; NUDIX_hydrolase. DR Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR01403; 8OXTPHPHTASE. DR PRINTS; PR00502; NUDIXFAMILY. DR PROSITE; PS00893; NUDIX; 1. KW Hydrolase. FT CHAIN 1 156 7,8-dihydro-8-oxoguanine triphosphatase. FT /FTId=PRO_0000057101. FT MOTIF 37 58 Nudix box. SQ SEQUENCE 156 AA; 18018 MW; 60AFB6522CB03E18 CRC64; MSTSRLYTLV LVLQPQRVLL GMKKRGFGAG RWNGFGGKVQ EGETIEDGAK RELLEESGLR VDTLHKVGHI SFEFVGSPEL MDVHIFSTDH VHGTPTESEE MRPQWFQLDQ IPFADMWPDD SYWFPLLLQK KKFCGHFKFH GQDTILSYSL REVDEF // ID 92KD_BACCE Reviewed; 10 AA. AC P83062; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 23-JAN-2007, entry version 13. DE 92 kDa protein (Fragment). OS Bacillus cereus. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1396; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=NCIMB 11796 / DSM 626; RX PubMed=11872115; DOI=10.1046/j.1365-2672.2002.01541.x; RA Browne N., Dowds B.C.A.; RT "Acid stress in the food pathogen Bacillus cereus."; RL J. Appl. Microbiol. 92:404-414(2002). CC -!- MISCELLANEOUS: Under acid-stress, this protein is expressed at a CC higher level in wild type B.cereus than in the acid-sensitive CC mutant strain NB1. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Direct protein sequencing. FT CHAIN 1 >10 92 kDa protein. FT /FTId=PRO_0000270972. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1045 MW; 36E840B73AEB0777 CRC64; AHPPEXLSIA // ID 9GL_ASFB7 Reviewed; 119 AA. AC Q65163; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 31-OCT-2006, entry version 25. DE Late protein 9GL. GN Name=9GL; ORFNames=B119L; OS African swine fever virus (strain BA71V) (ASFV). OC Viruses; dsDNA viruses, no RNA stage; Asfarviridae; Asfivirus. OX NCBI_TaxID=10498; OH NCBI_TaxID=265619; Ornithodoros erraticus. OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog). OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21820291; PubMed=11831707; RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C., RA Rodriguez J.F., Vinuela E.; RT "Analysis of the complete nucleotide sequence of African swine fever RT virus."; RL Virology 208:249-278(1995). RN [2] RP FUNCTION IN VIRULENCE. RX MEDLINE=20094914; PubMed=10627538; RX DOI=10.1128/JVI.74.3.1275-1285.2000; RA Lewis T., Zsak L., Burrage T.G., Lu Z., Kutish G.F., Neilan J.G., RA Rock D.L.; RT "An African swine fever virus ERV1-ALR homologue, 9GL, affects virion RT maturation and viral growth in macrophages and viral virulence in RT swine."; RL J. Virol. 74:1275-1285(2000). CC -!- SIMILARITY: Belongs to the ERV1/ALR family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U18466; AAA65303.1; -; Genomic_DNA. DR InterPro; IPR006863; Evr1_Alr. DR Pfam; PF04777; Evr1_Alr; 1. KW Virulence. FT CHAIN 1 119 Late protein 9GL. FT /FTId=PRO_0000208551. SQ SEQUENCE 119 AA; 14378 MW; A1EE2F073ABF9726 CRC64; MLHWGPKYWR SLHLYAIFFS DAPSWKEKYE AIQWILNFIE SLPCTRCQHH AFSYLTKNPL TLNNSEDFQY WTFAFHNNVN NRLNKKIISW SEYKNIYEQS ILKTIEYGKT DFIGAWSSL // ID 9KD_HUMAN Reviewed; 82 AA. AC P13994; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 20-FEB-2007, entry version 37. DE 9 kDa protein. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Fibroblast; RX MEDLINE=89078418; PubMed=3203696; RA Lammers R., Gross G., Mayr U., Collins J.; RT "Alternative mechanisms for gene activation induced by RT poly(rI).poly(rC) and Newcastle disease virus."; RL Eur. J. Biochem. 178:93-99(1988). CC -!- INDUCTION: By poly(RI), poly(RC) and Newcastle disease virus. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X13956; CAA32138.1; -; Genomic_DNA. DR PIR; S02660; S02660. DR UniGene; Hs.24998; -. DR Ensembl; ENSG00000104957; Homo sapiens. DR ArrayExpress; P13994; -. DR GermOnline; ENSG00000104957; Homo sapiens. DR RZPD-ProtExp; I0520; -. DR RZPD-ProtExp; IOH5688; -. DR RZPD-ProtExp; V0478; -. DR GO; GO:0009615; P:response to virus; IEP:UniProtKB. FT CHAIN 1 82 9 kDa protein. FT /FTId=PRO_0000064401. SQ SEQUENCE 82 AA; 8594 MW; 9B4A15552A489652 CRC64; MEPPSPSPTH LSCIFFLLIT VSPLEASSTR ARVFPCLPLY AECPEQSLAQ GKEKSHPGGG GERPGLAGQG EPDHPAGARD GR // ID A103_SCHMA Reviewed; 263 AA. AC P13492; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 31-OCT-2006, entry version 43. DE Antigen 10-3 precursor. OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida; OC Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC STRAIN=Puerto Rican; RX MEDLINE=89096846; PubMed=3211127; RA Davis R.E., Davis A.H., Carroll S.M., Rajkovic A., Rottman F.M.; RT "Tandemly repeated exons encode 81-base repeats in multiple, RT developmentally regulated Schistosoma mansoni transcripts."; RL Mol. Cell. Biol. 8:4745-4755(1988). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist; CC Name=1; CC IsoId=P13492-1; Sequence=Displayed; CC Name=2; CC IsoId=P13492-2; Sequence=VSP_004087; CC -!- DEVELOPMENTAL STAGE: Different-sized isoforms are expressed in the CC adult and cercarial stages. CC -!- MISCELLANEOUS: This antigen is recognized by sera from infected CC human. CC -!- MISCELLANEOUS: Isoforms are highly similar and contain variable CC numbers of identical direct tandem repeats of 81 bases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M22346; AAA29855.1; -; mRNA. DR PIR; A31561; A31561. KW Alternative splicing; Glycoprotein; Repeat; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 263 Antigen 10-3. FT /FTId=PRO_0000020578. FT REPEAT 81 107 1. FT REPEAT 108 134 2. FT REPEAT 135 161 3. FT REPEAT 162 188 4. FT REPEAT 189 206 5. FT REGION 81 189 5 X 27 AA tandem repeats. FT CARBOHYD 23 23 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 61 70 Missing (in isoform 2). FT /FTId=VSP_004087. SQ SEQUENCE 263 AA; 29641 MW; A33A70AA1E23E74E CRC64; MNIYLIGILC IVGLIISQGS TANGSPLDDR FNDVNTINKK QFTEEEFSRL INSMLKKYIE DKNVDIRIIG NKKDKQPTQK TTPKPTTPKQ INDGTSDKTS DTHTIKRTTP KPTTPKQIND GTSDKTSDTH TIKRTTPKPT TPKQINDGTS DKTSDTHTIK RTTPKPTTPK QINDGTSDKT SDTHTIKRTT PKPTTPKQIN DGTSDKPKSI ADIFLINKPK VPLWIVNPLY YMVEKFVQIM GYLLEDDDTL ELNLPKYYYD KSI // ID A10A5_SOYBN Reviewed; 93 AA. AC P33079; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 31-OCT-2006, entry version 24. DE Auxin-induced protein 10A5. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Wayne; RX MEDLINE=92404712; PubMed=2485235; DOI=10.1105/tpc.1.2.229; RA McClure B.A., Hagen G., Brown C.S., Gee M.A., Guilfoyle T.J.; RT "Transcription, organization, and sequence of an auxin-regulated gene RT cluster in soybean."; RL Plant Cell 1:229-239(1989). CC -!- INDUCTION: By auxin. CC -!- SIMILARITY: Belongs to the ARG7 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S44177; AAB23283.1; -; Genomic_DNA. DR PIR; JQ1100; JQ1100. DR InterPro; IPR003676; Auxin_inducible. DR Pfam; PF02519; Auxin_inducible; 1. KW Auxin signaling pathway. FT CHAIN 1 93 Auxin-induced protein 10A5. FT /FTId=PRO_0000064402. SQ SEQUENCE 93 AA; 10535 MW; 4CF422C352F64662 CRC64; MGFRIAGIVR RTSFYTTQAA SKRVDVPKGY AAVYVGDKMR RFTIPVSYLN EPSFQELLSQ AEEEFGYDHP MGGLTIPCKE EEFLNVTAHL NEL // ID A115_TOBAC Reviewed; 307 AA. AC P40691; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 28-NOV-2006, entry version 36. DE Auxin-induced protein PCNT115. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. White Burley; RA van der Zaal E.J.; RL Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases. CC -!- INDUCTION: By auxin. CC -!- SIMILARITY: Belongs to the aldo/keto reductase 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; X56267; CAA39708.1; -; mRNA. DR PIR; S16390; S16390. DR HSSP; P38918; 1GVE. DR InterPro; IPR001395; Aldo/ket_red. DR Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR ProDom; PD000288; Aldo/ket_red; 1. KW Auxin signaling pathway; NADP; Oxidoreductase. FT CHAIN 1 307 Auxin-induced protein PCNT115. FT /FTId=PRO_0000070380. FT NP_BIND 215 225 NADP (By similarity). FT ACT_SITE 64 64 Proton donor (By similarity). FT BINDING 136 136 Substrate (By similarity). FT SITE 90 90 Lowers pKa of active site Tyr (By FT similarity). SQ SEQUENCE 307 AA; 33857 MW; C4417DA852613360 CRC64; MAKEGTKVPR IKLGSQGLEV SAQGLGCMGM SAFYGPPKPE PDMIQLIHHA INSGITLLDT SDVYGPHTNE ILLGKALKGG TRERVVLATK FGIVLGDEKK AEGKRAVHGD PAYVRAACEA SLKRLDIDCI DLYYQHRVDT RVPIEITVGE LKKLVEEGKL KYIGLSEASA STIRRAHAVH PITAVQLEWS LWSRDVEEEI IPTCRELGIG IVAYSPLGRG FLSSGPKLLE DMSNEDYRKY LPRFQAENLE NNKNLYERIC EMAVRKGCTP SQLALAWVHH QGNDVCPIPG TTKIENLNQN MKPCPSS // ID A13CA_XENLA Reviewed; 510 AA. AC Q6NRD0; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 20-FEB-2007, entry version 18. DE Ankyrin repeat domain-containing protein 13C-A. GN Name=ankrd13c-A; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Egg; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains 3 ANK 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; BC070826; AAH70826.1; -; mRNA. DR UniGene; Xl.5359; -. DR InterPro; IPR002110; ANK. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. DR Pfam; PF00023; Ank; 2. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 2. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. KW ANK repeat; Repeat. FT CHAIN 1 510 Ankyrin repeat domain-containing protein FT 13C-A. FT /FTId=PRO_0000240648. FT REPEAT 80 111 ANK 1. FT REPEAT 112 141 ANK 2. FT REPEAT 145 174 ANK 3. FT COMPBIAS 383 386 Poly-Pro. SQ SEQUENCE 510 AA; 58219 MW; 06E820DD5CABD9A9 CRC64; MTGEKIRSLH KDQKPSKDED LLEPDEEATA GGTFTRTGKL KSSKMFSNHK VIRSPSNPAL LQNHHHQQIS PITPGESKSD VYFPVHECVL KGDIRRLSSL IRSHSIGQKD SHGNTPLHLA VMLGNKECAH LLLAHNAPVK VKNAQGWSPL AEAISYGDRQ MITALLRKLK QQSRESVEEK RPRLLKALKE LGDFYLELHW DFQSWVPLLS RILPSDACKI YKQGINIRLD TTLIDFTDMK CQRGDLSFIF NGDAAPSESF VVLDNEQKVY QRIHHEESEM ETEEEVDILM SSDIYSATLS TKSITFTRAQ TGWLFREDKT ERVGNFLADF YLVNGLILES RKRREHLTEE DILRNKAIME SLSKGGNLME QNFEPVRRQS LTPPPPNTIT WEEYISAENG KAPHLGRELV CKENKKTFKA TIAMSQDFPL GIESLLNVLE VIAPFKHFNK LREFVQMKLP PGFPVKLDIP VFPTITATVT FQEFRYGEFE DAIFTIPDDY KEDPSRFPDL // ID A13CB_XENLA Reviewed; 513 AA. AC Q7ZYD9; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 20-FEB-2007, entry version 21. DE Ankyrin repeat domain-containing protein 13C-B. GN Name=ankrd13c-B; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains 3 ANK 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; BC043828; AAH43828.1; -; mRNA. DR UniGene; Xl.61088; -. DR InterPro; IPR002110; ANK. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. DR Pfam; PF00023; Ank; 2. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 2. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. KW ANK repeat; Repeat. FT CHAIN 1 513 Ankyrin repeat domain-containing protein FT 13C-B. FT /FTId=PRO_0000240649. FT REPEAT 83 114 ANK 1. FT REPEAT 115 144 ANK 2. FT REPEAT 148 177 ANK 3. FT COMPBIAS 64 68 Poly-His. FT COMPBIAS 386 389 Poly-Pro. SQ SEQUENCE 513 AA; 58779 MW; 7CEC5B3D5032FF75 CRC64; MTGEKIRSLH RDQKPSKDED LLEPDEEATA DGTFTRTSKL KSSKMFSNHK VIRSPSNPAL LQNHHHHHQQ QISPMTPGES KTDVYFPVHE CVIKGDIRKL SSLIRSHNIG QKDNHGNTPL HLAVMLGNKE CAHLLLAHNA PVKVKNAQGW SPLAEAISYG DRQMITALLR KLKQQSRESV EEKRPRLLKA LKELGDFYLE LHWDFQSWVP LLSRILPSDA CKIYKQGINI RLDTTLIDFT DMKCQRGDLS FIFNGDAAPS ESFVVLDNEQ KVYQRIHHEE SEMETEEEVD ILMSSDIYSA TLSTKSITFS RAQTGWLFRE DKTERVGNFL ADFYTVNGLI LESRKRREHL TEEDILRNKA IMESLSKGGN LMEQTFEPVR RPSLTPPPPN TITWEEYISA ENGKAPHLGR ELVCKENKKT FKATIAMSQD FPLEIESLLN VLEVIAPFKH FNKLREFVQM KLPPGFPVKL DIPVFPTITA TVTFQEFHYG EFEDAIFTIP DDYKEDPSRF PDL // ID A16L1_HUMAN Reviewed; 607 AA. AC Q676U5; Q6IPN1; Q6UXW4; Q6ZVZ5; Q8NCY2; Q96JV5; Q9H619; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 2. DT 20-FEB-2007, entry version 35. DE Autophagy-related protein 16-1 (APG16-like 1). GN Name=ATG16L1; Synonyms=APG16L; ORFNames=UNQ9393/PRO34307; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-300. RC TISSUE=Fetal brain; RX PubMed=15620219; DOI=10.1080/10425170400004104; RA Zheng H., Ji C., Li J., Jiang H., Ren M., Lu Q., Gu S., Mao Y., RA Xie Y.; RT "Cloning and analysis of human Apg16L."; RL DNA Seq. 15:303-305(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX MEDLINE=22887296; PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-607 (ISOFORM 2). RC TISSUE=Brain, Placenta, and Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-607 (ISOFORM 2). 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 513-607. RC TISSUE=Testis; RG The German cDNA consortium; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays an essential role in autophagy (By similarity). CC -!- SUBUNIT: Homooligomer. Interacts with ATG5. Part of either the CC minor and major complexes respectively composed of 4 sets of CC ATG12-ATG5 and ATG16L1 (400 kDa) or 8 sets of ATG12-ATG5 and CC ATG16L1 (800 kDa) (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Preautophagosomal CC structure; preautophagosomal structure membrane; peripheral CC membrane protein (By similarity). Note=Localized to CC preautophagosomal structure (PAS) where it is involved in the CC membrane targeting of ATG5 (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=APG16L beta; CC IsoId=Q676U5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q676U5-2; Sequence=VSP_013386; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q676U5-3; Sequence=VSP_013387, VSP_013388; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q676U5-4; Sequence=VSP_013389, VSP_013390; CC Note=No experimental confirmation available; CC Name=5; CC IsoId=Q676U5-5; Sequence=VSP_013384, VSP_013385; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the WD repeat ATG16 family. CC -!- SIMILARITY: Contains 7 WD 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; AY398617; AAR32130.1; -; mRNA. DR EMBL; AY358182; AAQ88549.1; -; mRNA. DR EMBL; AK026330; BAB15448.1; -; mRNA. DR EMBL; AK027854; BAB55412.1; ALT_INIT; mRNA. DR EMBL; AK123876; BAC85713.1; -; mRNA. DR EMBL; BC071846; AAH71846.1; -; mRNA. DR EMBL; AL834526; CAD39182.1; -; mRNA. DR UniGene; Hs.529322; -. DR HSSP; P16649; 1ERJ. DR Ensembl; ENSG00000085978; Homo sapiens. DR KEGG; hsa:55054; -. DR HGNC; HGNC:21498; ATG16L1. DR ArrayExpress; Q676U5; -. DR GermOnline; ENSG00000085978; Homo sapiens. DR RZPD-ProtExp; IOH37886; -. DR RZPD-ProtExp; IOH42393; -. DR RZPD-ProtExp; IOH43648; -. DR RZPD-ProtExp; T3380; -. DR RZPD-ProtExp; V0897; -. DR InterPro; IPR013923; APG16. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 2. DR SMART; SM00320; WD40; 7. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Alternative splicing; Autophagy; Coiled coil; Membrane; Polymorphism; KW Protein transport; Repeat; Transport; WD repeat. FT CHAIN 1 607 Autophagy-related protein 16-1. FT /FTId=PRO_0000050848. FT REPEAT 320 359 WD 1. FT REPEAT 364 403 WD 2. FT REPEAT 406 445 WD 3. FT REPEAT 447 484 WD 4. FT REPEAT 486 525 WD 5. FT REPEAT 532 573 WD 6. FT REPEAT 575 607 WD 7. FT COILED 78 230 Potential. FT VAR_SEQ 1 434 Missing (in isoform 5). FT /FTId=VSP_013384. FT VAR_SEQ 70 213 Missing (in isoform 4). FT /FTId=VSP_013389. FT VAR_SEQ 266 284 Missing (in isoform 2). FT /FTId=VSP_013386. FT VAR_SEQ 334 368 Missing (in isoform 4). FT /FTId=VSP_013390. FT VAR_SEQ 435 442 WDLRSKVC -> MMFAFLSG (in isoform 5). FT /FTId=VSP_013385. FT VAR_SEQ 443 470 IKTVFAGSSCNDIVCTEQCVMSGHFDKK -> EEIQSLCLC FT ICLDVSVEVCVCTSEPAFM (in isoform 3). FT /FTId=VSP_013387. FT VAR_SEQ 471 607 Missing (in isoform 3). FT /FTId=VSP_013388. FT VARIANT 300 300 T -> A (in dbSNP:rs2241880). FT /FTId=VAR_021834. FT CONFLICT 151 151 K -> R (in Ref. 3; BAB55412). FT CONFLICT 328 328 V -> A (in Ref. 3; BAB55412). FT CONFLICT 529 529 P -> T (in Ref. 3; BAB55412). SQ SEQUENCE 607 AA; 68265 MW; 5A5816AE2CF03CA0 CRC64; MSSGLRAADF PRWKRHISEQ LRRRDRLQRQ AFEEIILQYN KLLEKSDLHS VLAQKLQAEK HDVPNRHEIS PGHDGTWNDN QLQEMAQLRI KHQEELTELH KKRGELAQLV IDLNNQMQRK DREMQMNEAK IAECLQTISD LETECLDLRT KLCDLERANQ TLKDEYDALQ ITFTALEGKL RKTTEENQEL VTRWMAEKAQ EANRLNAENE KDSRRRQARL QKELAEAAKE PLPVEQDDDI EVIVDETSDH TEETSPVRAI SRAATKRLSQ PAGGLLDSIT NIFGRRSVSS FPVPQDNVDT HPGSGKEVRV PATALCVFDA HDGEVNAVQF SPGSRLLATG GMDRRVKLWE VFGEKCEFKG SLSGSNAGIT SIEFDSAGSY LLAASNDFAS RIWTVDDYRL RHTLTGHSGK VLSAKFLLDN ARIVSGSHDR TLKLWDLRSK VCIKTVFAGS SCNDIVCTEQ CVMSGHFDKK IRFWDIRSES IVREMELLGK ITALDLNPER TELLSCSRDD LLKVIDLRTN AIKQTFSAPG FKCGSDWTRV VFSPDGSYVA AGSAEGSLYI WSVLTGKVEK VLSKQHSSSI NAVAWSPSGS HVVSVDKGCK AVLWAQY // ID A16L1_MOUSE Reviewed; 607 AA. AC Q8C0J2; Q6KAT7; Q80U97; Q80U98; Q80U99; Q80Y53; Q9DB63; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 23-JAN-2007, entry version 34. DE Autophagy-related protein 16-1 (APG16-like 1). GN Name=Atg16l1; Synonyms=Apg16l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE RP SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG5. RX MEDLINE=22552481; PubMed=12665549; DOI=10.1242/jcs.00381; RA Mizushima N., Kuma A., Kobayashi Y., Yamamoto A., Matsubae M., RA Takao T., Natsume T., Ohsumi Y., Yoshimori T.; RT "Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic RT isolation membrane with the Apg12-Apg5 conjugate."; RL J. Cell Sci. 116:1679-1688(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC STRAIN=C57BL/6J; TISSUE=Cerebellum, 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 5). RC TISSUE=Fetal brain; 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 [4] 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). CC -!- FUNCTION: Plays an essential role in autophagy. CC -!- SUBUNIT: Homooligomer. Interacts with ATG5. Part of either the CC minor and major complexes respectively composed of 4 sets of CC ATG12-ATG5 and ATG16L1 (400 kDa) or 8 sets of ATG12-ATG5 and CC ATG16L1 (800 kDa). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure; CC preautophagosomal structure membrane; peripheral membrane protein. CC Note=Localized to preautophagosomal structure (PAS) where it is CC involved in the membrane targeting of ATG5. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=Apg16Lbeta; CC IsoId=Q8C0J2-1; Sequence=Displayed; CC Name=2; Synonyms=Apg16Lalpha; CC IsoId=Q8C0J2-2; Sequence=VSP_013391; CC Note=No experimental confirmation available; CC Name=3; Synonyms=Apg16Lgamma; CC IsoId=Q8C0J2-3; Sequence=VSP_013392; CC Name=4; CC IsoId=Q8C0J2-4; Sequence=VSP_013392, VSP_013394, VSP_013395; CC Note=No experimental confirmation available; CC Name=5; CC IsoId=Q8C0J2-5; Sequence=VSP_013391, VSP_013393; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. In the liver, isoform 2 is CC highly expressed and isoform 1 is weakly expressed. Isoform 3 is CC expressed in the brain. CC -!- SIMILARITY: Belongs to the WD repeat ATG16 family. CC -!- SIMILARITY: Contains 7 WD 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; AB087879; BAC55090.1; -; mRNA. DR EMBL; AB087880; BAC55091.1; -; mRNA. DR EMBL; AB087881; BAC55092.1; -; mRNA. DR EMBL; AK005181; BAB23866.1; -; mRNA. DR EMBL; AK030983; BAC27201.1; -; mRNA. DR EMBL; AK131120; BAD21370.1; ALT_INIT; Other_RNA. DR EMBL; BC049122; AAH49122.1; -; mRNA. DR UniGene; Mm.272972; -. DR HSSP; P16649; 1ERJ. DR IntAct; Q8C0J2; -. DR Ensembl; ENSMUSG00000026289; Mus musculus. DR MGI; MGI:1924290; Atg16l1. DR ArrayExpress; Q8C0J2; -. DR GermOnline; ENSMUSG00000026289; Mus musculus. DR GO; GO:0005776; C:autophagic vacuole; IDA:MGI. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR GO; GO:0000045; P:autophagic vacuole formation; TAS:MGI. DR InterPro; IPR013923; APG16. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 2. DR SMART; SM00320; WD40; 7. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Alternative splicing; Autophagy; Coiled coil; Membrane; KW Protein transport; Repeat; Transport; WD repeat. FT CHAIN 1 607 Autophagy-related protein 16-1. FT /FTId=PRO_0000050849. FT REPEAT 320 359 WD 1. FT REPEAT 364 403 WD 2. FT REPEAT 406 445 WD 3. FT REPEAT 447 484 WD 4. FT REPEAT 486 525 WD 5. FT REPEAT 532 573 WD 6. FT REPEAT 575 607 WD 7. FT COILED 79 230 Potential. FT VAR_SEQ 266 284 Missing (in isoform 2 and isoform 5). FT /FTId=VSP_013391. FT VAR_SEQ 284 284 G -> GLSESPLLGHHSSDAAR (in isoform 3 and FT isoform 4). FT /FTId=VSP_013392. FT VAR_SEQ 442 442 C -> CEEMQSLCVLMVFGFLSG (in isoform 5). FT /FTId=VSP_013393. FT VAR_SEQ 443 452 IKTVFAGSSC -> EEMQSLCVFM (in isoform 4). FT /FTId=VSP_013394. FT VAR_SEQ 453 607 Missing (in isoform 4). FT /FTId=VSP_013395. FT CONFLICT 83 83 Q -> H (in Ref. 1 and 2; BAB23866). SQ SEQUENCE 607 AA; 68172 MW; 63920320883A69DF CRC64; MSSGLRAADF PRWKRHIAEE LRRRDRLQRQ AFEEIILQYT KLLEKSDLHS VLTQKLQAEK HDMPNRHEIS PGHDGAWNDS QLQEMAQLRI KHQEELTELH KKRGELAQLV IDLNNQMQQK DKEIQMNEAK ISEYLQTISD LETNCLDLRT KLQDLEVANQ TLKDEYDALQ ITFTALEEKL RKTTEENQEL VTRWMAEKAQ EANRLNAENE KDSRRRQARL QKELAEAAKE PLPVEQDDDI EVIVDETSDH TEETSPVRAV SRAATKRLSQ PAGGLLDSIT NIFGRRSVSS IPVPQDIMDT HPASGKDVRV PTTASYVFDA HDGEVNAVQF SPGSRLLATG GMDRRVKLWE AFGDKCEFKG SLSGSNAGIT SIEFDSAGAY LLAASNDFAS RIWTVDDYRL RHTLTGHSGK VLSAKFLLDN ARIVSGSHDR TLKLWDLRSK VCIKTVFAGS SCNDIVCTEQ CVMSGHFDKK IRFWDIRSES VVREMELLGK ITALDLNPER TELLSCSRDD LLKVIDLRTN AVKQTFSAPG FKCGSDWTRV VFSPDGSYVA AGSAEGSLYV WSVLTGKVEK VLSKQHSSSI NAVAWAPSGL HVVSVDKGSR AVLWAQP // ID A16L1_PONPY Reviewed; 607 AA. AC Q5RAC9; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 09-JAN-2007, entry version 16. DE Autophagy-related protein 16-1 (APG16-like 1). GN Name=ATG16L1; Synonyms=APG16L; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays an essential role in autophagy (By similarity). CC -!- SUBUNIT: Homooligomer. Interacts with ATG5. Part of a complex CC composed of ATG12-ATG5 and ATG16L1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Preautophagosomal CC structure; preautophagosomal structure membrane; peripheral CC membrane protein (By similarity). Note=Localized to CC preautophagosomal structure (PAS) where it is involved in the CC membrane targeting of ATG5 (By similarity). CC -!- SIMILARITY: Belongs to the WD repeat ATG16 family. CC -!- SIMILARITY: Contains 7 WD 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; CR859089; CAH91281.1; -; mRNA. DR InterPro; IPR013923; APG16. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 2. DR SMART; SM00320; WD40; 7. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Autophagy; Coiled coil; Membrane; Protein transport; Repeat; KW Transport; WD repeat. FT CHAIN 1 607 Autophagy-related protein 16-1. FT /FTId=PRO_0000050850. FT REPEAT 320 359 WD 1. FT REPEAT 364 403 WD 2. FT REPEAT 406 445 WD 3. FT REPEAT 447 484 WD 4. FT REPEAT 486 525 WD 5. FT REPEAT 532 573 WD 6. FT REPEAT 575 607 WD 7. FT COILED 79 230 Potential. SQ SEQUENCE 607 AA; 68230 MW; F0951C0720F2B213 CRC64; MSSGLRAADF PRWKRHISEQ LRRRDRLQRQ AFEEIILQYN KLLEKSDLHS VLAQKLQAEK HDVPNRHEIS PGHDGTWNDS QLQEMAQLRI KHQEELTELH KKRGELAQLV IDLNNQMQRK DREMQMNEAK IAECLQTISD LETECLDLRT KLCDLERANQ TLKDEYDALQ ITFTALEGKL RKTTEENQEL VTRWMAEKAQ EANRLNAENE KDSRRRQARL QKELAEAAKE PLPVEQDDDI EVIVDETSDH TEETSPVRAI SRAATKRLSQ PAGGLLDSIT NIFGRRSVSS FPVPQDNVDT HPGSGKEVRV PTTALCVFDA HDGEVNAVQF SPGSRLLATG GMDRRVKLWE VFGEKCEFKG SLSGSNAGIT SIEFDSAGSY LLAASNDFAS RIWTVDDSRL RHTLTGHSGK VLSAKFLLDN ARIVSGSHDR TLKHWDLRSK VCIKTVFAGS SCNDIVCTEQ CVMSGHFDKK IRFWDIRSES IVREMELLGK ITALDLNPER TELLSCSRDD LLKVIDLRTN AIKQTFSAPG FKCGSDWTRV VFSPDGSYVA AGSAEGSLYT WSVLTGKVEK VLSKQHSSSI NAVAWSPSGL HVVSVDKGCK AVLWAQY // ID A16_ANOGA Reviewed; 192 AA. AC Q93118; Q7Q2T9; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-FEB-2007, entry version 36. DE Protein A16 precursor. GN Name=CTL3; ORFNames=ENSANGG00000008945; OS Anopheles gambiae (African malaria mosquito). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; OC Anophelinae; Anopheles. OX NCBI_TaxID=7165; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, RP AND INDUCTION. RC STRAIN=G3; TISSUE=Larva; RX MEDLINE=97075119; PubMed=8917545; DOI=10.1073/pnas.93.23.13066; RA Dimopoulos G.M., Richman A.M., della Torre A., Kafatos F.C., Louis C.; RT "Identification and characterization of differentially expressed cDNAs RT of the vector mosquito, Anopheles gambiae."; RL Proc. Natl. Acad. Sci. U.S.A. 93:13066-13071(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEST; RX MEDLINE=22251359; PubMed=12364791; DOI=10.1126/science.1076181; RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., RA Salzberg S.L., Loftus B.J., Yandell M., Majoros W.H., Rusch D.B., RA Lai Z., Kraft C.L., Abril J.F., Anthouard V., Arensburger P., RA Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., RA Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., RA Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., RA Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., RA Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., RA Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., RA Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C., Kokoza E., RA Koutsos A., Letunic I., Levitsky A., Liang Y., Lin J.-J., Lobo N.F., RA Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J., RA Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., RA Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., RA Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., RA Ton L.Q., Topalis P., Tu Z., Unger M.F., Walenz B., Wang A., Wang J., RA Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., RA Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., RA Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., RA Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., RA Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.; RT "The genome sequence of the malaria mosquito Anopheles gambiae."; RL Science 298:129-149(2002). CC -!- TISSUE SPECIFICITY: Expressed in the gut of adults. CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic, larval and pupal CC stages. Highest expression is seen in late larval stages. CC -!- INDUCTION: Not induced by bacterial challenge in larvae. CC -!- SIMILARITY: Contains 1 C-type lectin 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; Y08163; CAA69355.1; -; mRNA. DR EMBL; AAAB01008968; EAA13236.2; -; Genomic_DNA. DR HSSP; P14151; 1KJB. DR Ensembl; ENSANGG00000008945; Anopheles gambiae. DR InterPro; IPR001304; Lectin_C. DR Pfam; PF00059; Lectin_C; 1. DR SMART; SM00034; CLECT; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; FALSE_NEG. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. KW Lectin; Signal. FT SIGNAL 1 22 Potential. FT CHAIN 23 192 Protein A16. FT /FTId=PRO_0000017555. FT DOMAIN 71 186 C-type lectin. FT DISULFID 163 177 By similarity. SQ SEQUENCE 192 AA; 20811 MW; EFEA2CBD9B0824A0 CRC64; MLLANTAAAV LLLIVCIGAS VGLPTVDEEN VVQAEQLPIL PTADSSKPTD DTVKAIAPQP RYLLPADFAV KNKKFTIGTL GVGSFFRAWR NCIDEGKGLA TIESEKEQKY LESLLKASST GSNYWIGATN IGASNTNKLT WITTDLPVQT KPPFLNVVAK STCIALTPTG SWTLRNCLNP LNIFPYICEE YF // ID A1AF_CAVPO Reviewed; 403 AA. AC P22324; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 31-OCT-2006, entry version 47. DE Alpha-1-antiproteinase F precursor (Alpha-1-antitrypsin) (Alpha-1- DE proteinase inhibitor) (APF) (Fragment). OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 23-42 AND 73-91. RX MEDLINE=91093294; PubMed=1985973; RA Suzuki Y., Yoshida K., Honda E., Sinohara H.; RT "Molecular cloning and sequence analysis of cDNAs coding for guinea RT pig alpha 1-antiproteinases S and F and contrapsin."; RL J. Biol. Chem. 266:928-932(1991). CC -!- FUNCTION: Inhibits elastase, chymotrypsin, cathepsin G, plasmin, CC and trypsin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- INDUCTION: APF rose about 2-fold during the acute phase reaction. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M57271; AAA62804.1; -; mRNA. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL <1 22 FT CHAIN 23 403 Alpha-1-antiproteinase F. FT /FTId=PRO_0000032381. FT REGION 358 377 RCL. FT SITE 367 368 Reactive bond; unorthodox type. FT CARBOHYD 55 55 N-linked (GlcNAc...) (Potential). FT CARBOHYD 92 92 N-linked (GlcNAc...) (Potential). FT CARBOHYD 155 155 N-linked (GlcNAc...) (Potential). FT CARBOHYD 222 222 N-linked (GlcNAc...) (Potential). FT CARBOHYD 256 256 N-linked (GlcNAc...) (Potential). FT NON_TER 1 1 SQ SEQUENCE 403 AA; 44920 MW; C39729EB364D909B CRC64; SAIPRGLLLL AGLCCLVFGI MAEDAQVAQG PSQQIPRSLA HFAHSMYRVL TQQSNTSNIF FSPVSIATAL AMVSLGAKGD THTQILWGLE FNLTEIAEAD IHDGFQNLLH TLNRPHSEHE LTTGNGLFLD QKLKLKEKFS EDVKTLYHAE AFPTNFSNPK EAEKQINAYV EKGTQGKIVD LVKDLSADTV LALVNYIFFR GKWEKPFDVK HTTQEDFLVD MNTTVNVPMM KRQGMYKAFH CSTIQSWVLL LDYEGNVTTL FLLPDKGKMQ HLEETLTPEL IFKFARKTER MFANVHLPKL SISGTYDLKE VLGHLGITNV FSGAADLSGI TEDMPLKISK GLHKALLTID EKGTEAAGAT ELEITPHSVP QDLFFNKPFL FLIIDHSTDT PLFVGKVMDP TKK // ID A1AF_RABIT Reviewed; 413 AA. AC P23035; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 31-OCT-2006, entry version 43. DE Alpha-1-antiproteinase F precursor (Alpha-1-antitrypsin) (Alpha-1- DE proteinase inhibitor) (APF). OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91201273; PubMed=2016265; RA Saito A., Sinohara H.; RT "Cloning and sequencing of cDNA coding for rabbit alpha-1- RT antiproteinase F: amino acid sequence comparison of alpha-1- RT antiproteinases of six mammals."; RL J. Biochem. 109:158-162(1991). RN [2] RP PROTEIN SEQUENCE OF 25-41. RX MEDLINE=88227895; PubMed=3259574; RA Saito A., Sinohara H.; RT "Differential interactions of rabbit plasma alpha-1-antiproteinases S RT and F with porcine trypsin."; RL J. Biochem. 103:247-253(1988). RN [3] RP PROTEIN SEQUENCE OF 374-380. RX MEDLINE=91035333; PubMed=2229014; RA Saito A., Sinohara H.; RT "Amino acid sequence at the reactive site of rabbit alpha-1- RT antiproteinases."; RL J. Biochem. 108:80-85(1990). CC -!- FUNCTION: Inhibitor of serine proteases. The primary target is CC elastase, but also has a moderate affinity for plasmin and CC thrombin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X57710; CAA40881.1; -; mRNA. DR EMBL; D00853; BAA00728.1; -; mRNA. DR PIR; JX0154; JX0154. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Direct protein sequencing; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL 1 24 FT CHAIN 25 413 Alpha-1-antiproteinase F. FT /FTId=PRO_0000032397. FT REGION 368 387 RCL. FT SITE 377 378 Reactive bond. FT CARBOHYD 65 65 N-linked (GlcNAc...) (Potential). FT CARBOHYD 102 102 N-linked (GlcNAc...) (Potential). FT CARBOHYD 230 230 N-linked (GlcNAc...) (Potential). FT CARBOHYD 266 266 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 413 AA; 45867 MW; E851F5DE63A592DF CRC64; MPPSVSRALL LLAGLGCLLP GFLADEAQET AVSSHEQDHP ACHRIAPSLA EFALSLYREV AHESNTTNIF FSPVSIALAF AMLSLGAKGD THTQVLEGLK FNLTETAEAQ IHDGFRHLLH TVNRPDSELQ LAARNALVVH ENLKLQHKFL EDAKNLYQSE AFLVDFRDPE QAKTKINSHV EKGTRGKIVD LVQELDARTL LALVNYVFFK GKWEKPFEPE NTKEEDFHVN ATTTVRVPMM SRLGRYDLFH CSTLASTVLR MDYKGNATAL FLLPDEGKLQ HLEDTLTTEL ITKFLAKSSL RSVTVHFPKL SISGTYDLKP LLGKLGITQV FSDNADLSGI TEQEPLKASQ ALHKAVLTID ERGTEAAGAT YMEIIPMSLP DSITLDRPFL FVIYSHEIKS PLFVGKVVDP TQH // ID A1AG1_HUMAN Reviewed; 201 AA. AC P02763; Q8TC16; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 20-FEB-2007, entry version 90. DE Alpha-1-acid glycoprotein 1 precursor (AGP 1) (Orosomucoid-1) (OMD 1). GN Name=ORM1; Synonyms=AGP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=88029318; PubMed=2822385; RA Dente L., Pizza M.G., Metspalu A., Cortese R.; RT "Structure and expression of the genes coding for human alpha 1-acid RT glycoprotein."; RL EMBO J. 6:2289-2296(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87031577; PubMed=3770479; DOI=10.1016/0378-1119(86)90051-X; RA Board P.G., Jones I.M., Bentley A.K.; RT "Molecular cloning and nucleotide sequence of human alpha 1 acid RT glycoprotein cDNA."; RL Gene 44:127-131(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=85242080; PubMed=2409529; DOI=10.1093/nar/13.11.3941; RA Dente L., Ciliberto G., Cortese R.; RT "Structure of the human alpha 1-acid glycoprotein gene: sequence RT homology with other human acute phase protein genes."; RL Nucleic Acids Res. 13:3941-3952(1985). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-38. 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 PROTEIN SEQUENCE OF 19-129. RX MEDLINE=73197484; PubMed=4711474; DOI=10.1021/bi00738a026; RA Schmid K., Kaufmann H., Isemura S., Bauer F., Emura J., Motoyama T., RA Ishiguro M., Nanno S.; RT "Structure of alpha 1-acid glycoprotein. The complete amino acid RT sequence, multiple amino acid substitutions, and homology with the RT immunoglobulins."; RL Biochemistry 12:2711-2724(1973). RN [6] RP PROTEIN SEQUENCE OF 129-201. RX MEDLINE=73006944; PubMed=4561179; DOI=10.1021/bi00770a022; RA Ikenaka T., Ishiguro M., Emura J., Kaufmann H., Isemura S., Bauer W., RA Schmid K.; RT "Isolation and partial characterization of the cyanogen bromide RT fragments of alpha 1-acid glycoprotein and the elucidation of the RT amino acid sequence of the carboxyl-terminal cyanogen bromide RT fragment."; RL Biochemistry 11:3817-3829(1972). RN [7] RP DISULFIDE BONDS. RX MEDLINE=74290014; PubMed=4603214; DOI=10.1021/bi00710a006; RA Schmid K., Buergi W., Collins J.H., Nanno S.; RT "The disulfide bonds of alpha1-acid glycoprotein."; RL Biochemistry 13:2694-2697(1974). RN [8] RP GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103. RX MEDLINE=92231810; PubMed=1567356; RA Treuheit M.J., Costello C.E., Halsall H.B.; RT "Analysis of the five glycosylation sites of human alpha 1-acid RT glycoprotein."; RL Biochem. J. 283:105-112(1992). RN [9] RP GLYCOSYLATION AT ASN-33. RX MEDLINE=22660472; PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [10] RP GLYCOSYLATION AT ASN-33; ASN-72 AND ASN-93, AND MASS SPECTROMETRY. RX PubMed=15253437; DOI=10.1021/pr034112b; RA Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.; RT "A new strategy for identification of N-glycosylated proteins and RT unambiguous assignment of their glycosylation sites using HILIC RT enrichment and partial deglycosylation."; RL J. Proteome Res. 3:556-566(2004). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 RP AND ASN-103, AND MASS SPECTROMETRY. RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 RP AND ASN-103, AND MASS SPECTROMETRY. RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, AND MASS SPECTROMETRY. RX PubMed=16740002; DOI=10.1021/pr050492k; RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., RA Loo J.A.; RT "Identification of N-linked glycoproteins in human saliva by RT glycoprotein capture and mass spectrometry."; RL J. Proteome Res. 5:1493-1503(2006). RN [14] RP 3D-STRUCTURE MODELING. RA Rojo-Dominguez A., Hernandez-Arana A.; RT "Three-dimensional modeling of the protein moiety of human alpha1-acid RT glycoprotein, a lipocalin-family member."; RL Protein Seq. Data Anal. 5:349-355(1993). RN [15] RP VARIANTS ARG-38 AND MET-174. RX MEDLINE=97203211; PubMed=9050929; DOI=10.1007/s004390050378; RA Yuasa I., Umetsu K., Vogt U., Nakamura H., Nanba E., Tamaki N., RA Irizawa Y.; RT "Human orosomucoid polymorphism: molecular basis of the three common RT ORM1 alleles, ORM1*F1, ORM1*F2, and ORM1*S."; RL Hum. Genet. 99:393-398(1997). CC -!- FUNCTION: Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. CC -!- INTERACTION: CC P05121:SERPINE1; NbExp=1; IntAct=EBI-976767, EBI-953978; CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- INDUCTION: Synthesis is controlled by glucocorticoids, CC interleukin-1 and interleukin-6, It increases 5- to 50-fold upon CC inflammation. CC -!- POLYMORPHISM: Three common alleles of ORM1 are known. ORM1*F1 has CC Gln-38/Val-174; ORM1*F2 has Gln-38/Met-174 and ORM1*S has Arg- CC 38/Val-174. CC -!- SIMILARITY: Belongs to the lipocalin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X02544; CAA26397.1; -; mRNA. DR EMBL; M13692; AAA35515.1; -; mRNA. DR EMBL; X05779; CAA29229.1; ALT_SEQ; Genomic_DNA. DR EMBL; X05780; CAA29229.1; JOINED; Genomic_DNA. DR EMBL; X05781; CAA29229.1; JOINED; Genomic_DNA. DR EMBL; X05782; CAA29229.1; JOINED; Genomic_DNA. DR EMBL; X05783; CAA29229.1; JOINED; Genomic_DNA. DR EMBL; X05784; CAA29229.1; JOINED; Genomic_DNA. DR EMBL; X06676; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X06680; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC026238; AAH26238.1; -; mRNA. DR PIR; A28346; OMHU1. DR UniGene; Hs.567311; -. DR IntAct; P02763; -. DR GlycoSuiteDB; P02763; -. DR SWISS-2DPAGE; P02763; HUMAN. DR Siena-2DPAGE; P02763; -. DR Ensembl; ENSG00000187681; Homo sapiens. DR KEGG; hsa:5004; -. DR H-InvDB; HIX0023218; -. DR HGNC; HGNC:8498; ORM1. DR MIM; 138600; gene. DR ArrayExpress; P02763; -. DR GermOnline; ENSG00000187681; Homo sapiens. DR RZPD-ProtExp; I0517; -. DR RZPD-ProtExp; IOH13560; -. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006953; P:acute-phase response; TAS:ProtInc. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin_like. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytFABP. DR Gene3D; G3DSA:2.40.128.20; Calycin; 1. DR PANTHER; PTHR11967; A1A_glycop; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG. KW Acute phase; Direct protein sequencing; Glycoprotein; Polymorphism; KW Pyrrolidone carboxylic acid; Signal. FT SIGNAL 1 18 FT CHAIN 19 201 Alpha-1-acid glycoprotein 1. FT /FTId=PRO_0000017860. FT MOD_RES 19 19 Pyrrolidone carboxylic acid. FT CARBOHYD 33 33 N-linked (GlcNAc...). FT CARBOHYD 56 56 N-linked (GlcNAc...). FT CARBOHYD 72 72 N-linked (GlcNAc...). FT CARBOHYD 93 93 N-linked (GlcNAc...). FT CARBOHYD 103 103 N-linked (GlcNAc...). FT /FTId=CAR_000170. FT DISULFID 23 165 FT DISULFID 90 183 FT VARIANT 38 38 Q -> R (in allele ORM1*S). FT /FTId=VAR_013840. FT VARIANT 174 174 V -> M (in allele ORM1*F2; FT dbSNP:rs2636890). FT /FTId=VAR_013841. FT CONFLICT 182 182 Missing (in Ref. 6). FT CONFLICT 193 193 Missing (in Ref. 6). SQ SEQUENCE 201 AA; 23512 MW; 63292233AD6EAD8B CRC64; MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDQIT GKWFYIASAF RNEEYNKSVQ EIQATFFYFT PNKTEDTIFL REYQTRQDQC IYNTTYLNVQ RENGTISRYV GGQEHFAHLL ILRDTKTYML AFDVNDEKNW GLSVYADKPE TTKEQLGEFY EALDCLRIPK SDVVYTDWKK DKCEPLEKQH EKERKQEEGE S // ID A1AG1_MOUSE Reviewed; 207 AA. AC Q60590; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 47. DE Alpha-1-acid glycoprotein 1 precursor (AGP 1) (Orosomucoid-1) (OMD 1). GN Name=Orm1; Synonyms=Agp1, Orm-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89356252; PubMed=2475311; RA Lee S.C., Chang C.J., Lee Y.M., Lei H.Y., Lai M.Y., Chen D.S.; RT "Molecular cloning of cDNAs corresponding to two genes of alpha 1-acid RT glycoprotein and characterization of two alleles of AGP-1 in the RT mouse."; RL DNA 8:245-251(1989). RN [2] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-34; ASN-76 AND RP ASN-94, AND MASS SPECTROMETRY. 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 [3] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-94 AND ASN-104, AND MASS RP SPECTROMETRY. RX 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. 0:0-0(2007). CC -!- FUNCTION: Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- SIMILARITY: Belongs to the lipocalin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M27008; AAA37194.1; -; mRNA. DR PIR; A32476; A32476. DR UniGene; Mm.4777; -. DR Ensembl; ENSMUSG00000039196; Mus musculus. DR KEGG; mmu:18405; -. DR MGI; MGI:97443; Orm1. DR ArrayExpress; Q60590; -. DR GermOnline; ENSMUSG00000039196; Mus musculus. DR RZPD-ProtExp; IOM16515; -. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin_like. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytFABP. DR Gene3D; G3DSA:2.40.128.20; Calycin; 1. DR PANTHER; PTHR11967; A1A_glycop; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG. KW Acute phase; Glycoprotein; Signal. FT SIGNAL 1 18 By similarity. FT CHAIN 19 207 Alpha-1-acid glycoprotein 1. FT /FTId=PRO_0000017862. FT CARBOHYD 25 25 N-linked (GlcNAc...). FT CARBOHYD 34 34 N-linked (GlcNAc...). FT CARBOHYD 76 76 N-linked (GlcNAc...). FT CARBOHYD 94 94 N-linked (GlcNAc...). FT CARBOHYD 104 104 N-linked (GlcNAc...). FT DISULFID 91 184 By similarity. SQ SEQUENCE 207 AA; 23895 MW; 34CA38BE40BC1863 CRC64; MALHTVLIIL SLLPMLEAQN PEHANFTIGE PITNETLSWL SDKWFFMGAA FRKLEYRQAI QTMQSEFFYL TTNLINDTIE LRESQTIGDQ CVYNSTHLGF QRENGTFSKY EGGVETFAHL IVLRKHGAFM LAFDLKDEKK RGLSLYAKRP DITPELREVF QKAVTHVGMD ESEIIFVDWK KDRCGQQEKK QLELGKETKK DPEEGQA // ID A1AG1_MUSCR Reviewed; 207 AA. AC P21350; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 28-NOV-2006, entry version 47. DE Alpha-1-acid glycoprotein 1 precursor (AGP 1) (Orosomucoid-1) (OMD 1). GN Name=Orm1; Synonyms=Agp-1, Orm-1; OS Mus caroli (Wild mouse) (Ricefield mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10089; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=90285134; PubMed=2354997; RA Prowse K.R., Baumann H.; RT "Molecular characterization and acute phase expression of the multiple RT Mus caroli alpha 1-acid glycoprotein (AGP) genes. Differences in RT glucocorticoid stimulation and regulatory elements between the rat and RT mouse AGP genes."; RL J. Biol. Chem. 265:10201-10209(1990). CC -!- FUNCTION: Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- MISCELLANEOUS: Eight genes coding for different forms of alpha-1- CC AGP are present in mus carolis. CC -!- SIMILARITY: Belongs to the lipocalin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M34648; AAA37195.1; -; mRNA. DR EMBL; M34647; AAA37197.1; -; mRNA. DR PIR; B35425; B35425. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin_like. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytFABP. DR Gene3D; G3DSA:2.40.128.20; Calycin; 1. DR PANTHER; PTHR11967; A1A_glycop; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG. KW Acute phase; Glycoprotein; Signal. FT SIGNAL 1 18 FT CHAIN 19 207 Alpha-1-acid glycoprotein 1. FT /FTId=PRO_0000017865. FT CARBOHYD 25 25 N-linked (GlcNAc...) (Potential). FT CARBOHYD 34 34 N-linked (GlcNAc...) (Potential). FT CARBOHYD 76 76 N-linked (GlcNAc...) (Potential). FT CARBOHYD 94 94 N-linked (GlcNAc...) (Potential). FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT DISULFID 91 184 By similarity. FT VARIANT 38 38 S -> G. SQ SEQUENCE 207 AA; 23896 MW; A196EE6676F4D4C0 CRC64; MALHMILVML SLLPLLEAQN PEHVNITIGE PITNETLSWL SDKWFFIGAA VLNPDYRQEI QKMQMVFFNI TPNLINDTME LREYHTIDDH CVYNSTHLGI QRENGTLSKY VGGVKIFADL IVLRKHGAFM LAFDLKDEKK RGLSLNAKRP DITPELREVF QKAVKHVGMD ESEIIFVDWK KDKCGQQEKK QLELEKETKK DPEEGQA // ID A1AG2_HUMAN Reviewed; 201 AA. AC P19652; Q16571; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 06-FEB-2007, entry version 81. DE Alpha-1-acid glycoprotein 2 precursor (AGP 2) (Orosomucoid-2) (OMD 2). GN Name=ORM2; Synonyms=AGP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88029318; PubMed=2822385; RA Dente L., Pizza M.G., Metspalu A., Cortese R.; RT "Structure and expression of the genes coding for human alpha 1-acid RT glycoprotein."; RL EMBO J. 6:2289-2296(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88329732; PubMed=2970990; DOI=10.1016/0378-1119(88)90228-4; RA Merritt C.M., Board P.G.; RT "Structure and characterisation of a duplicated human alpha 1 acid RT glycoprotein gene."; RL Gene 66:97-106(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 DISULFIDE BONDS. RX MEDLINE=74290014; PubMed=4603214; DOI=10.1021/bi00710a006; RA Schmid K., Buergi W., Collins J.H., Nanno S.; RT "The disulfide bonds of alpha1-acid glycoprotein."; RL Biochemistry 13:2694-2697(1974). RN [5] RP GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103. RX MEDLINE=92231810; PubMed=1567356; RA Treuheit M.J., Costello C.E., Halsall H.B.; RT "Analysis of the five glycosylation sites of human alpha 1-acid RT glycoprotein."; RL Biochem. J. 283:105-112(1992). RN [6] RP PYROGLUTAMATE FORMATION AT GLN-19, GLYCOSYLATION AT ASN-33 AND ASN-93, RP AND MASS SPECTROMETRY. RX PubMed=15253437; DOI=10.1021/pr034112b; RA Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.; RT "A new strategy for identification of N-glycosylated proteins and RT unambiguous assignment of their glycosylation sites using HILIC RT enrichment and partial deglycosylation."; RL J. Proteome Res. 3:556-566(2004). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72 AND RP ASN-93, AND MASS SPECTROMETRY. RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 RP AND ASN-103, AND MASS SPECTROMETRY. RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). CC -!- FUNCTION: Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- INDUCTION: Synthesis is controlled by glucocorticoids, CC interleukin-1 and interleukin-6, It increases 5- to 50-fold upon CC inflammation. CC -!- POLYMORPHISM: Many different variants of ORM2 are known. CC -!- SIMILARITY: Belongs to the lipocalin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X06675; CAA29874.1; ALT_SEQ; Genomic_DNA. DR EMBL; X05780; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X06674; CAA29873.2; ALT_SEQ; Genomic_DNA. DR EMBL; X06676; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06677; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06678; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06679; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06680; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X05784; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M21540; AAA51549.1; -; Genomic_DNA. DR EMBL; BC015964; AAH15964.1; -; mRNA. DR PIR; JT0326; OMHU2. DR UniGene; Hs.522356; -. DR GlycoSuiteDB; P19652; -. DR SWISS-2DPAGE; P19652; HUMAN. DR DOSAC-COBS-2DPAGE; P19652; HUMAN. DR Ensembl; ENSG00000187681; Homo sapiens. DR KEGG; hsa:5005; -. DR H-InvDB; HIX0008317; -. DR HGNC; HGNC:8499; ORM2. DR MIM; 138610; gene. DR ArrayExpress; P19652; -. DR GermOnline; ENSG00000204154; Homo sapiens. DR RZPD-ProtExp; RZPDo834A0116; -. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0006953; P:acute-phase response; TAS:ProtInc. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin_like. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytFABP. DR Gene3D; G3DSA:2.40.128.20; Calycin; 1. DR PANTHER; PTHR11967; A1A_glycop; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG. KW Acute phase; Glycoprotein; Polymorphism; Pyrrolidone carboxylic acid; KW Signal. FT SIGNAL 1 18 FT CHAIN 19 201 Alpha-1-acid glycoprotein 2. FT /FTId=PRO_0000017861. FT MOD_RES 19 19 Pyrrolidone carboxylic acid. FT CARBOHYD 33 33 N-linked (GlcNAc...). FT CARBOHYD 56 56 N-linked (GlcNAc...). FT CARBOHYD 72 72 N-linked (GlcNAc...). FT CARBOHYD 93 93 N-linked (GlcNAc...). FT CARBOHYD 103 103 N-linked (GlcNAc...). FT /FTId=CAR_000171. FT DISULFID 23 165 FT DISULFID 90 183 FT VARIANT 38 38 R -> Q (in dbSNP:rs17650). FT /FTId=VAR_014667. SQ SEQUENCE 201 AA; 23603 MW; 49167ABCC22933B9 CRC64; MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDRIT GKWFYIASAF RNEEYNKSVQ EIQATFFYFT PNKTEDTIFL REYQTRQNQC FYNSSYLNVQ RENGTVSRYE GGREHVAHLL FLRDTKTLMF GSYLDDEKNW GLSFYADKPE TTKEQLGEFY EALDCLCIPR SDVMYTDWKK DKCEPLEKQH EKERKQEEGE S // ID A1AG2_MOUSE Reviewed; 207 AA. AC P07361; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 23-JAN-2007, entry version 60. DE Alpha-1-acid glycoprotein 2 precursor (AGP 2) (Orosomucoid-2) (OMD 2). GN Name=Orm2; Synonyms=Agp-2, Orm-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BALB/c; RX MEDLINE=88050798; PubMed=3676251; DOI=10.1021/bi00391a006; RA Cooper R., Eckley D.M., Papaconstantinou J.; RT "Nucleotide sequence of the mouse alpha 1-acid glycoprotein gene 1."; RL Biochemistry 26:5244-5250(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89356252; PubMed=2475311; RA Lee S.C., Chang C.J., Lee Y.M., Lei H.Y., Lai M.Y., Chen D.S.; RT "Molecular cloning of cDNAs corresponding to two genes of alpha 1-acid RT glycoprotein and characterization of two alleles of AGP-1 in the RT mouse."; RL DNA 8:245-251(1989). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 70-207. RX MEDLINE=86111861; PubMed=3003086; RA Cooper R., Papaconstantinou J.; RT "Evidence for the existence of multiple alpha 1-acid glycoprotein RT genes in the mouse."; RL J. Biol. Chem. 261:1849-1853(1986). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-76, AND MASS SPECTROMETRY. 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). CC -!- FUNCTION: Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- INDUCTION: Synthesis is controlled by glucocorticoids, CC interleukin-1 and interleukin-6, It increases 5- to 50-fold upon CC inflammation. CC -!- SIMILARITY: Belongs to the lipocalin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M17376; AAA37193.1; -; Genomic_DNA. DR EMBL; M27009; AAA37196.1; -; mRNA. DR EMBL; BC057985; AAH57985.1; -; mRNA. DR EMBL; M12566; AAA91744.1; -; mRNA. DR PIR; A29294; OMMS1. DR UniGene; Mm.14173; -. DR Ensembl; ENSMUSG00000061540; Mus musculus. DR KEGG; mmu:18406; -. DR MGI; MGI:97444; Orm2. DR ArrayExpress; P07361; -. DR GermOnline; ENSMUSG00000061540; Mus musculus. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin_like. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytFABP. DR Gene3D; G3DSA:2.40.128.20; Calycin; 1. DR PANTHER; PTHR11967; A1A_glycop; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG. KW Acute phase; Glycoprotein; Signal. FT SIGNAL 1 18 FT CHAIN 19 207 Alpha-1-acid glycoprotein 2. FT /FTId=PRO_0000017863. FT CARBOHYD 25 25 N-linked (GlcNAc...) (Potential). FT CARBOHYD 34 34 N-linked (GlcNAc...) (Potential). FT CARBOHYD 76 76 N-linked (GlcNAc...). FT CARBOHYD 94 94 N-linked (GlcNAc...) (Potential). FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT DISULFID 91 184 By similarity. SQ SEQUENCE 207 AA; 23843 MW; 0FBCBEA99C558A6F CRC64; MALHMILVMV SLLPLLEAQN PEHVNITIGD PITNETLSWL SDKWFFIGAA VLNPDYRQEI QKTQMVFFNL TPNLINDTME LREYHTIDDH CVYNSTHLGI QRENGTLSKY VGGVKIFADL IVLKMHGAFM LAFDLKDEKK RGLSLNAKRP DITPELREVF QKAVTHVGMD ESEIIFVDWK KDRCSQQEKQ QLELEKETKK DPEEGQA // ID A1AG3_MOUSE Reviewed; 206 AA. AC Q63805; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 48. DE Alpha-1-acid glycoprotein 3 precursor (AGP 3) (Orosomucoid-3) (OMD 3). GN Name=Orm3; Synonyms=Agp-3, Orm-3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/6; TISSUE=Lymphocyte; RX MEDLINE=92297157; PubMed=1605854; RA Chang C.J., Lai M.Y., Chen D.S., Lee S.C.; RT "Structure and expression of mouse alpha 1-acid glycoprotein gene-3 RT (AGP-3)."; RL DNA Cell Biol. 11:315-320(1992). CC -!- FUNCTION: Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- SIMILARITY: Belongs to the lipocalin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S38219; AAB22378.2; -; Genomic_DNA. DR UniGene; Mm.381399; -. DR Ensembl; ENSMUSG00000028359; Mus musculus. DR MGI; MGI:97445; Orm3. DR ArrayExpress; Q63805; -. DR GermOnline; ENSMUSG00000028359; Mus musculus. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin_like. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytFABP. DR Gene3D; G3DSA:2.40.128.20; Calycin; 1. DR PANTHER; PTHR11967; A1A_glycop; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG. KW Acute phase; Glycoprotein; Signal. FT SIGNAL 1 18 By similarity. FT CHAIN 19 206 Alpha-1-acid glycoprotein 3. FT /FTId=PRO_0000017864. FT CARBOHYD 33 33 N-linked (GlcNAc...) (Potential). FT CARBOHYD 75 75 N-linked (GlcNAc...) (Potential). FT CARBOHYD 103 103 N-linked (GlcNAc...) (Potential). FT DISULFID 90 183 By similarity. SQ SEQUENCE 206 AA; 24069 MW; 5E98D1958BE1F0AB CRC64; MELHTVLIML SLLPLLEAQN PEHAINIGDP ITNETLSWLS GKWFLIAVAD SDPDYRQEIQ KVQTIFFYLT LNKINDTMEL REYHTKDDHC VYNSNLLGFQ RENGTLFKYE GEVENPSHLR VLEKHGAIML FFDLKDEKKR GLSLSARRPD IPPELREVFQ KAVTHVGMDE SEIIFVDWKK DRCSEQEKKH LELEKETKKD PEESQA // ID A1AG8_MUSCR Reviewed; 207 AA. AC P21352; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 28-NOV-2006, entry version 47. DE Alpha-1-acid glycoprotein 8 precursor (AGP 8) (Orosomucoid-8) (OMD 8). GN Name=Orm8; Synonyms=Agp-8, Orm-8; OS Mus caroli (Wild mouse) (Ricefield mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10089; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=90285134; PubMed=2354997; RA Prowse K.R., Baumann H.; RT "Molecular characterization and acute phase expression of the multiple RT Mus caroli alpha 1-acid glycoprotein (AGP) genes. Differences in RT glucocorticoid stimulation and regulatory elements between the rat and RT mouse AGP genes."; RL J. Biol. Chem. 265:10201-10209(1990). CC -!- FUNCTION: Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- MISCELLANEOUS: Eight genes coding for different forms of alpha-1- CC AGP are present in mus carolis. CC -!- SIMILARITY: Belongs to the lipocalin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M34649; AAA37198.1; -; mRNA. DR EMBL; M34646; AAB67844.1; -; mRNA. DR PIR; C35425; C35425. DR PIR; D35425; D35425. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin_like. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytFABP. DR Gene3D; G3DSA:2.40.128.20; Calycin; 1. DR PANTHER; PTHR11967; A1A_glycop; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG. KW Acute phase; Glycoprotein; Signal. FT SIGNAL 1 18 FT CHAIN 19 207 Alpha-1-acid glycoprotein 8. FT /FTId=PRO_0000017866. FT CARBOHYD 25 25 N-linked (GlcNAc...) (Potential). FT CARBOHYD 34 34 N-linked (GlcNAc...) (Potential). FT CARBOHYD 76 76 N-linked (GlcNAc...) (Potential). FT CARBOHYD 94 94 N-linked (GlcNAc...) (Potential). FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT DISULFID 91 184 By similarity. FT VARIANT 10 10 L -> V. FT VARIANT 24 24 A -> V. FT VARIANT 50 50 A -> R. FT VARIANT 98 98 L -> V. SQ SEQUENCE 207 AA; 23912 MW; 2BADBF5EF94E7EB7 CRC64; MALHTVLIML SLLPMLEAQN PEHANITIGE PITNETLGWL SDKWFFMGAA FRKLEYRQAI QMMQTEFFYL TTNLINDTIE LRESQTIGDQ CVYNSTHLGF QRENGTFSKY EGGVETFAHL IVLRKHGAFM LAFDLNDEKK RGLSLYAKRP DMTLELREVF QKAVKHVGMD ESEIIFVDWK KDKCGQQEKK QLELGKETKK DPEEGQA // ID A1AG_BOVIN Reviewed; 202 AA. AC Q3SZR3; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 20-FEB-2007, entry version 12. DE Alpha-1-acid glycoprotein precursor (Orosomucoid) (OMD). GN Name=ORM1; Synonyms=AGP; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Testis; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Appears to function in modulating the activity of the CC immune system during the acute-phase reaction (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- SIMILARITY: Belongs to the lipocalin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC102740; AAI02741.1; -; mRNA. DR UniGene; Bt.49064; -. DR KEGG; bta:497200; -. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin_like. DR InterPro; IPR000566; Lipocln_cytFABP. DR Gene3D; G3DSA:2.40.128.20; Calycin; 1. DR PANTHER; PTHR11967; A1A_glycop; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG. KW Acute phase; Glycoprotein; Signal. FT SIGNAL 1 18 By similarity. FT CHAIN 19 202 Alpha-1-acid glycoprotein. FT /FTId=PRO_0000271395. FT CARBOHYD 34 34 N-linked (GlcNAc...) (Potential). FT CARBOHYD 57 57 N-linked (GlcNAc...) (Potential). FT CARBOHYD 94 94 N-linked (GlcNAc...) (Potential). FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT CARBOHYD 136 136 N-linked (GlcNAc...) (Potential). FT DISULFID 91 184 By similarity. SQ SEQUENCE 202 AA; 23182 MW; B6EF3A1691BCCF2F CRC64; MALLWALAVL SHLPLLDAQS PECANLMTVA PITNATMDLL SGKWFYIGSA FRNPEYNKSA RAIQAAFFYL EPRHAEDKLI TREYQTIEDK CVYNCSFIKI YRQNGTLSKV ESDREHFVDL LLSKHFRTFM LAASWNGTKN VGVSFYADKP EVTQEQKKEF LDVIKCIGIQ ESEIIYTDEK KDACGPLEKQ HEEERKKETE AS // ID A1AG_RABIT Reviewed; 201 AA. AC P25227; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 09-JAN-2007, entry version 36. DE Alpha-1-acid glycoprotein precursor (Orosomucoid) (OMD). GN Name=ORM1; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=91315474; PubMed=1859410; RA Ray B.K., Ray A.; RT "Molecular cloning and nucleotide sequence of complementary DNA RT encoding rabbit alpha 1-acid glycoprotein."; RL Biochem. Biophys. Res. Commun. 178:507-513(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92287142; PubMed=1534658; RA Ray B.K., Ray A.; RT "Cloning and structural characterization of a rabbit genomic DNA for RT alpha 1 acid glycoprotein."; RL Biochem. Biophys. Res. Commun. 185:69-77(1992). CC -!- FUNCTION: Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- SIMILARITY: Belongs to the lipocalin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X58727; CAA41559.1; -; mRNA. DR EMBL; M93344; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; JH0617; JH0617. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin_like. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytFABP. DR Gene3D; G3DSA:2.40.128.20; Calycin; 1. DR PANTHER; PTHR11967; A1A_glycop; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG. KW Acute phase; Glycoprotein; Signal. FT SIGNAL 1 18 By similarity. FT CHAIN 19 201 Alpha-1-acid glycoprotein. FT /FTId=PRO_0000017867. FT CARBOHYD 25 25 N-linked (GlcNAc...) (Potential). FT CARBOHYD 33 33 N-linked (GlcNAc...) (Potential). FT CARBOHYD 87 87 N-linked (GlcNAc...) (Potential). FT CARBOHYD 93 93 N-linked (GlcNAc...) (Potential). FT CARBOHYD 103 103 N-linked (GlcNAc...) (Potential). FT CARBOHYD 169 169 N-linked (GlcNAc...) (Potential). FT DISULFID 90 183 By similarity. SQ SEQUENCE 201 AA; 23028 MW; 97DC40E41C7DAC4D CRC64; MALPWALAVL SLLPLLHAQD PACANFSTSP ITNATLDQLS HKWFFTASAF RNPKYKQLVQ HTQAAFFYFT AIKEEDTLLL REYITTNNTC FYNSSIVRVQ RENGTLSKHD GIRNSVADLL LLRDPGSFLL VFFAGKEQDK GMSFYTDKPK ASPEQLEEFY EALTCLGMNK TEVVYTDWTK DLCEPLEKQH EEERKKEKAE S // ID A1AG_RAT Reviewed; 205 AA. AC P02764; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 23-JAN-2007, entry version 50. DE Alpha-1-acid glycoprotein precursor (Orosomucoid) (OMD). GN Name=Orm1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=82030935; PubMed=6270146; RA Ricca G.A., Taylor J.M.; RT "Nucleotide sequence of rat alpha 1-acid glycoprotein messenger RNA."; RL J. Biol. Chem. 256:11199-11202(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86310846; PubMed=2943986; RA Liao Y.C.J., Taylor J.M., Vannice J.L., Clawson G.A., Smuckler E.A.; RT "Structure of the rat alpha 1-acid glycoprotein gene."; RL Mol. Cell. Biol. 5:3634-3639(1985). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=85157606; PubMed=3838547; RA Reinke R., Feigelson P.; RT "Rat alpha 1-acid glycoprotein. Gene sequence and regulation by RT glucocorticoids in transfected L-cells."; RL J. Biol. Chem. 260:4397-4403(1985). CC -!- FUNCTION: Appears to function in modulating the activity of the CC immune system during the acute-phase reaction. CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- INDUCTION: Alpha-1-AGP is synthesized in the liver, the synthesis CC being controlled by glucocorticoids, interleukin-1 and CC interleukin-6, it increases 5- to 50-fold upon inflammation. CC -!- SIMILARITY: Belongs to the lipocalin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J00696; AAA40699.1; -; mRNA. DR EMBL; V01216; CAA24527.1; -; mRNA. DR EMBL; M11329; AAA40700.1; -; Genomic_DNA. DR EMBL; M10614; AAA40701.1; -; Genomic_DNA. DR PIR; A93069; OMRT1. DR UniGene; Rn.10295; -. DR GlycoSuiteDB; P02764; -. DR Ensembl; ENSRNOG00000007886; Rattus norvegicus. DR KEGG; rno:24614; -. DR RGD; 67390; Orm1. DR ArrayExpress; P02764; -. DR GermOnline; ENSRNOG00000007886; Rattus norvegicus. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin_like. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytFABP. DR Gene3D; G3DSA:2.40.128.20; Calycin; 1. DR PANTHER; PTHR11967; A1A_glycop; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG. KW Acute phase; Glycoprotein; Signal. FT SIGNAL 1 18 FT CHAIN 19 205 Alpha-1-acid glycoprotein. FT /FTId=PRO_0000017868. FT CARBOHYD 25 25 N-linked (GlcNAc...) (Potential). FT CARBOHYD 34 34 N-linked (GlcNAc...) (Potential). FT CARBOHYD 76 76 N-linked (GlcNAc...) (Potential). FT CARBOHYD 94 94 N-linked (GlcNAc...) (Potential). FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT CARBOHYD 134 134 N-linked (GlcNAc...) (Potential). FT DISULFID 91 183 By similarity. SQ SEQUENCE 205 AA; 23575 MW; E363A742C2B2DE06 CRC64; MALHMVLVVL SLLPLLEAQN PEPANITLGI PITNETLKWL SDKWFYMGAA FRDPVFKQAV QTIQTEYFYL TPNLINDTIE LREFQTTDDQ CVYNFTHLGV QRENGTLSKC AGAVKIFAHL IVLKKHGTFM LAFNLTDENR GLSFYAKKPD LSPELRKIFQ QAVKDVGMDE SEIVFVDWTK DKCSEQQKQQ LELEKETKKE TKKDP // ID A1AS_CAVPO Reviewed; 405 AA. AC P22325; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 31-OCT-2006, entry version 48. DE Alpha-1-antiproteinase S precursor (Alpha-1-antitrypsin) (Alpha-1- DE proteinase inhibitor) (APS). OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-44 AND 75-93. RX MEDLINE=91093294; PubMed=1985973; RA Suzuki Y., Yoshida K., Honda E., Sinohara H.; RT "Molecular cloning and sequence analysis of cDNAs coding for guinea RT pig alpha 1-antiproteinases S and F and contrapsin."; RL J. Biol. Chem. 266:928-932(1991). CC -!- FUNCTION: Inhibits elastase, chymotrypsin, cathepsin G, plasmin, CC and trypsin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- INDUCTION: APS rose several hundred-fold during the acute phase CC reaction. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M57270; AAA62805.1; -; mRNA. DR PIR; A39088; A39088. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 FT CHAIN 25 405 Alpha-1-antiproteinase S. FT /FTId=PRO_0000032382. FT REGION 360 379 RCL. FT SITE 369 370 Reactive bond. FT CARBOHYD 57 57 N-linked (GlcNAc...) (Potential). FT CARBOHYD 94 94 N-linked (GlcNAc...) (Potential). FT CARBOHYD 157 157 N-linked (GlcNAc...) (Potential). FT CARBOHYD 258 258 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 405 AA; 45125 MW; 5D41D48E1E078AA8 CRC64; MPSAIPRGLL LLAGLCCLVF GIMAEDAQVA QGPSQQIPRS LAHFAHSMYR VLTQQSNTSN IFFSPVSIAT ALAMVSVGAK GDTHTQILRG LEFNLTEIAE ADIHNGFQNL LHTLNRPHSE HQLTTGNGLF LDQKLKLKEK FSEDVKTLYH AEAFPTNFSN PKEAEKQINA YVEKGTQGKI VDLVKDLSAD TVLALVNYIF FRGKWEKPFD VKHTTQEDFH VDTSTTVKVP MMKREGKYKA FHCSTIQSWV LLLDYEGNVT ALFLLPEEGK MQHLEETLTP ELIFKFARKT ERMFANVHLP KLSISGTYDL KEVLGHLGIT NVFSDAADLS GVTEDIPLKI SKGLHKALLT IDEKGTEAAG ATMMEFMPMS LPEDLSFNKP FLFLIIDHST DTPLFVGKVM DPTKK // ID A1AT1_MOUSE Reviewed; 413 AA. AC P07758; Q80YB8; Q8JZV6; Q91XB8; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 4. DT 20-FEB-2007, entry version 63. DE Alpha-1-antitrypsin 1-1 precursor (Serine protease inhibitor 1-1) DE (Alpha-1 protease inhibitor 1) (Alpha-1-antiproteinase) (AAT). GN Name=Serpina1a; Synonyms=Dom1, Spi1-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RX MEDLINE=92052104; PubMed=1946354; RA Borriello F., Krauter K.S.; RT "Multiple murine alpha 1-protease inhibitor genes show unusual RT evolutionary divergence."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9417-9421(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/J; RX MEDLINE=22296988; PubMed=12408969; DOI=10.1016/S0888-7543(02)96864-3; RA Barbour K.W., Wei F., Brannan C., Flotte T.R., Baumann H., RA Berger F.G.; RT "The murine alpha(1)-proteinase inhibitor gene family: polymorphism, RT chromosomal location, and structure."; RL Genomics 80:515-522(2002). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 211-413. RX MEDLINE=86163765; PubMed=3007061; RA Krauter K.S., Citron B.A., Hsu M.T., Powell D., Darnell J.E. Jr.; RT "Isolation and characterization of the alpha 1-antitrypsin gene of RT mice."; RL DNA 5:29-36(1986). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=96190670; PubMed=8619829; DOI=10.1006/bbrc.1996.0182; RA Paterson T., Moore S.; RT "The expression and characterization of five recombinant murine alpha RT 1-protease inhibitor proteins."; RL Biochem. Biophys. Res. Commun. 219:64-69(1996). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND REGION RCL. RX MEDLINE=21959334; PubMed=11961105; RA Barbour K.W., Goodwin R.L., Guillonneau F., Wang Y., Baumann H., RA Berger F.G.; RT "Functional diversification during evolution of the murine alpha(1)- RT proteinase inhibitor family: role of the hypervariable reactive center RT loop."; RL Mol. Biol. Evol. 19:718-727(2002). RN [7] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=12659817; DOI=10.1016/S0888-7543(02)00041-1; RA Forsyth S., Horvath A., Coughlin P.; RT "A review and comparison of the murine alpha1-antitrypsin and alpha1- RT antichymotrypsin multigene clusters with the human clade A serpins."; RL Genomics 81:336-345(2003). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64 AND ASN-101, AND MASS RP SPECTROMETRY. RX 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. 0:0-0(2007). CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is CC elastase, but it also has a moderate affinity for plasmin and CC thrombin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). Variability within the reactive center loop (RCL) CC sequences of Serpina1-related genes may determine target protease CC specificity. CC -!- MISCELLANEOUS: Murine alpha-1-antitrypsin is represented by a CC cluster of up to 5 individual Serpina1-related genes. The precise CC complement of Serpina1-related genes present varies according to CC the strain of the animal. While all strains seem to express CC Serpina1a and Serpina1b, individual strains may express either CC Spi1-6 alone or the three serpins Serpina1c, Serpina1d and CC Serpina1e together. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M75721; AAC28869.1; -; mRNA. DR EMBL; AF481949; AAM47488.1; -; Genomic_DNA. DR EMBL; BC011040; AAH11040.1; -; mRNA. DR EMBL; BC037007; AAH37007.2; -; mRNA. DR EMBL; BC049970; AAH49970.1; ALT_INIT; mRNA. DR EMBL; BC057982; AAH57982.1; -; mRNA. DR EMBL; BC057984; AAH57984.1; -; mRNA. DR EMBL; BC057989; AAH57989.1; -; mRNA. DR EMBL; M12586; AAA51624.1; -; mRNA. DR PIR; I49470; I49470. DR UniGene; Mm.312593; -. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR Ensembl; ENSMUSG00000060178; Mus musculus. DR KEGG; mmu:20700; -. DR MGI; MGI:891971; Serpina1a. DR ArrayExpress; P07758; -. DR GermOnline; ENSMUSG00000066366; Mus musculus. DR RZPD-ProtExp; IOM16662; -. DR RZPD-ProtExp; IOM16665; -. DR InterPro; IPR000215; Prot_inh_serpin. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL 1 24 By similarity. FT CHAIN 25 413 Alpha-1-antitrypsin 1-1. FT /FTId=PRO_0000032388. FT REGION 368 387 RCL. FT SITE 377 378 Reactive bond (By similarity). FT CARBOHYD 64 64 N-linked (GlcNAc...). FT CARBOHYD 101 101 N-linked (GlcNAc...). FT CARBOHYD 265 265 N-linked (GlcNAc...) (Potential). FT CONFLICT 246 246 H -> D (in Ref. 2, 3; AAH11040/AAH37007/ FT AAH49970/AAH57982/AAH57984/AAH57989 and FT 4). FT CONFLICT 323 323 P -> L (in Ref. 4). FT CONFLICT 404 404 L -> V (in Ref. 2, 3; AAH11040/AAH37007/ FT AAH49970/AAH57982/AAH57984/AAH57989 and FT 4). SQ SEQUENCE 413 AA; 46003 MW; 1124B2CC356232F4 CRC64; MTPSISWGLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HKSFQHLLQT LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE KGTQGKIAEA VKKLDQDTVF ALANYILFKG KWKKPFDPEN TEEAEFHVDE STTVKVPMMT LSGMLHVHHC STLSSWVLLM DYAGNATAVF LLPDDGKMQH LEQTLSKELI SKFLLNRRRR LAQIHFPRLS ISGEYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSQ AVHKAVLTID ETGTEAAAVT VLQMVPMSMP PILRFDHPFL FIIFEEHTQS PIFLGKVVDP THK // ID A1AT2_HORSE Reviewed; 421 AA. AC P38029; O46519; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 31-OCT-2006, entry version 42. DE Alpha-1-antiproteinase 2 precursor (Alpha-1-antitrypsin 2) (Alpha-1- DE proteinase inhibitor 2) (SPI2). OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Giffard J.M., Irvin Z.V., Bell T.K., Brandon R.B.; RT "Equine alpha-1-antitrypsin gene."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 25-43 AND 381-412. RC TISSUE=Plasma; RX MEDLINE=92126011; PubMed=1772402; RA Patterson S.D., Bell K., Shaw D.C.; RT "The equine major plasma serpin multigene family: partial RT characterization including sequence of the reactive-site regions."; RL Biochem. Genet. 29:477-499(1991). RN [3] RP STRUCTURE OF CARBOHYDRATES. RX MEDLINE=90267497; PubMed=2111994; RA Patterson S.D., Bell K.; RT "The carbohydrate side chains of the major plasma serpins of horse and RT wallaby: analyses of enzymatic and chemically treated (including RT 'Smith degradation') protein blots by lectin binding."; RL Biochem. Int. 20:429-436(1990). CC -!- FUNCTION: Inhibitor of serine proteases (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the serpin reactive site CC and the active site of the protease. The resulting inactive CC serpin-protease complex is highly stable (By similarity). CC -!- PTM: N-glycosylated with carbohydrates having biantennary side CC chains. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF034077; AAC83412.1; -; Genomic_DNA. DR PIR; B61219; B61219. DR HSSP; P01009; 9API. DR SMR; P38029; 48-421. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 FT CHAIN 25 421 Alpha-1-antiproteinase 2. FT /FTId=PRO_0000032385. FT REGION 376 395 RCL. FT SITE 385 386 Reactive bond (By similarity). FT CARBOHYD 73 73 N-linked (GlcNAc...) (Potential). FT CARBOHYD 110 110 N-linked (GlcNAc...) (Potential). FT CARBOHYD 274 274 N-linked (GlcNAc...) (Potential). FT CONFLICT 36 40 HATAH -> DADKD (in Ref. 2). FT CONFLICT 398 398 V -> I (in Ref. 2). SQ SEQUENCE 421 AA; 46942 MW; D79B101312AC8259 CRC64; MPSSVPWCLL LLAGLCCLVP SSLAEDLQGC AVQETHATAH DEEHLQEPAE HKIAPNLADF AFSLYRHVAH QSNTTNIFFS PVSIATAFAL LSLGAKGDTH TQILEGLSFN LTELAEAQIH DGFQHLLNAL NHSDNQLQLT TGNGLFIDES AKLLDKFLED VKKLYHSEAF SINFRDTEEA KKQINDYVEK GTQGKIVDLV KDLDKDTVLA LVNYIFFKGT WEKPFEPEYT TEQDFHVDEK TTVRVPMMHR LSSFDVQYSD TLSSWVLLLD YAGNATAFFI LPDQGKLQHL EDTLTKGILA RFLGNRHSSF VNVHLPKLSI SGTYDLTSIL PELGITKVFS RQADLSGITE EVPLTVSKAL HKAVLTIDEK GTEAAGTTMW EIMPISLPPD LKFNRPFVLI IYDRNTKSPL FVGKVVDPTQ K // ID A1AT2_MOUSE Reviewed; 413 AA. AC P22599; Q61283; Q80ZH5; Q8VC20; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 23-JAN-2007, entry version 57. DE Alpha-1-antitrypsin 1-2 precursor (Serine protease inhibitor 1-2) DE (Alpha-1 protease inhibitor 2) (Alpha-1-antiproteinase) (AAT). GN Name=Serpina1b; Synonyms=Aat2, Dom2, Spi1-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90152670; PubMed=2303252; RA Sifers R.N., Ledley F.D., Reed-Fourquet L., Ledbetter D.H., RA Ledbetter S.A., Woo S.L.C.; RT "Complete cDNA sequence and chromosomal localization of mouse alpha 1- RT antitrypsin."; RL Genomics 6:100-104(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/J; RX MEDLINE=22296988; PubMed=12408969; DOI=10.1016/S0888-7543(02)96864-3; RA Barbour K.W., Wei F., Brannan C., Flotte T.R., Baumann H., RA Berger F.G.; RT "The murine alpha(1)-proteinase inhibitor gene family: polymorphism, RT chromosomal location, and structure."; RL Genomics 80:515-522(2002). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 12-413. RC STRAIN=C57BL/6; TISSUE=Liver; RX MEDLINE=92052104; PubMed=1946354; RA Borriello F., Krauter K.S.; RT "Multiple murine alpha 1-protease inhibitor genes show unusual RT evolutionary divergence."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9417-9421(1991). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=96190670; PubMed=8619829; DOI=10.1006/bbrc.1996.0182; RA Paterson T., Moore S.; RT "The expression and characterization of five recombinant murine alpha RT 1-protease inhibitor proteins."; RL Biochem. Biophys. Res. Commun. 219:64-69(1996). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND REGION RCL. RX MEDLINE=21959334; PubMed=11961105; RA Barbour K.W., Goodwin R.L., Guillonneau F., Wang Y., Baumann H., RA Berger F.G.; RT "Functional diversification during evolution of the murine alpha(1)- RT proteinase inhibitor family: role of the hypervariable reactive center RT loop."; RL Mol. Biol. Evol. 19:718-727(2002). RN [7] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=12659817; DOI=10.1016/S0888-7543(02)00041-1; RA Forsyth S., Horvath A., Coughlin P.; RT "A review and comparison of the murine alpha1-antitrypsin and alpha1- RT antichymotrypsin multigene clusters with the human clade A serpins."; RL Genomics 81:336-345(2003). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-265, AND MASS RP SPECTROMETRY. 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). CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is CC elastase, but it also has a moderate affinity for plasmin and CC thrombin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). Variability within the reactive center loop (RCL) CC sequences of Serpina1-related genes may determine target protease CC specificity. CC -!- MISCELLANEOUS: Murine alpha-1-antitrypsin is represented by a CC cluster of up to 5 individual Serpina1-related genes. The precise CC complement of Serpina1-related genes present varies according to CC the strain of the animal. While all strains seem to express CC Serpina1a and Serpina1b, individual strains may express either CC Spi1-6 alone or the three serpins Serpina1c, Serpina1d and CC Serpina1e together. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M25529; AAA37132.1; -; mRNA. DR EMBL; AF481949; AAM47489.1; -; Genomic_DNA. DR EMBL; BC022109; AAH22109.1; -; mRNA. DR EMBL; BC025445; AAH25445.1; -; mRNA. DR EMBL; BC049255; AAH49255.2; -; mRNA. DR EMBL; M75716; AAC28865.1; -; mRNA. DR PIR; I49452; I49452. DR PIR; I49471; I49471. DR UniGene; Mm.312593; -. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR Ensembl; ENSMUSG00000058326; Mus musculus. DR KEGG; mmu:20701; -. DR MGI; MGI:891970; Serpina1b. DR ArrayExpress; P22599; -. DR GermOnline; ENSMUSG00000071178; Mus musculus. DR RZPD-ProtExp; IOM16662; -. DR RZPD-ProtExp; IOM16665; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL 1 24 By similarity. FT CHAIN 25 413 Alpha-1-antitrypsin 1-2. FT /FTId=PRO_0000032389. FT REGION 368 387 RCL. FT SITE 377 378 Reactive bond (By similarity). FT CARBOHYD 64 64 N-linked (GlcNAc...) (Potential). FT CARBOHYD 101 101 N-linked (GlcNAc...). FT CARBOHYD 265 265 N-linked (GlcNAc...). FT CONFLICT 18 18 M -> L (in Ref. 1, 2 and 3; AAH22109/ FT AAH25445/AAH49255). FT CONFLICT 203 203 A -> G (in Ref. 1). FT CONFLICT 240 240 M -> T (in Ref. 1, 2 and 3; AAH22109/ FT AAH25445/AAH49255). FT CONFLICT 252 252 I -> T (in Ref. 1, 2 and 3; AAH22109/ FT AAH25445/AAH49255). FT CONFLICT 263 263 A -> V (in Ref. 2 and 3; AAH22109/ FT AAH25445/AAH49255). FT CONFLICT 286 286 N -> S (in Ref. 2 and 3; AAH22109/ FT AAH25445/AAH49255). FT CONFLICT 298 298 R -> H (in Ref. 2 and 3; AAH22109/ FT AAH25445/AAH49255). FT CONFLICT 314 314 D -> E (in Ref. 1). SQ SEQUENCE 413 AA; 45975 MW; 92BD12B6D4768D7B CRC64; MTPSISWGLL LLAGLCCMVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HKSFQHLLQT LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE KGTQGKIVEA VKELDQDTVF ALANYILFKG KWKKPFDPEN TEEAEFHVDK STTVKVPMMM LSGMLDVHHC SILSSWVLLM DYAGNASAVF LLPEDGKMQH LEQTLNKELI SKILLNRRRR LVQIHIPRLS ISGDYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSK AVHKAVLTID ETGTEAAAAT VFEAVPMSMP PILRFDHPFL FIIFEEHTQS PIFVGKVVDP THK // ID A1AT3_MOUSE Reviewed; 413 AA. AC Q00896; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 06-FEB-2007, entry version 50. DE Alpha-1-antitrypsin 1-3 precursor (Serine protease inhibitor 1-3) DE (Alpha-1 protease inhibitor 3). GN Name=Serpina1c; Synonyms=Dom3, Spi1-3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RX MEDLINE=92052104; PubMed=1946354; RA Borriello F., Krauter K.S.; RT "Multiple murine alpha 1-protease inhibitor genes show unusual RT evolutionary divergence."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9417-9421(1991). RN [2] RP FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=96190670; PubMed=8619829; DOI=10.1006/bbrc.1996.0182; RA Paterson T., Moore S.; RT "The expression and characterization of five recombinant murine alpha RT 1-protease inhibitor proteins."; RL Biochem. Biophys. Res. Commun. 219:64-69(1996). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, AND REGION RCL. RX MEDLINE=21959334; PubMed=11961105; RA Barbour K.W., Goodwin R.L., Guillonneau F., Wang Y., Baumann H., RA Berger F.G.; RT "Functional diversification during evolution of the murine alpha(1)- RT proteinase inhibitor family: role of the hypervariable reactive center RT loop."; RL Mol. Biol. Evol. 19:718-727(2002). RN [4] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=12659817; DOI=10.1016/S0888-7543(02)00041-1; RA Forsyth S., Horvath A., Coughlin P.; RT "A review and comparison of the murine alpha1-antitrypsin and alpha1- RT antichymotrypsin multigene clusters with the human clade A serpins."; RL Genomics 81:336-345(2003). CC -!- FUNCTION: Inhibitor of serine proteases. Can inhibit trypsin and CC chymotrypsin; relatively ineffective against elastase. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). Variability within the reactive center loop (RCL) CC sequences of Serpina1-related genes may determine target protease CC specificity. CC -!- MISCELLANEOUS: Murine alpha-1-antitrypsin is represented by a CC cluster of up to 5 individual Serpina1-related genes. The precise CC complement of Serpina1-related genes present varies according to CC the strain of the animal. While all strains seem to express CC Serpina1a and Serpina1b, individual strains may express either CC Spi1-6 alone or the three serpins Serpina1c, Serpina1d and CC Serpina1e together. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M75720; AAC28868.1; -; mRNA. DR PIR; I49472; I49472. DR UniGene; Mm.312593; -. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR REPRODUCTION-2DPAGE; Q00896; MOUSE. DR Ensembl; ENSMUSG00000059035; Mus musculus. DR KEGG; mmu:20702; -. DR MGI; MGI:891969; Serpina1c. DR ArrayExpress; Q00896; -. DR GermOnline; ENSMUSG00000066366; Mus musculus. DR RZPD-ProtExp; IOM16662; -. DR RZPD-ProtExp; IOM16665; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 413 Alpha-1-antitrypsin 1-3. FT /FTId=PRO_0000032390. FT REGION 368 387 RCL. FT SITE 377 378 Reactive bond (By similarity). FT CARBOHYD 64 64 N-linked (GlcNAc...) (Potential). FT CARBOHYD 101 101 N-linked (GlcNAc...) (Potential). FT CARBOHYD 265 265 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 413 AA; 45854 MW; 7EAD710919EA1C5B CRC64; MTPSISWGLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HKSFQHLLQT LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE KGTQGKIAEA VKKLDQDTVF ALANYILFKG KWKKPFDPEN TEEAEFHVDE STTVKVPMMT LSGMLDVHHC STLSSWVLLM DYAGNATAVF LLPDDGKMQH LEQTLSKELI SKFLLKRPRR LAQIHFPRLS ISGEYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSQ AVHKAVLTMD ETGTEAAAAT VLLAVPYSMP PIVRFDHPFL FIIFEEHTQS PLFVGKVVDP THK // ID A1AT4_MOUSE Reviewed; 413 AA. AC Q00897; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 52. DE Alpha-1-antitrypsin 1-4 precursor (Serine protease inhibitor 1-4) DE (Alpha-1 protease inhibitor 4). GN Name=Serpina1d; Synonyms=Dom4, Spi1-4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RX MEDLINE=92052104; PubMed=1946354; RA Borriello F., Krauter K.S.; RT "Multiple murine alpha 1-protease inhibitor genes show unusual RT evolutionary divergence."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9417-9421(1991). 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 FUNCTION, AND SUBCELLULAR LOCATION. RX MEDLINE=96190670; PubMed=8619829; DOI=10.1006/bbrc.1996.0182; RA Paterson T., Moore S.; RT "The expression and characterization of five recombinant murine alpha RT 1-protease inhibitor proteins."; RL Biochem. Biophys. Res. Commun. 219:64-69(1996). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND REGION RCL. RX MEDLINE=21959334; PubMed=11961105; RA Barbour K.W., Goodwin R.L., Guillonneau F., Wang Y., Baumann H., RA Berger F.G.; RT "Functional diversification during evolution of the murine alpha(1)- RT proteinase inhibitor family: role of the hypervariable reactive center RT loop."; RL Mol. Biol. Evol. 19:718-727(2002). RN [5] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=12659817; DOI=10.1016/S0888-7543(02)00041-1; RA Forsyth S., Horvath A., Coughlin P.; RT "A review and comparison of the murine alpha1-antitrypsin and alpha1- RT antichymotrypsin multigene clusters with the human clade A serpins."; RL Genomics 81:336-345(2003). CC -!- FUNCTION: Inhibitor of serine proteases. Can inhibit trypsin and CC chymotrypsin; relatively ineffective against elastase. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). Variability within the reactive center loop (RCL) CC sequences of Serpina1-related genes may determine target protease CC specificity. CC -!- MISCELLANEOUS: Murine alpha-1-antitrypsin is represented by a CC cluster of up to 5 individual Serpina1-related genes. The precise CC complement of Serpina1-related genes present varies according to CC the strain of the animal. While all strains seem to express CC Serpina1a and Serpina1b, individual strains may express either CC Spi1-6 alone or the three serpins Serpina1c, Serpina1d and CC Serpina1e together. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M75718; AAC28867.1; -; mRNA. DR EMBL; AK002537; BAB22173.1; -; mRNA. DR PIR; I49473; I49473. DR UniGene; Mm.312593; -. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR Ensembl; ENSMUSG00000057255; Mus musculus. DR KEGG; mmu:20703; -. DR MGI; MGI:891968; Serpina1d. DR GermOnline; ENSMUSG00000071177; Mus musculus. DR RZPD-ProtExp; IOM14920; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 413 Alpha-1-antitrypsin 1-4. FT /FTId=PRO_0000032391. FT REGION 368 387 RCL. FT SITE 377 378 Reactive bond (By similarity). FT CARBOHYD 64 64 N-linked (GlcNAc...) (Potential). FT CARBOHYD 101 101 N-linked (GlcNAc...) (Potential). FT CARBOHYD 265 265 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 413 AA; 45998 MW; D8A90477F371A902 CRC64; MTPSISWSLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FALRLYRELV HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HKSFQHLLQT LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE KGTQGKIVEA VKKLDQDTVF ALANYILFKG KWKQPFDPEN TEEAEFHVDE STTVKVPMMT LSGMLDVHHC SMLSSWVLLM DYAGNTTAVF LLPDDGKMQH LEQTLNKELI SQFLLNRRRS DAQIHIPRLS ISGNYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSK AVHKAVLTID ETGTEAAAAT VLQVATYSMP PIVRFDHPFL FIIFEEHTQS PIFVGKVVDP THK // ID A1AT5_MOUSE Reviewed; 413 AA. AC Q00898; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 52. DE Alpha-1-antitrypsin 1-5 precursor (Serine protease inhibitor 1-5) DE (Alpha-1 protease inhibitor 5). GN Name=Serpina1e; Synonyms=Dom5, Spi1-5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RX MEDLINE=92052104; PubMed=1946354; RA Borriello F., Krauter K.S.; RT "Multiple murine alpha 1-protease inhibitor genes show unusual RT evolutionary divergence."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9417-9421(1991). 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 SUBCELLULAR LOCATION. RX MEDLINE=96190670; PubMed=8619829; DOI=10.1006/bbrc.1996.0182; RA Paterson T., Moore S.; RT "The expression and characterization of five recombinant murine alpha RT 1-protease inhibitor proteins."; RL Biochem. Biophys. Res. Commun. 219:64-69(1996). RN [4] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=12659817; DOI=10.1016/S0888-7543(02)00041-1; RA Forsyth S., Horvath A., Coughlin P.; RT "A review and comparison of the murine alpha1-antitrypsin and alpha1- RT antichymotrypsin multigene clusters with the human clade A serpins."; RL Genomics 81:336-345(2003). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64, AND MASS SPECTROMETRY. 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). CC -!- FUNCTION: Does not inhibit elastase or chymotrypsin. No target CC protease has been identified to date. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the serpin reactive site CC and the active site of the protease. The resulting inactive CC serpin-protease complex is highly stable (By similarity). CC Variability within the reactive center loop (RCL) sequences of CC Serpina1-related genes may determine target protease specificity. CC -!- MISCELLANEOUS: Murine alpha-1-antitrypsin is represented by a CC cluster of up to 5 individual Serpina1-related genes. The precise CC complement of Serpina1-related genes present varies according to CC the strain of the animal. While all strains seem to express CC Serpina1a and Serpina1b, individual strains may express either CC Spi1-6 alone or the three serpins Serpina1c, Serpina1d and CC Serpina1e together. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M75717; AAC28866.1; -; mRNA. DR EMBL; BC061176; AAH61176.1; -; mRNA. DR PIR; I49474; I49474. DR UniGene; Mm.312593; -. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR Ensembl; ENSMUSG00000064111; Mus musculus. DR KEGG; mmu:20704; -. DR MGI; MGI:891967; Serpina1e. DR GermOnline; ENSMUSG00000072849; Mus musculus. DR RZPD-ProtExp; IOM16662; -. DR RZPD-ProtExp; IOM16665; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 413 Alpha-1-antitrypsin 1-5. FT /FTId=PRO_0000032392. FT REGION 368 387 RCL. FT SITE 377 378 Reactive bond (By similarity). FT CARBOHYD 64 64 N-linked (GlcNAc...). FT CARBOHYD 101 101 N-linked (GlcNAc...) (Potential). FT CARBOHYD 265 265 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 413 AA; 45891 MW; 42331F107CA06C55 CRC64; MTPSISWCLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HNSFQHLLQT LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE KGTQGKIVEA VKKLEQDTVF VLANYILFKG KWKKPFDPEN TKQAEFHVDE STTVKVPMMT LSGMLDVHHC STLSSWVLLM DYAGNATAVF LLPDDGKMQH LEQTLNKELI SKFLLNRRRR LAQIHIPRLS ISGNYNLETL MSPLGITRIF NSGADLSGIT EENAPLKLSQ AVHKAVLTID ETGTEAAAAT VLQGGFLSMP PILHFNRPFL FIIFEEHSQS PLFVGKVVDP THK // ID A1AT6_MOUSE Reviewed; 412 AA. AC P81105; Q91V74; Q91WH5; Q91XC1; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 20-FEB-2007, entry version 48. DE Alpha-1-antitrypsin 1-6 precursor (Serine protease inhibitor 1-6) DE (Alpha-1 protease inhibitor 6). GN Name=Spi1-6; Synonyms=Dom6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; 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). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-412. RX MEDLINE=84295637; PubMed=6547997; DOI=10.1038/311175a0; RA Hill R.E., Shaw P.H., Boyd P.A., Baumann H., Hastie N.D.; RT "Plasma protease inhibitors in mouse and man: divergence within the RT reactive centre regions."; RL Nature 311:175-177(1984). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, AND REGION RCL. RX MEDLINE=21959334; PubMed=11961105; RA Barbour K.W., Goodwin R.L., Guillonneau F., Wang Y., Baumann H., RA Berger F.G.; RT "Functional diversification during evolution of the murine alpha(1)- RT proteinase inhibitor family: role of the hypervariable reactive center RT loop."; RL Mol. Biol. Evol. 19:718-727(2002). RN [4] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=12659817; DOI=10.1016/S0888-7543(02)00041-1; RA Forsyth S., Horvath A., Coughlin P.; RT "A review and comparison of the murine alpha1-antitrypsin and alpha1- RT antichymotrypsin multigene clusters with the human clade A serpins."; RL Genomics 81:336-345(2003). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265, AND MASS RP SPECTROMETRY. 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). CC -!- FUNCTION: Inhibitor of serine proteases. Can inhibit trypsin and CC chymotrypsin; relatively ineffective against elastase. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the serpin reactive site CC and the active site of the protease. The resulting inactive CC serpin-protease complex is highly stable (By similarity). CC Variability within the reactive center loop (RCL) sequences of CC Serpina1-related genes may determine target protease specificity. CC -!- MISCELLANEOUS: Murine alpha-1-antitrypsin is represented by a CC cluster of up to 5 individual Serpina1-related genes. The precise CC complement of Serpina1-related genes present varies according to CC the strain of the animal. While all strains seem to express CC Serpina1a and Serpina1b, individual strains may express either CC Spi1-6 alone or the three serpins Serpina1c, Serpina1d and CC Serpina1e together. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC009818; AAH09818.1; -; mRNA. DR EMBL; BC010984; AAH10984.1; -; mRNA. DR EMBL; BC010988; AAH10988.1; -; mRNA. DR EMBL; BC011041; AAH11041.1; -; mRNA. DR EMBL; BC015266; AAH15266.1; -; mRNA. DR EMBL; BC021325; AAH21325.1; -; mRNA. DR EMBL; BC021780; AAH21780.1; -; mRNA. DR EMBL; BC024108; AAH24108.1; -; mRNA. DR EMBL; BC031707; AAH31707.1; -; mRNA. DR EMBL; X00945; CAA25457.1; -; Genomic_DNA. DR UniGene; Mm.312593; -. DR HSSP; P01009; 1QMB. DR MGI; MGI:891966; Spi1-6. DR ArrayExpress; P81105; -. DR GermOnline; ENSMUSG00000066366; Mus musculus. DR RZPD-ProtExp; IOM16662; -. DR RZPD-ProtExp; IOM16665; -. DR InterPro; IPR000215; Prot_inh_serpin. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 412 Alpha-1-antitrypsin 1-6. FT /FTId=PRO_0000032393. FT REGION 368 387 RCL. FT SITE 377 378 Reactive bond. FT CARBOHYD 64 64 N-linked (GlcNAc...) (Potential). FT CARBOHYD 101 101 N-linked (GlcNAc...) (Potential). FT CARBOHYD 265 265 N-linked (GlcNAc...). FT CONFLICT 1 1 M -> HASGDLELADAWV (in Ref. 1; AAH10988). FT CONFLICT 188 188 V -> A (in Ref. 1; AAH10988). SQ SEQUENCE 412 AA; 45823 MW; FFA3BF10ABC1B8AE CRC64; MTPSISWGLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HKSFQHLLQT LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE KGTQGKIVEA VKKLDQDTVF ALANYILFKG KWKKPFDPEN TEEAEFHVDE STTVKVPMMT LSGMLDVHHC STLSSWVLLM DYAGNATAVF LLPDDGKMQH LEQTLSKELI SKFLLNRRRR LAQIHFPRLS ISGEYNLKTL MSPLGITRIF NNGADLSGIT EENAPLKLSQ AVHKAVLTID ETGTEAAAVT VLLAVPYSMP PILRFDHPFL FIIFEEHTQS PLFVGKVVDP TH // ID A1ATR_HUMAN Reviewed; 420 AA. AC P20848; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 20-FEB-2007, entry version 60. DE Alpha-1-antitrypsin-related protein precursor. GN Name=SERPINA2; Synonyms=ARGS, ATR, PIL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88314108; PubMed=2842251; RA Bao J.J., Reed-Fourquet L., Sifers R.N., Kidd V.J., Woo S.L.C.; RT "Molecular structure and sequence homology of a gene related to alpha RT 1-antitrypsin in the human genome."; RL Genomics 2:165-173(1988). CC -!- FUNCTION: Could be a serine protease inhibitor. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC -!- CAUTION: Could be the product of a pseudogene. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M19684; AAA51544.1; -; Genomic_DNA. DR EMBL; M19685; AAA51544.1; JOINED; Genomic_DNA. DR PIR; A28882; A28882. DR UniGene; Hs.525557; -. DR HSSP; P01009; 1QMB. DR MEROPS; I04.952; -. DR Ensembl; ENSG00000165951; Homo sapiens. DR HGNC; HGNC:8985; SERPINA2. DR MIM; 107410; gene. DR LinkHub; P20848; -. DR ArrayExpress; P20848; -. DR GermOnline; ENSG00000165951; Homo sapiens. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:ProtInc. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 420 Alpha-1-antitrypsin-related protein. FT /FTId=PRO_0000032410. FT SITE 384 385 Reactive bond (Potential). FT CARBOHYD 56 56 N-linked (GlcNAc...) (Potential). FT CARBOHYD 109 109 N-linked (GlcNAc...) (Potential). FT CARBOHYD 147 147 N-linked (GlcNAc...) (Potential). FT CARBOHYD 273 273 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 420 AA; 47891 MW; 4A5A7B9BE05BCEAA CRC64; MPFSVSWGVL LLAGLCCLVP SSLVEDPQGD AAQKTDTSHH DQGDWEDLAC QKISYNVTDL AFDLYKSWLI YHNQHVLVTP TSVAMAFRML SLGTKADTRT EILEGLNVNL TETPEAKIHE CFQQVLQALS RPDTRLQLTT GSSLFVNKSM KLVDTFLEDT KKLYHSEASS INFRDTEEAK EQINNYVEKR TGRKVVDLVK HLKKDTSLAL VDYISFHGKW KDKFKAERIM VEGFHVDDKT IIRVPMINHL GRFDIHRDRE LSSWVLAQHY VGNATAFFIL PDPKKMWQLE EKLTYSHLEN IQRAFDIRSI NLHFPKLSIS GTYKLKRVPR NLGITKIFSN EADLSGVSQE APLKLSKAVH VAVLTIDEKG TEATGAPHLE EKAWSKYQTV MFNRPFLVII KEYITNFPLF IGKVVNPTQK // ID A1AT_BOMMO Reviewed; 392 AA. AC P22922; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 20-FEB-2007, entry version 47. DE Antitrypsin precursor (AT). OS Bombyx mori (Silk moth). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Bombycidae; Bombyx. OX NCBI_TaxID=7091; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 17-47. RC TISSUE=Larval fat body; RX MEDLINE=91115781; PubMed=2277028; RA Takagi H., Narumi H., Nakamura K., Sasaki T.; RT "Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin RT deduced from its cDNA nucleotide sequence: confirmation of its RT homology with serpins."; RL J. Biochem. 108:372-378(1990). RN [2] RP PROTEIN SEQUENCE OF 352-376. RX MEDLINE=90344221; PubMed=1368515; RA Sasaki T., Kohara A., Takagi H., Shimidzu T.; RT "Limited proteolysis of silkworm antitrypsin by several proteinases."; RL Agric. Biol. Chem. 54:131-137(1990). CC -!- FUNCTION: May play a role in the prophenoloxydase activating CC system in the silkworm hemolymph. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Hemolymph. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the serpin reactive site CC and the active site of the protease. The resulting inactive CC serpin-protease complex is highly stable (By similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D00738; BAA00639.1; -; mRNA. DR UniGene; Bmo.2083; -. DR HSSP; P14754; 1SEK. DR MEROPS; I04.031; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Direct protein sequencing; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL 1 16 FT CHAIN 17 392 Antitrypsin. FT /FTId=PRO_0000032408. FT SITE 359 360 Reactive bond. SQ SEQUENCE 392 AA; 43499 MW; 2A40C345D94B1095 CRC64; MKTIICLFTI AIAAMAAVTN LSNVLKNGND NFTARMFTEV VKNNPGKSIV LSAFSVLPPL AQLALASDGE THEELLKAIG FPDDDAIRTE FASKSRDLRS IKGVELKMAN KVYVHDGGKL DENFAVVSRD VFNSDVQNID FSKNTVAAKS INDWVEENTN NRIKDLVNPD SLSSATAAVL VNAIYFKGAW SSKFDERLTS DRDFYVSKDK TIKVPMMYKR GDYKYGESAV LNAQLIEIPY KGDQSSLIVV LPKDKDGITQ LQEALKDPKT LETAQQSMYS TEVDLYLPKF KIETETNLKD VLSNMNVNKI FNNDAQITRL LKGESLSVSE AIQKAFIEIN EEGAEAAAAN AFTMTRSSKV YVRPPIVFNA NKPFYYALQV DGVIMFNGIF IN // ID A1AT_BOVIN Reviewed; 416 AA. AC P34955; Q3SZS3; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 31-OCT-2006, entry version 51. DE Alpha-1-antiproteinase precursor (Alpha-1-antitrypsin) (Alpha-1- DE proteinase inhibitor). GN Name=SERPINA1; Synonyms=PI; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=92223096; PubMed=1562597; DOI=10.1016/0167-4781(92)90530-D; RA Sinha D., Bakhshi M.R., Kirby E.P.; RT "Complete cDNA sequence of bovine alpha 1-antitrypsin."; RL Biochim. Biophys. Acta 1130:209-212(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP CHARACTERIZATION. RX PubMed=8056747; RA Sinha D., Yang X., Emig F., Kirby E.P.; RT "Isolation and characterization of two protease inhibitors from bovine RT plasma."; RL J. Biochem. 115:387-391(1994). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X63129; CAA44840.1; -; mRNA. DR EMBL; BT025459; ABF57415.1; -; mRNA. DR EMBL; BC102730; AAI02731.1; -; mRNA. DR PIR; S21097; S21097. DR UniGene; Bt.982; -. DR HSSP; P01009; 1QMB. DR SMR; P34955; 46-415. DR MEROPS; I04.001; -. DR KEGG; bta:280699; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 By similarity. FT CHAIN 25 416 Alpha-1-antiproteinase. FT /FTId=PRO_0000032380. FT REGION 371 390 RCL. FT SITE 380 381 Reactive bond. FT CARBOHYD 68 68 N-linked (GlcNAc...) (Potential). FT CARBOHYD 105 105 N-linked (GlcNAc...) (Potential). FT CARBOHYD 143 143 N-linked (GlcNAc...) (Potential). FT CARBOHYD 269 269 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 416 AA; 46104 MW; 3280CDAF42DA35E2 CRC64; MALSITRGLL LLAALCCLAP ISLAGVLQGH AVQETDDTSH QEAACHKIAP NLANFAFSIY HHLAHQSNTS NIFFSPVSIA SAFAMLSLGA KGNTHTEILK GLGFNLTELA EAEIHKGFQH LLHTLNQPNH QLQLTTGNGL FINESAKLVD TFLEDVKNLY HSEAFSINFR DAEEAKKKIN DYVEKGSHGK IVELVKVLDP NTVFALVNYI SFKGKWEKPF EMKHTTERDF HVDEQTTVKV PMMNRLGMFD LHYCDKLASW VLLLDYVGNV TACFILPDLG KLQQLEDKLN NELLAKFLEK KYASSANLHL PKLSISETYD LKSVLGDVGI TEVFSDRADL SGITKEQPLK VSKALHKAAL TIDEKGTEAV GSTFLEAIPM SLPPDVEFNR PFLCILYDRN TKSPLFVGKV VNPTQA // ID A1AT_CALCN Reviewed; 412 AA. AC O54763; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 31-OCT-2006, entry version 42. DE Alpha-1-antiproteinase precursor (Alpha-1-antitrypsin) (Alpha-1- DE proteinase inhibitor). OS Callosciurus caniceps (Gray-bellied squirrel). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Sciuridae; Callosciurinae; Callosciurini; Callosciurus. OX NCBI_TaxID=64664; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=98094263; PubMed=9434174; DOI=10.1016/S0378-1119(97)00532-5; RA Takamatsu N., Kojima M., Taniyama M., Ohba K., Uematsu T., Segawa C., RA Tsutou S., Watanabe M., Kondo J., Kondo N., Shiba T.; RT "Expression of multiple alpha1-antitrypsin-like genes in hibernating RT species of the squirrel family."; RL Gene 204:127-132(1997). CC -!- FUNCTION: Inhibitor of serine proteases (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB000552; BAA24422.1; -; mRNA. DR HSSP; P01009; 1QMB. DR SMR; O54763; 38-412. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 412 Alpha-1-antiproteinase. FT /FTId=PRO_0000032383. FT REGION 368 387 RCL. FT SITE 377 378 Reactive bond (By similarity). FT CARBOHYD 65 65 N-linked (GlcNAc...) (Potential). FT CARBOHYD 102 102 N-linked (GlcNAc...) (Potential). FT CARBOHYD 165 165 N-linked (GlcNAc...) (Potential). FT CARBOHYD 266 266 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 412 AA; 45729 MW; 7235668E9EE8FCC6 CRC64; MPSSISWGLL LLAGLCCLAP GSLAGDAQET DASKDDHEHP ACHKIAPNLA EFAFDLYRVL ARQSNTTNIF FSPVSVATAL AALSLGTKGD THTQILEGLD FNLTEMAETD IHQGFQHLLQ TLNRPNNQLQ LTTGNGLFID QSLKLADKFL EDVKNLYHSE AFSTNFTDSE EAKKQINGYV EKGTQGKIVD AVKTLDKNTV FALVNYIFFK GKWEKPFEVE HTTEGDFHVD QATTVKVPMM NRLGRFDLLY CTTLASWVLQ MDYLGNATAI FLLPDEGKLQ HLEDTITKEI LSKFLKNRHT RTVNLYFPKL SITGTYDLRS VLSTLGITKV FSNEADLSGV TEEAPLKLSK GVHKAVLTID ERGTEAAGVT VLEAIPMSLP PDVRFDRPFL IIIYEHYTKS PLFVGKVVNP TQ // ID A1AT_CERAE Reviewed; 396 AA. AC O00394; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 31-OCT-2006, entry version 37. DE Alpha-1-antitrypsin precursor (Alpha-1 protease inhibitor) (Alpha-1- DE antiproteinase) (Fragment). GN Name=SERPINA1; OS Cercopithecus aethiops (Green monkey) (Grivet). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=9534; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RA Yoshida K., Suzuki Y., Yamamoto K., Watanabe M., Sinohara H.; RT "Cloning and sequencing of complementary DNAs encoding alpha-2-HS RT glycoprotein, alpha-1-antitrypsin, and beta-actin from African green RT monkey, Cercopithecus aethiops."; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is CC elastase, but it also has a moderate affinity for plasmin and CC thrombin (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB004044; BAA20264.1; -; mRNA. DR HSSP; P01009; 1EZX. DR SMR; O00394; 25-396. DR MEROPS; I04.001; -. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB. DR GO; GO:0030162; P:regulation of proteolysis; NAS:UniProtKB. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL <1 2 Potential. FT CHAIN 3 396 Alpha-1-antitrypsin. FT /FTId=PRO_0000032376. FT REGION 351 370 RCL. FT SITE 360 361 Reactive bond (By similarity). FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT CARBOHYD 85 85 N-linked (GlcNAc...) (Potential). FT CARBOHYD 123 123 N-linked (GlcNAc...) (Potential). FT CARBOHYD 249 249 N-linked (GlcNAc...) (Potential). FT NON_TER 1 1 SQ SEQUENCE 396 AA; 44587 MW; 1042EABFAA0A2825 CRC64; HVEDPQGDAA QKTDTSHHDQ EHSTFNKITP SLAEFAFSLY RQLAHQSNST NIFFSPVSIA TAFAMLSLGT KADTHSEILE GLNFNLTEIP EAQIHEGFQE LLHTLNKPDS QLQLTTGNGL FLNKSVKVVD KFLEDVKKLY HSEAFSVNFE DTEEAKKQIN NYVEKGTQGK IVDLVKELDR DTVFALVNYI FFKGKWERPF EVEATKEEDF HVDQATTVKV PMMRRLGMFN IYHCEKLSSW VLLMKYLGNA TAIFFLPDEG KLQHLENELT HDIITKFLEN ENRRSANLHL PKLAITGTYD LKTVLGHLGI TKVFSNGADL SGVTEDAPLK LSKAVHKAVL TIDEKGTEAA GAMFLEAIPM SIPPEVKFNK PFVFLMIEQN TKSPLFMGKV VNPTQK // ID A1AT_CHIVI Reviewed; 30 AA. AC P38026; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 31-OCT-2006, entry version 38. DE Alpha-1-antiproteinase (Alpha-1-antitrypsin) (Alpha-1-proteinase DE inhibitor) (Fragment). OS Chinchilla villidera (Chinchilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Chinchillidae; Chinchilla. OX NCBI_TaxID=37013; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Plasma; RX MEDLINE=90235555; PubMed=2184987; RA Diven W.F., Vietmeier B., Hempel J., Chambers J.; RT "Purification and N-terminal characterization of Chinchilla villidera RT alpha-1-antitrypsin."; RL Comp. Biochem. Physiol. 95B:39-44(1990). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- PTM: N-glycosylated; contains bi- and triantennary glycans. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PROSITE; PS00284; SERPIN; PARTIAL. KW Acute phase; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor. FT CHAIN 1 >30 Alpha-1-antiproteinase. FT /FTId=PRO_0000094091. FT NON_TER 30 30 SQ SEQUENCE 30 AA; 3411 MW; C590F933E9B1E5DE CRC64; EDAQVTDLPD HEQEHLAXHK IAPXLAEFAY // ID A1AT_CYPCA Reviewed; 372 AA. AC P32759; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 31-OCT-2006, entry version 42. DE Alpha-1-antitrypsin homolog precursor. OS Cyprinus carpio (Common carp). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Cyprinus. OX NCBI_TaxID=7962; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cerebrospinal fluid; RX MEDLINE=95198028; PubMed=7891100; RA Huang C.-J., Lee M.S., Huang F.-L., Chang G.D.; RT "A protease inhibitor of the serpin family is a major protein in carp RT perimeningeal fluid: II. cDNA cloning, sequence analysis, and RT Escherichia coli expression."; RL J. Neurochem. 64:1721-1727(1995). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the serpin reactive site CC and the active site of the protease. The resulting inactive CC serpin-protease complex is highly stable (By similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L08689; AAA73953.1; -; mRNA. DR PIR; I50492; I50492. DR HSSP; P01009; 1QMB. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 19 Potential. FT CHAIN 20 372 Alpha-1-antitrypsin homolog. FT /FTId=PRO_0000032407. FT REGION 328 347 RCL. FT SITE 337 338 Reactive bond (By similarity). FT CARBOHYD 214 214 N-linked (GlcNAc...) (Potential). FT CARBOHYD 226 226 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 372 AA; 41900 MW; D5D67E3E40A91EE9 CRC64; MPATCLLHTM LTLPSPSTRN LRSIQMPRAR TFSSPSRYRN GFEHAGCRCQ GSTLSQIYSS LGYSGLQASQ VNEGYEHLIH MLGHSREAMQ LEAGAGVAIR EGFKVVDQFL KDVQHYYNSE AFSVDFSKPE IAAEEINQFI AKKTNDKITN MVKDLDSDTV MMLINYMYFR GKWDKPFDAQ LTHKADFKVD EDTTVQVDMM KRTGRYDIYQ DPVNQTTVMM VPYKGNTSMM IIFPDDGKMK ELEESISRHH LKNWHDKLFR SSVDLFMPKF SITATSKLKG ILEDMGVTDA FGDTADLSGL TEEVKVKVSQ VVHKAVLSVD EKGTEAAAAT TIEIMPMSLP DTVILNRPFL VLIVEDTTKS ILFMGKITNP TE // ID A1AT_DIDMA Reviewed; 410 AA. AC Q03044; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 31-OCT-2006, entry version 45. DE Alpha-1-antiproteinase precursor (Alpha-1-antitrypsin) (Alpha-1- DE proteinase inhibitor). OS Didelphis marsupialis virginiana (North American opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Didelphis. OX NCBI_TaxID=9267; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-37 AND 127-146. RC TISSUE=Liver; RX MEDLINE=93136143; PubMed=8422360; DOI=10.1021/bi00053a015; RA Catanese J.J., Kress L.F.; RT "Opossum serum alpha 1-proteinase inhibitor: purification, linear RT sequence, and resistance to inactivation by rattlesnake venom RT metalloproteinases."; RL Biochemistry 32:509-515(1993). CC -!- FUNCTION: Inhibitor of serine proteases. The primary target is CC elastase, but also has a moderate affinity for plasmin and CC thrombin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z18906; CAA79343.1; -; mRNA. DR EMBL; L06824; AAC02630.1; -; mRNA. DR PIR; A45457; A45457. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; FALSE_NEG. KW Acute phase; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 21 FT CHAIN 22 410 Alpha-1-antiproteinase. FT /FTId=PRO_0000032384. FT REGION 365 384 RCL. FT SITE 374 375 Reactive bond (By similarity). FT CARBOHYD 63 63 N-linked (GlcNAc...) (Potential). FT CARBOHYD 100 100 N-linked (GlcNAc...) (Potential). FT CARBOHYD 264 264 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 410 AA; 46441 MW; 2A6718C1B2FAA389 CRC64; MMPSTLSLCL MLAGLCSLVT SHLTEEIQAS NDTENEYSST RRISPYMTDF SIDFYRLLVS KSNTTNIFFS PISIYTAFTL LALGAKSATR DQILTGLRFN RTEISEEHIF EGFQQLLNTF NLPENELQLT TSNGLFIDKN LKLVAKFLED SKRLYASDTF STNFEDNMAA KKQINDYVEK ETQGKIVDLI QNLDSNVVFV LVNCIFFKGK WEKPFMTELT TECPFHVDSK TTVPVQTMRR LGMFNVFYDQ DLSCWVLKMK YMGNATALFI LPDTGKIEKV ENALNKMLFH KWTRNLKRRA ISLYFPKVSI SGNYDLKILR ELGITDVFGS NADLSGITEE TNLKLSQAVH KAVVNIDEKG TEASGATFAE GIPMSIPPTV EFLRPFIFII LEENTKSVLF MGKVMNPTGN // ID A1AT_HUMAN Reviewed; 418 AA. AC P01009; Q13672; Q5U0M1; Q96BF9; Q96ES1; Q9P1P0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 3. DT 20-FEB-2007, entry version 116. DE Alpha-1-antitrypsin precursor (Alpha-1 protease inhibitor) (Alpha-1- DE antiproteinase). GN Name=SERPINA1; Synonyms=AAT, PI; ORFNames=PRO0684, PRO2209; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=84107980; PubMed=6319097; RA Bollen A., Herzog A., Cravador A., Herion P., Chuchana P., RA van der Straten A., Loriau R., Jacobs P., van Elsen A.; RT "Cloning and expression in Escherichia coli of full-length RT complementary DNA coding for human alpha 1-antitrypsin."; RL DNA 2:255-264(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=85047190; PubMed=6093867; DOI=10.1021/bi00316a003; RA Long G.L., Chandra T., Woo S.L.C., Davie E.W., Kurachi K.; RT "Complete sequence of the cDNA for human alpha 1-antitrypsin and the RT gene for the S variant."; RL Biochemistry 23:4828-4837(1984). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF MET-382. RX MEDLINE=85036645; PubMed=6387509; DOI=10.1038/312077a0; RA Rosenberg S., Barr P.J., Najarian R.C., Hallewell R.A.; RT "Synthesis in yeast of a functional oxidation-resistant mutant of RT human alpha-antitrypsin."; RL Nature 312:77-80(1984). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=85176977; PubMed=2985281; RA Ciliberto G., Dente L., Cortese R.; RT "Cell-specific expression of a transfected human alpha 1-antitrypsin RT gene."; RL Cell 41:531-540(1985). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF VARIANT Z. RX MEDLINE=87057257; PubMed=3491072; RA Nukiwa T., Satoh K., Brantly M.L., Ogushi F., Fells G.A., Courtney M., RA Crystal R.G.; RT "Identification of a second mutation in the protein-coding sequence of RT the Z type alpha 1-antitrypsin gene."; RL J. Biol. Chem. 261:15989-15994(1986). RN [6] RP ERRATUM. RA Nukiwa T., Satoh K., Brantly M.L., Ogushi F., Fells G.A., Courtney M., RA Crystal R.G.; RL J. Biol. Chem. 262:10412-10412(1987). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., RA Zhou W., Bi J., Zhang Y., Liu M., He F.; RT "Functional prediction of the coding sequences of 32 new genes deduced RT by analysis of cDNA clones from human fetal liver."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-237. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, and Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67; 196-255 AND 387-418. RX MEDLINE=82220035; PubMed=6979715; DOI=10.1038/297655a0; RA Leicht M., Long G.L., Chandra T., Kurachi K., Kidd V.J., Mace M. Jr., RA Davie E.W., Woo S.L.C.; RT "Sequence homology and structural comparison between the chromosomal RT human alpha 1-antitrypsin and chicken ovalbumin genes."; RL Nature 297:655-659(1982). RN [11] RP PROTEIN SEQUENCE OF 25-418. RX MEDLINE=82220135; PubMed=7045697; DOI=10.1038/298329a0; RA Carrell R.W., Jeppsson J.-O., Laurell C.-B., Brennan S.O., Owen M.C., RA Vaughan L., Boswell D.R.; RT "Structure and variation of human alpha 1-antitrypsin."; RL Nature 298:329-334(1982). RN [12] RP PRELIMINARY PROTEIN SEQUENCE OF 25-418. RA Chan S.K.; RT "The covalent structure of human alpha1-protease inhibitor."; RL Fed. Proc. 41:1016-1016(1982). RN [13] RP PROTEIN SEQUENCE OF 30-48 AND 248-257, GLYCOSYLATION AT ASN-70; RP ASN-107 AND ASN-271, STRUCTURE OF CARBOHYDRATES, CYSTEINE BINDING, AND RP MASS SPECTROMETRY. RX PubMed=16622833; DOI=10.1002/pmic.200500751; RA Kolarich D., Weber A., Turecek P.L., Schwarz H.P., Altmann F.; RT "Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin RT and its charge isoforms."; RL Proteomics 6:3369-3380(2006). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 292-418. RX MEDLINE=86005469; PubMed=3876243; DOI=10.1016/0014-5793(85)81056-5; RA Riley J.H., Bathurst I.C., Edbrooke M.R., Carrell R.W., Craig R.K.; RT "Alpha 1-antitrypsin and serum albumin mRNA accumulation in normal, RT acute phase and ZZ human liver."; RL FEBS Lett. 189:361-366(1985). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 350-418. RX MEDLINE=82082539; PubMed=7031661; RA Kurachi K., Chandra T., Friezner Degen S.J., White T.T., RA Marchioro T.L., Woo S.L.C., Davie E.W.; RT "Cloning and sequence of cDNA coding for alpha 1-antitrypsin."; RL Proc. Natl. Acad. Sci. U.S.A. 78:6826-6830(1981). RN [16] RP NUCLEOTIDE SEQUENCE [MRNA] OF 387-418. RX MEDLINE=85225507; PubMed=3873938; RA Coutelle C., Speer A., Rogers J., Kalsheker N., Humphries S., RA Williamson R.; RT "Construction and partial characterization of a human liver cDNA RT library."; RL Biomed. Biochim. Acta 44:421-431(1985). RN [17] RP GLYCOSYLATION AT ASN-70 AND ASN-271. RX MEDLINE=22660472; PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271, AND MASS RP SPECTROMETRY. RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [19] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271, RP AND MASS SPECTROMETRY. RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70, AND MASS SPECTROMETRY. RX PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200; RA Lewandrowski U., Moebius J., Walter U., Sickmann A.; RT "Elucidation of N-glycosylation sites on human platelet proteins: a RT glycoproteomic approach."; RL Mol. Cell. Proteomics 5:226-233(2006). RN [21] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX MEDLINE=84292309; PubMed=6332197; RA Loebermann H., Tokuoka R., Deisenhofer J., Huber R.; RT "Human alpha 1-proteinase inhibitor. Crystal structure analysis of two RT crystal modifications, molecular model and preliminary analysis of the RT implications for function."; RL J. Mol. Biol. 177:531-556(1984). RN [22] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX MEDLINE=89221004; PubMed=2785270; DOI=10.1093/protein/2.6.407; RA Engh R., Loebermann H., Schneider M., Wiegand G., Huber R., RA Laurell C.-B.; RT "The S variant of human alpha 1-antitrypsin, structure and RT implications for function and metabolism."; RL Protein Eng. 2:407-415(1989). RN [23] RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 25-418. RX MEDLINE=96128217; PubMed=8543039; DOI=10.1016/0014-5793(95)01331-8; RA Song H.K., Lee K.N., Kwon K.-S., Yu M.-H., Suh S.W.; RT "Crystal structure of an uncleaved alpha 1-antitrypsin reveals the RT conformation of its inhibitory reactive loop."; RL FEBS Lett. 377:150-154(1995). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-418. RX MEDLINE=96313123; PubMed=8756325; RA Elliott P.R., Lomas D.A., Carrell R.W., Abrahams J.P.; RT "Inhibitory conformation of the reactive loop of alpha 1- RT antitrypsin."; RL Nat. Struct. Biol. 3:676-681(1996). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 45-418. RX MEDLINE=97094975; PubMed=8939743; DOI=10.1016/S0969-2126(96)00126-8; RA Ryu S.-E., Choi H.-J., Kwon K.-S., Lee K.N., Yu M.-H.; RT "The native strains in the hydrophobic core and flexible reactive loop RT of a serine protease inhibitor: crystal structure of an uncleaved RT alpha1-antitrypsin at 2.7 A."; RL Structure 4:1181-1192(1996). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-418. RX MEDLINE=98139957; PubMed=9466920; DOI=10.1006/jmbi.1997.1458; RA Elliott P.R., Abrahams J.P., Lomas D.A.; RT "Wild-type alpha 1-antitrypsin is in the canonical inhibitory RT conformation."; RL J. Mol. Biol. 275:419-425(1998). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 48-418 IN COMPLEX WITH BOVINE RP TRYPSIN. RX MEDLINE=20509356; PubMed=11057674; DOI=10.1038/35038119; RA Huntington J.A., Read R.J., Carrell R.W.; RT "Structure of a serpin-protease complex shows inhibition by RT deformation."; RL Nature 407:923-926(2000). RN [28] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 44-418. RX MEDLINE=20178938; PubMed=10716194; RA Dunstone M.A., Dai W., Whisstock J.C., Rossjohn J., Pike R.N., RA Feil S.C., Le Bonniec B.F., Parker M.W., Bottomley S.P.; RT "Cleaved antitrypsin polymers at atomic resolution."; RL Protein Sci. 9:417-420(2000). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=20386623; PubMed=10933492; RA Elliott P.R., Pei X.Y., Dafforn T.R., Lomas D.A.; RT "Topography of a 2.0 A structure of alpha1-antitrypsin reveals targets RT for rational drug design to prevent conformational disease."; RL Protein Sci. 9:1274-1281(2000). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-418. RX MEDLINE=21103710; PubMed=11178897; DOI=10.1006/jmbi.2000.4357; RA Kim S.-J., Woo J.-R., Seo E.J., Yu M.-H., Ryu S.-E.; RT "A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin RT shows variability of the reactive center and other loops."; RL J. Mol. Biol. 306:109-119(2001). RN [31] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-418. RX MEDLINE=22336385; PubMed=12244055; DOI=10.1074/jbc.M207682200; RA Im H., Woo M.-S., Hwang K.Y., Yu M.-H.; RT "Interactions causing the kinetic trap in serpin protein folding."; RL J. Biol. Chem. 277:46347-46354(2002). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-418 OF VARIANT PITTSBURGH RP ARG-382. RX MEDLINE=22863108; PubMed=12860985; DOI=10.1074/jbc.M305195200; RA Dementiev A., Simonovic M., Volz K., Gettins P.G.; RT "Canonical inhibitor-like interactions explain reactivity of alpha1- RT proteinase inhibitor Pittsburgh and antithrombin with proteinases."; RL J. Biol. Chem. 278:37881-37887(2003). RN [33] RP REVIEW. RX MEDLINE=89352843; PubMed=2669992; RA Kalsheker N.; RT "Alpha 1-antitrypsin: structure, function and molecular biology of the RT gene."; RL Biosci. Rep. 9:129-138(1989). RN [34] RP REVIEW. RX MEDLINE=91315455; PubMed=1859394; RA Wu Y., Foreman R.C.; RT "The molecular genetics of alpha 1 antitrypsin deficiency."; RL Bioessays 13:163-169(1991). RN [35] RP CHARACTERIZATION OF VARIANT M2. RX MEDLINE=88324438; PubMed=2901226; RA Nukiwa T., Brantly M.L., Ogushi F., Fells G.A., Crystal R.G.; RT "Characterization of the gene and protein of the common alpha 1- RT antitrypsin normal M2 allele."; RL Am. J. Hum. Genet. 43:322-330(1988). RN [36] RP VARIANT M3 ASP-400. RX MEDLINE=90368097; PubMed=2394452; DOI=10.1007/BF00206766; RA Graham A., Hayes K., Weidinger S., Newton C.R., Markham A.F., RA Kalsheker N.A.; RT "Characterisation of the alpha-1-antitrypsin M3 gene, a normal RT variant."; RL Hum. Genet. 85:381-382(1990). RN [37] RP VARIANT F CYS-247. RX MEDLINE=91241132; PubMed=2035534; RA Okayama H., Brantly M., Holmes M., Crystal R.G.; RT "Characterization of the molecular basis of the alpha 1-antitrypsin F RT allele."; RL Am. J. Hum. Genet. 48:1154-1158(1991). RN [38] RP VARIANT M-HEERLEN LEU-393. RX MEDLINE=89154435; PubMed=2784123; DOI=10.1007/BF00279001; RA Hofker M.H., Nukiwa T., van Paassen H.M.B., Nelen M., Kramps J.A., RA Klasen E.C., Frants R.R., Crystal R.G.; RT "A Pro-->Leu substitution in codon 369 of the alpha-1-antitrypsin RT deficiency variant PI M-Heerlen."; RL Hum. Genet. 81:264-268(1989). RN [39] RP VARIANT M-MALTON PHE-75 DEL. RX MEDLINE=89270478; PubMed=2786335; RA Fraizer G.C., Harrold T.R., Hofker M.H., Cox D.W.; RT "In-frame single codon deletion in the M-Malton deficiency allele of RT alpha 1-antitrypsin."; RL Am. J. Hum. Genet. 44:894-902(1989). RN [40] RP VARIANT M-MINERAL SPRINGS GLU-91. RX MEDLINE=90097863; PubMed=1967187; RA Curiel D.T., Vogelmeier C., Hubbard R.C., Stier L.E., Crystal R.G.; RT "Molecular basis of alpha 1-antitrypsin deficiency and emphysema RT associated with the alpha 1-antitrypsin M-Mineral springs allele."; RL Mol. Cell. Biol. 10:47-56(1990). RN [41] RP VARIANT M-NICHINAN PHE-75 DEL. RX MEDLINE=90178096; PubMed=2309708; RA Matsunaga E., Shiokawa S., Nakamura H., Maruyama T., Tsuda K., RA Fukumaki Y.; RT "Molecular analysis of the gene of the alpha 1-antitrypsin deficiency RT variant, M-Nichinan."; RL Am. J. Hum. Genet. 46:602-612(1990). RN [42] RP VARIANT M-PROCIDA PRO-65. RX MEDLINE=89008457; PubMed=3262617; RA Takahashi H., Nukiwa T., Satoh K., Ogushi F., Brantly M., Fells G., RA Stier L., Courtney M., Crystal R.G.; RT "Characterization of the gene and protein of the alpha 1-antitrypsin RT 'deficiency' allele M-Procida."; RL J. Biol. Chem. 263:15528-15534(1988). RN [43] RP VARIANT P-DUARTE VAL-280. RX MEDLINE=93372875; PubMed=8364590; RA Hildesheim J., Kinsley G., Bissell M., Pierce J., Brantly M.; RT "Genetic diversity from a limited repertoire of mutations on different RT common allelic backgrounds: alpha 1-antitrypsin deficiency variant P- RT Duarte."; RL Hum. Mutat. 2:221-228(1993). RN [44] RP VARIANT PITTSBURGH ARG-382. RX MEDLINE=83297520; PubMed=6604220; RA Owen M.C., Brennan S.O., Lewis J.H., Carrell R.W.; RT "Mutation of antitrypsin to antithrombin. Alpha 1-antitrypsin RT Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder."; RL N. Engl. J. Med. 309:694-698(1983). RN [45] RP VARIANT S-IIYAMA PHE-77. RX MEDLINE=91286296; PubMed=1905728; RA Seyama K., Nukiwa T., Takabe K., Takahashi H., Miyake K., Kira S.; RT "Siiyama (serine 53 (TCC) to phenylalanine 53 (TTC)). A new alpha 1- RT antitrypsin-deficient variant with mutation on a predicted conserved RT residue of the serpin backbone."; RL J. Biol. Chem. 266:12627-12632(1991). RN [46] RP VARIANT V-MUNICH ALA-26. RX MEDLINE=90196014; PubMed=2316526; RA Holmes M.D., Brantly M.L., Curiel D.T., Weidinger S., Crystal R.G.; RT "Characterization of the normal alpha 1-antitrypsin allele V-Munich: a RT variant associated with a unique protein isoelectric focusing RT pattern."; RL Am. J. Hum. Genet. 46:810-816(1990). RN [47] RP VARIANT W-BETHESDA THR-360. RX MEDLINE=90358792; PubMed=2390072; RA Holmes M.D., Brantly M.L., Fells G.A., Crystal R.G.; RT "Alpha 1-antitrypsin W-Bethesda: molecular basis of an unusual alpha RT 1-antitrypsin deficiency variant."; RL Biochem. Biophys. Res. Commun. 170:1013-1020(1990). RN [48] RP VARIANT Z-AUGSBURG LYS-366. RX MEDLINE=90252805; PubMed=2339709; RA Faber J.-P., Weidinger S., Olek K.; RT "Sequence data of the rare deficient alpha 1-antitrypsin variant PI RT Zaugsburg."; RL Am. J. Hum. Genet. 46:1158-1162(1990). RN [49] RP VARIANTS Z-WREXHAM LEU-4 AND Q0-NEWPORT SER-139. RX MEDLINE=91033789; PubMed=2227940; DOI=10.1007/BF00194233; RA Graham A., Kalsheker N.A., Bamforth F.J., Newton C.R., Markham A.F.; RT "Molecular characterisation of two alpha-1-antitrypsin deficiency RT variants: proteinase inhibitor (Pi) Null(Newport) (Gly115-->Ser) and RT (Pi) Z Wrexham (Ser-19-->Leu)."; RL Hum. Genet. 85:537-540(1990). RN [50] RP VARIANTS P-CARDIFF VAL-280; I CYS-63 AND M-MALTON PHE-75 DEL. RX MEDLINE=90109164; PubMed=2606478; DOI=10.1007/BF00210671; RA Graham A., Kalsheker N.A., Newton C.R., Bamforth F.J., Powell S.J., RA Markham A.F.; RT "Molecular characterisation of three alpha-1-antitrypsin deficiency RT variants: proteinase inhibitor (Pi) nullcardiff (Asp256-->Val); PiM- RT Malton (Phe51-->deletion) and PiI (Arg39-->Cys)."; RL Hum. Genet. 84:55-58(1989). RN [51] RP VARIANT QO-LUDWIGSHAFEN ASN-116. RX MEDLINE=91072661; PubMed=2254451; RA Fraizer G.C., Siewertsen M.A., Hofker M.H., Brubacher M.G., Cox D.W.; RT "A null deficiency allele of alpha 1-antitrypsin, QO-Ludwigshafen, RT with altered tertiary structure."; RL J. Clin. Invest. 86:1878-1884(1990). RN [52] RP VARIANTS. RX MEDLINE=95067973; PubMed=7977369; RA Faber J.-P., Poller W., Weidinger S., Kirchgesser M., Schwaab R., RA Bidlingmaier F., Olek K.; RT "Identification and DNA sequence analysis of 15 new alpha 1- RT antitrypsin variants, including two PI*Q0 alleles and one deficient RT PI*M allele."; RL Am. J. Hum. Genet. 55:1113-1121(1994). RN [53] RP VARIANT Z-BRISTOL MET-109. RX MEDLINE=98120621; PubMed=9459000; RA Lovegrove J.U., Jeremiah S., Gillett G.T., Temple I.K., Povey S., RA Whitehouse D.B.; RT "A new alpha 1-antitrypsin mutation, Thr-Met 85, (PI ZBristol) RT associated with novel electrophoretic properties."; RL Ann. Hum. Genet. 61:385-391(1997). RN [54] RP VARIANTS Y-BARCELONA VAL-280 AND HIS-415. RX PubMed=10651487; RA Jardi R., Rodriguez F., Miravitlles M., Vidal R., Cotrina M., Quer J., RA Pascual C., Weidinger S.; RT "Identification and molecular charaterization of the new alpha-1- RT antitrypsin deficient allele PI YBarcelona (Asp256Val and RT Pro391His)."; RL Hum. Mutat. 12:213-213(1998). RN [55] RP VARIANT SAO TOME HIS-386. RA Seixas S., Trovoada M.J., Santos M.T., Rocha J.; RT "A novel alpha-1-antitrypsin P362H variant found in a population RT sample from Sao Tome e Principe (Gulf of Guinea, West Africa)."; RL Hum. Mutat. 13:414-414(1999). RN [56] RP VARIANT BASQUE ARG-305 DEL. RX MEDLINE=20081076; PubMed=10612848; RX DOI=10.1002/(SICI)1098-1004(200001)15:1<121::AID-HUMU37>3.0.CO;2-U; RA Seixas S., Garcia O., Amorim A., Rocha J.; RT "A novel alpha-1-antitrypsin r281del variant found in a population RT sample from the Basque country."; RL Hum. Mutat. 15:121-122(2000). CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is CC elastase, but it also has a moderate affinity for plasmin and CC thrombin. CC -!- INTERACTION: CC P00760:- (xeno); NbExp=1; IntAct=EBI-986224, EBI-986385; CC P00772:ELA1 (xeno); NbExp=1; IntAct=EBI-986224, EBI-986248; CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable. CC -!- PTM: Several isomers are observed, resulting from the combination CC of different N-linked glycan structures and mature N-terminus. N- CC linked glycan at Asn-107 is alternatively di-antennary, tri- CC antennary or tetra-antennary, whereas glycan at Asn-70 is di- CC antennary with trace amounts of tri-antennary, and glycan at Asn- CC 271 is exclusively di-antennary. The structure of the antennas is CC Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure CC Man(alpha1-6)[Man(alpha1-3)]Man(beta1-4)GlcNAc(beta1-4)GlcNAc. CC Some antennas are fucosylated, which forms a Lewis-X determinant. CC -!- PTM: Proteolytic processing may yield the truncated form that CC ranges from Asp-30 to Lys-418. CC -!- POLYMORPHISM: The sequence shown is that of the M1V allele which CC is the most common form of PI (44 to 49%). Other frequent alleles CC are: M1A 20 to 23%; M2 10 to 11%; M3 14 to 19%. CC -!- DISEASE: The major physiological function of AAT is the protection CC of the lower respiratory tract against proteolytic destruction by CC human leukocyte elastase (HLE). A hereditary deficiency of AAT, is CC associated with a 20-30 fold increased risk of developing chronic CC obstructive pulmonary disease. CC -!- DISEASE: Deficiency of the normal inhibitor in individuals CC homozygous for allele Z or M-Malton can result in the development CC of chronic emphysema or infantile liver cirrhosis. CC -!- DISEASE: Variant Pittsburgh is the cause of bleeding diathesis. CC -!- SIMILARITY: Belongs to the serpin family. CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=SERPINA1". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K01396; AAB59375.1; -; mRNA. DR EMBL; K02212; AAB59495.1; -; Genomic_DNA. DR EMBL; X01683; CAA25838.1; -; mRNA. DR EMBL; M11465; AAA51546.1; -; mRNA. DR EMBL; J02619; AAA51547.1; -; Genomic_DNA. DR EMBL; AF113676; AAF29581.1; -; mRNA. DR EMBL; AF130068; AAG35496.1; -; mRNA. DR EMBL; BT019455; AAV38262.1; -; mRNA. DR EMBL; BC011991; AAH11991.1; -; mRNA. DR EMBL; BC015642; AAH15642.1; -; mRNA. DR EMBL; J00064; AAB59369.1; -; Genomic_DNA. DR EMBL; J00066; AAB59370.1; -; Genomic_DNA. DR EMBL; J00065; AAB59370.1; JOINED; Genomic_DNA. DR EMBL; J00067; AAB59371.1; -; Genomic_DNA. DR EMBL; X02920; CAA26677.1; -; mRNA. DR EMBL; V00496; CAA23755.1; -; mRNA. DR EMBL; M26123; AAA51545.1; -; mRNA. DR PIR; A21853; ITHU. DR UniGene; Hs.525557; -. DR PDB; 1ATU; X-ray; @=45-418. DR PDB; 1D5S; X-ray; A=44-377, B=378-418. DR PDB; 1EZX; X-ray; A=48-382, B=383-418. DR PDB; 1HP7; X-ray; A=25-418. DR PDB; 1IZ2; X-ray; A=25-418. DR PDB; 1KCT; X-ray; @=25-418. DR PDB; 1OO8; X-ray; A=26-418. DR PDB; 1OPH; X-ray; A=26-418. DR PDB; 1PSI; X-ray; @=26-418. DR PDB; 1QLP; X-ray; A=26-418. DR PDB; 1QMB; X-ray; A=49-376, B=377-418. DR PDB; 2D26; X-ray; A=26-382, B=383-418. DR PDB; 7API; X-ray; A=36-382, B=383-418. DR PDB; 8API; X-ray; A=36-382, B=383-418. DR PDB; 9API; X-ray; A=36-382, B=383-418. DR IntAct; P01009; -. DR MEROPS; I04.001; -. DR GlycoSuiteDB; P01009; -. DR SWISS-2DPAGE; P01009; HUMAN. DR Cornea-2DPAGE; P01009; HUMAN. DR DOSAC-COBS-2DPAGE; P01009; HUMAN. DR HSC-2DPAGE; P01009; HUMAN. DR OGP; P01009; -. DR REPRODUCTION-2DPAGE; P01009; HUMAN. DR Siena-2DPAGE; P01009; -. DR Ensembl; ENSG00000197249; Homo sapiens. DR KEGG; hsa:5265; -. DR H-InvDB; HIX0011929; -. DR HGNC; HGNC:8941; SERPINA1. DR MIM; 107400; gene+phenotype. DR Reactome; REACT_604.1; Hemostasis. DR LinkHub; P01009; -. DR ArrayExpress; P01009; -. DR GermOnline; ENSG00000197249; Homo sapiens. DR RZPD-ProtExp; F0215; -. DR RZPD-ProtExp; IOH10470; -. DR RZPD-ProtExp; IOH27904; -. DR GO; GO:0005615; C:extracellular space; IMP:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW 3D-structure; Acute phase; Direct protein sequencing; KW Disease mutation; Glycoprotein; Polymorphism; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL 1 24 FT CHAIN 25 418 Alpha-1-antitrypsin. FT /FTId=PRO_0000032377. FT REGION 368 392 RCL. FT BINDING 256 256 Cysteine (covalent). FT SITE 382 383 Reactive bond. FT CARBOHYD 70 70 N-linked (GlcNAc...). FT CARBOHYD 107 107 N-linked (GlcNAc...). FT CARBOHYD 271 271 N-linked (GlcNAc...). FT VARIANT 4 4 S -> L (in Z-Wrexham). FT /FTId=VAR_006978. FT VARIANT 26 26 D -> A (in V-Munich). FT /FTId=VAR_006979. FT VARIANT 58 58 A -> T (in M5-Karlsruhe). FT /FTId=VAR_006980. FT VARIANT 63 63 R -> C (in I). FT /FTId=VAR_006981. FT VARIANT 65 65 L -> P (in M-Procida). FT /FTId=VAR_006982. FT VARIANT 69 69 S -> F (in M6-Bonn). FT /FTId=VAR_006983. FT VARIANT 75 75 Missing (in M-Malton, M-Nichinan and M- FT Palermo; associated with very low serum FT levels of AAT). FT /FTId=VAR_006984. FT VARIANT 77 77 S -> F (in S-Iiyama). FT /FTId=VAR_006985. FT VARIANT 84 84 A -> T (in M6-Passau). FT /FTId=VAR_006986. FT VARIANT 91 91 G -> E (in M-Mineral springs; causes FT reduced AAT secretion). FT /FTId=VAR_006987. FT VARIANT 92 92 T -> I (in QO-Lisbon; deficient AAT with FT very low serum levels). FT /FTId=VAR_006988. FT VARIANT 109 109 T -> M (in Z-Bristol; deficient AA; FT disrupts the N-glycosylation site N-107). FT /FTId=VAR_011620. FT VARIANT 112 112 P -> T (in M5-Berlin). FT /FTId=VAR_006989. FT VARIANT 116 116 I -> N (in QO-Ludwigshafen). FT /FTId=VAR_006990. FT VARIANT 125 125 R -> H (in M2; associated with D-400; FT dbSNP:rs709932). FT /FTId=VAR_006991. FT VARIANT 139 139 G -> S (in QO-Newport; dbSNP:rs11558261). FT /FTId=VAR_006992. FT VARIANT 172 172 G -> R (in V and M-Nichinan). FT /FTId=VAR_006993. FT VARIANT 172 172 G -> W (in M2-Obernburg). FT /FTId=VAR_006994. FT VARIANT 180 180 Q -> E (in L-Frankfurt). FT /FTId=VAR_006995. FT VARIANT 228 228 E -> K (in X). FT /FTId=VAR_006996. FT VARIANT 237 237 V -> A (in M1A and Z; associated with K- FT 366 in Z; dbSNP:rs6647). FT /FTId=VAR_006997. FT VARIANT 247 247 R -> C (in F). FT /FTId=VAR_006998. FT VARIANT 280 280 D -> V (in P-Duarte/P-Cardiff/P-Lowell; FT associated with H-415 in Y-Barcelona). FT /FTId=VAR_006999. FT VARIANT 288 288 E -> V (in S and T; dbSNP:rs17580). FT /FTId=VAR_007000. FT VARIANT 305 305 Missing (in Basque). FT /FTId=VAR_009216. FT VARIANT 354 354 S -> F (in S-Munich). FT /FTId=VAR_007001. FT VARIANT 360 360 A -> T (in W-Bethesda; dbSNP:rs1802959). FT /FTId=VAR_007002. FT VARIANT 365 365 D -> N (in P-St.Albans/P-Donauwoerth). FT /FTId=VAR_007003. FT VARIANT 366 366 E -> K (in Z/Z-Augsburg/Z-Tun; associated FT with A-237 in Z). FT /FTId=VAR_007004. FT VARIANT 382 382 M -> R (in Pittsburgh; has antithrombin FT activity). FT /FTId=VAR_007005. FT VARIANT 386 386 P -> H (in Sao Tome). FT /FTId=VAR_007006. FT VARIANT 386 386 P -> T (in L-Offenbach). FT /FTId=VAR_007007. FT VARIANT 387 387 E -> K (in Christchurch). FT /FTId=VAR_007008. FT VARIANT 393 393 P -> L (in M-Heerlen). FT /FTId=VAR_007009. FT VARIANT 400 400 E -> D (in M2 and M3; associated with H- FT 125 in M2; dbSNP:rs1303). FT /FTId=VAR_007010. FT VARIANT 415 415 P -> H (in Y-Barcelona; associated with FT V-280). FT /FTId=VAR_007011. FT MUTAGEN 382 382 M->V: Oxidation-resistant inhibitor of FT therapeutic importance. FT CONFLICT 12 12 Missing (in Ref. 4). FT CONFLICT 61 61 L -> P (in Ref. 7; AAF29581). FT CONFLICT 139 140 GN -> DG (in Ref. 1). FT CONFLICT 174 174 T -> H (in Ref. 4). FT CONFLICT 229 229 E -> D (in Ref. 4). FT CONFLICT 273 273 T -> N (in Ref. 1). FT CONFLICT 326 326 V -> I (in Ref. 3). FT TURN 48 50 FT HELIX 51 68 FT STRAND 70 72 FT STRAND 74 76 FT HELIX 78 89 FT TURN 90 91 FT HELIX 94 103 FT TURN 104 105 FT TURN 108 110 FT HELIX 113 127 FT STRAND 135 145 FT TURN 146 147 FT HELIX 152 160 FT TURN 161 161 FT STRAND 165 169 FT TURN 171 172 FT HELIX 174 188 FT TURN 189 191 FT TURN 202 203 FT STRAND 206 215 FT STRAND 218 220 FT HELIX 224 226 FT STRAND 228 237 FT STRAND 239 256 FT TURN 257 260 FT STRAND 261 268 FT TURN 269 271 FT STRAND 272 279 FT TURN 281 282 FT HELIX 284 290 FT HELIX 293 299 FT TURN 300 301 FT STRAND 306 313 FT STRAND 315 322 FT HELIX 323 329 FT TURN 330 331 FT HELIX 334 336 FT TURN 338 339 FT TURN 343 345 FT STRAND 346 349 FT STRAND 355 364 FT TURN 370 371 FT STRAND 387 389 FT STRAND 394 400 FT TURN 401 403 FT STRAND 406 413 FT TURN 415 416 SQ SEQUENCE 418 AA; 46737 MW; 7016555F273B7F16 CRC64; MPSSVSWGIL LLAGLCCLVP VSLAEDPQGD AAQKTDTSHH DQDHPTFNKI TPNLAEFAFS LYRQLAHQSN STNIFFSPVS IATAFAMLSL GTKADTHDEI LEGLNFNLTE IPEAQIHEGF QELLRTLNQP DSQLQLTTGN GLFLSEGLKL VDKFLEDVKK LYHSEAFTVN FGDTEEAKKQ INDYVEKGTQ GKIVDLVKEL DRDTVFALVN YIFFKGKWER PFEVKDTEEE DFHVDQVTTV KVPMMKRLGM FNIQHCKKLS SWVLLMKYLG NATAIFFLPD EGKLQHLENE LTHDIITKFL ENEDRRSASL HLPKLSITGT YDLKSVLGQL GITKVFSNGA DLSGVTEEAP LKLSKAVHKA VLTIDEKGTE AAGAMFLEAI PMSIPPEVKF NKPFVFLMIE QNTKSPLFMG KVVNPTQK // ID A1AT_MERUN Reviewed; 406 AA. AC Q64118; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 36. DE Alpha-1-antitrypsin precursor (Alpha-1 protease inhibitor) (Alpha-1- DE antiproteinase). OS Meriones unguiculatus (Mongolian jird) (Mongolian gerbil). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Gerbillinae; Meriones. OX NCBI_TaxID=10047; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-44 AND 77-96, RP FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Plasma; RX MEDLINE=95155268; PubMed=7852275; RA Goto K., Suzuki Y., Yoshida K., Yamamoto K., Sinohara H.; RT "Plasma alpha-1-antiproteinase from the Mongolian gerbil, Meriones RT unguiculatus: isolation, partial characterization, sequencing of cDNA, RT and implications for molecular evolution."; RL J. Biochem. 116:582-588(1994). CC -!- FUNCTION: Inhibitor of serine proteases. Can inhibit elastase, CC trypsin, chymotrypsin and plasmin. CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the serpin reactive site CC and the active site of the protease. The resulting inactive CC serpin-protease complex is highly stable (By similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S77822; AAB33367.1; -; mRNA. DR PIR; JX0346; JX0346. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; FALSE_NEG. KW Direct protein sequencing; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 406 Alpha-1-antitrypsin. FT /FTId=PRO_0000032386. FT REGION 362 381 RCL. FT SITE 371 372 Reactive bond (By similarity). FT CARBOHYD 59 59 N-linked (GlcNAc...) (Potential). FT CARBOHYD 96 96 N-linked (GlcNAc...) (Potential). FT CARBOHYD 260 260 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 406 AA; 45127 MW; 814613E44C7AA469 CRC64; MTSSISWGLL LLAGLCCLVP SFLAEDAEKT DSSHQDHIMA SNLADFAFGL YRVLSHQSNT TNIFLSPLSI ATALAMLSLG SKDDTKAQLL QGLHFNLTET SEADIHKGFQ HLLKTLNRPD NELQLTTGSS LFVNNSLNLV EKFLEEVKNH YHSEAFFVNF ADSEEAKKTI NSFVEKATHG KIVDLVKDLE IDTVLALVNY IFFRGKWEKP FDPELTEEAD FHVDKSTTVK VPMMNRMGMF DVHYCDTLSS WVLLMDYLGN ATAIFILPDE GKMQHLEQTL TKEHIYKFLQ NRHTRSANVH LPKLSISGTY NLKKVLSPLG ITQVFSNGAD LSGITTDVPL KLSKAVHKAV LTLDERGTEA AGTTVLEAVP MSIPPDVCFK NPFVVIICDK HTQSPLFVGK VVNPTQ // ID A1AT_MESAU Reviewed; 413 AA. AC P97277; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 31-OCT-2006, entry version 36. DE Alpha-1-antitrypsin precursor (Alpha-1 protease inhibitor) (Alpha-1- DE antiproteinase). OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=96004896; PubMed=7548212; DOI=10.1016/0167-4781(95)00140-C; RA Nakatani T., Suzuki Y., Yoshida K., Sinohara H.; RT "Molecular cloning and sequence analysis of cDNA encoding plasma RT alpha-1-antiproteinase from Syrian hamster: implications for the RT evolution of Rodentia."; RL Biochim. Biophys. Acta 1263:245-248(1995). CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is CC elastase, but it also has a moderate affinity for plasmin and CC thrombin (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the serpin reactive site CC and the active site of the protease. The resulting inactive CC serpin-protease complex is highly stable (By similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D49709; BAA08557.1; -; mRNA. DR PIR; S60036; S60036. DR HSSP; P01009; 1QMB. DR SMR; P97277; 38-413. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; FALSE_NEG. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 413 Alpha-1-antitrypsin. FT /FTId=PRO_0000032387. FT REGION 368 387 RCL. FT SITE 377 378 Reactive bond (By similarity). FT CARBOHYD 65 65 N-linked (GlcNAc...) (Potential). FT CARBOHYD 102 102 N-linked (GlcNAc...) (Potential). FT CARBOHYD 165 165 N-linked (GlcNAc...) (Potential). FT CARBOHYD 266 266 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 413 AA; 45819 MW; 71D192E106A1EB36 CRC64; MKPSISWGIL LLAGLCCLVP SFLAEDAQET DASKQDQEHQ ACCKIAPNLA DFSFNLYREL VHQSNTTNIF FSPVSIATAF AMLSLGTKGV THTQILEGLG FNLTEIAEAE VHKGFHNLLQ TFNRPDNELQ LTTGNGLFIH NNLKLVDKFL EEVKNDYHSE AFSVNFTDSE EAKKVINGFV EKGTQGKIVD LVKDLDKDTV LALVNYIFFK GKWKKPFDAD NTEEADFHVD KTTTVKVPMM SRLGMFDVHY VSTLSSWVLL MDYLGNATAI FILPDDGKMQ HLEQTLNKEI IGKFLKDRHT RSANVHFPKL SISGTYNLKT ALDPLGITQV FSNGADLSGI TEDVPLKLGK AVHKAVLTID ERGTEAAGAT FMEIIPMSVP PEVNFNSPFI AIIYDRQTAK SPLFVGKVVD PTR // ID A1AT_MUSCR Reviewed; 412 AA. AC P26595; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 31-OCT-2006, entry version 45. DE Alpha-1-antiproteinase precursor (Alpha-1-antitrypsin) (Alpha-1- DE proteinase inhibitor) (AAT). GN Name=Serpina1; OS Mus caroli (Wild mouse) (Ricefield mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10089; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90136592; PubMed=1689000; RA Latimer J.J., Berger F.G., Baumann H.; RT "Highly conserved upstream regions of the alpha 1-antitrypsin gene in RT two mouse species govern liver-specific expression by different RT mechanisms."; RL Mol. Cell. Biol. 10:760-769(1990). CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is CC elastase, but it also has a moderate affinity for plasmin and CC thrombin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed not only in liver but also in kidney CC tubule cells, where it is regulated by androgens during CC development. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M33567; AAA37128.1; -; mRNA. DR PIR; A34730; ITMSC. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR MGI; MGI:98376; Serpina1. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 FT CHAIN 25 412 Alpha-1-antiproteinase. FT /FTId=PRO_0000032394. FT REGION 367 386 RCL. FT SITE 376 377 Reactive bond (By similarity). FT CARBOHYD 100 100 N-linked (GlcNAc...) (Potential). FT CARBOHYD 133 133 N-linked (GlcNAc...) (Potential). FT CARBOHYD 264 264 N-linked (GlcNAc...) (Potential). FT CARBOHYD 313 313 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 412 AA; 45872 MW; C1A167063CDAF4BD CRC64; MTPSISWGLL LLAGLFCLVP SFLAEDVQET DTSRRDSVPA SHDTPYNLEL SISLYRELGH KSTTSNIFFS QVSIATAFAM LSLGEKGDTH TQILEGLQFN LTQTSEADIH KAFQHLLQTL NRPDSELQLS TGNGSLLNND LKLVEKFLEE AKNNYHSEVF SVNFAESEEA KKVINDFVEK GTQGKIAEAV KDPDEDTVFA LANYILFKGK WKKPFDPKHT EEAEFHVDTV TTVKVPMMTL TGMLDVHHCS TLSSWVLLMD YLGNRTAVFL LPDDGKMQHL EQTLNKELIS KFLLNRHRRL AQVHLPRLSL SGNYTLNTLM SHLGITRIFN NGADLSGITE ENAPLKLSKA ADKAVLTMDE TGTEAAAATV LQAVPMSMPP ILNFNKPFIF IIVEEHTQSP LFVGKVVDPT RK // ID A1AT_MUSSA Reviewed; 413 AA. AC Q63969; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-OCT-2006, entry version 38. DE Alpha-1-antiproteinase precursor (Alpha-1-antitrypsin) (Alpha-1- DE proteinase inhibitor). GN Name=Serpina1; OS Mus saxicola (Spiny mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10094; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94223689; PubMed=8169957; RA Rheaume C., Goodwin R.L., Latimer J.J., Baumann H., Berger F.G.; RT "Evolution of murine alpha 1-proteinase inhibitors: gene amplification RT and reactive center divergence."; RL J. Mol. Evol. 38:121-131(1994). CC -!- FUNCTION: Inhibitor of serine proteases. The primary target is CC elastase, but also has a moderate affinity for plasmin and CC thrombin (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the serpin reactive site CC and the active site of the protease. The resulting inactive CC serpin-protease complex is highly stable (By similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S70316; AAB30633.1; -; mRNA. DR PIR; I56481; I56481. DR HSSP; P01009; 1QMB. DR MEROPS; I04.001; -. DR MGI; MGI:98376; Serpina1. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 413 Alpha-1-antiproteinase. FT /FTId=PRO_0000032395. FT REGION 368 387 RCL. FT SITE 377 378 Reactive bond (By similarity). FT CARBOHYD 64 64 N-linked (GlcNAc...) (Potential). FT CARBOHYD 101 101 N-linked (GlcNAc...) (Potential). FT CARBOHYD 265 265 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 413 AA; 46260 MW; B02CE28E691D32E0 CRC64; MTPSISWRLL LLAGLCCLVP SYLAEDVQET DTSQKDQSPA SHEMATNLGD FAFSLYRELV HQSNTSNIFF SPVSIATAFA LLSLGSKGDT QTQILEGLQF NLTQTSEADI HKVFQHLLQT LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQSEV FSVNFAKSEE ARKMINDFVE KGTQGKIVDA VKDLDEDTVF ALANYIFFQG KWKTPFDPEH TTEADFHVNE STTVRVPMMN LMRMLDVHYC STLSSWVLMM DYLGNATAVF LLPDDGKMQH LEQTLNKELI SKFLLNRHRS LAEIHFPRLS ISGSYNLKAL MAPLGITRVF NNGADLSGIT EENAPLRLSK AVHKAVLTID ERGTEAAATT IVEAVFMSLP PILHFNHPFV FTIVETHTQT PLFVGKVVDP TRK // ID A1AT_PAPAN Reviewed; 409 AA. AC P01010; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 31-OCT-2006, entry version 55. DE Alpha-1-antitrypsin precursor (Alpha-1 protease inhibitor) (Alpha-1- DE antiproteinase) (AAT) (Fragment). GN Name=SERPINA1; Synonyms=PI; OS Papio anubis (Olive baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Papio. OX NCBI_TaxID=9555; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=82082539; PubMed=7031661; RA Kurachi K., Chandra T., Friezner Degen S.J., White T.T., RA Marchioro T.L., Woo S.L.C., Davie E.W.; RT "Cloning and sequence of cDNA coding for alpha 1-antitrypsin."; RL Proc. Natl. Acad. Sci. U.S.A. 78:6826-6830(1981). CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is CC elastase, but it also has a moderate affinity for plasmin and CC thrombin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J00321; AAA35377.1; -; mRNA. DR HSSP; P01009; 1EZX. DR SMR; P01010; 38-409. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL <1 15 FT CHAIN 16 409 Alpha-1-antitrypsin. FT /FTId=PRO_0000032378. FT REGION 364 383 RCL. FT SITE 373 374 Reactive bond. FT CARBOHYD 61 61 N-linked (GlcNAc...) (Potential). FT CARBOHYD 98 98 N-linked (GlcNAc...) (Potential). FT CARBOHYD 136 136 N-linked (GlcNAc...) (Potential). FT CARBOHYD 262 262 N-linked (GlcNAc...) (Potential). FT NON_TER 1 1 SQ SEQUENCE 409 AA; 45694 MW; E19B0B7450FDBA9B CRC64; LLLAGLCCLL PGSLAEDPQG DAAQKTDTPP HDQNHPTLNK ITPSLAEFAF SLYRQLAHQS NSTNIFFSPV SIATAFAMLS LGTKADTHSE ILEGLNFNLT EIPEAQVHEG FQELLRTLNK PDSQLQLTTG NGLFLNKSLK VVDKFLEDVK NLYHSEAFSV NFEDTEEAKK QINNYVEKGT QGKVVDLVKE LDRDTVFALV NYIFFKGKWE RPFEVEATEE EDFHVDQATT VKVPMMRRLG MFNIYHCEKL SSWVLLMKYL GNATAIFFLP DEGKLQHLEN ELTHDIITKF LENENRRSAN LHLPKLAITG TYDLKTVLGH LGITKVFSNG ADLSGVTEDA PLKLSKAVHK AVLTIDEKGT EAAGAMFLEA IPMSIPPEVK FNKPFVFLMI EQNTKSPLFI GKVVNPTQK // ID A1AT_PIG Reviewed; 421 AA. AC P50447; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 31-OCT-2006, entry version 40. DE Alpha-1-antitrypsin precursor (Alpha-1 protease inhibitor) (Alpha-1- DE antiproteinase). GN Name=SERPINA1; Synonyms=PI; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=97009792; PubMed=8856896; RA Archibald A.L., Couperwhite S., Mellink C.H.M., Lahbib-Mansais Y., RA Gellin J.; RT "Porcine alpha-1-antitrypsin (PI): cDNA sequence, polymorphism and RT assignment to chromosome 7q2.4-q2.6."; RL Anim. Genet. 27:85-89(1996). CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is CC elastase, but it also has a moderate affinity for plasmin and CC thrombin (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X88780; CAA61259.1; -; mRNA. DR UniGene; Ssc.7090; -. DR HSSP; P01009; 1QMB. DR SMR; P50447; 51-421. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Glycoprotein; Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 421 Alpha-1-antitrypsin. FT /FTId=PRO_0000032396. FT REGION 376 395 RCL. FT SITE 385 386 Reactive bond. FT CARBOHYD 73 73 N-linked (GlcNAc...) (Potential). FT CARBOHYD 110 110 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 421 AA; 47194 MW; 08A4AB2A9E600690 CRC64; MASSSTWGLL LLAGLCCLVP ISLAEGLQGH AVQETDVPRH DHEQHQEAAC HRIAPNLADF AFSLYRQVAR QSNTSNIFLS PVTIARAFAM LSLGTKGATH AEILEGLQFN LTEKAEAEIH EGFQHLLHTL NQPDNQLQLT TGNGLFIDEK AKLVPKFLED VKNLYHSEAF SINFRDTEEA KKCINDYVEK GSQGKIVDLV DELDKDTVFA LVNYIFFKGK WEKPFEVEQT TEEDFHVDEE TTVKVPMMNR LGMFDLHHCD KLSSWVLLMD YVATATAFFI LPDQGKLHQL EDMLTKEIRA KFLEKRYPSS ANLHLPKLTI SGTYDLKSLL GNLGITKVFS DEADLSGVTE EQPLKLSKAL HRAVLTIDEK GTEATGATIL EAIPMSIPPN VKFNKPFLFL IYDTKTKAVL FMGKVMNPTQ K // ID A1AT_PONPY Reviewed; 418 AA. AC Q5RCW5; Q5NVR9; Q5RF76; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 31-OCT-2006, entry version 13. DE Alpha-1-antitrypsin precursor (Alpha-1 protease inhibitor) (Alpha-1- DE antiproteinase). GN Name=SERPINA1; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart, Kidney, and Liver; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is CC elastase, but it also has a moderate affinity for plasmin and CC thrombin (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR857285; CAH89581.1; -; mRNA. DR EMBL; CR858153; CAH90392.1; -; mRNA. DR EMBL; CR925936; CAI29594.1; -; mRNA. DR SMR; Q5RCW5; 47-418. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 418 Alpha-1-antitrypsin. FT /FTId=PRO_0000032379. FT REGION 373 392 RCL. FT SITE 382 383 Reactive bond (By similarity). FT CARBOHYD 70 70 N-linked (GlcNAc...) (Potential). FT CARBOHYD 107 107 N-linked (GlcNAc...) (Potential). FT CARBOHYD 271 271 N-linked (GlcNAc...) (Potential). FT CONFLICT 289 289 N -> D (in Ref. 1; CAH89581). FT CONFLICT 305 305 R -> RS (in Ref. 1; CAH89581/CAI29594). FT CONFLICT 332 332 I -> T (in Ref. 1; CAH89581). FT CONFLICT 396 404 FLMIEQNTK -> CLISVFQNA (in Ref. 1; FT CAI29594). SQ SEQUENCE 418 AA; 46861 MW; BF93D2080AEDBE56 CRC64; MPSSVSWGIL LLAGLCCLVP VSLAEDPQGD AAQKTDTSHH DQDHPTFNKI TPNLAEFAFS LYRQLAHQSN STNIFFSPVS IATAFAMLSL GTKADTHSEI LEGLHFNLTE IPEAQVHEGF QELLRTLNQP DSQLQLTTGN GLFLNESLKL VDKFLEDVKK LYHSDAFTVN FGDTEEAKKQ INDYVEKGTQ GKIVDLVKEL DRDTVFALVN YIFFKGKWER PFEVKDTKEE DFHVDEVTTV KVPMMRRLGM FNIHYCEKLS SWVLLMKYLG NATAIFFLPD EGKLQHLENE LTHDIITKFL ENENRRSASL HLPKLSITGT YDLKRVLGQL GITKVFSNGA DLSGVTEEAP LKLSKAVHKA VLTIDEKGTE AAGAMFLEAI PMSIPPEVKF NKPFVFLMIE QNTKSPLFVG KVVNPTQK // ID A1AT_RAT Reviewed; 411 AA. AC P17475; Q6AYZ5; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 2. DT 20-FEB-2007, entry version 63. DE Alpha-1-antiproteinase precursor (Alpha-1-antitrypsin) (Alpha-1- DE proteinase inhibitor). GN Name=Serpina1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Liver; RX MEDLINE=91035351; PubMed=2229024; RA Misumi Y., Sohda M., Ohkubo K., Takami N., Oda K., Ikehara Y.; RT "Molecular cloning and sequencing of the cDNA of rat alpha 1-protease RT inhibitor and its expression in COS-1 cells."; RL J. Biochem. 108:230-234(1990). 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 [MRNA] OF 4-411, PROTEIN SEQUENCE OF 25-57, AND RP TISSUE SPECIFICITY. RC TISSUE=Liver; RX MEDLINE=90148955; PubMed=2302382; DOI=10.1021/bi00454a004; RA Chao S., Chai K.X., Chao L., Chao J.; RT "Molecular cloning and primary structure of rat alpha 1-antitrypsin."; RL Biochemistry 29:323-329(1990). RN [4] RP PROTEIN SEQUENCE OF 44-57. RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord; RA Lubec G., Afjehi-Sadat L.; RL Submitted (NOV-2006) to Swiss-Prot. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 188-389. RC TISSUE=Liver; RA Flink I.L., Bailey T., Morkin E.; RL Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Inhibitor of serine proteases. The primary target is CC elastase, but also has a moderate affinity for plasmin and CC thrombin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D00675; BAA00579.1; -; mRNA. DR EMBL; BC078824; AAH78824.1; -; mRNA. DR EMBL; M32247; AAA40788.1; -; mRNA. DR EMBL; X16273; CAA34349.1; -; mRNA. DR PIR; A33892; ITRT. DR UniGene; Rn.1419; -. DR HSSP; P01009; 1QMB. DR SMR; P17475; 39-411. DR MEROPS; I04.001; -. DR Ensembl; ENSRNOG00000032669; Rattus norvegicus. DR KEGG; rno:24648; -. DR RGD; 3326; Serpina1. DR ArrayExpress; P17475; -. DR GermOnline; ENSRNOG00000032669; Rattus norvegicus. DR InterPro; IPR000215; Prot_inh_serpin. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor; Signal. FT SIGNAL 1 24 FT CHAIN 25 411 Alpha-1-antiproteinase. FT /FTId=PRO_0000032398. FT REGION 367 386 RCL. FT SITE 376 377 Reactive bond. FT CARBOHYD 64 64 N-linked (GlcNAc...) (Potential). FT CARBOHYD 101 101 N-linked (GlcNAc...) (Potential). FT CARBOHYD 265 265 N-linked (GlcNAc...) (Potential). FT CONFLICT 14 14 A -> G (in Ref. 1 and 2; AAH78824). FT CONFLICT 84 84 L -> V (in Ref. 1). FT CONFLICT 247 247 M -> I (in Ref. 5). FT CONFLICT 248 248 H -> Y (in Ref. 1). FT CONFLICT 318 318 K -> N (in Ref. 1). FT CONFLICT 322 322 S -> D (in Ref. 5). SQ SEQUENCE 411 AA; 46136 MW; B4245CFE21C5C761 CRC64; MAPSISRGLL LLAALCCLAP SFLAEDAQET DTSQQDQSPT YRKISSNLAD FAFSLYRELV HQSNTSNIFF SPMSITTAFA MLSLGSKGDT RKQILEGLEF NLTQIPEADI HKAFHHLLQT LNRPDSELQL NTGNGLFVNK NLKLVEKFLE EVKNNYHSEA FSVNFADSEE AKKVINDYVE KGTQGKIVDL MKQLDEDTVF ALVNYIFFKG KWKRPFNPEH TRDADFHVDK STTVKVPMMN RLGMFDMHYC STLSSWVLMM DYLGNATAIF LLPDDGKMQH LEQTLTKDLI SRFLLNRQTR SAILYFPKLS ISGTYNLKTL LSSLGITRVF NNDADLSGIT EDAPLKLSQA VHKAVLTLDE RGTEAAGATV VEAVPMSLPP QVKFDHPFIF MIVESETQSP LFVGKVIDPT R // ID A1AT_SHEEP Reviewed; 416 AA. AC P12725; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 20-FEB-2007, entry version 54. DE Alpha-1-antiproteinase precursor (Alpha-1-antitrypsin) (Alpha-1- DE proteinase inhibitor). OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=89366677; PubMed=2788872; DOI=10.1093/nar/17.15.6398; RA Brown W.M., Dziegielewska K.D., Foreman R.C., Saunders N.R., Wu Y.; RT "Nucleotide and deduced amino acid sequence of sheep alpha 1 RT antitrypsin."; RL Nucleic Acids Res. 17:6398-6398(1989). RN [2] RP PROTEIN SEQUENCE OF 25-55. RC TISSUE=Plasma; RX MEDLINE=91144555; PubMed=1899999; RA Mistry R., Snashall P.D., Totty N., Guz A., Tetley T.D.; RT "Isolation and characterization of sheep alpha 1-proteinase RT inhibitor."; RL Biochem. J. 273:685-690(1991). CC -!- FUNCTION: Inhibits human leukocyte elastase, pig pancreatic CC elastase and bovine trypsin on a 1:1 molar basis. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable (By CC similarity). CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X15555; CAA33561.1; -; mRNA. DR PIR; S05312; ITSH. DR UniGene; Oar.1120; -. DR HSSP; P01009; 1QMB. DR SMR; P12725; 46-415. DR MEROPS; I04.001; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Direct protein sequencing; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal. FT SIGNAL 1 24 FT CHAIN 25 416 Alpha-1-antiproteinase. FT /FTId=PRO_0000032399. FT REGION 371 390 RCL. FT SITE 380 381 Reactive bond. FT CARBOHYD 68 68 N-linked (GlcNAc...) (Potential). FT CARBOHYD 105 105 N-linked (GlcNAc...) (Potential). FT CARBOHYD 143 143 N-linked (GlcNAc...) (Potential). FT CARBOHYD 269 269 N-linked (GlcNAc...) (Potential). FT CONFLICT 39 39 A -> S (in Ref. 2). FT CONFLICT 45 45 C -> A (in Ref. 2). SQ SEQUENCE 416 AA; 45985 MW; 0B4702C0527321BF CRC64; MALSITRGLL LLAALCCLAP TSLAGVLQGH AVQETDDTAH QEAACHKIAP NLANFAFSIY HKLAHQSNTS NIFFSPVSIA SAFAMLSLGA KGNTHTEILE GLGFNLTELA EAEIHKGFQH LLHTLNQPNH QLQLTTGNGL FINESAKLVD TFLEDVKNLH HSKAFSINFR DAEEAKKKIN DYVEKGSHGK IVDLVKDLDQ DTVFALVNYI SFKGKWEKPF EVEHTTERDF HVNEQTTVKV PMMNRLGMFD LHYCDKLASW VLLLDYVGNV TACFILPDLG KLQQLEDKLN NELLAKFLEK KYASSANLHL PKLSISETYD LKTVLGELGI NRVFSNGADL SGITEEQPLM VSKALHKAAL TIDEKGTEAA GATFLEAIPM SLPPDVEFNR PFLCILYDRN TKSPLFVGKV VNPTQA // ID A1BG_EQUAS Reviewed; 20 AA. AC P39090; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 31-OCT-2006, entry version 25. DE Alpha-1B-glycoprotein (Alpha-1-B glycoprotein) (Postalbumin) DE (Fragment). GN Name=A1BG; OS Equus asinus (Donkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9793; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Plasma; RX MEDLINE=91330579; PubMed=1868686; RA Patterson S.D., Bell K., Shaw D.C.; RT "Donkey and horse alpha 1 B-glycoprotein: partial characterization and RT new alleles."; RL Comp. Biochem. Physiol. 98B:523-528(1991). CC -!- FUNCTION: Unknown. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- PTM: Glycosylated (Probable). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- KW Direct protein sequencing; Glycoprotein; Immunoglobulin domain. FT CHAIN 1 >20 Alpha-1B-glycoprotein. FT /FTId=PRO_0000072663. FT NON_TER 20 20 SQ SEQUENCE 20 AA; 2197 MW; 65857DFDA68EBD9F CRC64; AVVFDPQPAL WAEADTQLEP // ID A1BG_HORSE Reviewed; 41 AA. AC P39091; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 31-OCT-2006, entry version 25. DE Alpha-1B-glycoprotein (Alpha-1-B glycoprotein) (Plasma protein XK) DE (Fragment). GN Name=A1BG; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Plasma; RX MEDLINE=89250430; PubMed=3248368; RA van de Weghe A., Coppieters W., Bauw G., Vandekerckhove J., RA Bouquet Y.; RT "The homology between the serum proteins PO2 in pig, Xk in horse and RT alpha 1B-glycoprotein in human."; RL Comp. Biochem. Physiol. 90B:751-756(1988). CC -!- FUNCTION: Unknown. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- PTM: Glycosylated (Probable). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; PL0028; PL0028. KW Direct protein sequencing; Glycoprotein; Immunoglobulin domain. FT CHAIN 1 >41 Alpha-1B-glycoprotein. FT /FTId=PRO_0000072664. FT CARBOHYD 23 23 N-linked (GlcNAc...) (Potential). FT VARIANT 11 11 W -> L. FT VARIANT 26 26 Q -> V. FT VARIANT 37 37 G -> E. FT NON_TER 41 41 SQ SEQUENCE 41 AA; 4459 MW; 2AA928CBA51FFED6 CRC64; AVVFDPPPAL WAEADXQQEP LRNLTQTVGQ YLPTLSGXLA E // ID A1BG_HUMAN Reviewed; 495 AA. AC P04217; Q8IYJ6; Q96P39; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2004, sequence version 3. DT 20-FEB-2007, entry version 75. DE Alpha-1B-glycoprotein precursor (Alpha-1-B glycoprotein). GN Name=A1BG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zhao Y., Sun D.; RT "Molecular cloning and characterization of the human A1BG gene."; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-495. RC TISSUE=Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 22-495, DISULFIDE BONDS, AND GLYCOSYLATION AT RP ASN-44; ASN-179; ASN-363 AND ASN-371. RX MEDLINE=86205955; PubMed=3458201; RA Ishioka N., Takahashi N., Putnam F.W.; RT "Amino acid sequence of human plasma alpha 1B-glycoprotein: homology RT to the immunoglobulin supergene family."; RL Proc. Natl. Acad. Sci. U.S.A. 83:2363-2367(1986). RN [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44 AND ASN-179, AND MASS RP SPECTROMETRY. RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44; ASN-179; ASN-363 AND RP ASN-371, AND MASS SPECTROMETRY. RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). CC -!- FUNCTION: Not known. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- SIMILARITY: Contains 5 Ig-like V-type (immunoglobulin-like) CC domains. CC -!- WEB RESOURCE: NAME=SHMPD; CC NOTE=The Singapore human mutation and polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=alpha1B". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF414429; AAL07469.1; -; mRNA. DR EMBL; BC035719; AAH35719.1; ALT_INIT; mRNA. DR UniGene; Hs.529161; -. DR MEROPS; I43.950; -. DR SWISS-2DPAGE; P04217; HUMAN. DR Cornea-2DPAGE; P04217; HUMAN. DR DOSAC-COBS-2DPAGE; P04217; HUMAN. DR REPRODUCTION-2DPAGE; P04217; HUMAN. DR Siena-2DPAGE; P04217; -. DR Ensembl; ENSG00000121410; Homo sapiens. DR KEGG; hsa:1; -. DR HGNC; HGNC:5; A1BG. DR MIM; 138670; gene. DR ArrayExpress; P04217; -. DR GermOnline; ENSG00000121410; Homo sapiens. DR RZPD-ProtExp; T3535; -. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR InterPro; IPR013151; Ig. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003598; Ig_sub2. DR Pfam; PF00047; ig; 2. DR SMART; SM00408; IGc2; 1. DR PROSITE; PS50835; IG_LIKE; 1. KW Direct protein sequencing; Glycoprotein; Immunoglobulin domain; KW Polymorphism; Repeat; Signal. FT SIGNAL 1 21 FT CHAIN 22 495 Alpha-1B-glycoprotein. FT /FTId=PRO_0000014502. FT DOMAIN 22 113 Ig-like V-type 1. FT DOMAIN 114 206 Ig-like V-type 2. FT DOMAIN 207 299 Ig-like V-type 3. FT DOMAIN 300 397 Ig-like V-type 4. FT DOMAIN 398 495 Ig-like V-type 5. FT CARBOHYD 44 44 N-linked (GlcNAc...). FT CARBOHYD 179 179 N-linked (GlcNAc...). FT CARBOHYD 363 363 N-linked (GlcNAc...). FT CARBOHYD 371 371 N-linked (GlcNAc...). FT DISULFID 49 93 Probable. FT DISULFID 139 182 FT DISULFID 232 279 FT DISULFID 325 374 FT DISULFID 423 470 Probable. FT VARIANT 52 52 R -> H (in dbSNP:rs893184). FT /FTId=VAR_018369. FT VARIANT 395 395 H -> R (in dbSNP:rs2241788). FT /FTId=VAR_018370. FT CONFLICT 105 105 S -> G (in Ref. 1). FT CONFLICT 127 127 S -> P (in Ref. 1). FT CONFLICT 146 146 V -> E (in Ref. 1). FT CONFLICT 413 413 V -> A (in Ref. 1). FT CONFLICT 446 447 VR -> IP (in Ref. 1). SQ SEQUENCE 495 AA; 54273 MW; FBF648A8C62BE085 CRC64; MSMLVVFLLL WGVTWGPVTE AAIFYETQPS LWAESESLLK PLANVTLTCQ ARLETPDFQL FKNGVAQEPV HLDSPAIKHQ FLLTGDTQGR YRCRSGLSTG WTQLSKLLEL TGPKSLPAPW LSMAPVSWIT PGLKTTAVCR GVLRGVTFLL RREGDHEFLE VPEAQEDVEA TFPVHQPGNY SCSYRTDGEG ALSEPSATVT IEELAAPPPP VLMHHGESSQ VLHPGNKVTL TCVAPLSGVD FQLRRGEKEL LVPRSSTSPD RIFFHLNAVA LGDGGHYTCR YRLHDNQNGW SGDSAPVELI LSDETLPAPE FSPEPESGRA LRLRCLAPLE GARFALVRED RGGRRVHRFQ SPAGTEALFE LHNISVADSA NYSCVYVDLK PPFGGSAPSE RLELHVDGPP PRPQLRATWS GAVLAGRDAV LRCEGPIPDV TFELLREGET KAVKTVRTPG AAANLELIFV GPQHAGNYRC RYRSWVPHTF ESELSDPVEL LVAES // ID A1BG_PIG Reviewed; 40 AA. AC P39092; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 31-OCT-2006, entry version 24. DE Alpha-1B-glycoprotein (Alpha-1-B glycoprotein) (Plasma protein PO2-F) DE (Fragment). GN Name=A1BG; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Plasma; RX MEDLINE=89250430; PubMed=3248368; RA van de Weghe A., Coppieters W., Bauw G., Vandekerckhove J., RA Bouquet Y.; RT "The homology between the serum proteins PO2 in pig, Xk in horse and RT alpha 1B-glycoprotein in human."; RL Comp. Biochem. Physiol. 90B:751-756(1988). CC -!- FUNCTION: Unknown. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; PL0030; PL0030. KW Direct protein sequencing; Glycoprotein; Immunoglobulin domain. FT CHAIN 1 >40 Alpha-1B-glycoprotein. FT /FTId=PRO_0000072665. FT CARBOHYD 23 23 N-linked (GlcNAc...). FT VARIANT 30 30 S -> G. FT NON_TER 40 40 SQ SEQUENCE 40 AA; 4448 MW; BE2F7783EB5B9F0D CRC64; ALFLDPPPNL WAEAQSLLEP WANVTLTSQS RLPVLNFQGL // ID A1BG_RAT Reviewed; 513 AA. AC Q9EPH1; Q5EBD6; Q9JKL2; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 2. DT 20-FEB-2007, entry version 38. DE Alpha-1B-glycoprotein precursor (Liver regeneration-related protein 1) DE (C44). GN Name=A1bg; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND INDUCTION. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX MEDLINE=21255654; PubMed=11356721; DOI=10.1210/en.142.6.2695; RA Gardmo C., Persson B., Mode A.; RT "Cloning of a novel growth hormone-regulated rat complementary RT deoxyribonucleic acid with homology to the human alpha1B-glycoprotein, RT characterizing a new protein family."; RL Endocrinology 142:2695-2701(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 219-513 (ISOFORM 2), AND TISSUE RP SPECIFICITY. RC STRAIN=Wistar; TISSUE=Liver; RX MEDLINE=20551479; PubMed=11097837; DOI=10.1006/bbrc.2000.3792; RA Xu W., Wang S., Wang G., Wei H., He F., Yang X.; RT "Identification and characterization of differentially expressed genes RT in the early response phase during liver regeneration."; RL Biochem. Biophys. Res. Commun. 278:318-325(2000). CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9EPH1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9EPH1-2; Sequence=VSP_051640, VSP_051641; CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in normal liver. CC Isoform 2 is expressed in the regenerating liver after partial CC hepatectomy and at very low levels in the normal lung, brain and CC testis. CC -!- DEVELOPMENTAL STAGE: In females, isoform 1 is expressed at day 35 CC with higher levels detected at day 56. Isoform 1 is not detected CC in males of any age. CC -!- INDUCTION: Isoform 1 is up-regulated by continuous exposure to CC growth hormone. CC -!- SIMILARITY: Contains 5 Ig-like V-type (immunoglobulin-like) CC 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; AJ302031; CAC19029.1; -; mRNA. DR EMBL; BC089771; AAH89771.1; -; mRNA. DR EMBL; AF236054; AAF68963.1; ALT_INIT; mRNA. DR UniGene; Rn.53990; -. DR HSSP; Q8NHL6; 1G0X. DR Ensembl; ENSRNOG00000004692; Rattus norvegicus. DR KEGG; rno:140656; -. DR RGD; 69417; A1bg. DR GermOnline; ENSRNOG00000004692; Rattus norvegicus. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR InterPro; IPR013151; Ig. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR Pfam; PF00047; ig; 2. DR SMART; SM00409; IG; 1. DR PROSITE; PS50835; IG_LIKE; 1. KW Alternative splicing; Glycoprotein; Immunoglobulin domain; Repeat; KW Signal. FT SIGNAL 1 20 Potential. FT CHAIN 21 513 Alpha-1B-glycoprotein. FT /FTId=PRO_0000014503. FT DOMAIN 22 126 Ig-like V-type 1. FT DOMAIN 127 219 Ig-like V-type 2. FT DOMAIN 220 312 Ig-like V-type 3. FT DOMAIN 313 415 Ig-like V-type 4. FT DOMAIN 416 513 Ig-like V-type 5. FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential). FT CARBOHYD 89 89 N-linked (GlcNAc...) (Potential). FT CARBOHYD 192 192 N-linked (GlcNAc...) (Potential). FT CARBOHYD 369 369 N-linked (GlcNAc...) (Potential). FT CARBOHYD 381 381 N-linked (GlcNAc...) (Potential). FT CARBOHYD 389 389 N-linked (GlcNAc...) (Potential). FT CARBOHYD 485 485 N-linked (GlcNAc...) (Potential). FT DISULFID 49 96 By similarity. FT DISULFID 153 195 By similarity. FT DISULFID 245 292 By similarity. FT DISULFID 343 392 By similarity. FT DISULFID 441 488 By similarity. FT VAR_SEQ 417 473 PAPKPRLEALWKGKVPLGHEAIFQCHGHVPRVSMELVREGF FT KTPFWMASTTSTSAFL -> ELRRTMTEEGTERYSLRNQGS FT CAVISQLYLNEVLGFENLEEISLRCETWKSGLFRIL (in FT isoform 2). FT /FTId=VSP_051640. FT VAR_SEQ 474 513 Missing (in isoform 2). FT /FTId=VSP_051641. FT CONFLICT 24 24 D -> N (in Ref. 1). FT CONFLICT 204 204 K -> E (in Ref. 1). FT CONFLICT 239 239 T -> A (in Ref. 3). FT CONFLICT 242 242 T -> M (in Ref. 3). FT CONFLICT 283 283 E -> K (in Ref. 3). SQ SEQUENCE 513 AA; 56479 MW; 9CFA96A8BBC2ED1D CRC64; MSLLTTVLLL WGFTLGPGNA LWLDSGSEPE LRAEPQSLLE PWANLTLVCA VDLPTKVFEL IMNGWFLSQV RLETPVLSYR FSLGAITSNN SGVYRCRCGV EPPVDIQLPA LSKWTMLSNA LEVTGKEPLP PPSAHADPVS WITPGGLPVY IMCRVAMRGV TYLLRKEGVD GTQKPDVQHK GTAGFLIYKP GNYSCSYLTH AGGKPSEPSA IVTIKMSATQ LPPSLCLMGS YLTIYPQKTH ETLACKAPRN AAEFQLRQGE RVLNIQGFSP TRDATIYYVN LKELDNQSPF TCRYRMHKYM HVWSEDSKPV ELMWSDEKLP APVLTAEPSS HNLEPGSTVQ LRCTAHKAGL RFGLQRQGKP DLVVVQMLNS SGTEAVFELH NISTIDSGNY SCIYMEQAPP FSGSASSEPL ELRINGPAPK PRLEALWKGK VPLGHEAIFQ CHGHVPRVSM ELVREGFKTP FWMASTTSTS AFLKLSFVGP QHTGNYSCRY TALSPFTFES GISDPVEVVV EGS // ID A1I3_RAT Reviewed; 1477 AA. AC P14046; Q4G042; Q63266; Q6LDP2; Q6LDR8; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 20-FEB-2007, entry version 64. DE Alpha-1-inhibitor 3 precursor (Alpha-1-inhibitor III) (Alpha-1- DE inhibitor 3 variant II). GN Name=A1i3; Synonyms=Mug1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX MEDLINE=88153707; PubMed=2831216; RA Braciak T.A., Northemann W., Hudson G.O., Shiels B.R., Gehring M.R., RA Fey G.H.; RT "Sequence and acute phase regulation of rat alpha 1-inhibitor III RT messenger RNA."; RL J. Biol. Chem. 263:3999-4012(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-143. RC STRAIN=Fischer 344; TISSUE=Liver; RX MEDLINE=89207568; PubMed=2495816; DOI=10.1021/bi00427a013; RA Northemann W., Shiels B.R., Braciak T.A., Fey G.H.; RT "Structure and negative transcriptional regulation by glucocorticoids RT of the acute-phase rat alpha 1-inhibitor III gene."; RL Biochemistry 28:84-95(1989). RN [3] RP PROTEIN SEQUENCE OF 673-723. RX MEDLINE=89291900; PubMed=2472396; RA Enghild J.J., Salvesen G., Thogersen I.B., Pizzo S.V.; RT "Proteinase binding and inhibition by the monomeric alpha- RT macroglobulin rat alpha 1-inhibitor-3."; RL J. Biol. Chem. 264:11428-11435(1989). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 757-1477. 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 1253-1477. RC TISSUE=Liver; RX MEDLINE=87190405; PubMed=2436907; RA Schweizer M., Takabayashi K., Geiger T., Laux T., Biermann G., RA Buhler J.M., Gauthier F., Roberts L.M., Heinrich P.C.; RT "Identification and sequencing of cDNA clones for the rodent negative RT acute-phase protein alpha 1-inhibitor 3."; RL Eur. J. Biochem. 164:375-381(1987). CC -!- FUNCTION: Protease inhibitor with a wide spectrum of protein CC targets, which attaches through its thioester function. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J03552; AAA40628.1; -; mRNA. DR EMBL; M22993; AAA79025.1; -; Genomic_DNA. DR EMBL; M28297; AAA63493.1; -; mRNA. DR EMBL; M28298; AAA63494.1; -; mRNA. DR EMBL; BC098768; AAH98768.1; -; mRNA. DR PIR; A29952; A29952. DR UniGene; Rn.109457; -. DR UniGene; Rn.198689; -. DR HSSP; P01023; 1BV8. DR MEROPS; I39.004; -. DR Ensembl; ENSRNOG00000005599; Rattus norvegicus. DR KEGG; rno:297568; -. DR RGD; 621366; Mug1. DR ArrayExpress; P14046; -. DR GermOnline; ENSRNOG00000005599; Rattus norvegicus. DR GO; GO:0017114; F:wide-spectrum protease inhibitor activity; NAS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IEP:RGD. DR InterPro; IPR011626; A2M_comp. DR InterPro; IPR002890; A2M_N. DR InterPro; IPR011625; A2M_N_2. DR InterPro; IPR011627; A2M_rcpt. DR InterPro; IPR009048; AMG_rcpt_bd. DR InterPro; IPR001599; MacrogloblnA2. DR InterPro; IPR008930; Terp_cyc_toroid. DR Pfam; PF00207; A2M; 1. DR Pfam; PF07678; A2M_comp; 1. DR Pfam; PF01835; A2M_N; 1. DR Pfam; PF07703; A2M_N_2; 1. DR Pfam; PF07677; A2M_recep; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. KW Bait region; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor; Signal; Thioester bond. FT SIGNAL 1 24 FT CHAIN 25 1477 Alpha-1-inhibitor 3. FT /FTId=PRO_0000000061. FT REGION 601 750 Bait region (approximate). FT CARBOHYD 55 55 N-linked (GlcNAc...) (Potential). FT CARBOHYD 247 247 N-linked (GlcNAc...) (Potential). FT CARBOHYD 301 301 N-linked (GlcNAc...) (Potential). FT CARBOHYD 321 321 N-linked (GlcNAc...) (Potential). FT CARBOHYD 393 393 N-linked (GlcNAc...) (Potential). FT CARBOHYD 508 508 N-linked (GlcNAc...) (Potential). FT CARBOHYD 750 750 N-linked (GlcNAc...) (Potential). FT CARBOHYD 777 777 N-linked (GlcNAc...) (Potential). FT CARBOHYD 872 872 N-linked (GlcNAc...) (Potential). FT CARBOHYD 994 994 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1143 1143 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1314 1314 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1427 1427 N-linked (GlcNAc...) (Potential). FT DISULFID 48 86 By similarity. FT DISULFID 251 295 By similarity. FT DISULFID 269 283 By similarity. FT DISULFID 468 563 By similarity. FT DISULFID 595 774 By similarity. FT DISULFID 643 678 By similarity. FT DISULFID 850 886 By similarity. FT DISULFID 924 1324 By similarity. FT DISULFID 1082 1130 By similarity. FT DISULFID 1355 1470 By similarity. FT CROSSLNK 975 978 Isoglutamyl cysteine thioester (Cys-Gln). FT CONFLICT 677 677 Y -> T (in Ref. 3). FT CONFLICT 1373 1373 M -> T (in Ref. 5; AAH98768). FT CONFLICT 1406 1406 G -> E (in Ref. 5; AAA63494). FT CONFLICT 1474 1474 D -> N (in Ref. 5; AAA63494). SQ SEQUENCE 1477 AA; 163773 MW; 4DC05367C8385D2B CRC64; MKKDREAQLC LFSALLAFLP FASLLNGNSK YMVLVPSQLY TETPEKICLH LYHLNETVTV TASLISQRGT RKLFDELVVD KDLFHCVSFT IPRLPSSEEE ESLDINIEGA KHKFSERRVV LVKNKESVVF VQTDKPMYKP GQSVKFRVVS MDKNLHPLNE LFPLAYIEDP KMNRIMQWQD VKTENGLKQL SFSLSAEPIQ GPYKIVILKQ SGVKEEHSFT VMEFVLPRFG VDVKVPNAIS VYDEIINVTA CATYTYGKPV PGHVKISLCH GNPTFSSETK SGCKEEDSRL DNNGCSTQEV NITEFQLKEN YLKMHQAFHV NATVTEEGTG SEFSGSGRIE VERTRNKFLF LKADSHFRHG IPFFVKVRLV DIKGDPIPNE QVLIKARDAG YTNATTTDQH GLAKFSIDTN GISDYSLNIK VYHKEESSCI HSSCTAERHA EAHHTAYAVY SLSKSYIYLD TEAGVLPCNQ IHTVQAHFIL KGQVLGVLQQ IVFHYLVMAQ GSILQTGNHT HQVEPGESQV QGNFALEIPV EFSMVPVAKM LIYTILPDGE VIADSVKFQV EKCLRNKVHL SFSPSQSLPA SQTHMRVTAS PQSLCGLRAV DQSVLLQKPE AELSPSLIYD LPGMQDSNFI ASSNDPFEDE DYCLMYQPIA REKDVYRYVR ETGLMAFTNL KIKLPTYCNT DYDMVPLAVP AVALDSSTDR GMYESLPVVA VKSPLPQEPP RKDPPPKDPV IETIRNYFPE TWIWDLVTVN SSGVTELEMT VPDTITEWKA GALCLSNDTG LGLSSVASFQ AFQPFFVELT MPYSVIRGEA FTLKATVLNY LPTSLPMAVL LEASPDFTAV PVENNQDSYC LGANGRHTSS WLVTPKSLGN VNFSVSAEAR QSPGPCGSEV ATVPETGRKD TVVKVLIVEP EGIKKEHTFS SLLCASDAEL SETLSLLLPP TVVKDSARAH FSVMGDILSS AIKNTQNLIQ MPYGCGEQNM VLFAPNIYVL KYLNETQQLT EKIKSKALGY LRAGYQRELN YKHKDGSYSA FGDHNGQGQG NTWLTAFVLK SFAQARAFIF IDESHITDAF TWLSKQQKDS GCFRSSGSLL NNAMKGGVDD EITLSAYITM ALLESSLPDT DPVVSKALSC LESSWENIEQ GGNGSFVYTK ALMAYAFALA GNQEKRNEIL KSLDKEAIKE DNSIHWERPQ KPTKSEGYLY TPQASSAEVE MSAYVVLARL TAQPAPSPED LALSMGTIKW LTKQQNSYGG FSSTQDTVVA LDALSKYGAA TFSKSQKTPS VTVQSSGSFS QKFQVDKSNR LLLQQVSLPY IPGNYTVSVS GEGCVYAQTT LRYNVPLEKQ QPAFALKVQT VPLTCNNPKG QNSFQISLEI SYMGSRPASN MVIADVKMLS GFIPLKPTVK KLERLGHVSR TEVTTNNVLL YLDQVTNQTL SFSFIIQQDI PVKNLQPAIV KVYDYYETDE VAFAEYSSPC SSDDQNV // ID A1M_RAT Reviewed; 1500 AA. AC Q63041; Q63332; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-JAN-2007, entry version 33. DE Alpha-1-macroglobulin precursor (Alpha-1-M) [Contains: Alpha-1- DE macroglobulin 165 kDa subunit; Alpha-1-macroglobulin 45 kDa subunit]. GN Name=A1m; Synonyms=Pzp; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-54; 724-743; RP 901-930 AND 1245-1269, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=Fischer 344; TISSUE=Liver; RX PubMed=1725450; RA Eggertsen G., Hudson G., Shiels B., Reed D., Fey G.H.; RT "Sequence of rat alpha 1-macroglobulin, a broad-range proteinase RT inhibitor from the alpha-macroglobulin-complement family."; RL Mol. Biol. Med. 8:287-302(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX MEDLINE=92172859; PubMed=1371696; DOI=10.1021/bi00123a020; RA Warmegard B., Martin N., Johansson S.; RT "cDNA cloning and sequencing of rat alpha 1-macroglobulin."; RL Biochemistry 31:2346-2352(1992). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1362-1495. RX MEDLINE=20555747; PubMed=11106161; RA Xiao T., DeCamp D.L., Spran S.R.; RT "Structure of a rat alpha 1-macroglobulin receptor-binding domain RT dimer."; RL Protein Sci. 9:1889-1897(2000). CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a CC unique 'trapping' mechanism. This protein has a peptide stretch, CC called the 'bait region' which contains specific cleavage sites CC for different proteinases. When a proteinase cleaves the bait CC region, a conformational change is induced in the protein which CC traps the proteinase. The entrapped enzyme remains active against CC low molecular weight substrates (activity against high molecular CC weight substrates is greatly reduced). Following cleavage in the CC bait region a thioester bond is hydrolyzed and mediates the CC covalent binding of the protein to the proteinase (By similarity). CC -!- SUBUNIT: Homotetramer; disulfide-linked (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level in ovary, CC testis, uterus and prostate. Protein found in plasma. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M77183; AAA40723.1; -; mRNA. DR EMBL; M84000; AAA41591.1; -; mRNA. DR PIR; A42210; A42210. DR UniGene; Rn.11295; -. DR PDB; 1EDY; X-ray; A/B=1362-1495. DR MEROPS; I39.001; -. DR Ensembl; ENSRNOG00000006709; Rattus norvegicus. DR RGD; 628643; Pzp. DR ArrayExpress; Q63041; -. DR InterPro; IPR011626; A2M_comp. DR InterPro; IPR002890; A2M_N. DR InterPro; IPR011625; A2M_N_2. DR InterPro; IPR011627; A2M_rcpt. DR InterPro; IPR009048; AMG_rcpt_bd. DR InterPro; IPR001599; MacrogloblnA2. DR InterPro; IPR008930; Terp_cyc_toroid. DR Pfam; PF00207; A2M; 1. DR Pfam; PF07678; A2M_comp; 1. DR Pfam; PF01835; A2M_N; 1. DR Pfam; PF07703; A2M_N_2; 1. DR Pfam; PF07677; A2M_recep; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. KW 3D-structure; Bait region; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor; Signal; Thioester bond. FT SIGNAL 1 24 FT CHAIN 25 1500 Alpha-1-macroglobulin 165 kDa subunit. FT /FTId=PRO_0000271403. FT CHAIN 1245 1500 Alpha-1-macroglobulin 45 kDa subunit. FT /FTId=PRO_0000271404. FT REGION 686 746 Bait region (By similarity). FT REGION 1360 1500 Receptor-binding domain. FT CARBOHYD 55 55 N-linked (GlcNAc...) (Potential). FT CARBOHYD 61 61 N-linked (GlcNAc...) (Potential). FT CARBOHYD 157 157 N-linked (GlcNAc...) (Potential). FT CARBOHYD 382 382 N-linked (GlcNAc...) (Potential). FT CARBOHYD 412 412 N-linked (GlcNAc...) (Potential). FT CARBOHYD 568 568 N-linked (GlcNAc...) (Potential). FT CARBOHYD 883 883 N-linked (GlcNAc...) (Potential). FT CARBOHYD 944 944 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1005 1005 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1390 1390 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1448 1448 N-linked (GlcNAc...) (Potential). FT DISULFID 48 86 By similarity. FT DISULFID 249 298 By similarity. FT DISULFID 267 286 By similarity. FT DISULFID 277 277 Interchain (with C-430) (By similarity). FT DISULFID 430 430 Interchain (with C-277) (By similarity). FT DISULFID 469 562 By similarity. FT DISULFID 594 785 By similarity. FT DISULFID 642 689 By similarity. FT DISULFID 835 863 By similarity. FT DISULFID 861 897 By similarity. FT DISULFID 935 1344 By similarity. FT DISULFID 1094 1142 By similarity. FT CROSSLNK 986 989 Isoglutamyl cysteine thioester (Cys-Gln) FT (By similarity). FT CONFLICT 50 50 H -> A (in Ref. 1). FT CONFLICT 918 918 I -> P (in Ref. 1). FT CONFLICT 924 925 IE -> AT (in Ref. 1). SQ SEQUENCE 1500 AA; 167125 MW; 8ABB810985795AB2 CRC64; MRRNQLPIPV FLLLLLLLPR DATAATGKPR YVVLVPSELY AGVPEKVCVH LNHLNETVTL NVTLEYGVQY SNLLIDQAVD KDSSYCSSFT ISRPLSPSAL IAVEIKGPTH HFIKKKSMWI TKAESPVFVQ TDKPIYKPGQ TVKFRVVSVD ISFRPVNETF PVVYIENPKR NRIFQWQNVD LPGGLHQLSF PLSVEPALGI YKVVVQKDSG KKIEHSFEVK EYVLPKFEVQ VKMPKTMAFL EEELVVTACG LYTYGKPVPG LVTMKVCRKY TQSYSNCHGQ HSKSICEEFS KQADEKGCFR QVVKTKVFQP RQKGYDMKIE VEAKIKEDGT GIELTGTGSC EIANTLSKLK FTKANTFYRP GLPFFGQVLL VDEKGQPIPN KNLTVQVNSV RSQFTFTTDE HGLANILIDT TNFTFSFMGI RVIYKQNNIC FDNWWVDEYH TQADHSAARI FSPSRSYIQL ELVLGTLACG QTQEIRIHFL LNEDALKDAK DLTFYYLIKA RGSIFNSGSH VLPLEQGKVK GVVSFPIRVE PGMAPVAKLI VYTILPNEEL IADVQKFDIE KCFANTVNLS FPSAQSLPAS DTHLTVKATP LSLCALTAVD QSVLLLKPEA KLSPQSIYNL LPQKAEQGAY LGPLPYKGGE NCIKAEDITH NGIVYTPKQD LNDNDAYSVF QSIGLKIFTN TRVHKPRYCP MYQAYPPLPY VGEPQALAMS AIPGAGYRSS NIRTSSMMMM GASEVAQEVE VRETVRKYFP ETWIWDMVPL DLSGDGELPV KVPDTITEWK ASAFCLSGTT GLGLSSTISH KVFQPFFLEL TLPYSVVRGE AFILKATVLN YMPHCIRIHV SLEMSPDFLA VPVGSHEDSH CICGNERKTV SWAVTPKSLG EVNFTATAEA LQSPELCGNK VAEVPALVQK DTVVKPVIVE PEGIEKEQTY NTLLCPQDAE LQENWTLDLP ANVVEGSARA TQSVLGDILG SAMQNLQNLL QMPYGCGEQN MVLFVPNIYV LEYLNETQQL TEAIKSKAIS YLISGYQRQL NYQHSDGSYS TFGDRGMRHS QGNTWLTAFV LKAFAQAQSY IYIEKTHITN AFNWLSMKQR ENGCFQQSGS LLNNAMKGGV DDEVTLSAYI TIALLEMPLP VTHSVVRNAL FCLETAWASI SNSQESHVYT KALLAYAFAL AGNRAKRSEV LESLNKDAVN EEESVHWQRP KNVEENVREM RSFSYKPRAP SAEVEMTAYV LLAYLTSASS RPTRDLSSSD LTTASKIVKW ISKQQNSHGG FSSTQDTVVA LQALSKYGAA TFTKSNKEVS VTIESSGTVS GTLHVNNGNR LLLQEVRLAD LPGNYITKVS GSGCVYLQTS LKYNILPEAE GEAPFTLKVN TLPLNFDKAE HHRKFQIHIN VSYIGERPNS NMVIVDVKMV SGFIPVKPSV KKLQDQSNIQ RTEVNTNHVL IYIEKLTNQT MGFSFAVEQD IPVKNLKPAP VKVYDYYETD EFAIEEYSAP FSSDSEQGNA // ID A20A1_HUMAN Reviewed; 823 AA. AC Q5TYW2; Q9H0H6; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 20-FEB-2007, entry version 19. DE Ankyrin repeat domain-containing protein 20A1. GN Name=ANKRD20A1; Synonyms=ANKRD20A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX MEDLINE=21154917; PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). CC -!