ID A0A026VWG5_OOCBI Unreviewed; 1311 AA. AC A0A026VWG5; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 23-MAY-2018, entry version 26. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein {ECO:0000313|EMBL:EZA48108.1}; GN ORFNames=X777_14217 {ECO:0000313|EMBL:EZA48108.1}; OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Formicoidea; Formicidae; Dorylinae; Ooceraea. OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA48108.1, ECO:0000313|Proteomes:UP000053097}; RN [1] {ECO:0000313|EMBL:EZA48108.1, ECO:0000313|Proteomes:UP000053097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018; RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H., RA Zhang G., Kronauer D.J.; RT "The genome of the clonal raider ant Cerapachys biroi."; RL Curr. Biol. 24:451-458(2014). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK107681; EZA48108.1; -; Genomic_DNA. DR Proteomes; UP000053097; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053097}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:EZA48108.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000053097}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 1311 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001545273. FT TRANSMEM 792 816 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 269 473 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 478 566 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 714 751 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 407 407 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 411 411 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 417 417 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 538 558 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 741 750 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1311 AA; 146235 MW; 198DF61C6CE64DF3 CRC64; MFWLHCGLFV LVIAVPGFIS SLADTTSKRE ADYTLDDSFW NEDTPIGEAE RLLREYRQNQ ELVSNIGGNF YQIIYPVQLR HHEKMGISTR EVGVSKFPQR GYGDGGYQNS RSRGRTGRHF HRTSLLIKAF NHKFRLDLEL NTQLLAPNLM QKDFLTGNAE QTSKQEIEHC YYHGTVRDYP GASAAFHTCN GVSGVIHLGN ETFVIHPFYG GDLSKHPHII FEARTKANKG CANSANNERR VKSRRQKHIL GLPKTTSDRY KRDVREATKY IETAIIIDKA MFDKRNGSTR AEVVHDAIQV ANIADLYFRT LNTRVSVVYI ETWKGSNQAD IDKGIDIDLA LINLNDYTMR RMYQLAQDTT QLLTNYIYIY ICIYIAVPAT VCSQKSVGIS VDLNTYEPHL LAGTMAHMIG HNIGMSHDDG RNDCNCRDWH GCIMAQSIVG LENVQPYKFS ECSKSDYIEA LKSGHGYCLF NKPNELEIRR CGNRVIDEGE ECDCGTLDEC HELDPCCDPI TCKLRTEAEC ATGPCCSDCK LRVRGVVCRE STNECDLPEV CTGDSGQCPP DVYKKNGNPC SNIAGYCFNG VCPALDLQCE QVWGYGGIAA DKQCFEQFNS KGSINGHCGT DSSGHFIKCE AENVHCGSLQ CQQGSKQPVI DGMKDYYSRT IISIKSQEYE CKATTGKVEG SDMPGWGLVR DGTSCGDNLI CVNQTCTSLF PHIDQGKCPS NHDNSECSGN GVCTNVNKCY CFPGWSGPDC SIEQYIPTMS PTTSSPEVVG KADPKLEKKE TPYENYHGSN TVFLVGMLMS VVGGVFVVFA LMALCYRRKS TVQKYDLPYS KKPPQKSYSG VSGNHHAEAA ALETVNKILT FGRMPQYRDK PQPKRHGVEE EDGGTGAEEV VSFIDLPPNN LTKLPEKGIL KKHGGYGLGA GAIEHVERTL NQLNGYHEDI LEVLKNAASR RDLAGTPSGS SNLLDDDVLR KSLAEVGWHP DVYHKDTDGQ DNGIDNGQED EEEDVELQPP CGTIRIRTLE DLIRQLEHRA TARPYLPGQM SPSGSEEIRM SEGEPDRHYR IDSSVCSESS QGSRRCSRGR DEDASRFVYG RYRQPTSRSP YGNHQHTHQH SHQIHPEDEG IYETADPDRG SNTRGETPDC ESDAFIQAQQ QVARWTSEDG GGVQHRPPQQ PPPPPAMQLP VQQQAQQQQQ QSQQQPQQLQ QQQQHQLPVE QLPIKQRGYY PSPPTENSLD VGNNAEAESA QSQQQQQTLS DVRGIDVNHL PNIKKCPLDD NFSLDCNIMN NGSPKELTTN NNSDNENTAL LPPTHFPEYK H // ID A0A067QYF7_ZOONE Unreviewed; 1164 AA. AC A0A067QYF7; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 23-MAY-2018, entry version 24. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 {ECO:0000313|EMBL:KDR11298.1}; DE Flags: Fragment; GN ORFNames=L798_14912 {ECO:0000313|EMBL:KDR11298.1}; OS Zootermopsis nevadensis (Dampwood termite). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; OC Termitoidae; Termopsidae; Zootermopsis. OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR11298.1, ECO:0000313|Proteomes:UP000027135}; RN [1] {ECO:0000313|EMBL:KDR11298.1, ECO:0000313|Proteomes:UP000027135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR11298.1}; RX PubMed=24845553; DOI=10.1038/ncomms4636; RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z., RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W., RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M., RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T., RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., RA Zhou J., Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., RA Liberles D.A., Roe R.M., Vargo E.L., Vilcinskas A., Wang J., RA Bornberg-Bauer E., Korb J., Zhang G., Liebig J.; RT "Molecular traces of alternative social organization in a termite RT genome."; RL Nat. Commun. 5:3636-3636(2014). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK853105; KDR11298.1; -; Genomic_DNA. DR EnsemblMetazoa; KDR11298; KDR11298; L798_14912. DR OMA; QCFEQFN; -. DR Proteomes; UP000027135; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000027135}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KDR11298.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000027135}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 775 799 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 249 453 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 459 547 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 694 731 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 387 387 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 391 391 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 397 397 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 519 539 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 721 730 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KDR11298.1}. FT NON_TER 1164 1164 {ECO:0000313|EMBL:KDR11298.1}. SQ SEQUENCE 1164 AA; 129344 MW; A2A09F93EC2D2230 CRC64; DVHIGRSHWT VVFAVAGEVE RLLREYRQNQ DMVRGIGTHF YQIIYPVQLR HHEKMGISTR EIGAPKFPQR GYGEGTGYPG PPRGRVRTGK HFHRTSLLIK AFNHKFRLDL ELNTQLLAPN LVQKHYLPNG AEQVSKQEIE HCYYHGTVKD YPGATAAFHT CNGVSGVIHV GNETFVIHPF YGGDLSKHPH VIFEARTKTN KGCANSGNFE WRMNSFRRQK HISGMAEGTK ANASGEYARY RRDVRDVIKF IETALVIDKA MFEKRNGSSR MDVVHDAIQV ANIADLYFRT LNTRVSVVYI ETWQGTNQAP VEKNQDIIRS LLNFNDYTSR KLYKVDKDTT QLLTGEVFQG GETGMAVPET VCTTKSVGIN VDINTYEPHL LAGTMAHMIG HNIGMGHDDG REECFCRDWH GCIMARSIVG LENVQPYKFS ECSRSDYVDA LRIGHGICLM NKPNELVMRR TCGNSIVEEG EDCDCGTIDE CHDKDPCCDP ITCKLTTEAE CASGPCCSDC KLRPRGVICR DAVNECDLPE HCSGEDGNCP VDIYKKNGNP CGGNTGYCFN GICPTVNIQC GVVWGYGGIA GDKQCFDQFN SKGSINGHCG IDDNGQYIKC DPENVRCGSL QCKLGNRYPL NGKDQLYSTT IISIKGEEYE CKSTGGTKDS SGNRDMGLVR DGTPCGDNLI CVNQTCTSIF PHIDQGKCPS NHNNLECSGH GVCSNVNKCY CEMGWSGPDC SIQIEMTLPP EHTTARSADM QTTKEGTKVT KKETPYESYH STNTVFLVGM LMLVVGGVFI VFALMALCYR SVVVHKNFSL CLRRKSTVPK YDSPYVKKPM PKKYPGKGPN HNPEEAAMES VNKILTFGSM PSYREHKMQQ LKRMGVGSGS EEDATHSGEE ETVSFIDLPP NNLSKLPEKG ILKKSGPYGT VMGDACKEKW SEDSQSDNQE ILSQSDNNLG PDMMGGGGGA ISEVERTLKS LNGYHEDILE ALRNAASHRG AAMPSSSSSL LSEEILRKSL GSLLHHHGAQ QEEDDDDEVP PSCGPIRIRN LEDLIRQLEH HSARHMSPSG SEDIRMSETE ADRHYRLESA ACSESQSRCR GREEEPRFVY GRYRHPTGRH PPGYHHHHLQ EEEGIYETAD HDRGGDQLCG DTPDSESDEF IQAQQQLVRS ASEE // ID A0A068XJE2_HYMMI Unreviewed; 1788 AA. AC A0A068XJE2; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 23-MAY-2018, entry version 27. DE SubName: Full=Putative adam (A disintegrin and metalloprotease) {ECO:0000313|EMBL:CDS30928.1}; GN ORFNames=HmN_000326000 {ECO:0000313|EMBL:CDS30928.1}; OS Hymenolepis microstoma (Rodent tapeworm) (Rodentolepis microstoma). OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Hymenolepididae; Hymenolepis. OX NCBI_TaxID=85433 {ECO:0000313|EMBL:CDS30928.1, ECO:0000313|Proteomes:UP000017242}; RN [1] {ECO:0000313|EMBL:CDS30928.1, ECO:0000313|Proteomes:UP000017242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nottingham {ECO:0000313|Proteomes:UP000017242}; RX PubMed=23485966; DOI=10.1038/nature12031; RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., RA Sanchez-Flores A., Brooks K.L., Tracey A., Bobes R.J., Fragoso G., RA Sciutto E., Aslett M., Beasley H., Bennett H.M., Cai J., Camicia F., RA Clark R., Cucher M., De Silva N., Day T.A., Deplazes P., Estrada K., RA Fernandez C., Holland P.W., Hou J., Hu S., Huckvale T., Hung S.S., RA Kamenetzky L., Keane J.A., Kiss F., Koziol U., Lambert O., Liu K., RA Luo X., Luo Y., Macchiaroli N., Nichol S., Paps J., Parkinson J., RA Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M., Salinas G., RA Wasmuth J.D., Zamanian M., Zheng Y., Taenia solium Genome Consortium, RA Cai X., Olson P.D., Laclette J.P., Brehm K., Berriman M.; RT "The genomes of four tapeworm species reveal adaptations to RT parasitism."; RL Nature 496:57-63(2013). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN902985; CDS30928.1; -; Genomic_DNA. DR GeneDB; HmN_000326000.1:pep; -. DR Proteomes; UP000017242; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000017242}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Hydrolase {ECO:0000313|EMBL:CDS30928.1}; KW Integrin {ECO:0000313|EMBL:CDS30928.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metalloprotease {ECO:0000313|EMBL:CDS30928.1}; KW Protease {ECO:0000313|EMBL:CDS30928.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000017242}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 1788 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001657429. FT TRANSMEM 859 883 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 258 492 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 489 593 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 770 802 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 565 585 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 774 784 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 792 801 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1788 AA; 195209 MW; 4BF2B350C7290173 CRC64; MVDSSLLLLV TIITSWKLVL SQNNPGNYFN SPPISRDKHP AFTIGCDCFS VPDCFSNCSS VPDLLPLLRK SSQFLQTFPT PFSVTRPQQF RKRSFKFDTS TANKRSYFSQ AQFRLKLFGI PDAIQIKVRK SSVFSRDGEY LTLSYRDRNG IISEVESTKL EDCFYTGEVD SANSSYVAVD TCSGLRGAIF YRNTTYVILP LSCPSCEPQI SPHIVLPWSP SPIAQNASMR TFWQPVDVMA LMQKALDSGL PDPTNAMHDI WLEFIVDQNM LWEFNGSSTI TIRYVASVVN LVNLHFRDLP LRIHLLRTQI WNLGNRAPIE SSIKATLNSI QRYRADQTSS VHLNMNRRSR RDLDSDAEDN EFQEPSQAVY KQPGSRKADI TMLLTDAEKM EFVEGVDHLA VPGSICTPRA TAVVRVNVTD FEFRVASLVS RSIAEILGIH SFSCPELYSC SEDEVFSRGD VSRLRLALLS EMSACLRSSN LQAEESLHSD TCGNGIIDRG EECEPYQQGL PIGLPQSSDG SFNKSLNSPA FGCCDPKTCL ADVNAVCVTG GCCRSCQLVA RGRLCRPARD QCDLPEFCSG ADPECPADLY LENGMRCKGV GKNNDVEEGL CYEGRCPTRS SHCKALWGPN ARTADDYCYT NMNKKIDSAC GNGVVCEGDN TMCGLLHCQN GNDEPALPEA RSLSFFNLRT QNENQKIHCQ YVASTQKFSY VPEGASCNEG RFCFQNRCIK PTGIAVHSKC PKGSYLGPLQ DGVNADFIHP AVRRSLPVFT NSPVNITCAG RGICTNGAFC LCPPGWHGPS CTQRQPPANQ NSSLIKQSVG NIHASVYPDE DIASLIWMYI QTIDKSPEGN TEPAPGNTVF LVAILGAVIA CVFFCLCAII FLYRRRNMHK RDFHHLNKRA FNSNQTRMSP PLFDSKSPGQ GTASTTAANS MDSMCLCNRN SRPGGASLDD MELHYHSRHS RNRRHRHGSK NRNRRRKRGG NSSGDSLQAG NNGAIESGPE LGGRDDSVKE GKIKFGSMPS YREDKMKNAR NGEASGGTVV GTTTNETTVV TNSSTVTTGA HLPPPPPLID FSAAWSIPPP PPPLQQAFVM QSSSGNQVYV QQPPVSWMSP NMSAAVTSTG MTVNMTPPMS SPMQMLASSR MEGGSNGEIM SVQSTRKAMT TSTISTEETE QPVPQVTVIR ENSSRQPEKG ILKNKHEGTG VDLADSTNVN SSSSKRRKHS SKRTLSKKHR CGSSMSSTSS STSSSVSRSR SPSSGSSTGS TSSSLSSASS YSTSRATDDT NSTNFVTSAT NSGDEEGGER SGLISDSAST CSTARETGGK CKRKSHRHKR RQSKRKSSPG HRSHSHGHHH HGGHPNRRHQ QSSEEISTNN TSTTPPTTTT ASTSSNSSPC HRRCHRRRRT GTSRRYRMSS EEAESSIGIQ NHKVPTILCN AEQQTDEISL VRASGIIFES GQNDHQSFNP SKDAHHGGMT NYHHQQLNSS SNQQERELQS PTDQEDSEWE EVECTGGSDC EECRKNAAGG VGLANASTST NNGNAAVAIS SWNPSSAVPP TPPSAGGLLS RQYKLPSPPP LPPVASTTYY CTTQLSPQGE IDPYYQPPTE DGDSYIGEKT SLVPHLKYPG HTEEDDGLIS NRGNQGSGLP MNSSLNTPND CYMMKDSDGL TRKNSPGMPY IARHNYQGSD SDFSLPNSVK KSPTPGHHQT SISSGWLSPS NNLANSQPTT NHLDTSSHHQ WLDVAESDAS SLPDASCDLV HLAQLSHAAR INPNLSDLAR QQERIRLGAD VSYYSKQL // ID A0A068Y1Y5_ECHMU Unreviewed; 1788 AA. AC A0A068Y1Y5; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 28-FEB-2018, entry version 25. DE SubName: Full=Adam {ECO:0000313|EMBL:CDS36387.1}; GN ORFNames=EmuJ_000347500 {ECO:0000313|EMBL:CDS36387.1}; OS Echinococcus multilocularis (Fox tapeworm). OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Taeniidae; Echinococcus. OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS36387.1, ECO:0000313|Proteomes:UP000017246}; RN [1] {ECO:0000313|EMBL:CDS36387.1, ECO:0000313|Proteomes:UP000017246} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Java {ECO:0000313|Proteomes:UP000017246}; RX PubMed=23485966; DOI=10.1038/nature12031; RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., RA Sanchez-Flores A., Brooks K.L., Tracey A., Bobes R.J., Fragoso G., RA Sciutto E., Aslett M., Beasley H., Bennett H.M., Cai J., Camicia F., RA Clark R., Cucher M., De Silva N., Day T.A., Deplazes P., Estrada K., RA Fernandez C., Holland P.W., Hou J., Hu S., Huckvale T., Hung S.S., RA Kamenetzky L., Keane J.A., Kiss F., Koziol U., Lambert O., Liu K., RA Luo X., Luo Y., Macchiaroli N., Nichol S., Paps J., Parkinson J., RA Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M., Salinas G., RA Wasmuth J.D., Zamanian M., Zheng Y., Taenia solium Genome Consortium, RA Cai X., Olson P.D., Laclette J.P., Brehm K., Berriman M.; RT "The genomes of four tapeworm species reveal adaptations to RT parasitism."; RL Nature 496:57-63(2013). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN902849; CDS36387.1; -; Genomic_DNA. DR GeneDB; EmuJ_000347500.1:pep; -. DR Proteomes; UP000017246; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000017246}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000017246}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 1788 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5009741457. FT TRANSMEM 863 887 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 263 496 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 493 597 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 569 589 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 1788 AA; 194151 MW; 69987FBEB2F4699E CRC64; MSYLAIFCVA VILCCTPLIL SITAQNTPES YLNSPSNHHS KLSSSFRIGC DCYSVPNCFT NCSDVSGLLP QLQASSQFLQ SLPTPFCITR LEQLRKRGPK FDTSTANKRS YYSQAQFHLT LLGHAEPIQI KIRKSSVFNG GEEYSTLFYR NRNGVVSEVE FTKSEDCFYT GEVESAPNAS FVAVDTCSGL RGAIYYHNTT FVILPLPCPS CDPQTAPHIV LSWSSAPIAQ NASMRTFWKP VDLMAMMQET VDQRLADLSS TVHTIWLEFI VDEKLLHQFS GKFTTTLRYV ASMVNLVNLH FRDLPVQFHL LRTQIWNLGN LASIESSIKA TLNNFQRYRS EQSFGDKIGQ RRSRRDLDEG ETNDPHSSSP QGVFKQPGSR KADITMLLTD SAEIDFVEKV DHLAIPGSIC TPRGTAIVRV NVTDFELQVA TLVSKSIAEI LGIHSILCPE MYSCNENEVF SLGDISRLQL ALLSGMSACL RSPNLQGREF LRPDTCGNGI IDRGEECEPY QQGLPIGLPH STDSGFNKSL NSPAFGCCDS KTCLADVHAV CVEGGCCRGC RLVARGRLCR PARDQCDLPE FCSGSEAECP GDLYLENGMP CKGEKNDFEE EALCYEGRCP TRSSHCKALW GPNARTADDY CYSTMNRNID SACGKGVVCE EEDAMCGLLH CQNGSDEPLP VEARLLSFFN LRTQHEQQKI QCQYVASTRK FSYVPEGASC NEGRFCFQKR CIKPTAIVVH SKCPKGPFSD LWGVSDGSND YIHPAVRGSL PTATATPINI TCSGRGICTN GAFCLCPPRW HGPSCSQHQP SINPNASVTK PRVKVAYVSV YPDEDIASLI WMYIQAMDKN AEGLVEPGSV NTVYLISILA AVIACVFLCL CGIIFLYRRR NFNSRGLRFG AKSERCLSSP TNRFSPALFD SPLSKSSGTA TATTTAANSM DSMCLCNRNS RPSGASLDDM ELHYHTLRSS CSRRHRHTAS SSSSKNRNRR QKRGGGASSG DSLQTGANGT VESGPELGRN GEESVKDEGG NGVGKIKFGS MPSYREDKMK HAKDNATSTT ISDTAGISTI TDAVVTTTST TNNLFQQQQP ALMDFSASWS LPPPPPPPFV VPAVCSVVAS PNPIFAGSSS PWMSTPQTPL STSTNINTTT TTCANVICTD VGGMEVRVMS AQSSRKVMTT STISADEAET PQVTVIRENS CRQPEKGILK NKHEGGGGVD MPDLPTSTNG EGGSKKQEHS LKRSGKKHYC SSPHFSGTTS STSSSSTSTT GSQSLSASST GSSSSSLSSV SYCSTSRATD DTNSTNFVAS AMNSGEEEEG GVMDMVSDSG STCSTALETG EEERKMGGRE CRHKNHRQHK SQCKKKSSHR QHSHAHSHHR RHSHSHHRRS QRSSSTGGDT SAANTSTPPT TTTASTSSTS SPCHRRCHRR RRTGVSRRYR FSSEDAESSI GGQNHKVPTI LCNAEQQTDE ISLARAMGAI FPTPQKDLRS PSPLKDLQNS NSSNLQQQQQ LSSDVIDEED SEWEEVECTG GSDCEECRKN AAISWNSSAV PPTPPSAGGL LSRQYKLPSP PPLPPVIVTS TPYYCTTQLS SQSDIDPYYQ PPIDDTDSFV AGKPGLVSHR KYPGHAEEDD GLISSRGTQG GLTLTSSLNA PSDCYMTRDS DGLTRKTSPA VPYVSRHNYN GSDSDFSLST SVKKSPTLGH TVDWLSSGNS SQIGGLSNHV SATVAATAHQ WLDMAESDAS SLPDASCDLV HLAQLSHAAR MNPNLSDLAR QQERIRLGTE APFYSKQP // ID A0A077Z5D1_TRITR Unreviewed; 615 AA. AC A0A077Z5D1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 23-MAY-2018, entry version 25. DE SubName: Full=ADAM CR and EGF 2 and Pep M12B propep and Disinte grin and Reprolysin domain containing protein {ECO:0000313|EMBL:CDW55341.1}; GN ORFNames=TTRE_0000361301 {ECO:0000313|EMBL:CDW55341.1}; OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichuridae; Trichuris. OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW55341.1, ECO:0000313|Proteomes:UP000030665}; RN [1] {ECO:0000313|EMBL:CDW55341.1, ECO:0000313|Proteomes:UP000030665} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A., RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z., RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.; RT "The whipworm genome and dual-species transcriptomics of an intimate RT host-pathogen interaction."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG805948; CDW55341.1; -; Genomic_DNA. DR Proteomes; UP000030665; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030665}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000030665}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DOMAIN 147 351 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 354 406 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 556 588 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 281 281 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 285 285 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 291 291 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 560 570 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 578 587 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 615 AA; 69497 MW; 921BA8357779A4A0 CRC64; MLQRPRVLAP ADAKFTVFSK SYGLDNLVEQ NLKECLYHGE VVGRSRSSVA LSTCNGLSGT VILERNVYMI SPMKHRVSTT LSSHPHLFIR LRNDYESFCV PRERGRNQSS NPTYVLEHLV NNNETRVCRK IKGHNLKKYR TLRGRSRYLE LSVLVEKEMI EWKNVSNTDL FRYLLDCVNT LDLFLRQINV RVSLVHVELW TQENRIDVTS DDVSTLENLV KFSMNNSDDT AQDVTFLLTV SGENTSQIAV YPKSVCTVNA TGLIRAILKD HPVYISLLMT HGIGHILGLR HENSDKRNAE KDFLSIMGTP CRINNARRDK YRRAYLFTEC TKHEFTRLLN SNRADCLFNM PLQECESIDP CCDFMSCKLK RGAQCSQGPC CEKCKFVSSG KLCRPGKDAD CDFPEFYAYK PDGTACGDNK DRYCYNGKCV DADERCRKIN SEFMMADDFC YRKYNLVGSN VGRCSLDLSM KRVACTDKNY QCGMLICKRK VHLQGTGLPR DLNFTKDTNA FNCSNAVLLN FTLVEDGTKC GSNGLCEEQA CVSADTMLKR VSCSGEDEES SLPCNGHGTC TNLNTCSCDE GWEGSDCSFM SEDPKAGNDS VPFPTWDYES GITLY // ID A0A087YEJ0_POEFO Unreviewed; 951 AA. AC A0A087YEJ0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 2. DT 23-MAY-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000016443}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016443, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000016443, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000016443}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000016443} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYCK01006469; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_007556213.1; XM_007556151.2. DR Ensembl; ENSPFOT00000016465; ENSPFOP00000016443; ENSPFOG00000016101. DR GeneID; 103140831; -. DR CTD; 53616; -. DR GeneTree; ENSGT00910000144014; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 951 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001834387. FT TRANSMEM 739 762 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 242 441 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 447 534 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 678 715 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 506 526 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 705 714 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 951 AA; 105006 MW; 9973BF8F05E70396 CRC64; MMLRMPWWIS LLCVCGLMHV GHQSSLDASN GDALSSLEAL RDAGRFVGKE NTVPLRLVYS SQNHSQITHD ELSTRVKASP DSTQMEHVIQ ATFQVDAFGK TFILDVELNH DLLSSGYQER HLSENGKIVV TKGGEHCYYQ GRVRDAPRSF AALSTCHGLH GMFFDGNHTY MIEPGGQASN SGDLQVHLIY KSAGQEELSD FFGGDLPEPP FPSPPFPESK VVHWRKKRQA PRLSRSVEDE TKYIELMVIN DHVMYKKHRL SVGHTNNNAK TVVNIADMIF REQLNTQIVL VAMETWSVDN KFNIDDDPMV TLKEFMKYRK DFIKEKCDSV HLFSGNQFHS NRGAVSYTGG VCSLTKGGGV NEYGKTNEMA ITLAQSLGQN IGIFSDKKRI LNGECKCDDR WAGCIMDDVG FYLPKKFTDC NVEEYHNFLN SGGGACLFNK PRKLLDPPEC GNGILEAGEE CDCGSTEECA KEGENCCKNC TLTKGSNCSN GLCCRNCQME VVGVLCRDAV NDCDIPEKCT GNSSQCPPNV HKMDGYTCEK DQGRCFNGRC KTKDRQCKYI WGEKATAADK FCYEKLNIEG TEKGNCGKEK DTWIQCNKQD VHCGYLLCSN ISPAPRLGDL QGGLTSFSVA QHGAPLDCSG AHVLIDGDTD LGYVEDGTAC GTDSICLDHK CLPIEQFNFS TCPGTTDKTI CSGHGVCSNE LRCVCELGWT GDDCYSRSPF SNLVVGPTAP VSGITSTNII IGAITGSILF LALILAVTAW CYKSYKKRRY AESEVHRRFC RQIPPGDYVT KPGDADSFYS DMPPGVSTNS GCSSKKRSAC LSHLQICTLS FTPSFPSISQ NFSVFGFRSN GLSHSWSERI PDAKHITDIC ENGRPRSNSW QGNLSGNRKK LKGKKFRARS NSTETLSPAK SPTSSTGSIA SSRRYPYPMP PLPDDQRKAN RQNARLWETS I // ID A0A087ZSV8_APIME Unreviewed; 1433 AA. AC A0A087ZSV8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 23-MAY-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:GB41900-PA}; OS Apis mellifera (Honeybee). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Apoidea; Apidae; Apis. OX NCBI_TaxID=7460 {ECO:0000313|EnsemblMetazoa:GB41900-PA, ECO:0000313|Proteomes:UP000005203}; RN [1] {ECO:0000313|Proteomes:UP000005203} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DH4 {ECO:0000313|Proteomes:UP000005203}; RA Wu J.L., Liu J.H., Yuan Y.N., Qiao L.Y., Liu W.Z.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:GB41900-PA} RP IDENTIFICATION. RC STRAIN=DH4 {ECO:0000313|EnsemblMetazoa:GB41900-PA}; RG EnsemblMetazoa; RL Submitted (JAN-2017) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblMetazoa; GB41900-RA; GB41900-PA; GB41900. DR Proteomes; UP000005203; Linkage group 8. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005203}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000005203}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 797 819 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 848 870 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 270 474 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 480 568 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 714 751 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT COILED 1306 1331 {ECO:0000256|SAM:Coils}. FT METAL 408 408 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 412 412 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 418 418 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 540 560 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 741 750 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1433 AA; 160144 MW; 849F4F52CBB72913 CRC64; MERFRNGIAA FCLRPIYQTV ELAATSSTNE ADYTLDDSFW NEETSVGEAE RLLQEYRQNQ ELVQNIGAHY YQIIYPVQLR HHEKMGISTR EVSVSKFPQR GYGEGGYQNV KGRMRTGRHF HRTSLLIKAF NHKFRLDLEL NTQLLAPNLV QKDFLTVGAE QTSKQEIEHC YYHGTVRDYP GASAAFHTCN GVSGVIHLGN ETFVIHPFYG GDLSQKHPHV IFEARTKANK GCANSGNLEW RVKNRRQKHV LGLSETTSDR YKRDVRETTK YIETAIIIDK AMFEKRNGST RAEVVHDAIQ VANIADMYFR TLNTRVSVIY IETWQGINQA EIATGMDIDL ALLNLNDYMM RTMFRVPRDT TQLLTGETFA GGESGVAIPS TICKQKSVGI SVDLNTYEPH LLAGTMAHMI GHNIGMSHDD GRSECICREW HGCIMAQSIV GLENVQPYTF SECSKTDYIE VLRSGNGFCL LNKPNEVEVR RSCGNRVIDE GEQCDCGSIE ECHEYDPCCD PITCRLTSEA QCATGPCCSD CKLLARGVVC RESTNECDLP EVCTGETGQC PTDVYKKNGN PCSNNDGYCY NGVCPALNLQ CEQIWGYGGV AADQQCFEQF NSKGSLSGHC GTDSSGHYIK CELENVRCGS LQCQQGRKLP TVAGIDHSRT IISIKGEEYE CKSTTGKVEG SEMPGMGLVR DGTSCGDNLI CVNQTCMSLY PLIGNERCPS NHNNHECSGN GVCTNLNNCY CNLGWSGPDC SIEQDIPTRP PITSSTEAAG KNGTDTKLVK KETPYETTNN TLSTGTMVLI LVGVVKGVFI CFALMAVCYR YSSKKIKFLS GFDQRLSLSK NYHGSNTVFL VGVLMSVVGG VFIVFALMAL CYRSVVVHKN YSLCLRRKST VQKYDQPYVK KPPQRGYSGV SGNHHPGHAV LDNVNNKILT FSSMPNCSRG ETQRVVFRPP NNVATADGPR VKEHKSQVKR PGMSEEDGDT GADEVVSFID LPNNLTKLPE KGILKKHGGY GMGGGAVASV ERTLDQLNGY HEHIIEALRM AANQRETSGT TSAPMDDEAL TEPLTELLTE PLPECYPTDS YRKDIIKHID NQADEEYEEY VPSCGVIRIR NLEDLIKQLE RHSARNRSPS GSEDMRMSES EADRPYRKDS SVCSESSQGS RRCSRGRDDT YGRYCQPSSR SPYGTHQHTQ HSHQMYKEEG IYATADPDRG SNTRGETPDS ESDAFIQAQQ LARRTSEDGV QHRPPQQPPP PPPPPPPAMT GSTVQLLQLH HSQREHRQQP QQQHHCHHHA QQSQPQQQQQ PQPSSQQQHQ RQQQQQQQQQ QQQQQQQQQQ HQLPVEQLPI QQRGYYPSPP YTDNGLENDE TENAQSHQQQ KLPDVRGIDV NHLPNINKCP LDDNFSLDCN INNGSPKELN TNNTSDNENT ALLPPSHFPE YKH // ID A0A093C4K9_9AVES Unreviewed; 621 AA. AC A0A093C4K9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 23-MAY-2018, entry version 25. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 {ECO:0000313|EMBL:KFV07989.1}; DE Flags: Fragment; GN ORFNames=N339_08897 {ECO:0000313|EMBL:KFV07989.1}; OS Pterocles gutturalis (yellow-throated sandgrouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; OC Pterocles. OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV07989.1, ECO:0000313|Proteomes:UP000053149}; RN [1] {ECO:0000313|EMBL:KFV07989.1, ECO:0000313|Proteomes:UP000053149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV07989.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL234568; KFV07989.1; -; Genomic_DNA. DR MEROPS; M12.209; -. DR Proteomes; UP000053149; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053149}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KFV07989.1}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000053149}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DOMAIN 147 341 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 349 436 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 575 609 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 283 283 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 282 282 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 286 286 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 292 292 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 300 305 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 408 428 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 599 608 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFV07989.1}. FT NON_TER 621 621 {ECO:0000313|EMBL:KFV07989.1}. SQ SEQUENCE 621 AA; 68511 MW; AD07A4EC907C1E9E CRC64; DKVSYAIEIE GNEYTIHLEK NKELLPKDFT VYTYSKEGKL QSEYPDVQDH CHYQGYVEGT LDSVVAVSTC SGLRGLVTIG NVTYGIEPMD SSSDSKHILY RLDNVKKEPT MCGVTTEDHE MEHTEENHHP SMTQLLRRKR AVLHQTRYVE LFIVVDKEKF EDFGKSETDV REHMVQLANY LDSMYIMLNI RIVLVGLEIW KYDNIISTDG GAGDVLANFV QWREKNLVLR RRHDSAQFVL KKGFGGTAGM AYVGTVCSKS HAGGINVFGR ISIQMFASIM AHELGHNLGM NHDDERVCHC GASSCIMSSG ASGSRNFSSC SAEDFEKLTL NKGGSCLLNV PRPDETYSVP YCGNKLVDAG EECDCGSPKE CESDPCCEPG TCRLRAGAEC AYGDCCKNCR LLPGGTECRA SNNECDLPEY CNGTSQFCQP DFTIQNGHPC HNEEAYCYNG VCQYYDAQCQ DIFGPKAKAA PNICFAEVNS KGDRFGNCGF HGHDYKKCSS WNAMCGKLQC ENVKTMPVFG IKPAIIQTPI RGTTCWGVDF QLGSDVPDPG MVNEGTKCDT GKICRHFQCV SASVLNYDCD VEKQCHGHGV CNNNGNCHCE PGWAPPYCDT KGYGGSVNSG P // ID A0A096MIE1_POEFO Unreviewed; 875 AA. AC A0A096MIE1; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 23-MAY-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000031182}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000031182, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000031182, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000031182}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000031182} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYCK01006469; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000029053; ENSPFOP00000031182; ENSPFOG00000016101. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 712 735 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 215 414 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 420 507 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 651 688 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 479 499 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 678 687 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 875 AA; 96944 MW; 1D7D57C027CC6C67 CRC64; CAQAGDALSS LEALRDAGRF VGKENTVPLR LVYSSQNHSQ ITHDELSTRV KASPDSTQME HVIQATFQVD AFGKTFILDV ELNHDLLSSG YQERHLSENG KIVVTKGGEH CYYQGRVRDA PRSFAALSTC HGLHGMFFDG NHTYMIEPGG QNDVTKGDLQ VHLIYKSAGQ EELRDLPEPP FPSPPFPESK VVHWRKKRAK KQAPRLSRSV EDETKYIELM VINDHVMYKK HRLSVGHTNN NAKTVVNIAD MIFREQLNTQ IVLVAMETWS VDNKFNIDDD PMVTLKEFMK YRKDFIKEKC DSVHLFSGNQ FHSNRGAVSY TGGVCSLTKG GGVNEYGKTN EMAITLAQSL GQNIGIFSDK KRILNGECKC DDRWAGCIMD DVGFYLPKKF TDCNVEEYHN FLNSGGGACL FNKPRKLLDP PECGNGILEA GEECDCGSTE ECAKEGENCC KNCTLTKGSN CSNGLCCRNC QMEVVGVLCR DAVNDCDIPE KCTGNSSQCP PNVHKMDGYT CEKDQGRCFN GRCKTKDRQC KYIWGEKATA ADKFCYEKLN IEGTEKGNCG KEKDTWIQCN KQDVHCGYLL CSNISPAPRL GDLQGGLTSF SVAQHGAPLD CSGAHVLIDG DTDLGYVEDG TACGTDSICL DHKCLPIEQF NFSTCPGTTD KTICSGHGVC SNELRCVCEL GWTGDDCYSR SPFSNLVVGP TAPVSGITST NIIIGAITGS ILFLALILAV TAWCYKSYHH NRSNGLSHSW SERIPDAKHI TDICENGRPR SNSWQGNLSG NRKKLKGKKF RARSNSTEYL TPRNKSEFYD VTKWVEDVNK NTQGPFLRTL SPAKSPTSST GSIASSRRYP YPMPPLPDDQ RKANRQNARL WETSI // ID A0A096P637_PAPAN Unreviewed; 769 AA. AC A0A096P637; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 23-MAY-2018, entry version 26. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSPANP00000020812}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSPANP00000020812}; 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 {ECO:0000313|Ensembl:ENSPANP00000020812, ECO:0000313|Proteomes:UP000028761}; RN [1] {ECO:0000313|Ensembl:ENSPANP00000020812, ECO:0000313|Proteomes:UP000028761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., RA Aqrawi P.A., Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., RA Bandaranaike D.B., Battles P.B., Bell A.B., Beltran B.B., RA Berhane-Mersha D.B., Bess C.B., Bickham C.B., Bolden T.B., RA Carter K.C., Chau D.C., Chavez A.C., Clerc-Blankenburg K.C., RA Coyle M.C., Dao M.D., Davila M.L.D., Davy-Carroll L.D., Denson S.D., RA Dinh H.D., Fernandez S.F., Fernando P.F., Forbes L.F., Francis C.F., RA Francisco L.F., Fu Q.F., Garcia-Iii R.G., Garrett T.G., Gross S.G., RA Gubbala S.G., Hirani K.H., Hogues M.H., Hollins B.H., Jackson L.J., RA Javaid M.J., Jhangiani S.J., Johnson A.J., Johnson B.J., Jones J.J., RA Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., Kovar C.K., RA Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L., RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L., RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M., RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N., RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O., RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., RA Perez Y.P., Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., RA Rouhana J.R., Ruiz M.R., Ruiz S.-J.R., Saada N.S., Santibanez J.S., RA Scheel M.S., Schneider B.S., Simmons D.S., Sisson I.S., Tang L.-Y.T., RA Thornton R.T., Tisius J.T., Toledanes G.T., Trejos Z.T., Usmani K.U., RA Varghese R.V., Vattathil S.V., Vee V.V., Walker D.W., RA Weissenberger G.W., White C.W., Williams A.W., Woodworth J.W., RA Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., Nazareth L.N., RA Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.; RT "Whole Genome Assembly of Papio anubis."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPANP00000020812} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHZZ02010457; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPANT00000014536; ENSPANP00000020812; ENSPANG00000021280. DR GeneTree; ENSGT00910000144014; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000028761; Chromosome 16. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028761}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028761}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 700 709 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 769 AA; 83541 MW; CA501DA9AED09D8B CRC64; MRLLRRWAFA ALLLPLLPPP GLGTQGSAGA LRWGRLPQLG GPGAPEVTEP SRLVRESSGG EVRKQQLDTR VRQEPPGGPP VHLAQVSFVI PAFNSNFTLD LELNHHLLSS QYVERHFSRE GTTQHSTGAG DHCYYQGKLR GNLHSFAALS TCQGLHGVFS DGNLTYIVEP QDMAGPWGAP QGPLPHLIYR TPLLPDPLGC RELGCLFAVP AQSAPPNRPR LRRKRQVRRG HPTVHSETKY VELIVINDHQ LFEQMRQSVV LTSNFAKSVV NLADVIYKEQ LNTRIVLVAM ETWADGDKIQ VQDDLLETLA RLMVYRREGL PEPSDATHLF SGRTFQSTSS GAAYVGGICS LSRGGGVNEY GNMGAMAVTL AQTLGQNLGM MWNKHRSSAG DCKCPDIWLG CIMEDTGFYL PRKFSRCSID EYNQFLQEGG GSCLFNKPLK LLDPPECGNG FVEAGEECDC GSVQECSRAG GNCCKKCTLT HDAMCSDGLC CRRCKYEPRG VSCREAVNEC DIAETCTGDS SQCPPNLHKL DGYYCDHEQG RCYGGRCKTR DRQCQALWGH AAADRFCYEK LNVEGTERGS CGRKGSGWVQ CSKQDVLCGF LLCVNVSGAP RLGDLVGDIS SVTFYHQGKE LDCRGGHVQL ADGSDLSYVE DGTACGPNML CLDHRCLPAS AFNFSTCPGS GERRICSHHG VCSNEGKCIC QPDWTGKDCS IHNPLPTSPP TGETERYKGP SGTNIIIGSI AGAVLVAAIV LGGTGWGFKN IRRGRSGGA // ID A0A0D9RJ34_CHLSB Unreviewed; 902 AA. AC A0A0D9RJ34; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 28-MAR-2018, entry version 19. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSCSAP00000008623}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSCSAP00000008623}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000008623, ECO:0000313|Proteomes:UP000029965}; RN [1] {ECO:0000313|Ensembl:ENSCSAP00000008623, ECO:0000313|Proteomes:UP000029965} RP NUCLEOTIDE SEQUENCE. RA Warren W., Wilson R.K.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAP00000008623} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2015) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQIB01018764; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AQIB01018765; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AQIB01018766; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AQIB01018767; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCSAT00000010529; ENSCSAP00000008623; ENSCSAG00000012435. DR GeneTree; ENSGT00910000144014; -. DR OMA; TRDRQCK; -. DR Proteomes; UP000029965; Chromosome 21. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000029965}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000029965}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 704 727 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 206 405 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 411 498 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 470 490 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 902 AA; 100888 MW; 0CA9504A5F5FC002 CRC64; MELEKRKENR FLERQSIVPL RLIYRSGGED ETRHDALDTR VRGDPGGRQL THVDQASFQV DAFGTTFILD VVLNHDLLSS EYVERHIEHG GKTVEVKGGE HCYYQGHIRG NPASFVALST CHGLHGMFYD GNHTYLIEPE ENDTTQEDFH FHSVYKSRLF EFPLDDLPSE FQQVNITPPK FILKPRPKRS KRQLRRYPRN VEEETKYIEL MIVNDHLMFK KHRLSVVHTN TYAKSVVNMA DVIYKDQLKT RIVLVAMETW ATDNKFAMSE NPLITLREFM KYRRDFIKEK SDAVHLFSGS QFESSRSGAA YIGGICSLLK GGGVNEFGKT ELMAVTLAQS LAHNIGIISD KRKLASGECK CEDTWSGCIM GDTGYYLPKK FTQCNVEEYH DFLNSGGGAC LFNKPSKLLD PPECGNGFIE TGEECDCGTP AECVLEGAEC CKKCTLTQDS QCSDGLCCKK CKFQPMGTVC REAVNDCDIR ETCSGNSSQC APNIHKMDGY SCDGVQGICF GGRCKTRDRQ CKYIWGQKVT ASDKYCYEKL NIEGTEKGNC GKDKDTWIQC NKRDVLCGYL LCTNIGNIPR LGELDGEITS TLVVQQGRTL NCSGGHVKLE EDVDLGYVED GTPCGPQMMC LEHRCLPVAS FNFSTCLSSK EGTICSGNGV CSNELKCVCN RHWIGSDCNT YFPHNDDAKT GITLSGNGVA GTNIIIGIIA GTILVLALIL GITAWGYKNY REQRQLPQGD YVKKPGDGDS FYSDIPPGVS TNSASSSKKR SNGLSHSWSE RIPDTKHISD ICENGRPRSN SWQGNLGGNK KKIRGKRFRP RSNSTEYLNP WFKRDYNVAK WVEDVNKNTE GPYFRTLSPA KSPSSSTGSI ASSRKYPYPM PPLPDEEKKV NRQSARLWET SI // ID A0A0D9S0Q7_CHLSB Unreviewed; 769 AA. AC A0A0D9S0Q7; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 23-MAY-2018, entry version 24. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSCSAP00000014446}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSCSAP00000014446}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014446, ECO:0000313|Proteomes:UP000029965}; RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014446, ECO:0000313|Proteomes:UP000029965} RP NUCLEOTIDE SEQUENCE. RA Warren W., Wilson R.K.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAP00000014446} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2015) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQIB01145663; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_008010586.1; XM_008012395.1. DR Ensembl; ENSCSAT00000001635; ENSCSAP00000014446; ENSCSAG00000003607. DR GeneID; 103243313; -. DR KEGG; csab:103243313; -. DR CTD; 4185; -. DR GeneTree; ENSGT00910000144014; -. DR KO; K16067; -. DR OMA; ICSHHGV; -. DR Proteomes; UP000029965; Chromosome 16. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000029965}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000029965}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 769 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002346052. FT TRANSMEM 735 758 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 673 710 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 700 709 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 769 AA; 83541 MW; CA501DA9AED09D8B CRC64; MRLLRRWAFA ALLLPLLPPP GLGTQGSAGA LRWGRLPQLG GPGAPEVTEP SRLVRESSGG EVRKQQLDTR VRQEPPGGPP VHLAQVSFVI PAFNSNFTLD LELNHHLLSS QYVERHFSRE GTTQHSTGAG DHCYYQGKLR GNLHSFAALS TCQGLHGVFS DGNLTYIVEP QDMAGPWGAP QGPLPHLIYR TPLLPDPLGC RELGCLFAVP AQSAPPNRPR LRRKRQVRRG HPTVHSETKY VELIVINDHQ LFEQMRQSVV LTSNFAKSVV NLADVIYKEQ LNTRIVLVAM ETWADGDKIQ VQDDLLETLA RLMVYRREGL PEPSDATHLF SGRTFQSTSS GAAYVGGICS LSRGGGVNEY GNMGAMAVTL AQTLGQNLGM MWNKHRSSAG DCKCPDIWLG CIMEDTGFYL PRKFSRCSID EYNQFLQEGG GSCLFNKPLK LLDPPECGNG FVEAGEECDC GSVQECSRAG GNCCKKCTLT HDAMCSDGLC CRRCKYEPRG VSCREAVNEC DIAETCTGDS SQCPPNLHKL DGYYCDHEQG RCYGGRCKTR DRQCQALWGH AAADRFCYEK LNVEGTERGS CGRKGSGWVQ CSKQDVLCGF LLCVNVSGAP RLGDLVGDIS SVTFYHQGKE LDCRGGHVQL ADGSDLSYVE DGTACGPNML CLDHRCLPAS AFNFSTCPGS GERRICSHHG VCSNEGKCIC QPDWTGKDCS IHNPLPTSPP TGETERYKGP SGTNIIIGSI AGAVLVAAIV LGGTGWGFKN IRRGRSGGA // ID A0A0G2JX23_RAT Unreviewed; 769 AA. AC A0A0G2JX23; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 23-MAY-2018, entry version 24. DE SubName: Full=ADAM metallopeptidase domain 3A {ECO:0000313|Ensembl:ENSRNOP00000070106}; GN Name=Adam3a {ECO:0000313|Ensembl:ENSRNOP00000070106, GN ECO:0000313|RGD:621469}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000070106, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000070106, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070106, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000070106} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070106}; RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC107411; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC132163; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSRNOT00000078085; ENSRNOP00000070106; ENSRNOG00000017554. DR RGD; 621469; Adam3a. DR GeneTree; ENSGT00910000144019; -. DR OMA; TMFSQLN; -. DR Proteomes; UP000002494; Chromosome 16. DR Bgee; ENSRNOG00000017554; -. DR ExpressionAtlas; A0A0G2JX23; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008584; P:male gonad development; IEP:RGD. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 769 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002546899. FT TRANSMEM 691 710 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 187 384 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 395 484 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 620 654 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 340 345 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 456 476 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 644 653 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 769 AA; 85870 MW; 7BA5E53A6EB7A743 CRC64; MLPLFLVLSC LGQLIAVGKD IETPLIQITV PEKIETNIKD AKESETQVTY VIRIEGKAYT LQLEKQSFLH PHFVTNLHNK LGTLQPYFSL VKSHCFYQGH AVEIPASTVT LSTCSGLRGL LQLENVTYGI EPLESSTTLE HILYEIQNHK IDYSPLKENY TNSQDESGSY RILVKPLKSS NSKLRKRILT VKIIMDKGMF DHVGSEVGVA TQKVVQMFGL INTMFSQLKM TVMLNSLEIW SEENKIETNG DADEVLQRFL LWTHKEMPQT TKEITYLLLY KDHPDYVGAT YHGMACNPKF TAGIALHPKT LGVEGFAIVL SQLLGINLGL TYDDIYNCFC RGSTCIMNPS AIHSEGIKVF SSCSMDEFRQ LASQPDLDCL LKTQETEVVA LPQAAKVCGN YILEPPEQCD CGPAERCSHK KCCKSEDCTL LSDAECGSGA CCDKRTCKIA ERGRLCRKST DQCDFPEFCN GTSEFCVADI KAADLEPCNN ETAYCFKGVC QDRDRQCTDL FGKYAKGPNY VCAQEVNLQN DKFGNCHGRC NYSALFCGKA VCYWSFAELV KTDVFDVQYT YLGGQVCVSA HLRVRNDETK DDTYVRDGTI CGNGQVCYRG ECLRVHVLRG DRECEADDKC QGHGICNNQN NCQCEAGFAP PECDMTPSSP GGSMDDGFWL PLDKSTPLVI KRPGTQYKKG LLISFYVFLP FLIVTAIMVV KQNISKMFGQ GEEEFSEGEC QGMVQMFIGY TGHRRSPSPL CHLLTHRSIS EEINDSKQS // ID A0A0M8ZZW1_9HYME Unreviewed; 1343 AA. AC A0A0M8ZZW1; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 23-MAY-2018, entry version 18. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11 {ECO:0000313|EMBL:KOX72939.1}; GN ORFNames=WN51_01869 {ECO:0000313|EMBL:KOX72939.1}; OS Melipona quadrifasciata. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Apoidea; Apidae; Melipona. OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX72939.1, ECO:0000313|Proteomes:UP000053105}; RN [1] {ECO:0000313|EMBL:KOX72939.1, ECO:0000313|Proteomes:UP000053105} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX72939.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:KOX72939.1}; RA Pan H., Kapheim K.; RT "The genome of Melipona quadrifasciata."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ435810; KOX72939.1; -; Genomic_DNA. DR Proteomes; UP000053105; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053105}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KOX72939.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000053105}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 820 844 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 289 493 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 506 594 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 740 777 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 427 427 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 431 431 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 437 437 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 566 586 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 767 776 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1343 AA; 149807 MW; 696F571F13CDE285 CRC64; MAKRQTKKSR ELKAKESEDE TKAKESIIEP VEGDYTLDDS FWNEETSVGE AERLLQEYRQ NQELVQNIGN HYYQIIYPVQ LRHHEKMGIS TREVSVSKYP QRGYGEGGYQ NAKGRIRVKF STRTLDETSF HCILQTGRHF HRTSLLIKAF NHKFRLDLEL NTQLLAPNLM QKDFLANDAE QLFKQEIEHC YYHGTVRDYP GASAAFHTCN GVSGVIHLGN ETFVIHPFYG GDLSKHPHVI FEARTKANKG CANTGNLDWR TKNRRQKHVL GLSETTSDRY KRDVREATKY IETAIIIDKA MFEKRNGSTR AEVVHDAIQV ANIADMYFRT LNTRVSVIYI ETWQGKNQAD ITAGMDIGVA LLNLNDYAMR RMFQVSHDTT QLLTGETFYG GESGVAVPST VCKQKSVGIS VDLNTYEPHL LAGTMAHMIG HNIGMSHDDG RSECICREWH GCIMAQSIVG LENVQPYTFS ECSKTDYIES LRSGNGFCLL NKPNEVRDQG DQVEVRRSCG NRVIDDGEQC DCGSIEECPE LDPCCDPITC RLTSEAQCAS GPCCSDCKLL ARGVVCREST NECDLPEVCT GETGQCPQDV YKKNGNPCSN NAGYCYNGVC PALDLQCEQI WGYGGIAADK QCFEQFNSKG SLNGHCGTDT SGHYIKCEPE NVHCGSLQCQ KGSKQPMIIG IDHSRTIISI KGEEYECKST TGKVEGSEMP GMGLVRDGTS CGDNLICVNQ TCISLYPLIG NEKCPSNHNN NECSGNGVCT NMNKCYCNLG WSGPDCSIQQ DIPTLPPTTS STESAGKNSS DPKLGKKETP YENYHGSNTV FLVGVLMSVV GGVFIVFALM ALCYRRKSTV QKYDQPYVKK PPQRSYMVSG VSGNHHPGHA VLDNVNSKIL TFNSMPNVSR GETQRVVFRP PNSVATADGP RVKEHKSQMK RPGMADEDGD TGPDEVVSFI DLQQNSLKLP EKGILKKHGS YGMERGAVAN VERTLDQLNG YHEHIIEALR MAANQRETSG TTSTGGNAMD DEALTEPLTE LLTEHLPECY PTDTYRKDII KHIDNQADEE YDEYTPSCGI IRIRTLEDLI KQLERHTTRN RSPSGSEDMR MSESEADRPY RKDSSVCSES SQGSRRCSRG RDDTYGRYCQ PSSRSPYGTH QHTQHSHQMY KEEGIYATAD PDRGSNTRGE TPDSESDAFI QAQQLARRTS EDGVQHRPPQ QPPPPPPPPP AMTGSAQQQQ QQEQQQEQQQ HQLPVEQLPI QQRGYYPSPP HIDNGLDNNE AENAQSHQQQ MLPDVRGIDV NHLPNINKCP LDDNFSLDCN INNGSPKELN TNNTSDNENT ALLPPSHFPE YKH // ID A0A0N5DPG3_TRIMR Unreviewed; 1130 AA. AC A0A0N5DPG3; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 31-JAN-2018, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:TMUE_s0038003000}; OS Trichuris muris (Mouse whipworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichuridae; Trichuris. OX NCBI_TaxID=70415 {ECO:0000313|Proteomes:UP000046395, ECO:0000313|WBParaSite:TMUE_s0038003000}; RN [1] {ECO:0000313|Proteomes:UP000046395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Edinburgh {ECO:0000313|Proteomes:UP000046395}; RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D., RA Schwartz K.J., Yoon K.; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000046395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Edinburgh {ECO:0000313|Proteomes:UP000046395}; RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A., RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z., RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.; RT "The whipworm genome and dual-species transcriptomics of an intimate RT host-pathogen interaction."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|WBParaSite:TMUE_s0038003000} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Edinburgh {ECO:0000313|WBParaSite:TMUE_s0038003000}; RG Helminth Genomes Consortium; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|WBParaSite:TMUE_s0038003000} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; TMUE_s0038003000; TMUE_s0038003000; TMUE_s0038003000. DR Proteomes; UP000046395; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000046395}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00517240}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000046395}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 1130 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005896943. FT TRANSMEM 746 770 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 225 428 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 434 523 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT METAL 359 359 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 363 363 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 369 369 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. SQ SEQUENCE 1130 AA; 125242 MW; A91787FA47C3D058 CRC64; MQRVAFVLFL VPLLSHPGLR CVADQWQETD TFAVDPWNKE LIEHLVDDFE IVHPIQLRDR SRVGIDTRNY LFDNVTVHFE QCSFVLKTSY GRLRLHVQLN DVLIPIGAKY RRFLHLDSVA ETSGHSLANC YYQGQVHGHG DSQVALSTCF GLRGSIVLEN NTFLIVPMKG GNLTRRHPHL FMRMRRDEEA TCGNTDSTEW SRRGISRKRP LFRRLRKRDI DIETKFVELS IFVEQRLVNW LNLPSVELFR FLLECVNIVD LMFQQLNVRV SLVHAELWVS TNRISVQREI VPSLLNFVQF LSRESDTLSH DAALLVSTAE LNKAETMSVS DTVCTRRAAG MVKMADKFQP FYTSVLMAHS IGHILGMSHD DGDLECDDAD AFINIMGGLY SFTPSKRSRK IYRFTECSRK DFLALLNSAE DRCLFNQPLQ DNGLAKCGNK VIDEGELCDC GSVDECESVD PCCDAVTCKL KAGAQCASGP CCDKCKFVSN ETICRPSQDA ECDLPEHCAA ISGKCPADSY KIDGSPCGSD QQGYCYAGRC SRAANDCQKI WGPESTVADE ACFRKFNTLG IDFGHCGVDY LGRPIACADR DYLCGLLFCK GGTESPSFPF YFKTQFTEDG NVFECKAFID DKSPVNSSLV RNGAKCGTNK LCKAQSCIHL DQVQQNVDCP TNNVALHCSG HGTCTNLNTC YCDVGWSSID CSFKLNISHA AVVPSVGTDQ HGSALPIPSS SPDHHPSDSS SRLDTYAMLI ILGCVAVGIF LMLLLLLLCY RRRTNFSKAK MVGVTRAEYE RDSNSSTETA NRSIRFGPSR TYRCDVTPTS FGKRPLDQAK EKDGDDEPSI RNKEAVAELL LQTGDDCSNY YVDRPAKCHH SRSLLQRGCD GYESEPAYPV AEGLKVAPRQ CWLQVDTANG RTSINREGCL QVAKGAYESV DGKQTICRSR LNHTAAAIVS PYLYIRNQSL ANNSPSASSI EPKVVVCQKG AVHSEGLDPA MSCRHHHFAS PLLSPSRTAH DGSPDRSQVF RSSPANSTCS TSRLMLKPKP LKLTNIEFLL KQLEHKSANE NGKPIASTSP GSSAELSLPD DDNQPVDENC FISIGDSNEA DKQDNCNGRV SQERSGSLGR VNNRLYTMSE // ID A0A0P7W7F4_9TELE Unreviewed; 632 AA. AC A0A0P7W7F4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 23-MAY-2018, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KPP58622.1}; DE Flags: Fragment; GN ORFNames=Z043_123536 {ECO:0000313|EMBL:KPP58622.1}; OS Scleropages formosus (Asian bonytongue). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala; OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages. OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP58622.1, ECO:0000313|Proteomes:UP000034805}; RN [1] {ECO:0000313|EMBL:KPP58622.1, ECO:0000313|Proteomes:UP000034805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP58622.1}; RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.; RT "The genome of the Asian arowana (Scleropages formosus)."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP58622.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JARO02013595; KPP58622.1; -; Genomic_DNA. DR Proteomes; UP000034805; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000034805}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000034805}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DOMAIN 109 308 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 316 402 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 528 560 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 245 245 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 244 244 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 248 248 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 254 254 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 374 394 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 532 542 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 550 559 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KPP58622.1}. FT NON_TER 632 632 {ECO:0000313|EMBL:KPP58622.1}. SQ SEQUENCE 632 AA; 70582 MW; 3F9D77A8BE058D7F CRC64; EDMPVKSFCL VQDHCYYHGH VQDIKDSSVS VGICSGIRGF VRAKRSVYLI EPLAGSVDGD HAIYRHENLR SRRATCGNTN DTYYDHEPRV SRVYKASGWK SKPMVHEQRF VEMFLVVDNA EYRHYMRDMH VIKARMLEIA NHVDKLYRPM NIRVMLVGLE IWSYMDMFDV SADPDDTLTR FIQWRKNTLL KNTKHDNAQF ITGVDFQGDT VGLANKFAMC RDESGAVNQD HNENPFGVAS TIAHEMGHNL GLSHDATYCD CRTSYLSKNC IMADRVGKNY PETFSSCSQE ELKNFLEKIN PQCLLDKPSP DKLYGGPVCG NAFLEPGEEC DCGTVEECTN PCCNATTCRL TKGSRCAQGE CCESCQFKQA GSLCRSPAHD CDLAEYCTGS RAECPSNAFK MNGLPCNHNQ GYCYNGQCPT LEQHCEKLWG SGSSRSYSLT FDHMLLIVSI APKNLTFQDI KCGKLFCTGG SEFPITRQKA ILWVHGVQCN IVVDQSETED MGMVPTGTKC DHNKVCYENV CQDVQLYATE GCSAKCHNHG VCNHQRQCHC DPGWAPPYCE RKYSDTGKNT VVISVNMPST SGLSNPLFRD ANAKGNPCSR SADISQPTFV ESTFTQPCTP LAVTVPCHPP PE // ID A0A0P7X897_9TELE Unreviewed; 727 AA. AC A0A0P7X897; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KPP70642.1}; GN ORFNames=Z043_110510 {ECO:0000313|EMBL:KPP70642.1}; OS Scleropages formosus (Asian bonytongue). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala; OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages. OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP70642.1, ECO:0000313|Proteomes:UP000034805}; RN [1] {ECO:0000313|EMBL:KPP70642.1, ECO:0000313|Proteomes:UP000034805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP70642.1}; RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.; RT "The genome of the Asian arowana (Scleropages formosus)."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP70642.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JARO02003363; KPP70642.1; -; Genomic_DNA. DR Proteomes; UP000034805; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000034805}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000034805}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 620 643 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 148 347 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 355 441 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 575 607 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 284 284 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 283 283 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 287 287 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 293 293 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 413 433 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 579 589 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 597 606 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 727 AA; 80155 MW; 157F8EEFC5968E0E CRC64; MYPDEQQYSL TIEGKNYTVS LEKNKLLLGS NYTLTSYLEN GSEVTVSPAY RDHCYYHGHI QDVEDSAISV SLCSGIRGFV RAQHQVYLIE PLEGSTEGEH ALYRQEHLRR RRRAACGHSN GTVYDLSPRI SALFKEKPRH LLGPQVTRFV EMFLVVDHSE FKNFGRSMQT TESRMLEIAN HVDKLYRPLN IRVMLVGLEI WTDRDQIDVS PDPDETLTRF LKWRRESLLK KKKHDNAQFV TGVEFDGPTV GLATKFAMCT ESSGAVNEDH NKNPIGVAST IAHEMGHNLG MSHDTASCLC GPSLSSKKCV MSETVGLDYP EFFSTCSQAE LKSFLETTNP SCLLNVPETD QLFGGPVCGN AFVEPGEECD CGTVEECRNP CCNASTCRLA EGAECAEGEC CSQCQFKPAG SLCRNSAGDC DLVEYCTGQV ARCPKDAFKM NGIPCNFNQG YCYNGQCPTL TQHCRRLWGA GAQVAVDACF QQNVRGTKEA YCKKINNDYQ SCAFKDVKCG KIFCTGGNEY PITRHKATLS LGRTRCNSAV DLSEADDLGM VPTGTKCGLG KVCYDNTCQG IEIYGTEGCS AKCNNHGVCN HENQCHCDPG WATPYCNVKL SEFSTDFDIL VVYVTTAVAV FLVLVAGIIV YSMKRKRNLY PRKTKAPHSS GLCNPLFHDS SARGSPSCGT PQISRPTFIE SSVKQKCSPL HITVVPTRPA PEVRAHPSNI LGQLVAQ // ID A0A0V0SKF4_9BILA Unreviewed; 1097 AA. AC A0A0V0SKF4; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRX27327.1}; GN Name=ADAM28 {ECO:0000313|EMBL:KRX27327.1}; GN ORFNames=T07_7593 {ECO:0000313|EMBL:KRX27327.1}; OS Trichinella nelsoni. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX27327.1, ECO:0000313|Proteomes:UP000054630}; RN [1] {ECO:0000313|EMBL:KRX27327.1, ECO:0000313|Proteomes:UP000054630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX27327.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX27327.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDL01000004; KRX27327.1; -; Genomic_DNA. DR Proteomes; UP000054630; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054630}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRX27327.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054630}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 764 788 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 237 439 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 445 533 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 675 712 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 371 371 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 375 375 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 381 381 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 505 525 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 702 711 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1097 AA; 122675 MW; 7B496D3013EC6522 CRC64; MEKLISRRFV SFWESDYLKN LQIIENRSKL QQLRKHPVEC MEEFFKMDSW NKELFEHLVD DFEIVYPVQL RDRGRVGIDT QNYLFDNSTI HFERCSFVIK TSYGRWRIHV QLNDVLIQPA AKYVRYLKLD SPSETSGRSL PNCYYHGQVH GQPKSKVSLS TCFGLRGSIV MENQTFIIIP LKGGDLSRRH PHVFARLKWD DEASCGNTDN TEWSRKRFHR RRPHRRKLRR DVEKEVKYIE LGLFVDRKLH DFLNVGYREM TSYFLEAVNA VDLAFQQLNT RVSLVYFEIW TTENKIGVQR EILPSLMNFI QFSSYEFYNG PFDLALLLTA ADLTTSEMMS AADTVCSARA AGMIKVADKF QPYYLSLLMA HAIGHISGMS HDDSEFDCTN GENFIGIMNN VVSMTSKKNR RVYQFTECNK HDYLELIRSG QGRCLFNFPL QNNALTLCGN KVVDPGEFCD CGSVEECDSV DPCCDAVTCT LRADAQCAEG VCCEKCKFIT NRTLCRPSRD ECDVPEYCSG LSGNCPSDSY KPNGAACGIN RLGICYGGQC RQSDSECQRI WGPNASAADP ACFKKFNTLG IDFGHCGVNE NNKPLPCTEN NAMCGLLFCK GGQEVPNFSL YFKTEFTENG SVYECKVFID NKSPVNYSLI PDGSRCGKSE ACISQNCVPL RSIYQHVDCP TTNTALFCSG HGICTNLNIC HCDAGWTGRD CSVKANFTFE MLSIGESAIS EHGGSSFYGD SEMPVAVSFP DTFPSGDSSK LDTYAMLIIL GCVAIGMILM LALLLLCYRR RANFSKKTKT PTSEKCDFEK ESNSSTETGQ RSIRFGPSRT YKCADEVMTT NKRRTLDQIR ECDERESLSA KSRESANSAE RVTLTMNRLP SRGILKNGPQ SFTCERTAPE WRALLAANRP CDAGYDSEPP YQQSSTFGRY VGVNGGGCWT ASDDGRCPLQ TPNSARLTRG GLYESFNSKQ PRLNQTTAAI VSPYMYVRNR SLLKASPAAL DSFSNANNNN GCCSPSRSRG ADLAAYAVSP ADKQQLSQTR CSTSPCNSTC SSSRGATIQQ PKPLKLTNIE LLLKQLDGAA VLAEPSEDST LPSRRLS // ID A0A0V0U857_9BILA Unreviewed; 1104 AA. AC A0A0V0U857; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRX47496.1}; GN Name=ADAM28 {ECO:0000313|EMBL:KRX47496.1}; GN ORFNames=T05_9701 {ECO:0000313|EMBL:KRX47496.1}; OS Trichinella murrelli. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX47496.1, ECO:0000313|Proteomes:UP000055048}; RN [1] {ECO:0000313|EMBL:KRX47496.1, ECO:0000313|Proteomes:UP000055048} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX47496.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX47496.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDJ01000042; KRX47496.1; -; Genomic_DNA. DR Proteomes; UP000055048; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000055048}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRX47496.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000055048}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 772 796 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 237 439 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 445 533 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 683 720 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 371 371 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 375 375 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 381 381 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 505 525 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 710 719 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1104 AA; 123957 MW; 7C409CDC1BBF4753 CRC64; MEKLISRRFV SFWESDYLKN LQFIENRSKL QQLRKHPVEC MEEFFKMDSW NKELFEHLVD DFEIVYPVQL RDRGRVGIDT QNYLFDNSTI HFERCSFVIK TSYGRWRIHV QLNDVLIQPA AKYVRYLKLD SPSETNGRSL PNCYYHGQVH GQPKSKVSLS TCFGLRGSIV MENQTFIIIP LKGGDLSRRH PHVFARLKWD DEASCGNTDN TEWSRKRFHR RRPHRRKLRR DVEKEVKYIE LGLFVDRKLH DFLNVGYREM TSYFLEAVNA VDLAFQQLNT RVSLVYFEIW TTENKIGVQR EILPSLMNFI QFSSYEFYNG PFDLALLLTV ADLMTSEMMS AADTVCSARA AGMIKVADKF QPYYLSLLMA HAIGHISGMS HDDSEFDCTN GENFIGIMNN VVSMTSKKNR RVYQFTECNK HDYLELIRSG QGRCLFNFPL QNNALTLCGN KVVDPGEFCD CGSVEECDSV DPCCDAVTCT LRADAQCAEG VCCEKCKFIT NRTLCRPSRD ECDVPEYCSG LSGNCPSDSY KPNGAACGIN RLGICYGGQC RQSDSECQRI WGPSEIGYLI FHCLTDVTYL LIKFNTLGID FGHCGVNENN KPLPCTENNA MCGLLFCKGG QEVPNFSLYF KTEFTENGSV YECKVFIDNK SPVNYSLIPD GSRCGKSEAC ISQNCVPLRN IYQHVDCPTT NTALFCSGHG ICTNLNICHC DAGWTGHDCS VKANFTFEML SIGESAFSEH GGSSFYGDSE MPVAVSFPDT FPSGDSSKLD TYAMLIILGC VAIGMILMLA LLLLCYRRRA NFSKKTKIPT SEKCDFEKES NSSTETGQRS IRFGPSRTYK CADEVMTTNK RRTLDQIREC DERESLSAKS RESANSAERV TLTMNRLPSR VILKNGPQSF TCERTAPEWR ALLAANRPYD AGYDIEPPYQ QSATVGRYVG VNGGGCWTAS DDGRCPLQTP NSARLTRGGL YESFNSKQPR LNQTTAAIVS PYMYVRNRSL LKASPAALDS FSNANNNGCC SPSRSRGADL AAYAVSPADK QQLSQTRCST SPCNSTCSSS RGATMQQPKP LKLTNIELLL KQLGGAAVLA EPSEDPTLPS RRLR // ID A0A0V0U8A9_9BILA Unreviewed; 1096 AA. AC A0A0V0U8A9; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRX47497.1}; GN Name=ADAM28 {ECO:0000313|EMBL:KRX47497.1}; GN ORFNames=T05_9701 {ECO:0000313|EMBL:KRX47497.1}; OS Trichinella murrelli. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX47497.1, ECO:0000313|Proteomes:UP000055048}; RN [1] {ECO:0000313|EMBL:KRX47497.1, ECO:0000313|Proteomes:UP000055048} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX47497.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX47497.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDJ01000042; KRX47497.1; -; Genomic_DNA. DR Proteomes; UP000055048; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000055048}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRX47497.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000055048}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 764 788 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 237 439 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 445 533 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 675 712 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 371 371 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 375 375 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 381 381 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 505 525 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 702 711 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1096 AA; 122837 MW; A4B0C20F5BA8C533 CRC64; MEKLISRRFV SFWESDYLKN LQFIENRSKL QQLRKHPVEC MEEFFKMDSW NKELFEHLVD DFEIVYPVQL RDRGRVGIDT QNYLFDNSTI HFERCSFVIK TSYGRWRIHV QLNDVLIQPA AKYVRYLKLD SPSETNGRSL PNCYYHGQVH GQPKSKVSLS TCFGLRGSIV MENQTFIIIP LKGGDLSRRH PHVFARLKWD DEASCGNTDN TEWSRKRFHR RRPHRRKLRR DVEKEVKYIE LGLFVDRKLH DFLNVGYREM TSYFLEAVNA VDLAFQQLNT RVSLVYFEIW TTENKIGVQR EILPSLMNFI QFSSYEFYNG PFDLALLLTV ADLMTSEMMS AADTVCSARA AGMIKVADKF QPYYLSLLMA HAIGHISGMS HDDSEFDCTN GENFIGIMNN VVSMTSKKNR RVYQFTECNK HDYLELIRSG QGRCLFNFPL QNNALTLCGN KVVDPGEFCD CGSVEECDSV DPCCDAVTCT LRADAQCAEG VCCEKCKFIT NRTLCRPSRD ECDVPEYCSG LSGNCPSDSY KPNGAACGIN RLGICYGGQC RQSDSECQRI WGPNASAADP ACFKKFNTLG IDFGHCGVNE NNKPLPCTEN NAMCGLLFCK GGQEVPNFSL YFKTEFTENG SVYECKVFID NKSPVNYSLI PDGSRCGKSE ACISQNCVPL RNIYQHVDCP TTNTALFCSG HGICTNLNIC HCDAGWTGHD CSVKANFTFE MLSIGESAFS EHGGSSFYGD SEMPVAVSFP DTFPSGDSSK LDTYAMLIIL GCVAIGMILM LALLLLCYRR RANFSKKTKI PTSEKCDFEK ESNSSTETGQ RSIRFGPSRT YKCADEVMTT NKRRTLDQIR ECDERESLSA KSRESANSAE RVTLTMNRLP SRVILKNGPQ SFTCERTAPE WRALLAANRP YDAGYDIEPP YQQSATVGRY VGVNGGGCWT ASDDGRCPLQ TPNSARLTRG GLYESFNSKQ PRLNQTTAAI VSPYMYVRNR SLLKASPAAL DSFSNANNNG CCSPSRSRGA DLAAYAVSPA DKQQLSQTRC STSPCNSTCS SSRGATMQQP KPLKLTNIEL LLKQLGGAAV LAEPSEDPTL PSRRLR // ID A0A0V0UY82_9BILA Unreviewed; 1224 AA. AC A0A0V0UY82; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRX56228.1}; GN ORFNames=T09_6046 {ECO:0000313|EMBL:KRX56228.1}; OS Trichinella sp. T9. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX56228.1, ECO:0000313|Proteomes:UP000054681}; RN [1] {ECO:0000313|EMBL:KRX56228.1, ECO:0000313|Proteomes:UP000054681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX56228.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX56228.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDN01000127; KRX56228.1; -; Genomic_DNA. DR Proteomes; UP000054681; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054681}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRX56228.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054681}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 892 916 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 365 567 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 573 661 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 803 840 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 499 499 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 503 503 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 509 509 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 633 653 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 830 839 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1224 AA; 136228 MW; F8BE102CEC8CA645 CRC64; MTSFVLLNST FLTYCRRHIS SRCEALAEII SPFAVCAVSV LALGRPAFFI QARFRCESYS TFCFGFGNSC SVCSSLPASL LCPNGTKSPV GNRASSSVRL IARLTNAFQG FQTGEGRPAG RNWIFGSCRV LDAKPSDIDQ AKSDYLKNLQ FIENRSKLQQ LRKHPVECME EFFKMDSWNK ELFEHLVDDF EIVYPVQLRD RGRVGIDTQN YLFDNSTIHF ERCSFVIKTS YGRWRIHVQL NDVLIQPAAK YVRYLKLDSP SETNGRSLPN CYYHGQVHGQ PKSKVSLSTC FGLRGSIVME NQTFIIIPLK GGDLSRRHPH VFARLKWDDE ASCGNTDNTE WSRKRFHRRR PHRRKLRRDV EKEVKYIELG LFVDRKLHDF LNVGYREMTS YFLEAVNAVD LAFQQLNTRV SLVYFEIWTT ENKIGVQREI LPSLMNFIQF SSYEFYNGPF DLALLLTAAD LTTSEMMSAA DTVCSARAAG MIKVADKFQP YYLSLLMAHA IGHISGMSHD DSEFDCTNGE NFIGIMNNVV SMTSKKNRRV YQFTECNKHD YLELIRSGQG RCLFNFPLQN NALTLCGNKV VDPGEFCDCG SVEECDSVDP CCDAVTCTLR ADAQCAEGVC CEKCKFITNR TLCRPSRDEC DVPEYCSGLS GNCPSDSYKP NGAACGINRL GICYGGQCRQ SDSECQRIWG PNASAADPAC FKKFNTLGID FGHCGVNENN KPLPCTENNA MCGLLFCKGG QEVPNFSLYF KTEFTENGSV YECKVFIDNK SPVNYSLIPD GSRCGKSEAC ISQNCVPLRN IYQHVDCPTT NTALFCSGHG ICTNLNICHC DAGWTGRDCS VKANFTFEML SIGESAVSEH GGSSFYGDSE MPVAVSFPDT FPSGDSSKLD TYAMLIILGC VAIGMILMLA LLLLCYRRRA NFSKKTKTPT SEKCDFEKES NSSTETGQRS IRFGPSRTYK CADEMMTTNK RRTLDQIREC DERESLSAKS RESANSAERV TLTMNRLPSR GILKNGPQSF TCERTAPEWR ALLAANRPCD AGYDSEPPYQ QSSTFGRYVG VNGGGCWTAS DDGRCPLQTP NSARLTRGGL YESFNSKQPR LNQTTAAIVS PYMYVRNRSL LKASPAALDS FSNANNNGCC SPSRSRGADL AAYAVSPADK QQLSQTRCST SPCNSTCSSS RGATMQQPKP LKLTNIELLL KQLDGAAVLA EPSEDPTLPS RRLS // ID A0A0V0UYQ6_9BILA Unreviewed; 1197 AA. AC A0A0V0UYQ6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRX56229.1}; GN ORFNames=T09_6046 {ECO:0000313|EMBL:KRX56229.1}; OS Trichinella sp. T9. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX56229.1, ECO:0000313|Proteomes:UP000054681}; RN [1] {ECO:0000313|EMBL:KRX56229.1, ECO:0000313|Proteomes:UP000054681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX56229.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX56229.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDN01000127; KRX56229.1; -; Genomic_DNA. DR Proteomes; UP000054681; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054681}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRX56229.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054681}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 865 889 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 338 540 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 546 634 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 776 813 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 472 472 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 476 476 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 482 482 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 606 626 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 803 812 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1197 AA; 132931 MW; 5AD47D367E7BD50E CRC64; MTSFVLLNST FLTYCRRHIS SRCEALAEII SPFAVCAVSV LALGRPAFFI QARFRCESYS TFCFGFGNSC SVCSSLPASL LCPNGTKSPV GNRASSSVRL IARLTNAFQG FQTGEGRPAG RNWIFGSCRV LDAKPSDIDQ AMEEFFKMDS WNKELFEHLV DDFEIVYPVQ LRDRGRVGID TQNYLFDNST IHFERCSFVI KTSYGRWRIH VQLNDVLIQP AAKYVRYLKL DSPSETNGRS LPNCYYHGQV HGQPKSKVSL STCFGLRGSI VMENQTFIII PLKGGDLSRR HPHVFARLKW DDEASCGNTD NTEWSRKRFH RRRPHRRKLR RDVEKEVKYI ELGLFVDRKL HDFLNVGYRE MTSYFLEAVN AVDLAFQQLN TRVSLVYFEI WTTENKIGVQ REILPSLMNF IQFSSYEFYN GPFDLALLLT AADLTTSEMM SAADTVCSAR AAGMIKVADK FQPYYLSLLM AHAIGHISGM SHDDSEFDCT NGENFIGIMN NVVSMTSKKN RRVYQFTECN KHDYLELIRS GQGRCLFNFP LQNNALTLCG NKVVDPGEFC DCGSVEECDS VDPCCDAVTC TLRADAQCAE GVCCEKCKFI TNRTLCRPSR DECDVPEYCS GLSGNCPSDS YKPNGAACGI NRLGICYGGQ CRQSDSECQR IWGPNASAAD PACFKKFNTL GIDFGHCGVN ENNKPLPCTE NNAMCGLLFC KGGQEVPNFS LYFKTEFTEN GSVYECKVFI DNKSPVNYSL IPDGSRCGKS EACISQNCVP LRNIYQHVDC PTTNTALFCS GHGICTNLNI CHCDAGWTGR DCSVKANFTF EMLSIGESAV SEHGGSSFYG DSEMPVAVSF PDTFPSGDSS KLDTYAMLII LGCVAIGMIL MLALLLLCYR RRANFSKKTK TPTSEKCDFE KESNSSTETG QRSIRFGPSR TYKCADEMMT TNKRRTLDQI RECDERESLS AKSRESANSA ERVTLTMNRL PSRGILKNGP QSFTCERTAP EWRALLAANR PCDAGYDSEP PYQQSSTFGR YVGVNGGGCW TASDDGRCPL QTPNSARLTR GGLYESFNSK QPRLNQTTAA IVSPYMYVRN RSLLKASPAA LDSFSNANNN GCCSPSRSRG ADLAAYAVSP ADKQQLSQTR CSTSPCNSTC SSSRGATMQQ PKPLKLTNIE LLLKQLDGAA VLAEPSEDPT LPSRRLS // ID A0A0V0Y203_TRIPS Unreviewed; 1175 AA. AC A0A0V0Y203; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRX94237.1}; DE Flags: Fragment; GN Name=ADAM28 {ECO:0000313|EMBL:KRX94237.1}; GN ORFNames=T4E_8851 {ECO:0000313|EMBL:KRX94237.1}; OS Trichinella pseudospiralis (Parasitic roundworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX94237.1, ECO:0000313|Proteomes:UP000054815}; RN [1] {ECO:0000313|EMBL:KRX94237.1, ECO:0000313|Proteomes:UP000054815} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX94237.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX94237.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDU01000075; KRX94237.1; -; Genomic_DNA. DR Proteomes; UP000054815; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054815}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRX94237.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054815}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 841 865 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 311 513 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 519 607 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 749 786 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 445 445 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 449 449 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 455 455 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 579 599 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 776 785 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRX94237.1}. FT NON_TER 1175 1175 {ECO:0000313|EMBL:KRX94237.1}. SQ SEQUENCE 1175 AA; 130315 MW; 1521E59CB97B2C6C CRC64; LLFAVCAVSV LALGRPAFFI QARFRCESYS TFCFNFGNSC SVCSSLPASL LCPNGTKSPV GNRVSCLASS VGLIARLTNA FQGFQTGEGR PAGRNWIFGS CRVLDAKPSD IDQAMEEFFK MDSWNKELFE HLVDDFEIVY PVQLRDRGRV GIDTQNYLFD NSTVHFERCS FVIKTSYGRW RIHVQLNDVL IQPAAKYMRY LKLDSPSETS GRSLPNCYYH GQVHGHPKSK VSLSTCFGLR GSIIMENQTF IIIPLKGGDL SRRHPHVFVR LKWDDEASCG NTDDAEWSRK RFHRRRPHRR KLRRDVEKEV KYIELGLFID RKLHDFLNVG YREMTSYFLE AVNAVDLAFQ QLNTRVSLVY SEIWTTENKI GVQREILPSL MNFIQFSSYE FYNGPFDLAL LLTAADLTTS EMMSAADTVC SARAAGMIKV ADKFQPYYLS LLMAHAIGHI SGMSHDDSEF DCTNGENFIG IMNNVVSMTS KKNRRVYQFT ECNKHDYLEL IRSGQGRCLF NYPLQNSALT LCGNKVVDPG EFCDCGSVEE CDLIDPCCDA VTCTLRADAQ CAEGVCCEKC KFITNRTLCR PSRDECDVPE YCSGLSGSCP SDSYKPNGAA CGINRLGICY GGQCRQSDSE CQRIWGPNAS AADPACFKKF NTLGIDFGHC GVNENNKPLP CTENNAMCGL LFCKGGQEIP NFSLYFKTEF TENGSVYECK VFIDNKSPVN YSLIPDGSRC GKSEACISQN CVPLRNIYQH VDCPTTNTAL FCSGHGICTN LNICHCDAGW TGRDCSVKLN FTFEMLSIGQ SAVSEHGSFY GDSEMPVAVS FPDTFPSGVS DVSDSSKLDT YAMLIILGCV AIGMILMLAL LLLCYRRRAN FSKKSKTPTS EKCDFEKESN SSTETGQRSI RFGPSRTYKC ADEVMTTNKR RTLDQIRECD ERESLSAKSR ESGNSTERVT LTMNRLPSRG ILKNGPQSFT CERTAPEWRA LLAANRPCDN GYDSEPPYQQ SSTFGRYVGV NGSGXXXXXX XXXVAVGPPA MMTPNSARLT RGGLYESFNS KQPRLNQTTA AIVSPYMYVR NRSLLKASPA TLDSFSSNNG CCSPSRSRGA DLAAYAVSPA EKQLPTTRCS TSPCNSTCSS SRGATMQQPK PLKLTNIELL LKQLDGAAVL AEPSEDQSLS SRRLS // ID A0A0V0Y270_TRIPS Unreviewed; 1192 AA. AC A0A0V0Y270; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 19. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 {ECO:0000313|EMBL:KRX94235.1}; DE Flags: Fragment; GN Name=ADAM28 {ECO:0000313|EMBL:KRX94235.1}; GN ORFNames=T4E_8851 {ECO:0000313|EMBL:KRX94235.1}; OS Trichinella pseudospiralis (Parasitic roundworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX94235.1, ECO:0000313|Proteomes:UP000054815}; RN [1] {ECO:0000313|EMBL:KRX94235.1, ECO:0000313|Proteomes:UP000054815} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX94235.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX94235.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDU01000075; KRX94235.1; -; Genomic_DNA. DR Proteomes; UP000054815; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054815}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRX94235.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054815}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 858 882 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 311 513 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 519 596 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 766 803 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 445 445 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 449 449 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 455 455 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 793 802 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRX94235.1}. FT NON_TER 1192 1192 {ECO:0000313|EMBL:KRX94235.1}. SQ SEQUENCE 1192 AA; 132155 MW; 86CBF0BF5269EDDC CRC64; LLFAVCAVSV LALGRPAFFI QARFRCESYS TFCFNFGNSC SVCSSLPASL LCPNGTKSPV GNRVSCLASS VGLIARLTNA FQGFQTGEGR PAGRNWIFGS CRVLDAKPSD IDQAMEEFFK MDSWNKELFE HLVDDFEIVY PVQLRDRGRV GIDTQNYLFD NSTVHFERCS FVIKTSYGRW RIHVQLNDVL IQPAAKYMRY LKLDSPSETS GRSLPNCYYH GQVHGHPKSK VSLSTCFGLR GSIIMENQTF IIIPLKGGDL SRRHPHVFVR LKWDDEASCG NTDDAEWSRK RFHRRRPHRR KLRRDVEKEV KYIELGLFID RKLHDFLNVG YREMTSYFLE AVNAVDLAFQ QLNTRVSLVY SEIWTTENKI GVQREILPSL MNFIQFSSYE FYNGPFDLAL LLTAADLTTS EMMSAADTVC SARAAGMIKV ADKFQPYYLS LLMAHAIGHI SGMSHDDSEF DCTNGENFIG IMNNVVSMTS KKNRRVYQFT ECNKHDYLEL IRSGQGRCLF NYPLQNSALT LCGNKVVDPG EFCDCGSVEE CDLIDPCCDA VTCTLRADAQ CAEGVCCEKC KFITNRTLCR PSRDECDVPE YCSGLSGSVS LLCGFNELEL FGGLFCPSDS YKPNGAACGI NRLGICYGGQ CRQSDSECQR IWGPNASAAD PACFKKFNTL GIDFGHCGVN ENNKPLPCTE NNAMCGLLFC KGGQEIPNFS LYFKTEFTEN GSVYECKVFI DNKSPVNYSL IPDGSRCGKS EACISQNCVP LRNIYQHVDC PTTNTALFCS GHGICTNLNI CHCDAGWTGR DCSVKLNFTF EMLSIGQSAV SEHGSFYGDS EMPVAVSFPD TFPSGVSDVS DSSKLDTYAM LIILGCVAIG MILMLALLLL CYRRRANFSK KSKTPTSEKC DFEKESNSST ETGQRSIRFG PSRTYKCADE VMTTNKRRTL DQIRECDERE SLSAKSRESG NSTERVTLTM NRLPSRGILK NGPQSFTCER TAPEWRALLA ANRPCDNGYD SEPPYQQSST FGRYVGVNGS GXXXXXXXXX VAVGPPAMMT PNSARLTRGG LYESFNSKQP RLNQTTAAIV SPYMYVRNRS LLKASPATLD SFSSNNGCCS PSRSRGADLA AYAVSPAEKQ LPTTRCSTSP CNSTCSSSRG ATMQQPKPLK LTNIELLLKQ LDGAAVLAEP SEDQSLSSRR LS // ID A0A0V0Y2G0_TRIPS Unreviewed; 1187 AA. AC A0A0V0Y2G0; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRX94236.1}; DE Flags: Fragment; GN Name=ADAM28 {ECO:0000313|EMBL:KRX94236.1}; GN ORFNames=T4E_8851 {ECO:0000313|EMBL:KRX94236.1}; OS Trichinella pseudospiralis (Parasitic roundworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX94236.1, ECO:0000313|Proteomes:UP000054815}; RN [1] {ECO:0000313|EMBL:KRX94236.1, ECO:0000313|Proteomes:UP000054815} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX94236.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX94236.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDU01000075; KRX94236.1; -; Genomic_DNA. DR Proteomes; UP000054815; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054815}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRX94236.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054815}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 853 877 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 311 525 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 531 619 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 761 798 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 457 457 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 461 461 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 467 467 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 591 611 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 788 797 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRX94236.1}. FT NON_TER 1187 1187 {ECO:0000313|EMBL:KRX94236.1}. SQ SEQUENCE 1187 AA; 131875 MW; 80C0ED3D1A1E4016 CRC64; LLFAVCAVSV LALGRPAFFI QARFRCESYS TFCFNFGNSC SVCSSLPASL LCPNGTKSPV GNRVSCLASS VGLIARLTNA FQGFQTGEGR PAGRNWIFGS CRVLDAKPSD IDQAMEEFFK MDSWNKELFE HLVDDFEIVY PVQLRDRGRV GIDTQNYLFD NSTVHFERCS FVIKTSYGRW RIHVQLNDVL IQPAAKYMRY LKLDSPSETS GRSLPNCYYH GQVHGHPKSK VSLSTCFGLR GSIIMENQTF IIIPLKGGDL SRRHPHVFVR LKWDDEASCG NTDDAEWSRK RFHRRRPHRR KLRRDVEKEV KYIELGLFID RKLHDFLNVG YREMTSYFLE AVNAVDLAFQ QLNTRVSLVY SEIWTTENKI GVQREILPSL MNFIQFSSYE FYNGPFDLAL LLTAADLTTS EMMSAADTVC SARAAGMIKL INEFTYRFTF QVADKFQPYY LSLLMAHAIG HISGMSHDDS EFDCTNGENF IGIMNNVVSM TSKKNRRVYQ FTECNKHDYL ELIRSGQGRC LFNYPLQNSA LTLCGNKVVD PGEFCDCGSV EECDLIDPCC DAVTCTLRAD AQCAEGVCCE KCKFITNRTL CRPSRDECDV PEYCSGLSGS CPSDSYKPNG AACGINRLGI CYGGQCRQSD SECQRIWGPN ASAADPACFK KFNTLGIDFG HCGVNENNKP LPCTENNAMC GLLFCKGGQE IPNFSLYFKT EFTENGSVYE CKVFIDNKSP VNYSLIPDGS RCGKSEACIS QNCVPLRNIY QHVDCPTTNT ALFCSGHGIC TNLNICHCDA GWTGRDCSVK LNFTFEMLSI GQSAVSEHGS FYGDSEMPVA VSFPDTFPSG VSDVSDSSKL DTYAMLIILG CVAIGMILML ALLLLCYRRR ANFSKKSKTP TSEKCDFEKE SNSSTETGQR SIRFGPSRTY KCADEVMTTN KRRTLDQIRE CDERESLSAK SRESGNSTER VTLTMNRLPS RGILKNGPQS FTCERTAPEW RALLAANRPC DNGYDSEPPY QQSSTFGRYV GVNGSGXXXX XXXXXVAVGP PAMMTPNSAR LTRGGLYESF NSKQPRLNQT TAAIVSPYMY VRNRSLLKAS PATLDSFSSN NGCCSPSRSR GADLAAYAVS PAEKQLPTTR CSTSPCNSTC SSSRGATMQQ PKPLKLTNIE LLLKQLDGAA VLAEPSEDQS LSSRRLS // ID A0A0V1AF66_9BILA Unreviewed; 1157 AA. AC A0A0V1AF66; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRY23341.1}; DE Flags: Fragment; GN Name=ADAM28 {ECO:0000313|EMBL:KRY23341.1}; GN ORFNames=T12_11231 {ECO:0000313|EMBL:KRY23341.1}; OS Trichinella patagoniensis. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY23341.1, ECO:0000313|Proteomes:UP000054783}; RN [1] {ECO:0000313|EMBL:KRY23341.1, ECO:0000313|Proteomes:UP000054783} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY23341.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRY23341.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDQ01000004; KRY23341.1; -; Genomic_DNA. DR Proteomes; UP000054783; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054783}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRY23341.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054783}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 825 849 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 298 500 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 506 594 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 736 773 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 432 432 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 436 436 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 442 442 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 566 586 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 763 772 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRY23341.1}. SQ SEQUENCE 1157 AA; 128592 MW; B58F49391A292A61 CRC64; LALGRPAFFI QARFRCESYW TFCFGFGNSC SVCSSLPASL LCPNGTKSPV GNRASSSVRL IARLTNAFQG FQTGEGRPAG RNWIFGSCRV LDAKPSDIDQ AMEEFFKMDS WNKELFEHLV DDFEIVYPVQ LRDRGRVGID TQNYLFDNST IHFERCSFVI KTSYGRWRIH VQLNDVLIQP AAKYVRYLKL DSPSETNGRS LPNCYYHGQV HGQPKSKVSL STCFGLRGSI VMENQTFIII PLKGGDLSRR HPHVFARLKW DDEASCGNTD NTEWSRKRFH RRRPHRRKLR RDVEKEVKYI ELGLFVDRKL HDFLNVGYRE MTSYFLEAVN AVDLAFQQLN TRVSLVYFEI WTTENKIGVQ REILPSLMNF IQFSSYEFYN GPFDLALLLT AADLTTSEMM SAADTVCSAR AAGMIKVADK FQPYYLSLLM AHAIGHISGM SHDDSEFDCT NGENFIGIMN NVVSMTSKKN RRVYQFTECN KHDYLELIRS GQGRCLFNFP LQNNALTLCG NKVVDPGEFC DCGSVEECDS VDPCCDAVTC TLRADAQCAE GVCCEKCKFI TNRTLCRPSR DECDVPEYCS GLSGNCPSDS YKPNGAACGI NRLGICYGGQ CRQSDSECQR IWGPNASAAD PACFKKFNTL GIDFGHCGVN ENNKPLPCTE NNAMCGLLFC KGGQEVPNFS LYFKTEFTEN GSVYECKVFI DNKSPVNYSL IPDGSRCGKS EACISQNCVP LRNIYQHVDC PTTNTALFCS GHGICTNLNI CHCDAGWTGR DCSVKTNFTF EMLSIGESAV SEHGGSSFYG DSEMPVAVTF PDTFPSGDSS KLDTYAMLII LGCVAIGMIL MLALLLLCYR RRANFSKKTK TPTSEKCDFE KESNSSTETG QRSIRFGPSR TYKCADEVMT TNKRRTLDQI RECDERESLS AKSRESANSA ERVTLTMNRL PSRGILKNGP QSFTCERAAP EWRALLAANR PCDAGYDSEP PYQQSSTFGR YVGVNGGGCW TASDDGRCPL QTPNSARLTR GGLYESFNSK QPRLNQTTAA IVSPYMYVRN RSLLKASPAA LDSFSNANNN GCCSPSRSRG ADLAAYAVSP ADKQQLSQTR CSTSPCNSTC SSSRGATMQQ PKPLKLTNIE LLLKQLDGAA VLAEPSEDPT LPSRRLS // ID A0A0V1AFD1_9BILA Unreviewed; 1184 AA. AC A0A0V1AFD1; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRY23342.1}; DE Flags: Fragment; GN Name=ADAM28 {ECO:0000313|EMBL:KRY23342.1}; GN ORFNames=T12_11231 {ECO:0000313|EMBL:KRY23342.1}; OS Trichinella patagoniensis. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY23342.1, ECO:0000313|Proteomes:UP000054783}; RN [1] {ECO:0000313|EMBL:KRY23342.1, ECO:0000313|Proteomes:UP000054783} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY23342.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRY23342.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDQ01000004; KRY23342.1; -; Genomic_DNA. DR Proteomes; UP000054783; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054783}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRY23342.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054783}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 852 876 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 325 527 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 533 621 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 763 800 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 459 459 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 463 463 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 469 469 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 593 613 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 790 799 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRY23342.1}. SQ SEQUENCE 1184 AA; 131890 MW; E4F634979CA4C5A5 CRC64; LALGRPAFFI QARFRCESYW TFCFGFGNSC SVCSSLPASL LCPNGTKSPV GNRASSSVRL IARLTNAFQG FQTGEGRPAG RNWIFGSCRV LDAKPSDIDQ AKSDYLKNLQ FIENRSKLQQ LRKHPVECME EFFKMDSWNK ELFEHLVDDF EIVYPVQLRD RGRVGIDTQN YLFDNSTIHF ERCSFVIKTS YGRWRIHVQL NDVLIQPAAK YVRYLKLDSP SETNGRSLPN CYYHGQVHGQ PKSKVSLSTC FGLRGSIVME NQTFIIIPLK GGDLSRRHPH VFARLKWDDE ASCGNTDNTE WSRKRFHRRR PHRRKLRRDV EKEVKYIELG LFVDRKLHDF LNVGYREMTS YFLEAVNAVD LAFQQLNTRV SLVYFEIWTT ENKIGVQREI LPSLMNFIQF SSYEFYNGPF DLALLLTAAD LTTSEMMSAA DTVCSARAAG MIKVADKFQP YYLSLLMAHA IGHISGMSHD DSEFDCTNGE NFIGIMNNVV SMTSKKNRRV YQFTECNKHD YLELIRSGQG RCLFNFPLQN NALTLCGNKV VDPGEFCDCG SVEECDSVDP CCDAVTCTLR ADAQCAEGVC CEKCKFITNR TLCRPSRDEC DVPEYCSGLS GNCPSDSYKP NGAACGINRL GICYGGQCRQ SDSECQRIWG PNASAADPAC FKKFNTLGID FGHCGVNENN KPLPCTENNA MCGLLFCKGG QEVPNFSLYF KTEFTENGSV YECKVFIDNK SPVNYSLIPD GSRCGKSEAC ISQNCVPLRN IYQHVDCPTT NTALFCSGHG ICTNLNICHC DAGWTGRDCS VKTNFTFEML SIGESAVSEH GGSSFYGDSE MPVAVTFPDT FPSGDSSKLD TYAMLIILGC VAIGMILMLA LLLLCYRRRA NFSKKTKTPT SEKCDFEKES NSSTETGQRS IRFGPSRTYK CADEVMTTNK RRTLDQIREC DERESLSAKS RESANSAERV TLTMNRLPSR GILKNGPQSF TCERAAPEWR ALLAANRPCD AGYDSEPPYQ QSSTFGRYVG VNGGGCWTAS DDGRCPLQTP NSARLTRGGL YESFNSKQPR LNQTTAAIVS PYMYVRNRSL LKASPAALDS FSNANNNGCC SPSRSRGADL AAYAVSPADK QQLSQTRCST SPCNSTCSSS RGATMQQPKP LKLTNIELLL KQLDGAAVLA EPSEDPTLPS RRLS // ID A0A0V1D6K7_TRIBR Unreviewed; 1239 AA. AC A0A0V1D6K7; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRY57189.1}; DE Flags: Fragment; GN Name=ADAM28 {ECO:0000313|EMBL:KRY57189.1}; GN ORFNames=T03_11116 {ECO:0000313|EMBL:KRY57189.1}; OS Trichinella britovi (Parasitic roundworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY57189.1, ECO:0000313|Proteomes:UP000054653}; RN [1] {ECO:0000313|EMBL:KRY57189.1, ECO:0000313|Proteomes:UP000054653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY57189.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRY57189.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDI01000034; KRY57189.1; -; Genomic_DNA. DR Proteomes; UP000054653; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054653}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRY57189.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054653}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 907 931 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 380 582 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 588 676 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 818 855 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 514 514 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 518 518 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 524 524 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 648 668 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 845 854 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRY57189.1}. FT NON_TER 1239 1239 {ECO:0000313|EMBL:KRY57189.1}. SQ SEQUENCE 1239 AA; 138020 MW; 5B51F22FBFCED117 CRC64; LLVFFFELIS HCVEIMTSFV LLNSTFLTYC RRHISSRCEA LAEIISPFAV CAVSVLALGR PAFFIQARFR CESYSTFCFG FGNSCSVCSS LPASLLCPNG TKSPVGNRAS SSVRLIARLT NAFQGFQTGE GRPAGRNWIF GSCRVLDAKP SDIDQAKSDY LKNLQFIENR SKLQQLRKHP VECMEEFFKM DSWNKELFEH LVDDFEIVYP VQLRDRGRVG IDTQNYLFDN STIHFERCSF VIKTSYGRWR IHVQLNDVLI QPAAKYVRYL KLDSPSETNG RSLPNCYYHG QVHGQPKSKV SLSTCFGLRG SIVMENQTFI IIPLKGGDLS RRHPHVFARL KWDDEASCGN TDNTEWSRKR FHRRRPHRRK LRRDVEKEVK YIELGLFVDR KLHDFLNVGY REMTSYFLEA VNAVDLAFQQ LNTRVSLVYF EIWTTENKIG VQREILPSLM NFIQFSSYEF YNGPFDLALL LTAADLTTSE MMSAADTVCS ARAAGMIKVA DKFQPYYLSL LMAHAIGHIS GMSHDDSEFD CTNGENFIGI MNNVVSMTSK KNRRVYQFTE CNKHDYLELI RSGQGRCLFN FPLQNNALTL CGNKVVDPGE FCDCGSVEEC DSVDPCCDAV TCTLRADAQC AEGVCCEKCK FITNRTLCRP SRDECDVPEY CSGLSGNCPS DSYKPNGAAC GINRLGICYG GQCRQSDSEC QRIWGPNASA ADPACFKKFN TLGIDFGHCG VNENNKPLPC TENNAMCGLL FCKGGQEVPN FSLYFKTEFT ENGSVYECKV FIDNKSPVNY SLIPDGSRCG KSEACISQNC VPLRNIYQHV DCPTTNTALF CSGHGICTNL NICHCDAGWT GRDCSVKANF TFEMLSIGES AVSEHGGSSF YGDSEMPVAV SFPDTFPSGD SSKLDTYAML IILGCVAIGM ILMLALLLLC YRRRANFSKK TKTPTSEKCD FEKESNSSTE TGQRSIRFGP SRTYKCADEM MTTNKRRTLD QIRECDERES LSAKSRESAN SAERVTLTMN RLPSRGILKN GPQSFTCERT APEWRALLAA NRPCDAGYDS EPPYQQSSTF GRYVGVNGGG CWTASDDGRC PLQTPNSARL TRGGLYESFN SKQPRLNQTT AAIVSPYMYV RNRSLLKASP AALDSFSNAN NNGCCSPSRS RGADLAAYAV SPADKQQLSQ TRCSTSPCNS TCSSSRGATM QQPKPLKLTN IELLLKQLDG AAVLAEPSED PTLPSRRLS // ID A0A0V1D6Z6_TRIBR Unreviewed; 1212 AA. AC A0A0V1D6Z6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRY57190.1}; DE Flags: Fragment; GN Name=ADAM28 {ECO:0000313|EMBL:KRY57190.1}; GN ORFNames=T03_11116 {ECO:0000313|EMBL:KRY57190.1}; OS Trichinella britovi (Parasitic roundworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY57190.1, ECO:0000313|Proteomes:UP000054653}; RN [1] {ECO:0000313|EMBL:KRY57190.1, ECO:0000313|Proteomes:UP000054653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY57190.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRY57190.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDI01000034; KRY57190.1; -; Genomic_DNA. DR Proteomes; UP000054653; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054653}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRY57190.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054653}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 880 904 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 353 555 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 561 649 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 791 828 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 487 487 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 491 491 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 497 497 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 621 641 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 818 827 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRY57190.1}. FT NON_TER 1212 1212 {ECO:0000313|EMBL:KRY57190.1}. SQ SEQUENCE 1212 AA; 134722 MW; 02773416CAD9E749 CRC64; LLVFFFELIS HCVEIMTSFV LLNSTFLTYC RRHISSRCEA LAEIISPFAV CAVSVLALGR PAFFIQARFR CESYSTFCFG FGNSCSVCSS LPASLLCPNG TKSPVGNRAS SSVRLIARLT NAFQGFQTGE GRPAGRNWIF GSCRVLDAKP SDIDQAMEEF FKMDSWNKEL FEHLVDDFEI VYPVQLRDRG RVGIDTQNYL FDNSTIHFER CSFVIKTSYG RWRIHVQLND VLIQPAAKYV RYLKLDSPSE TNGRSLPNCY YHGQVHGQPK SKVSLSTCFG LRGSIVMENQ TFIIIPLKGG DLSRRHPHVF ARLKWDDEAS CGNTDNTEWS RKRFHRRRPH RRKLRRDVEK EVKYIELGLF VDRKLHDFLN VGYREMTSYF LEAVNAVDLA FQQLNTRVSL VYFEIWTTEN KIGVQREILP SLMNFIQFSS YEFYNGPFDL ALLLTAADLT TSEMMSAADT VCSARAAGMI KVADKFQPYY LSLLMAHAIG HISGMSHDDS EFDCTNGENF IGIMNNVVSM TSKKNRRVYQ FTECNKHDYL ELIRSGQGRC LFNFPLQNNA LTLCGNKVVD PGEFCDCGSV EECDSVDPCC DAVTCTLRAD AQCAEGVCCE KCKFITNRTL CRPSRDECDV PEYCSGLSGN CPSDSYKPNG AACGINRLGI CYGGQCRQSD SECQRIWGPN ASAADPACFK KFNTLGIDFG HCGVNENNKP LPCTENNAMC GLLFCKGGQE VPNFSLYFKT EFTENGSVYE CKVFIDNKSP VNYSLIPDGS RCGKSEACIS QNCVPLRNIY QHVDCPTTNT ALFCSGHGIC TNLNICHCDA GWTGRDCSVK ANFTFEMLSI GESAVSEHGG SSFYGDSEMP VAVSFPDTFP SGDSSKLDTY AMLIILGCVA IGMILMLALL LLCYRRRANF SKKTKTPTSE KCDFEKESNS STETGQRSIR FGPSRTYKCA DEMMTTNKRR TLDQIRECDE RESLSAKSRE SANSAERVTL TMNRLPSRGI LKNGPQSFTC ERTAPEWRAL LAANRPCDAG YDSEPPYQQS STFGRYVGVN GGGCWTASDD GRCPLQTPNS ARLTRGGLYE SFNSKQPRLN QTTAAIVSPY MYVRNRSLLK ASPAALDSFS NANNNGCCSP SRSRGADLAA YAVSPADKQQ LSQTRCSTSP CNSTCSSSRG ATMQQPKPLK LTNIELLLKQ LDGAAVLAEP SEDPTLPSRR LS // ID A0A0V1D734_TRIBR Unreviewed; 1220 AA. AC A0A0V1D734; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRY57188.1}; DE Flags: Fragment; GN Name=ADAM28 {ECO:0000313|EMBL:KRY57188.1}; GN ORFNames=T03_11116 {ECO:0000313|EMBL:KRY57188.1}; OS Trichinella britovi (Parasitic roundworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY57188.1, ECO:0000313|Proteomes:UP000054653}; RN [1] {ECO:0000313|EMBL:KRY57188.1, ECO:0000313|Proteomes:UP000054653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY57188.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRY57188.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDI01000034; KRY57188.1; -; Genomic_DNA. DR Proteomes; UP000054653; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054653}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRY57188.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054653}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 888 912 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 353 555 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 561 649 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 799 836 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 487 487 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 491 491 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 497 497 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 621 641 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 826 835 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRY57188.1}. FT NON_TER 1220 1220 {ECO:0000313|EMBL:KRY57188.1}. SQ SEQUENCE 1220 AA; 135841 MW; 8B1D979E898FB271 CRC64; LLVFFFELIS HCVEIMTSFV LLNSTFLTYC RRHISSRCEA LAEIISPFAV CAVSVLALGR PAFFIQARFR CESYSTFCFG FGNSCSVCSS LPASLLCPNG TKSPVGNRAS SSVRLIARLT NAFQGFQTGE GRPAGRNWIF GSCRVLDAKP SDIDQAMEEF FKMDSWNKEL FEHLVDDFEI VYPVQLRDRG RVGIDTQNYL FDNSTIHFER CSFVIKTSYG RWRIHVQLND VLIQPAAKYV RYLKLDSPSE TNGRSLPNCY YHGQVHGQPK SKVSLSTCFG LRGSIVMENQ TFIIIPLKGG DLSRRHPHVF ARLKWDDEAS CGNTDNTEWS RKRFHRRRPH RRKLRRDVEK EVKYIELGLF VDRKLHDFLN VGYREMTSYF LEAVNAVDLA FQQLNTRVSL VYFEIWTTEN KIGVQREILP SLMNFIQFSS YEFYNGPFDL ALLLTAADLT TSEMMSAADT VCSARAAGMI KVADKFQPYY LSLLMAHAIG HISGMSHDDS EFDCTNGENF IGIMNNVVSM TSKKNRRVYQ FTECNKHDYL ELIRSGQGRC LFNFPLQNNA LTLCGNKVVD PGEFCDCGSV EECDSVDPCC DAVTCTLRAD AQCAEGVCCE KCKFITNRTL CRPSRDECDV PEYCSGLSGN CPSDSYKPNG AACGINRLGI CYGGQCRQSD SECQRIWGPS EIGYLIFHCL TDVTYLLIKF NTLGIDFGHC GVNENNKPLP CTENNAMCGL LFCKGGQEVP NFSLYFKTEF TENGSVYECK VFIDNKSPVN YSLIPDGSRC GKSEACISQN CVPLRNIYQH VDCPTTNTAL FCSGHGICTN LNICHCDAGW TGRDCSVKAN FTFEMLSIGE SAVSEHGGSS FYGDSEMPVA VSFPDTFPSG DSSKLDTYAM LIILGCVAIG MILMLALLLL CYRRRANFSK KTKTPTSEKC DFEKESNSST ETGQRSIRFG PSRTYKCADE MMTTNKRRTL DQIRECDERE SLSAKSRESA NSAERVTLTM NRLPSRGILK NGPQSFTCER TAPEWRALLA ANRPCDAGYD SEPPYQQSST FGRYVGVNGG GCWTASDDGR CPLQTPNSAR LTRGGLYESF NSKQPRLNQT TAAIVSPYMY VRNRSLLKAS PAALDSFSNA NNNGCCSPSR SRGADLAAYA VSPADKQQLS QTRCSTSPCN STCSSSRGAT MQQPKPLKLT NIELLLKQLD GAAVLAEPSE DPTLPSRRLS // ID A0A0V1H8K0_9BILA Unreviewed; 1242 AA. AC A0A0V1H8K0; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 {ECO:0000313|EMBL:KRZ07144.1}; DE Flags: Fragment; GN Name=ADAM9 {ECO:0000313|EMBL:KRZ07144.1}; GN ORFNames=T11_6463 {ECO:0000313|EMBL:KRZ07144.1}; OS Trichinella zimbabwensis. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ07144.1, ECO:0000313|Proteomes:UP000055024}; RN [1] {ECO:0000313|EMBL:KRZ07144.1, ECO:0000313|Proteomes:UP000055024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ07144.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRZ07144.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDP01000107; KRZ07144.1; -; Genomic_DNA. DR Proteomes; UP000055024; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000055024}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRZ07144.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000055024}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 20 43 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 912 936 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 370 572 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 578 666 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 808 845 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 504 504 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 508 508 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 514 514 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 638 658 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 835 844 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRZ07144.1}. SQ SEQUENCE 1242 AA; 138203 MW; 8E67B12F70DE2CB5 CRC64; LCICGIVRSS LRHISSRCEA LAEIILPFAV CAVSILALGR PAFFIQARFR CESYSTFRFS FGNSCSVCSS LPASLLCPNG TKLEIDFYFS TVVFGPVTEE WTFGFRPDFI DCSISHPSVI VYLSSLASSV GLIARLTNAF QGFQTGEGRP AGRNWIFGSC RVLDAKPSDI DQAMEEFFKM DSWNKELFEH LVDDFEIVYP VQLRDRGRVG IDTQNYLFDN STVHFERCSF VIKTSYGRWR IHVQLNDVLI QPAAKYMRYL KLDSPSETSG RSLPNCYYHG QVHGQPKSKV SLSTCFGLRG SIVMENQTFI IIPLKGGDLS RRHPHVFVRL KWDDEASCGN TDNAEWSRKR FHKRRPHRRK LRRDVEKEVK YIELGLFIDR KLHDFLNVGY REMISYFLEA VNAVDLAFQQ LNTRVSLVYT EIWTTENKIG VQREILPSLM NFIQFSSYEF YNGPFDLALL LTAADLTTSE MMSAADTVCS ARAAGMIKVA DKFQPYYLSL LMAHAIGHIS GMSHDDSEFD CTNGENFIGI MNNVVSMTSK KNRRVYQFTE CNKHDYLELI RSGQGRCLFN FPLQNNALTL CGNKVVDPGE FCDCGSVEEC DSVDPCCDAV TCTLRADAQC AEGVCCEKCK FITNRTLCRP SRDECDVPEY CSGSSGSCPS DLYKPNGATC GINRLGICYG GQCRQSDSEC QRIWGPNASA ADPACFKKFN TLGIDFGHCG VNENNKPLPC TESNAMCGLL FCKGGQEIPN FSLYFKTEFT ENGSVYECKV FIDNKSPVNY SLIPDGSRCG KSEACISQNC VPLRNIYQHV DCPTTNTALF CSGHGICTNL NICHCDAGWT GRDCSVKLNF TFEMLSIGQS GVSEHGSFYG DSEMPVAVSF PDTFPSGGMW DFFFLNLFCC TFFSDSSKLD TYAMLIILGC VAIGMILMLA LLLLCYRRRA NFSKKSKTPT SEKCDFEKES NSSTETGQRS IRFGPSRTYK CADEVMTTNK RRTLDQIREC DERESLSAKS RESANSAERV TLTMNRLPSR GILKNGPQSF TCERTTPEWR ALLAANRPCD GGYDSEPPYQ QSSTFGRYVG VNGGGCWTAS DDGRCPLQTP NSARLTRGGL YESFNSKQPR LNQTTAAIVS PYMYVRNRSL LKASPATLDS FSSNNGCCSP SRSRGADLAA YAVSPAEKQL PPTRCSTSPC NSTCSSSRGA ATMQQPKPLK LTNIELLLKQ LDGAAVLAEP SEDPTLSSRR LS // ID A0A0V1H9B2_9BILA Unreviewed; 1225 AA. AC A0A0V1H9B2; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRZ07143.1}; DE Flags: Fragment; GN Name=ADAM9 {ECO:0000313|EMBL:KRZ07143.1}; GN ORFNames=T11_6463 {ECO:0000313|EMBL:KRZ07143.1}; OS Trichinella zimbabwensis. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ07143.1, ECO:0000313|Proteomes:UP000055024}; RN [1] {ECO:0000313|EMBL:KRZ07143.1, ECO:0000313|Proteomes:UP000055024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ07143.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRZ07143.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDP01000107; KRZ07143.1; -; Genomic_DNA. DR Proteomes; UP000055024; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000055024}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRZ07143.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000055024}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 20 43 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 895 919 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 370 572 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 578 666 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 808 845 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 504 504 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 508 508 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 514 514 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 638 658 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 835 844 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRZ07143.1}. SQ SEQUENCE 1225 AA; 136095 MW; 520A9F942EFC7592 CRC64; LCICGIVRSS LRHISSRCEA LAEIILPFAV CAVSILALGR PAFFIQARFR CESYSTFRFS FGNSCSVCSS LPASLLCPNG TKLEIDFYFS TVVFGPVTEE WTFGFRPDFI DCSISHPSVI VYLSSLASSV GLIARLTNAF QGFQTGEGRP AGRNWIFGSC RVLDAKPSDI DQAMEEFFKM DSWNKELFEH LVDDFEIVYP VQLRDRGRVG IDTQNYLFDN STVHFERCSF VIKTSYGRWR IHVQLNDVLI QPAAKYMRYL KLDSPSETSG RSLPNCYYHG QVHGQPKSKV SLSTCFGLRG SIVMENQTFI IIPLKGGDLS RRHPHVFVRL KWDDEASCGN TDNAEWSRKR FHKRRPHRRK LRRDVEKEVK YIELGLFIDR KLHDFLNVGY REMISYFLEA VNAVDLAFQQ LNTRVSLVYT EIWTTENKIG VQREILPSLM NFIQFSSYEF YNGPFDLALL LTAADLTTSE MMSAADTVCS ARAAGMIKVA DKFQPYYLSL LMAHAIGHIS GMSHDDSEFD CTNGENFIGI MNNVVSMTSK KNRRVYQFTE CNKHDYLELI RSGQGRCLFN FPLQNNALTL CGNKVVDPGE FCDCGSVEEC DSVDPCCDAV TCTLRADAQC AEGVCCEKCK FITNRTLCRP SRDECDVPEY CSGSSGSCPS DLYKPNGATC GINRLGICYG GQCRQSDSEC QRIWGPNASA ADPACFKKFN TLGIDFGHCG VNENNKPLPC TESNAMCGLL FCKGGQEIPN FSLYFKTEFT ENGSVYECKV FIDNKSPVNY SLIPDGSRCG KSEACISQNC VPLRNIYQHV DCPTTNTALF CSGHGICTNL NICHCDAGWT GRDCSVKLNF TFEMLSIGQS GVSEHGSFYG DSEMPVAVSF PDTFPSGDSS KLDTYAMLII LGCVAIGMIL MLALLLLCYR RRANFSKKSK TPTSEKCDFE KESNSSTETG QRSIRFGPSR TYKCADEVMT TNKRRTLDQI RECDERESLS AKSRESANSA ERVTLTMNRL PSRGILKNGP QSFTCERTTP EWRALLAANR PCDGGYDSEP PYQQSSTFGR YVGVNGGGCW TASDDGRCPL QTPNSARLTR GGLYESFNSK QPRLNQTTAA IVSPYMYVRN RSLLKASPAT LDSFSSNNGC CSPSRSRGAD LAAYAVSPAE KQLPPTRCST SPCNSTCSSS RGAATMQQPK PLKLTNIELL LKQLDGAAVL AEPSEDPTLS SRRLS // ID A0A0V1L5G7_9BILA Unreviewed; 1096 AA. AC A0A0V1L5G7; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRZ54694.1}; GN Name=ADAM28 {ECO:0000313|EMBL:KRZ54694.1}; GN ORFNames=T02_4492 {ECO:0000313|EMBL:KRZ54694.1}; OS Trichinella nativa. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ54694.1, ECO:0000313|Proteomes:UP000054721}; RN [1] {ECO:0000313|EMBL:KRZ54694.1, ECO:0000313|Proteomes:UP000054721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ54694.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRZ54694.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDW01000132; KRZ54694.1; -; Genomic_DNA. DR Proteomes; UP000054721; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054721}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRZ54694.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054721}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 764 788 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 237 439 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 445 533 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 675 712 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 371 371 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 375 375 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 381 381 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 505 525 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 702 711 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1096 AA; 122709 MW; B60622EF32AC3B14 CRC64; MEKLISRRFV SFWESDYLKN LQFIENRSKL QQLRKHPVEC MEEFFKMDSW NKELFEHLVD DFEIVYPVQL RDRGRVGIDT QNYLFDNSTI HFERCSFVIK TSYGRWRIHV QLNDVLIQPA AKYVRYLKLD SPSETNGRSL PNCYYHGQVH GQPKSKVSLS TCFGLRGSIV MENQTFIIIP LKGGDLSRRH PHVFARLKWD DEASCGNTDN TEWSRKRFHR RRPHRRKLRR DVEKEVKYIE LGLFVDRKLH DFLNVGYREM TSYFLEAVNA VDLAFQQLNT RVSLVYFEIW TTENKIGVQR EILPSLMNFI QFSSYEFYNG PFDLALLLTA ADLTTSEMMS AADTVCSARA AGMIKVADKF QPYYLSLLMA HAIGHISGMS HDDSEFDCTN GENFIGIMNN VVSMTSKKNR RVYQFTECNK HDYLELIRSG QGRCLFNFPL QNNALTLCGN KVVDPGEFCD CGSVEECDSV DPCCDAVTCT LRADAQCAEG VCCEKCKFIT NRTLCRPSRD ECDVPEYCSG LSGNCPSDSY KPNGAACGIN RLGICYGGQC RQSDSECQRI WGPNASAADP ACFKKFNTLG IDFGHCGVNE NNKPLPCTEN NAMCGLLFCK GGQEVPNFSL YFKTEFTENG SVYECKVFID NKSPVNYSLI PDGSRCGKSE ACISQNCVPL RNIYQHVDCP TTNTALFCSG HGICTNLNIC HCDAGWTGRD CSVKANFTFE MLSIGESAVS EHGGSSFYGD SEMPVAVTFP DTFPSGDSSK LDTYAMLIIL GCVAIGMILM LALLLLCYRR RANFSKKTKT PTSEKCDFEK ESNSSTETGQ RSIRFGPSRT YKCADEMMTT NKRRTLDQIR ECDERESLSA KSRESANSAE RVTLTMNRLP SRGILKNGPQ SFTCERTAPE WRALLAANRP CDAGYDSEPP YQQSSTFGRY VGVNGGGCWT ASDDGRCPLQ TPNSARLTRG GLYESFNSKQ PRLNQTTAAI VSPYMYVRNR SLLKASPAAL DSFSNANNNG CCSPSRSRGA DLAAYAVSPA DKQQLSQTRC STSPCNSTCS SSRGATMQQP KPLKLTNIEL LLKQLDGAAV LAEPSEDPTL PSRRLS // ID A0A0V1MSM7_9BILA Unreviewed; 1046 AA. AC A0A0V1MSM7; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KRZ74759.1}; GN Name=ADAM28 {ECO:0000313|EMBL:KRZ74759.1}; GN ORFNames=T10_3338 {ECO:0000313|EMBL:KRZ74759.1}; OS Trichinella papuae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ74759.1, ECO:0000313|Proteomes:UP000054843}; RN [1] {ECO:0000313|EMBL:KRZ74759.1, ECO:0000313|Proteomes:UP000054843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ74759.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRZ74759.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDO01000046; KRZ74759.1; -; Genomic_DNA. DR Proteomes; UP000054843; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054843}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KRZ74759.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000054843}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 716 740 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 191 393 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 399 487 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 629 666 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 325 325 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 329 329 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 335 335 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 459 479 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 656 665 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1046 AA; 116512 MW; 464B8D0467F36C40 CRC64; MDSWNKELFE HLVDDFEIVY PVQLRDRGRV GIDTQNYLFD NSTVHFERCS FVIKTSYGRW RIHVQLNDVL IQPAAKYMRY LKLDSPSETS GRSLPNCYYH GQVHGQPKSK VSLSTCFGLR GSIVMENQTF IIIPLRGGDL SRRHPHVFVR LKWDDEASCG NTDNAEWSRK RFHKRRPHRR KLRRDVEKEV KYIELGLFID RKLHDFLNVG YREMISYFLE AVNAVDLAFQ QLNTRVALVY TEIWTTENKI GVQREILPSL MNFIQFSSYE FYNGPFDLAL LLTAADLTTS EMMSAADTVC SARAAGMIKV ADKFQPYYLS LLMAHAIGHI SGMSHDDSEF DCTNGENFIG IMNNVVSMTS KKNRRVYQFT ECNKHDYLEL IRSGQGRCLF NFPLQNNALT LCGNKVVDPG EFCDCGSVEE CDSVDPCCDA VTCTLRADAQ CAEGVCCEKC KFITNRTLCR PSRDECDVPE YCSGSSGSCP SDSYKPNGAT CGINRLGICY GGQCRQSDSE CQRIWGPNAS AADPACFKKF NTLGIDFGHC GVNENNKPLP CTESNAMCGL LFCKGGQEIP NFSLYFKTEF TENGSVYECK VFIDNKSPVN YSLIPDGSRC GKSEACISQN CVPLRNIYQH VDCPTTNTAL FCSGHGICTN LNICHCDTGW TGRDCSVKLN FTFEMLSIGQ SGVSEHGSFY GDSEMPVAVS FPDTFPSGDS SKLDTYAMLI ILGCVAIGMI LMLALLLLCY RRRANFSKKS KTPTSEKCDF EKESNSSTET GQRSIRFGPS RTYKCADEVM TTNKRRTLDQ IRECDERESL SAKSRESANS AERVTLTMNR LPSRGILKNG PQSFTCERTA PEWRALLAAN RPCDGGYDSE PPYQQSSTFG RYVGRLNGGG CWTASDDGRC PLQTPNSARL TRGGLYESFN SKQPRLNQTT AAIVSPYMYV RNRSLLKASP ATLDSFSSNN GCCSPSRSRG ADLAAYAVSP AEKQLPPTRC STSPCNSTCS SSRGAPMQQP KPLKLTNIEL LLKQLDGAAV LAEPSEDPTL SSRRLS // ID A0A151MQ70_ALLMI Unreviewed; 1072 AA. AC A0A151MQ70; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 23-MAY-2018, entry version 16. DE SubName: Full=DBF4-like protein A isoform A {ECO:0000313|EMBL:KYO26623.1}; GN Name=DBF4 {ECO:0000313|EMBL:KYO26623.1}; GN ORFNames=Y1Q_0019112 {ECO:0000313|EMBL:KYO26623.1}; OS Alligator mississippiensis (American alligator). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae; OC Alligator. OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO26623.1}; RN [1] {ECO:0000313|EMBL:KYO26623.1, ECO:0000313|Proteomes:UP000050525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO26623.1}; RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415; RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., RA Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A., RA Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D., RA Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J., RA Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y., RA Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E., RA Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J., RA Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W., RA Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D., RA Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.; RT "Sequencing three crocodilian genomes to illuminate the evolution of RT archosaurs and amniotes."; RL Genome Biol. 13:415-415(2012). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO26623.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKHW03005461; KYO26623.1; -; Genomic_DNA. DR Proteomes; UP000050525; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.30.160.680; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR InterPro; IPR006572; Znf_DBF. DR InterPro; IPR038545; Znf_DBF_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR Pfam; PF07535; zf-DBF; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SMART; SM00586; ZnF_DBF; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS51265; ZF_DBF4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050525}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000050525}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 1023 1046 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 38 106 BRCT. {ECO:0000259|PROSITE:PS50172}. FT DOMAIN 291 339 DBF4-type. {ECO:0000259|PROSITE:PS51265}. FT DOMAIN 528 727 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 733 820 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 963 1000 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ZN_FING 291 339 DBF4-type. {ECO:0000256|PROSITE- FT ProRule:PRU00600}. FT DISULFID 792 812 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 990 999 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1072 AA; 119491 MW; 6A6CFFB079211379 CRC64; MKISGRAPPP AGDMQGKTDK TRPSLRTLKK DAAKPEQSKY KPLYGKVFYL DVPSSVISEK LEKDLKELGG RVEGFLSKDI SYLISNKKEA KFAQSLGQIS PVPSPESAHY GGNSSLHPSS RRDRDDRSSF KMADTVRVSR GKSLVEKAIK EQELIPSGSI LSNALSWGVK ILHVDDIKNY IEQKKKEFCL IKKEGTSGKD VGKRCANQKS KTGRLKNPFV KVEDRSCHYR PFYLQLSSFP VLNYSAPKPY SPFEADKKTN ASQKQIQSKQ RNKTNSDKDC GGIPVQLPLK DKRKRGYCEC CVKKFEDLQT HLESEQHQNF AQSTQYKVVD DIISKFVYDF VEYGNETQKS KRTKCSMGCF SPTTGSVTNT GWQSTHIARA SFQVDAFGLS FILDVMLNHD LLSSEYLERH IENGGKTVEV KGGEHCYYQG QIRGNPESFV ALSTCHGLHG MFYDGNHTYL IEPDENYTSN EDFHSVYKSK LFEFPLDNLP AEFKQMNTTS QKFVVKSRHK RSRRQVRQIP HKVEEETKYI ELMIVNDHLM CKKHRLSVGH TNSYAKSVVN MADLIYKEHL NTRIVLVAME TWATDNKFTI SENPLVTLRE FMKYRRDFIR EKSDAVHLFS GSRFQSSRSG AAYIGGICSL LKGGGVNEFG RPDLMAVTLA QSLAHNLGIF SDKRKLLSGE CECEDTWSGC IMGDTGYYLP SKFSKCDIEE YHDFLNNGGG ACLFNKPSKL LDPPECGNGF VEDGEECDCG TVAECAIEGG ECCTTCTLTA GSQCSNGLCC RKCLFEAKGV LCREAVNDCD IPESCTGNSS QCSPNIHKMD GYSCDNKQGI CFGGRCKTRD RQCKYIWGEK VTAADRYCYE KLNIEGTEKG NCGRDKDTWI QCNKQDVLCG YLLCSNISSV PRLGELDGEI TSSVIQLGKI YNCSGGHVKL DEETDLGYVE DGTPCGTNMM CLEHRCLPTD NFNFSTCPGT AEGKICSGHG VCSNEIKCVC DRLWRGDDCS TLFKGPASFD DDITSKGVVS TNIIIGAIAG TILVLALVLG ITAWGYRNYR RQSTSSVRLR TVCSKEVDPS SD // ID A0A151MVZ3_ALLMI Unreviewed; 708 AA. AC A0A151MVZ3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYO28733.1}; GN ORFNames=Y1Q_0018094 {ECO:0000313|EMBL:KYO28733.1}; OS Alligator mississippiensis (American alligator). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae; OC Alligator. OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO28733.1}; RN [1] {ECO:0000313|EMBL:KYO28733.1, ECO:0000313|Proteomes:UP000050525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO28733.1}; RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415; RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., RA Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A., RA Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D., RA Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J., RA Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y., RA Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E., RA Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J., RA Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W., RA Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D., RA Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.; RT "Sequencing three crocodilian genomes to illuminate the evolution of RT archosaurs and amniotes."; RL Genome Biol. 13:415-415(2012). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO28733.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKHW03004780; KYO28733.1; -; Genomic_DNA. DR Proteomes; UP000050525; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050525}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00276, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000050525}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 657 677 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 157 354 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 362 449 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 589 623 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 310 315 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 613 622 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 708 AA; 78072 MW; B7E8B5302B16B60D CRC64; MLHLTEPRRV LAGPGRVSYA LTMDGKPYTV HLQQQLFIPS EFRVYTYNGR GSLLSNFAAV KADCYYQGYI EGVPNSAVTL STCSGLRGLL QFENVSYGIE PLDSSSGFEH LVYQIKNGST ERPLFENDDM FRDGEQVTGE VSRTLHVELA AAIKSARYLE LAIVLDKGLY NYMGPDKNVV TQKIVQLIGF VNSMFSRLNV TIVLSSLEFW TDYNKIITTG EANELLHRFV KWKNSHLVLR PHDMAYLLVY RDHPRYAGTT FAGKMCVSNY SGAVALYQDA VTLESFSIIV AQLLGLSLGM TYDDARTCQC SGPTCIMHRN AILFSGVKSF SSCSIGDFET FIKHSGGHCL SNRPHLNPSY KSPSCGNGII EDGEQCDCGS AQECTQNRCC TTGCRLARGA RCATGLCCYS CQIKARNRKC RERVDNQCDL PEFCNGTSAF CPRDVFVQNG HKCEHNAGYC YNGYCQAADL QCQRIYGRGS KNGPDACYEE VNSQTDRFGH CGNDPNMGYK SCSWTNLKCG KLICTYPIRV PFIQENTAVI YAQVREDLCV SLDYMQPATA KDPMMVKDGT MCATGKVCMN GKCQVEGVLG YDCNPATKCN GHGVCNNKKN CHCDPGWQPP NCQTRGSVLG GSIDSGLRFL GSDDALERAA QRTMKNWLVL GFCLFLPVLV GAALMVAKRK ELSQLCSEEE SQGDEESPAP SLPEEPSA // ID A0A151MW55_ALLMI Unreviewed; 736 AA. AC A0A151MW55; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 23-MAY-2018, entry version 17. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 32 {ECO:0000313|EMBL:KYO28732.1}; GN Name=ADAM32 {ECO:0000313|EMBL:KYO28732.1}; GN ORFNames=Y1Q_0018093 {ECO:0000313|EMBL:KYO28732.1}; OS Alligator mississippiensis (American alligator). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae; OC Alligator. OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO28732.1}; RN [1] {ECO:0000313|EMBL:KYO28732.1, ECO:0000313|Proteomes:UP000050525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO28732.1}; RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415; RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., RA Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A., RA Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D., RA Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J., RA Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y., RA Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E., RA Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J., RA Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W., RA Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D., RA Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.; RT "Sequencing three crocodilian genomes to illuminate the evolution of RT archosaurs and amniotes."; RL Genome Biol. 13:415-415(2012). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO28732.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKHW03004780; KYO28732.1; -; Genomic_DNA. DR Proteomes; UP000050525; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050525}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00276, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KYO28732.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000050525}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 15 {ECO:0000256|SAM:SignalP}. FT CHAIN 16 736 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5013153403. FT TRANSMEM 686 706 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 189 386 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 394 481 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 620 654 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 342 347 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 644 653 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 736 AA; 80667 MW; 706D724750B8BFC0 CRC64; MRALLPLLLA ARLGATLPGA PASAAQRTAL HILVPWLLSS APPGAPKISY VLTIEGKPYT VHLQQQVFLP SDFRVYTYSR QGAVHAEIPT IKRDCFYRGY VVGFPSSVVT LSTCTGLRGV LQVENVTYGI EPLDSAPGFQ HLMYRVWNED VESRLFVEND TLSGDGGVIL QPDAGRDAIP IQGLSKSPRY VEMHVVVAKA LYDYMGSDKE VVTEKVVQLL SFVNSVFAPL NVTIILSSLE LWVDEDQMAT AGEAPELLWR FLRWKSLHRP LRPHDLSYLL VSRERPEHVG ASFAGQLCLR NYSGGVALYQ RAVTLETFSV VVAQLLGLSL GMTLEDPRTC RCAGATCVMH PGAVGASGPR AFSACSIRDL VRFLASEDGR CLLNRPHMNV SYRAPVCGNN IVEPGEECDC GSSWECQRSR CCQPTCRFRS NIKCSTGLCC WECQFLRNGT LCRSTVDGEC DLQEYCNGSS GACPPDFWVM DGHPCKRQSG YCYKSRCQLA DKQCTQVFGR GAKSAPLACY EEVNSKNDRM GNCGSQPRGY LSCPASDFLC GKLVCELPLK KPFVKTTAAV IYARAKSHLC VTLDYMQELG KTDPMAVSDG TVCGDKKICI NRKCVDVSVL GYNCDVAAKC NNRGVCNNRG NCHCESGWMP PDCTVKTKAG FGGSIDSNFR SSPITDGVHM TTVRNWLLLS CFLFLPVLVG SVILVMKRKK LAQCCDKEEL QADNLEDVGK PGDPRA // ID A0A151NSV9_ALLMI Unreviewed; 776 AA. AC A0A151NSV9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 23-MAY-2018, entry version 16. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 20 {ECO:0000313|EMBL:KYO39689.1}; GN Name=ADAM20 {ECO:0000313|EMBL:KYO39689.1}; GN ORFNames=Y1Q_0018733 {ECO:0000313|EMBL:KYO39689.1}; OS Alligator mississippiensis (American alligator). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae; OC Alligator. OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO39689.1}; RN [1] {ECO:0000313|EMBL:KYO39689.1, ECO:0000313|Proteomes:UP000050525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO39689.1}; RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415; RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., RA Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A., RA Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D., RA Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J., RA Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y., RA Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E., RA Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J., RA Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W., RA Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D., RA Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.; RT "Sequencing three crocodilian genomes to illuminate the evolution of RT archosaurs and amniotes."; RL Genome Biol. 13:415-415(2012). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO39689.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKHW03002185; KYO39689.1; -; Genomic_DNA. DR Proteomes; UP000050525; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050525}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KYO39689.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000050525}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 714 740 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 226 425 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 433 519 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 660 694 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 366 366 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 370 370 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 376 376 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 491 511 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 684 693 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 776 AA; 86226 MW; F1F9367E749849E3 CRC64; MLCWEAVPMD QIQRPVGLMR PWLRAGGGAQ ETGVLLGLGV PIMLLGLLLP STDCGPHPPP GFASYEVIVP RKFVSKEGNA AKDEMSYVIK VEGRNQIVHL KQKKRFIVKN LPVYTYDPQG RLLVDHPSIP EDCYYHGYVE DSPESLVVLS TCSGLRGLLR IGSLQYGIEP VESSLIFQHH LYRIGEAGPE PAACELTDGE REKQTAEVME ARKHASKKPF VWGQTKYLEF LVVVDKQRYD YADKNMTNVV LSVIEVVNLA DEFFSSLRLR ILLTALEVWT DDNPIKITKN VAEVLHNFNI WRKAQLLARV PHDVGHLFSF NDFGKDQQDK LTAKSYHYSA CDRSRASAVV SFINSPVKNF ALLVAHLLGH QVGMVHDEQA CACGNSSFCI MDPARREVYQ FSNCSERYYL NFMRQGKGNC LNNLPETGVF FLMQRCGNQI VEEEEECDCG SEKQCRKDPC CDHTCKKKEG ATCNVGKCCK NCQLLVEGTK CRDTVGECDL PEFCNGTSPY CPEDTHIQDG TVCSGDGYCF YGKCSSHNIQ CEKLFGKPAK AAPISCFREV NMKGDRFGNC WDGGENETFE KCKPENVLCG RLQCVDVKTL PWLEEHVTII QTLVSNIWCW GTDYYSLAES TDYGLTEDGA TCAADKICYN QTCFNHSVLL QLSCSPSSTC HGRGVCNNNG NCHCKDGWAP PLCQFPGFGG SRDSGPPPVS KIGILNLIML IIGIVLGAIA IIVILAVLIF RRAAVTQAVS RTVQNIRSRT LSPPSDDRSP QKDDTV // ID A0A151XE15_9HYME Unreviewed; 1328 AA. AC A0A151XE15; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 23-MAY-2018, entry version 15. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11 {ECO:0000313|EMBL:KYQ58599.1}; GN ORFNames=ALC60_02244 {ECO:0000313|EMBL:KYQ58599.1}; OS Trachymyrmex zeteki. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Formicoidea; Formicidae; Myrmicinae; Trachymyrmex. OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ58599.1, ECO:0000313|Proteomes:UP000075809}; RN [1] {ECO:0000313|EMBL:KYQ58599.1, ECO:0000313|Proteomes:UP000075809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ58599.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ58599.1}; RA Nygaard S., Hu H., Boomsma J., Zhang G.; RT "Trachymyrmex zeteki WGS genome."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ982254; KYQ58599.1; -; Genomic_DNA. DR Proteomes; UP000075809; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000075809}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KYQ58599.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000075809}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 1328 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007591872. FT TRANSMEM 825 848 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 298 502 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 508 596 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 744 781 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 436 436 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 440 440 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 446 446 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 568 588 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 771 780 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1328 AA; 147378 MW; CB44528286F8C7A7 CRC64; MFWLHCGLFV LVIAVRGFIS SLADTTSKRA RVLLFVVHVR TYLAIDPSRC RRAAINRKSR NNEAVDCRAP AVYIDVCVGS DDVMRVETRE VCQSKNSAVE LYPETTRQRI EMSKRRAART SAKRDFPQRG YGDGGYQNPR GRLRTGRHFH RTSLLIKAFN HKFRLDLELN TQLLAPNLIQ KDFLAGNAEQ MSKQEIEHCY YHGTVRDYPG ASAAFHTCNG VSGVIHLGNE TFVIHPFYGG DLSKHPHIIF EARTKVNKGC ANSGNLEWRV KNRRQKHIFG LSETTSDRYK RDVREATKYI ETAIIIDKAM FDKRNGSTRA EVVHDAIQVA NIADLYFRTL NTRVSVVYIE SWKGSNQAQI DNGIDIDQAL LSFNDYTMRR MYQVAQDTTQ LLTGETFSGG ESGVAVPETV CSQRSVGISV DLNTYEPHLL AGTMAHMIGH NIGMSHDDGR NDCNCRDWHG CIMAQSIVGL ENVQPYKFSE CSKTDYIEAL KSGHGICLFN KPNELEIRRS CGNRVIDDGE QCDCGSIEEC KEYDPCCDPI TCKLTTEAEC ATGPCCSDCK LRARGVVCRE STNECDLPEM CTGDTGQCPP DVYKKNGNPC ANNAGHCFNG ICPALDLQCE QVWGYGGIAA DQECFEQFNS KGSINGHCGT DSSGHLIKCE SENVRCGSLQ CQQGSKQPVI DGMKDLHTRT IISIKNQEYE CKATNGRVEG SDIPGMGLVR DGTSCGDNLI CVNQTCTSLF PYIDQEKCPS NHDDKECSGN GVCTNVNKCH CFLGWSGPDC SIEQSIPTPL PTTTEPEVIH KADSKLPEKK ETPYGGTNNN LSTGLMVVIL VGVVTGVFLC FALMAVCYRR KSTVQKYDPP YSKKPQQKSY SGVSGNHHAE AAALDTVNKI LTFGSMPQYR EHKPQPKRLG VEEEDGGTGA EEVVSFIDLP PNNLTKLPEK GILKKHGGYG LGGGAIEHVE RTLNQLNGYH EDILEVLKNA ASRRDLVGTP SGSNLLDEDA LRKSLAECGY PDVYRKDTDG QDNGIDNGQE EEEDDVELQP PCGTIRIRNL EDLIRQLEHR ASARPYMTGQ MSPSGSEEIR TSETEPDRHY RIDSSVCSES SQGSRRCSRG RDEDASRFVY GRYRQPTSRS PYGNHQHTHQ HSHQMHPEDE GIYETADPDR GSNTRGETPD CESDAFIQAQ QQVARWTSED GGGGGGGVQH RPPQQPPPPS AMPVQQQAQQ QQHQLPVEQL PITQRGYYPS PPQIENNLDA GSNAEVESAQ SQQQQTLSEV RGIDVNHMPN INKRPLDDNF SLDCNIMNND SPKELITNNT SDNENTALLP PHFPEYKH // ID A0A158NJV2_ATTCE Unreviewed; 1336 AA. AC A0A158NJV2; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 23-MAY-2018, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:XP_012057810.1}; GN Name=105620943 {ECO:0000313|EnsemblMetazoa:XP_012057810.1}; OS Atta cephalotes (Leafcutter ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Formicoidea; Formicidae; Myrmicinae; Atta. OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012057810.1}; RN [1] {ECO:0000313|EnsemblMetazoa:XP_012057810.1, ECO:0000313|Proteomes:UP000005205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007; RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E., RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E., RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E., RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E., RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S., RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S., RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F., RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., RA Smith C.D., Weinstock G.M., Gerardo N.M., Currie C.R.; RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals RT insights into its obligate symbiotic lifestyle."; RL PLoS Genet. 7:e1002007-e1002007(2011). RN [2] {ECO:0000313|EnsemblMetazoa:XP_012057810.1} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (APR-2016) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_012057810.1; XM_012202420.1. DR EnsemblMetazoa; XM_012202420.1; XP_012057810.1; LOC105620943. DR GeneID; 105620943; -. DR KEGG; acep:105620943; -. DR Proteomes; UP000005205; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005205}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000005205}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 1336 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007629240. FT DOMAIN 271 475 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 481 569 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 717 754 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 409 409 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 413 413 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 419 419 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 541 561 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 744 753 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1336 AA; 148691 MW; 412B79E8D9C3BE4D CRC64; MFWLHCGLFV LVIAVRGFIS SLADTTSKRE ADYTLDDSFW KEEETPAGEV ERLLHEYRQN QELIRNIGGH YYQIIYPVQL RHHEKMGIST REVGVPKFPQ RGYGDGGYQN PRGRLRTGRH FHRTSLLIKA FNHKFRLDLE LNTQLLAPNL IQKDFLAGNA EQMSKQEIEH CYYHGTVRDY PGASAAFHTC NGVSGVIHLG NETFVIHPFY GGDLSQKHPH IIFEARTKVN KGCANSGNLE WRVKNRRQKH IFGLSETISD RYKRDVREAT KYIETAIIID KAMFDKRNGS TRAEVVHDAI QVANIADLYF RTLNTRVSVV YIESWKGSNQ AQIDNGIDID QALLSFNDYT MRRMYQVAQD TTQLLTGETF SGGESGVAVP ETVCSQRSVG ISVDLNTYEP HLLAGTMAHM IGHNIGMSHD DGRNDCNCRD WHGCIMAQSI VGLENVQPYK FSECSKTDYI EALKSGHGIC LFNKPNELEI RRSCGNRVID DGEQCDCGSI EECKEYDPCC DPITCKLTTE AECATGPCCS DCKLRARGVV CRESTNECDL PEMCTGDTGQ CPPDVYKKNG NSCANNAGHC FNGICPALDL QCEQVWGYGG IAADQECFEQ FNSKGSINGH CGTDSSGHLI KCESENVRCG SLQCQQGSKQ PVIDGMKDLH TRTIISIKNQ EYECKATNGR VEGSDIPGMG LVRDGTSCGD NLICVNQTCT SLFPYIDQEK CPSNHDDKEC SGNGVCTNVN KCHCFLGWSG PDCSIEQSIP TALPTTPQTE VVPKSDSKLP EKKETPYENY HGSNTVFLVG MLMSVVGGVF VLFTLVALCY RSVVVHKNFS LCLRRKSTVQ KYDPPYSKKP QQKSYSGVSG NHHAEAAALD TVNKILTFGS MPQYSRGETQ RVLFRHPNNV VTADGPRVKE HKPQPKRLGV EEEDGGTGAE EVVSFIDLPP NNLTKLPEKG ILKKHGGYGL GGGAIEHVER TLNQLNGYHE DILEVLKNAA SRRDLVGTPS GSNLLDEDAL RKSLAECGYP DVYRKDTDGQ DNGIDNGQEE EEDDVELQPP CGTIRIRNLE DLIRQLEHRA SARPYMTSQM SPSGSEEIRT SETEPDRHYR IDSSVCSESS QGSRRCSRGR DEDASRFVYG RYRQPTSRSP YGNHQHTHQH SHQMHPEDEG IYETADPDRG SNTRGETPDC ESDAFIQAQQ QVARWTSEDG GGGGGGGVQH RPPQQPPPPP AMPVQQQAQQ QQHQLPVEQL PITQRGYYPS PPQIENNLDA GSNAEVESAQ SQQQQSEVRG IDVNHTPNIN KRPLDDNFSL DCNIMNNDSP KELITNNTSD NENTALLSHH FPEYKH // ID A0A158R5T3_9BILA Unreviewed; 1104 AA. AC A0A158R5T3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 31-JAN-2018, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:SMUV_0000805701-mRNA-1}; OS Syphacia muris. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Oxyurida; OC Oxyuroidea; Oxyuridae; Syphacia. OX NCBI_TaxID=451379 {ECO:0000313|WBParaSite:SMUV_0000805701-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000805701-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:SMUV_0000805701-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (APR-2016) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; SMUV_0000805701-mRNA-1; SMUV_0000805701-mRNA-1; SMUV_0000805701. DR Proteomes; UP000046393; Genome Assembly. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000046393}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000046393}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 740 762 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 212 412 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 421 508 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT METAL 349 349 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 353 353 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 359 359 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 366 371 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 480 500 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 1104 AA; 123292 MW; 18F03D7B15035AC4 CRC64; MKSRIVCIVR QIPINKQFIS RFPTGEFEVV YPFQQRERSD RTNVDTRIRH SSSNSTTHYK HTTVVIRSSY FGRFKLFLSL KEFIFANDTE FREYNSKESF TRRKGFENCY YEGNVNKSSN SFVGLSTCNG LRGMIYPGKG VSFGIWPLVG GEQNRGRRPH LLYVMRWSRE AVCGSQVPKV LQQVSSKVYL MLASIIVVLS VHDKRDVTDQ IKYAELAIIA DKSFMSDYSL SKNKAVDFIL ETVNVADSVF FYNFNIHLSI VYSELWLDTQ RIITDKDIER TLSEAVAYVT ADPLYHIKKD VAIFLTREQF ANNEITSSTY GDACSSRATA IVTVTDTYTT HETTSAVIHS LAHILGIGHD DSNCNCDQKL CLMERSFGQL NGTFAWEMSS CSVDHLNKNL KLGHLQCLLN KPHQFSQESS LDLCGNGVVN DGEECDCGSR DSCKDECCDP LTCTLRLQAQ CASHQACCNK CKFLPKGHVC RERRSACDVQ EECDGESGDC PPDGYLVDGT PCGINGQCWK SNCADSESQC KQLWGNNAST AQDRCFERNE MGTVDANCGI DEENRFKKCQ SENAKCGLLH CQGGLAVPSE KTLDFYTAHF HHHGRYIQCK TVNHTNISMV HDGSECGKGK VCVQGKCLLL EKVSPPVQCP TTNLALACSG HGHCTTSLKC VCFSGWIGEA CSVRTETNLN IHPTIAVDIK KSLTPVTTGK IFDVYYITLI NRHKHSFAFL AVKTFNTTTL LAILLCAGIL LLVLLVCLLF CYRRRSSSEF LDNPLGDKLN ESIPENTDRA IKFGNMPSYR DEKRKRKKNK RVYDALHRIN EATDERDSIS LKSRESGGKN SAVGSANGST VACSEQVVGY GVDNNRMFNR VINSSGSFAL KNSNSSKRLL NDGEIYSRSP CSEILASPSQ RIVYGQNDAQ FEKNRSGYAT DTELGTSPYP ARYIDNFSMT RVDLSPTLSD ASAARMTPTP LRLNNIGRLL KQLRYNDDMT SETDPCTVDE NGLNHTEFHI SEDLKGQFDR EAIKLSSSNE LPEVCEVRTA TPVILQAPGD TSASKKSETV NIAKWSDENT SANNEYENQP EKSQIPPQTE QTSSLFSDPF RLEL // ID A0A183CJR3_GLOPA Unreviewed; 908 AA. AC A0A183CJR3; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 28-MAR-2018, entry version 10. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:GPLIN_001311900}; OS Globodera pallida (Potato cyst nematode). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Tylenchida; OC Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae; Globodera. OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_001311900}; RN [1] {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_001311900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741, RC ECO:0000313|WBParaSite:GPLIN_001311900}; RA Li W., Chetelat R.T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_001311900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741, RC ECO:0000313|WBParaSite:GPLIN_001311900}; RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., RA Thorpe P., Tsai I.J., Beasley H., Blok V., Cock P.J.A., RA Van den Akker S.E., Holroyd N., Hunt M., Mantelin S., Naghra H., RA Pain A., Palomares-Rius J.E., Zarowiecki M., Berriman M., Jones J.T., RA Urwin P.E.; RT "The genome and life-stage specific transcriptomes of Globodera RT pallida elucidate key aspects of plant parasitism by a cyst RT nematode."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|WBParaSite:GPLIN_001311900} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (JUN-2016) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; GPLIN_001311900; GPLIN_001311900; GPLIN_001311900. DR Proteomes; UP000050741; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050741}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000050741}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 625 647 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 111 301 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 320 407 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT METAL 250 250 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 254 254 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 260 260 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 379 399 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 908 AA; 97475 MW; 599761E56900E513 CRC64; MNTFFMRGLD ASDKSLVKVE NCFYQGTING NSDTLSAMST CDGLLGLIAF PNGTVFAIWP LEGGDRLRRH PHVLYRVRMG KEEMKCGAAA QFVAKWHGEG AKEGKWRRAA EDQKLALIGD HSFTLQFNLS LQKAVEYALN VVNLADLLLR RDLGVCLSVP FAEFWTDSQR IESATTAVDT QRMLGNVLDY ATGNIYDVEK DATVLLTGQR MSGGDTMTSS FASLCTSRAV GVVQVSDPFS PHVNAMSLAH SVAHLLGIGH DSSECTCGDL DSPKGSTPSV EALPLHFSAC SMARLHALLH QSQSGQLQCL FVRPFQTSRL FQCGNGVLDG DEQCDCGRRE QCDDPCCDPL SCQLKAHAQC ASHQPCCQHC QLRSSGHFCR QSKSVCDIAE KCDGKSGECP LDEHLVDGVL CGLSGLCWKG ECVDAERQCQ ELWGPGAKPA DEQCFLHNSR GLEYGHCGKD AEGRFVECAG ENARCGVLHC RGGATSPLEA NASSFNLQFA REQRQLQCKV VANSAHGMVS DGTSCGSGRI CVRAVCVPLA QVSPPLACPS NNLALSCSGH GDCTTGRNCV CFDGWTGSSC AVRMPLTSHS RRIVSAPMDD DSGPVELLVP PSIRLGGRAL ETATLLGILL LVGFLLLLLL ICLLLCYRRK SSVRAFGRDV RHNERAKVAD EEDCGDGDGG TGGRAIKFGQ MPSYREEKRK RKANKKVYDA LQRITEANEV DSLSLKSRES SSVGAVLATD GRVPTNSQNQ SEMPFSPQPM ERLINSPIVT NGGIGKSRSM RGATSDDGTE KYATEMAHFG GPLSSDIGGH SIRADSEHFA GFGTFAAPPR LVHIQMLMRR LDGAMGDEPS AGEEDGHISS RTPSAGGSAP CPAASTDSGH PGSSFDIRAE SPSLFSDPYK LDRLDLPG // ID A8XMR2_CAEBR Unreviewed; 1045 AA. AC A8XMR2; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 2. DT 28-MAR-2018, entry version 78. DE SubName: Full=Protein CBR-UNC-71 {ECO:0000313|EMBL:CAP33938.2}; GN Name=unc-71 {ECO:0000313|WormBase:CBG15766}; GN Synonyms=Cbr-unc-71 {ECO:0000313|EMBL:CAP33938.2}; GN ORFNames=CBG15766 {ECO:0000313|WormBase:CBG15766}, GN CBG_15766 {ECO:0000313|EMBL:CAP33938.2}; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP33938.2, ECO:0000313|Proteomes:UP000008549}; RN [1] {ECO:0000313|EMBL:CAP33938.2, ECO:0000313|Proteomes:UP000008549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16 {ECO:0000313|EMBL:CAP33938.2, RC ECO:0000313|Proteomes:UP000008549}; 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., 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE600979; CAP33938.2; -; Genomic_DNA. DR STRING; 6238.CBG15766; -. DR WormBase; CBG15766; CBP38446; WBGene00035908; Cbr-unc-71. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR HOGENOM; HOG000020688; -. DR InParanoid; A8XMR2; -. DR OMA; PKKHFHR; -. DR OrthoDB; EOG091G01L9; -. DR Proteomes; UP000008549; Chromosome III. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008549}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008549}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 1045 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002730773. FT TRANSMEM 740 764 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 219 420 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 426 513 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 485 505 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 1045 AA; 115229 MW; 47C912FF30FB3250 CRC64; MVGLLMIVLC SIGEVIAKVD IRQTTANKAF METMRADGYE IRIGIDTRNY FLKAQEHYAH VTIVIRSTQL GRLKLVLERN NFVFLNQTAF HKLDADGERV IQNRVENCYY QGTVGGEESS FVALSSCNGL RGVISFANGT TYGIWPLDGG DRNSRRHPHI LYKSEWGQEA KCGSSMAHSV GERVKRSENI VQHKHRKHHR RYEGVEPNLA KRDVSKRTKY VEVALIADYE FMKQRGLHDM DAISYMLESL NVADSMLSRD LNIRLSAVYV ELWSDVQRID LHEDIERTLS GVVDYAAGHI YHIQKDASIL FTGAGGFANQ EVSNAAIRSI CTARSAVILR GVEQFATHWN GELLAQSIGH LLGLEHDTTA CSCEPSPECV MRQQPGRLGA PFTWQFSKCS VARMHGIWQD GNIQCLLNKP FQVSELRECG NGIVDGNEEC DCGTRENCQD PCCDPLTCTL RPHAQCAAHQ KCCHRCELRK SGETCRSSKS PCDVAEVCDG KSGDCPPDGH LIDGTVCGQD GQCWRGNCSD NHEQCQKLWG REARVAEPVC FEQNTKGAEY ANCGVQNDGN YHSCQLEDAR CGTLHCHSGS LTPTDATLKA FTFHFTENEK QVQCKSIALS TRASGSAYQA SMVSDGTNCG SGRVCVGGSC VEMSSVTSAT ACPTNNLALL CSGHGHCTTT AKCVCFNGWA GAACDIRSNT STYQAGMGFD PFKTSERDGH ISIGSKKIVI PHIGTTLDTI TLFAILLGFG MFLMLCLVCL MVCYRRRSIV EIPKPSDEKL EESPDRQIKF GNMPSYREEK RKRKSNKRIY GALNRITEAD ERDSTSLRSR DSVGSQPMLI RDPYATNEHI YAESTSSAAP RQFRGINSDG SYPLRSFGSW RSSAQISPAS SSGHLTDVST STTPLRLNKI GKLLKTMQQS DDEASVTTSP FSENHYHLQN LQQVNESVDL LIILQNQSHH PLLSGGRLDH GYTGEEELSA VEADHDVGSN TESSRGCEDP GDPGGCWDPP SLVNGSSSGN NYNFRQSPSL FSDPFKLEMT NSMHN // ID ADA11_HUMAN Reviewed; 769 AA. AC O75078; Q14808; Q14809; Q14810; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 3. DT 28-FEB-2018, entry version 161. DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 11; DE Short=ADAM 11; DE AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein; DE Short=MDC; DE Flags: Precursor; GN Name=ADAM11; Synonyms=MDC; 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). RC TISSUE=Brain; RX PubMed=9693107; DOI=10.1042/bj3340093; RA Sagane K., Ohya Y., Hasegawa Y., Tanaka I.; RT "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 RT and MDC3: novel human cellular disintegrins highly expressed in the RT brain."; RL Biochem. J. 334:93-98(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). RC TISSUE=Cerebellum; RX PubMed=8252040; DOI=10.1038/ng1093-151; RA Emi M., Katagiri T., Harada Y., Saito H., Inazawa J., Ito I., RA Kasumi F., Nakamura Y.; RT "A novel metalloprotease/disintegrin-like gene at 17q21.3 is RT somatically rearranged in two primary breast cancers."; RL Nat. Genet. 5:151-157(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-769 (ISOFORMS LONG AND RP SHORT). RC TISSUE=Brain, Mammary gland, Ovary, and Testis; RX PubMed=7956356; RA Katagiri T., Harada Y., Emi M., Nakamura Y.; RT "Human metalloprotease/disintegrin-like (MDC) gene: exon-intron RT organization and alternative splicing."; RL Cytogenet. Cell Genet. 68:39-44(1995). RN [4] 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:R8.1-R8.16(2004). RN [5] RP VARIANT [LARGE SCALE ANALYSIS] ARG-693. RX PubMed=18772397; DOI=10.1126/science.1164368; RA Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P., RA Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., RA Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., RA Nikolsky Y., Hartigan J., Smith D.R., Hidalgo M., Leach S.D., RA Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C., RA Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N., RA Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.; RT "Core signaling pathways in human pancreatic cancers revealed by RT global genomic analyses."; RL Science 321:1801-1806(2008). CC -!- FUNCTION: Probable ligand for integrin in the brain. This is a non CC catalytic metalloprotease-like protein. CC -!- SUBUNIT: Can bind to LGI1 and LGI4. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; Synonyms=MDC-769; CC IsoId=O75078-1; Sequence=Displayed; CC Name=Short; Synonyms=MDC-524; CC IsoId=O75078-2; Sequence=VSP_005472, VSP_005473, VSP_005474, CC VSP_005475; 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 predominantly in brain. Slightly CC detected or not at all in other tissues. CC -!- DOMAIN: A conserved motif [AVN[ED]CD] within the disintegrin-like CC domain could be involved in the binding to the integrin receptor. CC -!- PTM: The precursor is cleaved by a furin endopeptidase. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB009675; BAA32352.1; -; mRNA. DR EMBL; D17390; BAA04213.1; -; mRNA. DR EMBL; D31872; BAA06670.1; -; Genomic_DNA. DR EMBL; D31872; BAA06671.1; -; Genomic_DNA. DR CCDS; CCDS11486.1; -. [O75078-1] DR PIR; I65967; I65967. DR PIR; S38539; S38539. DR RefSeq; NP_002381.2; NM_002390.5. [O75078-1] DR UniGene; Hs.6088; -. DR ProteinModelPortal; O75078; -. DR SMR; O75078; -. DR BioGrid; 110351; 4. DR IntAct; O75078; 1. DR STRING; 9606.ENSP00000200557; -. DR MEROPS; M12.976; -. DR TCDB; 8.A.77.1.1; the sheddase (sheddase) family. DR iPTMnet; O75078; -. DR PhosphoSitePlus; O75078; -. DR BioMuta; ADAM11; -. DR PaxDb; O75078; -. DR PeptideAtlas; O75078; -. DR PRIDE; O75078; -. DR DNASU; 4185; -. DR Ensembl; ENST00000200557; ENSP00000200557; ENSG00000073670. [O75078-1] DR GeneID; 4185; -. DR KEGG; hsa:4185; -. DR UCSC; uc002ihh.4; human. [O75078-1] DR CTD; 4185; -. DR DisGeNET; 4185; -. DR EuPathDB; HostDB:ENSG00000073670.13; -. DR GeneCards; ADAM11; -. DR HGNC; HGNC:189; ADAM11. DR MIM; 155120; gene. DR neXtProt; NX_O75078; -. DR OpenTargets; ENSG00000073670; -. DR PharmGKB; PA24506; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR HOGENOM; HOG000231962; -. DR HOVERGEN; HBG050456; -. DR InParanoid; O75078; -. DR KO; K16067; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR PhylomeDB; O75078; -. DR TreeFam; TF314733; -. DR Reactome; R-HSA-5682910; LGI-ADAM interactions. DR ChiTaRS; ADAM11; human. DR GeneWiki; ADAM11; -. DR GenomeRNAi; 4185; -. DR PRO; PR:O75078; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; ENSG00000073670; -. DR CleanEx; HS_ADAM11; -. DR ExpressionAtlas; O75078; baseline and differential. DR Genevisible; O75078; HS. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005178; F:integrin binding; TAS:ProtInc. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc. DR GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:ProtInc. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Cleavage on pair of basic residues; KW Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein; KW Membrane; Polymorphism; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 23 {ECO:0000255}. FT PROPEP 24 225 {ECO:0000250}. FT /FTId=PRO_0000029074. FT CHAIN 226 769 Disintegrin and metalloproteinase domain- FT containing protein 11. FT /FTId=PRO_0000029075. FT TOPO_DOM 226 734 Extracellular. {ECO:0000255}. FT TRANSMEM 735 755 Helical. {ECO:0000255}. FT TOPO_DOM 756 769 Cytoplasmic. {ECO:0000255}. FT DOMAIN 239 438 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 444 531 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT DOMAIN 677 709 EGF-like. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT COMPBIAS 532 676 Cys-rich. FT CARBOHYD 96 96 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 163 163 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 605 605 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 673 673 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 349 433 {ECO:0000250}. FT DISULFID 392 417 {ECO:0000250}. FT DISULFID 394 401 {ECO:0000250}. FT DISULFID 503 523 {ECO:0000250}. FT DISULFID 677 692 {ECO:0000250}. FT DISULFID 686 698 {ECO:0000250}. FT DISULFID 700 709 {ECO:0000250}. FT VAR_SEQ 1 99 Missing (in isoform Short). FT {ECO:0000303|PubMed:8252040}. FT /FTId=VSP_005472. FT VAR_SEQ 100 104 DLELN -> MCWLS (in isoform Short). FT {ECO:0000303|PubMed:8252040}. FT /FTId=VSP_005473. FT VAR_SEQ 595 623 DVLCGFLLCVNISGAPRLGDLVGDISSVT -> PQQGRAVW FT LPPLCQHLWSSSARGPGGRHQ (in isoform Short). FT {ECO:0000303|PubMed:8252040}. FT /FTId=VSP_005474. FT VAR_SEQ 624 769 Missing (in isoform Short). FT {ECO:0000303|PubMed:8252040}. FT /FTId=VSP_005475. FT VARIANT 693 693 S -> R (in a pancreatic ductal FT adenocarcinoma sample; somatic mutation). FT {ECO:0000269|PubMed:18772397}. FT /FTId=VAR_062669. FT CONFLICT 106 106 H -> Q (in Ref. 2; BAA06670 and 3; FT BAA06671). {ECO:0000305}. FT CONFLICT 325 325 D -> N (in Ref. 2; BAA04213). FT {ECO:0000305}. SQ SEQUENCE 769 AA; 83418 MW; EEB091EB6730AC36 CRC64; MRLLRRWAFA ALLLSLLPTP GLGTQGPAGA LRWGGLPQLG GPGAPEVTEP SRLVRESSGG EVRKQQLDTR VRQEPPGGPP VHLAQVSFVI PAFNSNFTLD LELNHHLLSS QYVERHFSRE GTTQHSTGAG DHCYYQGKLR GNPHSFAALS TCQGLHGVFS DGNLTYIVEP QEVAGPWGAP QGPLPHLIYR TPLLPDPLGC REPGCLFAVP AQSAPPNRPR LRRKRQVRRG HPTVHSETKY VELIVINDHQ LFEQMRQSVV LTSNFAKSVV NLADVIYKEQ LNTRIVLVAM ETWADGDKIQ VQDDLLETLA RLMVYRREGL PEPSDATHLF SGRTFQSTSS GAAYVGGICS LSHGGGVNEY GNMGAMAVTL AQTLGQNLGM MWNKHRSSAG DCKCPDIWLG CIMEDTGFYL PRKFSRCSID EYNQFLQEGG GSCLFNKPLK LLDPPECGNG FVEAGEECDC GSVQECSRAG GNCCKKCTLT HDAMCSDGLC CRRCKYEPRG VSCREAVNEC DIAETCTGDS SQCPPNLHKL DGYYCDHEQG RCYGGRCKTR DRQCQVLWGH AAADRFCYEK LNVEGTERGS CGRKGSGWVQ CSKQDVLCGF LLCVNISGAP RLGDLVGDIS SVTFYHQGKE LDCRGGHVQL ADGSDLSYVE DGTACGPNML CLDHRCLPAS AFNFSTCPGS GERRICSHHG VCSNEGKCIC QPDWTGKDCS IHNPLPTSPP TGETERYKGP SGTNIIIGSI AGAVLVAAIV LGGTGWGFKN IRRGRSGGA // ID ADA11_MOUSE Reviewed; 773 AA. AC Q9R1V4; A2AUA8; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 28-FEB-2018, entry version 141. DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 11; DE Short=ADAM 11; DE AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein; DE Short=MDC; DE Flags: Precursor; GN Name=Adam11; Synonyms=Mdc; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=10433968; DOI=10.1016/S0378-1119(99)00253-X; RA Sagane K., Yamazaki K., Mizui Y., Tanaka I.; RT "Cloning and chromosomal mapping of mouse ADAM11, ADAM22 and ADAM23."; RL Gene 236:79-86(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP INTERACTION WITH LGI1 AND LGI4. RX PubMed=18974846; DOI=10.7150/ijbs.4.387; RA Sagane K., Ishihama Y., Sugimoto H.; RT "LGI1 and LGI4 bind to ADAM22, ADAM23 and ADAM11."; RL Int. J. Biol. Sci. 4:387-396(2008). CC -!- FUNCTION: Probable ligand for integrin in the brain. This is a non CC catalytic metalloprotease-like protein. CC -!- SUBUNIT: Can bind to LGI1 and LGI4. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Highly expressed in the brain. Weakly detected CC in the heart, liver and testis. CC -!- DOMAIN: A conserved motif [AVN[ED]CD] within the disintegrin-like CC domain could be involved in the binding to the integrin receptor. CC -!- PTM: The precursor is cleaved by a furin endopeptidase. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB009676; BAA83384.1; -; mRNA. DR EMBL; AL929067; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS25503.1; -. DR RefSeq; NP_033743.2; NM_009613.3. DR UniGene; Mm.89854; -. DR ProteinModelPortal; Q9R1V4; -. DR SMR; Q9R1V4; -. DR IntAct; Q9R1V4; 1. DR STRING; 10090.ENSMUSP00000069466; -. DR MEROPS; M12.976; -. DR iPTMnet; Q9R1V4; -. DR PhosphoSitePlus; Q9R1V4; -. DR MaxQB; Q9R1V4; -. DR PaxDb; Q9R1V4; -. DR PRIDE; Q9R1V4; -. DR Ensembl; ENSMUST00000103081; ENSMUSP00000099370; ENSMUSG00000020926. DR GeneID; 11488; -. DR KEGG; mmu:11488; -. DR UCSC; uc007lsi.2; mouse. DR CTD; 4185; -. DR MGI; MGI:1098667; Adam11. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR HOGENOM; HOG000231962; -. DR HOVERGEN; HBG050456; -. DR InParanoid; Q9R1V4; -. DR KO; K16067; -. DR Reactome; R-MMU-5682910; LGI-ADAM interactions. DR PRO; PR:Q9R1V4; -. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; ENSMUSG00000020926; -. DR CleanEx; MM_ADAM11; -. DR ExpressionAtlas; Q9R1V4; baseline and differential. DR Genevisible; Q9R1V4; MM. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Cleavage on pair of basic residues; Complete proteome; Disulfide bond; KW EGF-like domain; Glycoprotein; Membrane; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 24 {ECO:0000255}. FT PROPEP 25 229 {ECO:0000250}. FT /FTId=PRO_0000029076. FT CHAIN 230 773 Disintegrin and metalloproteinase domain- FT containing protein 11. FT /FTId=PRO_0000029077. FT TOPO_DOM 230 738 Extracellular. {ECO:0000255}. FT TRANSMEM 739 759 Helical. {ECO:0000255}. FT TOPO_DOM 760 773 Cytoplasmic. {ECO:0000255}. FT DOMAIN 243 442 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 448 535 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT DOMAIN 681 713 EGF-like. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT COMPBIAS 536 680 Cys-rich. FT CARBOHYD 100 100 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 167 167 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 609 609 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 677 677 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 353 437 {ECO:0000250}. FT DISULFID 396 421 {ECO:0000250}. FT DISULFID 398 405 {ECO:0000250}. FT DISULFID 507 527 {ECO:0000250}. FT DISULFID 681 696 {ECO:0000250}. FT DISULFID 690 702 {ECO:0000250}. FT DISULFID 704 713 {ECO:0000250}. FT CONFLICT 181 181 W -> R (in Ref. 1; BAA83384). FT {ECO:0000305}. FT CONFLICT 218 218 A -> T (in Ref. 1; BAA83384). FT {ECO:0000305}. FT CONFLICT 340 340 Q -> K (in Ref. 1; BAA83384). FT {ECO:0000305}. SQ SEQUENCE 773 AA; 84134 MW; F3F0131ECDA58D72 CRC64; MRRLRRWAIA ALLLLPLLPP PGLGALGPRG ALHWRSSAHV GSPESPEGSE VTEPSRLVRQ SSGGEVRKPQ LDTRVRQDPP RGTPVHLAQV SFVIPAFDSN FTLDLELNHH LLSSQYVERH FSREGTRQHS TGAGDHCYYH GKLRGNPQSF AALSTCQGLH GVFSDGNLTY IVEPKEIAGP WGPPQGPLPH LIYRTPLLPA PLGCREPGCL FAVPAQSALP NWPKLRRKRQ VRRGHPTVHS ETKYVELIVI NDHQLFEQMR QSVVLTSNFA KSVVNLADVI YKEQLNTRIV LVAMETWADG DKIQVQDDLL ETLARLMVYR REGLPEPSDA THLFSGRTFQ STSSGAAYVG GICSLSRGGG VNEYGNMGAM AVTLAQTLGQ NLGMMWNKHR SSAGDCKCPD IWLGCIMEDT GFYLPRKFSR CSIDEYNQFL QEGGGSCLFN KPLKLLDPPE CGNGFVEAGE ECDCGSVQEC SRAGGNCCKK CTLTHDAMCS DGLCCRRCKY EPRGVSCREA VNECDIAETC TGDSSQCPPN LHKLDGYYCD HEQGRCYGGR CKTRDRQCQA LWGHAAADRF CYEKLNVEGT ERGNCGRKGS GWVQCSKQDV LCGFLLCVNI SGAPRLGDLG GDISSVTFYH QGKELDCRGG HVQLADGSDL SYVEDGTACG PNMLCLDHRC LPASAFNFST CPGSGERRIC SHHGVCSNEG KCICQPDWTG KDCSIHNPLP TSPPTGETER YKGPSGTNII IGSIAGAVLV AAIVLGGTGW GFKNIRRGRS GGA // ID ADA22_HUMAN Reviewed; 906 AA. AC Q9P0K1; O75075; O75076; Q9P0K2; Q9UIA1; Q9UKK2; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 23-MAY-2018, entry version 171. DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 22; DE Short=ADAM 22; DE AltName: Full=Metalloproteinase-disintegrin ADAM22-3; DE AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 2; DE Flags: Precursor; GN Name=ADAM22; Synonyms=MDC2; 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 3 AND 4). RC TISSUE=Brain; RX PubMed=9693107; DOI=10.1042/bj3340093; RA Sagane K., Ohya Y., Hasegawa Y., Tanaka I.; RT "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 RT and MDC3: novel human cellular disintegrins highly expressed in the RT brain."; RL Biochem. J. 334:93-98(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX PubMed=11050470; DOI=10.1111/j.1349-7006.2000.tb00877.x; RA Harada T., Nishie A., Torigoe K., Ikezaki K., Shono T., Maehara Y., RA Kuwano M., Wada M.; RT "The specific expression of three novel splice variant forms of human RT metalloprotease-like disintegrin-like cysteine-rich protein 2 gene in RT brain tissues and gliomas."; RL Jpn. J. Cancer Res. 91:1001-1006(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANT ARG-81. RC TISSUE=Brain; RA Wada M., Torigoe K., Harada T., Kuwano M.; RT "Isolation and tissue specific expression of novel ADAM family from RT 7q21.1 region."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX 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 [MRNA] OF 40-906 (ISOFORM 1), AND VARIANT ARG-81. RC TISSUE=Cerebellum; RX PubMed=10524237; DOI=10.1016/S0378-1119(99)00302-9; RA Poindexter K., Nelson N., DuBose R.F., Black R.A., Cerretti D.P.; RT "The identification of seven metalloproteinase-disintegrin (ADAM) RT genes from genomic libraries."; RL Gene 237:61-70(1999). RN [6] RP FUNCTION, INTERACTION WITH YWHAZ, AND MUTAGENESIS OF SER-834 AND RP SER-857. RX PubMed=12589811; DOI=10.1016/S0006-291X(03)00056-1; RA Zhu P., Sun Y., Xu R., Sang Y., Zhao J., Liu G., Cai L., Li C., RA Zhao S.; RT "The interaction between ADAM 22 and 14-3-3zeta: regulation of cell RT adhesion and spreading."; RL Biochem. Biophys. Res. Commun. 301:991-999(2003). RN [7] 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:R8.1-R8.16(2004). RN [8] RP FUNCTION, INTERACTION WITH YWHAB, AND MUTAGENESIS OF SER-834 AND RP SER-857. RX PubMed=15882968; DOI=10.1016/j.bbrc.2005.03.229; RA Zhu P., Sang Y., Xu H., Zhao J., Xu R., Sun Y., Xu T., Wang X., RA Chen L., Feng H., Li C., Zhao S.; RT "ADAM22 plays an important role in cell adhesion and spreading with RT the assistance of 14-3-3."; RL Biochem. Biophys. Res. Commun. 331:938-946(2005). RN [9] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=16385342; DOI=10.1227/01.NEU.0000192363.84287.8B; RA D'Abaco G.M., Ng K., Paradiso L., Godde N.J., Kaye A., Novak U.; RT "ADAM22, expressed in normal brain but not in high-grade gliomas, RT inhibits cellular proliferation via the disintegrin domain."; RL Neurosurgery 58:179-186(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 233-736, GLYCOSYLATION AT RP ASN-519; ASN-634 AND ASN-675, DISULFIDE BONDS, AND FUNCTION. RX PubMed=19692335; DOI=10.1074/jbc.M109.014258; RA Liu H., Shim A.H., He X.; RT "Structural characterization of the ectodomain of a disintegrin and RT metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of RT metalloproteinase: insights on ADAM function."; RL J. Biol. Chem. 284:29077-29086(2009). CC -!- FUNCTION: Probable ligand for integrin in the brain. This is a non CC catalytic metalloprotease-like protein (PubMed:19692335). Involved CC in regulation of cell adhesion and spreading and in inhibition of CC cell proliferation. Neuronal receptor for LGI1. CC {ECO:0000269|PubMed:12589811, ECO:0000269|PubMed:15882968, CC ECO:0000269|PubMed:16385342, ECO:0000269|PubMed:19692335}. CC -!- SUBUNIT: Interacts with LGI1 and can bind to LGI4 (By similarity). CC Interacts with KCNA2, DLG2 and DLG4 (By similarity). Interacts CC through its C-terminal region with YWHAB/14-3-3 beta and YWHAZ/14- CC 3-3 zeta but not with YWHAE/14-3-3 epsilon or YWHAH/14-3-3 eta. CC {ECO:0000250|UniProtKB:Q9R1V6, ECO:0000269|PubMed:12589811, CC ECO:0000269|PubMed:15882968}. CC -!- INTERACTION: CC P31946:YWHAB; NbExp=2; IntAct=EBI-1567267, EBI-359815; CC P27348:YWHAQ; NbExp=2; IntAct=EBI-1567267, EBI-359854; CC P63104:YWHAZ; NbExp=3; IntAct=EBI-1567236, EBI-347088; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q9R1V6}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=Epsilon; CC IsoId=Q9P0K1-1; Sequence=Displayed; CC Name=2; Synonyms=Delta; CC IsoId=Q9P0K1-2; Sequence=VSP_005482, VSP_005484; 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 Ref.2 (AAF73288) sequence is in conflict in position: 848:G->E. CC {ECO:0000305}; CC Name=3; Synonyms=Alpha; CC IsoId=Q9P0K1-3; Sequence=VSP_005483; CC Name=4; Synonyms=Beta; CC IsoId=Q9P0K1-4; Sequence=VSP_005482, VSP_005483; CC Name=5; CC IsoId=Q9P0K1-5; Sequence=VSP_005482; CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and in some CC high-grade but not low-grade gliomas. Detected slightly or not at CC all in other tissues. {ECO:0000269|PubMed:16385342}. CC -!- PTM: The precursor is cleaved by a furin endopeptidase. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB009671; BAA32349.1; -; mRNA. DR EMBL; AB009671; BAA32350.1; -; mRNA. DR EMBL; AF155381; AAF73288.1; -; mRNA. DR EMBL; AF155382; AAF73289.1; -; mRNA. DR EMBL; AF073291; AAF22476.2; -; mRNA. DR EMBL; AC005075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF158637; AAD55251.1; -; mRNA. DR CCDS; CCDS43608.1; -. [Q9P0K1-2] DR CCDS; CCDS43609.1; -. [Q9P0K1-5] DR CCDS; CCDS43610.1; -. [Q9P0K1-3] DR CCDS; CCDS47637.1; -. [Q9P0K1-1] DR RefSeq; NP_004185.1; NM_004194.4. [Q9P0K1-3] DR RefSeq; NP_068367.1; NM_021721.4. [Q9P0K1-4] DR RefSeq; NP_068368.2; NM_021722.5. [Q9P0K1-2] DR RefSeq; NP_068369.1; NM_021723.4. [Q9P0K1-1] DR UniGene; Hs.256398; -. DR PDB; 3G5C; X-ray; 2.36 A; A/B=233-736. DR PDBsum; 3G5C; -. DR ProteinModelPortal; Q9P0K1; -. DR SMR; Q9P0K1; -. DR BioGrid; 119789; 13. DR ELM; Q9P0K1; -. DR IntAct; Q9P0K1; 12. DR MINT; Q9P0K1; -. DR STRING; 9606.ENSP00000265727; -. DR MEROPS; M12.978; -. DR iPTMnet; Q9P0K1; -. DR PhosphoSitePlus; Q9P0K1; -. DR BioMuta; ADAM22; -. DR DMDM; 14423634; -. DR MaxQB; Q9P0K1; -. DR PaxDb; Q9P0K1; -. DR PeptideAtlas; Q9P0K1; -. DR PRIDE; Q9P0K1; -. DR Ensembl; ENST00000265727; ENSP00000265727; ENSG00000008277. [Q9P0K1-1] DR Ensembl; ENST00000398201; ENSP00000381260; ENSG00000008277. [Q9P0K1-3] DR Ensembl; ENST00000398204; ENSP00000381262; ENSG00000008277. [Q9P0K1-5] DR Ensembl; ENST00000398209; ENSP00000381267; ENSG00000008277. [Q9P0K1-2] DR GeneID; 53616; -. DR KEGG; hsa:53616; -. DR UCSC; uc003ujk.3; human. [Q9P0K1-1] DR CTD; 53616; -. DR DisGeNET; 53616; -. DR EuPathDB; HostDB:ENSG00000008277.14; -. DR GeneCards; ADAM22; -. DR HGNC; HGNC:201; ADAM22. DR HPA; HPA050325; -. DR MIM; 603709; gene. DR neXtProt; NX_Q9P0K1; -. DR OpenTargets; ENSG00000008277; -. DR PharmGKB; PA24518; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR HOGENOM; HOG000231962; -. DR HOVERGEN; HBG050456; -. DR InParanoid; Q9P0K1; -. DR KO; K16068; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR PhylomeDB; Q9P0K1; -. DR TreeFam; TF314733; -. DR Reactome; R-HSA-5682910; LGI-ADAM interactions. DR ChiTaRS; ADAM22; human. DR EvolutionaryTrace; Q9P0K1; -. DR GeneWiki; ADAM22; -. DR GenomeRNAi; 53616; -. DR PRO; PR:Q9P0K1; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000008277; -. DR CleanEx; HS_ADAM22; -. DR ExpressionAtlas; Q9P0K1; baseline and differential. DR Genevisible; Q9P0K1; HS. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005178; F:integrin binding; NAS:UniProtKB. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR GO; GO:0007162; P:negative regulation of cell adhesion; NAS:UniProtKB. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell projection; KW Cleavage on pair of basic residues; Complete proteome; Disulfide bond; KW EGF-like domain; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; KW Receptor; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 25 {ECO:0000255}. FT PROPEP 26 222 {ECO:0000250}. FT /FTId=PRO_0000029112. FT CHAIN 223 906 Disintegrin and metalloproteinase domain- FT containing protein 22. FT /FTId=PRO_0000029113. FT TOPO_DOM 223 736 Extracellular. {ECO:0000255}. FT TRANSMEM 737 757 Helical. {ECO:0000255}. FT TOPO_DOM 758 906 Cytoplasmic. {ECO:0000255}. FT DOMAIN 239 438 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 444 531 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT DOMAIN 675 712 EGF-like. FT COMPBIAS 532 678 Cys-rich. FT MOD_RES 810 810 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9R1V6}. FT MOD_RES 834 834 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 857 857 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9R1V6}. FT MOD_RES 862 862 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9R1V6}. FT MOD_RES 866 866 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9R1V6}. FT MOD_RES 870 870 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9R1V6}. FT CARBOHYD 175 175 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 519 519 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19692335}. FT CARBOHYD 634 634 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19692335}. FT CARBOHYD 675 675 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19692335}. FT DISULFID 349 433 {ECO:0000269|PubMed:19692335}. FT DISULFID 392 417 {ECO:0000269|PubMed:19692335}. FT DISULFID 394 401 {ECO:0000269|PubMed:19692335}. FT DISULFID 447 477 {ECO:0000269|PubMed:19692335}. FT DISULFID 458 474 {ECO:0000269|PubMed:19692335}. FT DISULFID 460 466 {ECO:0000269|PubMed:19692335}. FT DISULFID 473 494 {ECO:0000269|PubMed:19692335}. FT DISULFID 485 491 {ECO:0000269|PubMed:19692335}. FT DISULFID 490 516 {ECO:0000269|PubMed:19692335}. FT DISULFID 503 523 {ECO:0000269|PubMed:19692335}. FT DISULFID 510 542 {ECO:0000269|PubMed:19692335}. FT DISULFID 535 547 {ECO:0000269|PubMed:19692335}. FT DISULFID 554 605 {ECO:0000269|PubMed:19692335}. FT DISULFID 569 635 {ECO:0000269|PubMed:19692335}. FT DISULFID 583 593 {ECO:0000269|PubMed:19692335}. FT DISULFID 600 663 {ECO:0000269|PubMed:19692335}. FT DISULFID 657 668 {ECO:0000269|PubMed:19692335}. FT DISULFID 679 694 {ECO:0000269|PubMed:19692335}. FT DISULFID 688 700 {ECO:0000269|PubMed:19692335}. FT DISULFID 702 711 {ECO:0000269|PubMed:19692335}. FT VAR_SEQ 768 803 Missing (in isoform 2, isoform 4 and FT isoform 5). {ECO:0000303|PubMed:11050470, FT ECO:0000303|PubMed:9693107, FT ECO:0000303|Ref.3}. FT /FTId=VSP_005482. FT VAR_SEQ 859 859 E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in FT isoform 2). FT {ECO:0000303|PubMed:11050470}. FT /FTId=VSP_005484. FT VAR_SEQ 860 906 Missing (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:9693107}. FT /FTId=VSP_005483. FT VARIANT 81 81 P -> R (in dbSNP:rs2279542). FT {ECO:0000269|PubMed:10524237, FT ECO:0000269|Ref.3}. FT /FTId=VAR_020057. FT VARIANT 119 119 H -> Y (in dbSNP:rs4728730). FT /FTId=VAR_051589. FT VARIANT 207 207 V -> I (in dbSNP:rs17255978). FT /FTId=VAR_051590. FT MUTAGEN 834 834 S->A: Abolishes interactions with YWHAB FT and YWHAZ; when associated with A-857. FT {ECO:0000269|PubMed:12589811, FT ECO:0000269|PubMed:15882968}. FT MUTAGEN 857 857 S->A: Abolishes interactions with YWHAB FT and YWHAZ; when associated with A-834. FT {ECO:0000269|PubMed:12589811, FT ECO:0000269|PubMed:15882968}. FT STRAND 235 237 {ECO:0000244|PDB:3G5C}. FT STRAND 239 247 {ECO:0000244|PDB:3G5C}. FT HELIX 249 253 {ECO:0000244|PDB:3G5C}. FT TURN 254 257 {ECO:0000244|PDB:3G5C}. FT HELIX 259 280 {ECO:0000244|PDB:3G5C}. FT STRAND 281 292 {ECO:0000244|PDB:3G5C}. FT HELIX 305 318 {ECO:0000244|PDB:3G5C}. FT STRAND 325 333 {ECO:0000244|PDB:3G5C}. FT STRAND 336 338 {ECO:0000244|PDB:3G5C}. FT STRAND 341 343 {ECO:0000244|PDB:3G5C}. FT TURN 351 353 {ECO:0000244|PDB:3G5C}. FT STRAND 354 359 {ECO:0000244|PDB:3G5C}. FT HELIX 363 378 {ECO:0000244|PDB:3G5C}. FT HELIX 384 389 {ECO:0000244|PDB:3G5C}. FT HELIX 416 427 {ECO:0000244|PDB:3G5C}. FT HELIX 432 435 {ECO:0000244|PDB:3G5C}. FT HELIX 463 466 {ECO:0000244|PDB:3G5C}. FT TURN 467 473 {ECO:0000244|PDB:3G5C}. FT STRAND 486 488 {ECO:0000244|PDB:3G5C}. FT STRAND 491 496 {ECO:0000244|PDB:3G5C}. FT STRAND 502 504 {ECO:0000244|PDB:3G5C}. FT TURN 536 539 {ECO:0000244|PDB:3G5C}. FT STRAND 540 543 {ECO:0000244|PDB:3G5C}. FT STRAND 546 548 {ECO:0000244|PDB:3G5C}. FT HELIX 550 558 {ECO:0000244|PDB:3G5C}. FT HELIX 567 573 {ECO:0000244|PDB:3G5C}. FT TURN 574 576 {ECO:0000244|PDB:3G5C}. FT STRAND 585 590 {ECO:0000244|PDB:3G5C}. FT HELIX 595 597 {ECO:0000244|PDB:3G5C}. FT STRAND 600 602 {ECO:0000244|PDB:3G5C}. FT STRAND 605 607 {ECO:0000244|PDB:3G5C}. FT STRAND 613 617 {ECO:0000244|PDB:3G5C}. FT STRAND 622 628 {ECO:0000244|PDB:3G5C}. FT STRAND 631 637 {ECO:0000244|PDB:3G5C}. FT STRAND 640 645 {ECO:0000244|PDB:3G5C}. FT STRAND 656 658 {ECO:0000244|PDB:3G5C}. FT STRAND 661 666 {ECO:0000244|PDB:3G5C}. FT STRAND 668 670 {ECO:0000244|PDB:3G5C}. FT HELIX 671 674 {ECO:0000244|PDB:3G5C}. FT HELIX 688 690 {ECO:0000244|PDB:3G5C}. FT STRAND 692 695 {ECO:0000244|PDB:3G5C}. FT STRAND 700 702 {ECO:0000244|PDB:3G5C}. FT STRAND 706 708 {ECO:0000244|PDB:3G5C}. SQ SEQUENCE 906 AA; 100433 MW; 265ECCD0FA6C088B CRC64; MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI VPLRLIYRSG GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE DKKVNRQSAR LWETSI // ID ADA22_MOUSE Reviewed; 904 AA. AC Q9R1V6; Q5TLI8; Q5TLI9; Q5TLJ0; Q5TLJ1; Q5TLJ2; Q5TLJ3; Q5TLJ4; AC Q5TLJ5; Q5TLJ6; Q5TLJ7; Q5TLJ8; Q5TLJ9; Q5TLK0; Q5TLK1; Q5TLK2; AC Q5TLK3; Q5TLK4; Q5TLK5; Q5TLK6; Q5TLK7; Q5TLK8; Q8BSF2; Q9R1V5; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 28-MAR-2018, entry version 152. DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 22; DE Short=ADAM 22; DE Flags: Precursor; GN Name=Adam22; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 17 AND 20). RC TISSUE=Brain; RX PubMed=10433968; DOI=10.1016/S0378-1119(99)00253-X; RA Sagane K., Yamazaki K., Mizui Y., Tanaka I.; RT "Cloning and chromosomal mapping of mouse ADAM11, ADAM22 and ADAM23."; RL Gene 236:79-86(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 619-904 (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 [MRNA] OF 709-904 (ISOFORMS 1; 2; 3; 4; 5; 6; 7; RP 8; 9; 10; 11; 12; 13; 14; 15; 16; 17; 18; 19; 20 AND 21), TISSUE RP SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=15876356; DOI=10.1186/1471-2202-6-33; RA Sagane K., Hayakawa K., Kai J., Hirohashi T., Takahashi E., RA Miyamoto N., Ino M., Oki T., Yamazaki K., Nagasu T.; RT "Ataxia and peripheral nerve hypomyelination in ADAM22-deficient RT mice."; RL BMC Neurosci. 6:33-33(2005). RN [4] RP FUNCTION, INTERACTION WITH LGI1, AND MUTAGENESIS OF ASP-509. RX PubMed=16990550; DOI=10.1126/science.1129947; RA Fukata Y., Adesnik H., Iwanaga T., Bredt D.S., Nicoll R.A., Fukata M.; RT "Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate RT synaptic transmission."; RL Science 313:1792-1795(2006). RN [5] RP INTERACTION WITH LIGI1 AND LGI4. RX PubMed=18974846; DOI=10.7150/ijbs.4.387; RA Sagane K., Ishihama Y., Sugimoto H.; RT "LGI1 and LGI4 bind to ADAM22, ADAM23 and ADAM11."; RL Int. J. Biol. Sci. 4:387-396(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-808; SER-832; SER-855; RP SER-860; SER-864 AND SER-868, PHOSPHORYLATION [LARGE SCALE ANALYSIS] RP AT SER-882 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT RP SER-817 (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Brain, and Kidney; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [7] RP INTERACTION WITH KCNA2; LGI1; DLG2 AND DLG4, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=20089912; DOI=10.1523/JNEUROSCI.4661-09.2010; RA Ogawa Y., Oses-Prieto J., Kim M.Y., Horresh I., Peles E., RA Burlingame A.L., Trimmer J.S., Meijer D., Rasband M.N.; RT "ADAM22, a Kv1 channel-interacting protein, recruits membrane- RT associated guanylate kinases to juxtaparanodes of myelinated axons."; RL J. Neurosci. 30:1038-1048(2010). CC -!- FUNCTION: Probable ligand for integrin in the brain. This is a non CC catalytic metalloprotease-like protein. Involved in regulation of CC cell adhesion and spreading and in inhibition of cell CC proliferation (By similarity). Neuronal receptor for LGI1. CC {ECO:0000250|UniProtKB:Q9P0K1, ECO:0000269|PubMed:16990550}. CC -!- SUBUNIT: Interacts with LGI1 (PubMed:18974846, PubMed:20089912). CC Can bind to LGI4(PubMed:18974846). Interacts with KCNA2, DLG2 and CC DLG4 (PubMed:20089912). {ECO:0000269|PubMed:16990550, CC ECO:0000269|PubMed:18974846, ECO:0000269|PubMed:20089912}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20089912}; CC Single-pass type I membrane protein {ECO:0000305}. Cell CC projection, axon {ECO:0000269|PubMed:20089912}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=21; CC Name=1; Synonyms=ADAM22-G01, 22g; CC IsoId=Q9R1V6-3; Sequence=Displayed; CC Name=2; Synonyms=ADAM22-G03, 22g(D27); CC IsoId=Q9R1V6-4; Sequence=VSP_018238; CC Name=3; Synonyms=ADAM22-G06, 22g(D26D27); CC IsoId=Q9R1V6-5; Sequence=VSP_018235; CC Name=4; Synonyms=ADAM22=G07, 22g(D26D27)+29.3; CC IsoId=Q9R1V6-6; Sequence=VSP_018235, VSP_018245; CC Name=5; Synonyms=ADAM22-G08, 22g(D27)+29.3; CC IsoId=Q9R1V6-7; Sequence=VSP_018238, VSP_018245; CC Name=6; Synonyms=ADAM22-G09, 22g+29.3; CC IsoId=Q9R1V6-8; Sequence=VSP_018245; CC Name=7; Synonyms=ADAM22-G10, 22g+29.1; CC IsoId=Q9R1V6-9; Sequence=VSP_018241; CC Name=8; Synonyms=ADAM22-G11, 22g(D27)+29.5+29.7; CC IsoId=Q9R1V6-10; Sequence=VSP_018238, VSP_018246; CC Note=Contains a phosphoserine at position 817. CC {ECO:0000244|PubMed:21183079}; CC Name=9; Synonyms=ADAM22-G12, 22g+29.3+29.7; CC IsoId=Q9R1V6-11; Sequence=VSP_018247; CC Name=10; Synonyms=ADAM22-G17, 22G[27L]+29.3+29.7; CC IsoId=Q9R1V6-12; Sequence=VSP_018239, VSP_018242; CC Name=11; Synonyms=ADAM22-G18, 22g(D26)[27L]; CC IsoId=Q9R1V6-13; Sequence=VSP_018236, VSP_018239; CC Name=12; Synonyms=ADAM22-G19, 22g[27L]+29.5; CC IsoId=Q9R1V6-14; Sequence=VSP_018239, VSP_018243; CC Note=Contains a phosphoserine at position 882. CC {ECO:0000244|PubMed:21183079}; CC Name=13; Synonyms=ADAM22-G20, 22g[27L]; CC IsoId=Q9R1V6-15; Sequence=VSP_018239; CC Name=14; Synonyms=ADAM22-G21, 22g(D26)[27S]; CC IsoId=Q9R1V6-16; Sequence=VSP_018234; CC Name=15; Synonyms=ADAM22-G22, 22g(D27)+29.7; CC IsoId=Q9R1V6-17; Sequence=VSP_018238, VSP_018244; CC Name=16; Synonyms=ADAM22-G23, 22g(D25D26D27); CC IsoId=Q9R1V6-18; Sequence=VSP_018233; CC Name=17; Synonyms=ADAM22-A05, Beta; CC IsoId=Q9R1V6-2; Sequence=VSP_018238, VSP_018248; CC Name=18; Synonyms=ADAM22-A13; CC IsoId=Q9R1V6-19; Sequence=VSP_018235, VSP_018248; CC Name=19; Synonyms=ADAM22-A15; CC IsoId=Q9R1V6-20; Sequence=VSP_018236, VSP_018248; CC Name=20; Synonyms=ADAM22-A04, Alpha; CC IsoId=Q9R1V6-1; Sequence=VSP_018248; CC Name=21; Synonyms=ADAM22-A16; CC IsoId=Q9R1V6-21; Sequence=VSP_018237, VSP_018240; CC -!- TISSUE SPECIFICITY: Detected in juxtaparanodal zones in the CC central nervous system and at nerve terminal plexuses of basket CC cells in the cerebellum (at protein level) (PubMed:20089912). CC Expressed at high levels in the brain. Strongly expressed in CC cerebellar granule cells and hippocampus. In spinal cord, CC expression is restricted to gray matter. CC {ECO:0000269|PubMed:15876356, ECO:0000269|PubMed:20089912}. CC -!- PTM: The precursor is cleaved by a furin endopeptidase. CC {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Mice display severe ataxia within one week CC after birth and die before weaning, probably due to convulsions. CC They display marked hypomyelination of the peripheral nerves. CC {ECO:0000269|PubMed:15876356}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB009674; BAA83382.1; -; mRNA. DR EMBL; AB009674; BAA83383.1; -; mRNA. DR EMBL; AK034528; BAC28742.1; -; mRNA. DR EMBL; AB179842; BAD72803.1; -; mRNA. DR EMBL; AB179843; BAD72804.1; -; mRNA. DR EMBL; AB179844; BAD72805.1; -; mRNA. DR EMBL; AB179845; BAD72806.1; -; mRNA. DR EMBL; AB179846; BAD72807.1; -; mRNA. DR EMBL; AB179847; BAD72808.1; -; mRNA. DR EMBL; AB179848; BAD72809.1; -; mRNA. DR EMBL; AB179849; BAD72810.1; -; mRNA. DR EMBL; AB179850; BAD72811.1; -; mRNA. DR EMBL; AB179851; BAD72812.1; -; mRNA. DR EMBL; AB179852; BAD72813.1; -; mRNA. DR EMBL; AB179853; BAD72814.1; -; mRNA. DR EMBL; AB179854; BAD72815.1; -; mRNA. DR EMBL; AB179855; BAD72816.1; -; mRNA. DR EMBL; AB179856; BAD72817.1; -; mRNA. DR EMBL; AB179857; BAD72818.1; -; mRNA. DR EMBL; AB179858; BAD72819.1; -; mRNA. DR EMBL; AB179859; BAD72820.1; -; mRNA. DR EMBL; AB179860; BAD72821.1; -; mRNA. DR EMBL; AB179861; BAD72822.1; -; mRNA. DR EMBL; AB179862; BAD72823.1; -; mRNA. DR CCDS; CCDS19080.1; -. [Q9R1V6-1] DR CCDS; CCDS51411.1; -. [Q9R1V6-4] DR CCDS; CCDS80205.1; -. [Q9R1V6-6] DR CCDS; CCDS80207.1; -. [Q9R1V6-3] DR RefSeq; NP_001007221.1; NM_001007220.3. [Q9R1V6-1] DR RefSeq; NP_001007222.1; NM_001007221.3. [Q9R1V6-2] DR RefSeq; NP_001091695.1; NM_001098225.2. [Q9R1V6-4] DR RefSeq; NP_001297368.1; NM_001310439.1. [Q9R1V6-6] DR RefSeq; NP_001297369.1; NM_001310440.1. [Q9R1V6-3] DR RefSeq; XP_006503592.1; XM_006503529.3. [Q9R1V6-12] DR RefSeq; XP_006503593.1; XM_006503530.3. [Q9R1V6-11] DR RefSeq; XP_006503594.1; XM_006503531.3. [Q9R1V6-14] DR RefSeq; XP_006503596.1; XM_006503533.3. [Q9R1V6-8] DR RefSeq; XP_006503598.1; XM_006503535.3. [Q9R1V6-15] DR RefSeq; XP_006503600.1; XM_006503537.3. [Q9R1V6-7] DR RefSeq; XP_006503605.1; XM_006503542.3. [Q9R1V6-5] DR UniGene; Mm.275895; -. DR ProteinModelPortal; Q9R1V6; -. DR SMR; Q9R1V6; -. DR BioGrid; 197967; 4. DR IntAct; Q9R1V6; 8. DR MINT; Q9R1V6; -. DR STRING; 10090.ENSMUSP00000055000; -. DR MEROPS; M12.978; -. DR iPTMnet; Q9R1V6; -. DR PhosphoSitePlus; Q9R1V6; -. DR MaxQB; Q9R1V6; -. DR PaxDb; Q9R1V6; -. DR PeptideAtlas; Q9R1V6; -. DR PRIDE; Q9R1V6; -. DR DNASU; 11496; -. DR Ensembl; ENSMUST00000046838; ENSMUSP00000049120; ENSMUSG00000040537. [Q9R1V6-1] DR Ensembl; ENSMUST00000050166; ENSMUSP00000055000; ENSMUSG00000040537. [Q9R1V6-4] DR Ensembl; ENSMUST00000088744; ENSMUSP00000086122; ENSMUSG00000040537. [Q9R1V6-13] DR Ensembl; ENSMUST00000088761; ENSMUSP00000086139; ENSMUSG00000040537. [Q9R1V6-3] DR Ensembl; ENSMUST00000115388; ENSMUSP00000111046; ENSMUSG00000040537. [Q9R1V6-6] DR GeneID; 11496; -. DR KEGG; mmu:11496; -. DR UCSC; uc008wjk.2; mouse. [Q9R1V6-3] DR UCSC; uc008wjv.1; mouse. [Q9R1V6-4] DR UCSC; uc008wjy.1; mouse. [Q9R1V6-2] DR CTD; 53616; -. DR MGI; MGI:1340046; Adam22. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR HOVERGEN; HBG050456; -. DR InParanoid; Q9R1V6; -. DR KO; K16068; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR PhylomeDB; Q9R1V6; -. DR TreeFam; TF314733; -. DR Reactome; R-MMU-5682910; LGI-ADAM interactions. DR ChiTaRS; Adam22; mouse. DR PRO; PR:Q9R1V6; -. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000040537; -. DR CleanEx; MM_ADAM22; -. DR ExpressionAtlas; Q9R1V6; baseline and differential. DR Genevisible; Q9R1V6; MM. DR GO; GO:0030424; C:axon; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI. DR GO; GO:0042063; P:gliogenesis; IGI:MGI. DR GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI. DR GO; GO:0014037; P:Schwann cell differentiation; IMP:MGI. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell projection; KW Cleavage on pair of basic residues; Complete proteome; Disulfide bond; KW EGF-like domain; Glycoprotein; Membrane; Phosphoprotein; Receptor; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 23 {ECO:0000255}. FT PROPEP 24 223 {ECO:0000250}. FT /FTId=PRO_0000029114. FT CHAIN 224 904 Disintegrin and metalloproteinase domain- FT containing protein 22. FT /FTId=PRO_0000029115. FT TOPO_DOM 24 734 Extracellular. {ECO:0000255}. FT TRANSMEM 735 755 Helical. {ECO:0000255}. FT TOPO_DOM 756 857 Cytoplasmic. {ECO:0000255}. FT DOMAIN 237 436 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 442 529 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT DOMAIN 673 710 EGF-like. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT COMPBIAS 533 666 Cys-rich. FT MOD_RES 808 808 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 832 832 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 855 855 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 860 860 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 864 864 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 868 868 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT CARBOHYD 163 163 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 517 517 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 632 632 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 673 673 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 347 431 {ECO:0000250}. FT DISULFID 390 415 {ECO:0000250}. FT DISULFID 392 399 {ECO:0000250}. FT DISULFID 445 475 {ECO:0000250}. FT DISULFID 456 472 {ECO:0000250}. FT DISULFID 458 464 {ECO:0000250}. FT DISULFID 471 492 {ECO:0000250}. FT DISULFID 483 489 {ECO:0000250}. FT DISULFID 488 514 {ECO:0000250}. FT DISULFID 501 521 {ECO:0000250}. FT DISULFID 508 540 {ECO:0000250}. FT DISULFID 533 545 {ECO:0000250}. FT DISULFID 552 603 {ECO:0000250}. FT DISULFID 567 633 {ECO:0000250}. FT DISULFID 581 591 {ECO:0000250}. FT DISULFID 598 661 {ECO:0000250}. FT DISULFID 655 666 {ECO:0000250}. FT DISULFID 677 692 {ECO:0000250}. FT DISULFID 686 698 {ECO:0000250}. FT DISULFID 700 709 {ECO:0000250}. FT VAR_SEQ 730 904 VAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQG FT DYVKKPGDGDSFYSDFPPGGSTNSASSSKKRSNGLSHSWSE FT RIPDTKHISDICENGRPRSNSWQGNMGGNKKKIRGKRFRPR FT SNSTETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEGKTAG FT RQSARLWETSI -> QMDSLILGVKGFQTQNIFQTSVKMGD FT LAVTPGKVTWEATKRKSEGKDLDLDLTQLRPCHLPSLLLHQ FT LGLLPPAENTRTLCLRFQTRGRQRADRAPGYGRHPF (in FT isoform 16). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018233. FT VAR_SEQ 760 904 NYREQRQLPQGDYVKKPGDGDSFYSDFPPGGSTNSASSSKK FT RSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNMGGNK FT KKIRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRKYPYPM FT PPLPDEGKTAGRQSARLWETSI -> FPPVPSHIIPLVRTF FT HYFAAGQMDSLILGVKGFQTQNIFQTSVKMGDLAVTPGKVT FT WEATKRKSEGKDLDLDLTQLRPCHLPSLLLHQLGLLPPAEN FT TRTLCLRFQTRGRQRADRAPGYGRHPF (in isoform FT 14). {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018234. FT VAR_SEQ 760 801 Missing (in isoform 3, isoform 4 and FT isoform 18). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018235. FT VAR_SEQ 760 765 Missing (in isoform 11 and isoform 19). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018236. FT VAR_SEQ 766 846 QLPQGDYVKKPGDGDSFYSDFPPGGSTNSASSSKKRSNGLS FT HSWSERIPDTKHISDICENGRPRSNSWQGNMGGNKKKIRG FT -> FPPVPSHIIPLVRTFHYFAAGQMDSLILGVKGFQTQNI FT FQTSVKMGDLAVTPGKVTWEATKRKSEGKDLDLDLTQLSKL FT YL (in isoform 21). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018237. FT VAR_SEQ 766 801 Missing (in isoform 2, isoform 5, isoform FT 8, isoform 15 and isoform 17). FT {ECO:0000303|PubMed:10433968, FT ECO:0000303|PubMed:15876356, FT ECO:0000303|PubMed:16141072}. FT /FTId=VSP_018238. FT VAR_SEQ 802 802 S -> SAFLSHFQISTCSITHYSISQNISLFCSRS (in FT isoform 10, isoform 11, isoform 12 and FT isoform 13). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018239. FT VAR_SEQ 847 904 Missing (in isoform 21). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018240. FT VAR_SEQ 857 904 ETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEGKTAGRQSA FT RLWETSI -> DLGIIT (in isoform 7). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018241. FT VAR_SEQ 857 857 E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLD FT HSSQDGPHQQDR (in isoform 10). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018242. FT VAR_SEQ 857 857 E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in FT isoform 12). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018243. FT VAR_SEQ 857 857 E -> DSQDGPHQQDR (in isoform 15). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018244. FT VAR_SEQ 857 857 E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLD FT HR (in isoform 4, isoform 5 and isoform FT 6). {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018245. FT VAR_SEQ 857 857 E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFSSQDSPH FT QQDR (in isoform 8). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018246. FT VAR_SEQ 857 857 E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLD FT HRYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in FT isoform 9). FT {ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018247. FT VAR_SEQ 858 904 Missing (in isoform 17, isoform 18, FT isoform 19 and isoform 20). FT {ECO:0000303|PubMed:10433968, FT ECO:0000303|PubMed:15876356}. FT /FTId=VSP_018248. FT MUTAGEN 509 509 D->N: Fails to bind to LGI1. FT {ECO:0000269|PubMed:16990550}. FT CONFLICT 639 639 K -> R (in Ref. 2; BAC28742). FT {ECO:0000305}. SQ SEQUENCE 904 AA; 99715 MW; 0FBBD09398EE0B97 CRC64; MQAAAAASFW LLCVLGTCPL ARCGRAGVAS LKGLERGKEN RFLERQSIIP LRLIYRLGGE DETQHNQLDT RVRGDPGGPQ LTHVDKASFR VDAFGTSFVL DVLLNHELLS SGYVERQIEH GGKVVENKGG EHCYYQGQIR GNPVSFVALS TCHGLHGMFY DGNHTYLIEP EENEKSQESS HCHSVYKSRQ FEFPLDDLPS EFQRVNITPP QFILKPRLKR RKRQLLRFPR NVEEETKYIE LMIVNDHLMF KKHRLSVVYT NTYAKSVVNM ADVIYKDQLK TRIVLVAMET WAADNKFAIS ENPLITLREF MKYRRDFIKE KADAVHLFSG SQFESSRSGA AYIGGICSLL RGGGVNEFGK TDLMAVTLAQ SLAHNVGIIS DKRKLASGEC KCEDTWSGCI MGDTGYYLPK KFTQCNVEEY HDFLNSGGGA CLFNKPSKLL DPPECGNGFI ETGEECDCGT PAECALEGAE CCKKCTLTQD SQCSDGLCCK KCKFQPLGTV CREAVNDCDI REICSGNSSQ CAPNVHKMDG YSCDGTQGIC FGGRCKTRDR QCKYIWGQKV TASDRYCYEK LNIEGTEKGN CGKDKDTWTQ CNKRDVLCGY LLCTNIGNIP RLGELDGEIT STLVVQQGRT LNCSGAHVKL EEDVDLGYVE DGTPCGPQMM CLEHRCLPVA SFNFSTCSSS KAGTVCSGNG VCSNELKCVC NRHWTGADCG THFPHNDDAK TGITLSGNGV AGTNIIIGII AGTILVLALI LGITAWGYKN YREQRQLPQG DYVKKPGDGD SFYSDFPPGG STNSASSSKK RSNGLSHSWS ERIPDTKHIS DICENGRPRS NSWQGNMGGN KKKIRGKRFR PRSNSTETLS PAKSPSSSTG SIASSRKYPY PMPPLPDEGK TAGRQSARLW ETSI // ID B4IKH3_DROSE Unreviewed; 788 AA. AC B4IKH3; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 23-MAY-2018, entry version 63. DE SubName: Full=GM22501 {ECO:0000313|EMBL:EDW51565.1}; GN Name=Dsec\GM22501 {ECO:0000313|EMBL:EDW51565.1}; GN ORFNames=Dsec_GM22501 {ECO:0000313|EMBL:EDW51565.1}, GN GM22501 {ECO:0000313|FlyBase:FBgn0177371}; OS Drosophila sechellia (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292}; RN [1] {ECO:0000313|EMBL:EDW51565.1, ECO:0000313|Proteomes:UP000001292} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rob3c / Tucson 14021-0248.25 RC {ECO:0000313|Proteomes:UP000001292}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH480852; EDW51565.1; -; Genomic_DNA. DR RefSeq; XP_002044233.1; XM_002044197.1. DR EnsemblMetazoa; FBtr0205486; FBpp0203978; FBgn0177371. DR GeneID; 6620021; -. DR KEGG; dse:Dsec_GM22501; -. DR FlyBase; FBgn0177371; Dsec\GM22501. DR OMA; PKKHFHR; -. DR OrthoDB; EOG091G01L9; -. DR PhylomeDB; B4IKH3; -. DR Proteomes; UP000001292; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001292}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000001292}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 788 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002807530. FT DOMAIN 270 473 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 479 566 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 718 755 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 407 407 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 411 411 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 417 417 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 538 558 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 745 754 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 788 AA; 87442 MW; 551FF4CA64DF38F2 CRC64; MWMNIANLIL IIAQLCVFVT SAGEADYTLD DSFWNEESPV GEVERLLKEY RQNQELVRRI GGHYYQIIYP VQLRHHEKMG ISTPEVSLPK PGQRPRPHDD SGFNRGRTKK HFHRTSLLIK AFNHKFRLDL ELNSQLLSPN IQQKHYHVGG YLVDGNRHDI EHCYYHGTVK DYPGASAAFH TCNGVSGVIH IGNETFVIHP FYGGDLSKHP HVIFEARTKA NKGCANSGNL DSWRLSRRTK HLSAGVAGVV EEILQAGVGR NKRDVREATK YIETAIIVDK AMFDKRNGST RAEVIHDAIQ VANIADLYFR TLNTRVSVVY IETWGKNQAV IDGSKDISKA ISNFNDYTSR NLFQIERDTT QLLTGETFAG GEAGMAVPET VCTPRAVGIS VDVNVYEPHL LAGTMAHMIG HNIGMGHDDG REECFCRDWH GCIMAQSIVG QENVQPYKFS ECSKKDYIDA LRTGHGLCLL NKPNEIELRR NCGNKVVEED EECDCGTFEE CALDQCCDGI TCKLKSEAQC ASGACCDQCR LRPKDYICRD SNNECDLPEY CDGEIGQCPS DVFKKNGSPC GLSKTGISGY CFQGYCPTLS LQCEAIWGYG GSAADRQCYE QFNSKGSING HCGRDANEHY IKCEPENVQC GTLQCKDGER QPVNDGIDQL YSRTIISIKG QEFECKATSG QVGSNSYPEH GLVKDGTPCG DNLICLNQTC VSLFPHVDQT KCPANSQGLE CSEHGVCTNT NRCFCDMGWG GNDCSSVVLL TTALPTEALP TPENTIKMEK KETPYGKK // ID B4R5K2_DROSI Unreviewed; 754 AA. AC B4R5K2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 23-MAY-2018, entry version 68. DE SubName: Full=Mmd {ECO:0000313|EMBL:EDX18047.1}; GN Name=mmd {ECO:0000313|FlyBase:FBgn0068590}; GN Synonyms=Dsim\mmd {ECO:0000313|EMBL:EDX18047.1}; GN ORFNames=Dsim_GD15769 {ECO:0000313|EMBL:EDX18047.1}, GN GD15769 {ECO:0000313|FlyBase:FBgn0068590}; OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX18047.1, ECO:0000313|Proteomes:UP000000304}; RN [1] {ECO:0000313|EMBL:EDX18047.1, ECO:0000313|Proteomes:UP000000304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mixed {ECO:0000313|EMBL:EDX18047.1}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000366; EDX18047.1; -; Genomic_DNA. DR ProteinModelPortal; B4R5K2; -. DR FlyBase; FBgn0068590; Dsim\mmd. DR OMA; PKKHFHR; -. DR OrthoDB; EOG091G01L9; -. DR PhylomeDB; B4R5K2; -. DR ChiTaRS; mmd; fly. DR Proteomes; UP000000304; Chromosome X. DR Bgee; FBgn0068590; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000304}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000000304}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DOMAIN 175 378 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 384 471 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 623 660 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 312 312 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 316 316 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 322 322 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 443 463 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 650 659 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 754 AA; 83142 MW; 5EBC95B21AF6CB3B CRC64; MGISTREVSL PKKHFHRTSL LIKAFNHKFR LDLELNSQLL SPNIQQKHYH VGGYLVDGNR HDIEHCYYHG TVKDYPGASA AFHTCNGVSG VIHIGNETFV IHPFYGGDLS KHPHVIFEAR TKANKGCANS GNLDSWRLSR RTKHLSAGVA GVVEEILQAG VGRNKRDRDV REATKYIETA IIVDKAMFDK RNGSTRAEVI HDAIQVANIA DLYFRTLNTR VSVVYIETWG KNQAVIDGSK DISKAISNFN DYTSRNLFQI ERDTTQLLTG ETFAGGEAGM AVPETVCTPR AVGISVDVNV YEPHLLAGTM AHMIGHNIGM GHDDGREECF CRDWHGCIMA QSIVGQENVQ PYKFSECSKK DYIDALRTGH GLCLLNKPNE IELRRNCGNK VVEEDEECDC GTFEECALDQ CCDGITCKLK SEAQCASGAC CDQCRLRPKD YICRDSNNEC DLPEYCDGEI GQCPSDVFKK NGSPCGLSKT GISGYCFQGY CPTLSLQCEA IWGYGGSAAD RQCYEQFNSK GSINGHCGRD ANEHYIKCEP ENVQCGTLQC KDGERQPVND GIDQLYSRTI ISIKGQEFEC KATSGQVGSN SYPEHGLVKD GTPCGDNLIC LNQTCVSLFP HVDQTKCPAN SQGLECSEHG VCTNTNRCFC DMGWGGNDCS SVVLLTTALP PKHCPRRKPH QMEKKKPIWR KTTTLKYDPP YSKKPIAKSY GGAATAPNHH SVEEVSLDGS SKLVYANQTG FRCVSSTDNI TIGM // ID D3YUP9_MOUSE Unreviewed; 897 AA. AC D3YUP9; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 23-MAY-2018, entry version 72. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 {ECO:0000313|Ensembl:ENSMUSP00000111044}; GN Name=Adam22 {ECO:0000313|Ensembl:ENSMUSP00000111044, GN ECO:0000313|MGI:MGI:1340046}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000111044, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000111044, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000111044, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000111044} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000111044}; RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC140364; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC152165; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC156022; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_006503603.1; XM_006503540.3. DR UniGene; Mm.275895; -. DR ProteinModelPortal; D3YUP9; -. DR SMR; D3YUP9; -. DR MaxQB; D3YUP9; -. DR PeptideAtlas; D3YUP9; -. DR PRIDE; D3YUP9; -. DR Ensembl; ENSMUST00000115386; ENSMUSP00000111044; ENSMUSG00000040537. DR GeneID; 11496; -. DR CTD; 53616; -. DR MGI; MGI:1340046; Adam22. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR HOGENOM; HOG000231962; -. DR ChiTaRS; Adam22; mouse. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000040537; -. DR ExpressionAtlas; D3YUP9; baseline and differential. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0000213|MaxQB:D3YUP9, KW ECO:0000213|PeptideAtlas:D3YUP9}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 897 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003052335. FT TRANSMEM 735 758 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 237 436 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 442 529 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 673 710 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 501 521 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 700 709 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 897 AA; 99559 MW; 83B1F02FFCBFD8C2 CRC64; MQAAAAASFW LLCVLGTCPL ARCGRAGVAS LKGLERGKEN RFLERQSIIP LRLIYRLGGE DETQHNQLDT RVRGDPGGPQ LTHVDKASFR VDAFGTSFVL DVLLNHELLS SGYVERQIEH GGKVVENKGG EHCYYQGQIR GNPVSFVALS TCHGLHGMFY DGNHTYLIEP EENEKSQESS HCHSVYKSRQ FEFPLDDLPS EFQRVNITPP QFILKPRLKR RKRQLLRFPR NVEEETKYIE LMIVNDHLMF KKHRLSVVYT NTYAKSVVNM ADVIYKDQLK TRIVLVAMET WAADNKFAIS ENPLITLREF MKYRRDFIKE KADAVHLFSG SQFESSRSGA AYIGGICSLL RGGGVNEFGK TDLMAVTLAQ SLAHNVGIIS DKRKLASGEC KCEDTWSGCI MGDTGYYLPK KFTQCNVEEY HDFLNSGGGA CLFNKPSKLL DPPECGNGFI ETGEECDCGT PAECALEGAE CCKKCTLTQD SQCSDGLCCK KCKFQPLGTV CREAVNDCDI REICSGNSSQ CAPNVHKMDG YSCDGTQGIC FGGRCKTRDR QCKYIWGQKV TASDRYCYEK LNIEGTEKGN CGKDKDTWTQ CNKRDVLCGY LLCTNIGNIP RLGELDGEIT STLVVQQGRT LNCSGAHVKL EEDVDLGYVE DGTPCGPQMM CLEHRCLPVA SFNFSTCSSS KAGTVCSGNG VCSNELKCVC NRHWTGADCG THFPHNDDAK TGITLSGNGV AGTNIIIGII AGTILVLALI LGITAWGYKN YREQRSNGLS HSWSERIPDT KHISDICENG RPRSNSWQGN MGGNKKKIRG KRFRPRSNST EYLNPWFKRD YNVAKWVEDV NKNTEGPYFR TLSPAKSPSS STGSIASSRK YPYPMPPLPD EGKTAGRQSA RLWETSI // ID D4A6U1_RAT Unreviewed; 739 AA. AC D4A6U1; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 2. DT 23-MAY-2018, entry version 69. DE SubName: Full=A disintegrin and metallopeptidase domain 11 (Predicted), isoform CRA_a {ECO:0000313|EMBL:EDM06228.1}; DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSRNOP00000061628}; GN Name=Adam11 {ECO:0000313|Ensembl:ENSRNOP00000061628, GN ECO:0000313|RGD:1307515}; GN Synonyms=Adam11_predicted {ECO:0000313|EMBL:EDM06228.1}; GN ORFNames=rCG_32562 {ECO:0000313|EMBL:EDM06228.1}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000061628, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000061628, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000061628, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|EMBL:EDM06228.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDM06228.1}; RX PubMed=15632090; DOI=10.1101/gr.2889405; RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., RA Istrail S., Li P., Sutton G.; RT "Gene and alternative splicing annotation with AIR."; RL Genome Res. 15:54-66(2005). RN [3] {ECO:0000313|EMBL:EDM06228.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDM06228.1}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., RA Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., RA Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSRNOP00000061628} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000061628}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABR07030499; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH473948; EDM06228.1; -; Genomic_DNA. DR RefSeq; NP_001101770.1; NM_001108300.1. DR UniGene; Rn.20276; -. DR STRING; 10116.ENSRNOP00000061628; -. DR MEROPS; M12.976; -. DR Ensembl; ENSRNOT00000064429; ENSRNOP00000061628; ENSRNOG00000002753. DR GeneID; 360638; -. DR KEGG; rno:360638; -. DR UCSC; RGD:1307515; rat. DR CTD; 4185; -. DR RGD; 1307515; Adam11. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR KO; K16067; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Reactome; R-RNO-5682910; LGI-ADAM interactions. DR Proteomes; UP000002494; Chromosome 10. DR Bgee; ENSRNOG00000002753; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:EDM06228.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 700 723 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 204 403 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 409 496 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 638 675 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 468 488 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 665 674 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 739 AA; 80666 MW; 88C987A03666BB11 CRC64; MGSPESPEGP EVTEPSRLVR ESSGGEVRKP QLDTRVRQDP PRGTPVHLAQ VSFVIPAFDS NFTLDLELNH HLLSSQYVER HFSREGTRQH STGAGDHCYY HGKLRDNPHS FAALSTCQGL HGVFSDGNLT YIVEPKEMAG PWGPPQGPLP HLIYRTPLLP APFGCREPGC LFAVPAQSAA PSRPKLRRKR QVRRGHPTVH SETKYVELIV INDHQLFEQM RQSVVLTSNF AKSVVNLADV IYKEQLNTRI VLVAMETWAD GDKIQVQDDL LETLARLMVY RREGLPEPSD ATHLFSGRTF QSTSSGAAYV GGICSLSRGG GVNEYGNMGA MAVTLAQTLG QNLGMMWNKH RSSAGDCKCP DIWLGCIMED TGFYLPRKFS RCSIDEYNQF LQEGGGSCLF NKPLKLLDPP ECGNGFVEAG EECDCGSVQE CSRAGGNCCK KCTLTHDAMC SDGLCCRRCK YEPRGVSCRE AVNECDIAET CTGDSSQCPP NLHKLDGYYC DHEQGRCYGG RCKTRDRQCQ ALWGHVAADR FCYEKLNVEG TERGNCGRKG SGWVQCNKQD VLCGFLLCVN ISGAPRLGDL GGDISSVTFY HQGKELDCRG GHVQLADGSD LSYVEDGTAC GPNMLCLDHR CLPASAFNFS TCPGSGERRI CSHHGVCSNE GKCICQPDWT GKDCSIHNPL PTSPPTGETE RYKGPSGTNI IIGSIAGAVL VAAIVLGGTG WGFKNIRRGR YDPTQQGAV // ID E0W1A6_PEDHC Unreviewed; 1144 AA. AC E0W1A6; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 23-MAY-2018, entry version 45. DE SubName: Full=ADAM 9 precursor, putative {ECO:0000313|VectorBase:PHUM572440-PA}; DE SubName: Full=ADAM 9, putative {ECO:0000313|EMBL:EEB19412.1}; DE EC=3.4.24.52 {ECO:0000313|EMBL:EEB19412.1}; GN Name=8234932 {ECO:0000313|VectorBase:PHUM572440-PA}; GN ORFNames=Phum_PHUM572440 {ECO:0000313|EMBL:EEB19412.1}; OS Pediculus humanus subsp. corporis (Body louse). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; OC Pediculidae; Pediculus. OX NCBI_TaxID=121224 {ECO:0000313|Proteomes:UP000009046}; RN [1] {ECO:0000313|EMBL:EEB19412.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA {ECO:0000313|EMBL:EEB19412.1}; RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S., RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K., RA Amedeo P., Strausberg R.; RT "Annotation of Pediculus humanus corporis strain USDA."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEB19412.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA {ECO:0000313|EMBL:EEB19412.1}; RG The Human Body Louse Genome Consortium; RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.; RT "The genome of the human body louse."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000009046, ECO:0000313|VectorBase:PHUM572440-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USDA {ECO:0000313|Proteomes:UP000009046, RC ECO:0000313|VectorBase:PHUM572440-PA}; RX PubMed=20566863; DOI=10.1073/pnas.1003379107; RA Kirkness E.F., Haas B.J., Sun W., Braig H.R., Perotti M.A., RA Clark J.M., Lee S.H., Robertson H.M., Kennedy R.C., Elhaik E., RA Gerlach D., Kriventseva E.V., Elsik C.G., Graur D., Hill C.A., RA Veenstra J.A., Walenz B., Tubio J.M., Ribeiro J.M., Rozas J., RA Johnston J.S., Reese J.T., Popadic A., Tojo M., Raoult D., Reed D.L., RA Tomoyasu Y., Krause E., Mittapalli O., Margam V.M., Li H.M., RA Meyer J.M., Johnson R.M., Romero-Severson J., Vanzee J.P., RA Alvarez-Ponce D., Vieira F.G., Aguade M., Guirao-Rico S., Anzola J.M., RA Yoon K.S., Strycharz J.P., Unger M.F., Christley S., Lobo N.F., RA Seufferheld M.J., Wang N., Dasch G.A., Struchiner C.J., Madey G., RA Hannick L.I., Bidwell S., Joardar V., Caler E., Shao R., Barker S.C., RA Cameron S., Bruggner R.V., Regier A., Johnson J., Viswanathan L., RA Utterback T.R., Sutton G.G., Lawson D., Waterhouse R.M., Venter J.C., RA Strausberg R.L., Berenbaum M.R., Collins F.H., Zdobnov E.M., RA Pittendrigh B.R.; RT "Genome sequences of the human body louse and its primary endosymbiont RT provide insights into the permanent parasitic lifestyle."; RL Proc. Natl. Acad. Sci. U.S.A. 107:12168-12173(2010). RN [4] {ECO:0000313|VectorBase:PHUM572440-PA} RP IDENTIFICATION. RC STRAIN=USDA {ECO:0000313|VectorBase:PHUM572440-PA}; RG VectorBase; RL Submitted (FEB-2017) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS235867; EEB19412.1; -; Genomic_DNA. DR RefSeq; XP_002432150.1; XM_002432105.1. DR ProteinModelPortal; E0W1A6; -. DR STRING; 121225.PHUM572440-PA; -. DR EnsemblMetazoa; PHUM572440-RA; PHUM572440-PA; PHUM572440. DR GeneID; 8234932; -. DR KEGG; phu:Phum_PHUM572440; -. DR VectorBase; PHUM572440-RA; PHUM572440-PA; PHUM572440. DR CTD; 8234932; -. DR InParanoid; E0W1A6; -. DR OMA; QCFEQFN; -. DR PhylomeDB; E0W1A6; -. DR Proteomes; UP000009046; Partially assembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009046}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Hydrolase {ECO:0000313|EMBL:EEB19412.