- SIMILARITY: Contains 5 ANK 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; AL136793; CAB66727.1; -; mRNA. DR EMBL; BX649567; CAH71137.1; -; Genomic_DNA. DR UniGene; Hs.632671; -. DR HSSP; Q60778; 1OY3. DR Ensembl; ENSG00000196774; Homo sapiens. DR HGNC; HGNC:23665; ANKRD20A1. DR GermOnline; ENSG00000196774; Homo sapiens. DR GO; GO:0005886; C:plasma membrane; IDA:LIFEdb. DR InterPro; IPR002110; ANK. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. DR Pfam; PF00023; Ank; 6. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 6. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 4. KW ANK repeat; Coiled coil; Repeat. FT CHAIN 1 823 Ankyrin repeat domain-containing protein FT 20A1. FT /FTId=PRO_0000240834. FT REPEAT 66 95 ANK 1. FT REPEAT 99 128 ANK 2. FT REPEAT 132 161 ANK 3. FT REPEAT 165 194 ANK 4. FT REPEAT 198 227 ANK 5. FT COILED 431 480 Potential. FT COILED 565 724 Potential. FT COILED 776 805 Potential. FT CONFLICT 76 76 T -> A (in Ref. 1). FT CONFLICT 128 128 L -> F (in Ref. 1). FT CONFLICT 499 499 W -> R (in Ref. 1). FT CONFLICT 679 679 R -> C (in Ref. 1). FT CONFLICT 772 772 G -> E (in Ref. 1). FT CONFLICT 805 805 E -> G (in Ref. 1). SQ SEQUENCE 823 AA; 94048 MW; 0AE8585829E6E91B CRC64; MKLFGFGSRR GQTAQGSIDH VYTGSGYRIR DSELQKIHRA AVKGDAAEVE RCLARRSGDL DALDKQHRTA LHLACTSGHV QVVTLLVNRK CQIDVCDKEN RTPLIQAVHC QEEACAVILL EHGANPNLKD IYGNTALHYA VYSESTSLAE KLLSHGAHIE ALDKDNNTPL LFAIICKKEK MVEFLLKKKA SSHAVDRLRR SALMLAVYYD SPGIVNILLK QNIDVFAQDM CGRDAEDYAI SHHLTKIQQQ ILEHKKKILK KEKSDVGSSD ESAVSIFHEL RVDSLPASDD KDLNVATKQC VPEKVSEPLP GSSHEKGNRI VNGQGEGPPA KHPSLKPSTE VEDPAVKGAV QRKNVQTLRA EQALPVASEE EQERHERSEK KQPQVKEGNN TNKSEKIQLS ENICDSTSSA AAGRLTQQRK IGKTYPQQFP KKLKEEHDRC TLKQENEEKT NVNMLYKKNR EELERKEKQY KKEVEAKQLE PTVQSLEMKS KTARNTPNWD FHNHEEMKGL MDENCILKAD IAILRQEICT MKNDNLEKEN KYLKDIKIVK ETNAALEKYI KLNEEMITET AFRYQQELND LKAENTRLNA ELLKEKESKK RLEADIESYQ SRLAAAISKH SESVKTERNL KLALERTRDV SVQVEMSSAI SKVKAENEFL TEQLSETQIK FNALKDKFRK TRDSLRKKSL ALETVQNDLS QTQQQTQEMK EMYQNAEAKV NNSTGKWNCV EERICHLQRE NAWLVQQLDD VHQKEDHKEI VTNIQRGFIE SGKKDLVLEE KSKKLMNECD HLKESLFQYE REKTEGVVSI KEDKYFQTSR KTI // ID A20A2_HUMAN Reviewed; 823 AA. AC Q4UJ75; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 20-FEB-2007, entry version 13. DE Ankyrin repeat domain-containing protein 20A2. GN Name=ANKRD20A2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). CC -!- SIMILARITY: Contains 5 ANK 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; CR769776; CAI95383.1; -; Genomic_DNA. DR UniGene; Hs.632663; -. DR UniGene; Hs.645502; -. DR HGNC; HGNC:31979; ANKRD20A2. DR GermOnline; ENSG00000172014; Homo sapiens. DR InterPro; IPR002110; ANK. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. DR Pfam; PF00023; Ank; 5. DR SMART; SM00248; ANK; 6. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 4. KW ANK repeat; Coiled coil; Repeat. FT CHAIN 1 823 Ankyrin repeat domain-containing protein FT 20A2. FT /FTId=PRO_0000240835. FT REPEAT 66 95 ANK 1. FT REPEAT 99 128 ANK 2. FT REPEAT 132 161 ANK 3. FT REPEAT 165 194 ANK 4. FT REPEAT 198 227 ANK 5. FT COILED 431 480 Potential. FT COILED 565 724 Potential. FT COILED 776 806 Potential. SQ SEQUENCE 823 AA; 94149 MW; 597B760D5733208A CRC64; MKLFGFGSRR GQTAQGSIDH VYTGSGYRIR DSELQKIHRA AVKGDAAEVE RCLARRSGEL DALDKQHRTA LHLACASGHV QVVTLLVNRK CQIDVCDKEN RTPLIQAVHC QEEACAVILL EHGANPNLKD IYGNTALHYA VYSESTSLAE KLLSHGAHIE ALDKDNNTPL LFAIICKKEK MVEFLLKKKA SSHAVDRLRR SALMLAVYYD SPGIVNILLK QNIDVFAQDM CGRDAEDYAI SHHLTKIQQQ ILEHKKKILK KEKSDVGSSD ESAVSIFHEL RVDSLPASDD KDLNVATKQC VPEKVSEPLP GSSHEKGNRI VNGQGEGPPA KHPSLKPSTE VEDPAVKGAV QRKNVQTLRA EQALPVASEE EQQRHERSEK KQPQVKEGNN TNKSEKIQLS ENICDSTSSA AAGRLTQQRK IGKTYPQQFP KKLKEEHDRC TLKQENEEKT NVNMLYKKNR EELERKEKQY KKEVEAKQLE PTVQSLEMKS KTARNTPNWD FHNHEEMKGL MDENCILKAD IAILRQEICT MKNDNLEKEN KYLKDIKIVK ETNAALEKYI KLNEEMITET AFRYQQELND LKAENTRLNA ELLKEKESKK RLEADIESYQ SRLAAAISKH SESVKTERNL KLALERTQDV SVQVEMSSAI SKVKDENEFL TEQLSETQIK FNALKDKFRK TRDSLRKKSL ALETVQNNLS QTQQQTQEMK EMYQNAEAKV NNSTGKWNCV EERICHLQRE NAWLVQQLDD VHQKEDHKEI VTNIQRGFIE SGKKDFVLEE KSKKLMNECD HLKESLFQYE REKTEVVVSI KEDKYFQTSR KKI // ID A20A3_HUMAN Reviewed; 823 AA. AC Q5VUR7; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 20-FEB-2007, entry version 20. DE Ankyrin repeat domain-containing protein 20A3. GN Name=ANKRD20A3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). CC -!- SIMILARITY: Contains 5 ANK 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; AL513478; CAH72532.1; -; Genomic_DNA. DR UniGene; Hs.632663; -. DR Ensembl; ENSG00000132498; Homo sapiens. DR HGNC; HGNC:31981; ANKRD20A3. DR LinkHub; Q5VUR7; -. DR GermOnline; ENSG00000132498; Homo sapiens. DR InterPro; IPR002110; ANK. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. DR Pfam; PF00023; Ank; 6. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 6. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 4. KW ANK repeat; Coiled coil; Repeat. FT CHAIN 1 823 Ankyrin repeat domain-containing protein FT 20A3. FT /FTId=PRO_0000240836. FT REPEAT 66 95 ANK 1. FT REPEAT 99 128 ANK 2. FT REPEAT 132 161 ANK 3. FT REPEAT 165 194 ANK 4. FT REPEAT 198 227 ANK 5. FT COILED 431 480 Potential. FT COILED 571 724 Potential. FT COILED 776 805 Potential. SQ SEQUENCE 823 AA; 94108 MW; CC0ED7895CA092E4 CRC64; MKLFGFGSRR GQTAQGSIDH VYTGSGYRIR DSELQKIHRA AVKGDAAEVE RCLARRSGDL DALDKQHRTA LHLACASGHV QVVTLLVNRK CQIDVCDKEN RTPLIQAVHC QEEACAVILL EHGANPNLKD IYGNTALHYA VYSESTSLAE KLLSHGAHIE ALDKDNNTPL LFAIICKKEK MVEFLLKRKA SSHAVDRLRR SALMLAVYYD SPGIVNILLK QNIDVFAQDM CGRDAEDYAI SHHLTKIQQQ ILEHKKKILK KEKSDVGSSD ESAVSIFHEL RVDSLPASDD KDLNVATKQC VPEKVSEPLP GSSHEKGNRI VNGQGEGPPA KHPSLKPSTE VEDPAVKGAV QRKNVQTLRA EQALPVASEE EQERHERSEK KQPQVKEGNN TNKSEKIQLS ENICDSTSSA AAGRLTQQRK IGKTYPQQFP KKLKEEHDRC TLKQENEEKT NVNMLYKKNR EELERKEKQY KKEVEAKQLE PTVQSLEMKS KTARNTPNRD FHNHEEMKGL MDENCILKAD IAILRQEICT MKNDNLEKEN KYLKDIKIVK ETNAALEKYI KLNEEMITET AFRYQQELNY LKAENTRLNA ELLKEKESKK RLEADIESYQ SRLAAAISKH SESVKTERNL KLALERTRDV SVQVEMSSAI SKVKDENEFL TEQLSETQIK FNALKDKFRK TRDSLRKKSL ALETVQNDLS QTQQQTQEMK EMYQNAEAKV NNSTGKWNCV EERICHLQRE NAWLVQQLDD VHQKEDHKEI VTNIQRGFIE SGKKDLVLEE KSKKLMNECD HLKESLFQYE REKTEGVVSI KEDKYFQTSR KTI // ID A20A4_HUMAN Reviewed; 823 AA. AC Q5SQ80; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 20-FEB-2007, entry version 20. DE Ankyrin repeat domain-containing protein 20A4. GN Name=ANKRD20A4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). CC -!- SIMILARITY: Contains 5 ANK 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; AL773545; CAI12706.1; -; Genomic_DNA. DR EMBL; BX664727; CAI12706.1; JOINED; Genomic_DNA. DR EMBL; BX664727; CAI39536.1; -; Genomic_DNA. DR EMBL; AL773545; CAI39536.1; JOINED; Genomic_DNA. DR UniGene; Hs.632663; -. DR Ensembl; ENSG00000183148; Homo sapiens. DR HGNC; HGNC:31982; ANKRD20A4. DR GermOnline; ENSG00000183148; Homo sapiens. DR InterPro; IPR002110; ANK. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. DR Pfam; PF00023; Ank; 6. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 6. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 4. KW ANK repeat; Coiled coil; Repeat. FT CHAIN 1 823 Ankyrin repeat domain-containing protein FT 20A4. FT /FTId=PRO_0000240837. FT REPEAT 66 95 ANK 1. FT REPEAT 99 128 ANK 2. FT REPEAT 132 161 ANK 3. FT REPEAT 165 194 ANK 4. FT REPEAT 198 227 ANK 5. FT COILED 431 480 Potential. FT COILED 565 724 Potential. FT COILED 776 805 Potential. SQ SEQUENCE 823 AA; 94087 MW; 6C1C478C3EE9B67F CRC64; MKLFGFGSRR GQTAQGSIDH VYTGSGYRIR DSELQKIHRA AVKGDAAEVE RCLARRSGDL DALDKQHRTA LHLACASGHV QVVTLLVNRK CQIDVCDKEN RTPLIQAVHC QEEACAVILL EHGANPNLKD IYGNTALHYA VYSESTSLAE KLLSHGAHIE ALDKDNNTPL LFAIICKKEK MVEFLLKRKA SSHAVDRLRR SALMLAVYYD SPGIVNILLK QNIDVFAQDM CGRDAEDYAI SHHLTKIQQQ ILEHKKKILK KEKSDVGSSD ESAVSIFHEL RVDSLPASDD KDLNVATKQC VPEKVSEPLP GSSHEKGNRI VNGQGEGPPA KHPSLKPSTE VEDPAVKGAV QRKNVQTLRA EQALPVASEE EQERHERSEK KQPQVKEGNN TNKSEKIQLS ENICDSTSSA AAGRLTQQRK IGKTYPQQFP KKLKEEHDRC TLKQENEEKT NVNMLYKKNR EELERKEKQY KKEVEAKQLE PTVQSLEMKS KTARNTPNRD FHNHEEMKGL MDENCILKAD IAILRQEICT MKNDNLEKEN KYLKDIKIVK ETNAALEKYI KLNEEMITET AFRYQQELND LKAENTRLNA ELLKEKESKK RLEADIESYQ SRLAAAISKH SESVKTERNL KLALERTRDV SVQVEMSSAI SKVKDENEFL TEQLSETQIK FNALKDKFRK TRDSLRKKSL ALETVQNDLS QTQQQTQEMK EMYQNAEAKV NNSTGKWNCV EERICHLQRE NAWLVQQLDD VHQKEDHKEI VTNIQRGFIE SGKKDLVLEE KSKKLMNECD HLKESLFQYE REKTEGVVSI KEDKYFQTSR KKI // ID A23D_DROME Reviewed; 398 AA. AC Q24093; Q9VQM6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-JAN-2003, sequence version 2. DT 23-JAN-2007, entry version 42. DE UPF0017 protein CG3488. GN Name=anon-23Da; Synonyms=anon-23D; ORFNames=CG3488; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE. RA Chartoff E.H., Gelbart W.M.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- INTERACTION: CC O01367-1:how; NbExp=1; IntAct=EBI-108903, EBI-200992; CC -!- SIMILARITY: Belongs to the UPF0017 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U29170; AAA99735.1; -; mRNA. DR EMBL; AE014134; AAF51139.1; -; Genomic_DNA. DR EMBL; BT010082; AAQ22551.1; -; mRNA. DR UniGene; Dm.3835; -. DR DIP; DIP:17906N; -. DR IntAct; Q24093; -. DR Ensembl; CG3488; Drosophila melanogaster. DR KEGG; dme:Dmel_CG3488; -. DR FlyBase; FBgn0014906; CG3488. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-007150-MONOMER; -. DR GermOnline; CG3488; Drosophila melanogaster. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR012020; AB-Hydro_YheT. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR000952; UPF0017_hydro-like. DR Pfam; PF00561; Abhydrolase_1; 1. DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1. DR PROSITE; PS01133; UPF0017; 1. KW Complete proteome. FT CHAIN 1 398 UPF0017 protein CG3488. FT /FTId=PRO_0000212459. FT CONFLICT 211 211 D -> N (in Ref. 1). FT CONFLICT 223 223 Y -> I (in Ref. 1). SQ SEQUENCE 398 AA; 45402 MW; 89A2F30F8DE3ECDD CRC64; MSTAFLTLIA VIVCILFRIL NVHSQPLKPS VWCLDAHFLD CLYKIAPVLR EPYIPPRLWG FSGHVQTVLH SIVGRVRCPW PLGERVYMSL KDGSTLTYDL YQPLNEQEDD ITVAICPGIA NSSESVYIRT FVHLAQCNGY RCAVLNHIGA LRSVQVTSTR IFTYGHTEDF AAMVEHLHQK YRQSRIVAVG FSLGGNLVTK YMGEDQKTKP DKVIGGISIC QGYNAVEGTK WLLNWQNFRR FYLYIMTENV KSIILRHRHI LLSDEVKARH NLNEREIIAA ATLPELDEAY TRRVYNFPST QELYKWSSSL FYFDTIKKPM IFINAKDDPL IPEDLLHPIK EYATTRQNTA YVEVAHGGHL GFYEGGFLYP NPVTWLDRTL VAMVGSLVMM HEVGKVAP // ID A29AB_DROME Reviewed; 234 AA. AC O46197; Q6VBE9; Q6VBF0; Q6VBF1; Q6VBF2; Q6VBF4; Q6VBF5; Q6VBF6; AC Q6VBF7; Q9TVT3; Q9TW05; Q9TW06; Q9TW07; Q9U976; Q9U977; Q9U978; AC Q9U979; Q9V3Q5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 23-JAN-2007, entry version 58. DE Accessory gland protein Acp29AB precursor. GN Name=Acp29AB; ORFNames=CG17797; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; DOI=10.1016/S0965-1748(97)00056-8; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=La1, La13, La14, La15, La16, La21, La25, La3, La34, La35, La4, RC La5, La6, La9, Ma13, Ma18, Ma20, Ma21, Ma43, Ma45, Ma48, Ma5, Ma50, RC Ma52, Ma67, Ma7, Ma8, Mo15b, Mo1b, Mo2b, Mo34a, Mo36a, Mo37a, Mo40b, RC Mo47a, Mo52b, Mo58b, Mo80b, and Mo8b; RX MEDLINE=99282496; PubMed=10353898; RA Aguade M.; RT "Positive selection drives the evolution of the Acp29AB accessory RT gland protein in Drosophila."; RL Genetics 152:543-551(1999). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WS1, WS12, WS16, WS19, WS26, WS47, WS56, WS6, WS9, Zim2, Zim26, RC Zim29, Zim30, Zim32, Zim37, Zim42, and Zim56; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NFS 5.1, NFS 5.2, NFS 5.3, NFS 5.4, NFS 6.1, NFS 6.2, NFS 6.3, RC NFS 6.4, NFS 7.8, SFS 1.1, SFS 1.2, SFS 1.3, SFS 1.4, SFS 2.2, RC SFS 2.3, SFS 2.4, SFS 3.1, SFS 3.2, SFS 3.3, and SFS 3.4; RX PubMed=14761057; RA Panhuis T.M., Swanson W.J., Nunney L.; RT "Population genetics of accessory gland proteins and sexual behavior RT in Drosophila melanogaster populations from Evolution Canyon."; RL Evolution 57:2785-2791(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [6] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: Responsible for physiological and behavioral changes in CC mated female flies. CC -!- INTERACTION: CC Q9V4B8:CG10323; NbExp=1; IntAct=EBI-153710, EBI-145217; CC Q9VSE9:ERR; NbExp=1; IntAct=EBI-153710, EBI-166804; CC P48592:RnrS; NbExp=1; IntAct=EBI-153710, EBI-93696; CC -!- SUBCELLULAR LOCATION: Secreted protein (Probable). CC -!- TISSUE SPECIFICITY: Main cells of the accessory gland and in CC seminal fluid. CC -!- SIMILARITY: Contains 1 C-type lectin 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; U85758; AAB96382.1; -; mRNA. DR EMBL; AJ240513; CAB53187.1; -; Genomic_DNA. DR EMBL; AJ240514; CAB53188.1; -; Genomic_DNA. DR EMBL; AJ240515; CAB53189.1; -; Genomic_DNA. DR EMBL; AJ240516; CAB53190.1; -; Genomic_DNA. DR EMBL; AJ240517; CAB53191.1; -; Genomic_DNA. DR EMBL; AJ240518; CAB53192.1; -; Genomic_DNA. DR EMBL; AJ240519; CAB53193.1; -; Genomic_DNA. DR EMBL; AJ240520; CAB53194.1; -; Genomic_DNA. DR EMBL; AJ240521; CAB53195.1; -; Genomic_DNA. DR EMBL; AJ240522; CAB53196.1; -; Genomic_DNA. DR EMBL; AJ240523; CAB53197.1; -; Genomic_DNA. DR EMBL; AJ240524; CAB53198.1; -; Genomic_DNA. DR EMBL; AJ240525; CAB53199.1; -; Genomic_DNA. DR EMBL; AJ240526; CAB53200.1; -; Genomic_DNA. DR EMBL; AJ240527; CAB53201.1; -; Genomic_DNA. DR EMBL; AJ240528; CAB53202.1; -; Genomic_DNA. DR EMBL; AJ240529; CAB53203.1; -; Genomic_DNA. DR EMBL; AJ240530; CAB53204.1; -; Genomic_DNA. DR EMBL; AJ240531; CAB53205.1; -; Genomic_DNA. DR EMBL; AJ240532; CAB53206.1; -; Genomic_DNA. DR EMBL; AJ240533; CAB53207.1; -; Genomic_DNA. DR EMBL; AJ240534; CAB53208.1; -; Genomic_DNA. DR EMBL; AJ240535; CAB53209.1; -; Genomic_DNA. DR EMBL; AJ240536; CAB53210.1; -; Genomic_DNA. DR EMBL; AJ240537; CAB53211.1; -; Genomic_DNA. DR EMBL; AJ240538; CAB53212.1; -; Genomic_DNA. DR EMBL; AJ240539; CAB53213.1; -; Genomic_DNA. DR EMBL; AJ240540; CAB53214.1; -; Genomic_DNA. DR EMBL; AJ240541; CAB53215.1; -; Genomic_DNA. DR EMBL; AJ240542; CAB53216.1; -; Genomic_DNA. DR EMBL; AJ240543; CAB53217.1; -; Genomic_DNA. DR EMBL; AJ240544; CAB53218.1; -; Genomic_DNA. DR EMBL; AJ240545; CAB53219.1; -; Genomic_DNA. DR EMBL; AJ240546; CAB53220.1; -; Genomic_DNA. DR EMBL; AJ240547; CAB53221.1; -; Genomic_DNA. DR EMBL; AJ240548; CAB53222.1; -; Genomic_DNA. DR EMBL; AJ240549; CAB53223.1; -; Genomic_DNA. DR EMBL; AJ240550; CAB53224.1; -; Genomic_DNA. DR EMBL; AJ240551; CAB53225.1; -; Genomic_DNA. DR EMBL; AY010527; AAG32559.1; -; Genomic_DNA. DR EMBL; AY010528; AAG32560.1; -; Genomic_DNA. DR EMBL; AY010529; AAG32561.1; -; Genomic_DNA. DR EMBL; AY010530; AAG32562.1; -; Genomic_DNA. DR EMBL; AY010531; AAG32563.1; -; Genomic_DNA. DR EMBL; AY010532; AAG32564.1; -; Genomic_DNA. DR EMBL; AY010533; AAG32565.1; -; Genomic_DNA. DR EMBL; AY010534; AAG32566.1; -; Genomic_DNA. DR EMBL; AY010535; AAG32567.1; -; Genomic_DNA. DR EMBL; AY010536; AAG32568.1; -; Genomic_DNA. DR EMBL; AY010537; AAG32569.1; -; Genomic_DNA. DR EMBL; AY010538; AAG32570.1; -; Genomic_DNA. DR EMBL; AY010539; AAG32571.1; -; Genomic_DNA. DR EMBL; AY010540; AAG32572.1; -; Genomic_DNA. DR EMBL; AY010541; AAG32573.1; -; Genomic_DNA. DR EMBL; AY010542; AAG32574.1; -; Genomic_DNA. DR EMBL; AY010543; AAG32575.1; -; Genomic_DNA. DR EMBL; AY344305; AAR05024.1; -; Genomic_DNA. DR EMBL; AY344306; AAR05025.1; -; Genomic_DNA. DR EMBL; AY344307; AAR05026.1; -; Genomic_DNA. DR EMBL; AY344308; AAR05027.1; -; Genomic_DNA. DR EMBL; AY344309; AAR05028.1; -; Genomic_DNA. DR EMBL; AY344310; AAR05029.1; -; Genomic_DNA. DR EMBL; AY344311; AAR05030.1; -; Genomic_DNA. DR EMBL; AY344312; AAR05031.1; -; Genomic_DNA. DR EMBL; AY344313; AAR05032.1; -; Genomic_DNA. DR EMBL; AY344314; AAR05033.1; -; Genomic_DNA. DR EMBL; AY344315; AAR05034.1; -; Genomic_DNA. DR EMBL; AY344316; AAR05035.1; -; Genomic_DNA. DR EMBL; AY344317; AAR05036.1; -; Genomic_DNA. DR EMBL; AY344318; AAR05037.1; -; Genomic_DNA. DR EMBL; AY344319; AAR05038.1; -; Genomic_DNA. DR EMBL; AY344320; AAR05039.1; -; Genomic_DNA. DR EMBL; AY344321; AAR05040.1; -; Genomic_DNA. DR EMBL; AY344322; AAR05041.1; -; Genomic_DNA. DR EMBL; AY344323; AAR05042.1; -; Genomic_DNA. DR EMBL; AY344324; AAR05043.1; -; Genomic_DNA. DR EMBL; AE014134; AAF52665.1; -; Genomic_DNA. DR UniGene; Dm.2600; -. DR IntAct; O46197; -. DR Ensembl; CG17797; Drosophila melanogaster. DR KEGG; dme:Dmel_CG17797; -. DR FlyBase; FBgn0015583; Acp29AB. DR GermOnline; CG17797; Drosophila melanogaster. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007321; P:sperm displacement; NAS:FlyBase. DR InterPro; IPR001304; Lectin_C. DR Pfam; PF00059; Lectin_C; 1. DR SMART; SM00034; CLECT; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; FALSE_NEG. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. KW Behavior; Complete proteome; Glycoprotein; Lectin; Polymorphism; KW Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 234 Accessory gland protein Acp29AB. FT /FTId=PRO_0000017556. FT DOMAIN 137 234 C-type lectin. FT CARBOHYD 61 61 N-linked (GlcNAc...) (Potential). FT CARBOHYD 164 164 N-linked (GlcNAc...) (Potential). FT DISULFID 139 228 By similarity. FT DISULFID 207 220 By similarity. FT VARIANT 27 27 N -> S (in strain: SFS 1.2). FT VARIANT 29 29 K -> N (in strain: Ma7, WS16 and WS26). FT VARIANT 59 59 K -> R (in strain: La1, La3, La4, La5, FT La14, La15, La16, La21, La25, La34, La35, FT Ma5, Ma8, Ma13, Ma18, Ma20, Ma21, Ma45, FT Ma48, Ma52, Ma67, Mo1b, Mo52b, Mo80b, NFS FT 6.1, SFS 1.2, WS6, WS19, Zim26, Zim29, FT Zim30 and Zim56). FT VARIANT 104 104 K -> E (in strain: SFS 1.2). FT VARIANT 105 105 A -> S (in strain: La16 and La35). FT VARIANT 108 108 N -> D (in strain: SFS 2.3). FT VARIANT 113 113 R -> L (in strain: La14, La14, La16, FT La35, Ma5, Ma7, Ma13, Ma18, Ma20, Ma21, FT Ma45, Ma48, Ma50, Ma52, Ma67, Mo2b, FT Mo15b, Mo34a, Mo36a, Mo37a, Mo47a, Mo52b, FT Mo58b, Mo80b, NFS 5.1, NFS 5.2, NFS 5.4, FT NFS 6.2, NFS 6.3, NFS 6.4, SFS 1.1, SFS FT 1.3, SFS 1.4, SFS 2.2, SFS 3.1, SFS 3.3, FT WS1, WS6, WS9, WS12, WS16, WS26, WS47, FT WS56, Zim2, Zim26, Zim29, Zim30, Zim32, FT Zim37, Zim42 and Zim56). FT VARIANT 153 153 K -> M (in strain: Berkeley, La13, La14, FT La15, La16, Ma5, Ma21, Ma45, Ma52, Ma67, FT Mo1b, Mo8b, Mo40b, Mo52b, NFS 5.3, NFS FT 6.1, NFS 7.8, SFS 1.1, SFS 1.2, SFS 1.4, FT SFS 2.3, SFS 2.4, SFS 3.2, SFS 3.4, FT Zim29, Zim30, Zim42 and Zim56). FT VARIANT 171 171 I -> V (in strain: NFS 5.2). FT VARIANT 214 214 E -> D (in strain: Ma7). SQ SEQUENCE 234 AA; 27173 MW; 8954CD3215480F3E CRC64; MYASNLLYLL ALWNLWDLSG GQQDIPNGKA TLPSPQTPQN TIDQIGINQN YWFTYNALKQ NETLAIIDTM EMRIASSLLE FKAQMEIQLQ PLKIIMRHHA SNIKASNNIK MRRFEKVGSR HFHIEKNLMQ TWFEAYVTCR KMNGHLANIQ DEKELDGILA LAPNNSYWID ISKLVENGGT FVSTLTGREP FFVKWKSNQD TKKKNQCVYI YAKEMSYDEC FEKKSFVCQA DQWA // ID A29AB_DROSI Reviewed; 234 AA. AC Q9U968; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 31-OCT-2006, entry version 37. DE Accessory gland protein Acp29AB precursor. GN Name=Acp29AB; OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7240; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S9; RX MEDLINE=99282496; PubMed=10353898; RA Aguade M.; RT "Positive selection drives the evolution of the Acp29AB accessory RT gland protein in Drosophila."; RL Genetics 152:543-551(1999). CC -!- FUNCTION: Responsible for physiological and behavioral changes in CC mated female flies. CC -!- SUBCELLULAR LOCATION: Secreted protein (Probable). CC -!- SIMILARITY: Contains 1 C-type lectin 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; AJ240552; CAB53227.1; -; Genomic_DNA. DR HSSP; P16581; 1G1T. DR FlyBase; FBgn0027418; Dsim\Acp29AB. DR InterPro; IPR001304; Lectin_C. DR Pfam; PF00059; Lectin_C; 1. DR SMART; SM00034; CLECT; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; FALSE_NEG. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. KW Behavior; Glycoprotein; Lectin; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 234 Accessory gland protein Acp29AB. FT /FTId=PRO_0000017557. FT DOMAIN 137 234 C-type lectin. FT CARBOHYD 29 29 N-linked (GlcNAc...) (Potential). FT CARBOHYD 61 61 N-linked (GlcNAc...) (Potential). FT CARBOHYD 127 127 N-linked (GlcNAc...) (Potential). FT CARBOHYD 164 164 N-linked (GlcNAc...) (Potential). FT DISULFID 139 228 By similarity. FT DISULFID 207 220 By similarity. SQ SEQUENCE 234 AA; 26915 MW; EE9C556E02EFED98 CRC64; MYATNLLYLL ALWNLWLVSG GQQDIPNGNA TLPSPQKPQN TIDQIGANQN YWFTYNALRQ NETLAIIDAM ESGIASSVLA FQAQMEIQLQ PLKIIMLHHA GNIKASNNIK MSRFEKVGSR YFHIEKNLTL TWFEAYVTCR EMNGHLANIR DEKELDGILA LAPNNSYWVD ISKLVEYGGT FVSTLTGREP IFVKWKPNQD KKKQHNCVYI YAKEMYYDEC FEKKSFVCQA NQWA // ID A2AP_BOVIN Reviewed; 492 AA. AC P28800; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 31-OCT-2006, entry version 55. DE Alpha-2-antiplasmin precursor (Alpha-2-plasmin inhibitor) (Alpha-2-PI) DE (Alpha-2-AP). GN Name=SERPINF2; Synonyms=PLI; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], DISULFIDE BOND, AND GLYCOSYLATION AT RP ASN-127; ASN-249; ASN-296; ASN-310 AND ASN-317. RX MEDLINE=94229242; PubMed=7513654; DOI=10.1016/0014-5793(94)80560-1; RA Christensen S., Berglund L., Sottrup-Jensen L.; RT "Primary structure of bovine alpha 2-antiplasmin."; RL FEBS Lett. 343:223-228(1994). RN [2] RP PROTEIN SEQUENCE OF 23-45 AND 374-410. RC TISSUE=Plasma; RX MEDLINE=93050153; PubMed=1385210; DOI=10.1016/0014-5793(92)81419-M; RA Christensen S., Sottrup-Jensen L.; RT "Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence."; RL FEBS Lett. 312:100-104(1992). CC -!- FUNCTION: The major targets of this inhibitor are plasmin and CC trypsin, but it also inactivates chymotrypsin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X78436; CAA55200.1; -; mRNA. DR PIR; S43977; S43977. DR UniGene; Bt.9352; -. DR HSSP; P01008; 1ANT. DR MEROPS; I04.023; -. DR KEGG; bta:282522; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 2. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor; Signal; Sulfation. FT SIGNAL 1 22 FT CHAIN 23 492 Alpha-2-antiplasmin. FT /FTId=PRO_0000032510. FT SITE 404 405 Reactive bond for plasmin. FT SITE 405 406 Reactive bond for chymotrypsin. FT MOD_RES 485 485 Sulfotyrosine (By similarity). FT CARBOHYD 127 127 N-linked (GlcNAc...). FT CARBOHYD 249 249 N-linked (GlcNAc...). FT CARBOHYD 296 296 N-linked (GlcNAc...). FT CARBOHYD 310 310 N-linked (GlcNAc...). FT CARBOHYD 317 317 N-linked (GlcNAc...). FT DISULFID 71 144 FT CONFLICT 28 28 T -> Q (in Ref. 2). FT CONFLICT 40 40 Q -> P (in Ref. 2). FT CONFLICT 43 43 Q -> E (in Ref. 2). SQ SEQUENCE 492 AA; 54711 MW; 0755D6FC89B2DF5D CRC64; MALLWGLLAL ILSCLSSLCS AQFSPVSTME PLDLQLMDGQ AQQKLPPLSL LKLDNQEPGG QIAPKKAPED CKLSPTPEQT RRLARAMMTF TTDLFSLVAQ SSTRPNLILS PLSVALALSH LALGAQNQTL QRLKEVLHAD SGPCLPHLLS RLCQDLGPGA FRLAARMYLQ KGFPIKEDFL EQSEQLFGAK PMSLTGMKGE DLANINRWVK EATEGKIEDF LSDLPDDTVL LLLNAIHFQG FWRSKFDPNL TQRGAFHLDE QFTVPVDMMQ ALTYPLHWFL LEQPEIQVAH FPFKNNMSFV VLMPTRFEWN ASQVLANLTW DILHQPSLSE RPTKVQLPKL HLKYQLDLVA TLSQLGLQEL FQAPDLRGIS DERLVVSSVQ HQSALELSEA GVQAAAATST AMSRMSLSSF IVNRPFLFFI LEDSTSLPLF VGSVRNPNPG AQPERKEQQD SPDGKDSFQD HKGLPRGDKP FDPDLKLGPP SEEDYAQPSS PK // ID A2AP_HUMAN Reviewed; 491 AA. AC P08697; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 3. DT 20-FEB-2007, entry version 87. DE Alpha-2-antiplasmin precursor (Alpha-2-plasmin inhibitor) (Alpha-2-PI) DE (Alpha-2-AP). GN Name=SERPINF2; Synonyms=AAP, PLI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=88139254; PubMed=2830248; RA Tone M., Kikuno R., Kume-Iwaki A., Hashimoto-Gotoh T.; RT "Structure of human alpha 2-plasmin inhibitor deduced from the cDNA RT sequence."; RL J. Biochem. 102:1033-1041(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88320531; PubMed=3166140; RA Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.; RT "Organization of the human alpha 2-plasmin inhibitor gene."; RL Proc. Natl. Acad. Sci. U.S.A. 85:6836-6840(1988). RN [3] RP ERRATUM. RA Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.; RL Proc. Natl. Acad. Sci. U.S.A. 86:1612-1613(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-491. RX MEDLINE=87109313; PubMed=2433286; RA Holmes W.E., Nelles L., Lijnen H.R., Collen D.; RT "Primary structure of human alpha 2-antiplasmin, a serine protease RT inhibitor (serpin)."; RL J. Biol. Chem. 262:1659-1664(1987). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 218-491. RX MEDLINE=87137400; PubMed=3818581; RA Sumi Y., Nakamura Y., Aoki N., Sakai M., Muramatsu M.; RT "Structure of the carboxyl-terminal half of human alpha 2-plasmin RT inhibitor deduced from that of cDNA."; RL J. Biochem. 100:1399-1402(1986). RN [6] RP PROTEIN SEQUENCE OF 40-491. RX MEDLINE=87275946; PubMed=2440681; RA Lijnen H.R., Holmes W.E., van Hoef B., Wiman B., Rodriguez H., RA Collen D.; RT "Amino-acid sequence of human alpha 2-antiplasmin."; RL Eur. J. Biochem. 166:565-574(1987). RN [7] RP PROTEIN SEQUENCE OF 40-43. RX MEDLINE=78023887; PubMed=21075; RA Wiman B., Collen D.; RT "Purification and characterization of human antiplasmin, the fast- RT acting plasmin inhibitor in plasma."; RL Eur. J. Biochem. 78:19-26(1977). RN [8] RP PROTEIN SEQUENCE OF 28-52. RC TISSUE=Plasma; RX MEDLINE=93050153; PubMed=1385210; DOI=10.1016/0014-5793(92)81419-M; RA Christensen S., Sottrup-Jensen L.; RT "Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence."; RL FEBS Lett. 312:100-104(1992). RN [9] RP ACTIVE SITES. RX MEDLINE=88290696; PubMed=2456616; RA Potempa J., Shieh B.-H., Travis J.; RT "Alpha-2-antiplasmin: a serpin with two separate but overlapping RT reactive sites."; RL Science 241:699-700(1988). RN [10] RP DISULFIDE BOND. RX MEDLINE=97270633; PubMed=9169621; RA Christensen S., Valnickova Z., Thogersen I.B., Olsen E.H., RA Enghild J.J.; RT "Assignment of a single disulphide bridge in human alpha2-antiplasmin: RT implications for the structural and functional properties."; RL Biochem. J. 323:847-852(1997). RN [11] RP PROTEIN SEQUENCE OF 481-491, AND SULFATION. RX MEDLINE=87137577; PubMed=2434496; RA Hortin G., Fok K.F., Toren P.C., Strauss A.W.; RT "Sulfation of a tyrosine residue in the plasmin-binding domain of RT alpha 2-antiplasmin."; RL J. Biol. Chem. 262:3082-3085(1987). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-295 AND ASN-309, RP AND MASS SPECTROMETRY. RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [13] RP VARIANT ALPHA-2-PLASMIN INHIBITOR DEFICIENCY GLU-176 DEL. RX MEDLINE=90036902; PubMed=2572590; RA Miura O., Sugahara Y., Aoki N.; RT "Hereditary alpha 2-plasmin inhibitor deficiency caused by a RT transport-deficient mutation (alpha 2-PI-Okinawa). Deletion of Glu137 RT by a trinucleotide deletion blocks intracellular transport."; RL J. Biol. Chem. 264:18213-18219(1989). RN [14] RP VARIANT ALPHA-2-PLASMIN INHIBITOR DEFICIENCY MET-411, AND VARIANTS RP VAL-27; TRP-33 AND LYS-434. RX MEDLINE=20051147; PubMed=10583218; RX DOI=10.1046/j.1365-2141.1999.01708.x; RA Lind B., Thorsen S.; RT "A novel missense mutation in the human plasmin inhibitor (alpha2- RT antiplasmin) gene associated with a bleeding tendency."; RL Br. J. Haematol. 107:317-322(1999). CC -!- FUNCTION: The major targets of this inhibitor are plasmin and CC trypsin, but it also inactivates chymotrypsin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- DISEASE: Defects in SERPINF2 are the cause of alpha-2-plasmin CC inhibitor deficiency [MIM:262850]; a disease resulting in severe CC hemorrhagic diathesis. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D00116; BAA00070.1; -; mRNA. DR EMBL; D00174; BAA00124.1; -; mRNA. DR EMBL; M20786; AAA51554.1; -; Genomic_DNA. DR EMBL; M20782; AAA51554.1; JOINED; Genomic_DNA. DR EMBL; M20783; AAA51554.1; JOINED; Genomic_DNA. DR EMBL; M20784; AAA51554.1; JOINED; Genomic_DNA. DR EMBL; M20785; AAA51554.1; JOINED; Genomic_DNA. DR EMBL; J02654; AAA35543.1; -; mRNA. DR PIR; A31402; ITHUA2. DR UniGene; Hs.159509; -. DR HSSP; P01008; 1ANT. DR MEROPS; I04.023; -. DR SWISS-2DPAGE; P08697; HUMAN. DR Ensembl; ENSG00000167711; Homo sapiens. DR KEGG; hsa:5345; -. DR H-InvDB; HIX0013407; -. DR HGNC; HGNC:9075; SERPINF2. DR HPA; HPA001885; -. DR MIM; 262850; gene+phenotype. DR Reactome; REACT_604.1; Hemostasis. DR ArrayExpress; P08697; -. DR RZPD-ProtExp; F0116; -. DR RZPD-ProtExp; IOH22703; -. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB. DR InterPro; IPR000215; Prot_inh_serpin. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Direct protein sequencing; Disease mutation; KW Glycoprotein; Polymorphism; Protease inhibitor; KW Serine protease inhibitor; Signal; Sulfation. FT SIGNAL 1 27 FT PROPEP 28 39 FT /FTId=PRO_0000032511. FT CHAIN 40 491 Alpha-2-antiplasmin. FT /FTId=PRO_0000032512. FT SITE 403 404 Reactive bond for plasmin. FT SITE 404 405 Reactive bond for chymotrypsin. FT MOD_RES 484 484 Sulfotyrosine. FT CARBOHYD 126 126 N-linked (GlcNAc...). FT CARBOHYD 295 295 N-linked (GlcNAc...). FT CARBOHYD 309 309 N-linked (GlcNAc...). FT CARBOHYD 316 316 N-linked (GlcNAc...) (Potential). FT DISULFID 70 143 FT CROSSLNK 41 41 Isoglutamyl lysine isopeptide (Gln-Lys) FT (interchain with K-322 in alpha- FT fibrinogen). FT VARIANT 27 27 A -> V. FT /FTId=VAR_013252. FT VARIANT 33 33 R -> W. FT /FTId=VAR_013253. FT VARIANT 176 176 Missing (in alpha-2-plasmin inhibitor FT deficiency; variant Okinawa; probably FT blocks intracellular transport of alpha- FT 2-plasmin inhibitor). FT /FTId=VAR_013254. FT VARIANT 411 411 V -> M (in alpha-2-plasmin inhibitor FT deficiency). FT /FTId=VAR_013255. FT VARIANT 434 434 R -> K. FT /FTId=VAR_013256. FT CONFLICT 49 49 L -> G (in Ref. 6). FT CONFLICT 105 105 N -> D (in Ref. 6). FT CONFLICT 289 289 H -> D (in Ref. 4). FT CONFLICT 408 408 S -> G (in Ref. 6). FT CONFLICT 455 455 D -> N (in Ref. 6). SQ SEQUENCE 491 AA; 54566 MW; 385A1C90E91A63CB CRC64; MALLWGLLVL SWSCLQGPCS VFSPVSAMEP LGRQLTSGPN QEQVSPLTLL KLGNQEPGGQ TALKSPPGVC SRDPTPEQTH RLARAMMAFT ADLFSLVAQT STCPNLILSP LSVALALSHL ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR LCQDLGPGAF RLAARMYLQK GFPIKEDFLE QSEQLFGAKP VSLTGKQEDD LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF WRNKFDPSLT QRDSFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT LSQLGLQELF QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA MSRMSLSSFS VNRPFLFFIF EDTTGLPLFV GSVRNPNPSA PRELKEQQDS PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM EEDYPQFGSP K // ID A2AP_MOUSE Reviewed; 491 AA. AC Q61247; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 23-JAN-2007, entry version 61. DE Alpha-2-antiplasmin precursor (Alpha-2-plasmin inhibitor) (Alpha-2-PI) DE (Alpha-2-AP). GN Name=Serpinf2; Synonyms=Pli; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX MEDLINE=96249418; PubMed=8647939; RA Menoud P.A., Sappino N., Boudal-Khoshbeen M., Vassalli J.-D., RA Sappino A.P.; RT "The kidney is a major site of alpha(2)-antiplasmin production."; RL J. Clin. Invest. 97:2478-2484(1996). 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 28-33. RX MEDLINE=95010076; PubMed=7523120; RA Lijnen H.R., van Hoef B., Beelen V., Collen D.; RT "Characterization of the murine plasma fibrinolytic system."; RL Eur. J. Biochem. 224:863-871(1994). CC -!- FUNCTION: The major targets of this inhibitor are plasmin and CC trypsin, but it also inactivates chymotrypsin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z36774; CAA85350.1; -; mRNA. DR EMBL; BC026756; AAH26756.1; -; mRNA. DR PIR; S47217; S47217. DR UniGene; Mm.279733; -. DR HSSP; P01008; 1ANT. DR MEROPS; I04.023; -. DR Ensembl; ENSMUSG00000038224; Mus musculus. DR KEGG; mmu:18816; -. DR MGI; MGI:107173; Serpinf2. DR ArrayExpress; Q61247; -. DR GermOnline; ENSMUSG00000038224; Mus musculus. DR RZPD-ProtExp; IOM20923; -. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Acute phase; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor; Signal; Sulfation. FT SIGNAL 1 27 FT CHAIN 28 491 Alpha-2-antiplasmin. FT /FTId=PRO_0000032513. FT SITE 403 404 Reactive bond for plasmin. FT SITE 404 405 Reactive bond for chymotrypsin (By FT similarity). FT MOD_RES 484 484 Sulfotyrosine (By similarity). FT CARBOHYD 126 126 N-linked (GlcNAc...) (Potential). FT CARBOHYD 295 295 N-linked (GlcNAc...) (Potential). FT CARBOHYD 309 309 N-linked (GlcNAc...) (Potential). FT CARBOHYD 316 316 N-linked (GlcNAc...) (Potential). FT DISULFID 70 143 By similarity. SQ SEQUENCE 491 AA; 54972 MW; B828DECADF0BB5B4 CRC64; MALLRGLLVL SLSCLQGPCF TFSPVSAVDL PGQQPVSEQA QQKLPLPALF KLDNQDFGDH ATLKRSPGHC KSVPTAEETR RLAQAMMAFT TDLFSLVAQT STSSNLVLSP LSVALALSHL ALGAQNQTLH SLHRVLHMNT GSCLPHLLSH FYQNLGPGTI RLAARIYLQK GFPIKDDFLE QSERLFGAKP VKLTGKQEED LANINQWVKE ATEGKIEDFL SELPDSTVLL LLNAIHFHGF WRTKFDPSLT QKDFFHLDER FTVSVDMMHA VSYPLRWFLL EQPEIQVAHF PFKNNMSFVV VMPTYFEWNV SEVLANLTWD TLYHPSLQER PTKVWLPKLH LQQQLDLVAT LSQLGLQELF QGPDLRGISE QNLVVSSVQH QSTMELSEAG VEAAAATSVA MNRMSLSSFT VNRPFLFFIM EDTIGVPLFV GSVRNPNPSA LPQLQEQRDS PDNRLIGQND KADFHGGKTF GPDLKLAPRM EEDYPQFSSP K // ID A2AP_STRCA Reviewed; 11 AA. AC P83168; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 31-OCT-2006, entry version 22. DE Alpha-2-antiplasmin (Alpha-2-plasmin inhibitor) (Alpha-2-PI) (Alpha-2- DE AP) (Fragment). GN Name=SERPINF2; OS Struthio camelus (Ostrich). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae; OC Struthio. OX NCBI_TaxID=8801; RN [1] RP PROTEIN SEQUENCE, AND FUNCTION. RC TISSUE=Plasma; RX MEDLINE=21328857; PubMed=11435135; DOI=10.1016/S1096-4959(01)00396-7; RA Thomas A.R., Naude R.J., Oelofsen W., Naganuma T., Muramoto K.; RT "Purification and partial characterisation of alpha(2)-antiplasmin and RT plasmin(ogen) from ostrich plasma."; RL Comp. Biochem. Physiol. 129B:809-820(2001). CC -!- FUNCTION: The major targets of this inhibitor are plasmin and CC trypsin, but it also inactivates chymotrypsin. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:UniProtKB. DR GO; GO:0030162; P:regulation of proteolysis; NAS:UniProtKB. DR InterPro; IPR000215; Prot_inh_serpin. DR PROSITE; PS00284; SERPIN; PARTIAL. KW Direct protein sequencing; Protease inhibitor; KW Serine protease inhibitor. FT CHAIN 1 >11 Alpha-2-antiplasmin. FT /FTId=PRO_0000094125. FT NON_TER 11 11 SQ SEQUENCE 11 AA; 1261 MW; 9B08C06B32C73B5A CRC64; LQVDYLVLEV A // ID A2BP1_HUMAN Reviewed; 397 AA. AC Q9NWB1; Q9NS20; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-FEB-2007, entry version 52. DE Ataxin-2-binding protein 1. GN Name=A2BP1; Synonyms=A2BP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-397. RX MEDLINE=20275619; PubMed=10814712; DOI=10.1093/hmg/9.9.1303; RA Shibata H., Huynh D.P., Pulst S.-M.; RT "A novel protein with RNA-binding motifs interacts with ataxin-2."; RL Hum. Mol. Genet. 9:1303-1313(2000). CC -!- SUBUNIT: Binds to the C-terminal of ataxin-2. CC -!- INTERACTION: CC P54259:ATN1; NbExp=1; IntAct=EBI-945906, EBI-945980; CC P54253:ATXN1; NbExp=1; IntAct=EBI-945906, EBI-930964; CC Q9Y6R0:NUMBL; NbExp=1; IntAct=EBI-945906, EBI-945925; CC Q9HAU0:PLEKHA5; NbExp=1; IntAct=EBI-945906, EBI-945934; CC Q92530:PSMF1; NbExp=1; IntAct=EBI-945906, EBI-945916; CC Q96EJ3:QKI; NbExp=1; IntAct=EBI-945906, EBI-945792; CC O43251:RBM9; NbExp=1; IntAct=EBI-945906, EBI-746056; CC -!- TISSUE SPECIFICITY: Predominantly expressed in muscle and brain. 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; AK001027; BAA91472.1; -; mRNA. DR EMBL; AF107203; AAF78291.1; -; mRNA. DR UniGene; Hs.459842; -. DR PDB; 2ERR; NMR; A=109-196. DR IntAct; Q9NWB1; -. DR Ensembl; ENSG00000078328; Homo sapiens. DR KEGG; hsa:54715; -. DR H-InvDB; HIX0012802; -. DR MIM; 605104; gene. DR ArrayExpress; Q9NWB1; -. DR GermOnline; ENSG00000078328; Homo sapiens. DR RZPD-ProtExp; T4606; -. DR RZPD-ProtExp; U1121; -. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0003723; F:RNA binding; TAS:ProtInc. DR InterPro; IPR012677; a_b_plait_nuc_bd. DR InterPro; IPR000504; RNP1_RNA_bd. DR Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. KW 3D-structure; RNA-binding. FT CHAIN 1 397 Ataxin-2-binding protein 1. FT /FTId=PRO_0000081480. FT DOMAIN 117 193 RRM. FT CONFLICT 92 92 A -> T (in Ref. 2). FT TURN 113 114 FT STRAND 118 123 FT TURN 126 127 FT HELIX 130 136 FT HELIX 137 139 FT TURN 140 140 FT STRAND 146 148 FT TURN 152 153 FT TURN 156 157 FT STRAND 158 162 FT HELIX 167 176 FT TURN 177 178 FT TURN 182 183 FT STRAND 187 190 SQ SEQUENCE 397 AA; 42754 MW; E3E9060B68C79880 CRC64; MNCEREQLRG NQEAAAAPDT MAQPYASAQF APPQNGIPAE YTAPHPHPAP EYTGQTTVPE HTLNLYPPAQ THSEQSPADT SAQTVSGTAT QADDAAPTDG QPQTQPSENT ENKSQPKRLH VSNIPFRFRD PDLRQMFGQF GKILDVEIIF NERGSKGFGF VTFENSADAD RAREKLHGTV VEGRKIEVNN ATARVMTNKK TVNPYTNGWK LNPVVGAVYS PEFYAGTVLL CQANQEGSSM YSAPSSLVYT SAMPGFPYPA ATAAAAYRGA HLRGRGRTVY NTFRAAAPPP PIPAYGGVVY QDGFYGADIY GGYAAYRYAQ PTPATAAAYS DSYGRVYAAD PYHHALAPAP TYGVGAMNAF APLTDAKTRS HADDVGLVLS SLQASIYRGG YNRFAPY // ID A2BP1_MOUSE Reviewed; 396 AA. AC Q9JJ43; Q9JJB5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 20-FEB-2007, entry version 47. DE Ataxin-2-binding protein 1. GN Name=A2bp1; Synonyms=A2bp; ORFNames=MNCb-3035; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; 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 [MRNA] OF 21-396. RX MEDLINE=20275619; PubMed=10814712; DOI=10.1093/hmg/9.9.1303; RA Shibata H., Huynh D.P., Pulst S.-M.; RT "A novel protein with RNA-binding motifs interacts with ataxin-2."; RL Hum. Mol. Genet. 9:1303-1313(2000). CC -!- SUBUNIT: Binds to the C-terminal of ataxin-2. 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; AB041596; BAA95079.1; -; mRNA. DR EMBL; AF107204; AAF78292.1; -; mRNA. DR UniGene; Mm.370334; -. DR HSSP; P11940; 1CVJ. DR SMR; Q9JJ43; 108-195. DR Ensembl; ENSMUSG00000008658; Mus musculus. DR MGI; MGI:1926224; A2bp1. DR ArrayExpress; Q9JJ43; -. DR GermOnline; ENSMUSG00000008658; Mus musculus. DR InterPro; IPR012677; a_b_plait_nuc_bd. DR InterPro; IPR000504; RNP1_RNA_bd. DR Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. KW RNA-binding. FT CHAIN 1 396 Ataxin-2-binding protein 1. FT /FTId=PRO_0000081481. FT DOMAIN 116 192 RRM. FT CONFLICT 60 60 G -> D (in Ref. 2). FT CONFLICT 128 128 R -> RFR (in Ref. 2). FT CONFLICT 369 369 G -> S (in Ref. 2). SQ SEQUENCE 396 AA; 42590 MW; 9A0C59C5E687F39F CRC64; MNCEREQLRG NQEAAAAPDT MAQPYASAQF APPQNGIPAE YTAPHPHPAP EYTGQTTVPG HTLNLYPPTQ THSEQSADTS AQTVSGTATQ TDDAAPTDGQ PQTQPSENTE SKSQPKRLHV SNIPFRFRDP DLRQMFGQFG KILDVEIIFN ERGSKGFGFV TFENSADADR AREKLHGTVV EGRKIEVNNA TARVMTNKKT VNPYTNGWKL NPVVGAVYSP DFYAGTVLLC QANQEGSSMY SGPSSLVYTS AMPGFPYPAA TAAAAYRGAH LRGRGRTVYN TFRAAAPPPP IPAYGGVVYQ DGFYGADIYG GYAAYRYAQP TPATAAAYSD SYGRVYAADP YHHTLAPAPT YGVGAMNAFA PLTDAKTRGH ADDVGLVLSS LQASIYRGGY NRFAPY // ID A2GL_HUMAN Reviewed; 347 AA. AC P02750; Q8N4F5; Q96QZ4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2002, sequence version 2. DT 20-FEB-2007, entry version 68. DE Leucine-rich alpha-2-glycoprotein precursor (LRG). GN Name=LRG1; Synonyms=LRG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12223515; RA O'Donnell L.C., Druhan L.J., Avalos B.R.; RT "Molecular characterization and expression analysis of leucine-rich RT alpha2-glycoprotein, a novel marker of granulocytic differentiation."; RL J. Leukoc. Biol. 72:478-485(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-133. RC TISSUE=Colon, Kidney, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 36-347. RX MEDLINE=85166241; PubMed=3856868; RA Takahashi N., Takahashi Y., Putnam F.W.; RT "Periodicity of leucine and tandem repetition of a 24-amino acid RT segment in the primary structure of leucine-rich alpha 2-glycoprotein RT of human serum."; RL Proc. Natl. Acad. Sci. U.S.A. 82:1906-1910(1985). RN [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186, AND MASS RP SPECTROMETRY. RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186; ASN-269 AND ASN-325, RP AND MASS SPECTROMETRY. RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186, AND MASS RP SPECTROMETRY. RX PubMed=16740002; DOI=10.1021/pr050492k; RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., RA Loo J.A.; RT "Identification of N-linked glycoproteins in human saliva by RT glycoprotein capture and mass spectrometry."; RL J. Proteome Res. 5:1493-1503(2006). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- SIMILARITY: Contains 8 LRR (leucine-rich) 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; AF403428; AAK95527.1; -; mRNA. DR EMBL; BC034389; AAH34389.1; -; mRNA. DR EMBL; BC070198; AAH70198.1; -; mRNA. DR UniGene; Hs.131034; -. DR HSSP; P07359; 1P9A. DR SWISS-2DPAGE; P02750; HUMAN. DR DOSAC-COBS-2DPAGE; P02750; HUMAN. DR Siena-2DPAGE; P02750; -. DR Ensembl; ENSG00000171236; Homo sapiens. DR KEGG; hsa:116844; -. DR H-InvDB; HIX0014668; -. DR HGNC; HGNC:29480; LRG1. DR HPA; HPA001888; -. DR HPA; HPA001889; -. DR ArrayExpress; P02750; -. DR GermOnline; ENSG00000171236; Homo sapiens. DR RZPD-ProtExp; IOH22693; -. DR RZPD-ProtExp; T3430; -. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR InterPro; IPR001611; LRR. DR InterPro; IPR000483; LRR_C. DR InterPro; IPR003591; LRR_typ. DR Pfam; PF00560; LRR_1; 8. DR PRINTS; PR00019; LEURICHRPT. DR SMART; SM00369; LRR_TYP; 4. DR SMART; SM00082; LRRCT; 1. KW Direct protein sequencing; Glycoprotein; Leucine-rich repeat; KW Polymorphism; Repeat; Signal. FT SIGNAL 1 35 FT CHAIN 36 347 Leucine-rich alpha-2-glycoprotein. FT /FTId=PRO_0000020579. FT REPEAT 91 114 LRR 1. FT REPEAT 115 138 LRR 2. FT REPEAT 140 162 LRR 3. FT REPEAT 163 186 LRR 4. FT REPEAT 188 210 LRR 5. FT REPEAT 212 234 LRR 6. FT REPEAT 235 258 LRR 7. FT REPEAT 259 282 LRR 8. FT SITE 306 306 Not glycosylated. FT CARBOHYD 37 37 O-linked (GalNAc...). FT CARBOHYD 79 79 N-linked (GlcNAc...). FT CARBOHYD 186 186 N-linked (GlcNAc...). FT CARBOHYD 269 269 N-linked (GlcNAc...). FT CARBOHYD 325 325 N-linked (GlcNAc...). FT DISULFID 43 56 FT DISULFID 303 329 FT VARIANT 133 133 P -> S (in dbSNP:rs966384). FT /FTId=VAR_024245. SQ SEQUENCE 347 AA; 38178 MW; 20C99ED50152FA9C CRC64; MSSWSRQRPK SPGGIQPHVS RTLFLLLLLA ASAWGVTLSP KDCQVFRSDH GSSISCQPPA EIPGYLPADT VHLAVEFFNL THLPANLLQG ASKLQELHLS SNGLESLSPE FLRPVPQLRV LDLTRNALTG LPPGLFQASA TLDTLVLKEN QLEVLEVSWL HGLKALGHLD LSGNRLRKLP PGLLANFTLL RTLDLGENQL ETLPPDLLRG PLQLERLHLE GNKLQVLGKD LLLPQPDLRY LFLNGNKLAR VAAGAFQGLR QLDMLDLSNN SLASVPEGLW ASLGQPNWDM RDGFDISGNP WICDQNLSDL YRWLQAQKDK MFSQNDTRCA GPEAVKGQTL LAVAKSQ // ID A2MG_BOVIN Reviewed; 130 AA. AC Q7SIH1; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 31-OCT-2006, entry version 23. DE Alpha-2-macroglobulin (Alpha-2-M) (Fragment). GN Name=A2M; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), PARTIAL PROTEIN SEQUENCE, AND RP GLYCOSYLATION AT ASN-66. RX PubMed=9634697; DOI=10.1016/S0969-2126(98)00061-6; RA Jenner L., Husted L., Thirup S., Sottrup-Jensen L., Nyborg J.; RT "Crystal structure of the receptor-binding domain of alpha 2- RT macroglobulin."; RL Structure 6:595-604(1998). CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a CC unique 'trapping' mechanism. This protein has a peptide stretch, CC called the 'bait region' which contains specific cleavage sites CC for different proteinases. When a proteinase cleaves the bait CC region, a conformational change is induced in the protein which CC traps the proteinase. The entrapped enzyme remains active against CC low molecular weight substrates (activity against high molecular CC weight substrates is greatly reduced). Following cleavage in the CC bait region a thioester bond is hydrolyzed and mediates the CC covalent binding of the protein to the proteinase (By similarity). CC -!- SUBUNIT: Homotetramer; disulfide-linked (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PDB; 1AYO; X-ray; A/B=1-130. DR MEROPS; I39.001; -. DR KEGG; bta:513856; -. DR InterPro; IPR011627; A2M_rcpt. DR InterPro; IPR009048; AMG_rcpt_bd. DR InterPro; IPR001599; MacrogloblnA2. DR Pfam; PF07677; A2M_recep; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; PARTIAL. KW 3D-structure; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor. FT CHAIN <1 >130 Alpha-2-macroglobulin. FT /FTId=PRO_0000093790. FT CARBOHYD 66 66 N-linked (GlcNAc...). FT CARBOHYD 86 86 N-linked (GlcNAc...) (By similarity). FT DISULFID 15 129 FT NON_TER 1 1 FT NON_TER 130 130 FT STRAND 3 14 FT HELIX 18 21 FT TURN 22 22 FT STRAND 23 32 FT STRAND 34 47 FT TURN 50 51 FT STRAND 52 54 FT HELIX 56 60 FT TURN 61 62 FT STRAND 64 73 FT TURN 74 75 FT STRAND 76 82 FT STRAND 89 99 FT STRAND 107 115 FT TURN 117 118 FT STRAND 120 125 FT TURN 128 129 SQ SEQUENCE 130 AA; 14493 MW; 947E47A4584777CE CRC64; EFPFALEVQT LPQTCDGPKA HTSFQISLSV SYIGSRPASN MAIVDVKMVS GFIPLKPTVK MLERSNVSRT EVSNNHVLIY LDKVTNETLT LTFTVLQDIP VRDLKPAIVK VYDYYETDEF AVAEYSAPCS // ID A2MG_HUMAN Reviewed; 1474 AA. AC P01023; Q13677; Q59F47; Q5QTS0; Q68DN2; Q6PIY3; Q6PN97; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 20-FEB-2007, entry version 93. DE Alpha-2-macroglobulin precursor (Alpha-2-M). GN Name=A2M; ORFNames=FWP007; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=85190481; PubMed=2581245; RA Kan C.-C., Solomon E., Belt K.T., Chain A.C., Hiorns L.R., Fey G.H.; RT "Nucleotide sequence of cDNA encoding human alpha 2-macroglobulin and RT assignment of the chromosomal locus."; RL Proc. Natl. Acad. Sci. U.S.A. 82:2282-2286(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-704. RC TISSUE=Placenta; RX MEDLINE=92246939; PubMed=1374237; RA Matthijs G., Devriendt K., Cassiman J.-J., van den Berghe H., RA Marynen P.; RT "Structure of the human alpha-2 macroglobulin gene and its promotor."; RL Biochem. Biophys. Res. Commun. 184:596-603(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Prostate; RX PubMed=15611997; DOI=10.1002/pros.20183; RA Lin V.K., Wang S.-Y., Boetticher N.C., Vazquez D.V., Saboorian H., RA McConnell J.D., Roehrborn C.G.; RT "Alpha(2) macroglobulin, a PSA-binding protein, is expressed in human RT prostate stroma."; RL Prostate 63:299-308(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RG The German cDNA consortium; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-1000. RC TISSUE=Spleen; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno F.R.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 24-1474, SUBUNIT, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DISULFIDE BONDS. RX MEDLINE=84239807; PubMed=6203908; RA Sottrup-Jensen L., Stepanik T.M., Kristensen T., Wierzbicki D.M., RA Jones C.M., Loenblad P.B., Magnusson S., Petersen T.E.; RT "Primary structure of human alpha 2-macroglobulin. V. The complete RT structure."; RL J. Biol. Chem. 259:8318-8327(1984). RN [8] RP ERRATUM. RA Sottrup-Jensen L., Stepanik T.M., Kristensen T., Wierzbicki D.M., RA Jones C.M., Loenblad P.B., Magnusson S., Petersen T.E.; RL J. Biol. Chem. 260:6500-6500(1985). RN [9] RP PROTEIN SEQUENCE OF 273-286 AND 426-436, AND DISULFIDE BONDS. RX PubMed=2430963; RA Jensen P.E.H., Sottrup-Jensen L.; RT "Primary structure of human alpha 2-macroglobulin. Complete disulfide RT bridge assignment and localization of two interchain bridges in the RT dimeric proteinase binding unit."; RL J. Biol. Chem. 261:15863-15869(1986). RN [10] RP PROTEIN SEQUENCE OF 672-747. RX MEDLINE=90242963; PubMed=1692292; DOI=10.1016/0014-5793(90)80226-9; RA Marynen P., Devriendt K., van den Berghe H., Cassiman J.-J.; RT "A genetic polymorphism in a functional domain of human pregnancy zone RT protein: the bait region. Genomic structure of the bait domains of RT human pregnancy zone protein and alpha 2 macroglobulin."; RL FEBS Lett. 262:349-352(1990). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 672-746, AND VARIANTS TYR-972 AND RP ILE-1000. RX MEDLINE=92128897; PubMed=1370808; DOI=10.1007/BF00197266; RA Poller W., Faber J.-P., Klobeck G., Olek K.; RT "Cloning of the human alpha 2-macroglobulin gene and detection of RT mutations in two functional domains: the bait region and the RT thiolester site."; RL Hum. Genet. 88:313-319(1992). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 832-1474. RC TISSUE=Liver; RX MEDLINE=85219061; PubMed=2408344; RA Bell G.I., Rall L.B., Sanchez-Pescador R., Merryweather J.P., RA Scott J., Eddy R.L., Shows T.B.; RT "Human alpha 2-macroglobulin gene is located on chromosome 12."; RL Somat. Cell Mol. Genet. 11:285-289(1985). RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1208-1474. RC TISSUE=Aorta; RA Liu B., Zhao B., Wang X.Y., Xu Y.Y., Liu Y.Q., Song L., Ye J., RA Sheng H., Gao Y., Zhang C.L., Wei Y.J., Zhang J., Song L., Jiang Y.X., RA Zhao Z.W., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y., Qiang B.Q., RA Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [14] RP GLYCOSYLATION AT ASN-991. RX MEDLINE=22660472; PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [15] RP INHIBITORY SITE. RX MEDLINE=84030513; PubMed=6195065; RA Virca G.D., Salvesen G.S., Travis J.; RT "Human neutrophil elastase and cathepsin G cleavage sites in the bait RT region of alpha 2-macroglobulin. Proposed structural limits of the RT bait region."; RL Hoppe-Seyler's Z. Physiol. Chem. 364:1297-1302(1983). RN [16] RP INHIBITORY SITE. RX MEDLINE=81212827; PubMed=6165619; DOI=10.1016/0014-5793(81)80197-4; RA Sottrup-Jensen L., Loenblad P.B., Stepanik T.M., Petersen T.E., RA Magnusson S., Joernvall H.; RT "Primary structure of the 'bait' region for proteinases in alpha 2- RT macroglobulin. Nature of the complex."; RL FEBS Lett. 127:167-173(1981). RN [17] RP INHIBITORY SITE. RX MEDLINE=81255805; PubMed=6167263; RA Hall P.K., Nelles L.P., Travis J., Roberts R.C.; RT "Proteolytic cleavage sites on alpha 2-macroglobulin resulting in RT proteinase binding are different for trypsin and Staphylococcus aureus RT V-8 proteinase."; RL Biochem. Biophys. Res. Commun. 100:8-16(1981). RN [18] RP INHIBITORY SITE. RX MEDLINE=82095610; PubMed=6172288; DOI=10.1016/0014-5793(81)80804-6; RA Mortensen S.B., Sottrup-Jensen L., Hansen H.F., Petersen T.E., RA Magnusson S.; RT "Primary and secondary cleavage sites in the bait region of alpha 2- RT macroglobulin."; RL FEBS Lett. 135:295-300(1981). RN [19] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-869 AND ASN-1424, AND MASS RP SPECTROMETRY. RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55; ASN-247; ASN-396; RP ASN-410; ASN-869; ASN-991 AND ASN-1424, AND MASS SPECTROMETRY. RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [21] RP STRUCTURE BY NMR OF 1337-1474. RX MEDLINE=99081553; PubMed=9865955; RA Huang W., Dolmer K., Liao X., Gettins P.G.W.; RT "Localization of basic residues required for receptor binding to the RT single alpha-helix of the receptor binding domain of human alpha2- RT macroglobulin."; RL Protein Sci. 7:2602-2612(1998). RN [22] RP VARIANT ILE-1000. RX MEDLINE=91187639; PubMed=1707161; DOI=10.1093/nar/19.1.198-a; RA Poller W., Faber J.-P., Olek K.; RT "Sequence polymorphism in the human alpha2-macroglobulin (A2M) gene."; RL Nucleic Acids Res. 19:198-198(1991). CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a CC unique 'trapping' mechanism. This protein has a peptide stretch, CC called the 'bait region' which contains specific cleavage sites CC for different proteinases. When a proteinase cleaves the bait CC region, a conformational change is induced in the protein which CC traps the proteinase. The entrapped enzyme remains active against CC low molecular weight substrates (activity against high molecular CC weight substrates is greatly reduced). Following cleavage in the CC bait region a thioester bond is hydrolyzed and mediates the CC covalent binding of the protein to the proteinase. CC -!- SUBUNIT: Homotetramer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- DEVELOPMENTAL STAGE: Contrary to the rat protein, which is an CC acute phase protein, this protein is always present at high levels CC in circulation. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M11313; AAA51551.1; -; mRNA. DR EMBL; Z11711; CAA77774.1; -; Genomic_DNA. DR EMBL; AY591530; AAT02228.1; ALT_INIT; mRNA. DR EMBL; CR749334; CAH18188.1; -; mRNA. DR EMBL; AB209614; BAD92851.1; ALT_INIT; mRNA. DR EMBL; BC026246; AAH26246.1; -; mRNA. DR EMBL; BC040071; AAH40071.1; -; mRNA. DR EMBL; X68728; CAA48670.1; -; Genomic_DNA. DR EMBL; X68729; CAA48670.1; JOINED; Genomic_DNA. DR EMBL; M36501; AAA51552.1; -; mRNA. DR EMBL; AF109189; AAQ13498.1; -; mRNA. DR PIR; A94033; MAHU. DR UniGene; Hs.212838; -. DR PDB; 1BV8; NMR; A=1337-1474. DR DIP; DIP:1118N; -. DR MEROPS; I39.001; -. DR SWISS-2DPAGE; P01023; HUMAN. DR DOSAC-COBS-2DPAGE; P01023; HUMAN. DR Ensembl; ENSG00000175899; Homo sapiens. DR KEGG; hsa:2; -. DR HGNC; HGNC:7; A2M. DR HPA; HPA002265; -. DR MIM; 103950; gene+phenotype. DR Reactome; REACT_604.1; Hemostasis. DR LinkHub; P01023; -. DR ArrayExpress; P01023; -. DR GermOnline; ENSG00000175899; Homo sapiens. DR RZPD-ProtExp; IOH26170; -. DR RZPD-ProtExp; K2646; -. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0004866; F:endopeptidase inhibitor activity; NAS:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0019966; F:interleukin-1 binding; IDA:UniProtKB. DR GO; GO:0019959; F:interleukin-8 binding; IPI:UniProtKB. DR GO; GO:0043120; F:tumor necrosis factor binding; IDA:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; NAS:UniProtKB. DR InterPro; IPR011626; A2M_comp. DR InterPro; IPR002890; A2M_N. DR InterPro; IPR011625; A2M_N_2. DR InterPro; IPR011627; A2M_rcpt. DR InterPro; IPR009048; AMG_rcpt_bd. DR InterPro; IPR001599; MacrogloblnA2. DR InterPro; IPR008930; Terp_cyc_toroid. DR Pfam; PF00207; A2M; 1. DR Pfam; PF07678; A2M_comp; 1. DR Pfam; PF01835; A2M_N; 1. DR Pfam; PF07703; A2M_N_2; 1. DR Pfam; PF07677; A2M_recep; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. KW 3D-structure; Bait region; Direct protein sequencing; Glycoprotein; KW Polymorphism; Protease inhibitor; Serine protease inhibitor; Signal; KW Thioester bond. FT SIGNAL 1 23 FT CHAIN 24 1474 Alpha-2-macroglobulin. FT /FTId=PRO_0000000055. FT REGION 690 728 Bait region. FT REGION 704 709 Inhibitory. FT REGION 719 723 Inhibitory. FT REGION 730 735 Inhibitory. FT CARBOHYD 55 55 N-linked (GlcNAc...). FT CARBOHYD 70 70 N-linked (GlcNAc...). FT CARBOHYD 247 247 N-linked (GlcNAc...). FT CARBOHYD 396 396 N-linked (GlcNAc...). FT CARBOHYD 410 410 N-linked (GlcNAc...). FT CARBOHYD 869 869 N-linked (GlcNAc...). FT CARBOHYD 991 991 N-linked (GlcNAc...). FT CARBOHYD 1424 1424 N-linked (GlcNAc...). FT DISULFID 48 86 FT DISULFID 251 299 FT DISULFID 269 287 FT DISULFID 278 278 Interchain (with C-431). FT DISULFID 431 431 Interchain (with C-278). FT DISULFID 470 563 FT DISULFID 595 771 FT DISULFID 642 689 FT DISULFID 821 849 FT DISULFID 847 883 FT DISULFID 921 1321 FT DISULFID 1079 1127 FT DISULFID 1352 1467 FT CROSSLNK 693 693 Isoglutamyl lysine isopeptide (Gln-Lys) FT (interchain with K-? in other proteins) FT (Potential). FT CROSSLNK 694 694 Isoglutamyl lysine isopeptide (Gln-Lys) FT (interchain with K-? in other proteins) FT (Potential). FT CROSSLNK 972 975 Isoglutamyl cysteine thioester (Cys-Gln). FT VARIANT 639 639 D -> N (in dbSNP:rs226405). FT /FTId=VAR_026820. FT VARIANT 704 704 R -> H (in dbSNP:rs1800434). FT /FTId=VAR_000012. FT VARIANT 815 815 L -> Q (in dbSNP:rs3180392). FT /FTId=VAR_026821. FT VARIANT 972 972 C -> Y (probably interferes with the FT activity; dbSNP:rs1800433). FT /FTId=VAR_000013. FT VARIANT 1000 1000 V -> I (in dbSNP:rs669). FT /FTId=VAR_000014. FT CONFLICT 63 63 Missing (in Ref. 7). FT CONFLICT 82 82 D -> V (in Ref. 3). FT CONFLICT 350 353 LSFV -> ACCS (in Ref. 6; AAH26246). FT CONFLICT 563 563 C -> E (in Ref. 7). FT CONFLICT 844 844 A -> V (in Ref. 5). FT CONFLICT 872 872 V -> M (in Ref. 4). FT CONFLICT 1148 1148 A -> D (in Ref. 12). FT CONFLICT 1195 1195 H -> D (in Ref. 12). FT STRAND 1341 1347 FT TURN 1352 1353 FT HELIX 1355 1359 FT STRAND 1360 1369 FT STRAND 1379 1384 FT STRAND 1389 1391 FT HELIX 1393 1400 FT TURN 1401 1403 FT STRAND 1407 1410 FT STRAND 1412 1419 FT STRAND 1427 1434 FT STRAND 1445 1450 FT STRAND 1454 1456 FT STRAND 1459 1463 SQ SEQUENCE 1474 AA; 163278 MW; F1D517427971CEFE CRC64; MGKNKLLHPS LVLLLLVLLP TDASVSGKPQ YMVLVPSLLH TETTEKGCVL LSYLNETVTV SASLESVRGN RSLFTDLEAE NDVLHCVAFA VPKSSSNEEV MFLTVQVKGP TQEFKKRTTV MVKNEDSLVF VQTDKSIYKP GQTVKFRVVS MDENFHPLNE LIPLVYIQDP KGNRIAQWQS FQLEGGLKQF SFPLSSEPFQ GSYKVVVQKK SGGRTEHPFT VEEFVLPKFE VQVTVPKIIT ILEEEMNVSV CGLYTYGKPV PGHVTVSICR KYSDASDCHG EDSQAFCEKF SGQLNSHGCF YQQVKTKVFQ LKRKEYEMKL HTEAQIQEEG TVVELTGRQS SEITRTITKL SFVKVDSHFR QGIPFFGQVR LVDGKGVPIP NKVIFIRGNE ANYYSNATTD EHGLVQFSIN TTNVMGTSLT VRVNYKDRSP CYGYQWVSEE HEEAHHTAYL VFSPSKSFVH LEPMSHELPC GHTQTVQAHY ILNGGTLLGL KKLSFYYLIM AKGGIVRTGT HGLLVKQEDM KGHFSISIPV KSDIAPVARL LIYAVLPTGD VIGDSAKYDV ENCLANKVDL SFSPSQSLPA SHAHLRVTAA PQSVCALRAV DQSVLLMKPD AELSASSVYN LLPEKDLTGF PGPLNDQDDE DCINRHNVYI NGITYTPVSS TNEKDMYSFL EDMGLKAFTN SKIRKPKMCP QLQQYEMHGP EGLRVGFYES DVMGRGHARL VHVEEPHTET VRKYFPETWI WDLVVVNSAG VAEVGVTVPD TITEWKAGAF CLSEDAGLGI SSTASLRAFQ PFFVELTMPY SVIRGEAFTL KATVLNYLPK CIRVSVQLEA SPAFLAVPVE KEQAPHCICA NGRQTVSWAV TPKSLGNVNF TVSAEALESQ ELCGTEVPSV PEHGRKDTVI KPLLVEPEGL EKETTFNSLL CPSGGEVSEE LSLKLPPNVV EESARASVSV LGDILGSAMQ NTQNLLQMPY GCGEQNMVLF APNIYVLDYL NETQQLTPEV KSKAIGYLNT GYQRQLNYKH YDGSYSTFGE RYGRNQGNTW LTAFVLKTFA QARAYIFIDE AHITQALIWL SQRQKDNGCF RSSGSLLNNA IKGGVEDEVT LSAYITIALL EIPLTVTHPV VRNALFCLES AWKTAQEGDH GSHVYTKALL AYAFALAGNQ DKRKEVLKSL NEEAVKKDNS VHWERPQKPK APVGHFYEPQ APSAEVEMTS YVLLAYLTAQ PAPTSEDLTS ATNIVKWITK QQNAQGGFSS TQDTVVALHA LSKYGAATFT RTGKAAQVTI QSSGTFSSKF QVDNNNRLLL QQVSLPELPG EYSMKVTGEG CVYLQTSLKY NILPEKEEFP FALGVQTLPQ TCDEPKAHTS FQISLSVSYT GSRSASNMAI VDVKMVSGFI PLKPTVKMLE RSNHVSRTEV SSNHVLIYLD KVSNQTLSLF FTVLQDVPVR DLKPAIVKVY DYYETDEFAI AEYNAPCSKD LGNA // ID A2MG_PONPY Reviewed; 1474 AA. AC Q5R4N8; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 31-OCT-2006, entry version 18. DE Alpha-2-macroglobulin precursor (Alpha-2-M). GN Name=A2M; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a CC unique 'trapping' mechanism. This protein has a peptide stretch, CC called the 'bait region' which contains specific cleavage sites CC for different proteinases. When a proteinase cleaves the bait CC region, a conformational change is induced in the protein which CC traps the proteinase. The entrapped enzyme remains active against CC low molecular weight substrates (activity against high molecular CC weight substrates is greatly reduced). Following cleavage in the CC bait region a thioester bond is hydrolyzed and mediates the CC covalent binding of the protein to the proteinase (By similarity). CC -!- SUBUNIT: Homotetramer; disulfide-linked (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- TISSUE SPECIFICITY: Plasma. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR861207; CAH93278.1; -; mRNA. DR SMR; Q5R4N8; 1338-1468. DR InterPro; IPR011626; A2M_comp. DR InterPro; IPR002890; A2M_N. DR InterPro; IPR011625; A2M_N_2. DR InterPro; IPR011627; A2M_rcpt. DR InterPro; IPR009048; AMG_rcpt_bd. DR InterPro; IPR008964; Invasin_intimin. DR InterPro; IPR001599; MacrogloblnA2. DR InterPro; IPR008930; Terp_cyc_toroid. DR Pfam; PF00207; A2M; 1. DR Pfam; PF07678; A2M_comp; 1. DR Pfam; PF01835; A2M_N; 1. DR Pfam; PF07703; A2M_N_2; 1. DR Pfam; PF07677; A2M_recep; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. KW Bait region; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal; Thioester bond. FT SIGNAL 1 23 Potential. FT CHAIN 24 1474 Alpha-2-macroglobulin. FT /FTId=PRO_0000042695. FT REGION 690 728 Bait region (By similarity). FT REGION 704 709 Inhibitory (By similarity). FT REGION 719 723 Inhibitory (By similarity). FT REGION 730 735 Inhibitory (By similarity). FT CARBOHYD 55 55 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 70 70 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 247 247 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 396 396 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 410 410 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 869 869 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 991 991 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 1424 1424 N-linked (GlcNAc...) (By similarity). FT DISULFID 48 86 By similarity. FT DISULFID 251 299 By similarity. FT DISULFID 269 287 By similarity. FT DISULFID 278 278 Interchain (with C-431) (By similarity). FT DISULFID 431 431 Interchain (with C-278) (By similarity). FT DISULFID 470 563 By similarity. FT DISULFID 595 771 By similarity. FT DISULFID 642 689 By similarity. FT DISULFID 821 849 By similarity. FT DISULFID 847 883 By similarity. FT DISULFID 921 1321 By similarity. FT DISULFID 1079 1127 By similarity. FT DISULFID 1352 1467 By similarity. FT CROSSLNK 693 693 Isoglutamyl lysine isopeptide (Gln-Lys) FT (interchain with K-? in other proteins) FT (Potential). FT CROSSLNK 694 694 Isoglutamyl lysine isopeptide (Gln-Lys) FT (interchain with K-? in other proteins) FT (Potential). FT CROSSLNK 972 975 Isoglutamyl cysteine thioester (Cys-Gln) FT (By similarity). SQ SEQUENCE 1474 AA; 163262 MW; 14F19160ACBCAB6B CRC64; MGKNKLLHPS LVLLLLVLLP TDASVSGKPQ YMVLVPSLLH TEAAEKGCVL LSYLNETVTV SASLESVRGN RSLFTDLEAE NDVLHCVAFA IPKSSSNEEV MFLTVQVKGP TQEFKKRTTV MVKNEDSLVF VQTDKSIYKP AQTVKFRVVS MDENFHPLNE LIPLVYIQDP KGNRIAQWQS FQLEGGLKQF SFPLSSEPFQ GSYKVVVQKK SGRRTEHPFT VEEFVLPKFE VQVTVPKIIT ILEEEMNVSV CGLYTYGKPV PGHVTVSICR KYSDASNCHG EDSQAFCEKF SGQLNSHGCF YQQVKTKVFQ LKRKEYEMKL HTKAQIQEEG TVVELTGRQS SEITRTITKL SFVKADSHFR QGIPFFGQVR LVDGKGVPIP NKVIFIRGNE ANYYSNATTD EHGLVQFSIN TTNVMGTSLT VRVKYKDRSP CYGYQWVSEE HEEAHHTAYL VFSPSKSFVH LEPVSHELPC GQTQTVQAHY ILNGGALQGL KKLSFYYLIM AKGGIVRTGT HGLLVKQEDM KGHFSISIPV KSDIAPVARL LIYAVLPTGD VIGDSAKYDV ENCLANKVDL SFSPSQSLPA LHAHLRVTAA PQSLCALRAV DQSVLLMKPD AELSASSVYN LLPEKDLTGF PGPLNDQGDE DCINRHNVYI NGITYTPVSS TNEKDMYSFL EDMGLKAFTN SKIRKPKLCP QLQQYEMHGP EGLRVGFYES DVMGRGHARL VHAEEPPTET VRKYFPETWI WDLVVVNSSG VAEVGVTVPD TITEWKAGAF CLSEDAGLGI SSTASLRAFQ PFFVELTMPY SVIRGEVFTL KATVLNYLPK CIRVSVQLEA SPAFLAVPVE KEQAPHCICA NGRQTVSWAI TPKSLGNVNF TVSAEALESQ ELCGTEVASV PEYGKKDTVI KPLLVEPEGL EKETTFNSLL CPSGGEVSEE LSLKLPPNVV EESARASVSV LGDILGSAMQ NTQNLLQMPY GCGEQNMVLF APNIYVLDYL NETQQLTPEI KSKAIGYLNT GYQRQLNYKH YDGSYSTFGE RYGRNQGNTW LTAFVLKTFA QARAYIFIDE AHITQALIWL SQRQKDNGCF RSSGSLLNNA IKGGVEDEVT LSAYITIALL EIPLTVTHPV VRNALFCLES AWKTAQEGDH GSHVYTKALL AYAFALAGNQ DKRKEVLQSL HEEAVKKDNS VHWERPQKPK APVGHFYEPQ APSAEVEMTS YALLAYLTAQ PAPTSEDLTS ATNIVKWITK QQNAQGGFSS TQDTVVALHA LSKYGAATFT RTGKAAQVTI QSSGTFSNKF QVDNNNRLLL QQVSLPELPG EYSMKVTGEG CVYLQTSLKY NILPEKEEFP FALGVQTLPQ TCDEPKAHTS FQISLSVSYT GSRSASNMAI VDVKMVSGFI PLKPTVKMLE RSNHVSRTEV SNNHVLIYLD KVSNQTLSLF FTVLQDVPVR DLKPAIVKVY DYYETDEFAI AEYNAPCSKD LGNA // ID A2MG_RAT Reviewed; 1472 AA. AC P06238; Q4FZY3; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 20-FEB-2007, entry version 67. DE Alpha-2-macroglobulin precursor (Alpha-2-M). GN Name=A2m; Synonyms=A2m1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION. RC TISSUE=Liver; RX MEDLINE=87083488; PubMed=2432068; RA Gehring M.R., Shiels B.R., Northemann W., de Bruijn M.H.L., Kan C.-C., RA Chain A.C., Noonan D.J., Fey G.H.; RT "Sequence of rat liver alpha 2-macroglobulin and acute phase control RT of its messenger RNA."; RL J. Biol. Chem. 262:446-454(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 1-164. RC STRAIN=Wistar; TISSUE=Liver; RX MEDLINE=89160243; PubMed=2466233; DOI=10.1093/nar/17.3.1121; RA Kunz D., Zimmermann R., Heisig M., Heinrich P.C.; RT "Identification of the promoter sequences involved in the interleukin- RT 6 dependent expression of the rat alpha 2-macroglobulin gene."; RL Nucleic Acids Res. 17:1121-1138(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 178-227 AND 420-526. RX MEDLINE=86033908; PubMed=2414291; RA Hayashida K., Okubo H., Noguchi M., Yoshida H., Kangawa K., Matsuo H., RA Sakaki Y.; RT "Molecular cloning of DNA complementary to rat alpha 2-macroglobulin RT mRNA."; RL J. Biol. Chem. 260:14224-14229(1985). RN [5] RP TISSUE SPECIFICITY. RC STRAIN=Fischer 344; TISSUE=Liver; RX PubMed=1725450; RA Eggertsen G., Hudson G., Shiels B., Reed D., Fey G.H.; RT "Sequence of rat alpha 1-macroglobulin, a broad-range proteinase RT inhibitor from the alpha-macroglobulin-complement family."; RL Mol. Biol. Med. 8:287-302(1991). CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a CC unique 'trapping' mechanism. This protein has a peptide stretch, CC called the 'bait region' which contains specific cleavage sites CC for different proteinases. When a proteinase cleaves the bait CC region, a conformational change is induced in the protein which CC traps the proteinase. The entrapped enzyme remains active against CC low molecular weight substrates (activity against high molecular CC weight substrates is greatly reduced). Following cleavage in the CC bait region a thioester bond is hydrolyzed and mediates the CC covalent binding of the protein to the proteinase. CC -!- SUBUNIT: Homotetramer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Highest constitutive expression in ovary. Low CC level in testis, uterus and non-acute phase liver. Protein found CC in plasma. CC -!- INDUCTION: By inflammatory stimulus in liver. The level of this CC protein increases during acute phase, then decreases again. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J02635; AAA40636.1; -; mRNA. DR EMBL; BC098922; AAH98922.1; -; mRNA. DR EMBL; X13983; CAA32164.1; -; Genomic_DNA. DR EMBL; X13984; CAA32164.1; JOINED; Genomic_DNA. DR EMBL; X13985; CAA32164.1; JOINED; Genomic_DNA. DR EMBL; M11792; AAA40637.1; -; mRNA. DR EMBL; M11793; AAA40638.1; -; mRNA. DR PIR; A26122; A26122. DR UniGene; Rn.198688; -. DR HSSP; P01023; 1BV8. DR SMR; P06238; 1336-1466. DR MEROPS; I39.001; -. DR Ensembl; ENSRNOG00000028896; Rattus norvegicus. DR KEGG; rno:24153; -. DR RGD; 2004; A2m1. DR ArrayExpress; P06238; -. DR GermOnline; ENSRNOG00000028896; Rattus norvegicus. DR GO; GO:0004866; F:endopeptidase inhibitor activity; NAS:UniProtKB. DR GO; GO:0005102; F:receptor binding; TAS:RGD. DR GO; GO:0006953; P:acute-phase response; IEP:RGD. DR GO; GO:0010037; P:response to carbon dioxide; IEP:RGD. DR GO; GO:0051384; P:response to glucocorticoid stimulus; IEP:RGD. DR GO; GO:0007584; P:response to nutrient; IEP:RGD. DR InterPro; IPR011626; A2M_comp. DR InterPro; IPR002890; A2M_N. DR InterPro; IPR011625; A2M_N_2. DR InterPro; IPR011627; A2M_rcpt. DR InterPro; IPR009048; AMG_rcpt_bd. DR InterPro; IPR001599; MacrogloblnA2. DR InterPro; IPR008930; Terp_cyc_toroid. DR Pfam; PF00207; A2M; 1. DR Pfam; PF07678; A2M_comp; 1. DR Pfam; PF01835; A2M_N; 1. DR Pfam; PF07703; A2M_N_2; 1. DR Pfam; PF07677; A2M_recep; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. KW Acute phase; Bait region; Glycoprotein; Protease inhibitor; KW Serine protease inhibitor; Signal; Thioester bond. FT SIGNAL 1 27 FT CHAIN 28 1472 Alpha-2-macroglobulin. FT /FTId=PRO_0000000058. FT REGION 620 750 Bait region. FT CARBOHYD 59 59 N-linked (GlcNAc...) (Potential). FT CARBOHYD 74 74 N-linked (GlcNAc...) (Potential). FT CARBOHYD 250 250 N-linked (GlcNAc...) (Potential). FT CARBOHYD 399 399 N-linked (GlcNAc...) (Potential). FT CARBOHYD 651 651 N-linked (GlcNAc...) (Potential). FT CARBOHYD 772 772 N-linked (GlcNAc...) (Potential). FT CARBOHYD 867 867 N-linked (GlcNAc...) (Potential). FT CARBOHYD 989 989 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1364 1364 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1422 1422 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1426 1426 N-linked (GlcNAc...) (Potential). FT DISULFID 52 90 By similarity. FT DISULFID 254 302 By similarity. FT DISULFID 272 290 By similarity. FT DISULFID 281 281 Interchain (with C-434) (By similarity). FT DISULFID 434 434 Interchain (with C-281) (By similarity). FT DISULFID 473 566 By similarity. FT DISULFID 598 769 By similarity. FT DISULFID 647 694 By similarity. FT DISULFID 819 847 By similarity. FT DISULFID 845 881 By similarity. FT DISULFID 919 1319 By similarity. FT DISULFID 1077 1125 By similarity. FT DISULFID 1350 1465 By similarity. FT CROSSLNK 970 973 Isoglutamyl cysteine thioester (Cys-Gln). FT CONFLICT 23 23 L -> V (in Ref. 3; CAA32164). FT CONFLICT 72 72 R -> H (in Ref. 1; AAA40636 and 3; FT CAA32164). FT CONFLICT 103 103 V -> L (in Ref. 1; AAA40636 and 3; FT CAA32164). FT CONFLICT 120 120 R -> Q (in Ref. 1; AAA40636 and 3; FT CAA32164). FT CONFLICT 490 490 M -> L (in Ref. 4; AAA40638). FT CONFLICT 1025 1025 T -> A (in Ref. 1; AAA40636). FT CONFLICT 1192 1192 A -> G (in Ref. 1; AAA40636). FT CONFLICT 1200 1200 P -> T (in Ref. 1; AAA40636). FT CONFLICT 1279 1279 H -> R (in Ref. 1; AAA40636). FT CONFLICT 1340 1340 T -> A (in Ref. 1; AAA40636). SQ SEQUENCE 1472 AA; 163785 MW; BFD63B8A4F6A2632 CRC64; MGKHRLRSLA LLPLLLRLLL LLLPTDASAP QKPIYMVMVP SLLHAGTPEK ACFLFSHLNE TVAVRVSLES VRGNQSLFTD LVVDKDLFHC TSFTVPQSSS DEVMFFTVQV KGATHEFRRR STVLVKKKES LVFAQTDKPI YKPGQTVRFR VVSLDESFHP LNELIPLLYI QDPKNNRIAQ WQNFNLEGGL KQLSFPLSSE PTQGSYKVVI RTESGRTVEH PFSVEEFVLP KFEVRVTVPE TITILEEEMN VSVCGIYTYG KPVPGRVTVN ICRKYSNPSN CFGEESVAFC EKLSQQLDGR GCFSQLVKTK SFQLKRQEYE MQLDVHAKIQ EEGTGVEETG KGLTKITRTI TKLSFVNVDS HFRQGIPFVG QVLLVDGRGT PIPYETIFIG ADEANLYINT TTDKHGLARF SINTDDIMGT SLTVRAKYKD SNACYGFRWL TEENVEAWHT AYAVFSPSRS FLHLESLPDK LRCDQTLEVQ AHYILNGEAM QELKELVFYY LMMAKGGIVR AGTHVLPLKQ GQMRGHFSIL ISMETDLAPV ARLVLYAILP NGEVVGDTAK YEIENCLANK VDLVFRPNSG LPATRALLSV MASPQSLCGL RAVDQSVLLM KPETELSASL IYDLLPVKDL TGFPQGADQR EEDTNGCVKQ NDTYINGILY SPVQNTNEED MYGFLKDMGL KVFTNSNIRK PKVCERLRDN KGIPAAYHLV SQSHMDAFLE SSESPTETRR SYFPETWIWD LVVVDSAGVA EVEVTVPDTI TEWKAGAFCL SNDTGLGLSP VVQFQAFQPF FVELTMPYSV IRGEAFTLKA TVLNYLPTCI RVAVQLEASP DFLAAPEEKE QRSHCICMNQ RHTASWAVIP KSLGNVNFTV SAEALNSKEL CGNEVPVVPE QGKKDTIIKS LLVEPEGLEN EVTFNSLLCP MGAEVSELIA LKLPSDVVEE SARASVTVLG DILGSAMQNT QDLLKMPYGC GEQNMVLFAP NIYVLDYLNE TQQLTQEIKT KAIAYLNTGY QRQLNYKHRD GSYSTFGDKP GRNHANTWLT AFVLKSFAQA RKYIFIDEVH ITQALLWLSQ QQKDNGCFRS SGSLLNNAMK GGVEDEVTLS AYITIALLEM SLPVTHPVVR NALFCLDTAW KSARGGAGGS HVYTKALLAY AFALAGNQDT KKEILKSLDE EAVKEEDSVH WTRPQKPSVS VALWYQPQAP SAEVEMTAYV LLAYLTTEPA PTQEDLTAAM LIVKWLTKQQ NSHGGFSSTQ DTVVALHALS KYGSATFTRA KKAAQVTIHS SGTFSTKFQV NNNNQLLLQR VTLPTVPGDY TVKVTGEGCV YLQTSLKYSV LPREEEFPFT VVVQTLPGTC EDPKAHTSFQ ISLNISYTGS RSESNMAIAD VKMVSGFIPL KPTVKMLERS VHVSRTEVSN NHVLIYLDKV SNQTVNLSFT VQQDIPIRDL KPAVVKVYDY YEKDEFAVAK YSAPCSTDYG NA // ID A2MP_MOUSE Reviewed; 1474 AA. AC Q6GQT1; Q811S0; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 09-JAN-2007, entry version 16. DE Alpha-2-macroglobulin-P precursor (Alpha-2-macroglobulin). GN Name=A2mp; Synonyms=A2m; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=C57BL/6; TISSUE=Placenta; RX PubMed=15355875; DOI=10.1095/biolreprod.104.029835; RA He H., McCartney D.J., Wei Q., Esadeg S., Zhang J., Foster R.A., RA Hayes M.A., Tayade C., Van Leuven F., Croy B.A.; RT "Characterization of a murine alpha 2 macroglobulin gene expressed in RT reproductive and cardiovascular tissue."; RL Biol. Reprod. 72:266-275(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: Is able to inhibit all four classes of proteinases by a CC unique 'trapping' mechanism. This protein has a peptide stretch, CC called the 'bait region' which contains specific cleavage sites CC for different proteinases. When a proteinase cleaves the bait CC region, a conformational change is induced in the protein which CC traps the proteinase. The entrapped enzyme remains active against CC low molecular weight substrates (activity against high molecular CC weight substrates is greatly reduced). Following cleavage in the CC bait region a thioester bond is hydrolyzed and mediates the CC covalent binding of the protein to the proteinase (By similarity). CC -!- SUBUNIT: Homotetramer; disulfide-linked (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in uterus, mesometrial lympoid CC aggregate and mammary tissue during pregnancy. Expressed in ovary, CC testis and kidney. Low level expression in heart. Not expressed in CC liver. CC -!- DEVELOPMENTAL STAGE: Expressed in uterus of pregnant females CC during decidualization from 6 dpc with highest level around 10 dpc CC declining throughout the rest of the pregnancy. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY185125; AAO25741.1; -; mRNA. DR EMBL; BC072642; AAH72642.1; -; mRNA. DR UniGene; Mm.30151; -. DR HSSP; P01023; 1BV8. DR SMR; Q6GQT1; 1338-1468. DR MEROPS; I39.001; -. DR Ensembl; ENSMUSG00000030111; Mus musculus. DR MGI; MGI:2449119; A2m. DR ArrayExpress; Q6GQT1; -. DR GO; GO:0030414; F:protease inhibitor activity; TAS:MGI. DR InterPro; IPR011626; A2M_comp. DR InterPro; IPR002890; A2M_N. DR InterPro; IPR011625; A2M_N_2. DR InterPro; IPR011627; A2M_rcpt. DR InterPro; IPR009048; AMG_rcpt_bd. DR InterPro; IPR001599; MacrogloblnA2. DR InterPro; IPR008930; Terp_cyc_toroid. DR Pfam; PF00207; A2M; 1. DR Pfam; PF07678; A2M_comp; 1. DR Pfam; PF01835; A2M_N; 1. DR Pfam; PF07703; A2M_N_2; 1. DR Pfam; PF07677; A2M_recep; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. KW Bait region; Glycoprotein; Pregnancy; Protease inhibitor; KW Serine protease inhibitor; Signal; Thioester bond. FT SIGNAL 1 32 Potential. FT CHAIN 33 1474 Alpha-2-macroglobulin-P. FT /FTId=PRO_0000271402. FT REGION 623 752 Bait region (By similarity). FT CARBOHYD 62 62 N-linked (GlcNAc...) (Potential). FT CARBOHYD 77 77 N-linked (GlcNAc...) (Potential). FT CARBOHYD 253 253 N-linked (GlcNAc...) (Potential). FT CARBOHYD 402 402 N-linked (GlcNAc...) (Potential). FT CARBOHYD 654 654 N-linked (GlcNAc...) (Potential). FT CARBOHYD 774 774 N-linked (GlcNAc...) (Potential). FT CARBOHYD 869 869 N-linked (GlcNAc...) (Potential). FT CARBOHYD 991 991 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1366 1366 N-linked (GlcNAc...) (Potential). FT DISULFID 257 305 By similarity. FT DISULFID 275 293 By similarity. FT DISULFID 284 284 Interchain (with C-437) (By similarity). FT DISULFID 437 437 Interchain (with C-284) (By similarity). FT DISULFID 476 569 By similarity. FT DISULFID 601 771 By similarity. FT DISULFID 650 697 By similarity. FT DISULFID 821 849 By similarity. FT DISULFID 847 883 By similarity. FT DISULFID 921 1321 By similarity. FT DISULFID 1079 1127 By similarity. FT DISULFID 1352 1467 By similarity. FT CROSSLNK 972 975 Isoglutamyl cysteine thioester (Cys-Gln) FT (By similarity). FT CONFLICT 366 366 R -> G (in Ref. 1; AAO25741). FT CONFLICT 452 452 H -> R (in Ref. 1; AAO25741). FT CONFLICT 659 666 NGILYSPV -> RNPVLPR (in Ref. 1; FT AAO25741). FT CONFLICT 799 799 A -> P (in Ref. 1; AAO25741). SQ SEQUENCE 1474 AA; 164327 MW; 14C6F4F0819EC1ED CRC64; MGKRWLPSLA LLPLPPPLLL LLLLLLPTNA SAPQKPIYMV MVPSLLHAGT PEKGCLLFNH LNETVTVKVS MESVRGNQSL FTDLVVDKDL FHCASFIVPQ SSSNEVMFLT VQVKGPTHEF RRRSTVLIKT KESLVFAQTD KPIYKPGQMV RFRVVSLDEN FHPLNELIPL LYIQDSKKNR IAQWQNFRLE GGLKQLSFPL SSEPTQGSYK VVIRTESGRT VEHPFSVKEF VLPKFEVKVA VPETITILEE EMNVSVCGIY TYGKPVPGHV TVNICRKYSN PSSCFGEESL AFCEKFSQQL DGRGCFSQLV KTKSFQLKRQ EYEMQLDVNA KIQEEGTGVE ETGKGLTKIT RTITKLSFVN VDTHFRQGIP FVGQVLLVDG RGTPIPYEMI FIGADEANQN INTTTDKNGL ARFSINTDDI MGTSLTVRAK YKDSNVCYGF RWLTEENVEA WHTANAVFSP SRSFVHLESL PYKLRCEQTL AVQAHYILND EAVLERKELV FYYLMMAKGG IVRAGTHVLP VTQGHKKGHF SILISMETDL APVARLVLYT ILPNGEVVGD TVKYEIEKCL ANKVDLVFHP NIGLPATRAF LSVMASPQSL CGLRAVDQSV LLTKPEAELS ASLVYDLLPV KDLTGFPKGV NQQEEDTNGC LKQNDTYING ILYSPVQNTN EEDMYGFLKD MGLKVFTNLN IRKPKVCERL GVNKIPAAYH LVSQGHMDAF LESSESPTET TRSYFPETWI WDLVIVDSTG VAEMEVTVPD TITEWKAGAF CLSNDTGLGL SPVIDFQAFQ PFFVDLTMAY SVIRGEAFTL KATVLNYLQT CIRVGVQLEA SPDFLATPEE KEQKSHCICM NERHTMSWAV IPKSLGNVNF TVSAEALDSK ELCRNEVPVV PERGKKDTII KSLLVEPEGL ENEVTFNSLL CPTGAEVSEQ ISLKLPSDVV EESARASVTV LGDILGSAMQ NTQDLLKMPY GCGEQNMVLF APNIYVLDYL NETEQLTQEI KTKAITYLNT GYQRQLNYKH RDGSYSTFGD KPGRSHANTW LTAFVLKSFA QARRYIFIDE SHITQALTWL SQQQKDNGCF RSSGSLLNNA MKGGVEDEVT LSAYITIALL EMSLPVTHPV VRNALFCLDT AWKSARRGAS GNHVYTKALL AYAFALAGNQ DTKKEILKSL DEEAVKEDNS VHWTRAQKPR VPADLWYQPQ APSAEVEMTA YVLLAYLTTE LVPTREDLTA AMLIVKWLTK QQNSHGGFSS TQDTVVALHA LSKYGAATFT RAKKAAHVTI QSSGAFYTKF QVNNDNQLLL QRVTLPTVPG DYTAKVAGEG CVYLQTSLKY SVLPREKEFP FALVVQTLPG TCEDLKAHTT FQISLNISYI GSRSDSNMAI ADVKMVSGFI PLKPTVKMLE RSVHVSRTEV SNNHVLIYLD KVSNQMLTLF FMVQQDIPVR DLKPAIVKVY DYYEKDEFAV AKYSAPCSAG YGNA // ID A2M_MOUSE Reviewed; 1495 AA. AC Q61838; Q60628; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-FEB-2007, entry version 58. DE Alpha-2-macroglobulin precursor (Pregnancy zone protein) (Alpha-2-M) DE [Contains: Alpha-2-macroglobulin 165 kDa subunit; Alpha-2- DE macroglobulin 35 kDa subunit]. GN Name=A2m; Synonyms=Pzp; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-44 AND RP 1240-1259. RC TISSUE=Liver; RX MEDLINE=93076803; PubMed=1280217; RA van Leuven F., Torrekens S., Overbergh L., Lorent K., de Strooper B., RA van den Berghe H.; RT "The primary sequence and the subunit structure of mouse alpha-2- RT macroglobulin, deduced from protein sequencing of the isolated RT subunits and from molecular cloning of the cDNA."; RL Eur. J. Biochem. 210:319-327(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-161. RC STRAIN=129/J; RX MEDLINE=95095249; PubMed=7528166; RA Umans L., Serneels L., Hilliker C., Stas L., Overbergh L., RA de Strooper B., van Leuven F., van den Berghe H.; RT "Molecular cloning of the mouse gene coding for alpha 2-macroglobulin RT and targeting of the gene in embryonic stem cells."; RL Genomics 22:519-529(1994). RN [3] RP TISSUE SPECIFICITY. RC STRAIN=C57BL/6; TISSUE=Placenta; RX PubMed=15355875; DOI=10.1095/biolreprod.104.029835; RA He H., McCartney D.J., Wei Q., Esadeg S., Zhang J., Foster R.A., RA Hayes M.A., Tayade C., Van Leuven F., Croy B.A.; RT "Characterization of a murine alpha 2 macroglobulin gene expressed in RT reproductive and cardiovascular tissue."; RL Biol. Reprod. 72:266-275(2005). RN [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157; ASN-405; ASN-412; RP ASN-1003; ASN-1385 AND ASN-1443, AND MASS SPECTROMETRY. 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 [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157; ASN-568; ASN-1003; RP ASN-1385 AND ASN-1443, AND MASS SPECTROMETRY. RX 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. 0:0-0(2007). CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a CC unique 'trapping' mechanism. This protein has a peptide stretch, CC called the 'bait region' which contains specific cleavage sites CC for different proteinases. When a proteinase cleaves the bait CC region, a conformational change is induced in the protein which CC traps the proteinase. The entrapped enzyme remains active against CC low molecular weight substrates (activity against high molecular CC weight substrates is greatly reduced). Following cleavage in the CC bait region a thioester bond is hydrolyzed and mediates the CC covalent binding of the protein to the proteinase. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- TISSUE SPECIFICITY: Highest expression in liver, medium expression CC in ovary, heart and stomach. Low expression in lung, kidney and CC uterus. Protein found in plasma. CC -!- DEVELOPMENTAL STAGE: Contrary to the rat protein, which is an CC acute phase protein, this protein is always present at high levels CC in circulation. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M93264; AAA39508.1; -; mRNA. DR EMBL; U06977; AAA87890.1; -; Genomic_DNA. DR PIR; S27001; S27001. DR UniGene; Mm.260144; -. DR HSSP; Q63332; 1EDY. DR SMR; Q61838; 1357-1490. DR MEROPS; I39.001; -. DR Ensembl; ENSMUSG00000030359; Mus musculus. DR KEGG; mmu:11287; -. DR MGI; MGI:87854; Pzp. DR ArrayExpress; Q61838; -. DR GermOnline; ENSMUSG00000030359; Mus musculus. DR GO; GO:0004866; F:endopeptidase inhibitor activity; NAS:UniProtKB. DR InterPro; IPR011626; A2M_comp. DR InterPro; IPR002890; A2M_N. DR InterPro; IPR011625; A2M_N_2. DR InterPro; IPR011627; A2M_rcpt. DR InterPro; IPR009048; AMG_rcpt_bd. DR InterPro; IPR001599; MacrogloblnA2. DR InterPro; IPR008930; Terp_cyc_toroid. DR Pfam; PF00207; A2M; 1. DR Pfam; PF07678; A2M_comp; 1. DR Pfam; PF01835; A2M_N; 1. DR Pfam; PF07703; A2M_N_2; 1. DR Pfam; PF07677; A2M_recep; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. KW Bait region; Direct protein sequencing; Glycoprotein; KW Protease inhibitor; Serine protease inhibitor; Signal; Thioester bond. FT SIGNAL 1 24 Potential. FT CHAIN 25 1239 Alpha-2-macroglobulin 165 kDa subunit. FT /FTId=PRO_0000000056. FT CHAIN 1240 1495 Alpha-2-macroglobulin 35 kDa subunit. FT /FTId=PRO_0000000057. FT REGION 686 744 Bait region. FT CARBOHYD 55 55 N-linked (GlcNAc...) (Potential). FT CARBOHYD 157 157 N-linked (GlcNAc...). FT CARBOHYD 382 382 N-linked (GlcNAc...) (Potential). FT CARBOHYD 405 405 N-linked (GlcNAc...). FT CARBOHYD 412 412 N-linked (GlcNAc...). FT CARBOHYD 568 568 N-linked (GlcNAc...). FT CARBOHYD 881 881 N-linked (GlcNAc...) (Potential). FT CARBOHYD 942 942 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1003 1003 N-linked (GlcNAc...). FT CARBOHYD 1385 1385 N-linked (GlcNAc...). FT CARBOHYD 1443 1443 N-linked (GlcNAc...). FT DISULFID 48 86 By similarity. FT DISULFID 249 298 By similarity. FT DISULFID 267 286 By similarity. FT DISULFID 277 277 Interchain (with C-430) (By similarity). FT DISULFID 430 430 Interchain (with C-277) (By similarity). FT DISULFID 469 562 By similarity. FT DISULFID 594 783 By similarity. FT DISULFID 642 689 By similarity. FT DISULFID 833 861 By similarity. FT DISULFID 859 895 By similarity. FT DISULFID 933 1339 By similarity. FT DISULFID 1092 1140 By similarity. FT CROSSLNK 984 987 Isoglutamyl cysteine thioester (Cys-Gln) FT (By similarity). FT CONFLICT 41 47 QESLKRP -> SGIPEKA (in Ref. 2). FT CONFLICT 91 91 I -> V (in Ref. 2). FT CONFLICT 142 144 VKF -> GII (in Ref. 2). FT CONFLICT 160 161 FP -> VS (in Ref. 2). SQ SEQUENCE 1495 AA; 165828 MW; 0D215688E80B4CCB CRC64; MRRNQLPTPA FLLLFLLLPR DATTATAKPQ YVVLVPSEVY QESLKRPCVS LNHVNETVML SLTLEYAMQQ TKLLTDQAVD KDSFYCSPFT ISGSPLPYTF ITVEIKGPTQ RFIKKKSIQI IKAESPVFVQ TDKPIYKPGQ IVKFRVVSVD ISFRPLNETF PVVYIETPKR NRIFQWQNIH LAGGLHQLSF PLSVEPALGI YKVVVQKDSG KKIEHSFEVK EYVLPKFEVI IKMQKTMAFL EEELPITACG VYTYGKPVPG LVTLRVCRKY SRYRSTCHNQ NSMSICAEFS QQADDKGCFS QVVKTKVFQL SQKGHDMKIE VEAKIKEEGT GIELTGIGSC EIANALSKLK FTKVNTNYRP GLPFSGQVLL VDEKGKPIPN KNITSVVSPL GYLSIFTTDE HGLANISIDT SNFTAPFLRV VVTYKQNHVC YDNWWLDEFH TQADHSATLV FSPSQSYIQL ELVFGTLACG QTQEIRIHYL LNEDIMKNEK TLTFYYLIKA RGSIGNLGSH VLSLEQGNMK GVFSLPIQVE PGMAPEAQLL IYAILPNEEL VADAQNFEIE KCFANKVNLS FPSAQSLPAS DTHLKVKAAP LSLCALTAVD QSVLLLKPEA KLSPQSIYNL LPGKTVQGAF FGVPVYKDHE NCISGEDITH NGIVYTPKHS LGDNDAHSIF QSVGINIFTN SKIHKPRFCQ EFQHYPAMGG VAPQALAVAA SGPGSSFRAM GVPMMGLDYS DEINQVVEVR ETVRKYFPET WIWDLVPLDV SGDGELAVKV PDTITEWKAS AFCLSGTTGL GSSSTISLQA FQPFFLELTL PYSVVRGEAF TLKATVLNYM SHCIQIRVDL EISPDFLAVP VGGHENSHCI CGNERKTVSW AVTPKSLGEV NFTRTAEALE SQELCGNKLT EVPALVHKDT VVKSVIVEPE GIEKEQTYNT LLCPQDTELQ DNSSLELPPN VVEGSARATH SVLGDILGSA MQNLQNLLQM PYGCGEQNMV LFVPNIYVLN YLNETQQLTE AIKSKAINYL ISGYQRQLNY QHSDGSYSTF GNHGGGNTPG NTWLTAFVLK AFAQAQSHIF IEKTHITNAF NWLSMKQKEN GCFQQSGYLL NNAMKGGVDD EVTLSAYITI ALLEMPLPVT HSAVRNALFC LETAWASISQ SQESHVYTKA LLAYAFALAG NKAKRSELLE SLNKDAVKEE DSLHWQRPGD VQKVKALSFY QPRAPSAEVE MTAYVLLAYL TSESSRPTRD LSSSDLSTAS KIVKWISKQQ NSDGGLLLTQ DTVVALQALS KYGSATFTRS QKEVLVTSRS SGTFSKTFHV NSGNRLLLQE VRLPDLPGNY VTKGSGSGCV YLQTSLKYNI LPVADGKAPF ALQVNTLPLN FDKAEDHRTF QIRINVSYTG ERPSSNMVIV DVKMVSGFIP MKPSVKRLQD QPNIQRTEVN TNHVLIYIEK LTNQTLGFSF AVEQDIPVKN LKPAPIKVYD YYETDEFTVE EYSAPFSDGS EQGNA // ID A2M_OCTVU Reviewed; 18 AA. AC P30800; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 31-OCT-2006, entry version 41. DE Alpha-2-macroglobulin homolog (Alpha-2-M) (Fragment). OS Octopus vulgaris (Octopus). OC Eukaryota; Metazoa; Mollusca; Cephalopoda; Coleoidea; Neocoleoidea; OC Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus. OX NCBI_TaxID=6645; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=92344633; PubMed=1379044; RA Thoegersen I.B., Salvesen G., Brucato F.H., Pizzo S.V., Enghild J.J.; RT "Purification and characterization of an alpha-macroglobulin RT proteinase inhibitor from the mollusc Octopus vulgaris."; RL Biochem. J. 285:521-527(1992). CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a CC unique 'trapping' mechanism. This protein has a peptide stretch, CC called the 'bait region' which contains specific cleavage sites CC for different proteinases. When a proteinase cleaves the bait CC region, a conformational change is induced in the protein which CC traps the proteinase. The entrapped enzyme remains active against CC low molecular weight substrates (activity against high molecular CC weight substrates is greatly reduced). Following cleavage in the CC bait region a thioester bond is hydrolyzed and mediates the CC covalent binding of the protein to the proteinase. CC -!- SUBUNIT: Homodimer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S23971; S23971. DR GO; GO:0004866; F:endopeptidase inhibitor activity; NAS:UniProtKB. DR InterPro; IPR001599; MacrogloblnA2. DR InterPro; IPR008930; Terp_cyc_toroid. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. KW Bait region; Direct protein sequencing; Protease inhibitor; KW Serine protease inhibitor; Thioester bond. FT CHAIN <1 >18 Alpha-2-macroglobulin homolog. FT /FTId=PRO_0000093792. FT CROSSLNK 5 8 Isoglutamyl cysteine thioester (Cys-Gln). FT NON_TER 1 1 FT NON_TER 18 18 SQ SEQUENCE 18 AA; 2011 MW; D8D61C473D901C9D CRC64; KPSGCGEQNM INFYPNVL // ID A32CD_DROME Reviewed; 329 AA. AC O46203; O46225; Q8T4D3; Q9TY45; Q9VKL2; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 23-JAN-2007, entry version 50. DE Accessory gland protein Acp32CD precursor. GN Name=Acp32CD; ORFNames=CG4605; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; DOI=10.1016/S0965-1748(97)00056-8; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Testis; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP NUCLEOTIDE SEQUENCE OF 24-289. RC STRAIN=7, WS1, WS12, WS16, WS17, WS19, WS26, WS47, WS9, Zim10, Zim22, RC Zim24, Zim30, Zim32, Zim35, and Zim5; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). CC -!- FUNCTION: Responsible for physiological and behavioral changes in CC mated female flies. CC -!- SUBCELLULAR LOCATION: Secreted protein (Probable). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; CC IsoId=O46203-1; Sequence=Displayed; CC Name=Short; CC IsoId=O46203-2; Sequence=VSP_018775; CC -!- TISSUE SPECIFICITY: Seminal fluid. CC -!- CAUTION: Ref.2 (AAF53055) sequence differs from that shown due to CC several frameshifts. CC -!- CAUTION: Ref.4 (AAL89983) sequence differs from that shown due to CC several frameshifts. CC -!- CAUTION: Could be the product of a pseudogene in strain Berkeley. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U85764; AAB96388.1; -; Genomic_DNA. DR EMBL; U85764; AAB96389.1; -; Genomic_DNA. DR EMBL; U90948; AAB96395.1; -; mRNA. DR EMBL; AE014134; AAF53055.2; ALT_FRAME; Genomic_DNA. DR EMBL; AY089245; AAL89983.1; ALT_FRAME; mRNA. DR EMBL; AY010544; AAG32576.1; -; Genomic_DNA. DR EMBL; AY010545; AAG32577.2; -; Genomic_DNA. DR EMBL; AY010546; AAG32578.1; -; Genomic_DNA. DR EMBL; AY010547; AAG32579.1; -; Genomic_DNA. DR EMBL; AY010548; AAG32580.1; -; Genomic_DNA. DR EMBL; AY010549; AAG32581.2; -; Genomic_DNA. DR EMBL; AY010550; AAG32582.1; -; Genomic_DNA. DR EMBL; AY010551; AAG32583.1; -; Genomic_DNA. DR EMBL; AY010552; AAG32584.1; -; Genomic_DNA. DR EMBL; AY010553; AAG32585.1; -; Genomic_DNA. DR EMBL; AY010554; AAG32586.1; -; Genomic_DNA. DR EMBL; AY010555; AAG32587.1; -; Genomic_DNA. DR EMBL; AY010556; AAG32588.1; -; Genomic_DNA. DR EMBL; AY010557; AAG32589.1; -; Genomic_DNA. DR EMBL; AY010558; AAG32590.1; -; Genomic_DNA. DR EMBL; AY010559; AAG32591.1; -; Genomic_DNA. DR UniGene; Dm.4870; -. DR KEGG; dme:Dmel_CG4605; -. DR FlyBase; FBgn0023415; Acp32CD. DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB. DR GO; GO:0005179; F:hormone activity; NAS:UniProtKB. DR GO; GO:0045434; P:negative regulation of female receptivity, ...; NAS:UniProtKB. KW Alternative initiation; Behavior; Complete proteome; Polymorphism; KW Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 329 Accessory gland protein Acp32CD. FT /FTId=PRO_0000020580. FT COMPBIAS 100 182 Gly-rich. FT COMPBIAS 200 326 Arg-rich. FT VAR_SEQ 1 88 Missing (in isoform Short). FT /FTId=VSP_018775. FT VARIANT 45 45 D -> E (in strain: WS1, WS9, WS16, Zim5, FT Zim10, Zim24, Zim30, Zim32 and Zim35). FT VARIANT 52 52 A -> D (in strain: 7, WS1, WS12, WS16, FT WS17, Zim10, Zim22, Zim32 and Zim35). FT VARIANT 63 63 A -> T (in strain: 7, WS1, WS9, WS16, FT WS17 and Zim10). FT VARIANT 69 69 L -> P (in strain: WS9 and WS19). FT VARIANT 273 275 TRM -> PRT (in strain: WS9, Zim30 and FT Zim22). FT VARIANT 275 275 M -> T (in strain: WS12, WS17 and WS26). SQ SEQUENCE 329 AA; 35557 MW; 5655CCA73759CFEA CRC64; MPPLLRHCFG HAFIGLPLFN GQEQPRPQSN RFDSGQRRSS LYIRDGRTAR AAQRCSDVAD ADAATHWLLG PVALGQLPEH GALGQKYYMN FAFNNNNPDG EGGTGVDGGG GGAGGGAAGP GGGTGDSPHS QEGDGSAATD NPNDDHATSA DNSLATDGDA IGKKESGGGS DGKSDSKDSS GGNDATPANG HDDDNDDSDR RMPRIDKIRK RRPDRRGSAP ITAITVATRS DRRQLWRAVR AVHLREQREP RTFGSNAGSN QRTMEPVRAV RRTRMPRKWP AKRLLNGQAT CQMDPKLEPR KMTTRRCNTT GRSDHRFARG TLEERRHFN // ID A33A_DROME Reviewed; 47 AA. AC O46227; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 23-JAN-2007, entry version 42. DE Accessory gland peptide Acp33A precursor. GN Name=Acp33A; ORFNames=CG6555; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; DOI=10.1016/S0965-1748(97)00056-8; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE OF 11-47. RC STRAIN=WS1, WS16, WS17, WS19, WS26, WS47, WS49, WS9, ZIM10C, ZIM22C, RC ZIM24C, ZIM30C, ZIM32C, ZIM35C, ZIM49C, ZIM5C, and ZIM7C; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). CC -!- FUNCTION: Responsible for physiological and behavioral changes in CC mated female flies. CC -!- SUBCELLULAR LOCATION: Secreted protein (Probable). CC -!- TISSUE SPECIFICITY: Main cells of accessory gland and seminal CC fluid. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U90950; AAB96397.1; -; mRNA. DR EMBL; AE014134; AAF53108.2; -; Genomic_DNA. DR EMBL; AY010560; AAG32771.1; -; Genomic_DNA. DR EMBL; AY010561; AAG32772.1; -; Genomic_DNA. DR EMBL; AY010562; AAG32773.1; -; Genomic_DNA. DR EMBL; AY010563; AAG32774.1; -; Genomic_DNA. DR EMBL; AY010564; AAG32775.1; -; Genomic_DNA. DR EMBL; AY010565; AAG32776.1; -; Genomic_DNA. DR EMBL; AY010566; AAG32777.1; -; Genomic_DNA. DR EMBL; AY010567; AAG32778.1; -; Genomic_DNA. DR EMBL; AY010568; AAG32779.1; -; Genomic_DNA. DR EMBL; AY010569; AAG32780.1; -; Genomic_DNA. DR EMBL; AY010570; AAG32781.1; -; Genomic_DNA. DR EMBL; AY010571; AAG32782.1; -; Genomic_DNA. DR EMBL; AY010572; AAG32783.1; -; Genomic_DNA. DR EMBL; AY010573; AAG32784.1; -; Genomic_DNA. DR EMBL; AY010574; AAG32785.1; -; Genomic_DNA. DR EMBL; AY010575; AAG32786.1; -; Genomic_DNA. DR EMBL; AY010576; AAG32787.1; -; Genomic_DNA. DR UniGene; Dm.12779; -. DR Ensembl; CG32952; Drosophila melanogaster. DR KEGG; dme:Dmel_CG6555; -. DR FlyBase; FBgn0032367; CG6555. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-008571-MONOMER; -. DR GermOnline; CG6555; Drosophila melanogaster. DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB. DR GO; GO:0005179; F:hormone activity; NAS:UniProtKB. DR GO; GO:0045434; P:negative regulation of female receptivity, ...; NAS:UniProtKB. KW Behavior; Complete proteome; Polymorphism; Signal. FT SIGNAL 1 21 Potential. FT PEPTIDE 22 47 Accessory gland peptide Acp33A. FT /FTId=PRO_0000020582. FT VARIANT 44 47 PCCM -> RVACK (in strain: ZIM30C). SQ SEQUENCE 47 AA; 5282 MW; 8AF0CCFA95797328 CRC64; MLPSKRVPFL FTIILFLAGL GQHTTESVLP DCVLYPRCLI TKDPCCM // ID A33_PLEWA Reviewed; 625 AA. AC Q02084; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 09-JAN-2007, entry version 46. DE Zinc-binding protein A33. OS Pleurodeles waltlii (Iberian ribbed newt). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Caudata; Salamandroidea; Salamandridae; OC Pleurodeles. OX NCBI_TaxID=8319; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL RP STAGE. RC TISSUE=Ovary; RX MEDLINE=93154311; PubMed=7679068; RA Bellini M., Lacroix J.-C., Gall J.G.; RT "A putative zinc-binding protein on lampbrush chromosome loops."; RL EMBO J. 12:107-114(1993). RN [2] RP SEQUENCE REVISION TO 15-60 AND 427-429. RA Bellini M., Lacroix J.-C., Gall J.G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION, SUBCELLULAR LOCATION, ZINC-BINDING, AND MUTAGENESIS OF RP CYS-178; CYS-202 AND HIS-267. RX PubMed=7593179; DOI=10.1083/jcb.131.3.563; RA Bellini M., Lacroix J.-C., Gall J.G.; RT "A zinc-binding domain is required for targeting the maternal nuclear RT protein PwA33 to lampbrush chromosome loops."; RL J. Cell Biol. 131:563-570(1995). CC -!- FUNCTION: May be a nuclear regulatory protein that is stored in CC the germinal vesicle for use during early embryogenesis and may CC play a role in the synthesis or processing of pre-mRNA during CC oogenesis. Binds 3 Zn(2+) ions. CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Lampbrush chromosome loops and CC in some nucleoplasmic particles of the germinal vesicle. CC -!- DEVELOPMENTAL STAGE: It first appears on the chromosome loops and CC in the nucleoplasm of the germinal vesicle (GV). It is transmitted CC to the egg at GV breakdown and appears in embryonic nuclei at the CC mid-blastula stage and is found in many but not all nuclei at CC still later stages of embryogenesis. CC -!- DOMAIN: B box-type zinc binding domain is required for targeting CC this protein to lampbrush chromosome loops and for normal CC functioning of this protein in the oocyte. CC -!- SIMILARITY: Contains 1 B box-type zinc finger. CC -!- SIMILARITY: Contains 1 B30.2/SPRY domain. CC -!- SIMILARITY: Contains 1 RING-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; L04190; AAA49614.2; -; mRNA. DR PIR; S28418; S28418. DR HSSP; Q92021; 1FRE. DR InterPro; IPR001870; B302. DR InterPro; IPR003649; Bbox_C. DR InterPro; IPR003879; Butyrophylin. DR InterPro; IPR000953; Chromo. DR InterPro; IPR006574; PRY. DR InterPro; IPR003877; SPRY_rcpt. DR InterPro; IPR000315; Znf_Bbox. DR InterPro; IPR001841; Znf_RING. DR Pfam; PF00622; SPRY; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR PRINTS; PR01406; BBOXZNFINGER. DR PRINTS; PR01407; BUTYPHLNCDUF. DR SMART; SM00502; BBC; 1. DR SMART; SM00336; BBOX; 1. DR SMART; SM00298; CHROMO; 1. DR SMART; SM00589; PRY; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00449; SPRY; 1. DR PROSITE; PS50188; B302_SPRY; 1. DR PROSITE; PS50119; ZF_BBOX; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Coiled coil; Developmental protein; Metal-binding; Nuclear protein; KW RNA-binding; Zinc; Zinc-finger. FT CHAIN 1 625 Zinc-binding protein A33. FT /FTId=PRO_0000055746. FT DOMAIN 429 625 B30.2/SPRY. FT ZN_FING 163 203 RING-type. FT ZN_FING 234 275 B box-type. FT COILED 337 386 FT MUTAGEN 178 178 C->F: No effect on intranuclear FT localization. FT MUTAGEN 202 202 C->F: No effect on intranuclear FT localization. FT MUTAGEN 267 267 H->N: No Zn(2+) binding. Inhibits the FT targeting to lampbrush chromosome loops FT and to nucleoplasmic particles. SQ SEQUENCE 625 AA; 71053 MW; BCE8003BB6BF5B13 CRC64; MANSTVAEPE KMEQSGTCEE DEEEENMEGD EDECDDDEEE NMEPAETVTI GSTYKCRRSD NTLHAAEIIK TRKTKENAEE FYVHYVGLNR RQNEWVDKSR VLQAKQIKTE ELNNTEDETN GVSDQSEGKA ARSNKRKIED GDGDQKKRKV DDEEDDFTED LTCPLCRSLF KEPVILECGH NFCKHCIDKS WESASAFSCP ECKEVLTERK YTTNRVLANL VKKAAVGVKD KDVKPKEKCD EHDERLKLFC KDDGTLACVI CRDSLKHSNH NFLPIQDAVG VYRDQLIALV SPLETTMKEN QKLKCDQSQK ISLHRENIVD CKKHIECEFE KLHQFLREKE AKMVEDLNAE REGLLKDMEA NLVKMTDNCE FIEEAISTTQ SRLNESDPIA FLTDIKSFIE KCCEEHRKGV PAESVLVNKE LSQGRFKGPL QYIIWKELKS VVQPGLAPLT LDPNTAHPNL VLSEGLTSVK YTDTKQQLPD NPKRFSQCIL VLGAEGFDSG KHYWEVEVGN KTAWDVGMAS ESSNRKGKIK LNPKNGYWAI WLRNGNAFKA LESPSKTLNL TSKPSKIGVY LDYEGGQVSF YNADDMSPIY TFNGSFTEKL YPYLSPFLQD SGKNAEPLKL VHTKL // ID A36A_DROME Reviewed; 292 AA. AC Q9NK57; Q9VJL4; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 3. DT 23-JAN-2007, entry version 42. DE Protein anon-35F/36A. GN Name=anon-35F/36A; ORFNames=CG4278; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=99403001; PubMed=10471707; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., RA Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., RA Martin C., Moshrefi A.R., Palazzolo M., Reese M.G., Spradling A.C., RA Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-170000, EBI-170000; CC -!- SIMILARITY: Belongs to the UPF0135 (NIF3) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014134; AAF53525.2; -; Genomic_DNA. DR EMBL; AY069556; AAL39701.2; ALT_INIT; mRNA. DR UniGene; Dm.8784; -. DR DIP; DIP:23705N; -. DR IntAct; Q9NK57; -. DR Ensembl; CG4278; Drosophila melanogaster. DR KEGG; dme:Dmel_CG4278; -. DR FlyBase; FBgn0014092; CG4278. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-009140-MONOMER; -. DR GermOnline; CG4278; Drosophila melanogaster. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR InterPro; IPR002678; interacting_NIF3. DR Pfam; PF01784; NIF3; 1. DR TIGRFAMs; TIGR00486; DUF34; 1. KW Complete proteome. FT CHAIN 1 292 Protein anon-35F/36A. FT /FTId=PRO_0000147352. SQ SEQUENCE 292 AA; 32363 MW; 775D27E7721150CC CRC64; MLRRMNTFSG QKLAAVVKEL ENFAPTSWAE KWDNVGLLIE PHREKQIKKI LLTNDLTEPV VKEALEKEAE LIISYHPPIF KPLTRITQSH WKERVVAACL ANDIALYSPH TAWDKKSGGV NDWLSKAVNI ISIRPLEPEL GAPPGTGSGR YIETKMELSQ VVESLQKRIR NSVHVALAVG HTPKTLIQSV GICAGSGASL LKGIQADLII TGEMSHHEVL EFTHNNTTVL LCNHSNSERG FLHEFCPILA KSLNEECLVF VSEVDKDPLV TVASDINKEL SAFVDVYKST SK // ID A36DE_DROME Reviewed; 912 AA. AC Q9V3R1; O46198; Q9U9Y5; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 20-FEB-2007, entry version 46. DE Accessory gland protein Acp36DE precursor. GN Name=Acp36DE; ORFNames=CG7157; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Canton-S; TISSUE=Male accessory gland; RX MEDLINE=98135120; PubMed=9474779; DOI=10.1016/S0965-1748(97)00056-8; RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RT "New genes for male accessory gland proteins in Drosophila RT melanogaster."; RL Insect Biochem. Mol. Biol. 27:825-834(1997). RN [2] RP SEQUENCE REVISION TO N-TERMINUS AND C-TERMINUS. RA Wolfner M.F., Harada H.A., Bertram M.J., Stelick T.J., Kraus K.W., RA Kalb J.M., Lung Y.O., Neubaum D.M., Park M., Tram U.K.; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP NUCLEOTIDE SEQUENCE OF 144-889. RC STRAIN=SENGWA2, SENGWA22, SENGWA29, SENGWA30, SENGWA32, SENGWA37, RC SENGWA51, WSII1, WSII12, WSII16, WSII19, WSII26, WSII47, WSII49, RC WSII6, and WSII9; RX MEDLINE=20556153; PubMed=11102381; RA Begun D.J., Whitley P., Todd B.L., Waldrip-Dail H.M., Clark A.G.; RT "Molecular population genetics of male accessory gland proteins in RT Drosophila."; RL Genetics 156:1879-1888(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 401-912. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=20196012; PubMed=10731138; DOI=10.1126/science.287.5461.2222; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [8] RP FUNCTION. RX PubMed=12939382; DOI=10.1242/jeb.00585; RA Bloch-Qazi M.C., Wolfner M.F.; RT "An early role for the Drosophila melanogaster male seminal protein RT Acp36DE in female sperm storage."; RL J. Exp. Biol. 206:3521-3528(2003). CC -!- FUNCTION: Responsible for physiological and behavioral changes in CC mated female flies. Associates with sperm and localizes to CC specific regions of the female reproductive tract, including the CC sperm storage organs. It accelerates sperm accumulation into CC storage but does not mediate the entry of the first sperm into CC storage. Once sperm storage has initiated it seems to acts as a CC guidance factor helping subsequent sperm move into storage, a CC corral concentrating sperm around the SSO entrances and/or a CC trigger for responses within the female that accelerate storage of CC sperm. CC -!- SUBCELLULAR LOCATION: Secreted protein (Probable). CC -!- TISSUE SPECIFICITY: Main cells of accessory gland and seminal CC fluid. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U85759; AAB96383.2; -; mRNA. DR EMBL; AF157488; AAD40185.1; -; Genomic_DNA. DR EMBL; AE014134; AAF53664.1; -; Genomic_DNA. DR EMBL; AY113344; AAM29349.1; -; mRNA. DR EMBL; AY010577; AAG37359.1; -; Genomic_DNA. DR EMBL; AY010578; AAG37360.1; -; Genomic_DNA. DR EMBL; AY010579; AAG37361.1; -; Genomic_DNA. DR EMBL; AY010580; AAG37362.1; -; Genomic_DNA. DR EMBL; AY010581; AAG37363.1; -; Genomic_DNA. DR EMBL; AY010582; AAG37364.1; -; Genomic_DNA. DR EMBL; AY010583; AAG37365.1; -; Genomic_DNA. DR EMBL; AY010584; AAG37366.1; -; Genomic_DNA. DR EMBL; AY010585; AAG37367.1; -; Genomic_DNA. DR EMBL; AY010586; AAG37368.1; -; Genomic_DNA. DR EMBL; AY010587; AAG37369.1; -; Genomic_DNA. DR EMBL; AY010588; AAG37370.1; -; Genomic_DNA. DR EMBL; AY010589; AAG37371.1; -; Genomic_DNA. DR EMBL; AY010590; AAG37372.1; -; Genomic_DNA. DR EMBL; AY010591; AAG37373.1; -; Genomic_DNA. DR EMBL; AY010592; AAG37374.1; -; Genomic_DNA. DR EMBL; AF145666; AAD38641.1; -; mRNA. DR UniGene; Dm.29426; -. DR DIP; DIP:24017N; -. DR Ensembl; CG7157; Drosophila melanogaster. DR KEGG; dme:Dmel_CG7157; -. DR FlyBase; FBgn0011559; Acp36DE. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-009343-MONOMER; -. DR GermOnline; CG7157; Drosophila melanogaster. DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB. DR GO; GO:0005179; F:hormone activity; NAS:UniProtKB. DR GO; GO:0042628; P:mating plug formation; TAS:FlyBase. DR GO; GO:0045434; P:negative regulation of female receptivity, ...; NAS:UniProtKB. DR GO; GO:0046693; P:sperm storage; IMP:FlyBase. KW Behavior; Complete proteome; Polymorphism; Signal. FT SIGNAL 1 23 Potential. FT CHAIN 24 912 Accessory gland protein Acp36DE. FT /FTId=PRO_0000020583. FT COMPBIAS 183 897 Gln/Ser-rich. FT VARIANT 148 148 N -> S (in strain: WSII16). FT VARIANT 190 190 A -> V (in strain: WSII16). FT VARIANT 198 198 T -> S (in strain: SENGWA2, SENGWA22, FT SENGWA29, SENGWA32, SENGWA37, SENGWA51, FT WSII19 and WSII49). FT VARIANT 223 223 Missing (in strain: SENGWA22). FT VARIANT 231 231 E -> G (in strain: WSII6). FT VARIANT 253 253 Q -> QSQ (in strain: SENGWA2, SENGWA29, FT SENGWA32, SENGWA51, WSII19 and WSII49). FT VARIANT 307 307 E -> G (in strain: WSII6). FT VARIANT 316 316 I -> F (in strain: WSII16). FT VARIANT 325 325 K -> T (in strain: SENGWA37). FT VARIANT 335 335 S -> P (in strain: SENGWA30). FT VARIANT 352 352 Q -> QLLREAQQK (in strain: SENGWA2, FT SENGWA22, SENGWA29, SENGWA30, SENGWA32, FT SENGWA37, SENGWA51, WSII16, WSII19 and FT WSII49). FT VARIANT 385 385 F -> HQN (in strain: WSII1). FT VARIANT 430 430 V -> I (in strain: WSII16). FT VARIANT 464 464 L -> F (in strain: Canton-S, SENGWA2, FT SENGWA22, SENGWA29, SENGWA32 and FT SENGWA51). FT VARIANT 496 496 E -> G (in strain: WSII6). FT VARIANT 507 507 L -> V (in strain: SENGWA22, SENGWA29, FT SENGWA37 and SENGWA51). FT VARIANT 575 575 L -> Q (in strain: WSII16). FT VARIANT 601 601 S -> I (in strain: WSII26 and WSII49). FT VARIANT 613 613 E -> K (in strain: SENGWA30). FT VARIANT 650 650 P -> A (in strain: SENGWA22, SENGWA30 and FT WSII16). FT VARIANT 666 666 L -> V (in strain: SENGWA29, SENGWA30, FT SENGWA37 and SENGWA51). FT VARIANT 670 670 G -> E (in strain: SENGWA29, SENGWA30, FT SENGWA37 and SENGWA51). FT VARIANT 758 758 T -> A (in strain: SENGWA37 and FT SENGWA51). FT VARIANT 782 786 Missing (in strain: SENGWA37 and FT SENGWA51). FT VARIANT 830 830 Q -> E (in strain: WSII26). FT VARIANT 844 844 Q -> R (in strain: WSII16). SQ SEQUENCE 912 AA; 101921 MW; 81E2C53431EAFBC5 CRC64; MWTLTCQQFI ALILLGTLVP SESFLCKHCF RKNLEKVHES FRDILSPPIF GVNPQPLIEV QQPKVTPKPE SSQVIHVHQP QVILKPIYYP KVDTISTKNQ IGIHGPYSQY PSLLPSANLL GIPNQQLINA QDVLSDKDQK QTQVQNNNLH IRFGVSALRE GRNNPSLETI SRDKVDKISP ALQLQLLRYA DSQSQSQTQS QSASQSESNA SSQFQAQEQS NRLLENPPVS ESQSQSESQS QSESQKQSQS QSQRQQQIQT QLQILRQLQQ KSNEQSAAQS ASQIQSQRQS DSQSNLQLQE QSQSQSEQGK PIQSQIQILQ GLQQKELDDK SASQSQSESK TRQEQQKQLN LQQLEELSSS LSQSRLGLGQ QIQSQLQKNQ LDKQFASQFQ SQSKSQLEQQ MQLQLQSLRQ LQQKQLDEQS ASQSQPQSQV AQQIQSHLQL LRLLQSRLKT QSALKSDLEQ QILLQLKKLT EVQQKQLAEQ PTLRPSSKSQ SPGQLEQQIL LQLQNLLQFQ QNQLKSDTQT QSQLQESKSN SLSQSQSQSQ EQLQLQRDQN LRQLEQIKLE MQNIRELLQK GKSELQTQSD SQRRIHELYQ NILQLNKEKL SYQLKQLKLK ELEDQKKSQA EISKGSNPSN LFIIGQLPSE GKPAPGNQGP SIEPKLVPQP GSLDKLPSGG GLIGKPASTG LYILSPDFND LSDYRDQFRL QQELKKHQNI LSLLQRRQND IKKQQNAQLL LGQQQKEQQA QESINKQQSS SAGSSSQTKL QQDIQSTGAQ GSQQGLQAGS TGLQTSSLQG TESSASQSAA LQRLKEQEQL RIQTENDQKT SSSSSHSNSQ NSQSSSSQSS QASQSEAQRQ EAGNRNTLLL DQSSSKTQSE SKSESSSQSS SHSSSQSTSN SSSNVQSKLQ GESQALLNNL SG // ID A37C_DROLE Reviewed; 544 AA. AC O96570; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 31-OCT-2006, entry version 27. DE Protein anon-37Cs. GN Name=anon-37Cs; Synonyms=Cs; ORFNames=CG10561; OS Drosophila lebanonensis (Fruit fly) (Scaptodrosophila lebanonensis). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Scaptodrosophila. OX NCBI_TaxID=7225; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Beirut; RX MEDLINE=99250256; PubMed=10231575; DOI=10.1016/S0378-1119(99)00096-7; RA Tatarenkov A., Saez A.G., Ayala F.J.; RT "A compact gene cluster in Drosophila: the unrelated Cs gene is RT compressed between duplicated amd and Ddc."; RL Gene 231:111-120(1999). CC -!- FUNCTION: Has a non-vital function (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; AF091329; AAC67584.1; -; Genomic_DNA. DR FlyBase; FBgn0025668; Dleb\CG10561. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR InterPro; IPR002937; Amino_oxidase. DR Pfam; PF01593; Amino_oxidase; 1. FT CHAIN 1 544 Protein anon-37Cs. FT /FTId=PRO_0000064403. SQ SEQUENCE 544 AA; 61027 MW; CF003E2CBB7D6DBE CRC64; MVHPQLKRSI ESLSFSGYKL TRRNLYNAPA LKVMGRSVNN SSSNNNDQQQ YNLESAKQNT QIVVIGAGLA GLSAAQHLLR HGFRSTIVLE ATDRYGGRVN SKRFGDTYCE LGAKWVNMNI DGAHNTIYEL LRNAEGLRKQ LKQRECANYV HTQGREVPPN MVELIDMQFR QLCRGFKVSE KVKSGGDLHV LDNVMAYFKT ESEKLVGHSY PDPEKRALAR EIFQSLFKEF SSILGCCLEY VNIEHITSCP VQQELRPLYV PTGLDNVLDT LTQHISKEQL QTGKPVGSIQ WQTLSDFGAP TSPLPQERKC VACLDGTLYS ADHIICTLPL GVLKNFSAIL FKPALPLEKL QAIRNLGYGN PVKIYLAYKR PISRWLKSNL RPLGAQLGKD EPAITVNGRQ ERLWTQQVVE ISQLPSSQHV LEIRVGGGYY DEIEKLPDVT LLEQITALLR QCLRNRLVPY PQALLRSNWS TSACYLGGRP YFSTTSSARD VQRLAEPLGD IAPTLLFAGD ATALKGFGTI DGARTSGIRE AQRIIDYYYL KQYM // ID A37C_DROME Reviewed; 504 AA. AC P18487; O18376; O18377; O18378; O96568; Q95TY1; Q9VIZ7; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 15-AUG-2003, sequence version 3. DT 23-JAN-2007, entry version 66. DE Protein anon-37Cs. GN Name=anon-37Cs; Synonyms=cs, l(2)37Cs; ORFNames=CG10561; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=St. Lucia; RX MEDLINE=99250256; PubMed=10231575; DOI=10.1016/S0378-1119(99)00096-7; RA Tatarenkov A., Saez A.G., Ayala F.J.; RT "A compact gene cluster in Drosophila: the unrelated Cs gene is RT compressed between duplicated amd and Ddc."; RL Gene 231:111-120(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88038375; PubMed=3478553; DOI=10.1007/BF00329656; RA Eveleth D.D., Marsh J.L.; RT "Overlapping transcription units in Drosophila: sequence and structure RT of the Cs gene."; RL Mol. Gen. Genet. 209:290-298(1987). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX MEDLINE=86284963; PubMed=2874495; DOI=10.1038/322279a0; RA Spencer C.A., Gietz R.D., Hodgetts R.B.; RT "Overlapping transcription units in the dopa decarboxylase region of RT Drosophila."; RL Nature 322:279-281(1986). RN [7] RP DEVELOPMENTAL STAGE. RX MEDLINE=86165362; PubMed=3007242; RA Spencer C.A., Gietz R.D., Hodgetts R.B.; RT "Analysis of the transcription unit adjacent to the 3'-end of the dopa RT decarboxylase gene in Drosophila melanogaster."; RL Dev. Biol. 114:260-264(1986). CC -!- FUNCTION: Has a non-vital function. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Low levels seen in adult heads, thorax, CC abdomen and ovaries, high levels in testes. CC -!- DEVELOPMENTAL STAGE: Abundant in embryos and adults. CC -!- CAUTION: Ref.2 (CAA29405, CAA29406, CAA29407 and CAA29408) CC sequences differ from that shown due to erroneous gene model CC prediction. CC -!- CAUTION: Ref.2 (CAA29405, CAA29406, CAA29407 and CAA29408) CC sequences differ from that shown due to several frameshifts. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF091328; AAC67581.1; -; Genomic_DNA. DR EMBL; X05991; CAA29405.1; ALT_SEQ; Genomic_DNA. DR EMBL; X05991; CAA29406.1; ALT_SEQ; Genomic_DNA. DR EMBL; X05991; CAA29407.1; ALT_SEQ; Genomic_DNA. DR EMBL; X05991; CAA29408.1; ALT_SEQ; Genomic_DNA. DR EMBL; AE014134; AAF53761.2; -; Genomic_DNA. DR EMBL; AY058445; AAL13674.1; -; mRNA. DR PIR; S01102; S01102. DR PIR; S01103; S01103. DR PIR; S01104; S01104. DR PIR; S01105; S01105. DR UniGene; Dm.467; -. DR DIP; DIP:18447N; -. DR Ensembl; CG10561; Drosophila melanogaster. DR KEGG; dme:Dmel_CG10561; -. DR FlyBase; FBgn0002036; CG10561. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-009458-MONOMER; -. DR GermOnline; CG10561; Drosophila melanogaster. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR InterPro; IPR002937; Amino_oxidase. DR Pfam; PF01593; Amino_oxidase; 1. KW Complete proteome. FT CHAIN 1 504 Protein anon-37Cs. FT /FTId=PRO_0000064404. FT CONFLICT 53 53 A -> S (in Ref. 5). FT CONFLICT 234 234 L -> R (in Ref. 1). FT CONFLICT 458 458 G -> D (in Ref. 1). FT CONFLICT 475 475 G -> S (in Ref. 1). SQ SEQUENCE 504 AA; 56202 MW; 7C594AE7417A6687 CRC64; MQCFKLASRR SLYNARVLQA DNIGDKQRSP DLEAARQNTQ IVVVGAGLAG LSAAQHLLSH GFRRTVILEA TDRYGGRINT QRFGDTYCEL GAKWVKIDGS QDSMYELLRN TEGLGKQIKQ PDRATYLQDG SRINPAMVEL IDTLFRQLCR GFKVSERVKT GGDLHSLDNV MNYFRTESDR IIGVSFQHPK DQLAAREIFQ SLFKEFGSIL GCCLEYVNIE HITKCPVQQE QRPLYVPTGL DNVVDDLIQN MDKAQLQTGK PVGQIQWTPA PMKSVGCLDG SLYNADHIIC TLPLGVLKSF AGVLFRPTLP LDKMLAIRNL GFGNPLKIYL SYKKPIGRWL KGSLRPLGTL LNPSVEQQPE RNWTQQVVEI SQVPSSQHVL EVHVGGGYYE EIEKLPDEEL LEQITGLLRR CVSSHLVPYP QELLRSNWST SACYLGGRPY FSTNSSARDV QRLAAPLGEK SPGLLFAGDA TSLRGFGTID AARSSGIREA QRIIDYYLKS VHCG // ID A37C_DROSI Reviewed; 501 AA. AC O96566; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 31-OCT-2006, entry version 27. DE Protein anon-37Cs (Fragment). GN Name=anon-37Cs; Synonyms=Cs; ORFNames=CG10561; OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7240; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=St. Lucia; RX MEDLINE=99250256; PubMed=10231575; DOI=10.1016/S0378-1119(99)00096-7; RA Tatarenkov A., Saez A.G., Ayala F.J.; RT "A compact gene cluster in Drosophila: the unrelated Cs gene is RT compressed between duplicated amd and Ddc."; RL Gene 231:111-120(1999). CC -!- FUNCTION: Has a non-vital function (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; AF091327; AAC67579.1; -; Genomic_DNA. DR FlyBase; FBgn0025651; Dsim\CG10561. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR InterPro; IPR002937; Amino_oxidase. DR Pfam; PF01593; Amino_oxidase; 1. FT CHAIN <1 501 Protein anon-37Cs. FT /FTId=PRO_0000064405. FT NON_TER 1 1 SQ SEQUENCE 501 AA; 56019 MW; 1F140F1E45FC1249 CRC64; FKLASRRRLY NARVLQADNI GDKQRNPDVD AARQNTQIVV VGAGLPGLSA AQHLLYNGFR RTVILEATDR YGGRINTQRF GDTYCELGAK WVKIDGSQDS MYELLRNTEG LDKQIKQPDR ATYLQDGSHI NPAMVELIDT LFRQLCRGFK VSERVKTGGD LHSLDNVMNY FRTESDRIIG TSFQQPKDQL AAREIFQSLF KEFGSILGCC LEYVNIEHIT KCPVQQELRP LYVPTGLDNV VDDLIQNMDK AQLQTGKPVG QIQWTPAPMK SVGCLDGSLY NADHIICTLP LGVLKSFAGV LFRPTLPLDK MLAIRNLGFG NPLKIYLSYK KPIGRWLKGS LRPLGTLLNP SAEQQPERNW TQQVVEISQV PSSQHVLEVH VGGGYYEEIE KLPDDELLEQ ITGLLRRCVS NNLVPYPQEL LRSNWSTSAC YLGGRPYFST INSARDVQRL AAPLGEKSPG LLFAGDATSL NGFGTIDAAR SSGIREAQRI IDFYLKRAHF G // ID A41_LEIDO Reviewed; 288 AA. AC P55905; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 12-DEC-2006, entry version 33. DE Putative ubiquinone biosynthesis methyltransferase A41 (EC 2.1.1.-) DE (Amastigote-specific protein A41). OS Leishmania donovani. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania. OX NCBI_TaxID=5661; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=MHOM/SD/00/1S-C12D; RX MEDLINE=93241226; PubMed=8479459; DOI=10.1016/0166-6851(93)90057-5; RA Nakhasi H.L., Joshi M., Dwyer D.; RT "Cloning and characterization of differentially expressed genes from RT in vitro-grown 'amastigotes' of Leishmania donovani."; RL Mol. Biochem. Parasitol. 58:345-354(1993). CC -!- FUNCTION: Converts DDMQH2 into DMQH2 (By similarity). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 2-polyprenyl-6- CC methoxy-1,4-benzoquinol = S-adenosyl-L-homocysteine + 2- CC polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol. CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. UbiE 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; L06118; AAK14902.1; -; mRNA. DR PIR; B48583; B48583. DR InterPro; IPR004033; UbiE/COQ5mtfrase. DR Pfam; PF01209; Ubie_methyltran; 1. DR TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 1. DR PROSITE; PS01183; UBIE_1; 1. DR PROSITE; PS01184; UBIE_2; 1. KW Methyltransferase; Transferase; Ubiquinone biosynthesis. FT CHAIN 1 288 Putative ubiquinone biosynthesis FT methyltransferase A41. FT /FTId=PRO_0000193363. SQ SEQUENCE 288 AA; 31975 MW; 0D17D477E37C5CEB CRC64; MLHYTRLGRN MGLGDAYVKK VFDSVATKYD MMNDVLSLGI HRIWKKHFVE DCVCPLPGSK FLDVAGGTGD IAFRITDSIR ARGQSFGIVP KTLDGTKVVV CDINAMMLKE GQKRAEREGY MDIDWVCASG EELPFEDGAF DSYTVSFGIR NFSDRPKALR EAFRVLKVGG ALHVLEFSRV TCPLLSVPYE LWSYGFMPQA GRMLADEESY RYLVDSIRAF PDQETFAQMI RDAGFGYVRY ENLTGGIACI HTGVKTTPTP ITPTTSSDIP AQNTSEATCE VKPEPNSA // ID A45K_MYCBP Reviewed; 17 AA. AC P80069; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 20-FEB-2007, entry version 25. DE 45/47 kDa antigen (Fragment). OS Mycobacterium bovis (strain BCG / Paris 1173P2). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=410289; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=93138802; PubMed=8423100; RA Romain F., Laqueyrerie A., Militzer P., Pescher P., Chavarot P., RA Lagranderie M., Auregan G., Gheorghiu M., Marchal G.A.; RT "Identification of a Mycobacterium bovis BCG 45/47-kilodalton antigen RT complex, an immunodominant target for antibody response after RT immunization with living bacteria."; RL Infect. Immun. 61:742-750(1993). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- SIMILARITY: To M.leprae NL43, and M.tuberculosis MPT32. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A49237; A49237. KW Direct protein sequencing. FT CHAIN 1 >17 45/47 kDa antigen. FT /FTId=PRO_0000064406. FT NON_TER 17 17 SQ SEQUENCE 17 AA; 1521 MW; 4492CC389D9D9893 CRC64; APEPAPPVPP AAAAPPA // ID A464_PBCV1 Reviewed; 275 AA. AC Q98514; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 31-OCT-2006, entry version 37. DE Putative protein A464R. GN OrderedLocusNames=A464R; OS Paramecium bursaria Chlorella virus 1 (PBCV-1). OC Viruses; dsDNA viruses, no RNA stage; Phycodnaviridae; Chlorovirus. OX NCBI_TaxID=10506; OH NCBI_TaxID=114049; Chlorella. RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=96400190; PubMed=8806566; DOI=10.1006/viro.1996.0482; RA Kutish G.F., Li Y., Lu Z., Furuta M., Rock D.L., van Etten J.L.; RT "Analysis of 76 kb of the chlorella virus PBCV-1 330-kb genome: map RT positions 182 to 258."; RL Virology 223:303-317(1996). CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain. CC -!- SIMILARITY: Contains 1 RNase III 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; U42580; AAC96831.1; -; Genomic_DNA. DR PIR; T17966; T17966. DR HSSP; O67082; 1JFZ. DR InterPro; IPR001159; Ds_RNA_bd. DR InterPro; IPR000999; RNase_III. DR InterPro; IPR011907; RNaseIII_bac. DR Pfam; PF00035; dsrm; 1. DR Pfam; PF00636; Ribonuclease_3; 1. DR SMART; SM00358; DSRM; 1. DR SMART; SM00535; RIBOc; 1. DR TIGRFAMs; TIGR02191; RNaseIII; 1. DR PROSITE; PS50137; DS_RBD; 1. DR PROSITE; PS00517; RNASE_3_1; 1. DR PROSITE; PS50142; RNASE_3_2; 1. KW Endonuclease; Hydrolase; Hypothetical protein; Nuclease; RNA-binding. FT CHAIN 1 275 Putative protein A464R. FT /FTId=PRO_0000180465. FT DOMAIN 51 175 RNase III. FT DOMAIN 201 269 DRBM. SQ SEQUENCE 275 AA; 31170 MW; 251CE9AD59146C75 CRC64; MENISKCMER GTTVGTMMVS ERFKDQVQIP NTDDNFPEGP PSTKSGVMFT KEDVEYLIGM PIIDFSYYKT AFSYNAIVEG EATYERMEFV GDSVLGFIIA RYLYDNFPGK DEGFLSRLRT KFVSGKFLSS IALRMGLHNY VIMHQKGLYR GWNTNPRILE DVFEALMGAI YFDLGINAAK QFFMTTLAKY ADMQSLMLDT NYKDRLLKHT RKVELPRPEF VSVFEKGGAN PSFIVDVVIN GQKISTGTGK SRKDAEQNAS KIALHTMGVP EEFIH // ID A494_ARATH Reviewed; 361 AA. AC P43295; Q9SJT5; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 23-JAN-2007, entry version 56. DE Probable cysteine proteinase A494 precursor (EC 3.4.22.-). GN OrderedLocusNames=At2g21430; ORFNames=F3K23.19; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-361. RC STRAIN=cv. Landsberg erecta; RX MEDLINE=94289649; PubMed=8018874; RA Williams J., Bulman M., Huttly A.K., Phillips A., Neill S.; RT "Characterization of a cDNA from Arabidopsis thaliana encoding a RT potential thiol protease whose expression is induced independently by RT wilting and abscisic acid."; RL Plant Mol. Biol. 25:259-270(1994). CC -!- INDUCTION: By wilting and abscisic acid (ABA). CC -!- SIMILARITY: Belongs to the peptidase C1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC006841; AAD23687.1; -; Genomic_DNA. DR EMBL; X74359; CAA52403.1; -; mRNA. DR PIR; B84601; B84601. DR UniGene; At.14069; -. DR HSSP; P07711; 1CJL. DR MEROPS; C01.022; -. DR GenomeReviews; CT485783_GR; AT2G21430. DR KEGG; ath:At2g21430; -. DR TAIR; At2g21430; -. DR GermOnline; AT2G21430; Arabidopsis thaliana. DR InterPro; IPR000169; Pept_cys_AS. DR InterPro; IPR000668; Peptidase_C1A_C. DR InterPro; IPR013201; Prot_inhib_I29. DR Pfam; PF08246; Inhibitor_I29; 1. DR Pfam; PF00112; Peptidase_C1; 1. DR PRINTS; PR00705; PAPAIN. DR ProDom; PD000158; Peptidase_C1; 1. DR SMART; SM00645; Pept_C1; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1. KW Glycoprotein; Hydrolase; Protease; Signal; Thiol protease; Zymogen. FT SIGNAL 1 23 Potential. FT PROPEP 24 131 Activation peptide (Potential). FT /FTId=PRO_0000026453. FT CHAIN 132 361 Probable cysteine proteinase A494. FT /FTId=PRO_0000026454. FT ACT_SITE 156 156 By similarity. FT ACT_SITE 299 299 By similarity. FT ACT_SITE 326 326 By similarity. FT CARBOHYD 250 250 N-linked (GlcNAc...) (Potential). FT DISULFID 153 203 By similarity. FT DISULFID 187 237 By similarity. FT DISULFID 293 347 By similarity. FT CONFLICT 49 49 T -> A (in Ref. 2). SQ SEQUENCE 361 AA; 39819 MW; D09A2CE5654642DD CRC64; MDYHLRVLFS VSLIFVFVSV SVCGDEDVLI RQVVDETEPK VLSSEDHFTL FKKKFGKVYG SIEEHYYRFS VFKANLLRAM RHQKMDPSAR HGVTQFSDLT RSEFRRKHLG VKGGFKLPKD ANQAPILPTQ NLPEEFDWRD RGAVTPVKNQ GSCGSCWSFS TTGALEGAHF LATGKLVSLS EQQLVDCDHE CDPEEEGSCD SGCNGGLMNS AFEYTLKTGG LMREKDYPYT GTDGGSCKLD RSKIVASVSN FSVVSINEDQ IAANLIKNGP LAVAINAAYM QTYIGGVSCP YICSRRLNHG VLLVGYGSAG FSQARLKEKP YWIIKNSWGE SWGENGFYKI CKGRNICGVD SLVSTVAATT S // ID A4GAT_GORGO Reviewed; 327 AA. AC Q9N290; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 06-FEB-2007, entry version 32. DE Lactosylceramide 4-alpha-galactosyltransferase (EC 2.4.1.228) (Alpha- DE 1,4-galactosyltransferase) (UDP-galactose:beta-D-galactosyl-beta1-R 4- DE alpha-D-galactosyltransferase) (Alpha-1,4-N- DE acetylglucosaminyltransferase) (Globotriaosylceramide synthase) (Gb3 DE synthase) (Fragment). GN Name=A4GALT; Synonyms=A14GALT, A4GALT1; OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Liu Y., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of galactose to lactosylceramide CC and galactosylceramide. Necessary for the synthesis of the CC receptor for bacterial verotoxins (By similarity). CC -!- CATALYTIC ACTIVITY: UDP-galactose + beta-D-galactosyl-(1->4)-D- CC glucosylceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D- CC galactosyl-(1->4)-D-glucosylceramide. CC -!- PATHWAY: Glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus; Golgi apparatus membrane; CC single-pass type II membrane protein (Probable). CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity (By CC similarity). CC -!- SIMILARITY: Belongs to the alpha 1,4-glycosyltransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041420; BAA94505.1; -; Genomic_DNA. DR GO; GO:0030173; C:integral to Golgi membrane; ISS:UniProtKB. DR GO; GO:0008378; F:galactosyltransferase activity; ISS:UniProtKB. DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB. DR InterPro; IPR007652; Gb3_synth. DR InterPro; IPR007577; Glyco_trans_s_bd. DR Pfam; PF04572; Gb3_synth; 1. DR Pfam; PF04488; Gly_transf_sug; 1. KW Glycosyltransferase; Golgi apparatus; Lipid synthesis; Transferase. FT CHAIN <1 327 Lactosylceramide 4-alpha- FT galactosyltransferase. FT /FTId=PRO_0000080577. FT MOTIF 166 168 DXD motif (By similarity). FT NON_TER 1 1 SQ SEQUENCE 327 AA; 37394 MW; ED9A9A37A19F66B8 CRC64; GFKFTFFVSI MIYWHVVGEP KEKGQLYNLP AEIPCPTLAP PTPPSHGPAP GNIFFLETSD RTNPNFLFMC SVESAARTHP ESHVLVLMKG LPGGNASLPR HLGISLLSCF PNVQMLPLDL RELFRDTPLA DWYAAVQGRW EPYLLPVLSD ASRIALMWKF GGIYLDTDFI VLKNLRNLTN VLGTQSRYVL NGAFLAFERX HEFMALCMXD FVDHYNGWIW GHQGPQLLTR VFKKWCSIRS LAESRACRGV TTLPPEAFYP IPWQDWKKYF EDINPEELPR LFSATYAVHV WNKKSQGTRF EATSRALLAQ LHARYCPTTH EAMKMYL // ID A4GAT_HUMAN Reviewed; 353 AA. AC Q9NPC4; Q9P1X5; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 06-FEB-2007, entry version 56. DE Lactosylceramide 4-alpha-galactosyltransferase (EC 2.4.1.228) (Alpha- DE 1,4-galactosyltransferase) (UDP-galactose:beta-D-galactosyl-beta1-R 4- DE alpha-D-galactosyltransferase) (Alpha-1,4-N- DE acetylglucosaminyltransferase) (Alpha4Gal-T1) (Globotriaosylceramide DE synthase) (Gb3 synthase) (CD77 synthase) (P1/Pk synthase). GN Name=A4GALT; Synonyms=A14GALT, A4GALT1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Melanoma; RX MEDLINE=20270223; PubMed=10748143; DOI=10.1074/jbc.M909620199; RA Kojima Y., Fukumoto S., Furukawa K., Okajima T., Wiels J., RA Yokoyama K., Suzuki Y., Urano T., Ohta M., Furukawa K.; RT "Molecular cloning of globotriaosylceramide/CD77 synthase, a RT glycosyltransferase that initiates the synthesis of globo series RT glycosphingolipids."; RL J. Biol. Chem. 275:15152-15156(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-37 AND LYS-183. RX MEDLINE=20287540; PubMed=10747952; DOI=10.1074/jbc.M000728200; RA Steffensen R., Carlier K., Wiels J., Levery S.B., Stroud M., RA Cedergren B., Nilsson Sojka B., Bennett E.P., Jersild C., Clausen H.; RT "Cloning and expression of the histo-blood group Pk UDP- RT galactose:Galbeta1-4Glcbeta1-Cer alpha1,4-galactosyltransferase. RT Molecular genetic basis of the p phenotype."; RL J. Biol. Chem. 275:16723-16729(2000). RN [3] RP NUCLEOTIDE SEQUENCE. RA Liu Y., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-37 AND ARG-163. RA Rieder M.J., Johanson E.J., da Ponte S.H., Hastings N.C., Ahearn M.O., RA Bertucci C.B., Wong M.W., Yi Q., Nickerson D.A.; RT "SeattleSNPs. NHLBI HL66682 program for genomic applications, UW- RT FHCRC, Seattle, WA (URL: http://pga.gs.washington.edu)."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=20057165; PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, 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 VARIANTS VAL-37; LYS-183; ASP-187 AND LEU-251. RX PubMed=10993874; DOI=10.1074/jbc.C000625200; RA Furukawa K., Iwamura K., Uchikawa M., Sojka B.N., Wiels J., RA Okajima T., Urano T., Furukawa K.; RT "Molecular basis for the p phenotype. Identification of distinct and RT multiple mutations in the alpha 1,4-galactosyltransferase gene in RT Swedish and Japanese individuals."; RL J. Biol. Chem. 275:37752-37756(2000). RN [8] RP VARIANT PHE-80 DEL. RX PubMed=11896312; DOI=10.1046/j.1537-2995.2002.00014.x; RA Koda Y., Soejima M., Sato H., Maeda Y., Kimura H.; RT "Three-base deletion and one-base insertion of the RT alpha(1,4)galactosyltransferase gene responsible for the P RT phenotype."; RL Transfusion 42:48-51(2002). CC -!- FUNCTION: Necessary for the biosynthesis of the Pk antigen of CC blood histogroup P. Catalyzes the transfer of galactose to CC lactosylceramide and galactosylceramide. Necessary for the CC synthesis of the receptor for bacterial verotoxins. CC -!- CATALYTIC ACTIVITY: UDP-galactose + beta-D-galactosyl-(1->4)-D- CC glucosylceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D- CC galactosyl-(1->4)-D-glucosylceramide. CC -!- PATHWAY: Glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus; Golgi apparatus membrane; CC single-pass type II membrane protein (Probable). CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in kidney, heart, CC spleen, liver, testis and placenta. CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity (By CC similarity). CC -!- POLYMORPHISM: Different combinations or absence of the P blood CC group system antigens define 5 different phenotypes: P1, P2, CC P1(k), P2(k), and p. Genetic variation in A4GALT determines the p CC phenotype, which is rare and does not express any antigens. It is CC also known as null phenotype; p individuals have antibodies CC against P, P1 and Pk antigens in their sera. These antibodies are CC clinically important because they can cause severe transfusion CC reactions and miscarriage. CC -!- SIMILARITY: Belongs to the alpha 1,4-glycosyltransferase family. CC -!- WEB RESOURCE: NAME=GGDB; NOTE=GlycoGene database"; CC URL="http://ggdb.muse.aist.go.jp/GGDB/index.jsp". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB037883; BAA95915.1; -; mRNA. DR EMBL; AJ245581; CAB93532.1; -; mRNA. DR EMBL; AB041418; BAA94503.1; -; Genomic_DNA. DR EMBL; AY941797; AAX20109.1; -; Genomic_DNA. DR EMBL; Z82176; CAI18757.1; -; Genomic_DNA. DR EMBL; BC017068; AAH17068.1; -; mRNA. DR UniGene; Hs.105956; -. DR Ensembl; ENSG00000128274; Homo sapiens. DR KEGG; hsa:53947; -. DR H-InvDB; HIX0016546; -. DR HGNC; HGNC:18149; A4GALT. DR HPA; HPA001141; -. DR MIM; 111400; phenotype. DR MIM; 607922; gene. DR ArrayExpress; Q9NPC4; -. DR GermOnline; ENSG00000128274; Homo sapiens. DR RZPD-ProtExp; IOH11211; -. DR RZPD-ProtExp; U0876; -. DR GO; GO:0030173; C:integral to Golgi membrane; NAS:UniProtKB. DR GO; GO:0005624; C:membrane fraction; IDA:MGI. DR GO; GO:0008378; F:galactosyltransferase activity; IDA:UniProtKB. DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; NAS:UniProtKB. DR GO; GO:0007009; P:plasma membrane organization and biogenesis; IDA:MGI. DR InterPro; IPR007652; Gb3_synth. DR InterPro; IPR007577; Glyco_trans_s_bd. DR Pfam; PF04572; Gb3_synth; 1. DR Pfam; PF04488; Gly_transf_sug; 1. KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid synthesis; KW Membrane; Polymorphism; Signal-anchor; Transferase; Transmembrane. FT CHAIN 1 353 Lactosylceramide 4-alpha- FT galactosyltransferase. FT /FTId=PRO_0000080578. FT TOPO_DOM 1 22 Cytoplasmic (Potential). FT TRANSMEM 23 43 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 44 353 Lumenal (Potential). FT MOTIF 192 194 DXD motif (By similarity). FT CARBOHYD 121 121 N-linked (GlcNAc...) (Potential). FT CARBOHYD 203 203 N-linked (GlcNAc...) (Potential). FT VARIANT 37 37 M -> V (in dbSNP:rs11541159). FT /FTId=VAR_014296. FT VARIANT 80 80 Missing (in p individuals). FT /FTId=VAR_017507. FT VARIANT 163 163 Q -> R (in dbSNP:rs28915383). FT /FTId=VAR_022320. FT VARIANT 183 183 M -> K (in p individuals; complete loss FT of activity). FT /FTId=VAR_014297. FT VARIANT 187 187 G -> D (in p individuals; partial loss of FT activity; dbSNP:rs28940572). FT /FTId=VAR_017508. FT VARIANT 251 251 P -> L (in p individuals; complete loss FT of activity; dbSNP:rs28940571). FT /FTId=VAR_017509. SQ SEQUENCE 353 AA; 40499 MW; 8755865BDA5DA205 CRC64; MSKPPDLLLR LLRGAPRQRV CTLFIIGFKF TFFVSIMIYW HVVGEPKEKG QLYNLPAEIP CPTLTPPTPP SHGPTPGNIF FLETSDRTNP NFLFMCSVES AARTHPESHV LVLMKGLPGG NASLPRHLGI SLLSCFPNVQ MLPLDLRELF RDTPLADWYA AVQGRWEPYL LPVLSDASRI ALMWKFGGIY LDTDFIVLKN LRNLTNVLGT QSRYVLNGAF LAFERRHEFM ALCMRDFVDH YNGWIWGHQG PQLLTRVFKK WCSIRSLAES RACRGVTTLP PEAFYPIPWQ DWKKYFEDIN PEELPRLLSA TYAVHVWNKK SQGTRFEATS RALLAQLHAR YCPTTHEAMK MYL // ID A4GAT_MOUSE Reviewed; 359 AA. AC Q67BJ4; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 23-JAN-2007, entry version 22. DE Lactosylceramide 4-alpha-galactosyltransferase (EC 2.4.1.228) (Alpha- DE 1,4-galactosyltransferase) (UDP-galactose:beta-D-galactosyl-beta1-R 4- DE alpha-D-galactosyltransferase) (Alpha-1,4-N- DE acetylglucosaminyltransferase) (Alpha4Gal-T1) (Globotriaosylceramide DE synthase) (Gb3 synthase). GN Name=A4galt; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Li Y., Abe A., Hiraoka M., Shayman J.A.; RT "Mouse Gb3 synthase."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Necessary for the biosynthesis of the Pk antigen of CC blood histogroup P. Catalyzes the transfer of galactose to CC lactosylceramide and galactosylceramide. Necessary for the CC synthesis of the receptor for bacterial verotoxins (By CC similarity). CC -!- CATALYTIC ACTIVITY: UDP-galactose + beta-D-galactosyl-(1->4)-D- CC glucosylceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D- CC galactosyl-(1->4)-D-glucosylceramide. CC -!- PATHWAY: Glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus; Golgi apparatus membrane; CC single-pass type II membrane protein (By similarity). CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity (By CC similarity). CC -!- SIMILARITY: Belongs to the alpha 1,4-glycosyltransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY371179; AAR18365.1; -; mRNA. DR UniGene; Mm.323805; -. DR KEGG; mmu:239559; -. DR MGI; MGI:3512453; A4galt. DR ArrayExpress; Q67BJ4; -. DR GermOnline; ENSMUSG00000047878; Mus musculus. DR GO; GO:0050512; F:lactosylceramide 4-alpha-galactosyltransfer...; IEA:EC. DR InterPro; IPR007652; Gb3_synth. DR InterPro; IPR007577; Glyco_trans_s_bd. DR Pfam; PF04572; Gb3_synth; 1. DR Pfam; PF04488; Gly_transf_sug; 1. KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid synthesis; KW Membrane; Signal-anchor; Transferase; Transmembrane. FT CHAIN 1 359 Lactosylceramide 4-alpha- FT galactosyltransferase. FT /FTId=PRO_0000080579. FT TOPO_DOM 1 30 Cytoplasmic (Potential). FT TRANSMEM 31 51 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 52 359 Lumenal (Potential). FT MOTIF 198 200 DXD motif (By similarity). FT CARBOHYD 209 209 N-linked (GlcNAc...) (Potential). FT CARBOHYD 315 315 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 359 AA; 41366 MW; B6380E88BF0A4676 CRC64; MGISCSHLEE TMSKPPDCLL RMLRGTPRQR VFTFFIISFK FMFLISILIY WHTVGAPKDQ REYSLPVDFS CPQLAFPRVS APGNIFFLET SDRTSPNFLF MCSVESAARA HPESQVVVLM KGLPRDTTAQ PRNLGISLLS CFPNVWIRPL DLQELFEDTP LAAWYSEARH RWEPYQLPVL SDASRIALLW KFGGIYLDTD FIVLKNLLNL TNTLGIQSRY VLNGAFLAFE RKHEFLALCL HDFVANYNGW IWGHQGPQLL TRVFKKWCSI QSLEKSHACR GVTALPPEAF YPIPWQNWKK YFEDISPEEL TQLLNATYAV HVWNKKSQGT HLEATSKALL AQLHARYCPT THRAMKMYL // ID A4GAT_PANTR Reviewed; 353 AA. AC Q9N291; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 06-FEB-2007, entry version 37. DE Lactosylceramide 4-alpha-galactosyltransferase (EC 2.4.1.228) (Alpha- DE 1,4-galactosyltransferase) (UDP-galactose:beta-D-galactosyl-beta1-R 4- DE alpha-D-galactosyltransferase) (Alpha-1,4-N- DE acetylglucosaminyltransferase) (Globotriaosylceramide synthase) (Gb3 DE synthase). GN Name=A4GALT; Synonyms=A14GALT, A4GALT1; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Liu Y., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of galactose to lactosylceramide CC and galactosylceramide. Necessary for the synthesis of the CC receptor for bacterial verotoxins (By similarity). CC -!- CATALYTIC ACTIVITY: UDP-galactose + beta-D-galactosyl-(1->4)-D- CC glucosylceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D- CC galactosyl-(1->4)-D-glucosylceramide. CC -!- PATHWAY: Glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus; Golgi apparatus membrane; CC single-pass type II membrane protein (Probable). CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity (By CC similarity). CC -!- SIMILARITY: Belongs to the alpha 1,4-glycosyltransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041419; BAA94504.1; -; Genomic_DNA. DR KEGG; ptr:470230; -. DR GO; GO:0030173; C:integral to Golgi membrane; ISS:UniProtKB. DR GO; GO:0008378; F:galactosyltransferase activity; ISS:UniProtKB. DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB. DR InterPro; IPR007652; Gb3_synth. DR InterPro; IPR007577; Glyco_trans_s_bd. DR Pfam; PF04572; Gb3_synth; 1. DR Pfam; PF04488; Gly_transf_sug; 1. KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid synthesis; KW Membrane; Signal-anchor; Transferase; Transmembrane. FT CHAIN 1 353 Lactosylceramide 4-alpha- FT galactosyltransferase. FT /FTId=PRO_0000080580. FT TOPO_DOM 1 22 Cytoplasmic (Potential). FT TRANSMEM 23 43 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 44 353 Lumenal (Potential). FT MOTIF 192 194 DXD motif (By similarity). FT CARBOHYD 121 121 N-linked (GlcNAc...) (Potential). FT CARBOHYD 203 203 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 353 AA; 40487 MW; F9D9F58B7AE2BFD4 CRC64; MSKPPDLLLR LLRGAPRQRV CTLFIIGFKF TFFVSIMIYW HVVGEPKEKG QLYNLPAEIP CPTLTPPTPP SHGPTPGNIF FLETSDRTNP NFLFMCSVES AARTHPESHV LVLMKGLPGG NASLPRHLGI SLLSCFPNVQ MLPLDLRELF QDTPLADWYA AVQGRWEPYL LPVLSDASRI ALMWKFGGIY LDTDFIVLKN LRNLTNVLGT QSRYVLNGAF LAFERRHEFM ALCMRDFVDH YNGWIWGHQG PQLLTRVFKK WCSIRSLAES RSCRGVTTLP PEAFYPIPWQ DWKKYFEDIN PEELPRLLSA TYAVHVWNKK SQGTRFEATS RALLAQLHAR YCPTTHEAMK MYL // ID A4GAT_PONPY Reviewed; 218 AA. AC Q9N289; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 31-OCT-2006, entry version 31. DE Lactosylceramide 4-alpha-galactosyltransferase (EC 2.4.1.228) (Alpha- DE 1,4-galactosyltransferase) (UDP-galactose:beta-D-galactosyl-beta1-R 4- DE alpha-D-galactosyltransferase) (Alpha-1,4-N- DE acetylglucosaminyltransferase) (Globotriaosylceramide synthase) (Gb3 DE synthase) (Fragment). GN Name=A4GALT; Synonyms=A14GALT, A4GALT1; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Liu Y., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of galactose to lactosylceramide CC and galactosylceramide. Necessary for the synthesis of the CC receptor for bacterial verotoxins (By similarity). CC -!- CATALYTIC ACTIVITY: UDP-galactose + beta-D-galactosyl-(1->4)-D- CC glucosylceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D- CC galactosyl-(1->4)-D-glucosylceramide. CC -!- PATHWAY: Glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus; Golgi apparatus membrane; CC single-pass type II membrane protein (Probable). CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity (By CC similarity). CC -!- SIMILARITY: Belongs to the alpha 1,4-glycosyltransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041421; BAA94506.1; -; Genomic_DNA. DR GO; GO:0050512; F:lactosylceramide 4-alpha-galactosyltransfer...; IEA:EC. DR InterPro; IPR007652; Gb3_synth. DR InterPro; IPR007577; Glyco_trans_s_bd. DR Pfam; PF04572; Gb3_synth; 1. DR Pfam; PF04488; Gly_transf_sug; 1. KW Glycosyltransferase; Golgi apparatus; Lipid synthesis; Transferase. FT CHAIN <1 218 Lactosylceramide 4-alpha- FT galactosyltransferase. FT /FTId=PRO_0000080581. FT MOTIF 57 59 DXD motif (By similarity). FT NON_TER 1 1 SQ SEQUENCE 218 AA; 25622 MW; 57958B41C318ABC5 CRC64; FPNVQMLPLD LRELFRDTPL ADWYTAVQGR WEPYLLPVLS DASRIALMWK FGGIYLDTDF IVLKNLRNLT NVLGTQSRYV LNGAFLAFQR RHEFMALCMR DFVDHYNGWI WGHQGPQLLT RVFKKWCSIR SLAESRACRG VTTLPPEAFY PIPWQDWKKY FEDISPEELP RLLNATYAVH VWNKKSQGTR FEATSRALLA QLHARYCPTT HEAMKMYL // ID A4GAT_RAT Reviewed; 360 AA. AC Q9JI93; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 06-FEB-2007, entry version 28. DE Lactosylceramide 4-alpha-galactosyltransferase (EC 2.4.1.228) (Alpha- DE 1,4-galactosyltransferase) (UDP-galactose:beta-D-galactosyl-beta1-R 4- DE alpha-D-galactosyltransferase) (Alpha-1,4-N- DE acetylglucosaminyltransferase) (Alpha4Gal-T1) (Globotriaosylceramide DE synthase) (Gb3 synthase). GN Name=A4galt; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF 199-ASP--ASP-201. RC STRAIN=Sprague-Dawley; TISSUE=Placenta; RX MEDLINE=20400459; PubMed=10854428; DOI=10.1074/jbc.M002630200; RA Keusch J.J., Manzella S.M., Nyame K.A., Cummings R.D., Baenziger J.U.; RT "Cloning of Gb3 synthase, the key enzyme in globo-series RT glycosphingolipid synthesis, predicts a family of alpha1,4- RT glycosyltransferases conserved in plants, insects and mammals."; RL J. Biol. Chem. 275:25315-25321(2000). CC -!- FUNCTION: Necessary for the biosynthesis of the Pk antigen of CC blood histogroup P. Catalyzes the transfer of galactose to CC lactosylceramide and galactosylceramide. Necessary for the CC synthesis of the receptor for bacterial verotoxins. CC -!- CATALYTIC ACTIVITY: UDP-galactose + beta-D-galactosyl-(1->4)-D- CC glucosylceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D- CC galactosyl-(1->4)-D-glucosylceramide. CC -!- PATHWAY: Glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus; Golgi apparatus membrane; CC single-pass type II membrane protein (By similarity). CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in kidney, CC mesenteric lymph node, spleen and brain. CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity. CC -!- SIMILARITY: Belongs to the alpha 1,4-glycosyltransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF248544; AAF82758.1; -; mRNA. DR UniGene; Rn.48584; -. DR KEGG; rno:63888; -. DR RGD; 621583; A4galt. DR GO; GO:0030173; C:integral to Golgi membrane; ISS:UniProtKB. DR GO; GO:0008378; F:galactosyltransferase activity; ISS:UniProtKB. DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB. DR InterPro; IPR007652; Gb3_synth. DR InterPro; IPR007577; Glyco_trans_s_bd. DR Pfam; PF04572; Gb3_synth; 1. DR Pfam; PF04488; Gly_transf_sug; 1. KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid synthesis; KW Membrane; Signal-anchor; Transferase; Transmembrane. FT CHAIN 1 360 Lactosylceramide 4-alpha- FT galactosyltransferase. FT /FTId=PRO_0000080582. FT TOPO_DOM 1 30 Cytoplasmic (Potential). FT TRANSMEM 31 51 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 52 360 Lumenal (Potential). FT MOTIF 199 201 DXD motif. FT CARBOHYD 210 210 N-linked (GlcNAc...) (Potential). FT CARBOHYD 316 316 N-linked (GlcNAc...) (Potential). FT MUTAGEN 199 201 DTD->ATA: Loss of activity. SQ SEQUENCE 360 AA; 41551 MW; 0A4181886DB49D6A CRC64; MGISRSDLEE TMSKPPDCLP RMLRGTPRQR VFTLFIISFK FTFLVSILIY WHTVGAPKDQ RRQYSLPVDF PCPQLAFPRV SAPGNIFFLE TSDRTNPSFL FMCSVESAAR AHPESQVVVL MKGLPRDTTA WPRNLGISLL SCFPNVQIRP LDLQELFEDT PLAAWYLEAQ HRWEPYLLPV LSDASRIALL WKFGGIYLDT DFIVLKNLRN LTNMLGIQSR YVLNGAFLAF ERKHEFLALC IRDFVAHYNG WIWGHQGPQL LTRVFKKWCS IHSLKESRAC RGVTALPPEA FYPIPWQNWK KYFEDVSPEE LAQLLNATYA VHVWNKKSQG THLEATSRAL LAQLHARYCP TTHRAMTMYL // ID A4GCT_HUMAN Reviewed; 340 AA. AC Q9UNA3; Q0VDK1; Q0VDK2; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 06-FEB-2007, entry version 48. DE Alpha-1,4-N-acetylglucosaminyltransferase (EC 2.4.1.-) (Alpha4GnT). GN Name=A4GNT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Stomach; RX MEDLINE=99362698; PubMed=10430883; DOI=10.1073/pnas.96.16.8991; RA Nakayama J., Yeh J.-C., Misra A.K., Ito S., Katsuyama T., Fukuda M.; RT "Expression cloning of a human alpha1, 4-N- RT acetylglucosaminyltransferase that forms GlcNAcalpha1-->4Galbeta-->R, RT a glycan specifically expressed in the gastric gland mucous cell-type RT mucin."; RL Proc. Natl. Acad. Sci. U.S.A. 96:8991-8996(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-218. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The 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: Necessary for the synthesis of type III mucin. Catalyzes CC the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O- CC glycans. CC -!- PATHWAY: Glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus; Golgi apparatus membrane; CC single-pass type II membrane protein (Probable). CC -!- TISSUE SPECIFICITY: Detected in stomach and pancreas. CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity (By CC similarity). CC -!- SIMILARITY: Belongs to the alpha 1,4-glycosyltransferase family. CC -!- WEB RESOURCE: NAME=GGDB; NOTE=GlycoGene database"; CC URL="http://ggdb.muse.aist.go.jp/GGDB/index.jsp". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF141315; AAD48406.1; -; mRNA. DR EMBL; BC119639; AAI19640.1; -; mRNA. DR EMBL; BC119640; AAI19641.1; -; mRNA. DR UniGene; Hs.278960; -. DR Ensembl; ENSG00000118017; Homo sapiens. DR KEGG; hsa:51146; -. DR HGNC; HGNC:17968; A4GNT. DR LinkHub; Q9UNA3; -. DR ArrayExpress; Q9UNA3; -. DR GermOnline; ENSG00000118017; Homo sapiens. DR RZPD-ProtExp; U0796; -. DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc. DR GO; GO:0005624; C:membrane fraction; TAS:ProtInc. DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:MGI. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc. DR GO; GO:0006493; P:protein amino acid O-linked glycosylation; TAS:ProtInc. DR InterPro; IPR007652; Gb3_synth. DR InterPro; IPR007577; Glyco_trans_s_bd. DR Pfam; PF04572; Gb3_synth; 1. DR Pfam; PF04488; Gly_transf_sug; 1. KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane; KW Polymorphism; Signal-anchor; Transferase; Transmembrane. FT CHAIN 1 340 Alpha-1,4-N- FT acetylglucosaminyltransferase. FT /FTId=PRO_0000080583. FT TOPO_DOM 1 4 Cytoplasmic (Potential). FT TRANSMEM 5 25 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 26 340 Lumenal (Potential). FT MOTIF 167 169 DXD motif (By similarity). FT CARBOHYD 99 99 N-linked (GlcNAc...) (Potential). FT CARBOHYD 138 138 N-linked (GlcNAc...) (Potential). FT CARBOHYD 251 251 N-linked (GlcNAc...) (Potential). FT CARBOHYD 282 282 N-linked (GlcNAc...) (Potential). FT VARIANT 218 218 A -> D (in dbSNP:rs2246945). FT /FTId=VAR_022096. SQ SEQUENCE 340 AA; 39497 MW; 00D667A8394300AB CRC64; MRKELQLSLS VTLLLVCGFL YQFTLKSSCL FCLPSFKSHQ GLEALLSHRR GIVFLETSER MEPPHLVSCS VESAAKIYPE WPVVFFMKGL TDSTPMPSNS TYPAFSFLSA IDNVFLFPLD MKRLLEDTPL FSWYNQINAS AERNWLHISS DASRLAIIWK YGGIYMDTDV ISIRPIPEEN FLAAQASRYS SNGIFGFLPH HPFLWECMEN FVEHYNSAIW GNQGPELMTR MLRVWCKLED FQEVSDLRCL NISFLHPQRF YPISYREWRR YYEVWDTEPS FNVSYALHLW NHMNQEGRAV IRGSNTLVEN LYRKHCPRTY RDLIKGPEGS VTGELGPGNK // ID A4_BOVIN Reviewed; 59 AA. AC Q28053; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-FEB-2007, entry version 42. DE Amyloid beta A4 protein (APP) (ABPP) (Alzheimer disease amyloid A4 DE protein homolog) [Contains: Soluble APP-beta (S-APP-beta); CTF-alpha; DE Beta-amyloid protein 42 (Beta-APP42); Beta-amyloid protein 40 (Beta- DE APP40); Gamma-CTF(59) (Gamma-secretase C-terminal fragment 59); Gamma- DE CTF(57) (Gamma-secretase C-terminal fragment 57)] (Fragment). GN Name=APP; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=92017079; PubMed=1656157; DOI=10.1016/0169-328X(91)90088-F; RA Johnstone E.M., Chaney M.O., Norris F.H., Pascual R., Little S.P.; RT "Conservation of the sequence of the Alzheimer's disease amyloid RT peptide in dog, polar bear and five other mammals by cross-species RT polymerase chain reaction analysis."; RL Brain Res. Mol. Brain Res. 10:299-305(1991). CC -!- FUNCTION: Functional neuronal receptor which couples to CC intracellular signaling pathway through the GTP-binding protein CC G(O) (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the APP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X56124; CAA39589.1; -; mRNA. DR EMBL; X56126; CAA39591.1; -; mRNA. DR UniGene; Bt.34436; -. DR HSSP; P08592; 1NMJ. DR InterPro; IPR008155; Amyloid_glyco. DR InterPro; IPR013803; Amyloid_glyco_Abeta. DR PROSITE; PS00319; A4_EXTRA; PARTIAL. DR PROSITE; PS00320; A4_INTRA; PARTIAL. KW Amyloid; Membrane; Transmembrane. FT CHAIN <1 6 Soluble APP-beta (By similarity). FT /FTId=PRO_0000000064. FT CHAIN 7 >59 CTF-alpha (By similarity). FT /FTId=PRO_0000000065. FT CHAIN 7 48 Beta-amyloid protein 42 (By similarity). FT /FTId=PRO_0000000066. FT CHAIN 7 46 Beta-amyloid protein 40 (By similarity). FT /FTId=PRO_0000000067. FT CHAIN 47 >59 Gamma-CTF(59) (By similarity). FT /FTId=PRO_0000000068. FT CHAIN 49 >59 Gamma-CTF(57) (By similarity). FT /FTId=PRO_0000000069. FT TOPO_DOM <1 34 Extracellular (Potential). FT TRANSMEM 35 58 Potential. FT TOPO_DOM 59 >59 Cytoplasmic (Potential). FT NON_TER 1 1 FT NON_TER 59 59 SQ SEQUENCE 59 AA; 6414 MW; F43469D488A2E12D CRC64; ISEVKMDAEF RHDSGYEVHH QKLVFFAEDV GSNKGAIIGL MVGGVVIATV IVITLVMLK // ID A4_CAEEL Reviewed; 686 AA. AC Q10651; Q18583; Q95ZX1; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2002, sequence version 2. DT 12-DEC-2006, entry version 47. DE Beta-amyloid-like protein precursor. GN Name=apl-1; ORFNames=C42D8.8; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [2] RP SEQUENCE REVISION, AND ALTERNATIVE SPLICING. RG WormBase consortium; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-686. RC STRAIN=Bristol N2; RX MEDLINE=94089766; PubMed=8265668; RA Daigle I., Li C.; RT "apl-1, a Caenorhabditis elegans gene encoding a protein related to RT the human beta-amyloid protein precursor."; RL Proc. Natl. Acad. Sci. U.S.A. 90:12045-12049(1993). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; CC IsoId=Q10651-1; Sequence=Displayed; CC Name=b; CC IsoId=Q10651-2; Sequence=VSP_000017; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the APP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U56966; AAA98722.1; -; Genomic_DNA. DR EMBL; U56966; AAK68242.1; -; Genomic_DNA. DR EMBL; U00240; AAC46470.1; ALT_INIT; mRNA. DR PIR; T15795; T15795. DR UniGene; Cel.6164; -. DR HSSP; P05067; 1MWP. DR DIP; DIP:25431N; -. DR Ensembl; C42D8.8; Caenorhabditis elegans. DR KEGG; cel:C42D8.8a; -. DR KEGG; cel:C42D8.8b; -. DR WormBase; WBGene00000149; apl-1. DR WormPep; C42D8.8a; CE04209. DR WormPep; C42D8.8b; CE27845. DR InterPro; IPR008155; Amyloid_glyco. DR InterPro; IPR008154; Amyloid_glyco_extra. DR Pfam; PF02177; A4_EXTRA; 1. DR PRINTS; PR00203; AMYLOIDA4. DR SMART; SM00006; A4_EXTRA; 1. DR PROSITE; PS00319; A4_EXTRA; 1. KW Alternative splicing; Amyloid; Complete proteome; KW Developmental protein; Differentiation; Glycoprotein; Membrane; KW Neurogenesis; Signal; Transmembrane. FT SIGNAL 1 21 Potential. FT CHAIN 22 686 Beta-amyloid-like protein. FT /FTId=PRO_0000000201. FT TOPO_DOM 22 621 Extracellular (Potential). FT TRANSMEM 622 642 Potential. FT TOPO_DOM 643 686 Cytoplasmic (Potential). FT MOTIF 676 679 Clathrin-binding (Potential). FT COMPBIAS 205 228 Asp-rich. FT CARBOHYD 84 84 N-linked (GlcNAc...) (Potential). FT CARBOHYD 201 201 N-linked (GlcNAc...) (Potential). FT CARBOHYD 249 249 N-linked (GlcNAc...) (Potential). FT CARBOHYD 417 417 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 538 539 Missing (in isoform b). FT /FTId=VSP_000017. SQ SEQUENCE 686 AA; 79435 MW; A0816858FDD48608 CRC64; MTVGKLMIGL LIPILVATVY AEGSPAGSKR HEKFIPMVAF SCGYRNQYMT EEGSWKTDDE RYATCFSGKL DILKYCRKAY PSMNITNIVE YSHEVSISDW CREEGSPCKW THSVRPYHCI DGEFHSEALQ VPHDCQFSHV NSRDQCNDYQ HWKDEAGKQC KTKKSKGNKD MIVRSFAVLE PCALDMFTGV EFVCCPNDQT NKTDVQKTKE DEDDDDDEDD AYEDDYSEES DEKDEEEPSS QDPYFKIANW TNEHDDFKKA EMRMDEKHRK KVDKVMKEWG DLETRYNEQK AKDPKGAEKF KSQMNARFQK TVSSLEEEHK RMRKEIEAVH EERVQAMLNE KKRDATHDYR QALATHVNKP NKHSVLQSLK AYIRAEEKDR MHTLNRYRHL LKADSKEAAA YKPTVIHRLR YIDLRINGTL AMLRDFPDLE KYVRPIAVTY WKDYRDEVSP DISVEDSELT PIIHDDEFSK NAKLDVKAPT TTAKPVKETD NAKVLPTEAS DSEEEADEYY EDEDDEQVKK TPDMKKKVKV VDIKPKEIKV TIEEEKKAPK LVETSVQTDD EDDDEDSSSS TSSESDEDED KNIKELRVDI EPIIDEPASF YRHDKLIQSP EVERSASSVF QPYVLASAMF ITAICIIAFA ITNARRRRAM RGFIEVDVYT PEERHVAGMQ VNGYENPTYS FFDSKA // ID A4_CANFA Reviewed; 58 AA. AC Q28280; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-FEB-2007, entry version 44. DE Amyloid beta A4 protein (APP) (ABPP) (Alzheimer disease amyloid A4 DE protein homolog) [Contains: Soluble APP-beta (S-APP-beta); CTF-alpha; DE Beta-amyloid protein 42 (Beta-APP42); Beta-amyloid protein 40 (Beta- DE APP40); Gamma-CTF(59) (Gamma-secretase C-terminal fragment 59); Gamma- DE CTF(57) (Gamma-secretase C-terminal fragment 57)] (Fragment). GN Name=APP; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RX MEDLINE=92017079; PubMed=1656157; DOI=10.1016/0169-328X(91)90088-F; RA Johnstone E.M., Chaney M.O., Norris F.H., Pascual R., Little S.P.; RT "Conservation of the sequence of the Alzheimer's disease amyloid RT peptide in dog, polar bear and five other mammals by cross-species RT polymerase chain reaction analysis."; RL Brain Res. Mol. Brain Res. 10:299-305(1991). CC -!- FUNCTION: Functional neuronal receptor which couples to CC intracellular signaling pathway through the GTP-binding protein CC G(O) (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the APP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X56125; CAA39590.1; -; mRNA. DR UniGene; Cfa.24091; -. DR HSSP; P08592; 1NMJ. DR Ensembl; ENSCAFG00000008557; Canis familiaris. DR InterPro; IPR008155; Amyloid_glyco. DR InterPro; IPR013803; Amyloid_glyco_Abeta. DR PROSITE; PS00319; A4_EXTRA; PARTIAL. DR PROSITE; PS00320; A4_INTRA; PARTIAL. KW Amyloid; Membrane; Transmembrane. FT CHAIN <1 >58 Amyloid beta A4 protein. FT /FTId=PRO_0000226241. FT CHAIN <1 6 Soluble APP-beta (By similarity). FT /FTId=PRO_0000000070. FT CHAIN 7 >58 CTF-alpha (By similarity). FT /FTId=PRO_0000000071. FT CHAIN 7 48 Beta-amyloid protein 42 (By similarity). FT /FTId=PRO_0000000072. FT CHAIN 7 46 Beta-amyloid protein 40 (By similarity). FT /FTId=PRO_0000000073. FT CHAIN 47 >58 Gamma-CTF(59) (By similarity). FT /FTId=PRO_0000000074. FT CHAIN 49 >58 Gamma-CTF(57) (By similarity). FT /FTId=PRO_0000000075. FT TOPO_DOM <1 34 Extracellular (Potential). FT TRANSMEM 35 58 Potential. FT NON_TER 1 1 FT NON_TER 58 58 SQ SEQUENCE 58 AA; 6285 MW; 8469D488A2E12DFA CRC64; ISEVKMDAEF RHDSGYEVHH QKLVFFAEDV GSNKGAIIGL MVGGVVIATV IVITLVML // ID A4_CAVPO Reviewed; 770 AA. AC Q60495; Q60496; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-APR-2003, sequence version 2. DT 20-FEB-2007, entry version 64. DE Amyloid beta A4 protein precursor (APP) (ABPP) (Alzheimer disease DE amyloid protein homolog) [Contains: Soluble APP-alpha (S-APP-alpha); DE Soluble APP-beta (S-APP-beta); CTF-alpha; CTF-beta; Beta-amyloid DE protein 42 (Beta-APP42); Beta-amyloid protein 40 (Beta-APP40); P3(42); DE P3(40); Gamma-CTF(59) (Gamma-secretase C-terminal fragment 59); Gamma- DE CTF(57) (Gamma-secretase C-terminal fragment 57); C31]. GN Name=APP; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RC TISSUE=Brain, and Liver; RX MEDLINE=97236426; PubMed=9116031; DOI=10.1016/S0167-4781(96)00232-1; RA Beck M., Mueller D., Bigl V.; RT "Amyloid precursor protein in Guinea pigs - complete cDNA sequence and RT alternative splicing."; RL Biochim. Biophys. Acta 1351:17-21(1997). RN [2] RP INTERACTION OF BETA-APP40 WITH APOE. RX MEDLINE=98007700; PubMed=9349544; RA Martel C.L., Mackic J.B., Matsubara E., Governale S., Miguel C., RA Miao W., McComb J.G., Frangione B., Ghiso J., Zlokovic B.V.; RT "Isoform-specific effects of apolipoproteins E2, E3, and E4 on RT cerebral capillary sequestration and blood-brain barrier transport of RT circulating Alzheimer's amyloid beta."; RL J. Neurochem. 69:1995-2004(1997). RN [3] RP PROCESSING. RX MEDLINE=20084499; PubMed=10619481; DOI=10.1016/S0306-4522(99)00390-5; RA Beck M., Brueckner M.K., Holzer M., Kaap S., Pannicke T., Arendt T., RA Bigl V.; RT "Guinea-pig primary cell cultures provide a model to study expression RT and amyloidogenic processing of endogenous amyloid precursor RT protein."; RL Neuroscience 95:243-254(2000). RN [4] RP GAMMA-SECRETASE PROCESSING. RX MEDLINE=20576391; PubMed=11035007; DOI=10.1074/jbc.M005968200; RA Pinnix I., Musunuru U., Tun H., Sridharan A., Golde T., Eckman C., RA Ziani-Cherif C., Onstead L., Sambamurti K.; RT "A novel gamma-secretase assay based on detection of the putative C- RT terminal fragment-gamma of amyloid beta protein precursor."; RL J. Biol. Chem. 276:481-487(2001). CC -!- FUNCTION: Functions as a cell surface receptor and performs CC physiological functions on the surface of neurons relevant to CC neurite growth, neuronal adhesion and axonogenesis. Involved in CC cell mobility and transcription regulation through protein-protein CC interactions (By similarity). Can promote transcription activation CC through binding to APBB1/Tip60 and inhibit Notch signaling through CC interaction with Numb (By similarity). Couples to apoptosis- CC inducing pathways such as those mediated by G(O) and JIP (By CC similarity). Inhibits G(o) alpha ATPase activity (By similarity). CC Acts as a kinesin I membrane receptor, mediating the axonal CC transport of beta-secretase and presenilin 1 (By similarity). May CC be involved in copper homeostasis/oxidative stress through copper CC ion reduction (By similarity). In vitro, copper-metallated APP CC induces neuronal death directly or is potentiated through Cu(2+)- CC mediated low-density lipoprotein oxidation (By similarity). Can CC regulate neurite outgrowth through binding to components of the CC extracellular matrix such as heparin and collagen I and IV (By CC similarity). The splice isoforms that contain the BPTI domain CC possess protease inhibitor activity (By similarity). CC -!- FUNCTION: Beta-amyloid peptides are lipophilic metal chelators CC with metal-reducing activity. Bind transient metals such as CC copper, zinc and iron. Beta-amyloid peptides bind to lipoproteins CC and apolipoproteins E and J in the CSF and to HDL particles in CC plasma, inhibiting metal-catalyzed oxidation of lipoproteins. CC -!- FUNCTION: Appicans elicit adhesion of neural cells to the CC extracellular matrix and may regulate neurite outgrowth in the CC brain (By similarity). CC -!- FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved CC peptides, including C31, are potent enhancers of neuronal CC apoptosis (By similarity). CC -!- SUBUNIT: Binds, via its C-terminus, to the PID domain of several CC cytoplasmic proteins, including APBB family members, the APBA CC family, MAPK8IP1, SHC1 and Numb and Dab1 (By similarity). Also CC interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 CC (via its TPR domains), APPBP2 (via BaSS) and DDB1 (By similarity). CC Associates with microtubules in the presence of ATP and in a CC kinesin-dependent manner (By similarity). Soluble Abeta40 binds CC all three isoforms of APOE, in vitro and in vivo. When lipidated, CC ApoE3 appears to be the preferred amyloid binding isoform, while CC the apoE4 isoform-beta-APP40 complex is capable of being CC transported across the blood-brain barrier. Interacts with CPEB1 CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein (By similarity). Note=Cell surface protein that rapidly CC becomes internalized via clathrin-coated pits (By similarity). CC During maturation, the immature APP (N-glycosylated in the CC endoplasmic reticulum) moves to the Golgi complex where complete CC maturation occurs (O-glycosylated and sulfated) (By similarity). CC After alpha-secretase cleavage, soluble APP is released into the CC extracellular space and the C-terminal is internalized to CC endosomes and lysosomes (By similarity). Some APP accumulates in CC secretory transport vesicles leaving the late Golgi compartment CC and returns to the cell surface (By similarity). APP sorts to the CC basolateral surface in epithelial cells (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms, missing exons 7,8 and 15, seem to CC exist. The L-isoforms, missing exon 15, are referred to as CC appicans; CC Name=APP770; CC IsoId=Q60495-1; Sequence=Displayed; CC Name=APP695; CC IsoId=Q60495-2; Sequence=VSP_007221, VSP_007222; CC -!- TISSUE SPECIFICITY: Isoform APP695 is the major isoform found in CC brain. The longer isoforms containing the BPTI domain are CC predominantly expressed in peripheral organs such as muscle and CC liver. CC -!- INDUCTION: Increased levels during neuronal differentiation. CC -!- DOMAIN: The basolateral sorting signal (BaSS) is required for CC sorting of membrane proteins to the basolateral surface of CC epithelial cells. CC -!- DOMAIN: The NPXY sequence motif found in many tyrosine- CC phosphorylated proteins is required for the specific binding of CC the PID domain. However, additional amino acids either N- or C- CC terminal to the NPXY motif are often required for complete CC interaction. The PID domain-containing proteins which bind APP CC require the YENPTY motif for full interaction. These interactions CC are independent of phosphorylation on the terminal tyrosine CC residue (By similarity). The NPXY site is also involved in CC clathrin-mediated endocytosis. CC -!- PTM: Proteolytically processed under normal cellular conditions. CC Cleavage by alpha-secretase or alternatively by beta-secretase CC leads to generation and extracellular release of soluble APP CC peptides, S-APP-alpha and S-APP-beta, respectively, and the CC retention of corresponding membrane-anchored C-terminal fragments, CC CTF-alpha and CTF-beta. Subsequent processing of CTF-alpha by CC gamma-secretase yields P3 peptides. This is the major secretory CC pathway and is non-amyloidogenic. Alternatively, CC presenilin/nicastrin-mediated gamma-secretase processing of CTF- CC beta releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) CC and amyloid-beta 42 (Abeta42), major components of amyloid CC plaques, and the corresponding cytotoxic C-terminal fragments CC (CTFs). CC -!- PTM: Proteolytically cleaved by caspase-3 during neuronal CC apoptosis (By similarity). CC -!- PTM: N- and O-glycosylated. O-linkage of chondroitin sulfate to CC the L-APP isoforms produces the APP proteoglycan core proteins, CC the appicans (By similarity). CC -!- PTM: Phosphorylation in the C-terminal on tyrosine, threonine and CC serine residues is neuron-specific (By similarity). CC Phosphorylation can affect APP processing, neuronal CC differentiation and interaction with other proteins. CC -!- PTM: Extracellular binding and reduction of copper, results in a CC corresponding oxidation of Cys-144 and Cys-158, and the formation CC of a disulfide bond (By similarity). CC -!- MISCELLANEOUS: Chelation of metal ions, notably copper, iron and CC zinc, can induce histidine-bridging between beta-amyloid molecules CC resulting in beta-amyloid-metal aggregates. CC -!- SIMILARITY: Belongs to the APP family. CC -!- SIMILARITY: Contains 1 BPTI/Kunitz inhibitor 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; X97631; CAA66230.1; -; mRNA. DR EMBL; X99198; CAA67589.1; -; mRNA. DR HSSP; P08592; 1NMJ. DR SMR; Q60495; 28-123, 124-189, 287-342, 460-569. DR MEROPS; I02.015; -. DR InterPro; IPR008155; Amyloid_glyco. DR InterPro; IPR013803; Amyloid_glyco_Abeta. DR InterPro; IPR008154; Amyloid_glyco_extra. DR InterPro; IPR002223; Prot_inh_Kunz-m. DR Gene3D; G3DSA:4.10.410.10; Prot_inh_Kunz-m; 1. DR Pfam; PF02177; A4_EXTRA; 1. DR Pfam; PF00014; Kunitz_BPTI; 1. DR PRINTS; PR00203; AMYLOIDA4. DR PRINTS; PR00759; BASICPTASE. DR ProDom; PD000222; Prot_Inh_Kunz-m; 1. DR SMART; SM00006; A4_EXTRA; 1. DR SMART; SM00131; KU; 1. DR PROSITE; PS00319; A4_EXTRA; 1. DR PROSITE; PS00320; A4_INTRA; 1. DR PROSITE; PS00280; BPTI_KUNITZ_1; 1. DR PROSITE; PS50279; BPTI_KUNITZ_2; 1. KW Alternative splicing; Amyloid; Apoptosis; Cell adhesion; Coated pits; KW Copper; Endocytosis; Glycoprotein; Heparin-binding; Iron; Membrane; KW Metal-binding; Notch signaling pathway; Phosphorylation; KW Protease inhibitor; Proteoglycan; Serine protease inhibitor; Signal; KW Transmembrane; Zinc. FT SIGNAL 1 17 By similarity. FT CHAIN 18 770 Amyloid beta A4 protein. FT /FTId=PRO_0000000076. FT CHAIN 18 687 Soluble APP-alpha (By similarity). FT /FTId=PRO_0000000077. FT CHAIN 18 671 Soluble APP-beta (By similarity). FT /FTId=PRO_0000000078. FT CHAIN 672 770 CTF-alpha (By similarity). FT /FTId=PRO_0000000079. FT CHAIN 672 713 Beta-amyloid protein 42 (By similarity). FT /FTId=PRO_0000000080. FT CHAIN 672 711 Beta-amyloid protein 40 (By similarity). FT /FTId=PRO_0000000081. FT CHAIN 688 770 CTF-beta (By similarity). FT /FTId=PRO_0000000082. FT PEPTIDE 688 713 P3(42) (By similarity). FT /FTId=PRO_0000000083. FT PEPTIDE 688 711 P3(40) (By similarity). FT /FTId=PRO_0000000084. FT CHAIN 712 770 Gamma-CTF(59) (By similarity). FT /FTId=PRO_0000000085. FT CHAIN 714 770 Gamma-CTF(57) (By similarity). FT /FTId=PRO_0000000086. FT CHAIN 740 770 C31 (By similarity). FT /FTId=PRO_0000000087. FT TOPO_DOM 18 699 Extracellular (Potential). FT TRANSMEM 700 723 Potential. FT TOPO_DOM 724 770 Cytoplasmic (Potential). FT DOMAIN 291 341 BPTI/Kunitz inhibitor. FT REGION 96 110 Heparin-binding (By similarity). FT REGION 135 155 Copper-binding (By similarity). FT REGION 181 188 Zinc-binding (By similarity). FT REGION 391 423 Heparin-binding (By similarity). FT REGION 491 522 Heparin-binding (By similarity). FT REGION 523 540 Collagen-binding (By similarity). FT REGION 732 751 Interaction with G(o)-alpha (By FT similarity). FT MOTIF 724 734 Basolateral sorting signal. FT MOTIF 759 762 NPXY motif; contains endocytosis signal. FT COMPBIAS 230 260 Asp/Glu-rich (acidic). FT COMPBIAS 274 280 Poly-Thr. FT METAL 137 137 Copper (By similarity). FT METAL 147 147 Copper (By similarity). FT METAL 149 149 Copper (By similarity). FT METAL 151 151 Copper (Probable). FT METAL 677 677 Copper or zinc (By similarity). FT METAL 681 681 Copper or zinc (Probable). FT METAL 684 684 Copper or zinc (By similarity). FT METAL 685 685 Copper or zinc (By similarity). FT SITE 144 144 Required for Cu(2+) reduction (By FT similarity). FT SITE 301 302 Reactive bond (By similarity). FT SITE 671 672 Cleavage (by beta-secretase) (By FT similarity). FT SITE 672 673 Cleavage (by caspase-6) (By similarity). FT SITE 687 688 Cleavage (by alpha-secretase) (By FT similarity). FT SITE 704 704 Implicated in free radical propagation FT (By similarity). FT SITE 706 706 Susceptible to oxidation (By similarity). FT SITE 713 714 Cleavage (by gamma-secretase) (By FT similarity). FT SITE 739 740 Cleavage (by caspase-3) (By similarity). FT MOD_RES 198 198 Phosphoserine (by CK2) (By similarity). FT MOD_RES 206 206 Phosphoserine (by CK1) (By similarity). FT MOD_RES 729 729 Phosphothreonine (By similarity). FT MOD_RES 730 730 Phosphoserine (by APP-kinase I) (By FT similarity). FT MOD_RES 743 743 Phosphothreonine (by CDK5 and MAPK10) (By FT similarity). FT MOD_RES 757 757 Phosphotyrosine (By similarity). FT CARBOHYD 542 542 N-linked (GlcNAc...) (Potential). FT CARBOHYD 571 571 N-linked (GlcNAc...) (Potential). FT CARBOHYD 656 656 O-linked (Xyl...) (chondroitin sulfate) FT (By similarity). FT DISULFID 144 158 By similarity. FT DISULFID 291 341 By similarity. FT DISULFID 300 324 By similarity. FT DISULFID 316 337 By similarity. FT VAR_SEQ 289 289 E -> V (in isoform APP695). FT /FTId=VSP_007221. FT VAR_SEQ 290 364 Missing (in isoform APP695). FT /FTId=VSP_007222. SQ SEQUENCE 770 AA; 86883 MW; 0AFD36C90F0D8B6C CRC64; MLPSLALLLL TTWTARALEV PTDGNAGLLA EPQIAMFCGK LNMHMNVQNG KWEPDPSGTK TCIGSKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR SRKQCKTHPH FVIPYRCLVG EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR GVEFVCCPLA EESDNIDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVADVEEE EADDDEDVED GDEVEEEAEE PYEEATEKTT SIATTTTTTT ESVEEVVREV CSEQAETGPC RSMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSVMSQNLL KTSGEPVSQG PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL QAVPPRPRHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET KTTVELLPVN GEFSLDDLQP WHPFGVDSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN IKTEEISEVK MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN // ID A4_DROME Reviewed; 887 AA. AC P14599; Q9TVV0; Q9U4H3; Q9W5F1; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2002, sequence version 2. DT 23-JAN-2007, entry version 78. DE Beta-amyloid-like protein precursor. GN Name=Appl; Synonyms=VND; ORFNames=CG7727; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89184650; PubMed=2494667; RA Rosen D.R., Martin-Morris L., Luo L., White K.; RT "A Drosophila gene encoding a protein resembling the human beta- RT amyloid protein precursor."; RL Proc. Natl. Acad. Sci. U.S.A. 86:2478-2482(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Oregon-R; RX MEDLINE=20196011; PubMed=10731137; DOI=10.1126/science.287.5461.2220; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Ovary; RX MEDLINE=20196012; PubMed=10731138; DOI=10.1126/science.287.5461.2222; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-83. RX MEDLINE=91184006; PubMed=2127912; RA Martin-Morris L.E., White K.; RT "The Drosophila transcript encoded by the beta-amyloid protein RT precursor-like gene is restricted to the nervous system."; RL Development 110:185-195(1990). CC -!- FUNCTION: Probably corresponds to the protein encoded by the CC essential locus vnd, a gene required for embryonic nervous system CC development. CC -!- INTERACTION: CC Q9W0K0:Aplip1; NbExp=2; IntAct=EBI-74135, EBI-74120; CC Q9WV19:Cyp2g1 (xeno); NbExp=1; IntAct=EBI-74135, EBI-74563; CC Q9WVI9:Mapk8ip1 (xeno); NbExp=1; IntAct=EBI-74135, EBI-74515; CC Q9ERE9:Mapk8ip2 (xeno); NbExp=2; IntAct=EBI-74135, EBI-74576; CC Q9VX41:X11L; NbExp=2; IntAct=EBI-74135, EBI-74153; CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Expressed in post-mitotic neurons in the CC central and peripheral nervous systems. Within the nervous system CC transcripts are not observed in neuroblasts, newly generated CC neurons and at least one class of presumed glial cells. CC -!- DEVELOPMENTAL STAGE: Expressed in all developmental stages. CC -!- DOMAIN: The clathrin-binding site is essential for its association CC with X11-alpha, -beta, and -gamma. The sequence specific CC recognition extends to peptide residues that are C-terminal to the CC NPXY motif. This interaction appears to be independent of CC phosphorylation (By similarity). CC -!- SIMILARITY: Belongs to the APP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J04516; AAA28874.1; -; Genomic_DNA. DR EMBL; AE014298; AAF45520.2; -; Genomic_DNA. DR EMBL; AL031883; CAA21409.1; -; Genomic_DNA. DR EMBL; AL022139; CAA21409.1; JOINED; Genomic_DNA. DR EMBL; AL022139; CAA18093.1; -; Genomic_DNA. DR EMBL; AL031883; CAA18093.1; JOINED; Genomic_DNA. DR EMBL; AF181628; AAD55414.1; -; mRNA. DR EMBL; X55774; CAA39294.1; -; Genomic_DNA. DR EMBL; X55775; CAA39294.1; JOINED; Genomic_DNA. DR PIR; A32758; A32758. DR UniGene; Dm.4862; -. DR HSSP; P05067; 1MWP. DR IntAct; P14599; -. DR Ensembl; CG7727; Drosophila melanogaster. DR KEGG; dme:Dmel_CG7727; -. DR FlyBase; FBgn0000108; Appl. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-000043-MONOMER; -. DR GermOnline; CG7727; Drosophila melanogaster. DR GO; GO:0005576; C:extracellular region; IDA:FlyBase. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0048812; P:neurite morphogenesis; IMP:FlyBase. DR GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase. DR GO; GO:0048678; P:response to axon injury; IMP:FlyBase. DR InterPro; IPR008155; Amyloid_glyco. DR InterPro; IPR008154; Amyloid_glyco_extra. DR Pfam; PF02177; A4_EXTRA; 1. DR PRINTS; PR00203; AMYLOIDA4. DR SMART; SM00006; A4_EXTRA; 1. DR PROSITE; PS00319; A4_EXTRA; 1. DR PROSITE; PS00320; A4_INTRA; 1. KW Amyloid; Complete proteome; Developmental protein; Differentiation; KW Glycoprotein; Membrane; Neurogenesis; Signal; Transmembrane. FT SIGNAL 1 27 Potential. FT CHAIN 28 887 Beta-amyloid-like protein. FT /FTId=PRO_0000000202. FT TOPO_DOM 28 813 Extracellular (Potential). FT TRANSMEM 814 834 Potential. FT TOPO_DOM 835 887 Cytoplasmic (Potential). FT MOTIF 877 880 Clathrin-binding (Potential). FT CARBOHYD 150 150 N-linked (GlcNAc...) (Potential). FT CARBOHYD 161 161 N-linked (GlcNAc...) (Potential). FT CARBOHYD 237 237 N-linked (GlcNAc...) (Potential). FT CARBOHYD 240 240 N-linked (GlcNAc...) (Potential). FT CARBOHYD 574 574 N-linked (GlcNAc...) (Potential). FT CONFLICT 177 177 S -> T (in Ref. 1). FT CONFLICT 229 229 Missing (in Ref. 1). FT CONFLICT 332 332 V -> M (in Ref. 4). FT CONFLICT 743 743 S -> T (in Ref. 1). SQ SEQUENCE 887 AA; 98333 MW; F0F0855AD65A5275 CRC64; MCAALRRNLL LRSLWVVLAI GTAQVQAASP RWEPQIAVLC EAGQIYQPQY LSEEGRWVTD LSKKTTGPTC LRDKMDLLDY CKKAYPNRDI TNIVESSHYQ KIGGWCRQGA LNAAKCKGSH RWIKPFRCLG PFQSDALLVP EGCLFDHIHN ASRCWPFVRW NQTGAAACQE RGMQMRSFAM LLPCGISVFS GVEFVCCPKH FKTDEIHVKK TDLPVMPAAQ INSANDELVM NDEDDSNDSN YSKDANEDDL DDEDDLMGDD EEDDMVADEA ATAGGSPNTG SSGDSNSGSL DDINAEYDSG EEGDNYEEDG AGSESEAEVE ASWDQSGGAK VVSLKSDSSS PSSAPVAPAP EKAPVKSESV TSTPQLSASA AAFVAANSGN SGTGAGAPPS TAQPTSDPYF THFDPHYEHQ SYKVSQKRLE ESHREKVTRV MKDWSDLEEK YQDMRLADPK AAQSFKQRMT ARFQTSVQAL EEEGNAEKHQ LAAMHQQRVL AHINQRKREA MTCYTQALTE QPPNAHHVEK CLQKLLRALH KDRAHALAHY RHLLNSGGPG GLEAAASERP RTLERLIDID RAVNQSMTML KRYPELSAKI AQLMNDYILA LRSKDDIPGS SLGMSEEAEA GILDKYRVEI ERKVAEKERL RLAEKQRKEQ RAAEREKLRE EKLRLEAKKV DDMLKSQVAE QQSQPTQSST QSQAQQQQQE KSLPGKELGP DAALVTAANP NLETTKSEKD LSDTEYGEAT VSSTKVQTVL PTVDDDAVQR AVEDVAAAVA HQEAEPQVQH FMTHDLGHRE SSFSLRREFA QHAHAAKEGR NVYFTLSFAG IALMAAVFVG VAVAKWRTSR SPHAQGFIEV DQNVTTHHPI VREEKIVPNM QINGYENPTY KYFEVKE // ID A4_FUGRU Reviewed; 737 AA. AC O93279; DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 28-NOV-2006, entry version 45. DE Amyloid beta A4 protein precursor (APP) (ABPP) (Alzheimer disease DE amyloid A4 A4 protein homolog) [Contains: Beta-amyloid protein (Beta- DE APP) (A-beta)]. GN Name=APP; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=98252138; PubMed=9599080; DOI=10.1016/S0378-1119(98)00032-8; RA Villard L., Tassone F., Crnogorac-Jurcevic T., Clancy K., Gardiner K.; RT "Analysis of pufferfish homologues of the AT-rich human APP gene."; RL Gene 210:17-24(1998). CC -!- FUNCTION: Functional neuronal receptor which couples to CC intracellular signaling pathway through the GTP-binding protein CC G(O) (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the APP family. CC -!- SIMILARITY: Contains 1 BPTI/Kunitz inhibitor 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; AF090120; AAD13392.1; -; Genomic_DNA. DR HSSP; P10646; 1IRH. DR SMR; O93279; 29-124, 440-542. DR Ensembl; SINFRUG00000150276; Fugu rubripes. DR InterPro; IPR008155; Amyloid_glyco. DR InterPro; IPR013803; Amyloid_glyco_Abeta. DR InterPro; IPR008154; Amyloid_glyco_extra. DR InterPro; IPR002223; Prot_inh_Kunz-m. DR Gene3D; G3DSA:4.10.410.10; Prot_inh_Kunz-m; 1. DR Pfam; PF02177; A4_EXTRA; 1. DR Pfam; PF00014; Kunitz_BPTI; 1. DR PRINTS; PR00203; AMYLOIDA4. DR PRINTS; PR00759; BASICPTASE. DR ProDom; PD000222; Prot_Inh_Kunz-m; 1. DR SMART; SM00006; A4_EXTRA; 1. DR SMART; SM00131; KU; 1. DR PROSITE; PS00319; A4_EXTRA; 1. DR PROSITE; PS00320; A4_INTRA; 1. DR PROSITE; PS00280; BPTI_KUNITZ_1; 1. DR PROSITE; PS50279; BPTI_KUNITZ_2; 1. KW Amyloid; Glycoprotein; Membrane; Protease inhibitor; KW Serine protease inhibitor; Signal; Transmembrane. FT SIGNAL 1 18 Potential. FT CHAIN 19 737 Amyloid beta A4 protein. FT /FTId=PRO_0000000197. FT CHAIN 639 681 Beta-amyloid protein (Potential). FT /FTId=PRO_0000000198. FT TOPO_DOM 19 668 Extracellular (Potential). FT TRANSMEM 669 689 Potential. FT TOPO_DOM 690 737 Cytoplasmic (Potential). FT DOMAIN 286 344 BPTI/Kunitz inhibitor. FT REGION 726 729 Clathrin-binding (By similarity). FT SITE 300 301 Reactive bond. FT CARBOHYD 522 522 N-linked (GlcNAc...) (Potential). FT DISULFID 290 340 By similarity. FT DISULFID 299 323 By similarity. FT DISULFID 315 336 By similarity. SQ SEQUENCE 737 AA; 82857 MW; 6FAD01E2E3B2B7E2 CRC64; MGETTAFVLL LVATLTRSSE IPADDTVGLL TEPQVAMFCG KLNMHINVQN GKWESDPSGT KSCLNTKEGI LQYCQEVYPE LQITNVVEAN QPVSIQNWCK KGRKQCRSHT HIVVPYRCLV GEFVSDALLV PDKCKFLHQE RMNQCESHLH WHTVAKESCG DRSMNLHDYG MLLPCGIDRF RGVKFVCCPA ETEQETDSSE VEGEESDVWW GGADPEYSEN SPPTPSRATY VAGDAFERDE NGDGDEDEED DEDVDPTDEQ ESDERTANVA MTTTTTTTTE SVEEVVRAVC WAQAESGPCR AMLERWYFNP KKRRCVPFLF GGCGGNRNNF ESEEYCLAVC SSSLPTVAPS PPDAVDQYFE APGDDNEHAD FRKAKESLEA KHRERMSQVM REWEEAERQA KNLPRADKKA VIQHFQEKVE ALEQEAAGER QQLVETHMAR VEALLNSRRR LTLENYLGAL QANPPRARQV LSLLKKYVRA EQKDRQHTLK HYEHVRTVDP KKAAQIRPQV LTHLRVIDER MNQSLALLYK VPSVASEIQN QIYPAAGSDC KDPVEHCVCP QVDGLVSYGN DALMPDQAYS SAPMDMGVDG LGSIDQSFNQ ANTENHVEPV DARPIPDRGL PTRPVSSLKL EEMPEVRTET DKRQSAGYEV YHQKLVFFAD DVGSNKGAII GLMVGGVVIA TVIVITLVML RKKQYTSIHH GVIEVDAAVT PEERHLARMQ QNGYENPTYK FFEQMQN //