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000009046}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 652 675 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 117 321 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 327 415 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 564 601 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 255 255 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 259 259 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 265 265 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 387 407 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 591 600 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1144 AA; 125942 MW; 7B43C1AA8CB587D0 CRC64; MEKFSIESFE IEHCYYHGTV KDYPGAAAAF HTCNGVSGVI HIGNETFVIH PFYGGDLSKH PHVIFEARAK QNKGCANSGN LDWRKNPRKT KHVSELIEEA ETILGLRYKR DVREATKYVE TALVLDKAMF EKRNGSTRAD VIHDAIQVAN IADLYYRALN TRVSIVYIET WQSINKITID KTQDISRALL NFNDYTSRKM FKIDKDTSQL LTGESFIGGE AGMAVPEAVC TTKSVGISVD VNTYEPHILA ATMAHMIGHN IGMGHDDGRE ECYCRDWHGC LMAQGIAGLE NVQPYKFSDC SKSDYIDSLR IGHGICLLNK PNEFDSHRSC GNGIVEEGEM CDCGTIEECH EIDPCCDPIT CKLTSESECA SGPCCENCRL RSRGVTCRDA VNECDLPEYC NGETGFCPVD IHKKNGSPCS QDSGYCFNGV CPTLNLQCEA IWGYGGIAAD KQCFEQFNSK GSLNGHCGMD ENGQYIKCDP ENARCGSLQC QLGNRHPVAA GVDQLFSRTI ISIKGVEYEC KSISAKIQGQ KNIPVDGLVR DGTPCGDQLI CINQTCTSIF LHLDSVKCPS NHNDLECSGH GVCSNINKCH CELGWSGPDC SIQLEVDESK SSSPSSTGKT PASKEDLKAI LESQMQKKVT PYENYHSTNT GFLVGVLMSV VGGVFILFAL MALCYRSVVV HKNFSLCLRK STMPKYEPPN IKKPMLKKTS SASATEDTSI DSVNKILTFG NMPNSQRVLF CPGNHSDQQA TAHILEHKSQ QLKRGTIGSG SEEDPTISGE EESVAFIDIP PNNLSKLPEK GILKKPYGSI GESKEKWSED SQSDNQEILS QSDNNVGDST ATMSEVERAL KNLNGYHEDI LEALRTAASH STHRGPPGGL GMHTPSGSSS LLSEEILRKS LLDRRSSRGG SQEKICDHGQ THTVLVDSHR RIDDEDEELP PSCGPIRIRN LEDLVRQLEH HSARHMSPSG SEDIRMSETE ADRHYRLEAS DPQSVRTRGQ RGEDEPRFVY GRYRHPSTTG RAHSSPHSHQ HTHGYMQEEE GIYESADHDR VVDCGDTPDS ESDEFIQAQP ALVRSASEEL VPGVSVSGTG SGSGHRSRHH RESQQLNTSS GGMSQREYYP SPLSSTDSDD SNNDSPSMAP EYKH // ID E1ZWX5_CAMFO Unreviewed; 1282 AA. AC E1ZWX5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=ADAM 11 {ECO:0000313|EMBL:EFN74315.1}; GN ORFNames=EAG_08578 {ECO:0000313|EMBL:EFN74315.1}; OS Camponotus floridanus (Florida carpenter ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Formicoidea; Formicidae; Formicinae; Camponotus. OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311}; RN [1] {ECO:0000313|EMBL:EFN74315.1, ECO:0000313|Proteomes:UP000000311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(2010). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL434909; EFN74315.1; -; Genomic_DNA. DR ProteinModelPortal; E1ZWX5; -. DR InParanoid; E1ZWX5; -. DR OMA; QCFEQFN; -. DR Proteomes; UP000000311; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000311}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000000311}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 792 816 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 261 465 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 470 564 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 712 749 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 399 399 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 403 403 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 409 409 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 536 556 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 739 748 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1282 AA; 142640 MW; 301ADB8F015F99B8 CRC64; MFEVAKRLKS ETNARKSSSQ PEADYTLDDS FWKEEETPVG EVERLLREYR QNQELVRNIG GHFYQIIYPV QLRHHEKMGI STREVGVSKF PQRGYGDGGY QNARGRMRTG RHFHRTSLLI KAFNHKFRLD LELNTQLLAP NLMQKDFLSG AEQISKQEIE HCYYHGTVRD YPGASAAFHT CNGVSGVIHL GNETFVIHPF YGGDLSKHPH IIFEARTKVN KGCANSGSLD WRTKNRRQKH IYGLSKITSD RYKRDVREAT KYIETAIIID KAMFDKRNGS TRAEVVHDAI QVANIADLYF RTLNTRVSVV YIETWKGSNQ AQIDNGIDIG QALLNFNDYT MRRMFQVSQD TTQLLTGETF SGGESGVAVS STVCTQRSVG ISVDLNTYEP HLLAGTMAHM IGHNIGMSHD DGRNDCNCRD WHGCIMAQSI VGLENVQPYK FSECSKTDYI EALKNGQGFC LFNKPNEVEM RKCGNRVIDD GEQCDCGSID ECKEYDPCCD PITCKLTTEA ECATGPCCSN CKAREIRSLH ARGVICRDSM NECDLPEMCS GDTGQCPPDV YKKNGSPCSN NAGSCFNGVC PALDLQCEQV WGYGGIVADQ QCFEQFNSKG SINGHCGTDA SGHLIKCEAE NVRCGSLQCQ QGSKQPVIEE MKDYYSRTII SIKSQEYECK ATTGRVEGSD IPGMGLVRDG TSCGDNLICV NQTCTSLFPH IDQEKCPSNH DNNECSGNGV CTNVNKCYCY PGWSGPDCSL PQSIPTVLPT ATADTEVVQT KSDSKLEKKE TPYENYHGSN TVFLVGMLMS VVGGVFVVFA LMALCYRSVV VHKNFSLCLR RKSTVQKYDP PYSKKPQQKS YSGVSGNHHA EAAALDTVNK ILTFGRMPHY REHKPQPKRH VEEEDGGTGA EEVVSFIDLP PNNLTKLPEK GILKKHGGYG LGGGAIEHVE RTLNQLNGYH EDILEVLKNA ASRRDLAGTP SGSSNLLDED ALRKSLAECG YPDVYRKDTD GQDNGIDNGQ EEDDDDVEPY LTGQMSPSGS EEIRISEGEP DRHYRIDSSV CSESSQGSRR CSRGRDEDAS RFVYGRYRQP TSRSPYGNHQ HTHQHSHQMH PEDEGIYETA DPDRGSNTRG ETPDCESDAF IQAQQQVARW TSEDGGGGVQ HRPPQQPPPP PAMPLPVQQQ QQQQQQHQLP VEQLPIKQRG YYPSPPQTEN SPDAGNNAEA ESAQSQQQTL SDVRGIDVNH LPNINKRPLD DNFSLDCNIM NNGSPKELIT NNSSDNENTA LLPPTHFPEY KH // ID E2BF62_HARSA Unreviewed; 1250 AA. AC E2BF62; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 23-MAY-2018, entry version 42. DE SubName: Full=ADAM 11 {ECO:0000313|EMBL:EFN85648.1}; GN ORFNames=EAI_04428 {ECO:0000313|EMBL:EFN85648.1}; OS Harpegnathos saltator (Jerdon's jumping ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Formicoidea; Formicidae; Ponerinae; Ponerini; Harpegnathos. OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237}; RN [1] {ECO:0000313|EMBL:EFN85648.1, ECO:0000313|Proteomes:UP000008237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN85648.1, RC ECO:0000313|Proteomes:UP000008237}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(2010). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL447952; EFN85648.1; -; Genomic_DNA. DR ProteinModelPortal; E2BF62; -. DR InParanoid; E2BF62; -. DR OMA; QCFEQFN; -. DR Proteomes; UP000008237; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008237}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000008237}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DOMAIN 185 389 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 395 483 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 629 666 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 323 323 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 327 327 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 333 333 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 455 475 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 656 665 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1250 AA; 139575 MW; 68A63AF12315112F CRC64; MGISTREVGV SKYPQRGYGD GGYQNSRGRM RTGRHFHRTS LLIKAFNHKF RLDLELNTQL LAPNLIQKDF LDNDAEQMSK QEIEHCYYHG TVRDYPGASA AFHTCNGVSG VIHLGNETFV IHPFYGGDLS KHPHIIFEAR TKANKGCANS GNLEWRVKSR RQKHTRGLSE TTSDRYKRDV REAIKYIETA IIIDKAMFDK RNGSTRAEVV HDAIQVANIA DLYFRTINTR VSVVYIETWK GSNQAQIDKG MEIDLALLNF NDYVMRRMYQ VAQDTTQLLT GETFAGGESG VAIPATVCSQ KSVGISVDLN TYEPHLLAGT MAHMIGHNIG MSHDDGKNDC NCRDWHGCIM AQSIVGLENV QPYKFSECSK TEYIETLKSG HAFCLFNKPN ELEVRRSCGN RVIDDGEQCD CGSIDECHEL DPCCDPITCK LTTEAECATG PCCSDCKLRA RGVVCRESTN ECDLPEVCSG DTGQCPPDVY KKNGNPCSNN AGHCFNGVCP ALDLQCEQVW GYGGIAADKQ CFEQFNSKGS INGHCGTDAT GHLIKCEAEN VRCGSLQCQQ GSKQPIIDGM KDFYSRTIIS IKSQEYECKA TTGKVDGPDM PGLVRDGTSC GDNLICVNQT CTSLFPHIDQ EKCPSNHDNS ECSGNGVCTN VNKCYCFPGW SGPDCSIEQY IPTVTPTTPS VEVVSKADPK LEKKETPYEN YHGSNTVFLV GMLMSVVGGV FVVFALMALC YRSVVVHKNF SLCLRRKGTV QKYDPPYSKK PPQKSYSGVS GNHHAEAAAL DTVNKILTFG RMPQYREHKQ QEEEDGGTGA EEVVSFIDLP PNNHTKLPEK GILKKHGGYG LSSGGFDVQR TLNQLNSYHD NVLEVLKNAA SRGDSGTPSG SGNLDEDALR KSLAECGYPD MYRKDTDGQD NGIDNQEDEE EDEELQPPCG TIRIRNLEDI IRQLEHHTAR YMTGQMSPSG SEEIRISEGE PDRHYRIDSS VCSESSQGSR RCSRGRDEDA SRFVYGRYRQ PTSRSPYGNH QHTHQHSHQM HEEEGIYETA DPDRGSNTRG ETPDCESDAF IQAQQQVARW TSEDGVQHRP PQQPPPPPSM QLPVQEQAQQ KAQQQPQQQQ PQQQQQQQQQ QQPQQQPQPQ PQQQQQQQQQ QQQQHQLPVE QLPIKQRGYY PPPPQTDKNL DSNAEVEYAQ TQQQQQPLSE VRGIDVNHMP NINKCPLDDY FSLDCNIMNN GSPQELTTNN TSDNENTALL PPTHFPEYKH // ID E3LW70_CAERE Unreviewed; 1053 AA. AC E3LW70; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 23-MAY-2018, entry version 45. DE SubName: Full=CRE-UNC-71 protein {ECO:0000313|EMBL:EFO83641.1}; GN Name=Cre-unc-71 {ECO:0000313|EMBL:EFO83641.1}; GN ORFNames=CRE_02845 {ECO:0000313|EMBL:EFO83641.1}; OS Caenorhabditis remanei (Caenorhabditis vulgaris). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281}; RN [1] {ECO:0000313|Proteomes:UP000008281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281}; RG Caenorhabditis remanei Sequencing Consortium; RA Wilson R.K.; RT "PCAP assembly of the Caenorhabditis remanei genome."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS268417; EFO83641.1; -; Genomic_DNA. DR RefSeq; XP_003111780.1; XM_003111732.1. DR ProteinModelPortal; E3LW70; -. DR STRING; 31234.CRE02845; -. DR EnsemblMetazoa; CRE02845; CRE02845; WBGene00063439. DR GeneID; 9811110; -. DR CTD; 9811110; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR InParanoid; E3LW70; -. DR OMA; PKKHFHR; -. DR OrthoDB; EOG091G01L9; -. DR Proteomes; UP000008281; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008281}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008281}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 745 769 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 233 433 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 439 526 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 663 700 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT COILED 201 228 {ECO:0000256|SAM:Coils}. FT DISULFID 498 518 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 690 699 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1053 AA; 116611 MW; ABDBEC48D00F35E1 CRC64; MFSVDIRQTT ANKAFMETMS PDGYEVVHPF QIRDKNERIG IDTRNYFLKA QEHYSHVTIV IRSNQLGRLK LVLERNNFIF LNQTAFHKLD ADGERVLQNR VENCYYQGTV GGEESSFVAL SSCNGLRGVI SFANGTTYGI WPLDGGDRNS RRHPHILYKS EWTKEAKCGS SMAHAVGQRI RRGAEPDLEG AEPKQKKHKH RKHHRRHMKD EEEEEDELKI RVANRRDASK RTKYVEVALI ADYEFMKQRG LHDMDAISYM LESLNIADSM LSRDLNIRLS AVYVELWSDV QRIDLWEDIE RTLSGVVDYA AGHIYHIQKD ASILFTAGSF ANQEVSNAAI RSICTARSAV IVRAIEPFAT HWNGELVAQS VGHLLGLEHD TTACSCEPSP ECVMRQQPGR VGAPFSWQFS KCSVARMHGI WQDGNIQCLL NKPFQVSELR ECGNGIVDGS EECDCGTREN CNDPCCDPLT CTLRPHAQCA AHHKCCHRCE LRKAGETCRS SQSPCDVAES CDGKSGDCPP DGHLIDGTVC GNDGQCWRGN CSDSHQQCQK LWGREARVAE EVCFEQNTKG AEYANCGMQS DGSYHPCQLE DTKCGTLHCH SGSLTPTDST LKAFTFHFTQ NAQQIQCKSI AGSLSGLIQD GTNCGSGKVC VAGSCVEMSS VSSGTACPTN NLALLCSGHG HCTTTAKCVC FNGWTGNACD IRSNTSTYQG SMGFRDEDHE QMGHGGARKT IMIPHLNIGT TLETAYLFGI LFGFGAFLLL CLVCLMLCYR RRSVVEIPKP SDEKLEESPD RQIKFGNMPS YREEKRKRKS SKRIYGALNR ITEADERDST SLRSRDSAGS QQLLDRNGQP VMAGIRDPYS TDHHIYAESV AASSSNRQFR GINSDGSYPL RSFGSWRSSA PISPASSSGH LTDVSNATTP LRLNKIGKLL KTMQQSDDEA GSPFSDHSMQ FQNHQGIQNL QSLQNLQNHS LLGRLDHGYT GEEELSAVEA DHDVGSNTES SRGCEDSSGG RDSGGWDPPS LVNGSTSNNY NFRQSPSLFS DPFKLEMTNS MHN // ID E5SBW4_TRISP Unreviewed; 1056 AA. AC E5SBW4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=Putative ADAM 28 {ECO:0000313|EMBL:EFV57720.1}; GN ORFNames=Tsp_01232 {ECO:0000313|EMBL:EFV57720.1}; OS Trichinella spiralis (Trichina worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichinellidae; Trichinella. OX NCBI_TaxID=6334 {ECO:0000313|EMBL:EFV57720.1, ECO:0000313|Proteomes:UP000006823}; RN [1] {ECO:0000313|EMBL:EFV57720.1, ECO:0000313|Proteomes:UP000006823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS 195 {ECO:0000313|EMBL:EFV57720.1, RC ECO:0000313|Proteomes:UP000006823}; RX PubMed=21336279; DOI=10.1038/ng.769; RA Mitreva M., Jasmer D.P., Zarlenga D.S., Wang Z., Abubucker S., RA Martin J., Taylor C.M., Yin Y., Fulton L., Minx P., Yang S.P., RA Warren W.C., Fulton R.S., Bhonagiri V., Zhang X., Hallsworth-Pepin K., RA Clifton S.W., McCarter J.P., Appleton J., Mardis E.R., Wilson R.K.; RT "The draft genome of the parasitic nematode Trichinella spiralis."; RL Nat. Genet. 43:228-235(2011). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV57720.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIR02000788; EFV57720.1; -; Genomic_DNA. DR RefSeq; XP_003377035.1; XM_003376987.1. DR ProteinModelPortal; E5SBW4; -. DR EnsemblMetazoa; EFV57720; EFV57720; EFV57720. DR GeneID; 10905612; -. DR KEGG; tsp:Tsp_01232; -. DR CTD; 10905612; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR InParanoid; E5SBW4; -. DR OrthoDB; EOG091G01L9; -. DR Proteomes; UP000006823; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006823}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000006823}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 734 751 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 191 393 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 399 476 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 646 683 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 325 325 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 329 329 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 335 335 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 673 682 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1056 AA; 118793 MW; AAA950D2A42BBB1C CRC64; MDSWNKELFE HLVDDFEIVY PVQLRDRGRV GIDTQNYLFD NSTIHFERCS FVIKTSYGRW RIHVQLNDVL IQPAAKYVRY LKLDSPSETS GRSLPNCYYH GQVHGQPKSK VSLSTCFGLR GSIVMENQTF IIIPLKGGDL SRRHPHVFAR LKWDDEASCG NTDNTEWSRK RFHRRRPHRR KLRRDVEKKV KYIELGLFVD RKLHDFLNVG YREMTSYFLE AVNAVDLAFQ QLNTRVSLVY FEIWTTENKI GVQREILPSL MNFIQFSSYE FYNGPFDLAL LLTAADLTTS EMMSAADTVC SARAAGMIKV ADKFQPYYLS LLMAHAIGHI SGMSHDDSEF DCTNGENFIG IMNNVVSMTS KKNRRVYQFT ECNKHDYLEL IRSGQGRCLF NFPLQNNALT LCGNKVVDPG EFCDCGSVEE CDSVDPCCDA VTCTLRADAQ CAEGVCCEKC KFITNRTLCR PSRDECDVPE YCSGLSGNVS LLYGFDELEL GGGLFCPSDS YKPNGAACGI NRLGICYGGQ CRQSDSECQR IWGPNASAAD PACFKKFNTL GIDFGHCGVN ENNKPLPCAE NNAMCGLLFC KGGQEVPNFS LYFKTEFTEN GSVYECKVFI DNKSPVNYSL IPDGSRCGKS EACISQNCVP LRSIYQHVDC PTTNTALFCS GHGICTNLNI CHCDAGWTGR DCSVKANFTF EMLSIGESAV SEHGGSSFYG DSEMPVAVSF PDTFPSGDSS KLDTYAMLII LGCVAIGMIL IRRANFSKKA KTPTSEKCDF EKESNSSTET GQRSIRFGPS RTYKCADEVM TTNKRRTLDQ IRECDERESL SAKSRESANS AERVTLTMNR LPSRGILKNG PQSFTCERTA PEWRALLAAN RPCDAGYDIV DFWSIRGCER RRLLDRQRRW AVSIADAEQR PADPWGPLRV VQQQAAETQP NYRRHSEPVH VRAESKFAES VSGCSGQLFQ RQQQRLLFPV EKPWRRFGRL RGLARGQAAA VPDPLQHQSL QQHLLVVQRC NDAAAEAAEV DQHRAAFEAT RRRRRPRRTV RRSKSAVPSA ELSSRG // ID E9G3K5_DAPPU Unreviewed; 795 AA. AC E9G3K5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 23-MAY-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFX85790.1}; DE Flags: Fragment; GN ORFNames=DAPPUDRAFT_45366 {ECO:0000313|EMBL:EFX85790.1}; OS Daphnia pulex (Water flea). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda; OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia. OX NCBI_TaxID=6669 {ECO:0000313|Proteomes:UP000000305}; RN [1] {ECO:0000313|EMBL:EFX85790.1, ECO:0000313|Proteomes:UP000000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21292972; DOI=10.1126/science.1197761; RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A., RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., RA Bauer D.J., Caceres C.E., Carmel L., Casola C., Choi J.H., RA Detter J.C., Dong Q., Dusheyko S., Eads B.D., Frohlich T., RA Geiler-Samerotte K.A., Gerlach D., Hatcher P., Jogdeo S., RA Krijgsveld J., Kriventseva E.V., Kultz D., Laforsch C., Lindquist E., RA Lopez J., Manak J.R., Muller J., Pangilinan J., Patwardhan R.P., RA Pitluck S., Pritham E.J., Rechtsteiner A., Rho M., Rogozin I.B., RA Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y., RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., RA Tu H., Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., RA Shaw J.R., Andrews J., Crease T.J., Tang H., Lucas S.M., RA Robertson H.M., Bork P., Koonin E.V., Zdobnov E.M., Grigoriev I.V., RA Lynch M., Boore J.L.; RT "The ecoresponsive genome of Daphnia pulex."; RL Science 331:555-561(2011). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL732531; EFX85790.1; -; Genomic_DNA. DR ProteinModelPortal; E9G3K5; -. DR STRING; 6669.DappuP45366; -. DR EnsemblMetazoa; EFX85790; EFX85790; DAPPUDRAFT_45366. DR KEGG; dpx:DAPPUDRAFT_45366; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR InParanoid; E9G3K5; -. DR OMA; PKKHFHR; -. DR PhylomeDB; E9G3K5; -. DR Proteomes; UP000000305; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000305}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000000305}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 714 738 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 214 417 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 423 511 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 659 696 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 351 351 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 355 355 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 361 361 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 483 503 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 686 695 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:EFX85790.1}. SQ SEQUENCE 795 AA; 88094 MW; 56B694BF2A2094E9 CRC64; RHPGDVEKLL KEHRENQDLV RSIGGSHYQI VFPVQLRHRE KMGISTREIG ATKTGKHYHR TSLLIKAFSH KFRLDLELNS QLLAPNLIQK HFLPGGVEQF SKQEIEHCYY HGTVKDYPGA VAAFRTCSGV SGIIHIGNET FVIHPFYGGD LSRKHPHVIF EARTKVKQMC ANTGMLEYGL RSGNYRGGGG GGKGQSKQPK SNERQKRDVR EVTKYVETAL VLDKAMFEKR NGSRRIEVVQ DAIQIANIAD LYFRTLNTRV SVVYIETWAS ENQAPVDRSQ DIHRALLNFN DYISRKLYNV IKDTTQLLSG ETFAGGSGMA APDTICTPRS VGLSVDINPY EPHLVAGTMA HMIGHNIGMG HDDGRDECHC GDWHGCIMSQ SIMGLESVQP YKFSECSLSD YIEKLKIGHS ICLFNRPNQL EDFRTCGNGV VEDGEECDCG TIEECHDSDP CCDPITCKLT AEAECASGPC CDDCKLRPKG YLCRDATNEC DLPEICNGRS GQCPLDIYKK NGNQCEINKG YCFNGVCPTL DSQCRLIWGD GGLSGDRKCF EQFNSQGSIN GHCGQDAHNN YIRCDAEHVM CGSLQCQMGT RYPIVAGMDQ MYSRTLVSMA GREFECKITS GTVAAADLPD LGIVRDGTPC GNSLICMNKT CSSIYPHIDR SKCPSNNVAL DCSGHGVCSN INSCFCDAGW TGHDCSTQTN DSYIRIDRSG HSTVFMVVML VSVVGGVFIV FALMALCYRS VVVHRNLSLC LRLVESFHYV ARRDGPKKVQ TKKNKNKIQI KFQTKSNQKT ASVVS // ID F1LXB5_RAT Unreviewed; 804 AA. AC F1LXB5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 2. DT 23-MAY-2018, entry version 53. DE SubName: Full=RCG21419-like {ECO:0000313|Ensembl:ENSRNOP00000060323}; GN Name=LOC100360238 {ECO:0000313|Ensembl:ENSRNOP00000060323}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000060323, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000060323, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060323, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000060323} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060323}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABR07036374; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 10116.ENSRNOP00000060323; -. DR PaxDb; F1LXB5; -. DR Ensembl; ENSRNOT00000057396; ENSRNOP00000060323; ENSRNOG00000037801. DR RGD; 2322512; LOC100360238. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR InParanoid; F1LXB5; -. DR OMA; KIKFQTW; -. DR OrthoDB; EOG091G02N2; -. DR TreeFam; TF314733; -. DR Proteomes; UP000002494; Chromosome 12. DR Bgee; ENSRNOG00000037801; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 13 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 704 726 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 203 396 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 405 489 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 630 664 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 339 339 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 338 338 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 342 342 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 348 348 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 461 481 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 654 663 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 804 AA; 88167 MW; 41EF6EB229A8AEE5 CRC64; MERLKLEQIQ TQLCIRLVAM LLLAIIFLLS TLCDLGSVYD SSYETVIPER LPGQGSDDPG GKVSYVLLMQ GQKQLLHLEV KGHYSERNFP VYSYHHGILG QEVPLLSQAC HYEGHIEGVP GSFVSVSICS GLRGVLIKEE TAYGIEPLLF STNFEHILYT MAHQPVVLCN VTPTDSLGDS SQRQGSSKTD ELLALSDLWS HAKYVEMFVV VNHQRFQMWG SDVNTTVQAV VDIIALANSF TRGINTEVVL VGLEIWTEGD PIEVPVDLQA TLRNFNLWRQ EKLMGRVRHD VAHLIVGHRP GANEGQAFLD GACSGGFAAA VEAFHHEDVL LFAALMAHEL GHNLGIRHDR PGCTCGPKHL CLMHEISKTS GFSNCSSDHF LRFLHDHRGA CLLDRPWHQS HKRRDAHCGN GVVEESEECD CGNACDKNQC CDEKCKLKEG AQCSNELCCL HCKFKNKGAV CRPAQGLCDL EEYCNGTSAV CPNDRIAQDG SICQESYFCF GGQCRDPSSQ CSHIFGFGSR SAPDECYTSL NKRGNRFGNC GPSSDSPGTY VKCSDQNILC GKLICTEVGY LPPIKDKHML IQIPQVEDWC WSMDAFDKTD AFDEGYVWTN TSCGTGKVCE NSICKDYTIV PNPCKAESIC NEHGVCNDLG NCHCLFGFAP PDCKEEGTGG SVDSGPTVIP PDDFNTGQNA TQSSREDLIL NLKLIVLAVI LVLMILLIIT CIITAYSKSE PASEGEPSEI EKVPEEEEEG EALPEEEEIK EEEGEGAIGE EEEEGAIGEE GAIGEEEGEG AIEEEGAEEE EGEE // ID F1M542_RAT Unreviewed; 739 AA. AC F1M542; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 3. DT 23-MAY-2018, entry version 49. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSRNOP00000059289}; GN Name=Adam22 {ECO:0000313|Ensembl:ENSRNOP00000059289, GN ECO:0000313|RGD:1585016}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000059289, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000059289, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000059289, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000059289} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000059289}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {ECO:0000213|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., RA Lundby C., Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 RT different rat organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABR07059516; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059517; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059518; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059519; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059520; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059521; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059522; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059523; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059524; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059525; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSRNOT00000068410; ENSRNOP00000059289; ENSRNOG00000042478. DR RGD; 1585016; Adam22. DR GeneTree; ENSGT00910000144014; -. DR Reactome; R-RNO-5682910; LGI-ADAM interactions. DR Proteomes; UP000002494; Chromosome 4. DR Bgee; ENSRNOG00000042478; -. DR ExpressionAtlas; F1M542; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 606 629 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 108 307 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 313 400 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 544 581 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 372 392 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 571 580 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 739 AA; 81936 MW; 48A0FC3E88EDAC1B CRC64; QGGEHCYYQG QIRGNPASFV ALSTCHGLQM FADCKHDEFS TPQRNTHIQE SQFHSVYKSR LLEFPLDDLP SEFQRINITA PQFTLKPRLK RRKRQLLRFP RNVEEETKYI ELMIVNDHLM FKKHRLSVVY TNTYAKSVVN MADVIYKDQL KTRIVLVAME TWAADNKFAI SENPLVTLRE FMKYRRDFIK EKADAVHLFS GSQFESSRSG AAYIGGICSL LRGGGVNEFG KTDLMAVTLA QSLAHNIGII SDKRKLASGE CKCEDTWSGC IMGDTGYYLP KKFTQCNIEE YHDFLNSGGG ACLFNKPSKL LDPPECGNGF IETGEECDCG TPAECALEGA ECCKKCTLTQ DSQCSDGLCC KKCKFQPLGT VCREAVNDCD IREICSGNSS QCAPNVHKMD GYSCDGTQGI CFGGRCKTRD RQCKYIWGQK VTASDRYCYE KLNIEGTEKG NCGKDKDTWT QCNKRDVLCG FLLCTNIGNI PRLGELDGEI TSTLVVQQGR TLNCSGGHVK LEEDVDLGYV EDGTPCGPQM MCLEHRCLPM ASFNFSTCLS NKAGTVCSGN GVCSNELKCV CNRHWTGADC GTHFPHNDDA KTGITLSGNG VAGTNIIIGI IAGTILVLAL ILGITAWGYK NYREQRSNGL SHSWSERIPD TKHISDICEN GRPRSNSWQG NVGGNKKKIR GKRFRPRSNS TETLSPAKSP SSSTGSIASS RKYPYPMPPL PDEEKTVNRQ SARLWETSI // ID F1N5I4_BOVIN Unreviewed; 765 AA. AC F1N5I4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 23-MAY-2018, entry version 49. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSBTAP00000002276}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSBTAP00000002276}; 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 {ECO:0000313|Ensembl:ENSBTAP00000002276, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000002276, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000002276, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [2] {ECO:0000313|Ensembl:ENSBTAP00000002276} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000002276}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DAAA02049256; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9913.ENSBTAP00000002276; -. DR PaxDb; F1N5I4; -. DR Ensembl; ENSBTAT00000002276; ENSBTAP00000002276; ENSBTAG00000001735. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F1N5I4; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Reactome; R-BTA-5682910; LGI-ADAM interactions. DR Proteomes; UP000009136; Chromosome 19. DR Bgee; ENSBTAG00000001735; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 731 754 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 235 434 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 440 527 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 669 706 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 499 519 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 696 705 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 765 AA; 83257 MW; 319337F2BE350E32 CRC64; LPHRWASVCS HGLLSPGVGT WGPAGALRWR VSPHLGGPEA PEITEPSRLV GESSGGEVRK QQLDTRVRQE PPGGPPVHLA QVRKKIPAFI SNFTLDLELN HHLLSSQYVE RHFSREGLTQ HSTGAGDHCY YQGKLRGNPH SFAALSTCQG LHGVFSDGNF TYIVEPREMA GPWENAQGPL PHLIYRTPLL PAPLGCREPG CLFAAPDHPA PLNRPRLRRK RQVRRGHPTV HSETKYVELI VINDHQLFGQ MRQSVVLTSN FAKSVVNLAD VMYKEQLNTR IVLVAMETWA DGDKIQVQDD LLETLARLMV YRREGLPEAS DATHLFSGRT FQSTSSGAAY VGGICSLSRG GGVNEYDNMG AMAVTLAQTL GQNLGMMWNK HRSSAGDCKC PDNWLGCIME DTGFYLPRKF SRCSIDEYNQ FLQEGGGSCL FNKPLKLLDP PECGNGFVEA GEECDCGSVQ ECSRAGGNCC KKCTLTHDAM CSDGLCCRRC KYEPRGVSCR EAVNECDIAE TCTGDSSQCP PNLHKLDGYY CDHEQGRCYG GRCKTRDRQC QALWGHAAAD RFCYEKLNVE GTERGNCGRK GSGWVQCNKQ DVLCGFLLCV NISGAPRLGD LGGDISSVTF YHQGKELDCR GGHVQLADGS DLSYVEDGTA CGPNMLCLDH RCLPASAFNF STCPGSGERR ICSHHGVCSN EGKCICQPDW TGKDCSIHNP LPTSPPTGET ERYKGPSGTN IIIGSIAGAV LVAAIVLGGT GWGFKNIRRG RSGGA // ID F1PF76_CANLF Unreviewed; 904 AA. AC F1PF76; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 2. DT 28-MAR-2018, entry version 45. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSCAFP00000002703}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSCAFP00000002703, GN ECO:0000313|VGNC:VGNC:37580}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000002703, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000002703, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000002703, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000002703} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000002703}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEX03009298; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCAFT00000002915; ENSCAFP00000002703; ENSCAFG00000001852. DR VGNC; VGNC:37580; ADAM22. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Reactome; R-CFA-5682910; LGI-ADAM interactions. DR Proteomes; UP000002254; Chromosome 14. DR Bgee; ENSCAFG00000001852; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 904 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003267530. FT TRANSMEM 735 758 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 237 436 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 442 529 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 501 521 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 904 AA; 100034 MW; 3698D0636F6BEB6E CRC64; AAAAASVPFL LLCALGTCPP ARCGRAGDAS LTELERRDEN RFLERQSIVP LRLLYRSGGD DETGHDALDT RVRGHAAGGQ LTHVDQASFQ VDAFGTSFIL DIMLNHDLLS SEYIERHVEH GGKTVEVKGG EHCYYQGHVR GNPDSFVALS TCHGLHGMFY DGNHTYLIEP EENDTSQEDF HFHSVYKSRL FEFPLDDLPS EFQQVHITPP KFTLKPRPKR SKRQLRRHPR NVEEETKYIE LMIVNDHLMF KKHRLSVVHT NTYAKSVVNM ADLIYKDQLK TRIVLVAMET WAADNKFAIS ENPLITLREF MKYRRDFIKE KSDAVHLFSG SQFESSRSGA AYIGGICSLL KGGGVNEFGK TDLMAVTLAQ SLAHNIGIIS DKRKLASGEC KCEDTWSGCI MGDTGYYLPK KFTQCNIEEY HDFLNSGGGA CLFNKPSKLL DPPECGNGFI ETGEECDCGT PAECVLEGAE CCKKCTLTQE SQCSDGLCCK KCKFQPMGTV CREAVNDCDI RETCSGNSSQ CAPNIHKMDG YSCDGIQGIC FGGRCKTRDR QCKYIWGQKV MASDKYCYEK LNIEGTEKGN CGKDKDTWIQ CNKRDVLCGY LLCTNIGNIP RLGELDGEIT STLVVQQGRT LNCSGGHVKL EEDVDLGYVE DGTPCGPQMM CLEHRCLPVA SFNFSTCLSN KEGTVCSGNG ICSNELKCVC NRHWIGADCS TYFPHNDDAK TGITLSGNGV AGTNIIIGII AGTILVLALI LGITAWGYKN YREQRQLPQG DYVKKPGDGD SFYSDIPPGV STNSASSSKK RSNGLSHSWS ERIPDTKHIS DICENGRPRS NSWQGNLGGN RKKIRGKRFR PRSNSTETLS PAKSPSSSTG SIASSRKYPY PMPPLPDEEK KVNRQSARLW ETSI // ID F1PU85_CANLF Unreviewed; 775 AA. AC F1PU85; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 2. DT 23-MAY-2018, entry version 55. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSCAFP00000020791}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSCAFP00000020791, GN ECO:0000313|VGNC:VGNC:37573}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000020791, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000020791, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000020791, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000020791} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000020791}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEX03006411; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAEX03006412; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAEX03006413; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005624443.1; XM_005624386.2. DR ProteinModelPortal; F1PU85; -. DR STRING; 9615.ENSCAFP00000020791; -. DR MEROPS; M12.976; -. DR PaxDb; F1PU85; -. DR Ensembl; ENSCAFT00000022389; ENSCAFP00000020791; ENSCAFG00000014102. DR GeneID; 606958; -. DR CTD; 4185; -. DR VGNC; VGNC:37573; ADAM11. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F1PU85; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Reactome; R-CFA-5682910; LGI-ADAM interactions. DR Proteomes; UP000002254; Chromosome 9. DR Bgee; ENSCAFG00000014102; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 741 764 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 245 444 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 450 537 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 679 716 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 509 529 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 706 715 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 775 AA; 84229 MW; 36E435938F3E28FE CRC64; MRCAHPCPKS LAPRRASACS SGLVSPGLGT RGPFGALRWR VSPHLGRPGA PEVTEPSRLV GESTGGEVRK QQLDTRVRQE PPGGPPVHLA QVSFVIPAFN SNFTLDLELN HHLLSSQYVE RHFSREGTTQ HSSGAGDHCY YQGKLRGNPH SFAALSTCQG LHGVFSDGNF TYIVEPREMA RPQEPPQGPL PHLIYRTPLL PAPLGCREPG CLFAAPAHTA PVNRPRLRRK RQVRRGHPTV HSETKYVELI VVNDHQLFEQ MRQSVVLTSN FAKSVVNLAD VMYKEQLNTR IVLVAMETWA DGDKIQVQDD LLETLARLMV YRREGLPEPS DATHLFSGRT FQSSSSGAAY VGGICSLSRG GGVNEYDNMG AMAVTLAQTL GQNLGMMWNK HRSSAGDCKC PDNWLGCIME DTGFYLPRKF SRCSIDEYNQ FLQEGGGSCL FNKPLKLLDP PECGNGFVEA GEECDCGSVQ ECSRAGGNCC KKCTLTHDAM CSDGLCCRRC KYEPRGVSCR EAVNECDIAE TCTGDSSQCP PNLHKLDGYY CDHEQGRCYG GRCKTRDRQC QALWGHAAAD RFCYEKLNVE GTERGNCGRK GSGWVQCNKQ DVLCGFLLCV NISGAPRLGD LGGDISSVTF YHQGKELDCR GGHVQLADGS DLSYVEDGTA CGPNMLCLDH RCLPASAFNF STCPGSGERR ICSHHGVCSN EGKCICQPDW TGKDCSIHNP LPTSPPTGET ERYKGPSGTN IIIGSIAGAV LVAAIVLGGT GWGFKNIRRG RSGGA // ID F1RQZ7_PIG Unreviewed; 775 AA. AC F1RQZ7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 3. DT 23-MAY-2018, entry version 55. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSSSCP00000018381}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSSSCP00000018381}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000018381, ECO:0000313|Proteomes:UP000008227}; RN [1] {ECO:0000313|Ensembl:ENSSSCP00000018381, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000018381}; RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSSCP00000018381} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEMK02000080; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9823.ENSSSCP00000018381; -. DR PaxDb; F1RQZ7; -. DR PRIDE; F1RQZ7; -. DR Ensembl; ENSSSCT00000018885; ENSSSCP00000018381; ENSSSCG00000017349. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F1RQZ7; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Reactome; R-SSC-5682910; LGI-ADAM interactions. DR Proteomes; UP000008227; Chromosome 12. DR Bgee; ENSSSCG00000017349; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 775 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5012610050. FT TRANSMEM 736 759 Helical. {ECO:0000256|SAM:Phobius}. FT DISULFID 504 524 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 701 710 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 775 AA; 84331 MW; 19821295A399BBDF CRC64; MRRLRGWAIA ALLLLPLLPL PGLGTRGPAG ALRWRLSPQL GGPEAPEVTE PSRLVGGSSG GEVPKQQLDT RVRQEPPGGP PVHLAQVSFV IPAFNSNFTL DLELNHHLLS SQYVERHFSR EGTTQHSTGA GDHCYYQGKL RGNPHSFAAL STCQGLHGVF SDGNFTYIVE PREMAGPREP PQGPLPHLIY RTPLLPAPLG CREPGCLFAA PAHSAPPNRP RLRRKRQVRR GHPTVHSETK YVELIVINDH QLFEQMRQSV VLTSNFAKSV VNLADVMYKE QLNTRIVLVA METWADGDKI QVQDDLLETL ARLMVYRREG LPEPSDATHL FSGRTFQSTS SGAAYVGGIC SLSRGGGVNE YDNMGAMAVT LAQTLGQNLG MMWNKHRSSA GDCKCPDNWL GCIMEDTGFY LPRKFSRCSI DEYNQFLQEG GGSCLFNKPL KLLDPPECGN GFVEAGEECD CGSVQECSRS GGNCCKKCTL THDAMCSDGL CCRRCKYEPR GVSCREAVNE CDIAETCTGD SSQCPPNLHK LDGYYCDHEQ GRCYGGRCKT RDRQCQALWG HAAADRFCYE KLNVEGTERG NCGRKGSGWV QCNKQDVLCG FLLCVNISGA PRLGDLGGDI SSVTFYHQGK ELDCRGGHVQ LADGSDLSYV EDGTACGPNM LCLDHRCLPA SAFNFSTCPG SGDRRICSHH GVCSNEGKCI CQPDWTGKDC SIHNPLPTSP PTGETERYKG PSGTNIIIGS IAGAVLVAAI VLGGTGWGFK NIRRGRYDPT QQGAV // ID F4X5Z5_ACREC Unreviewed; 1264 AA. AC F4X5Z5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 23-MAY-2018, entry version 35. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11 {ECO:0000313|EMBL:EGI58128.1}; DE Flags: Fragment; GN ORFNames=G5I_13790 {ECO:0000313|EMBL:EGI58128.1}; OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex OS octospinosus echinatior). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Formicoidea; Formicidae; Myrmicinae; Acromyrmex. OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755}; RN [1] {ECO:0000313|Proteomes:UP000007755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21719571; DOI=10.1101/gr.121392.111; RA Nygaard S., Zhang G., Schiott M., Li C., Wurm Y., Hu H., Zhou J., RA Ji L., Qiu F., Rasmussen M., Pan H., Hauser F., Krogh A., RA Grimmelikhuijzen C.J., Wang J., Boomsma J.J.; RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key RT adaptations to advanced social life and fungus farming."; RL Genome Res. 0:0-0(2011). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL888755; EGI58128.1; -; Genomic_DNA. DR ProteinModelPortal; F4X5Z5; -. DR InParanoid; F4X5Z5; -. DR Proteomes; UP000007755; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007755}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:EGI58128.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000007755}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DOMAIN 223 427 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 433 521 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 669 706 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 361 361 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 365 365 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 371 371 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 493 513 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 696 705 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:EGI58128.1}. SQ SEQUENCE 1264 AA; 140392 MW; 482D07CE18008723 CRC64; GEVERLLHEY RQNQELIRNI GGHYYQIIYP VQLRHHEKMG ISTREVGVPK FPQRGYGDGG YQNPRGRLRT GRHFHRTSLL IKAFNHKFRL DLELNTQLLA PNLIQKDFLA GNAEQMSKQE IEHCYYHGTV RDYPGASAAF HTCNGVSGVI HLGNETFVIH PFYGGDLSKH PHIIFEARTK VNKGCANSGN LEWRVKNRRQ KHIFGLSETT SDRYKRDVRE ATKYIETAII IDKAMFDKRN GSTRAEVVHD AIQVANIADL YFRTLNTRVS VVYIESWKGS NQAQIDNGID IDQALLSFND YTMRRMYQVA QDTTQLLTGE TFSGGESGVA VPETVCSQRS VGISVDLNTY EPHLLAGTMA HMIGHNIGMS HDDGRNDCNC RDWHGCIMAQ SIVGLENVQP YKFSECSKTD YIEALKSGHG ICLFNKPNEL EIRRSCGNRV IDDGEQCDCG SIEECKEYDP CCDPITCKLT TEAECATGPC CSDCKLRARG VVCRESTNEC DLPEMCTGDT GQCPPDVYKK NGNPCANNAG HCFNGICPAL DLQCEQVWGY GGIAADQECF EQFNSKGSIN GHCGTDSSGH LIKCESENVR CGSLQCQQGS KQPVIDGMKD LHTRTIISIK NQEYECKATN GRVEGSDIPG MGLVRDGTSC GDNLICVNQT CTSLFPYIDQ EKCPSNHDDK ECSGNGVCTN VNKCHCFLGW SGPDCSIEQS IPTALPTTPP TEVVVKSDSK LPEKKETPYE NYHGSNTVFL VGMLMSVVGG VFVLFTLVAL CYRSVVVHKN FSLCLRRKST VQKYDPPYSK KPQQKSYSGV SGNHHAEAAA LDTVNKILTF GSMPQYREHK PQPKRLGVEE EDGGTGAEEV VSFIDLPPNN LTKLPEKGIL KKHGGYGLGG GAIEHVERTL NQLNGYHEDI LEVLKNAASR RDLVGTPSGS NLLDEDALRK SLAECGYPDV YRKDTDGQDN GIDNGQEEEE DDVELQPPCG TIRIRNLEDL IRQLEHRASA RPYMTGQMSP SGSEEIRTSE TEPDRHYRID SSVCSESSQG SRRCSRGRDE DASRFVYGRY RQPTSRSPYG NHQHTHQHSH QMHPEDEGIY ETADPDRGSN TRGETPDCES DAFIQAQQQV ARWTSEDGGG GGGGGGVQHR PPQQPPPPPA MPVQQQAQQQ QHQLPVEQLP ITQRGYYPSP PQIENNLDAG SNAEVESAQS QQQSEVRGID VNHTPNINKR PLDDNFSLDC NIMNNDSPKE LITNNTSDNE NTALLSHHFP EYKH // ID F6S926_MONDO Unreviewed; 915 AA. AC F6S926; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 23-MAY-2018, entry version 52. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSMODP00000012957}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSMODP00000012957}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000012957, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000012957, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000012957} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_007505033.1; XM_007504971.1. DR STRING; 13616.ENSMODP00000012957; -. DR Ensembl; ENSMODT00000013194; ENSMODP00000012957; ENSMODG00000010338. DR GeneID; 100027437; -. DR CTD; 53616; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F6S926; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000002280; Chromosome 8. DR Bgee; ENSMODG00000010338; -. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 746 769 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 248 447 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 453 540 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 684 721 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 512 532 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 711 720 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 915 AA; 101664 MW; 35772EB0427778BD CRC64; MRAAEAAEAA ALLPWLLLGI SGIFPLALCR LPGDALLTEL ERRNENRFLE RENTVPLRLI YRSGGEDQTR HDVLTTRIRG APAGGGAGGR QSTHVDQASF QVDAFGSTFI LDVVLNHDLL SSEYLERHID HGGKIVEVKG GEHCYYHGHI RGYPDSFVAL STCHGLHGMF YDGNHTYLIE PEENDTSQED FHFHSVYKSK LFEFPLDDLP SEFQQMNITS PKFIVKPRLK RSKRQLRRHP RNVEEETKYV ELMIVNDHLM FKKHRLSVMH TNTYAKSVVN MADLIYKEQL KTRIVLVAME TWAADNKFTI SEKPLTTLRE FMKYRKDFIK EKSDAVHLFS GSRFESSRSG AAYIGGICSL LKGGGVNEFG KTDLMAVTLA QSLAYNLGIF SDKRKLVSGE CKCEDTWSGC IMGDTGYYLP KKFSQCNVDE YHDFLNNGGG ACLFNKPSKL LDPPECGNGF IETGEECDCG TLAECAREGA DCCKKCTLTE DSQCSDGLCC KKCKFQPMGT VCREAVNDCD IQETCTGNSS QCAPNIHKMD GYSCDNFQGI CFGGRCKTRD RQCKYIWGQN VTASDKYCYE KLNIEGTEKG NCGRDKDTWI QCNKQDVLCG YLLCTNIGNI PRLGELDGEI TSSLVVQQGR TLNCSGGHVK LEEEIDLGYV EDGTPCGPEM MCLERRCLPT ASFNFSTCLS KKENAICSGH GVCSNEIKCV CNKHWSGADC NTYLPYNDGS KSDISLSGNG VAGTNIIIGI ITGTILVLVL ILGIAAWGYK NYREQRQLPQ GDYVKKPGDA DSFYSDMPPG VSTNSASSSK KRSNGLSHSW SERIPDTKHI SDICENGRPR SNSWQGNLGG NRKKVRGKRF RPRSNSTETL SPAKSPSSST GSIASSRKYP YPMPPLPDEE KKANRQSARL WETSI // ID F6V2P1_XENTR Unreviewed; 840 AA. AC F6V2P1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 47. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSXETP00000062542}; GN Name=adam22 {ECO:0000313|Ensembl:ENSXETP00000062542, GN ECO:0000313|Xenbase:XB-GENE-957019}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000062542, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000062542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000062542}; RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000062542} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMC01087816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087818; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087819; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087821; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087822; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087823; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 8364.ENSXETP00000062542; -. DR PaxDb; F6V2P1; -. DR Ensembl; ENSXETT00000064931; ENSXETP00000062542; ENSXETG00000007431. DR Xenbase; XB-GENE-957019; adam22. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F6V2P1; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Reactome; R-XTR-5682910; LGI-ADAM interactions. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; ENSXETG00000007431; -. DR ExpressionAtlas; F6V2P1; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 640 663 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 142 341 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 347 435 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 579 615 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 407 427 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 605 614 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 840 AA; 93580 MW; 1FDF4A0D41899077 CRC64; MILIINVSHH SDLLSSEYRE RHVTQDGKTV EFKGGEHCYY QGQIRGKAKS FVALSTCYGL HGMFCDGNHT YLIEPGEKYN PNEDYQFHSV YKSKVLEFPI DELPSEFWPL NDTSPRLSQQ TRNQRKKRQT RRYPRNVEDE TKYVELMIVN DHLMYKKHRL SVGHTNSYAK SVVNMADLIY KEQLNTRIVL VAMETWATDN KFSISENPLL TLKEFMKYRR DFIKDKSDAV HLFSGSQFES SRSGAAYIGG VCSLLKGGGV NEFGKPDVMA VTLAQSLAHN LGIFSDKKKL LSGECKCEDT WSGCIMGDIG YYLPSKFSVC NIEEYHEFLN NGGGSCLFNK PLKLLDPPEC GNGFVEAGEE CDCGTIAECA VEGGECCKKC TLTQDSECSD GLCCSDCKKF NPKEMICREA VNDCDIPETC TGNSSQCPAN IHKLDGYQCE SMQGLCFGGR CKTRERQCKY IWGEKVSAAD KYCYEKLNIE GTEKGNCGRN KETWIQCNKQ DVLCGYLLCT NISSVPRLGE LDGDVTTSSV VNQGKLYNCS GGHVKLDEDT DLGYVEDGTP CGTGMMCLEH RCLPIDSFNF STCLGSTNKI CSGHGVCSNE VKCICDSFWT GDDCSNFLPY DGIIKPDEGH RDEGVISTNI IIGAIAGTIL VLALVLGITA WGYKKRNYRR ERQIPQGDYV KKPGDADSFY SDLPPGVSSN SASSSKKRSA ILSHFQISAC SIPHYSISQN ISLFCRRSNG LSHSWSERIP DTKHVSDVCE NGRPRSNSWQ GNVSSSRKKL RGKRFRPRSN STETLSPAKS PSSSTGSIAS SRKYPYPMPP LPDEERKANK QSARLWETSI // ID F6VBC2_CIOIN Unreviewed; 818 AA. AC F6VBC2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 2. DT 23-MAY-2018, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCINP00000010576}; OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000010576, ECO:0000313|Proteomes:UP000008144}; RN [1] {ECO:0000313|Proteomes:UP000008144} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12481130; DOI=10.1126/science.1080049; RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., RA De Tomaso A., Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., RA Harafuji N., Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., RA Lemaire P., Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., RA Putnam N., Rash S., Saiga H., Satake M., Terry A., Yamada L., RA Wang H.G., Awazu S., Azumi K., Boore J., Branno M., Chin-Bow S., RA DeSantis R., Doyle S., Francino P., Keys D.N., Haga S., Hayashi H., RA Hino K., Imai K.S., Inaba K., Kano S., Kobayashi K., Kobayashi M., RA Lee B.I., Makabe K.W., Manohar C., Matassi G., Medina M., RA Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A., RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M., RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., RA Stainier D., Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., RA Yoshizaki F., Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., RA Doggett N., Glavina T., Hawkins T., Richardson P., Lucas S., RA Kohara Y., Levine M., Satoh N., Rokhsar D.S.; RT "The draft genome of Ciona intestinalis: insights into chordate and RT vertebrate origins."; RL Science 298:2157-2167(2002). RN [2] {ECO:0000313|Ensembl:ENSCINP00000010576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15114417; DOI=10.1007/s00239-003-2559-6; RA Gissi C., Iannelli F., Pesole G.; RT "Complete mtDNA of Ciona intestinalis reveals extensive gene RT rearrangement and the presence of an atp8 and an extra trnM gene in RT ascidians."; RL J. Mol. Evol. 58:376-389(2004). RN [3] {ECO:0000313|Ensembl:ENSCINP00000010576} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 7719.ENSCINP00000010576; -. DR Ensembl; ENSCINT00000010576; ENSCINP00000010576; ENSCING00000005135. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F6VBC2; -. DR OMA; NFHSHSL; -. DR OrthoDB; EOG091G01NX; -. DR TreeFam; TF314733; -. DR Proteomes; UP000008144; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008144}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00276, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000008144}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 818 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003348592. FT TRANSMEM 702 721 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 222 422 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 430 517 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 647 679 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 362 362 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 361 361 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 365 365 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 371 371 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 337 417 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 651 661 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 669 678 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 818 AA; 89319 MW; D0F586A29217A210 CRC64; MELLKLVFIC FVLVENSNAS FFVGSSSSFA STLLTRLKQY TIVIPHQAED KHARLKKRDL STELHVVPGI HSKQTYFSFK FENQTYILEL KLNEELLPKD FSTSIHTDDG QVIMDKPNLQ ERNHCYYQGH VVNMEGSHVI MSTCDGLRGC IALSDDFLLI EPLSPHSTQH VVYRPKDQTL NEVGTCGNQD MGHAVVNVDS FAGMLRQNEQ HRQKREATTE KKFLELLIVA DKAQAAKYSR VDLDNRIKEL VNYINGFYKK LKIHVVLSHI EVWKTQDKIP LKTNAQEVLN EFLSYRQRKI SSEPPNSYWK YTDNAQLLYG GSFEGSTIGM ASVKTMCTSR SGGVNQDHQT NVFYTATTLA HEMGHNFGMH HDSASCVCPP GAQCLMASSS GSSFKKDWSS CSKEYLAQSI TEGLGNCLLN VPDPSRLYGG PKCGNDIIEM GEDCDCGGVD ECLSQCCNAT TCKLISGASC DTGPCCFGCQ YSPAGQICRD TNNNICDLAE YCTGTSANCP GNVYRQNGSP CNGNQAACAQ GVCLTHDLQC QGIWGEGAVS GNDICYSFSR PPSECFTPPS LRTNSKCGKL QCSGGADRPI VARDRYAFKN TIDRKYECKT ISSDDNATDV SDPGLVRDGT RCGDGKICND GKCDDLPPMA CDATCNGHGV CNNLGNCHCN RGWAPPFCSS EGNGGSVNSG PITSNTMDTQ TILMLVMFLV VFPIVVSILL GKNTDRIMEK RSAPPPPLPP PVQPQATTTL ASNHPQPPRH PPPPAITKPS NQSAVRPNFP PPPPTTKPPL PPVGQPPPTV SKKPTPEKPI FKPLVANK // ID F6WJE0_XENTR Unreviewed; 789 AA. AC F6WJE0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 45. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSXETP00000062783}; GN Name=adam22 {ECO:0000313|Ensembl:ENSXETP00000062783, GN ECO:0000313|Xenbase:XB-GENE-957019}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000062783, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000062783} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000062783}; RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000062783} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMC01087816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087818; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087819; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087821; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087822; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087823; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSXETT00000062797; ENSXETP00000062783; ENSXETG00000007431. DR Xenbase; XB-GENE-957019; adam22. DR GeneTree; ENSGT00910000144014; -. DR Reactome; R-XTR-5682910; LGI-ADAM interactions. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; ENSXETG00000007431; -. DR ExpressionAtlas; F6WJE0; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 655 678 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 158 357 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 363 450 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 594 630 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 422 442 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 620 629 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 789 AA; 87830 MW; 9237C2F096137BCC CRC64; QLTHVARASF QIDAFGSSFI LDVELNHDLL SSEYRERHVT QDGKTVEFKG GEHCYYQGQI RGKAKSFVAL STCYGLHGMF CDGNHTYLIE PGEKYNPNED YQFHSVYKSK VLEFPIDELP SEFWPLNDTS PRLSQQTRNQ RKKRQTRRYP RNVEDETKYV ELMIVNDHLM YKKHRLSVGH TNSYAKSVVN MADLIYKEQL NTRIVLVAME TWATDNKFSI SENPLLTLKE FMKYRRDFIK DKSDAVHLFS GSQFESSRSG AAYIGGVCSL LKGGGVNEFG KPDVMAVTLA QSLAHNLGIF SDKKKLLSGE CKCEDTWSGC IMGDIGYYLP SKFSVCNIEE YHEFLNNGGG SCLFNKPLKL LDPPECGNGF VEAGEECDCG TIAECAVEGG ECCKKCTLTQ DSECSDGLCC SDCKFNPKEM ICREAVNDCD IPETCTGNSS QCPANIHKLD GYQCESMQGL CFGGRCKTRE RQCKYIWGEK VSAADKYCYE KLNIEGTEKG NCGRNKETWI QCNKQDVLCG YLLCTNISSV PRLGELDGDV TTSSVVNQGK LYNCSGGHVK LDEDTDLGYV EDGTPCGTGM MCLEHRCLPI DSFNFSTCLG STNKICSGHG VCSNEVKCIC DSFWTGDDCS NFLPYDGIIK PDEGHRDEGV ISTNIIIGAI AGTILVLALV LGITAWGYKF CLLLPRSNGL SHSWSERIPD TKHVSDVCEN GRPRSNSWQG NVSSSRKKLR GKRFRPRSNS TETLSPAKSP SSSTGSIASS RKYPYPMPPL PDEERKANKQ SARLWETSI // ID F6WM09_HORSE Unreviewed; 755 AA. AC F6WM09; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSECAP00000021420}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSECAP00000021420, GN ECO:0000313|VGNC:VGNC:15046}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000021420, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000021420, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000021420, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000021420} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000021420}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 9796.ENSECAP00000021420; -. DR PaxDb; F6WM09; -. DR Ensembl; ENSECAT00000025733; ENSECAP00000021420; ENSECAG00000023662. DR VGNC; VGNC:15046; ADAM11. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F6WM09; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000002281; Chromosome 11. DR Bgee; ENSECAG00000023662; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 716 739 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 220 419 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 425 512 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 654 691 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 484 504 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 681 690 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 755 AA; 82331 MW; B90450E4615F02F5 CRC64; PGLGIRGPAG ALRWRVSPQL GVSEAPEVTE PSRLLQKSSG GEVRKQQLDT RVRQEPPGGP PAHLAQVSFV IPAFNSDFTL DLELNHHLLS SQYVERHFSR EGTTQHSTGA GDHCYYQGQL RGNPRSFAAL STCQGLHGVF SDGNFTYVVE PREMARPQEA PQGPLPHLIY RTPLLPAPLG CREPGCLFTA PAHSAPPNRP RLRRKRQVRR GHPTVHSETK YVELIVINDH QLFEQMRQSV VLTSNFAKSV VNLADVMYKE QLNTRIVLVA METWADGDKI QVQDDLLETL ARLMVYRREG LPEPSDATHL FSGRTFQSTS SGAAYVGGIC SLSRGGGVNE YDNMGAMAVT LAQTLGQNLG MMWNKHRSSA GDCKCPDNWL GCIMEDTGFY LPRKFSRCSI DEYNQFLQEG GGSCLFNKPL KLLDPPECGN GFVEAGEECD CGSVQECSRA GGNCCKKCTL THDAMCSDGL CCRRCKYEPR GVSCREAVNE CDIAETCTGD SSQCPPNLHK LDGYYCDHEQ GRCYGGRCKT RDQQCQALWG HAAADRFCYE KLNVEGTERG NCGRKGSGWV QCNKQDVLCG FLLCVNISGA PRLGDLGGDI SSVTFYHQGK ELDCRGGHVQ LADGSDLSYV EDGTACGPNM LCLDHRCLPA SAFNFSTCPG SGERRICSHH GVCSNEGKCI CQPDWTGKDC SIHNPLPTSP PTGETERYKG PSGTNIIIGS IAGAVLVAAI VLGGTGWGFK NIRRGRYDPT QQGAV // ID F6WML4_HORSE Unreviewed; 751 AA. AC F6WML4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSECAP00000021415}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSECAP00000021415, GN ECO:0000313|VGNC:VGNC:15046}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000021415, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000021415, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000021415, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000021415} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000021415}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSECAT00000025727; ENSECAP00000021415; ENSECAG00000023662. DR VGNC; VGNC:15046; ADAM11. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000002281; Chromosome 11. DR Bgee; ENSECAG00000023662; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 717 740 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 221 420 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 426 513 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 655 692 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 485 505 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 682 691 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 751 AA; 81730 MW; C742127A26B804B7 CRC64; SPGLGIRGPA GALRWRVSPQ LGVSEAPEVT EPSRLLQKSS GGEVRKQQLD TRVRQEPPGG PPAHLAQVSF VIPAFNSDFT LDLELNHHLL SSQYVERHFS REGTTQHSTG AGDHCYYQGQ LRGNPRSFAA LSTCQGLHGV FSDGNFTYVV EPREMARPQE APQGPLPHLI YRTPLLPAPL GCREPGCLFT APAHSAPPNR PRLRRKRQVR RGHPTVHSET KYVELIVIND HQLFEQMRQS VVLTSNFAKS VVNLADVMYK EQLNTRIVLV AMETWADGDK IQVQDDLLET LARLMVYRRE GLPEPSDATH LFSGRTFQST SSGAAYVGGI CSLSRGGGVN EYDNMGAMAV TLAQTLGQNL GMMWNKHRSS AGDCKCPDNW LGCIMEDTGF YLPRKFSRCS IDEYNQFLQE GGGSCLFNKP LKLLDPPECG NGFVEAGEEC DCGSVQECSR AGGNCCKKCT LTHDAMCSDG LCCRRCKYEP RGVSCREAVN ECDIAETCTG DSSQCPPNLH KLDGYYCDHE QGRCYGGRCK TRDQQCQALW GHAAADRFCY EKLNVEGTER GNCGRKGSGW VQCNKQDVLC GFLLCVNISG APRLGDLGGD ISSVTFYHQG KELDCRGGHV QLADGSDLSY VEDGTACGPN MLCLDHRCLP ASAFNFSTCP GSGERRICSH HGVCSNEGKC ICQPDWTGKD CSIHNPLPTS PPTGETERYK GPSGTNIIIG SIAGAVLVAA IVLGGTGWGF KNIRRGRSGG A // ID F6X3E3_XENTR Unreviewed; 770 AA. AC F6X3E3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 49. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSXETP00000007348}; GN Name=adam11 {ECO:0000313|Ensembl:ENSXETP00000007348, GN ECO:0000313|Xenbase:XB-GENE-966539}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000007348, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000007348} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000007348}; RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000007348} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMC01047350; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F6X3E3; -. DR STRING; 8364.ENSXETP00000007348; -. DR PaxDb; F6X3E3; -. DR Ensembl; ENSXETT00000007348; ENSXETP00000007348; ENSXETG00000003388. DR Xenbase; XB-GENE-966539; adam11. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F6X3E3; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Reactome; R-XTR-5682910; LGI-ADAM interactions. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; ENSXETG00000003388; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 736 759 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 231 433 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 439 528 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 674 711 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 500 520 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 701 710 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 770 AA; 84733 MW; 98AB342E7EC4B0C0 CRC64; MHPLGSSLVN TIVPPITAHS DSPKRWYQKL DHTQITHPSR LVGHTSGAET HRYQLNTRVR SENPNDQDAH VAHASFLVTF LEKKMILDLE LNHLLLSSKY VERHYDEDNN SYVKTGGTSG DHCYYQGKLR GVEDSWAAIS TCHGLSGAFS DGVYTYTIYP LKQSTEPCTG FPYHPEPDLL LNSSLIPSSH ACIQDFARAA PLLWNSLPQS SKIRRKRQVR RTSHSALTET KYVELMVVND RYLFDQQRQS VVLTSSFAKS VVNLADVLYR IGTEVISNIF VIFSRETWTS TDKITGSEDP LQVLDEFMRY RRAEILDHSD TTHLFSGRTF KSSRSGAAYF GGICSPSHGG GVNEYGNIGV MAVTLAQTLG QNLGMMWNKL RTTAGDCKCP DLWLGCIMED TGYYLPQKFS RCSVDEYSQF LQDGGGSCLF NKPLKLLDPP SCGNGFVELG EECDCGSPAQ ECNKSGAGNC CKKCTLSHDA MCSDGLCCRG CKYEPRGTVC RGSLNECDVP ETCPGDSSVC PANLHKQDGY FCDNEQGRCF GGRCKTRDRQ CHALWGRSAS DRFCYEKLNI EGTEKGNCGR DRQNWIQCSK QDVLCGYLLC SNISGIPQIG ELNGDITSMS FYHQNRYLDC RCAHRGGQVM LPDGSCLGYV EDGTPCGPNM MCLERRCLPA SAFNFSTCPG SWNGVICSDH GVCSNEGKCI CHPEWTGKDC SVYDPLPIPK PTGVVEKYKG PSGTNIIIGS IAGAVLIAAI VLGGTGWGFK NIRRGRSGGG // ID F6YUB2_XENTR Unreviewed; 656 AA. AC F6YUB2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 49. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSXETP00000000457}; GN Name=adam22 {ECO:0000313|Ensembl:ENSXETP00000000457, GN ECO:0000313|Xenbase:XB-GENE-957019}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000000457, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000000457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000000457}; RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000000457} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMC01087816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087818; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087819; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087821; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087822; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087823; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSXETT00000000457; ENSXETP00000000457; ENSXETG00000007431. DR Xenbase; XB-GENE-957019; adam22. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Reactome; R-XTR-5682910; LGI-ADAM interactions. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; ENSXETG00000007431; -. DR ExpressionAtlas; F6YUB2; baseline. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}. FT DOMAIN 158 357 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 363 450 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 594 630 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 422 442 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 620 629 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 656 AA; 73287 MW; 7DE5AFEAFC25A531 CRC64; QLTHVARASF QIDAFGSSFI LDVELNHDLL SSEYRERHVT QDGKTVEFKG GEHCYYQGQI RGKAKSFVAL STCYGLHGMF CDGNHTYLIE PGEKYNPNED YQFHSVYKSK VLEFPIDELP SEFWPLNDTS PRLSQQTRNQ RKKRQTRRYP RNVEDETKYV ELMIVNDHLM YKKHRLSVGH TNSYAKSVVN MADLIYKEQL NTRIVLVAME TWATDNKFSI SENPLLTLKE FMKYRRDFIK DKSDAVHLFS GSQFESSRSG AAYIGGVCSL LKGGGVNEFG KPDVMAVTLA QSLAHNLGIF SDKKKLLSGE CKCEDTWSGC IMGDIGYYLP SKFSVCNIEE YHEFLNNGGG SCLFNKPLKL LDPPECGNGF VEAGEECDCG TIAECAVEGG ECCKKCTLTQ DSECSDGLCC SDCKFNPKEM ICREAVNDCD IPETCTGNSS QCPANIHKLD GYQCESMQGL CFGGRCKTRE RQCKYIWGEK VSAADKYCYE KLNIEGTEKG NCGRNKETWI QCNKQDVLCG YLLCTNISSV PRLGELDGDV TTSSVVNQGK LYNCSGGHVK LDEDTDLGYV EDGTPCGTGM MCLEHRCLPI DSFNFSTCLG STNKICSGHG VCSNEVKCIC DSFWTGDDCS NFLPYDGIIK PDEGHRDEGQ YKLIVT // ID F6ZBS0_HORSE Unreviewed; 740 AA. AC F6ZBS0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000019826}; GN Name=LOC100056890 {ECO:0000313|Ensembl:ENSECAP00000019826}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000019826, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000019826, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019826, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000019826} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019826}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSECAT00000023894; ENSECAP00000019826; ENSECAG00000022220. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR Proteomes; UP000002281; Chromosome 27. DR Bgee; ENSECAG00000022220; -. DR ExpressionAtlas; F6ZBS0; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 740 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003352213. FT TRANSMEM 687 707 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 186 383 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 393 482 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 616 650 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 339 344 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 454 474 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 640 649 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 740 AA; 82809 MW; 97BD9B1CA3F51DBB CRC64; MLSLFLILSG LGRLTTAVHD SETPLIQITV PWKIGTNSSD DAVSGNHVAY AIKIDGKIYT FHLKKQSFLD PHFLVYSYNK SGTLYPDSSF IKSHCFYQGY AAEVPKSVVT LSTCSGLRGL LKLENVSYGI EPLGSAATYE HMLHRIKNNK ISFPPLQETY PMTELVDKSF RIFVKSEKNS DALTKRILKM QIVMDKALYN YMGSEVAVAT EKVVHIFSLI NTMFSQLKMT VMLTSLEIWS DQNKISSNGD ADEVLQRFVS WKEKFLFQRS HDMAFLLIYR DHQNYVGATY HGMACDPKFA AGIALYPKTI TLDAFSIVMV QLLGINLGLT YDDIYNCYCP GTTCIMNPQA IRSHGVKFFS SCSVNEFKHV VSQPQFECLQ NQTVSKVVYQ EKSSTCGNQV LEQFEECDCG SVEECSHKKC CHPENCTLIG NAECGSGICC DKKTCEIIGR GTICRESKDP CDFTEYCNGI SEFCVPDTKA FDLEPCNNKT AFCYGGTCRD PDVQCLELFG KFARGSTYLC TQEVNFQSDD YGNCNRGRCN YKQIHCGKMV CHWTHSQIVP STTYDIQYTF LGHVCMSAFI RNRSVSVAND RTYAVDGTIC DEQKVNKTRG DKVVLALNIC PVKTKCQGHG ICNNFLNCQC DAGYAPPTCE PTSSSPGGSV DDGFWTVESK NTYSFIKRRA AAPRKNGLLI SFYVFLPFLI LTAVIALKWN KIKRSWKREE TVSEGSISED SSSNSIQSHV // ID F7BKZ2_HORSE Unreviewed; 907 AA. AC F7BKZ2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSECAP00000016874}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSECAP00000016874, GN ECO:0000313|VGNC:VGNC:15052}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000016874, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000016874, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000016874, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000016874} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000016874}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 9796.ENSECAP00000016874; -. DR PaxDb; F7BKZ2; -. DR Ensembl; ENSECAT00000020549; ENSECAP00000016874; ENSECAG00000019027. DR VGNC; VGNC:15052; ADAM22. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F7BKZ2; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000002281; Chromosome 4. DR Bgee; ENSECAG00000019027; -. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 907 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003354257. FT TRANSMEM 738 761 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 532 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 676 713 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 504 524 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 703 712 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 907 AA; 100003 MW; 769F27CEB41A91BB CRC64; MRAAAAASVP FLLLCALGSC PPAALRPGGD ASLTELERRN ENRFLERQSI VPLRLLYRSG GEDETGHDAL DTRVRSDPGG GQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSGYIERHI EYGGKTVEVK GGEHCFYQGH IRGNPASFVA LSTCHGLHGM FCDGNHTYLI EPGDNDTSQE DFRFHSVYKS RLFEFPLDDL PSEFQQVNIT PPKFILKPRP KRIKRQLRRH PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADVIYQDQ LKTRIVLVAM ETWAADNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKTKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECALEG AECCKKCTLT QDSQCSDGLC CKTCVFFQPV GTVCREAVND CDIRETCSGN SSQCAPNIHK MDGYSCDGVQ GICFGGRCKT RDRQCKYIWG QKVMASDKYC YEKLNIEGTE KGNCGKDKDT WIQCNKRDVL CGYLLCTNIG NIPRLGELDG EITSTLVVQQ GRTLNCSGGH VKLEEDVDLG YVEDGTPCGP QMMCLEHRCL PVASFNFSTC LSNKEGTVCS GNGVCSNELK CVCNRHWIGA DCSTYFPHND DAKTGITLSG NGVAGTNIII GIIAGTILVL ALLLGITAWG YKNYREQRQL PQGDYVKKPG DGDSFYSDIP PGVSTNSASS SKKRSNGLSH SWSERIPDTK HISDICENGR PRSNSWQGNL GGNRKKIRGK RFRPRSNSTE TLSPAKSPSS STGSIASSRK YPYPMPPLPD EEKRVNRQSA RLWETSI // ID F7BQB4_HORSE Unreviewed; 730 AA. AC F7BQB4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000019871}; GN Name=LOC100056890 {ECO:0000313|Ensembl:ENSECAP00000019871}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000019871, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000019871, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019871, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000019871} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019871}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSECAT00000023947; ENSECAP00000019871; ENSECAG00000022220. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR Proteomes; UP000002281; Chromosome 27. DR Bgee; ENSECAG00000022220; -. DR ExpressionAtlas; F7BQB4; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 730 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003348886. FT TRANSMEM 692 712 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 186 383 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 393 482 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 619 653 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 339 344 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 454 474 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 643 652 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 730 AA; 81965 MW; A74DCFCAB75650D7 CRC64; MLSLFLILSG LGRLTTAVHD SETPLIQITV PWKIGTNSSD DAVSGNHVAY AIKIDGKIYT FHLKKQSFLD PHFLVYSYNK SGTLYPDSSF IKSHCFYQGY AAEVPKSVVT LSTCSGLRGL LKLENVSYGI EPLGSAATYE HMLHRIKNNK ISFPPLQETY PMTELVDKSF RIFVKSEKNS DALTKRILKM QIVMDKALYN YMGSEVAVAT EKVVHIFSLI NTMFSQLKMT VMLTSLEIWS DQNKISSNGD ADEVLQRFVS WKEKFLFQRS HDMAFLLIYR DHQNYVGATY HGMACDPKFA AGIALYPKTI TLDAFSIVMV QLLGINLGLT YDDIYNCYCP GTTCIMNPQA IRSHGVKFFS SCSVNEFKHV VSQPQFECLQ NQTVSKVVYQ EKSSTCGNQV LEQFEECDCG SVEECSHKKC CHPENCTLIG NAECGSGICC DKKTCEIIGR GTICRESKDP CDFTEYCNGI SEFCVPDTKA FDLEPCNNKT AFCYGGTCRD PDVQCLELFG KFARGSTYLC TQEVNFQSDD YGNCNRGRCN YKQIHCGKMV CHWTHSQIVP STTYDIQYTF LGHVCMSAFI RNRSVSVAND RTYAVDGTIC DEQKYCSRGA CLFVSDYPGK NRCISETKCQ GHGICNNFLN CQCDAGYAPP TCEPTSSSPG GSVDDGFWTV EREENNTYSF IKRRAAAPRK NGLLISFYVF LPFLILTAVI ALKWNKIKRS WKREETVSEG // ID F7BQP8_HORSE Unreviewed; 741 AA. AC F7BQP8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000019860}; GN Name=LOC100056890 {ECO:0000313|Ensembl:ENSECAP00000019860}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000019860, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000019860, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019860, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000019860} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019860}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F7BQP8; -. DR PaxDb; F7BQP8; -. DR Ensembl; ENSECAT00000023933; ENSECAP00000019860; ENSECAG00000022220. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR InParanoid; F7BQP8; -. DR OMA; TMFSQLN; -. DR OrthoDB; EOG091G0302; -. DR TreeFam; TF314733; -. DR Proteomes; UP000002281; Chromosome 27. DR Bgee; ENSECAG00000022220; -. DR ExpressionAtlas; F7BQP8; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 741 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003354386. FT TRANSMEM 693 713 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 186 383 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 393 482 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 619 653 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 339 344 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 454 474 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 643 652 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 741 AA; 82911 MW; BBFD8968346DDC48 CRC64; MLSLFLILSG LGRLTTAVHD SETPLIQITV PWKIGTNSSD DAVSGNHVAY AIKIDGKIYT FHLKKQSFLD PHFLVYSYNK SGTLYPDSSF IKSHCFYQGY AAEVPKSVVT LSTCSGLRGL LKLENVSYGI EPLGSAATYE HMLHRIKNNK ISFPPLQETY PMTELVDKSF RIFVKSEKNS DALTKRILKM QIVMDKALYN YMGSEVAVAT EKVVHIFSLI NTMFSQLKMT VMLTSLEIWS DQNKISSNGD ADEVLQRFVS WKEKFLFQRS HDMAFLLIYR DHQNYVGATY HGMACDPKFA AGIALYPKTI TLDAFSIVMV QLLGINLGLT YDDIYNCYCP GTTCIMNPQA IRSHGVKFFS SCSVNEFKHV VSQPQFECLQ NQTVSKVVYQ EKSSTCGNQV LEQFEECDCG SVEECSHKKC CHPENCTLIG NAECGSGICC DKKTCEIIGR GTICRESKDP CDFTEYCNGI SEFCVPDTKA FDLEPCNNKT AFCYGGTCRD PDVQCLELFG KFARGSTYLC TQEVNFQSDD YGNCNRGRCN YKQIHCGKMV CHWTHSQIVP STTYDIQYTF LGGVCMSAFI RNRSVSVAND RTYAVDGTIC DEQKYCSRGA CLFVSDYPGK NRCISETKCQ GHGICNNFLN CQCDAGYAPP TCEPTSSSPG GSVDDGFWTV EITDCKNTYS FIKRRAAAPR KNGLLISFYV FLPFLILTAV IALKWNKIKR SWKREETVSE GSISEDSSSN S // ID F7CA21_XENTR Unreviewed; 835 AA. AC F7CA21; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSXETP00000016173}; GN Name=adam22 {ECO:0000313|Ensembl:ENSXETP00000016173, GN ECO:0000313|Xenbase:XB-GENE-957019}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000016173, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000016173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000016173}; RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000016173} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMC01087816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087818; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087819; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087821; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087822; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01087823; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSXETT00000016173; ENSXETP00000016173; ENSXETG00000007431. DR Xenbase; XB-GENE-957019; adam22. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Reactome; R-XTR-5682910; LGI-ADAM interactions. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; ENSXETG00000007431; -. DR ExpressionAtlas; F7CA21; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 655 678 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 158 357 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 363 450 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 594 630 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 422 442 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 620 629 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 835 AA; 92708 MW; 913E9EA45E985593 CRC64; QLTHVARASF QIDAFGSSFI LDVELNHDLL SSEYRERHVT QDGKTVEFKG GEHCYYQGQI RGKAKSFVAL STCYGLHGMF CDGNHTYLIE PGEKYNPNED YQFHSVYKSK VLEFPIDELP SEFWPLNDTS PRLSQQTRNQ RKKRQTRRYP RNVEDETKYV ELMIVNDHLM YKKHRLSVGH TNSYAKSVVN MADLIYKEQL NTRIVLVAME TWATDNKFSI SENPLLTLKE FMKYRRDFIK DKSDAVHLFS GSQFESSRSG AAYIGGVCSL LKGGGVNEFG KPDVMAVTLA QSLAHNLGIF SDKKKLLSGE CKCEDTWSGC IMGDIGYYLP SKFSVCNIEE YHEFLNNGGG SCLFNKPLKL LDPPECGNGF VEAGEECDCG TIAECAVEGG ECCKKCTLTQ DSECSDGLCC SDCKFNPKEM ICREAVNDCD IPETCTGNSS QCPANIHKLD GYQCESMQGL CFGGRCKTRE RQCKYIWGEK VSAADKYCYE KLNIEGTEKG NCGRNKETWI QCNKQDVLCG YLLCTNISSV PRLGELDGDV TTSSVVNQGK LYNCSGGHVK LDEDTDLGYV EDGTPCGTGM MCLEHRCLPI DSFNFSTCLG STNKICSGHG VCSNEVKCIC DSFWTGDDCS NFLPYDGIIK PDEGHRDEGV ISTNIIIGAI AGTILVLALV LGITAWGYNA VGHSGQIPQG DYVKKPGDAD SFYSDLPPGV SSNSASSSKK RSAILSHFQI SACSIPHYSI SQNISLFCRR SNGLSHSWSE RIPDTKHVSD VCENGRPRSN SWQGNVSSSR KKLRGKRFRP RSNSTDLGSK QILLRKILDS HGSNKMCIWC IPTFK // ID F7G5P9_MACMU Unreviewed; 769 AA. AC F7G5P9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 23-MAY-2018, entry version 48. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSMMUP00000007214}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSMMUP00000007214}; 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 {ECO:0000313|Ensembl:ENSMMUP00000007214, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000007214, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000007214, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000007214} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000007214}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSUE03016975; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_014975368.1; XM_015119882.1. DR UniGene; Mmu.29553; -. DR STRING; 9544.ENSMMUP00000007214; -. DR Ensembl; ENSMMUT00000007682; ENSMMUP00000007214; ENSMMUG00000029927. DR GeneID; 100430916; -. DR KEGG; mcc:100430916; -. DR CTD; 4185; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F7G5P9; -. DR KO; K16067; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000006718; Chromosome 16. DR Bgee; ENSMMUG00000029927; -. DR ExpressionAtlas; F7G5P9; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 769 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008957012. FT TRANSMEM 735 758 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 673 710 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 700 709 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 769 AA; 83541 MW; 9482346C0B697525 CRC64; MRLLRRWAFA ALLLPLLPPP GLGTQGSAGA LRWGRLPQLG GPGAPEVTEP SRLVRESSGG EVRKQQLDTR VRQEPPGGPP VHLAQVSFVI PAFNSNFTLD LELNHHLLSS KYVERHFSRE GTTQHSTGAG DHCYYQGKLR GNLHSFAALS TCQGLHGVFS DGNLTYIVEP QDMAGPWGAP QGPLPHLIYR TPLLPDPLGC RELGCLFAVP AQSAPPNRPR LRRKRQVRRG HPTVHSETKY VELIVINDHQ LFEQMRQSVV LTSNFAKSVV NLADVIYKEQ LNTRIVLVAM ETWADGDKIQ VQDDLLETLA RLMVYRREGL PEPSDATHLF SGRTFQSTSS GAAYVGGICS LSRGGGVNEY GNMGAMAVTL AQTLGQNLGM MWNKHRSSAG DCKCPDIWLG CIMEDTGFYL PRKFSRCSID EYNQFLQEGG GSCLFNKPLK LLDPPECGNG FVEAGEECDC GSVQECSRAG GNCCKKCTLT HDAMCSDGLC CRRCKYEPRG VSCREAVNEC DIAETCTGDS SQCPPNLHKL DGYYCDHEQG RCYGGRCKTR DRQCQALWGH AAADRFCYEK LNVEGTERGS CGRKGSGWVQ CSKQDVLCGF LLCVNVSGAP RLGDLVGDIS SVTFYHQGKE LDCRGGHVQL ADGSDLSYVE DGTACGPNML CLDHRCLPAS AFNFSTCPGS GERRICSHHG VCSNEGKCIC QPDWTGKDCS IHNPLPTSPP TGETERYKGP SGTNIIIGSI AGAVLVAAIV LGGTGWGFKN IRRGRSGGA // ID F7GSM9_MACMU Unreviewed; 854 AA. AC F7GSM9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 28-MAR-2018, entry version 49. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSMMUP00000029882}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSMMUP00000029882}; 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 {ECO:0000313|Ensembl:ENSMMUP00000029882, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000029882, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000029882, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000029882} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000029882}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSUE03028831; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03028832; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03028833; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03028834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMMUT00000031938; ENSMMUP00000029882; ENSMMUG00000022695. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000006718; Chromosome 3. DR Bgee; ENSMMUG00000022695; -. DR ExpressionAtlas; F7GSM9; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 854 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008957160. FT TRANSMEM 300 324 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 692 715 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 331 404 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 410 487 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. SQ SEQUENCE 854 AA; 95736 MW; 1EC716E84DF3351F CRC64; MQAAVAVSVP FLLLCALGTC PPARCGQAGD ASLMELEKRK ENRFLERQSI VPLRLIYRSG GEDETRHDAL DTRVRGDPGG RQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYVERHI EHGGKTVEVK GGEHCYYQGH IRGNPASFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFPLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MVGFAVVFKP VLCAPKLKTR IVLVAMETWA TGTQFMKYRR EFYSEEKNDI VTFFSGSFSV TSWIYIYFIF VFVFQFGKTD LMAVTLAQSL AHNIGIISDK RKLASGECKC EDTWSGCIMG DTGYYLPKKF TQCNVEEYHD FLNSGGGACL FNKPSKLLDP PECGNGFIET GEECDCGTPA ECVLEGAECC KKCTLTQDSQ CSDGLCCKKC KFQPMGTVCR EAVNDCDIRE TCSGNSSQVI YRITGICFGG RCKTRDRQCK YIWGQKVTAS DKYCYEKLNI EGTEKGNCGK NKDTWIQCNK RDVLCGYLLC TNIGNIPRLG ELDGEITSTL VVQQGRTLNC SGGHVKLEED VDLGYVEDGT PCGPQMMCLE HRCLPVASFN FSTCLSSKEG TICSGNGVCS NELKCVCNRH WIGSDCNTYF PHNDDAKTGI TLSGNGVAGT NIIIGIIAGT ILVLALILGI TAWGYKNYRE QRSNGLSHSW SERIPDTKHI SDICENGRPR SNSWQGNLGG NKKKIRGKRF RPRSNSTEYL NPWFKRDYNV AKWVEDVNKN TEGPYFRTLS PAKSPSSSTG SIASSRKYPY PMPPLPDEEK KVNRQSARLW ETSI // ID F7GSN2_MACMU Unreviewed; 861 AA. AC F7GSN2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 28-MAR-2018, entry version 51. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSMMUP00000029881}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSMMUP00000029881}; 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 {ECO:0000313|Ensembl:ENSMMUP00000029881, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000029881, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000029881, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000029881} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000029881}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSUE03028831; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03028832; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03028833; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03028834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9544.ENSMMUP00000029881; -. DR Ensembl; ENSMMUT00000031937; ENSMMUP00000029881; ENSMMUG00000022695. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F7GSN2; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000006718; Chromosome 3. DR Bgee; ENSMMUG00000022695; -. DR ExpressionAtlas; F7GSN2; baseline. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 861 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008957157. FT TRANSMEM 300 324 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 692 715 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 331 404 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 410 487 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. SQ SEQUENCE 861 AA; 95900 MW; 446892960DB25325 CRC64; MQAAVAVSVP FLLLCALGTC PPARCGQAGD ASLMELEKRK ENRFLERQSI VPLRLIYRSG GEDETRHDAL DTRVRGDPGG RQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYVERHI EHGGKTVEVK GGEHCYYQGH IRGNPASFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFPLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MVGFAVVFKP VLCAPKLKTR IVLVAMETWA TGTQFMKYRR EFYSEEKNDI VTFFSGSFSV TSWIYIYFIF VFVFQFGKTD LMAVTLAQSL AHNIGIISDK RKLASGECKC EDTWSGCIMG DTGYYLPKKF TQCNVEEYHD FLNSGGGACL FNKPSKLLDP PECGNGFIET GEECDCGTPA ECVLEGAECC KKCTLTQDSQ CSDGLCCKKC KFQPMGTVCR EAVNDCDIRE TCSGNSSQVI YRITGICFGG RCKTRDRQCK YIWGQKVTAS DKYCYEKLNI EGTEKGNCGK NKDTWIQCNK RDVLCGYLLC TNIGNIPRLG ELDGEITSTL VVQQGRTLNC SGGHVKLEED VDLGYVEDGT PCGPQMMCLE HRCLPVASFN FSTCLSSKEG TICSGNGVCS NELKCVCNRH WIGSDCNTYF PHNDDAKTGI TLSGNGVAGT NIIIGIIAGT ILVLALILGI TAWGYKNYRE QRQLPQGDYV KKPGDGDSFY SDIPPGVSTN SASSSKKRSN GLSHSWSERI PDTKHISDIC ENGRPRSNSW QGNLGGNKKK IRGKRFRPRS NSTETLSPAK SPSSSTGSIA SSRKYPYPMP PLPDEEKKVN RQSARLWETS I // ID F7I630_CALJA Unreviewed; 747 AA. AC F7I630; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSCJAP00000022586}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSCJAP00000022586}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000022586, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000022586, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000022586} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01125075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01125076; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9483.ENSCJAP00000022586; -. DR Ensembl; ENSCJAT00000023892; ENSCJAP00000022586; ENSCJAG00000012274. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; F7I630; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000008225; Chromosome 5. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 713 736 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 217 416 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 422 509 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 651 688 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 481 501 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 678 687 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 747 AA; 80962 MW; 133E34D523B8E4FA CRC64; PGLGTRGPAG ALRWGSLSQL GGPEAPEVTE PSRLVRKSSG GEVRKQQLDT RVRQEPPGGP PVHLAQVSFV IPAFNSNFTL DLELNHHLLS SQYVERHFSR EGTTQHSTGA GDHCYYQGKL RGNTHSFAAL STCQGLHGVF SDGNVTYIVE PQEVAGPWGA PQGPLPHLIY RTPLLPDPLP TGCLFTVPAQ SAPPNHPRLR RKRQVRRGHP TVHSETKYVE LIVINDHQLF EQMRQSVVLT SNLGKSVVNL ADEIYKEQLN TRIVLVAMET WADGDKIQVQ DDLLETLARL MVYRREGLPE PSDATHLFSG RTFQSTSSGA AYVGGICSLS RGGGVNEYGN MGAMAVTLAQ TLGQNLGMMW NKHRSSAGDC KCPDIWLGCI MEDTGFYLPR KFSRCSIDEY NQFLQEGGGS CLFNKPLKLL DPPECGNGFV EAGEECDCGS VQECSRAGGN CCKKCTLTHD AMCSDGLCCR RCKYEPRGVS CREAVNECDI AETCTGDSSQ CPPNLHKLDG YYCDHEQGRC YGGRCKTRDR QCQALWGQVA ADRFCYEKLN VEGTERGSCG RKGSGWVQCS KQDVLCGFLL CVNISGAPRL GDLVGDISSV TFYHQGKELD CRGGHVQLAD GSDLSYVEDG TACGPNMLCL DHRCLPASAF NFSTCPGSGE RRICSHHGVC SNEGKCICQP DWTGKDCSIH NPLPTSPPTG ETERYKGPSG TNIIIGSIAG AVLVAAIVLG GTGWGFKNIR RGRSGGA // ID F7IGK7_CALJA Unreviewed; 899 AA. AC F7IGK7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 28-MAR-2018, entry version 48. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSCJAP00000026306}; DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 isoform 2 preproprotein {ECO:0000313|EMBL:JAB18767.1}; GN Name=ADAM22 {ECO:0000313|EMBL:JAB18767.1, GN ECO:0000313|Ensembl:ENSCJAP00000026306}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000026306, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000026306, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000026306} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. RN [3] {ECO:0000313|EMBL:JAB18767.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Hippocampus {ECO:0000313|EMBL:JAB18767.1}; RX PubMed=25243066; DOI=10.1186/2047-217X-3-14; RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C., RA Moriyama E.N., French J.A., Norgren R.B.Jr.; RT "De novo assembly of the common marmoset transcriptome from NextGen RT mRNA sequences."; RL Gigascience 3:14-14(2014). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01062606; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062607; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062608; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062609; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062610; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062611; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062612; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062613; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062614; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062615; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; GAMS01004369; JAB18767.1; -; mRNA. DR RefSeq; XP_002751672.1; XM_002751626.3. DR MEROPS; M12.978; -. DR Ensembl; ENSCJAT00000027801; ENSCJAP00000026306; ENSCJAG00000014311. DR GeneID; 100395237; -. DR CTD; 53616; -. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000008225; Chromosome 8. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Integrin {ECO:0000313|EMBL:JAB18767.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 899 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014091273. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 899 AA; 100226 MW; EDB69EE3F9152FB1 CRC64; MLAAAAASVP FLLLCALGTC PPARCGQAGD ALLTELEKRK EDRFLERQSI VPLRLIYRSG GEDETQRDAL DTLVRGDPGG QKLTHVDRAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI EPGDKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFPLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPMITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIEAGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRSNG LSHSWSERIP DTKHISDICE NGRPRSNSWQ GNLGGNKKKI RGKRFRPRSN STEYLNPWFK RDYNVAKWVE DVNKNTEGPY FRTLSPAKSP SSSTGSIASS RKYPYPMPPL PDEEKKVNRQ SARLWETSI // ID F7IQU2_CALJA Unreviewed; 906 AA. AC F7IQU2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 25-APR-2018, entry version 50. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSCJAP00000026487}; DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 isoform 1 preproprotein {ECO:0000313|EMBL:JAB18766.1}; GN Name=ADAM22 {ECO:0000313|EMBL:JAB18766.1, GN ECO:0000313|Ensembl:ENSCJAP00000026487}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000026487, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000026487, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000026487} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. RN [3] {ECO:0000313|EMBL:JAB18766.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Hippocampus {ECO:0000313|EMBL:JAB18766.1}; RX PubMed=25243066; DOI=10.1186/2047-217X-3-14; RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C., RA Moriyama E.N., French J.A., Norgren R.B.Jr.; RT "De novo assembly of the common marmoset transcriptome from NextGen RT mRNA sequences."; RL Gigascience 3:14-14(2014). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01062606; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062607; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062608; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062609; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062610; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062611; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062612; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062613; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062614; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062615; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; GAMS01004370; JAB18766.1; -; mRNA. DR RefSeq; XP_002751671.2; XM_002751625.4. DR STRING; 9483.ENSCJAP00000026487; -. DR MEROPS; M12.978; -. DR Ensembl; ENSCJAT00000027999; ENSCJAP00000026487; ENSCJAG00000014311. DR GeneID; 100395237; -. DR KEGG; cjc:100395237; -. DR CTD; 53616; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR KO; K16068; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000008225; Chromosome 8. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Integrin {ECO:0000313|EMBL:JAB18766.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 906 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014091302. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 906 AA; 100390 MW; 040D1D354A0755F6 CRC64; MLAAAAASVP FLLLCALGTC PPARCGQAGD ALLTELEKRK EDRFLERQSI VPLRLIYRSG GEDETQRDAL DTLVRGDPGG QKLTHVDRAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI EPGDKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFPLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPMITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIEAGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE EKKVNRQSAR LWETSI // ID F7IT50_CALJA Unreviewed; 870 AA. AC F7IT50; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 28-MAR-2018, entry version 43. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSCJAP00000026478}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSCJAP00000026478}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000026478, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000026478, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000026478} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01062606; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062607; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062608; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062609; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062610; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062611; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062612; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062613; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062614; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01062615; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002751673.1; XM_002751627.3. DR ProteinModelPortal; F7IT50; -. DR MEROPS; M12.978; -. DR Ensembl; ENSCJAT00000027991; ENSCJAP00000026478; ENSCJAG00000014311. DR GeneID; 100395237; -. DR CTD; 53616; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000008225; Chromosome 8. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 870 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003355883. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 870 AA; 96594 MW; CBC00F8E9327C6BB CRC64; MLAAAAASVP FLLLCALGTC PPARCGQAGD ALLTELEKRK EDRFLERQSI VPLRLIYRSG GEDETQRDAL DTLVRGDPGG QKLTHVDRAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI EPGDKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFPLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPMITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIEAGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRSNG LSHSWSERIP DTKHISDICE NGRPRSNSWQ GNLGGNKKKI RGKRFRPRSN STETLSPAKS PSSSTGSIAS SRKYPYPMPP LPDEEKKVNR QSARLWETSI // ID ADAM3_MOUSE Reviewed; 822 AA. AC F8VQ03; DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot. DT 21-SEP-2011, sequence version 1. DT 23-MAY-2018, entry version 68. DE RecName: Full=A disintegrin and metallopeptidase domain 3 {ECO:0000312|MGI:MGI:102518}; DE AltName: Full=Cyritestin {ECO:0000312|MGI:MGI:102518}; DE Flags: Precursor; GN Name=Adam3 {ECO:0000312|MGI:MGI:102518}; GN Synonyms=Cyrn1 {ECO:0000312|MGI:MGI:102518}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP CHARACTERIZATION. RX PubMed=11439107; RA Grzmil P., Kim Y., Shamsadin R., Neesen J., Adham I.M., Heinlein U.A., RA Schwarzer U.J., Engel W.; RT "Human cyritestin genes (CYRN1 and CYRN2) are non-functional."; RL Biochem. J. 357:551-556(2001). RN [3] RP SUBCELLULAR LOCATION, AND PROCESSING. RX PubMed=15514464; RA Kim E., Nishimura H., Iwase S., Yamagata K., Kashiwabara S., Baba T.; RT "Synthesis, processing, and subcellular localization of mouse ADAM3 RT during spermatogenesis and epididymal sperm transport."; RL J. Reprod. Dev. 50:571-578(2004). RN [4] RP FUNCTION. RX PubMed=19339711; DOI=10.1095/biolreprod.108.074021; RA Yamaguchi R., Muro Y., Isotani A., Tokuhiro K., Takumi K., Adham I., RA Ikawa M., Okabe M.; RT "Disruption of ADAM3 impairs the migration of sperm into oviduct in RT mouse."; RL Biol. Reprod. 81:142-146(2009). RN [5] RP INTERACTION WITH TEX101. RX PubMed=23633567; DOI=10.1073/pnas.1222166110; RA Fujihara Y., Tokuhiro K., Muro Y., Kondoh G., Araki Y., Ikawa M., RA Okabe M.; RT "Expression of TEX101, regulated by ACE, is essential for the RT production of fertile mouse spermatozoa."; RL Proc. Natl. Acad. Sci. U.S.A. 110:8111-8116(2013). RN [6] RP INTERACTION WITH LY6K, AND PROCESSING. RX PubMed=24501175; DOI=10.1095/biolreprod.113.112888; RA Fujihara Y., Okabe M., Ikawa M.; RT "GPI-anchored protein complex, LY6K/TEX101, is required for sperm RT migration into the oviduct and male fertility in mice."; RL Biol. Reprod. 90:60-60(2014). CC -!- FUNCTION: Involved in fertilization by controlling sperm migration CC into oviduct. {ECO:0000269|PubMed:19339711}. CC -!- SUBUNIT: Interacts with LY6K (PubMed:24501175). Interacts with CC TEX101 (PubMed:23633567). {ECO:0000269|PubMed:23633567, CC ECO:0000269|PubMed:24501175}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15514464}; CC Single-pass membrane protein {ECO:0000255}. Note=Localized in CC round and elongating spermatids. Localized on the anterior part of CC the sperm head, and is removed during the acrosome reaction. CC {ECO:0000269|PubMed:15514464}. CC -!- PTM: Initially synthesized as a 110-kDa precursor in round CC spermatids, and the precursor is then processed into a 42-kDa CC mature protein during the sperm transport into and/or once in the CC epididymis. {ECO:0000269|PubMed:15514464, CC ECO:0000269|PubMed:24501175}. CC -!- CAUTION: There are two genes in human, ADAM3A and ADAM3B that are CC non-functional (PubMed:11439107). ADAM3A gene is deleted in CC infertile men and in some fertile men. ADAM3B transcripts, from CC testicular RNA of ADAM3A-deficient men, present many stop codons CC in all possible reading frames. Moreover these two proteins are CC neither detected in extracts from the testis of a man with the CC ADAM3A-positive genotype, nor of a man with a ADAM3A-deficient CC genotype. {ECO:0000305|PubMed:11439107}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC138355; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS22196.1; -. DR RefSeq; NP_033749.2; NM_009619.5. DR UniGene; Mm.5168; -. DR STRING; 10090.ENSMUSP00000033958; -. DR MaxQB; F8VQ03; -. DR PaxDb; F8VQ03; -. DR PRIDE; F8VQ03; -. DR DNASU; 11497; -. DR Ensembl; ENSMUST00000033958; ENSMUSP00000033958; ENSMUSG00000031553. DR Ensembl; ENSMUST00000171438; ENSMUSP00000132651; ENSMUSG00000031553. DR GeneID; 11497; -. DR KEGG; mmu:11497; -. DR UCSC; uc009lfc.1; mouse. DR CTD; 11497; -. DR MGI; MGI:102518; Adam3. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR OMA; TMFSQLN; -. DR OrthoDB; EOG091G0302; -. DR TreeFam; TF314733; -. DR ChiTaRS; Adam3; mouse. DR PRO; PR:F8VQ03; -. DR Proteomes; UP000000589; Chromosome 8. DR Bgee; ENSMUSG00000031553; -. DR ExpressionAtlas; F8VQ03; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0045121; C:membrane raft; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0061827; C:sperm head; IDA:UniProtKB. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI. DR GO; GO:0009566; P:fertilization; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI. DR GO; GO:0050684; P:regulation of mRNA processing; IMP:MGI. DR GO; GO:0007338; P:single fertilization; IGI:MGI. DR GO; GO:0097722; P:sperm motility; IMP:UniProtKB. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; EGF-like domain; KW Membrane; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 16 {ECO:0000255}. FT CHAIN 17 822 A disintegrin and metallopeptidase domain FT 3. {ECO:0000255}. FT /FTId=PRO_5010674208. FT TRANSMEM 689 709 Helical. {ECO:0000255}. FT DOMAIN 187 384 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 395 484 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT DOMAIN 619 653 EGF-like. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DISULFID 296 379 {ECO:0000255|PROSITE-ProRule:PRU00276}. FT DISULFID 338 363 {ECO:0000255|PROSITE-ProRule:PRU00276}. FT DISULFID 340 345 {ECO:0000255|PROSITE-ProRule:PRU00276}. FT DISULFID 456 476 {ECO:0000255|PROSITE-ProRule:PRU00068}. FT DISULFID 623 635 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 629 641 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 643 652 {ECO:0000255|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 822 AA; 91444 MW; C38E63DC72558094 CRC64; MLPLFLVLSY LGQVIAAGKD VETPLLQITV PEKIDTNIQD AKEAETQVTY VVRIEGKAYT LQLEKQSFLH PLFGTYLRDK LGTLQPYFSL VKTHCFYQGH AAEIPVSTVT LSTCSGLRGL LQLENITYGI EPLESSATFE HILYEIKNNK IDYSPLKENF ANSEQESQSY RILVKPEKGS NSTLTKRILR IKIIMDKAMF DHMGSEVGVA TQKVVHIFGL INTMFSQLKM TVMLNSLEIW SEQDKIETNG DADEVLQRFL LWKSKEISQK AQDITYLLLY KDHPDYVGAT YHGMACNPNF TAGIALHPKT LAVEGFAIVL SQLLGINLGL AYDDVYNCFC PGSTCIMNPS AIRSQGIKVF SSCSVDEFKQ LASQPELDCL RNTSETEFVV QPQGGSYCGN HLLEVPEQCD CGPPETCTHK KCCNPKDCTL IDAAQCGTGP CCDKRTCTIA ERGRLCRKSK DQCDFPEFCN GETEGCAPDT KAADLEPCNN ETAYCFGGVC RDPDRQCTDL FGKYAKGPNY VCAQEVNLQN DKFGNCHGRC NYSAIFCGKA VCYWNFAEVI QTEKYDVQYT YLGGQVCVSA HLRSQTGTRD DTYVHDGTVC GSGQVCFRGD CLRVHVLRGT RECEADDKCQ GHGICNNLNN CQCESGFAPP ECDMTPSSPG GSMDDGFWLP FDKSTPLIFK RHGLKYKKVL LISFYILLPF LVVLAFMAVK RMIGKRLAKQ NISKALEHKE EAFNRGSMNP GVVSGGNTDQ NLMTVPGSFN SYAYHGNTDQ NFMTVPGSFN SYSYHGNTDQ NFMTVPGSFN SYSYQDVPYY RSIPEDGNDS QQ // ID F8WAD8_HUMAN Unreviewed; 804 AA. AC F8WAD8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 23-MAY-2018, entry version 56. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 {ECO:0000313|Ensembl:ENSP00000381261}; DE Flags: Fragment; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSP00000381261}; 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 {ECO:0000313|Ensembl:ENSP00000381261, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000381261, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX 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] {ECO:0000313|Ensembl:ENSP00000381261} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC004992; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005164; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F8WAD8; -. DR MaxQB; F8WAD8; -. DR PeptideAtlas; F8WAD8; -. DR PRIDE; F8WAD8; -. DR Ensembl; ENST00000398203; ENSP00000381261; ENSG00000008277. DR UCSC; uc064fcf.1; human. DR EuPathDB; HostDB:ENSG00000008277.14; -. DR HGNC; HGNC:201; ADAM22. DR OpenTargets; ENSG00000008277; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR ChiTaRS; ADAM22; human. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000008277; -. DR ExpressionAtlas; F8WAD8; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0000213|MaxQB:F8WAD8, KW ECO:0000213|PeptideAtlas:F8WAD8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 704 727 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 206 405 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 411 498 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 470 490 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT NON_TER 804 804 {ECO:0000313|Ensembl:ENSP00000381261}. SQ SEQUENCE 804 AA; 89520 MW; 8348B9C555C51C39 CRC64; MELEKRKENR FVERQSIVPL RLIYRSGGED ESRHDALDTR VRGDLGGPQL THVDQASFQV DAFGTSFILD VVLNHDLLSS EYIERHIEHG GKTVEVKGGE HCYYQGHIRG NPDSFVALST CHGLHGMFYD GNHTYLIEPE ENDTTQEDFH FHSVYKSRLF EFSLDDLPSE FQQVNITPSK FILKPRPKRS KRQLRRYPRN VEEETKYIEL MIVNDHLMFK KHRLSVVHTN TYAKSVVNMA DLIYKDQLKT RIVLVAMETW ATDNKFAISE NPLITLREFM KYRRDFIKEK SDAVHLFSGS QFESSRSGAA YIGGICSLLK GGGVNEFGKT DLMAVTLAQS LAHNIGIISD KRKLASGECK CEDTWSGCIM GDTGYYLPKK FTQCNIEEYH DFLNSGGGAC LFNKPSKLLD PPECGNGFIE TGEECDCGTP AECVLEGAEC CKKCTLTQDS QCSDGLCCKK CKFQPMGTVC REAVNDCDIR ETCSGNSSQC APNIHKMDGY SCDGVQGICF GGRCKTRDRQ CKYIWGQKVT ASDKYCYEKL NIEGTEKGNC GKDKDTWIQC NKRDVLCGYL LCTNIGNIPR LGELDGEITS TLVVQQGRTL NCSGGHVKLE EDVDLGYVED GTPCGPQMMC LEHRCLPVAS FNFSTCLSSK EGTICSGNGV CSNELKCVCN RHWIGSDCNT YFPHNDDAKT GITLSGNGVA GTNIIIGIIA GTILVLALIL GITAWGYKNY REQRQLPQGD YVKKPGDGDS FYSDIPPGVS TNSASSSKKR SNGLSHSWSE RIPDTKHISD ICENGRPRSN SWQG // ID G0NSF5_CAEBE Unreviewed; 1036 AA. AC G0NSF5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 22-NOV-2017, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGT36733.1}; GN ORFNames=CAEBREN_16546 {ECO:0000313|EMBL:EGT36733.1}; OS Caenorhabditis brenneri (Nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068}; RN [1] {ECO:0000313|Proteomes:UP000008068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068}; RG Caenorhabditis brenneri Sequencing and Analysis Consortium; RA Wilson R.K.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL379937; EGT36733.1; -; Genomic_DNA. DR ProteinModelPortal; G0NSF5; -. DR STRING; 135651.CBN16546; -. DR EnsemblMetazoa; CBN16546; CBN16546; WBGene00155271. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR InParanoid; G0NSF5; -. DR OMA; PKKHFHR; -. DR OrthoDB; EOG091G01L9; -. DR Proteomes; UP000008068; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008068}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008068}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 1036 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003406341. FT TRANSMEM 742 764 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 225 425 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 431 518 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 490 510 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 1036 AA; 113912 MW; 068605D5D7152B7B CRC64; MLVFVFLVIC SIGGVMAKVD IRQTTANKAF METMRPDGYE IVHPFQIRDK NERIGIDTRN YFLKAQEHYS HVTIVIRSNQ LGRLKLVLER NNFVFLNQTA FHKLDADGER VIQNRVENCY YQGTVGGEES SFVALSSCNG LRGVISFANG TTYGIWPLDG GDRNSRRHPH ILYKSEWSQD AKCGSSMAHA VGQRIRREHK HRKHHKKIHD EDNQKMRRDA SKRTKYVEVA LIADYEFMKQ RGLHDMDAIS YMLESLNIAD SMLSRDLNIR LSAVYVELWS DVQRIDLWED IERTLSGVVD YAAGHIYHIQ KDASILFTAG SFANQEVSNA AIRSICTARS AVILRSIEQF ATHWNGELMA QSVGHLLGLE HDTAACSCEP SPECLMRQQP GRVGAPFSWQ FSKCSVARMH GIWQDGNIQC LLNKPFQVSE LRECGNGIVD GSEECDCGTR ENCNDPCCDP LTCTLRPHAQ CAAHHKCCHR CELRKAGETC RASKSPCDVA ESCDGKSGDC PPDGHLIDGT VCGTDGQCWR GNCSDSHQQC QKLWGRDARV ADQVCFDQNT KGAEYANCGV QADGSYHPCQ IEDTKCGTLH CHSGSITPLD QALKAFTFHF TENSQQIQCK SIAPSGGVLL GQSQDGTNCG SGKVCVAGSC VEMSSVTSAT ACPTNNLALL CSGHGHCTTT AKCVCFNGWS GGACDIRSNT STYQGSMGFS EENRGGQGAQ GGRKTIMIPH LNIGTTLETA TLFAILLGFG VFLMLCLVCL MLCYRRKSVV EIPKPTDEKL EESPDRQIKF GNMPSYREEK RKRKSNKRIY GALNRITEAD ERDSTSLRSR DSAGSQQLLD RNGQPAMMGG IRDPYAGEHI YAESSSTSQN LATRQFRGIN SDGSYPLRSF GSWRSSGPIS PASSSGHLTD VSTATTPLRL NKIGKLLKTM QSDDEGGSPF SDHPLLRGPT GLDYTSLAGP SYSNPGNGEE ELSAVEADHD VGSNTESSRG CEDGPIDGWD PPSIVNGASS NNYQFRQSPS LFSDPFKLEM TNSMHN // ID G0NSI8_CAEBE Unreviewed; 1021 AA. AC G0NSI8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGT36807.1}; GN ORFNames=CAEBREN_24136 {ECO:0000313|EMBL:EGT36807.1}; OS Caenorhabditis brenneri (Nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068}; RN [1] {ECO:0000313|Proteomes:UP000008068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068}; RG Caenorhabditis brenneri Sequencing and Analysis Consortium; RA Wilson R.K.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL379938; EGT36807.1; -; Genomic_DNA. DR ProteinModelPortal; G0NSI8; -. DR STRING; 135651.CBN24136; -. DR EnsemblMetazoa; CBN24136; CBN24136; WBGene00162861. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR InParanoid; G0NSI8; -. DR OMA; QIEDARC; -. DR OrthoDB; EOG091G01L9; -. DR Proteomes; UP000008068; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008068}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008068}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 727 749 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 210 410 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 416 503 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 475 495 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 1021 AA; 112335 MW; 196C03B47D410CA6 CRC64; MAKVDIRQTT ANKAFMETMR PDGYEIVHPF QIRDKNERIG IDTRNYFLKA QEHYSHVTIV IRSNQLGRLK LVLERNNFVF LNQTAFHKLD ADGERVIQNR VENCYYQGTV GGEESSFVAL SSCNGLRGVI SFANGTTYGI WPLDGGDRNS RRHPHILYKS EWSQDAKCGS SMAHAVGQRI RREHKHRKHH KKIHDEENQK MRRDASKRTK YVEVALIADY EFMKQRGLHD MDAISYMLES LNIADSMLSR DLNIRLSAVY VELWSDAQRI DLWEDIERTL SGVVDYAAGH IYHIQKDASI LFTAGSFANQ EVSNAAIRSI CTARSAVILR SIEQFATHWN GELLAQSVGH LLGLEHDTAA CSCEPSPECL MRQQPGRVGA PFSWQFSKCS VARMHGIWQD GNIQCLLNKP FQVSELRECG NGIVDGSEEC DCGTRENCND PCCDPLTCTL RPHAQCAAHH KCCHRCELRK AGETCRASKS PCDVAESCDG KSGDCPPDGH LIDGTVCGTD GQCWRGNCSD SHQQCQKLWG RDARVADQVC FDQNTKGAEY ANCGVQADGS YHPCQIEDTK CGTLHCHSGS ITPLDQALKA FTFHFTENSQ QIQCKSIAPS GGVLFGQSQD GTNCGSGKVC VAGSCVEMSS VTSATACPTN NLALLCSGHG HCTTTAKCVC FNGWSGGACD IRSNTSTYQG SMGFSEENRG GQGAQGGRKT IMIPHLNIGT TLETATLFAI LLGFGVFLML CLVCLMLCYR RKSVVEIPKP TDEKLEESPD RQIKFGNMPS YREEKRKRKS NKRIYGALNR ITEADERDST SLRSRDSAGS QQLLDRNGQP AMMGGIRDPY AGEHIYAESS STSQNLATRQ FRGINSDGSY PLRSFGSWRS SGPISPASSS GHLTDVSTAT TPLRLNKIGK LLKTMQSDDE GGSPFSDHPL LRGPTGLDYT SLAGPSYSNP GNGEEELSAV EADHDVGSNT ESSRGCEDGP IDGWDPPSIV NGASSNNYQF RQSPSLFSDP FKLEMTNSMH N // ID G1L370_AILME Unreviewed; 956 AA. AC G1L370; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 23-MAY-2018, entry version 46. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSAMEP00000001330}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSAMEP00000001330}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000001330, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000001330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000001330} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTA01024830; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01032830; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01040829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01048829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01056829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01064829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01072829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01080829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9646.ENSAMEP00000001330; -. DR Ensembl; ENSAMET00000001382; ENSAMEP00000001330; ENSAMEG00000001215. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G1L370; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 787 810 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 289 488 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 494 581 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 725 762 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 553 573 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 752 761 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 956 AA; 105981 MW; 1E7A35F3D490610A CRC64; MRRMGKGCRA SGPRSWMISD ELVQGSPAGV SASFSERDRE GGGSDFHRGD VGPQKAQVWV RVIIFSFSPH SLFTLFLPGG DASLTELERR NENRFLERQS IVPLRLLYRS GGEDETGHDA LDTRVRGHPG GVQLTHVDQA SFQVDAFGTS FILDVVLNHD LLSSEYIERY VEHGKTVEVK GGEHCYYQGH IRGNPASFVA LSTCHGLHGM FYDGNHTYLI EPEENDTSQE DFHFHSVYKS RLSEFPLDDL PSEFQQVHIT PPKFILKPRP KRSKRQLRRH PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWAADNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIHETCSGNS SQCAPNIHKM DGYSCDGIQG ICFGGRCKTR DRQCKYIWGQ KVMASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTVCSG NGVCSNELKC VCNRHWIGAD CSTYFPHNDD AKTGITLAGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNRKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE EKKVNRQSAR LWETSI // ID G1MJ94_AILME Unreviewed; 767 AA. AC G1MJ94; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 23-MAY-2018, entry version 46. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSAMEP00000019429}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSAMEP00000019429}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000019429, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000019429} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000019429} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTA01090248; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9646.ENSAMEP00000019429; -. DR Ensembl; ENSAMET00000020198; ENSAMEP00000019429; ENSAMEG00000018382. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G1MJ94; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 733 756 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 237 436 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 442 529 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 671 708 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 501 521 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 698 707 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 767 AA; 83533 MW; 15C1AEB6DB8D26FE CRC64; KSPAPRWASA CSSGLVSPGL GTRGPFGALR WRISPQLGRP GAPEVTEPSR LVRESSGGEV RKQQLDTRVR QEPPAGPSVH LAQVSFVIPA FNSNFTLDLE LNHHLLSSQY VERHFSREGT TQHNTGAGDH CYYQGKLRGN PHTFAPARGC SEYGGVFSDG NFTYIVEPRE MARPQEPPQG PLPHLIYRTP LLPAPLGCRE PGCLFAAPAH SAPVNRPRLR RKRQVRRGHP TVHSETKYVE LIVVNDHQLF EQMRQSVVLT SNFAKSVVNL ADVMYKEQLN TRIVLVAMET WADGDKIQVQ DDLLETLAQL MVYRREGLPE PSDATHLFSG RTFQSTSSGA AYVGGICSLS RGGGVNEYDN MGAMAVTLAQ TLGQNLGMMW NKHRSSAGDC KCPDNWLGCI MEDTGFYLPR KFSRCSIDEY NQFLQEGGGS CLFNKPLKLL DPPECGNGFV EAGEECDCGS VQECSRAGGN CCKKCTLTHD AMCSDGLCCR RCKYEPRGVS CREAVNECDI AETCTGDSSQ CPPNLHKLDG YYCDHEQGRC YGGRCKTRDR QCQALWGHAA ADRFCYEKLN VEGTERGNCG RKGSGWVQCN KQDVLCGFLL CVNISGAPRL GDLGGDINSI TFYHQGKELD CRGGHVQLAD GSDLSYVEDG TACGPNMLCL DHRCLPASAF NFSTCPGSGE RRICSHHGVC SNEGKCICQP DWTGKDCSIH NPLPTSPPTG ETERYKGPSG TNIIIGSIAG AVLVAAIVLG GTGWGFKNIR RARSGGA // ID G1MND1_AILME Unreviewed; 731 AA. AC G1MND1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 23-MAY-2018, entry version 45. DE SubName: Full=ADAM metallopeptidase domain 20 {ECO:0000313|Ensembl:ENSAMEP00000020880}; GN Name=ADAM20 {ECO:0000313|Ensembl:ENSAMEP00000020880}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000020880, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000020880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000020880} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTA01052844; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9646.ENSAMEP00000020880; -. DR Ensembl; ENSAMET00000021649; ENSAMEP00000020880; ENSAMEG00000019828. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR InParanoid; G1MND1; -. DR OMA; WAPPYCK; -. DR OrthoDB; EOG091G03BZ; -. DR TreeFam; TF314733; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 709 730 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 226 402 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 425 511 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 649 683 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 361 361 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 360 360 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 364 364 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 370 370 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 377 382 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 483 503 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 673 682 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 731 AA; 82700 MW; 8BCADB10C8948400 CRC64; VPHTLPSSAL DRWLHNYSSV MAVNEALVHI RVTLLLLWVG MPLFISGHSQ ARPSQHFSPE LVIPLKVTGR GRGIKGAGWL SYSLQFGGKR HIVHMRVKKL LVSRHFPVFT YTDQHALRQD QPFVPDDCYY HGYVEGIPES LVALSTCSGG FRGMLQINDL AYEIEPMRFS ATFEHLVYKI DSDDTQFPPM RCGLTEEEIA RHLQLRASYN STLMQSSYMG WWTHLRFLEL VVVVDHLRFL YYESNVTVVQ REVFDVVNII DVLYYPLEVD IILTGIEIWS ERNLVATDNM EQLVEDFAIW KFFNLDARLH HDTAHLFIKK YFGIKLGIAF VGGICQRPFN SGVDVFEGDS LYFFALTVSH ELGHNLGMSH DTEQCVCGLQ WCIMYPSQVA TTRFSNCSYA QYWNTSLTSG VCIHSPPHPG NIFRVQYCGN LAVEEGEECD CGTVHQCVND PCCLLNCTLK PGATCTFGIC CKDCKFMPSG TLCRHQINEC DLPEWCNGTF HQCPEDVYLQ DGIPCGDDAY CYEGRCNNHD KQCREIFGKD ARSASQNCYK EINTQGNRFG HCGITDLIYV KCEAPDILCG RVQCENVRVI PNLIQHSTVH QLHFNDTTCW GTDYHLGMSI PDIGQVKDGT VCGPQKICIH KKCVNKTYPP RDCQTDETCH MHGVCNNKEH CHCSRGWEPP YCEHPGYGGS IDSGPPPGKP VILVEPKAML GHLSLLWLIP FTAFVLFCLL V // ID G1P4I3_MYOLU Unreviewed; 835 AA. AC G1P4I3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 23-MAY-2018, entry version 50. DE SubName: Full=ADAM metallopeptidase domain 8 {ECO:0000313|Ensembl:ENSMLUP00000004869}; GN Name=ADAM8 {ECO:0000313|Ensembl:ENSMLUP00000004869}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000004869, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000004869, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000004869} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPE02037766; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59463.ENSMLUP00000004869; -. DR Ensembl; ENSMLUT00000005336; ENSMLUP00000004869; ENSMLUG00000005324. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G1P4I3; -. DR OMA; DENVQGC; -. DR OrthoDB; EOG091G01NX; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0071133; C:alpha9-beta1 integrin-ADAM8 complex; IEA:Ensembl. DR GO; GO:0071065; C:alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0032127; C:dense core granule membrane; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl. DR GO; GO:0032010; C:phagolysosome; IEA:Ensembl. DR GO; GO:0002102; C:podosome; IEA:Ensembl. DR GO; GO:0042581; C:specific granule; IEA:Ensembl. DR GO; GO:0070820; C:tertiary granule; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl. DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl. DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl. DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl. DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEA:Ensembl. DR GO; GO:0048247; P:lymphocyte chemotaxis; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0002675; P:positive regulation of acute inflammatory response; IEA:Ensembl. DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl. DR GO; GO:2000418; P:positive regulation of eosinophil migration; IEA:Ensembl. DR GO; GO:2000415; P:positive regulation of fibronectin-dependent thymocyte migration; IEA:Ensembl. DR GO; GO:0045089; P:positive regulation of innate immune response; IEA:Ensembl. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl. DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl. DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IEA:Ensembl. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl. DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl. DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl. DR GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; IEA:Ensembl. DR GO; GO:2000309; P:positive regulation of tumor necrosis factor (ligand) superfamily member 11 production; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 835 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003416683. FT TRANSMEM 656 680 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 196 396 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 404 490 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 611 643 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 331 331 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 330 330 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 334 334 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 340 340 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 462 482 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 615 625 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 633 642 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 835 AA; 90236 MW; 8C35AC46B312EDE6 CRC64; HLGLWLLSVW WLQVAAPSPT LPHVEQYKVV RPQRLPGPRA RRALPSDVGL YPESVSYVLG APGNTFTLHL RKNRDLVGSG YTETYTAANG SQVTEQLQRQ DHCFYQGHVE GHPLSAASLS TCDGLRGFFQ AGSAVHLIEP LDGSGEEGEH ALYKAQHLQQ KAGTCGVSNT SLENMLGPRT LAAFRPRNRP LSRKTRFVEL YVVTDSREFQ KLGSREAVRR RVLEVVNHVD KLYQELKFRV VLVGLDIWNH ADKIQVSSDA GVTLENFLTW RAQNLVGRHP HDNVQLITGI DFAGATVGLA KVSAMCSQNS GAVNQDHNPN PIGVACTLAH EMGHNLGMDH DENVQGCYCP ESRTRGGCVM AGSIGSTFPT LFSQCSQDDL ETFVEKPRIT CIANAPDPDR LVGGPVCGNG FVEQGEQCDC GYPQDCRDRC CNTTTCQLAE GAECAHGACC HECRVKPAGE LCRPGKDDCD LEEYCDGQRP SCPEDAFQEN GTPCPGGYCY NGACPTRAQR CQDLWGPGTQ TARETCYSFR VLPGCQSSRL GAKRTECESL LCEGGQKPPE RASCTFTYNS AICQALNLDG GSGFEQVLEG TKCGDKRVCW KGQCQDFHVY RSRNCSAQCN GHGVCNHKGK CHCHPGWAPP HCTELLAELR VASGSLLMSV MVPVVTLVTL ALIVLGVFIY RKAGSRIRGR NVAPKTAMGL SNPLFQKSGF GPETGMAPAP TTHSPVPVTP MYANNSGPLP RPTASAVTPT RPPPAPPATM SSPPFPVPMY TQQAPAQLRP APPTKPLPEL KPRQVIKPTS VPPMPPVKPK AGGANPGTTE GVGPKVALKP PVLRR // ID G1PHY5_MYOLU Unreviewed; 728 AA. AC G1PHY5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 23-MAY-2018, entry version 51. DE SubName: Full=ADAM metallopeptidase domain 32 {ECO:0000313|Ensembl:ENSMLUP00000010298}; GN Name=ADAM32 {ECO:0000313|Ensembl:ENSMLUP00000010298}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000010298, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000010298, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000010298} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPE02012487; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02012488; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02012489; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02012490; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59463.ENSMLUP00000010298; -. DR Ensembl; ENSMLUT00000011303; ENSMLUP00000010298; ENSMLUG00000011280. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR InParanoid; G1PHY5; -. DR OMA; PLYLEMH; -. DR OrthoDB; EOG091G02F0; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00276, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 728 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003417103. FT TRANSMEM 690 714 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 189 386 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 393 481 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 628 660 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 342 347 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 632 642 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 650 659 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 728 AA; 81073 MW; 1444897918C39248 CRC64; MFRSVVLLAG LGALLRASPD FQNSSLQIVV PEKIQENTSN NSEVENKQIS YIIPINEKPY TVHLKQRFFL AENFMVYLYK QGSVNSHSSN IQTQCYYEGY VEGYPNSIVI LSTCSGLRRG LLQLENVSYG IEPLEVEVEF QHLLYKLKNE NNVFVVHAEN SRGLEQKPMD YSISISEKSE SAVQDLIPLY LEMHIVVDKV LYDYLGSDSM LATDKVIEII GLVNSVFAQL NVTIVLSSLE LWSDKNKIST VGEADELLQR FLEWKKSYLT LRPHDIAYLF MYRDYPNDVG ATFPGKMCTA QYSAGIALYS EEITLEAFSV IVTQMVGLSL GISYDDPKKC QCSGAICVMN AEAVQSSGVK TFSNCSLSDF KSFILNMGAK CLQNKPQMQV RQKAVCGNGK VETPEVCDCG TEDQCGKDSC CDPKLCVLKA GSACDTGLCC SNCQIQQAGS PCRPSVHPEC DLPELCNGSS SACPTDVMII NGHSCKNKYI CYNGEQLSPL DSSCDGGSLV GNTLTGSKNA PFACYEEIQS QLDRFGNCGK ERGQYKFCQW RNLICGRLIC TYPTLTPYIQ RNVAVLYAYV RNVICITLDY SLHGSNVDPL VVNDGSECDS ERVCINRQCV ESRFLKKDSL NCSAKCSGHG VCTSELKCHC DSGWTGQDCN TQSRGFGTYW VCPFKLIMER DAWKSAKNRW LLGFYITLPV LIIVIITAIT LNYLKKRFSK EEESRSSK // ID G1PN00_MYOLU Unreviewed; 772 AA. AC G1PN00; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 23-MAY-2018, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000012295}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000012295, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000012295, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000012295} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPE02053242; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02053243; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02053244; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02053245; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59463.ENSMLUP00000012295; -. DR Ensembl; ENSMLUT00000013511; ENSMLUP00000012295; ENSMLUG00000013504. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G1PN00; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 738 761 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 251 441 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 447 534 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 676 713 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 506 526 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 703 712 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 772 AA; 83942 MW; 630FB72F2828187A CRC64; PRAMPAWRVG VPNPFPGLPP HGLGTWGPAG VLRWRVAPQL WGPEVPEVTE PSRLVGESSG GEVRKPQLDT RVRQEPPGGP PVHLAQVSFV IPAFNSNFTL DLELNHHLLS SKYVERHFSR EGTTQRSTGA GDHCYYQGRL RGNPHSFAAL STCQGLHGVF SDGNFTYIVE PREMAGPREA PRGPHPHLIY RTPLLPAPIG CREPDCLFAA PAHAAPPDRP RLRRKRQVRG PHRPRAAETS GCGPEQEDTX QLFEQMRQSV VLTSNFAKSV VNLADVMYKE QLNTRIVLVA METWADGDKI QVQDDLLETL ARLMVYRREG LPELSDATHL FSGRTFQSTS SGAAYVGGIC SLSRGGGVNE PKYDNMGAMA VTLAQTLGQN LGMMWNKHRS SAGDCKCPDN WLGCIMEDTG FYLPRKFSRC SIDEYNQFLQ EGGGSCLFNK PLKLLDPPEC GNGFVEAGEE CDCGSVQECS RAGGNCCKKC TLTHDAMCSD GLCCRRCKYE PRGVSCREAV NECDIAETCT GDSSQCPPNL HKLDGYYCDH EQGRCYGGRC KTRDRQCQAL WGHVAADRFC YEKLNVEGTE RGNCGRKGSG WVQCNKQDVL CGFLLCVNVS GAPRLGDLGG DISSVTFYHQ GKELDCRGGH VQLADGSDLS YVEDGTACGP NMLCLDHRCL PASAFNFSTC PGSGERRICS HHGVCSNEGK CICQPDWTGK DCSIHNPLPT SPPTGETEKY KGPSGTNIII GSIAGAVLVA AIVLGGTGWG FKNIRRGRSG GA // ID G1PP18_MYOLU Unreviewed; 794 AA. AC G1PP18; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 23-MAY-2018, entry version 50. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSMLUP00000012725}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSMLUP00000012725}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000012725, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000012725, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000012725} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPE02037859; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02037860; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02037861; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59463.ENSMLUP00000012725; -. DR Ensembl; ENSMLUT00000013985; ENSMLUP00000012725; ENSMLUG00000013971. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G1PP18; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 624 647 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 325 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 331 418 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 562 599 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 390 410 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 589 598 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 794 AA; 88411 MW; 373811B171B911C2 CRC64; MYLQPHSKSN FKRISLKGGE HCYYQGHIRG NPASFVALST CHGLHGMFYD GNHTYLIEPE ENDTSQEDFR FHSVYKSRLF EFPLDDLPSE FQQVNITPPK FILKPRPKRT KRQLHRHPRN VEEETKYIEL MIVNDHLMFK KHRLSVVHTN TYAKSVVNMA DLIYKDQLKT RIVLVAMETW AADNKFAISE NPLITLREFM KYRRDFIKEK SDAVHLFSGS QFESSRSGAA YIGGICSLLK GGGVNEFGKT DLMAVTLAQS LAHNIGIISD KRKLASGECK CEDTWSGCIM GDTGYYLPKK FTQCNVEEYH DFLNSGGGAC LFNKPSKLLD PPECGNGFIE TGEECDCGTP AECVLEGAEC CKKCTLTQDS QCSDGLCCKK CKFQPMGTVC REAVNDCDIR ESCSGNSSQC APNIHKMDGY SCDGVQGICF GGRCKTRDRQ CKYIWGQRVM ASDKYCYEKL NIEGTEKGNC GRDKDTWIQC NKRDVLCGYL LCTNIGNIPR LGELDGEITS TLVVQQGRTL NCSGGHVKLE EDVDLGYVED GTPCGPRMMC LEHRCLPVAS FNFSTCLSNK EGIVCSGNGV CSNELKCVCN RHWTGADCST YFPLNDEEKT GITLSGNGVA GTNIIIGIIA GTILVLALIL GMTAWGYKKR NYREQRQLPQ GDYVKKPGDG DSFYSDIPPG VSTNSASSSK KRSNGLSHSW SERIPDTKHT DICENGRPRS NSWQGNVGGN RKKIRGKRFR PRSNSTETLS PAKSPSSSTG SIASSRKYPY PMPPLPDEEK KVNRQSARVC ENFL // ID G1QZF7_NOMLE Unreviewed; 682 AA. AC G1QZF7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 23-MAY-2018, entry version 47. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSNLEP00000006328}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSNLEP00000006328}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000006328}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000006328} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000006328} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFV01061671; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01061672; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01061673; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 61853.ENSNLEP00000006328; -. DR Ensembl; ENSNLET00000006650; ENSNLEP00000006328; ENSNLEG00000005231. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G1QZF7; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001073; Chromosome 19. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 658 681 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 153 352 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 358 454 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 596 633 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 426 446 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 623 632 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 682 AA; 73910 MW; 4035DBBC8835C623 CRC64; PVHLAQVSFV IPAFNSNLTL DLELNHHLLS SQYVERHFSR EGTTQHSTGA GDHCYYQGKL RGNPHSFAAL STCQGLHGVF SDGNLTYIVE PQEVAGPWGA PQGPLPHLIY RTPLLPDPLG CREPGPILGK PRLPCPPTPQ VRRGHPTVHS ETKYVELIVI NDHQLFEQMR QSVVLTSNFA KSVVNLADVI YKEQLNTRIV LVAMETWADG DKIQVQDDLL ETLARLMVYR REGLPEPSDA THLFSGRTFQ STSSGAAYVG GICSLSRGGG VNEYGNMGAM AVTLAQTLGQ NLGMMWNKHR SSAGDCKCPD IWLGCIMEDT GFYLPRKFSR CSIDEYNQFL QEGGGSCLFN KPLKLLDPPE CGNGFVEAGE ECDCGSVQEC SRAGGNCCKK CTLTHDAMCS DGLLLSPLQG KQDRPGGRYE PRGVSCREAV NECDIAETCT GDSSQCPPNL HKLDGYYCDH EQGRCYGGRC KTRDRQCQAL WGHAAADRFC YEKLNVEGTE RGSCGRKGSG WVQCSKQDVL CGFLLCVNIS GAPRLGDLVG DISSVTFYHQ GKELDCRGGH VQLADGSDLS YVEDGTACGP NMLCLDHRCL PASAFNFSTC PGSGERRICS HHGVCSNEGK CICQPDWTGK DCSIHNPLPT SPPTGETERY KGPSGTNIII GSIAGAVLVA AIVLGGTGWG FK // ID G1RYK9_NOMLE Unreviewed; 906 AA. AC G1RYK9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 47. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSNLEP00000018336}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSNLEP00000018336}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000018336, ECO:0000313|Proteomes:UP000001073}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000018336} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000018336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFV01000680; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01000681; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01000682; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01000683; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01000684; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01000685; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01000686; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01000687; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01000688; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01000689; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003252400.1; XM_003252352.3. DR ProteinModelPortal; G1RYK9; -. DR STRING; 61853.ENSNLEP00000018336; -. DR MEROPS; M12.978; -. DR Ensembl; ENSNLET00000019247; ENSNLEP00000018336; ENSNLEG00000015048. DR GeneID; 100581065; -. DR KEGG; nle:100581065; -. DR CTD; 53616; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G1RYK9; -. DR KO; K16068; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001073; Chromosome 11. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 906 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003421510. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 906 AA; 100504 MW; D504AF55677B2AEB CRC64; MQAVVAVSVS FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFLERQSM VPLRLIYRLG GEDESRHDAL DTRVRGDPGG RQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI EHGGKTVEVK GGEHCYYQGH IRGNPASFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADVIYKDQ LKTRIVLVAM ETWATDNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE DKKVNRQSAR LWETSI // ID G1T9G9_RABIT Unreviewed; 825 AA. AC G1T9G9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSOCUP00000013276}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSOCUP00000013276}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000013276, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000013276, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSOCUP00000013276} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000013276}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAGW02061981; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02061982; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02061983; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02061984; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02061985; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02061986; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02061987; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02061988; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02061989; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02061990; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9986.ENSOCUP00000013276; -. DR Ensembl; ENSOCUT00000015452; ENSOCUP00000013276; ENSOCUG00000015436. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G1T9G9; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001811; Chromosome 10. DR Bgee; ENSOCUG00000015436; -. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 656 679 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 158 357 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 363 450 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 594 631 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 422 442 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 621 630 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 825 AA; 91439 MW; D8994314A49EDB35 CRC64; QLTHVDQASF QVDAFGASFV LDVRLNHDLL SSEYIERYID HGGKTVEVEG GEHCYYQGHV RGNPASFVAL STCHGLHGMF YDGNHTYLIE PEENETSQED FHFHSVYKSR LFEFPLDDLP SEFQQVNISL PEVTLKSRPK ITVLQRLRHP RNVEEETKYI ELMIVNDHLM FKRHRLSVVH TNTYAKSVVN MADLIYKDQL KTRIVLVAME TWAADNKFAI SENPLITLRE FMKYRRDFIK EKSDAVHLFS GSQFESSRSG AAYIGGICSL LKGGGVNEYG KTDLMAVTLA QSLAHNIGII SDKRKLASGE CKCEDTWLGC IMGDTGYYLP KKFTQCNIEE YHDFLNSGGG ACLFNKPSKL LDPPECGNGF IETGEECDCG TPAECVLEGA ECCKKCTLTQ DSQCSDGLCC KKCKFQPMGT VCREAVNDCD IRETCSGNSS QCAPNIHKMD GYPCDGVQGI CFGGRCKTRD RQCKYIWGQK VKASDKYCYE KLNIEGTEKG NCGKDKDTWI QCNKRDVLCG YLLCTNVGNI PRLGELDGEI TSAVVVQQGR TLNCSGGHVK LEEDVDLGYV EDGTPCGPQM MCLEHRCLPV ASFNFSTCLS SKEGTVCSGN GVCSNELKCV CNRHWTGADC NTYFPHNDDT KAGITLSGNG VAGTNIIIGI IAGTILVLAL ILGITAWGYK NYREQRQLPQ GDYVKKPGDG DSFYSDIPPG VSTNSASSSK KRSNGLSHSW SERIPDTKHI SDICENGRPR SNSWQGNLGG NRKKIRGKRF RPRSNSTETL SPAKSPSSST GSIASSRKYP YPMPPLPDEE KKVNRQSARL WETSI // ID G1U0Z2_RABIT Unreviewed; 774 AA. AC G1U0Z2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSOCUP00000023025}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSOCUP00000023025}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000023025, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000023025, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSOCUP00000023025} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000023025}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAGW02039834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02039835; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02039836; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9986.ENSOCUP00000023025; -. DR Ensembl; ENSOCUT00000028206; ENSOCUP00000023025; ENSOCUG00000000736. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G1U0Z2; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001811; Chromosome 19. DR Bgee; ENSOCUG00000000736; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 740 763 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 244 443 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 449 536 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 678 715 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 508 528 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 705 714 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 774 AA; 83918 MW; EB5CD5192075663C CRC64; SRTLRRLSAE SLRPSPLHVR FSPRPGLGVR GPAGALRWGV SPQVGGPEAP EVTEPSRLVG QSSGGEIRKQ QLDTRVRQEP PGGPPVHLAQ VSFVIPAFNS NFTLDLELNH HLLSSQYVER HFSREGTAQR STGAGDHCYY QGKLRGNPHS FAALSTCQGL HGVFSDGNLT YIVEPQEMAG PWGASQGPLP HLIYRTPLLP APLGCRGPGC LFAAPVHSAP PNRPRLRRKR QVRRGHPTVH SETKYVELIV INDHQLFEQM RQSVVLTSNF AKSVVNLADV MYKEQLNTRI VLVAMETWAD GDKIQVQDDL LETLARLMVY RREGLPEPSD ATHLFSGRTF HSTSSGAAYV GGICSLSRGG GVNEYGNMGA MAVTLAQTLG QNLGMMWNKH RSSAGDCKCP DIWLGCIMED TGFYLPRKFS RCSIDEYNQF LQEGGGSCLF NKPLKLLDPP ECGNGFVEAG EECDCGSVQE CSRAGGNCCK KCTLTHDAMC SDGLCCRRCK YEPRGVSCRE AENECDIAET CTGDSSQCPP NLHKLDGHFC DHEQGRCYGG RCKTRDRQCQ ALWGHAAADR FCYEKLNVEG TERGNCGRKG SGWVQCNKQD VLCGFLLCVN ISGAPRLGDL GGDISSVTFY HQGKELDCRG GHVQLADGSD LSYVEDGTAC GPNMLCLDHR CLPASAFNFS TCPGSGDRRI CSHHGVCSNE GKCICQPDWT GKDCSIHNPL PTSPPTGETE RYKGPSGTNI IIGSIAGAVL VAAIVLGGTG WGFKNIRRGR SGGA // ID G3HLL0_CRIGR Unreviewed; 707 AA. AC G3HLL0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 41. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11 {ECO:0000313|EMBL:EGW08189.1}; GN ORFNames=I79_011600 {ECO:0000313|EMBL:EGW08189.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW08189.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH000492; EGW08189.1; -; Genomic_DNA. DR ProteinModelPortal; G3HLL0; -. DR MEROPS; M12.976; -. DR PRIDE; G3HLL0; -. DR InParanoid; G3HLL0; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:EGW08189.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 683 706 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 187 386 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 392 479 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 621 658 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 451 471 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 648 657 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 707 AA; 76651 MW; 0696497EBBEDC653 CRC64; MPTCSFTSQS GLGALGPSGA LHWRSSAQVG IPESPEGPEV TEPSRLVRES SGGEVRKHQV DTRVRQDPPR GTPVHLAQVS FVIPAFNTNF TLDLELNHHL LSSQYVERHF SREGTTQHST GAGDHCYYHG RLRGNPHSLA ALSTCQGLHG VFSDGNLTYI IEPKEMAGPW GPPQVRRGHP TVHSETKYVE LIVINDHQLF EQMRQSVVLT SNFAKSVVNL ADVIYKEQLN TRIVLVAMET WADGDKIQVQ DDLLETLARL MVYRREGLPE PSDATHLFSG RTFQSTSSGA AYVGGICSLS RGGGVNEYGN MGAMAVTLAQ TLGQNLGMMW NKHRSSAGDC KCPDIWLGCI MEDTGFYLPR KFSRCSIDEY NQFLQEGGGS CLFNKPLKLL DPPECGNGFV EAGEECDCGS VQECSRAGGN CCKKCTLTHD AMCSDGLCCR RCKYEPRGVS CREAVNECDI AETCTGDSSQ CPPNLHKLDG YYCDHEQGRC YGGRCKTRDR QCQALWGHGA ADRFCYEKLN VEGTERGNCG RKGSGWVQCN KQDVLCGFLL CVNISGAPRL GDLGGDISSV TFYHQGKELD CRGGHVQLAD GSDLSYVEDG TACGPNMLCL GHRCLPASAF NFSTCPGSGE RRICSHHGVC SNEGKCICQP DWTGKDCSIH NPLPTSPPTG ETERYKGPSG TNIIIGSIAG AVLVAAIVLG GTGWGFK // ID G3HRX4_CRIGR Unreviewed; 744 AA. AC G3HRX4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 {ECO:0000313|EMBL:EGW07202.1}; GN ORFNames=I79_013598 {ECO:0000313|EMBL:EGW07202.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW07202.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH000645; EGW07202.1; -; Genomic_DNA. DR ProteinModelPortal; G3HRX4; -. DR PRIDE; G3HRX4; -. DR InParanoid; G3HRX4; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005840; C:ribosome; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.30.1740.20; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR InterPro; IPR000892; Ribosomal_S26e. DR InterPro; IPR038551; Ribosomal_S26e_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR Pfam; PF01283; Ribosomal_S26e; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:EGW07202.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 583 606 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 324 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 330 417 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 521 558 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 389 409 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 548 557 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 744 AA; 82058 MW; 068D77EDE4406E9C CRC64; MHCMNCAQCV PKDKAIKKFI IQNLVEAAAV KDIPKASVSN AYVLPNFCVK LCYCVSCAIQ SKGGEHCYYQ GQIRGNPASF VALSTCHGLH GMFYDGNHTY LIEPEENETS QLLRLPRNVE EETKYIELMI VNDHIMFKKH RLSVVHTNTY AKSVVNMADM IYKDQLKTRI VLVAMETWAA DNKFAISENP LITLREFMKY RRDFIKEKSD AVHLFSGSQF ESSRSGAAYI GGICSLLRGG GVNEVGVNIC AIQSAKAASV QLRSVCNRLC LGFPLGECKC EDTWSGCVMG DTGYYLPKKF TQCNIEEYHD FLNSGGGACL FNKPSKLLDP PECGNGFIET GEECDCGTTA ECALEGAECC KKCTLTQDSQ CSDGLCCKKC KFQPLGTVCR EAVNDCDIRE ICSGNSSQCA PNVHKMDGYS CDGTQGICFG GRCKTRDRQC KYIWGQKVTA SDKYCYEKLN IEGTEKGNCG KDKDTWIQCN KRGGHVKLEE DVDLGYVEDG TPCGPQMMCL EHRCLSVASF NFSTCLNSKA GTVCSGNGVC SNELKCVCNR HWTGADCSIH SPHNDDAKAG ITLSGNGVAG TNIIIGIIAG TILVLALILG ITAWGYKNYR EQRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE EKTVNRQSAR VHSNSHMLYT WSQLVISKLT FHLYPPLLKQ NFIV // ID G3NSU5_GASAC Unreviewed; 737 AA. AC G3NSU5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000008413}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000008413, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000008413} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000008413} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3NSU5; -. DR STRING; 69293.ENSGACP00000008413; -. DR Ensembl; ENSGACT00000008432; ENSGACP00000008413; ENSGACG00000006346. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G3NSU5; -. DR OMA; ICSHHGV; -. DR TreeFam; TF314733; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 700 723 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 200 399 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 405 492 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 636 675 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 464 484 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 665 674 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 737 AA; 81026 MW; 8C32ED3E0E7031C5 CRC64; PPAEELVQPK RLLLRRIHSE EELLHGRLDT RVKNYTAEAQ PVHVAHSSFL VEAFGKSFVL DLELNHNLLS RDYVERHYDE NGQLSQNKGG EHCYYHGRVR GRPGSWAALS TCHGLRGMFS DGNVSYGIEP VGSGQDHNDH VVYRVPDVDL FPTPCPVNPC CPPPSTWQVP AAGLKLIFPG KFSPKKKVRR GQRTVQTETK YIELMVVNDH ELFVQLRRSA TQTKNFAKAV VNMADAIYKE QLNTRIVLVA METWSSENKV SVGEDALLTL RDFMKYRKES IKERCDAVHL FSGRTFMSSR SEAAYIGGIC SVSRGGGINE FGSVGPMAIT LSQSLGQNIG MLRNKERLAA GDCRCPDPWL GCIMEDTGYY LPRKFSRCSI DEYLRFLQVG GGSCLFNKPS KLLDPPECGN GFVEPGEECD CGSLVECARN GANCCKKCTL THNAMCSNGL CCRDCRYELR GVTCREAVND CDIPEACMGD SSQCPHNVHK LDGYTCEAGQ GRCYGGRCKT RDGQCRTLWG YNSADRFCYE KLNSEGTEKG NCGPDSSGQG WVQCNKQDVL CGLLLCTNLT ERPRFGELQG KVTSLTIHHQ NRYLDCRGGH AVLDDGLDMG YVEDGAPCGP NMMCSERRCL PVTTFNLSTC PGSSASASRI CSHHGTCSNE VKCICDPDYT GKDCSVFDPI LVPTPADGPE KYKGPSGTNI IIGSVAGAIL VAAIVLGGTG WGFKNIRRGR YDPAFQS // ID G3QI27_GORGO Unreviewed; 906 AA. AC G3QI27; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 23-MAY-2018, entry version 46. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSGGOP00000002025}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSGGOP00000002025}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000002025, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000002025, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000002025} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CABD030053697; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030053698; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030053699; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030053700; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030053701; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030053702; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030053703; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030053704; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_018886770.1; XM_019031225.1. DR STRING; 9593.ENSGGOP00000002025; -. DR Ensembl; ENSGGOT00000002068; ENSGGOP00000002025; ENSGGOG00000002042. DR GeneID; 101143378; -. DR CTD; 53616; -. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G3QI27; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001519; Chromosome 7. DR Bgee; ENSGGOG00000002042; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 906 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014147953. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 906 AA; 100500 MW; C9411BCE4D3BB49B CRC64; MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFLERQSI VPLRLIYRSG GEDESRHDAL DTRVRGDPGG RQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE DKKVNRQSAR LWETSI // ID G3T3H8_LOXAF Unreviewed; 982 AA. AC G3T3H8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 44. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSLAFP00000007810}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSLAFP00000007810}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000007810}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000007810} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007810}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000007810} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007810}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 9785.ENSLAFP00000007810; -. DR Ensembl; ENSLAFT00000009319; ENSLAFP00000007810; ENSLAFG00000009316. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G3T3H8; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 982 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003454665. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 982 AA; 108469 MW; DF644F394D36ADF4 CRC64; MQAAAAASVP FLLLCALGTC PPARCARQGD ASLTELGRRN DNRFLERQSI VPLRLIYRSS AEDETRQDVL DTRVRGDPGG QQLTHVDQAA FQVDAFGTSF ILDVVLNHDL LSSNYVERHT EHGGKTVEVK GGEHCYYQGR IRGNPASFVA LSTCHGLHGM FHDGNHTYLI EPEENDTSEE DFQFHSVYKS RLFEFPLDDL PSEFQQVNFT SPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWAADNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYPCDGVEG ICFGGRCKTR NRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGT IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPK MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGAD CNTYFPHNVD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIAP GVSTNSASSS KKRSAFLSHF QISTCSITHY SISQNISLFC SRSNGLSHSW SERIPDTKHI SDICENGRPR SNSWQGNLGG NRKKIRGKRF RPRSNSTERE PQAPEPGHSL AQTVPSQGIS PGGSDSPQTG SLDHSSQDGQ RQEDRTLSPA KSPSSSTGSI ASSRKYPYPM PPLPDEEKKV NRQSARLWET SI // ID G3T7B7_LOXAF Unreviewed; 771 AA. AC G3T7B7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 44. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSLAFP00000009484}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSLAFP00000009484}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000009484, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000009484} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000009484}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000009484} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000009484}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSLAFT00000011349; ENSLAFP00000009484; ENSLAFG00000011340. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 771 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003455048. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 241 440 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 446 533 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 675 712 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 505 525 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 702 711 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 771 AA; 83935 MW; 4A87566AD5EDB4ED CRC64; MRRLRGWAFA ALLLLLPLLP PPSLEARGPA GALRWGSSPQ VGDQEAPEVM EPSRLVGESS GGEVRKQQLD TRVRQEPPGG PPVHLAQVSF VIPAFNSNFT LDLELNHHLL SSQYVERHFS REGTTQHSTG AGDHCYYQGK LRGNPHSFAA LATCQGLHGV FSDGNFTYIV EPREMAGPRE ARQGPFPHLI YRTPLLPAPL GCREPGCLFA APAHVAPLNQ QKLRRKRQVR RGHPTVHSET KYVELIVIND HQLFEQMRQS VVLTSNFAKS VVNLADVIYK EQLNTRIVLV AMETWADGDK IQVQDDLLET LARLMVYRRE GLPEPSDATH LFSGKTFQST SSGAAYMGGI CSMARGGGVN EFGNVGAMAV TLAQTLGQNL GMMWNKHRSS AGDCKCPDIW LGCIMEDTGF YLPRKFSRCS IDEYNQFLQE GGGSCLFNKP LKLLDPPECG NGFVEAGEEC DCGSLQECSR TGGNCCKKCT LTHDAMCSDG LCCRRCKYEP RGVSCREAVN ECDIAETCTG DSSQCPPNLH KLDGYYCDHE QGRCYGGRCK TRDRQCQALW GHAAADRFCY EKLNVEGTER GNCGRKGSGW VQCNKQDVLC GFLLCVNISG VPRLGDLGGD ISSVTFYHQG KELDCRGGHV QLADGSDLSY VEDGTACGPN MLCLDHRCLP ASAFNFSTCP GSGERQICSH HGVCSNEGKC ICQPDWTGKD CSIHNPLPTS PPTGETERYK GPSGTNIIIG SIAGAVLVAA IVLGGTGWGF KNIRRGRSGG A // ID G3TS75_LOXAF Unreviewed; 776 AA. AC G3TS75; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 46. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSLAFP00000018433}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSLAFP00000018433}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000018433, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000018433} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018433}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000018433} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018433}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3TS75; -. DR STRING; 9785.ENSLAFP00000018433; -. DR Ensembl; ENSLAFT00000029876; ENSLAFP00000018433; ENSLAFG00000011340. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; G3TS75; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 776 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003455665. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 241 440 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 446 533 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 675 712 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 505 525 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 702 711 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 776 AA; 84623 MW; 812720658E16E844 CRC64; MRRLRGWAFA ALLLLLPLLP PPSLEARGPA GALRWGSSPQ VGDQEAPEVM EPSRLVGESS GGEVRKQQLD TRVRQEPPGG PPVHLAQVSF VIPAFNSNFT LDLELNHHLL SSQYVERHFS REGTTQHSTG AGDHCYYQGK LRGNPHSFAA LATCQGLHGV FSDGNFTYIV EPREMAGPRE ARQGPFPHLI YRTPLLPAPL GCREPGCLFA APAHVAPLNQ QKLRRKRQVR RGHPTVHSET KYVELIVIND HQLFEQMRQS VVLTSNFAKS VVNLADVIYK EQLNTRIVLV AMETWADGDK IQVQDDLLET LARLMVYRRE GLPEPSDATH LFSGKTFQST SSGAAYMGGI CSMARGGGVN EFGNVGAMAV TLAQTLGQNL GMMWNKHRSS AGDCKCPDIW LGCIMEDTGF YLPRKFSRCS IDEYNQFLQE GGGSCLFNKP LKLLDPPECG NGFVEAGEEC DCGSLQECSR TGGNCCKKCT LTHDAMCSDG LCCRRCKYEP RGVSCREAVN ECDIAETCTG DSSQCPPNLH KLDGYYCDHE QGRCYGGRCK TRDRQCQALW GHAAADRFCY EKLNVEGTER GNCGRKGSGW VQCNKQDVLC GFLLCVNISG VPRLGDLGGD ISSVTFYHQG KELDCRGGHV QLADGSDLSY VEDGTACGPN MLCLDHRCLP ASAFNFSTCP GSGERQICSH HGVCSNEGKC ICQPDWTGKD CSIHNPLPTS PPTGETERYK GPSGTNIIIG SIAGAVLVAA IVLGGTGWGF KNIRRGRYDP TQQGAV // ID G3TVJ5_LOXAF Unreviewed; 847 AA. AC G3TVJ5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 43. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSLAFP00000019603}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSLAFP00000019603}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000019603}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000019603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019603}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000019603} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019603}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSLAFT00000031116; ENSLAFP00000019603; ENSLAFG00000009316. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 608 631 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 110 309 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 315 402 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 374 394 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 847 AA; 93477 MW; 79B0455D57E372C6 CRC64; QGGEHCYYQG RIRGNPASFV ALSTCHGLHG MFHDGNHTYL IEPEENDTSE EDFQFHSVYK SRLFEFPLDD LPSEFQQVNF TSPKFILKPR PKRSKRQLRR YPRNVEEETK YIELMIVNDH LMFKKHRLSV VHTNTYAKSV VNMADLIYKD QLKTRIVLVA METWAADNKF AISENPLITL REFMKYRRDF IKEKSDAVHL FSGSQFESSR SGAAYIGGIC SLLKGGGVNE FGKTDLMAVT LAQSLAHNIG IISDKRKLAS GECKCEDTWS GCIMGDTGYY LPKKFTQCNI EEYHDFLNSG GGACLFNKPS KLLDPPECGN GFIETGEECD CGTPAECVLE GAECCKKCTL TQDSQCSDGL CCKKCKFQPM GTVCREAVND CDIRETCSGN SSQCAPNIHK MDGYPCDGVE GICFGGRCKT RNRQCKYIWG QKVTASDKYC YEKLNIEGTE KGNCGKDKDT WIQCNKRDVL CGYLLCTNIG TIPRLGELDG EITSTLVVQQ GRTLNCSGGH VKLEEDVDLG YVEDGTPCGP KMMCLEHRCL PVASFNFSTC LSSKEGTICS GNGVCSNELK CVCNRHWIGA DCNTYFPHNV DAKTGITLSG NGVAGTNIII GIIAGTILVL ALILGITAWG YKQLPQGDYV KKPGDGDSFY SDIAPGVSTN SASSSKKRSA FLSHFQISTC SITHYSISQN ISLFCSRSNG LSHSWSERIP DTKHISDICE NGRPRSNSWQ GNLGGNRKKI RGKRFRPRSN STEREPQAPE PGHSLAQTVP SQGISPGGSD SPQTGSLDHS SQDGQRQEDR TLSPAKSPSS STGSIASSRK YPYPMPPLPD EEKKVNRQSA RLWETSI // ID G3U641_LOXAF Unreviewed; 779 AA. AC G3U641; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 39. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSLAFP00000023299}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSLAFP00000023299}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000023299}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000023299} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023299}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000023299} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023299}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSLAFT00000027277; ENSLAFP00000023299; ENSLAFG00000009316. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 608 631 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 110 309 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 315 402 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 374 394 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 779 AA; 86455 MW; 6C93A6EAC9C05531 CRC64; QGGEHCYYQG RIRGNPASFV ALSTCHGLHG MFHDGNHTYL IEPEENDTSE EDFQFHSVYK SRLFEFPLDD LPSEFQQVNF TSPKFILKPR PKRSKRQLRR YPRNVEEETK YIELMIVNDH LMFKKHRLSV VHTNTYAKSV VNMADLIYKD QLKTRIVLVA METWAADNKF AISENPLITL REFMKYRRDF IKEKSDAVHL FSGSQFESSR SGAAYIGGIC SLLKGGGVNE FGKTDLMAVT LAQSLAHNIG IISDKRKLAS GECKCEDTWS GCIMGDTGYY LPKKFTQCNI EEYHDFLNSG GGACLFNKPS KLLDPPECGN GFIETGEECD CGTPAECVLE GAECCKKCTL TQDSQCSDGL CCKKCKFQPM GTVCREAVND CDIRETCSGN SSQCAPNIHK MDGYPCDGVE GICFGGRCKT RNRQCKYIWG QKVTASDKYC YEKLNIEGTE KGNCGKDKDT WIQCNKRDVL CGYLLCTNIG TIPRLGELDG EITSTLVVQQ GRTLNCSGGH VKLEEDVDLG YVEDGTPCGP KMMCLEHRCL PVASFNFSTC LSSKEGTICS GNGVCSNELK CVCNRHWIGA DCNTYFPHNV DAKTGITLSG NGVAGTNIII GIIAGTILVL ALILGITAWG YKKRNYREQR QLPQGDYVKK PGDGDSFYSD IAPGVSTNSA SSSKKRSNGL SHSWSERIPD TKHISDICEN GRPRSNSWQG NLGGNRKKIR GKRFRPRSNS TETLSPAKSP SSSTGSIASS RKYPYPMPPL PDEEKKVNRQ SARLWETSI // ID G5C4X7_HETGA Unreviewed; 913 AA. AC G5C4X7; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 22-NOV-2017, entry version 29. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 {ECO:0000313|EMBL:EHB16588.1}; GN ORFNames=GW7_15205 {ECO:0000313|EMBL:EHB16588.1}; OS Heterocephalus glaber (Naked mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Heterocephalus. OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB16588.1, ECO:0000313|Proteomes:UP000006813}; RN [1] {ECO:0000313|EMBL:EHB16588.1, ECO:0000313|Proteomes:UP000006813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993625; DOI=10.1038/nature10533; RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L., RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X., RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A., RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., RA Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L., RA Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.; RT "Genome sequencing reveals insights into physiology and longevity of RT the naked mole rat."; RL Nature 479:223-227(2011). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH173394; EHB16588.1; -; Genomic_DNA. DR ProteinModelPortal; G5C4X7; -. DR MEROPS; M12.978; -. DR InParanoid; G5C4X7; -. DR Proteomes; UP000006813; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006813}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Integrin {ECO:0000313|EMBL:EHB16588.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000006813}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 913 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003475150. FT TRANSMEM 736 759 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 238 437 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 443 530 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 502 522 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 913 AA; 100967 MW; 1C389FFE971B3826 CRC64; MRAAAASLPF VLLCALGTCP WVRCGPAGDA SLTKLQRGNE NRFPERQSIV PLRLIYRSGG DDETRHDELN TRVRGDPGGL QSTHVAQASF QVNAFGTSFI LDVMLNHDLL SSGYIERHIE RGGKIVEVKG GEHCYYQGQI RGNPASFVAL STCHGLHGMF YDGNHTYLIE PKENETSPEN FHFHSVYKSR VFEFPLDDLP SEFQQVNISL PKFISKPGLK RSKRQLLRYP RNVEEETKYI ELMIVNDHLM FKKHRLSVVH TNTYAKSVVN MADLIYKDQL KTRIVLVAME TWAADNKFAI SENPLITLRE FMKYRRDFIK EKSDAVHLFS GSQFESSRSG AAYIGGICSL LKGGGVNEFG KTDLMAVTLA QSLAHNIGII SDKRKLASGE CKCEDMWSGC IMGDTGYYLP KKFTQCNIEE YHDFLNSGGG ACLFNKPSKL LDPPECGNGF IETGEECDCG TSTECVLEGA ECCKKCTLTQ DSQCSDGLCC KKCKFQPMGM VCREAVNDCD IRETCSGNSS QCAPNVHKMD GYQCDGAQGI CFGGRCKTRD RQCKYIWGQK VMASDRYCYE KLNIEGTEKG NCGKDKDTWI QCNKRDVLCG YLLCTNIGNI PRLGELDGEI TSTLVVQQGK TLNCSGGHVK LEEDIDLGYV EDGTPCGPKM MCLEHRCLSM ASFNFSTCLS NKEGTVCSGN GFCSNELTCV CNRHWTGADC SIYFPYDEDA KTGITLSGNG VAGTNIIIGI IAGTILVLAL ILGITAWGYK QLPQGDYVKK PGDGDSFYSD IPPGVSTNSA SSSKKRSNGL SHSWSERIPD TKHISDICEN GRPRSNSWQG NLGGTRKKIR GKRFRPRSNS TETLSPAKSP SSSTGSIASS RKYPYPMPPL PDEEKKVNRQ SARVRGDIFS TYTYSCHSHF ICE // ID UNC71_CAEEL Reviewed; 1042 AA. AC G5EFD5; DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot. DT 14-DEC-2011, sequence version 1. DT 25-APR-2018, entry version 65. DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein unc-71 {ECO:0000305}; DE AltName: Full=Uncoordinated protein 71 {ECO:0000312|WormBase:Y37D8A.13}; DE Flags: Precursor; GN Name=unc-71 {ECO:0000312|WormBase:Y37D8A.13}; GN Synonyms=adm-1 {ECO:0000312|WormBase:Y37D8A.13}; GN ORFNames=Y37D8A.13 {ECO:0000312|WormBase:Y37D8A.13}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940}; RN [1] {ECO:0000312|EMBL:AAC47444.1} RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL RP STAGE. RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC47444.1}; RX PubMed=8970152; RA Podbilewicz B.; RT "ADM-1, a protein with metalloprotease- and disintegrin-like domains, RT is expressed in syncytial organs, sperm, and sheath cells of sensory RT organs in Caenorhabditis elegans."; RL Mol. Biol. Cell 7:1877-1893(1996). RN [2] {ECO:0000312|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940}; RX 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] {ECO:0000305} RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=9073451; DOI=10.1006/dbio.1996.8473; RA Chen E.B., Branda C.S., Stern M.J.; RT "Genetic enhancers of sem-5 define components of the gonad-independent RT guidance mechanism controlling sex myoblast migration in RT Caenorhabditis elegans hermaphrodites."; RL Dev. Biol. 182:88-100(1997). RN [4] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION RP PHENOTYPE, AND MUTAGENESIS OF GLY-149; ASP-461; LEU-471; CYS-477; RP ASP-504; CYS-509; ALA-557; GLY-594; SER-628; CYS-687; PRO-902 AND RP ARG-990. RX PubMed=12783787; RA Huang X., Huang P., Robinson M.K., Stern M.J., Jin Y.; RT "UNC-71, a disintegrin and metalloprotease (ADAM) protein, regulates RT motor axon guidance and sex myoblast migration in C. elegans."; RL Development 130:3147-3161(2003). RN [5] {ECO:0000305} RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=22293500; DOI=10.1016/j.febslet.2012.01.031; RA Masuda H., Nakamura K., Takata N., Itoh B., Hirose T., Moribe H., RA Mekada E., Okada M.; RT "MIG-13 controls anteroposterior cell migration by interacting with RT UNC-71/ADM-1 and SRC-1 in Caenorhabditis elegans."; RL FEBS Lett. 586:740-746(2012). CC -!- FUNCTION: Involved in the migration of sex myoblasts (progenitors CC of egg-laying muscles), Q neuroblasts and BDU interneurons during CC development (PubMed:9073451, PubMed:12783787, PubMed:22293500). CC Involved in axon branching and guidance of neurons including CC GABAergic type D motor neurons (PubMed:12783787). Promotes sex CC myoblast migration and positioning independently of gonad CC attraction cues (PubMed:9073451, PubMed:12783787). May act CC downstream of mig-13 in order to promote the guidance, migration CC and positioning of Q neuroblasts and their descendants along the CC anteroposterior body axis (PubMed:22293500). Required for CC coordinated movements (PubMed:12783787). CC {ECO:0000269|PubMed:12783787, ECO:0000269|PubMed:22293500, CC ECO:0000269|PubMed:9073451}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12783787, CC ECO:0000305|PubMed:8970152}; Single-pass type I membrane protein CC {ECO:0000255}. CC -!- DEVELOPMENTAL STAGE: Expressed throughout development CC (PubMed:8970152, PubMed:12783787, PubMed:22293500). First CC expressed in several posterior cells of comma stage embryos CC (PubMed:12783787). Expressed in the excretory cell and in some CC head neurons in threefold stage embryos (PubMed:12783787). At the CC L1 stage of larval development expressed in the syncytial CC hypodermis (PubMed:8970152). From the L1 stage of larval CC development to adulthood, expressed in head neurons, the excretory CC cell, excretory gland cells and in the sphincter muscle CC (PubMed:12783787, PubMed:22293500). From the L4 stage of larval CC development to adulthood, expressed in hypodermal cells CC surrounding the vulva (PubMed:12783787). CC {ECO:0000269|PubMed:12783787, ECO:0000269|PubMed:22293500, CC ECO:0000269|PubMed:8970152}. CC -!- DISRUPTION PHENOTYPE: Defective sex myoblast migration CC (PubMed:9073451). Motor neuron axon guidance defects with aberrant CC axon branching in type D motor neurons (PubMed:12783787). CC {ECO:0000269|PubMed:12783787, ECO:0000269|PubMed:9073451}. CC -!- CAUTION: Contains a metallopeptidase domain, but the active site CC is not conserved, so the protein is not expected to have protease CC activity. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U68185; AAC47444.1; -; mRNA. DR EMBL; BX284603; CAA21545.1; -; Genomic_DNA. DR PIR; T26644; T26644. DR RefSeq; NP_499680.1; NM_067279.6. DR UniGene; Cel.7111; -. DR STRING; 6239.Y37D8A.13; -. DR EPD; G5EFD5; -. DR PaxDb; G5EFD5; -. DR PeptideAtlas; G5EFD5; -. DR EnsemblMetazoa; Y37D8A.13; Y37D8A.13; WBGene00006804. DR GeneID; 176706; -. DR KEGG; cel:CELE_Y37D8A.13; -. DR CTD; 176706; -. DR WormBase; Y37D8A.13; CE20217; WBGene00006804; unc-71. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR OMA; PKKHFHR; -. DR OrthoDB; EOG091G01L9; -. DR PRO; PR:G5EFD5; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00006804; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IDA:WormBase. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008237; F:metallopeptidase activity; ISS:WormBase. DR GO; GO:0098609; P:cell-cell adhesion; TAS:WormBase. DR GO; GO:0045026; P:plasma membrane fusion; TAS:WormBase. DR GO; GO:0006508; P:proteolysis; ISS:WormBase. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; EGF-like domain; KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 1042 Disintegrin and metalloproteinase domain- FT containing protein unc-71. {ECO:0000305}. FT /FTId=PRO_5008958430. FT TOPO_DOM 24 746 Extracellular. {ECO:0000305}. FT TRANSMEM 747 767 Helical. {ECO:0000255}. FT TOPO_DOM 768 1042 Cytoplasmic. {ECO:0000305}. FT DOMAIN 227 431 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 437 524 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT DOMAIN 662 699 EGF-like. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT COMPBIAS 205 216 His-rich. {ECO:0000255|PROSITE- FT ProRule:PRU00009}. FT CARBOHYD 103 103 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 155 155 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 538 538 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 703 703 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT DISULFID 338 426 {ECO:0000255|PROSITE-ProRule:PRU00276}. FT DISULFID 378 410 {ECO:0000255|PROSITE-ProRule:PRU00276}. FT DISULFID 380 386 {ECO:0000255|PROSITE-ProRule:PRU00276}. FT DISULFID 496 516 {ECO:0000255|PROSITE-ProRule:PRU00068}. FT DISULFID 666 681 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 675 687 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 689 698 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT MUTAGEN 149 149 G->R: In ju161; axon guidance defects. FT {ECO:0000269|PubMed:12783787}. FT MUTAGEN 461 461 D->N: In ay64; sex myoblast migration FT defects. {ECO:0000269|PubMed:12783787}. FT MUTAGEN 471 471 L->P: In ay46; sex myoblast migration FT defects. {ECO:0000269|PubMed:12783787}. FT MUTAGEN 477 477 C->Y: In ay17; sex myoblast migration FT defects. {ECO:0000269|PubMed:12783787}. FT MUTAGEN 504 504 D->N: In ju160; axon guidance defects. FT {ECO:0000269|PubMed:12783787}. FT MUTAGEN 509 509 C->Y: In ju159; axon guidance defects. FT {ECO:0000269|PubMed:12783787}. FT MUTAGEN 557 557 A->T: In e541; uncoordinated movement. FT {ECO:0000269|PubMed:12783787}. FT MUTAGEN 594 594 G->E: In ju157; axon guidance defects. FT {ECO:0000269|PubMed:12783787}. FT MUTAGEN 628 628 S->L: In ay47; sex myoblast migration FT defects. {ECO:0000269|PubMed:12783787}. FT MUTAGEN 687 687 C->S: In ay44; sex myoblast migration FT defects. {ECO:0000269|PubMed:12783787}. FT MUTAGEN 902 902 P->L: In ay48; sex myoblast migration FT defects. {ECO:0000269|PubMed:12783787}. FT MUTAGEN 990 990 R->K: In ju255; axon guidance defects. FT {ECO:0000269|PubMed:12783787}. SQ SEQUENCE 1042 AA; 114196 MW; BA6A33593927D4C4 CRC64; MICASKITML GLLVMCTLGG VLGKVDIRQT TANKAFMETM RADGYEVVHP FQIRDKNERI GIDTRNYFLK AQEHYSHVTI VIRSNQLGRL KLVLERNNFI FLNQTAFHKL DADGERVIQN RVENCYYQGT VGGEESSFVA LSSCNGLRGV ISFANGTTFG IWPLDGGDRN SRRHPHILYK SEWSQEAKCG SSMAHAVGQR RMKKHVHKHR SHHHEHNKKR DVSKRTKYVE VALIADYEFM KARGLHDLDA ISYMLESLNI ADSMLSRDLN IRLSAVYVEL WTDVQRIDLW EDIERTLSGV VDYASGHIYH IQKDASILFT AGSFANQEVS NAAIRSICTA RSAVIVKGVE QFATHWNGEL LAQSIGHLLG LEHDTTACSC EPSPECVMRQ QPGRVGGGGG SPFSWQFSKC SVARMHGIWQ DGNIQCLLNK PFQVSELREC GNGVVDGSEE CDCGSRENCQ DPCCDPLTCT LRPHAQCAAH HKCCHRCELR KAGDTCRSSK SPCDVAEQCD GKSGDCPPDG HLIDGTVCGT DGQCWRGNCS DSHQQCQKLW GREARVAEPV CFEQNTKGAE YANCGQRQAD GTYHPCQIED TRCGTLHCHS GSITPIDSSL KAFTFHFTEN SHQIQCKSIA SAAVGLTSDG TNCASGRVCV AGSCVEMSSV SSATACPTNN LALLCSGHGH CTTTARCVCF NGWSGVACDI RSNSSTYQGS MGFGEEGSGG SSQKSSERKT IMIPHLNIGT TLETATLFAI LLGFGVFLLL CLVCLMLCYR RRSVVEIPKP SDEKDEESPD RQIKFGNMPS YREEKRKRKS NKKIYGALNR ITEADERDST SLRSRDSAGG SQQLVDRRNG APVVVGGIRD PYAGEHIYAE SSSNHLTRQF RGINSDGSYP LRSFGSWRSS APISPASSSG QLTDVSTATT PLRLNKIGKF LKTLQSDDES PSPFSDHQSF TTGIGIGARL EQMQFGGGGD EELSAVEADH DVGSNTESSR GCEEPMDPGS WDSPTLVNGA SSSSTSNNYN FRQSPSLFSD PFKLEMTNSM HN // ID G7P1V4_MACFA Unreviewed; 958 AA. AC G7P1V4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 22-NOV-2017, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHH52367.1}; GN ORFNames=EGM_12796 {ECO:0000313|EMBL:EHH52367.1}; 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 {ECO:0000313|Proteomes:UP000009130}; RN [1] {ECO:0000313|EMBL:EHH52367.1, ECO:0000313|Proteomes:UP000009130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH52367.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001278; EHH52367.1; -; Genomic_DNA. DR ProteinModelPortal; G7P1V4; -. DR MEROPS; M12.978; -. DR Proteomes; UP000009130; Chromosome 3. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009130}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000009130}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 789 812 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 291 490 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 496 583 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 555 575 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 958 AA; 105957 MW; 7A09DBB321B060CF CRC64; MGRMGKGCLA SGPRSWMLSD ELVQGSPAVV SASFPDGFRE GGGGGDFRRG DVGPQDGGVR VRVIIFAFSL HSLLSPFLPG GDASLMELEK RKENRFLERQ SIVPLRLIYR SGGEDETRHD ALDTRVRGDP GGRQLTHVDQ ASFQVDAFGT SFILDVVLNH DLLSSEYVER HIEHGGKTVE VKGGEHCYYQ GHIRGNPASF VALSTCHGLH GMFYDGNHTY LIEPEENDTT QEDFHFHSVY KSRLFEFPLD DLPSEFQQVN ITPPKFILKP RPKRSKRQLR RYPRNVEEET KYIELMIVND HLMFKKHRLS VVHTNTYAKS VVNMADIIYK DQLKTRIVLV AMETWATDNK FAISENPLIT LREFMKYRRD FIKEKSDAVH LFSGSQFESS RSGAAYIGGI CSLLKGGGVN EFGKTDLMAV TLAQSLAHNI GIISDKRKLA SGECKCEDTW SGCIMGDTGY YLPKKFTQCN VEEYHDFLNS GGGACLFNKP SKLLDPPECG NGFIETGEEC DCGTPAECVL EGAECCKKCT LTQDSQCSDG ICCKKCKFQP MGTVCREAVN DCDIRETCSG NSSQCAPNIH KMDGYSCDGV QGICFGGRCK TRDRQCKYIW GQKVTASDKY CYEKLNIEGT EKGNCGKNKD TWIQCNKRDV LCGYLLCTNI GNIPRLGELD GEITSTLVVQ QGRTLNCSGG HVKLEEDVDL GYVEDGTPCG PQMMCLEHRC LPVASFNFST CLSSKEGTIC SGNGVCSNEL KCVCNRHWIG SDCNTYFPHN DDAKTGITLS GNGVAGTNII IGIIAGTILV LALILGITAW GYKNYREQRQ LPQGDYVKKP GDGDSFYSDI PPGVSTNSAS SSKKRSNGLS HSWSERIPDT KHISDICENG RPRSNSWQGN LGGNKKKIRG KRFRPRSNST ETLSPAKSPS SSTGSIASSR KYPYPMPPLP DEEKKVNRQS ARLWETSI // ID H0VG36_CAVPO Unreviewed; 905 AA. AC H0VG36; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 2. DT 28-MAR-2018, entry version 47. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSCPOP00000009056}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSCPOP00000009056}; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Caviidae; Cavia. OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000009056}; RN [1] {ECO:0000313|Ensembl:ENSCPOP00000009056} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000009056}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSCPOP00000009056} RP IDENTIFICATION. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000009056}; RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAKN02016691; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAKN02016692; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAKN02016693; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005006083.1; XM_005006026.2. DR STRING; 10141.ENSCPOP00000009056; -. DR Ensembl; ENSCPOT00000010176; ENSCPOP00000009056; ENSCPOG00000010085. DR GeneID; 100727244; -. DR CTD; 53616; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; H0VG36; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR Bgee; ENSCPOG00000010085; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005447}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005447}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 905 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5011751946. FT TRANSMEM 736 759 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 238 437 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 443 530 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 502 522 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 905 AA; 100303 MW; 2A2FC73A10CB1A14 CRC64; MQAAAASLPW LLLCALGFCP AARCGPAGEA SWTELQRSNE NRFLERQSIV PLRLVYRSGG DDETLHDELT TRVRGDPGGL QSTHVNRASF QVEAFGTPFI LDVVLNHDLL SSDYVERHIE HGGRTVEVKG GEHCYYQGHI RGNPASFVAL STCHGLHGMF YDGNHTYLIE PEENETSPED FRSHLVYKSR VFEFPLDDLP SEFQQVNITL PKFIPKPRLR RSKRQLLRYP RNVEEETKYI ELMIVNDHLM FKKHRLSVVH TNTYAKSVVN MADLIYKDQL KTRIVLVAME TWAADNKFAI SENPLITLRE FMKYRRDFIK EKSDAVHLFS GSQFESSRSG AAYIGGICSL LKGGGVNEFG KTDLMAVTLA QSLAHNIGII SDKRKLASGE CKCDDTWSGC IMGDTGYYLP KKFTQCNIEE YHDFLNSGGG TCLFNKPSKL LDPPECGNGF IETGEECDCG TSAECVLEGA ECCKKCTLTQ DSQCSDGLCC QKCKFQPMGT VCREAVNDCD IRETCSGNSS QCAPNVHKMD GYQCDGVQGI CFGGRCKTRD RQCKYIWGQK VTASDKYCYE KLNIEGTEKG NCGKDKDTWI QCNKRDVLCG YLLCTNIGNI PRLGELDGEI TSTLVVQQGR TLNCSGGHVK LEEDVDLGYV EDGTPCGPKM MCLEHRCLPV ASFNFSTCLS NKEGIVCSGN GFCSNELTCV CNRHWTGADC SIYFPYNEDA KTGITLSGNG VAGTNIIIGI IAGTILVLAL ILGITAWGYK NYREQRQLPQ GDYVKKPGDG DSFYSDIPPG VSTNSASSSK KRSNGLSHSW SERIPDTKHI SDICENGRPR SNSWQGNLGG NRKKIRGKRF RPRSNSTETL SPAKSPSSST GSIASSRKYP YPMPPLPDEE KAVNRHSARL WETSI // ID H0WSN9_OTOGA Unreviewed; 788 AA. AC H0WSN9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 28-MAR-2018, entry version 42. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSOGAP00000005107}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSOGAP00000005107}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000005107, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000005107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000005107} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQR03012528; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03012529; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03012530; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03012531; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03012532; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 30611.ENSOGAP00000005107; -. DR Ensembl; ENSOGAT00000005717; ENSOGAP00000005107; ENSOGAG00000005710. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; H0WSN9; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361}. FT DOMAIN 119 318 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 324 411 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 383 403 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 788 AA; 87571 MW; 91AFD40DBE2BE258 CRC64; ENGGKVIYLK GGEHCYYQGH IRGNPASFVA LSTCHGLHGM FYDGNHTYLI EPEENDTSQE DFHFHSVYKS RLFEFPLDDL PSEFQQVNIT SPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV YTNTYAKSVV NMADVIYKDQ LKTRIVLVAM ETWAADNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNVE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV RLEEDIDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGAD CNTYFPHNDD EKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KKRNYREQRQ LPQGDYVKKP GDGDSFYSDI PPGVSTNSAS SSKKRSNGLS HSWSERIPDT KHISDICENG RPRSNSWQGN MGGNRKKIRG KRFRPRSNST ETLSPAKSPS SSTGSIASSR KYPYPMPPLP DEEKKVNRQS ARLWETSI // ID H0XE24_OTOGA Unreviewed; 771 AA. AC H0XE24; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 23-MAY-2018, entry version 47. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSOGAP00000014165}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSOGAP00000014165}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000014165, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000014165} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000014165} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQR03042422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03042423; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003786313.1; XM_003786265.1. DR ProteinModelPortal; H0XE24; -. DR STRING; 30611.ENSOGAP00000014165; -. DR MEROPS; M12.976; -. DR Ensembl; ENSOGAT00000015819; ENSOGAP00000014165; ENSOGAG00000015813. DR GeneID; 100962759; -. DR CTD; 4185; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; H0XE24; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 771 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003545524. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 241 440 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 446 533 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 675 712 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 505 525 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 702 711 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 771 AA; 83800 MW; F38D09C4D1F0EB88 CRC64; MRLLRRWAFA ALPLLLPLLP PPGLGAQGPA GALQWRGSPQ VGGPEAPEVT EPSRLIRESS GGEVRKQQLD TRVRQEPPGG LPVHLAQVSF VIPAFNSNFT LDLELNHHLL SSQYVERHFS REGPTQHSTG AGDHCYYQGK LRGNPHSFAA LSTCQGLHGV FSDGNLTYIV EPQEMAGPWG PPQGPLPHLI YRTPLLPAPL GCREPGCLFT APAQSAPPNR PRLRRKRQVR RGHPTVHSET KYVELIVIND HQLFEQMRQS VVLTSNFAKS VVNLADVMYK EQLNTRIVLV AMETWADGDK IQVQDDLLET LARLMVYRRE GLPEPSDATH LFSGRTFQST SSGAAYVGGI CSLSRGGGVN EYGNMGAMAV TLAQTLGQNL GMMWNKHRSS AGDCKCPDIW LGCIMEDTGF YLPRKFSRCS IDEYNQFLQE GGGSCLFNKP LKLLDPPECG NGFVEAGEEC DCGSVQECSR AGGNCCKKCT LTHDAMCSDG LCCRRCKYEP RGVSCREAVN ECDIAETCTG DSSQCPPNLH KLDGYYCDHE QGRCYGGRCK TRDRQCQALW GHQAADRFCY EKLNVEGTER GNCGRKGSGW VQCNKQDVLC GFLLCVNISG APRLGDLGGD ISSVTFYHQG KELDCRGGHV QLADGSDLSY VEDGTACGPN MLCLDHRCLP ASAFNFSTCP GSGERRICSH HGVCSNEGKC ICQPDWTGKD CSIHNPLPTS PPTGETEKYK GPSGTNIIIG SIAGAVLVAA IVLGGTGWGF KNIRRGRSGG A // ID H2M022_ORYLA Unreviewed; 894 AA. AC H2M022; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 47. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSORLP00000011745}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000011745, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Ensembl:ENSORLP00000011745, ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000011745, RC ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000011745} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000011745}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAAF04003813; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BAAF04003814; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BAAF04003815; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BAAF04003816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BAAF04003817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BAAF04003818; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2M022; -. DR STRING; 8090.ENSORLP00000011745; -. DR Ensembl; ENSORLT00000011746; ENSORLP00000011745; ENSORLG00000009366. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; H2M022; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001038; Chromosome 16. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 694 717 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 197 396 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 402 489 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 633 670 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 461 481 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 660 669 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 894 AA; 98014 MW; 84BF380E71D49C4C CRC64; VGVEDTVPVR LLYSMSSLQQ VPHHGLSTRV KANSPAHNSE ADHVAQASFQ VDAFGRNFIL DVELNHELLS SGYVEKHVSE KGRTVVFSGG EHCYYQGKVR GIPQSFVALS TCHGLHGMFS DGNHTYMIEP GGHDSSNKAK IWGSVSKNVM IVYPLKSLKK LLWSLSATSK KLPKTCNSEN RINQQRSHPS PMAEKLASID VLVVFQTFMF KKHRLSVGHT NNNAKTVVNM ADMIFREQLN TRIVLVAMET WSTDNKFNID DDPMVTLKEF MKYRKDFIKE KCDSVHLFSG NHFHSNRMGA SYLGGVCSLT KGGGISEFGK THEMAIFLAQ SLGQNIGIFS DKKRILSGEC ECDDRWAGCI MDDMGYYMPN KFSSCNVEEY HNFLNSGGGV CLFNIPLKLL NPPECGNGFV EPGEECDCGS PAECAREGQN CCRNCTLTKG SNCSNGLCCN KCQMERIGVV CREAVNDCDI PENCSGNSSQ CPPNVHKMDG YTCEKDQGRC FNGRCKTKDR QCKYIWGEKA MAADKFCYEK LNIEGTEKGN CGKDKDTWIQ CNKQDVHCGY LLCSNISPAP RLGELQGGLT SFSVAQHSAS LDCSGAHVMI DGDTDLGYVE DGTACGTDSI CFNHKCLPVQ QFNFSTCPGT TDNSICSGHG VCSNELKCVC HLGWTGEDCG SISPFSYLVV GPTAPVSGIT STNIIVGAIA GSILFLGLIL AVTAWCYKSY KKRRQIPPGD YVTKPGDADS FYSDMPPGIS TNSGCSSKKR SACLSHLQIC TLSFTASIPS ISQNISLFGF RSNGLSHSWS ERIPDAKHIS DICENGRPRS NSWQGNLSGN RKKLKGKKFR ARSNSTETLS PAKSPTSSTG SIASSRRYPY PMPPLPDDQR KANRQSARLW ETSI // ID H2PMZ4_PONAB Unreviewed; 899 AA. AC H2PMZ4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 28-MAR-2018, entry version 40. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSPPYP00000019993}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSPPYP00000019993}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019993, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000019993, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000019993} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGA01257039; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257040; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257041; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257042; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257043; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257044; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257045; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257046; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257047; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPPYT00000020781; ENSPPYP00000019993; ENSPPYG00000017839. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000001595; Chromosome 7. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 899 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003568791. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 899 AA; 100343 MW; D444DF2E2C479A2F CRC64; MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFLERQSI VPLRLIYRSG GEDESRHDAL DTRVRGDPGG RQLTHVDQAS FQVDAFGTSF ILDVMLNHDL LSSEYIERHI ERGGKTVEVK GGEHCYYQGH IRGNPASFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRSNG LSHSWSERIP DTKHISDICE NGRPRSNSWQ GNLGGNKKKI RGKRFRPRSN STEYLNPWFK RDYNVAKWVE DVNKNTEGPY FRTLSPAKSP SSSTGSIASS RKYPYPMPPL PDEDKKVNRQ SARLWETSI // ID H2R3K1_PANTR Unreviewed; 769 AA. AC H2R3K1; A0A2J8IVF2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 23-MAY-2018, entry version 44. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSPTRP00000045659}; DE SubName: Full=ADAM11 isoform 1 {ECO:0000313|EMBL:PNI14506.1}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSPTRP00000045659, GN ECO:0000313|VGNC:VGNC:6327}; GN ORFNames=CK820_G0052918 {ECO:0000313|EMBL:PNI14506.1}; 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 {ECO:0000313|Ensembl:ENSPTRP00000045659, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000045659, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000045659} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:PNI14506.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Yerkes chimp pedigree #C0471 {ECO:0000313|EMBL:PNI14506.1}; RC TISSUE=Blood {ECO:0000313|EMBL:PNI14506.1}; RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., RA Chaisson M., Hoppe E., Hill C., Pang A., Hillier L., Baker C., RA Armstrong J., Shendure J., Paten B., Wilson R., Chao H., Schneider V., RA Ventura M., Kronenberg Z., Murali S., Gordon D., Cantsilieris S., RA Munson K., Nelson B., Raja A., Underwood J., Diekhans M., Fiddes I., RA Haussler D., Eichler E.; RT "High-resolution comparative analysis of great ape genomes."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACZ04061660; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; NBAG03000579; PNI14506.1; -; Genomic_DNA. DR RefSeq; XP_016787118.1; XM_016931629.1. DR STRING; 9598.ENSPTRP00000045659; -. DR PaxDb; H2R3K1; -. DR Ensembl; ENSPTRT00000048595; ENSPTRP00000045659; ENSPTRG00000009284. DR GeneID; 454735; -. DR CTD; 4185; -. DR VGNC; VGNC:6327; ADAM11. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; H2R3K1; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000002277; Chromosome 17. DR Bgee; ENSPTRG00000009284; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 769 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014576427. FT TRANSMEM 735 758 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 673 710 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 700 709 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 769 AA; 83497 MW; EE2C9B9F34F499D3 CRC64; MRLLRRWAFA ALLLPLLPPP GLGTQGPAGA LRWGDLPQLG GPGAPEVTEP SRLVRESSGG EVRKQQLDTR VRQEPPGGPP VHLAQVSFVI PAFNSNFTLD LELNHHLLSS QYVERHFSRE GTTQHSTGAG DHCYYQGKLR GNPHSFAALS TCQGLHGVFS DGNLTYIVEP QEVAGPWGAP QGPLPHLIYR TPLLPDPLGC REPGCLFALP AQSAPPNRPR LRRKRQVRRG HPTVHSETKY VELIVINDHQ LFEQMRQSVV LTSNFAKSVV NLADVIYKEQ LNTRIVLVAM ETWADGDKIQ VQDDLLETLA RLMVYRREGL PEPSDATHLF SGRTFQSTSS GAAYVGGICS LSHGGGVNEY GNMGAMAVTL AQTLGQNLGM MWNKHRSSAG DCKCPDIWLG CIMEDTGFYL PRKFSRCSID EYNQFLQEGG GSCLFNKPLK LLDPPECGNG FVEAGEECDC GSVQECSRAG GNCCKKCTLT HDAMCSDGLC CRRCKYEPRG VSCREAVNEC DIAETCTGDS SQCPPNLHKL DGYYCDHEQG RCYGGRCKTR DRQCQVLWGH AAADRFCYEK LNVEGTERGS CGRKGSGWVQ CSKQDVLCGF LLCVNISGAP RLGDLVGDIS SVTFYHQGKE LDCRGGHVQL ADGSDLSYVE DGTACGPNML CLDHRCLPAS AFNFSTCPGS GERRICSHHG VCSNEGKCIC QPDWTGKDCS IHNPLPTSPP TGETERYKGP SGTNIIIGSI AGAVLVAAIV LGGTGWGFKN IRRGRSGGA // ID H2RBY3_PANTR Unreviewed; 906 AA. AC H2RBY3; A0A2J8LGN5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 45. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSPTRP00000056483}; DE SubName: Full=ADAM22 isoform 5 {ECO:0000313|EMBL:PNI46411.1}; GN Name=ADAM22 {ECO:0000313|VGNC:VGNC:4247}; GN Synonyms=LOC107966418 {ECO:0000313|Ensembl:ENSPTRP00000056483}; GN ORFNames=CK820_G0029099 {ECO:0000313|EMBL:PNI46411.1}; 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 {ECO:0000313|Ensembl:ENSPTRP00000056483, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000056483, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000056483} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:PNI46411.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Yerkes chimp pedigree #C0471 {ECO:0000313|EMBL:PNI46411.1}; RC TISSUE=Blood {ECO:0000313|EMBL:PNI46411.1}; RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., RA Chaisson M., Hoppe E., Hill C., Pang A., Hillier L., Baker C., RA Armstrong J., Shendure J., Paten B., Wilson R., Chao H., Schneider V., RA Ventura M., Kronenberg Z., Murali S., Gordon D., Cantsilieris S., RA Munson K., Nelson B., Raja A., Underwood J., Diekhans M., Fiddes I., RA Haussler D., Eichler E.; RT "High-resolution comparative analysis of great ape genomes."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSPTRP00000065558} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2018) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC161123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC188765; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC188795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; NBAG03000292; PNI46411.1; -; Genomic_DNA. DR RefSeq; XP_001164271.1; XM_001164271.5. DR RefSeq; XP_016813181.1; XM_016957692.1. DR STRING; 9598.ENSPTRP00000056483; -. DR MEROPS; M12.978; -. DR PaxDb; H2RBY3; -. DR Ensembl; ENSPTRT00000064920; ENSPTRP00000056483; ENSPTRG00000019374. DR Ensembl; ENSPTRT00000108414; ENSPTRP00000065558; ENSPTRG00000048692. DR GeneID; 463517; -. DR CTD; 53616; -. DR VGNC; VGNC:4247; ADAM22. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; H2RBY3; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000002277; Chromosome 7. DR Bgee; ENSPTRG00000019374; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 906 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014576604. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 906 AA; 100486 MW; 5C573FADFD1BE7B8 CRC64; MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFLERQSI VPLRLIYRSG GEDESRHDAL DTRVRGDPGG RQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYVERHI EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE DKKVNRQSAR LWETSI // ID H2SAA1_TAKRU Unreviewed; 692 AA. AC H2SAA1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSTRUP00000009327}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000009327, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000009327} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000009327} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000009382; ENSTRUP00000009327; ENSTRUG00000003940. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 652 675 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 156 354 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 360 447 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 591 628 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 419 439 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 618 627 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 692 AA; 76288 MW; 6B161EDA876957C9 CRC64; ANHLAHASFQ IDAFSRKFIL DVDLNHDLLS SAYVERHLSE KGKPVITNGG EHCYYQGKVR DILHSFAALS TCHGLHGMFF DGNHTYTIEP GGSPAWARTA GRRSQWEETL VGEMAEARKL AREGTHWRPP FPGSKVQRRK KRQAPHVPRN VEDETKYIEL MVINDHLMYK KHRLSVGHTN NYAKSVVNMA DMIFKEQLNT RIVLVAMETW SADNKFNIDD DPMVTLREFM KYRKDFIKER CDSVHLFSGS RFLSSWGGAS YMGGVCSTKG GGVNEYGKTD EMAITLAQSL GQNIGIFSDK KRILNGECVC DDRWSGCIMD DVGYYLPKRF SDCNVEEYYN FLNSGGGACL FNKPIKFLDP PVCGNGLVEP GEECDCGSPV ECAREGGACC NKCALTQGSK CSNGLCCSDC QMEFMGVVCR DAVNDCDIPE NCTGDSSQCP PNVHKMDGYT CEKDQGRCFN GRCKTKDRQC KYIWGEKATA ADKFCYEKLN IEGTEKGNCG KDKDTWVQCN KQDVHCGYLL CSNISPAPRL GELQGGLTSF SVARHSASLD CSGAHVLIDG DTDLGYVEDG TACGTDHVCF NHKCLPIHQF NFSTCPGSTD KTICSGHGVC SNELKCVCHL GWTGEGCNST SPRSHLVVGP TASVSGITVT NIIIGAIVGS ILFLVLILAA TAWCYKSYKQ RRYANPGTQT PF // ID H2SAA2_TAKRU Unreviewed; 728 AA. AC H2SAA2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSTRUP00000009328}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000009328, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000009328} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000009328} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000009383; ENSTRUP00000009328; ENSTRUG00000003940. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 689 712 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 193 391 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 397 484 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 628 665 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 456 476 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 655 664 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 728 AA; 80378 MW; 87005CAD845485E6 CRC64; GKEDTVPLRL LYNRDNRGQV AQDELSTRVK SGPASAKANH LAHASFQIDA FSRKFILDVD LNHDLLSSAY VERHLSEKGK PVITNGGEHC YYQGKVRDIL HSFAALSTCH GLHGMFFDGN HTYTIEPGGQ GNGHTFRLVL PTAAIQLKYI CAAGVCVFRY SQQDYCRPYG SKVQRRKKRQ APHVPRNVED ETKYIELMVI NDHLMYKKHR LSVGHTNNYA KSVVNMADMI FKEQLNTRIV LVAMETWSAD NKFNIDDDPM VTLREFMKYR KDFIKERCDS VHLFSGSRFL SSWGGASYMG GVCLTKGGGV NEYGKTDEMA ITLAQSLGQN IGIFSDKKRI LNGECVCDDR WSGCIMDDVG YYLPKRFSDC NVEEYYNFLN SGGGACLFNK PIKFLDPPVC GNGLVEPGEE CDCGSPVECA REGGACCNKC ALTQGSKCSN GLCCSDCQME FMGVVCRDAV NDCDIPENCT GDSSQCPPNV HKMDGYTCEK DQGRCFNGRC KTKDRQCKYI WGEKATAADK FCYEKLNIEG TEKGNCGKDK DTWVQCNKQD VHCGYLLCSN ISPAPRLGEL QGGLTSFSVA RHSASLDCSG AHVLIDGDTD LGYVEDGTAC GTDHVCFNHK CLPIHQFNFS TCPGSTDKTI CSGHGVCSNE LKCVCHLGWT GEGCNSTSPR SHLVVGPTAS VSGITVTNII IGAIVGSILF LVLILAATAW CYKSYKQRRY VESEVHRR // ID H2SAA3_TAKRU Unreviewed; 726 AA. AC H2SAA3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 41. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSTRUP00000009329}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000009329, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000009329} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000009329} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000009384; ENSTRUP00000009329; ENSTRUG00000003940. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 693 716 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 197 395 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 401 488 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 632 669 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 460 480 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 659 668 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 726 AA; 79680 MW; 8F6E7B8ADB78D0FA CRC64; RWKALRDADR LAGKEDTVPL RLLYNRDNRG QVAQDELSTR VKSGPASAKA NHLAHASFQI DAFSRKFILD VDLNHDLLSS AYVERHLSEK GKPVITNGGE HCYYQGKVRD ILHSFAALST CHGLHGMFFD GNHTYTIEPG GQGNGHGDVQ VHMVYKSPGT DVPEPPFPSP PFPGSKVQRR KKRQAPHVPR NVEDETKYIE LMVINDHLMY KKHRLSVGHT NNYAKSVVNM ADMIFKEQLN TRIVLVAMET WSADNKFNID DDPMVTLREF MKYRKDFIKE RCDSVHLFSG SRFLSSWGGA SYMGGVCLTK GGGVNEYGKT DEMAITLAQS LGQNIGIFSD KKRILNGECV CDDRWSGCIM DDVGYYLPKR FSDCNVEEYY NFLNSGGGAC LFNKPIKFLD PPVCGNGLVE PGEECDCGSP VECAREGGAC CNKCALTQGS KCSNGLCCSD CQMEFMGVVC RDAVNDCDIP ENCTGDSSQC PPNVHKMDGY TCEKDQGRCF NGRCKTKDRQ CKYIWGEKAT AADKFCYEKL NIEGTEKGNC GKDKDTWVQC NKQDVHCGYL LCSNISPAPR LGELQGGLTS FSVARHSASL DCSGAHVLID GDTDLGYVED GTACGTDHVC FNHKCLPIHQ FNFSTCPGST DKTICSGHGV CSNELKCVCH LGWTGEGCNS TSPRSHLVVG PTASVSGITV TNIIIGAIVG SILFLVLILA ATAWCYKNGK SRTFGL // ID H2TH58_TAKRU Unreviewed; 731 AA. AC H2TH58; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000024007}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000024007, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000024007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000024007} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR ProteinModelPortal; H2TH58; -. DR STRING; 31033.ENSTRUP00000024007; -. DR Ensembl; ENSTRUT00000024106; ENSTRUP00000024007; ENSTRUG00000009555. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 694 717 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 196 395 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 401 488 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 632 669 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 460 480 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 659 668 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 731 AA; 81154 MW; 2F246619E0D53460 CRC64; SGDGRVLVQP KRLLQQMHGQ EELHHNRLDT RIHNQAAGPQ NIHLAQTSFL VEAFETSFIL DLELNHNLLS TEYVERHYEE DGRLCENTGG EHCYYHGHVR GMPQSWAALS TCLGLQGMFS DGNFSYGIEP IDSDEMWKRL FPYSPSPLVV ISPSLFVLLS CRRRTSTLCI VCRTWTFFHL TVQVRRGQRT VQSETKYIEL MVVNDHELFV QRRRSTTHTK TFAKSVVNMA DAIYKEQLNT RIVLVAMETW SSENKISVGD DVLLTLRDFM KYRKESIKEH CDAVHLFSGR TFMSSRSEAA YFGGICSLTK GGGINEFGGV GPLAITLCQS LGQNLGMLRN KEQSAAGDCR CPDPWLGCIM EETSYHLPRK FSRCSVDEYL RFLQQGGGSC LFNKPSKLLD PPECGNGYVE LGEECDCGLI TECARSGANC CKKCTLTHNA MCSNGLCCRD CKYELRGVTC RESVNECDIP ETCTGDSSQC PHNVHKLDGY MCDAGQGRCF DARCKTRDGQ CMALWGYSSA DRFCYEKLNS EGTEKGNCGP DPTGQGWVQC TKQDVLCGLL LCNNLTAKPS FGELQGKLTS LTIQHQNRYM DCRGGHAVLD DGLDLGYVED GTPCGPNMMC LDRRCIPVTT FNLSTCPGSS YSRICSHHGT CSNEMKCICD PDYTGKDCSV FDPIPIPTPL EGPEKYRGPS GTNIIIGSVA GAILLAAIVL GGTGWGFKNI RRGRYDPAYE S // ID H2TH59_TAKRU Unreviewed; 717 AA. AC H2TH59; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000024008}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000024008, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000024008} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000024008} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000024107; ENSTRUP00000024008; ENSTRUG00000009555. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 693 716 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 195 394 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 400 487 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 631 668 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 459 479 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 658 667 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 717 AA; 79700 MW; 18E3A2ECB349F957 CRC64; RVLVQPKRLL QQMHGQEELH HNRLDTRIHN QAAGPQNIHL AQTSFLVEAF ETSFILDLEL NHNLLSTEYV ERHYEEDGRL CENTGGEHCY YHGHVRGMPQ SWAALSTCLG LQGMFSDGNF SYGIEPIDSD EEKNQHVVYR VPDMDLFSFD CPGDTDPMEE EEEEEEEEKL VSREGVRRSK RQVRRGQRTV QSETKYIELM VVNDHELFVQ RRRSTTHTKT FAKSVVNMAD AIYKEQLNTR IVLVAMETWS SENKISVGDD VLLTLRDFMK YRKESIKEHC DAVHLFSGRT FMSSRSEAAY FGGICSLTKG GGINEFGGVG PLAITLCQSL GQNLGMLRNK EQSAAGDCRC PDPWLGCIME ETSYHLPRKF SRCSVDEYLR FLQQGGGSCL FNKPSKLLDP PECGNGYVEL GEECDCGLIT ECARSGANCC KKCTLTHNAM CSNGLCCRDC KYELRGVTCR ESVNECDIPE TCTGDSSQCP HNVHKLDGYM CDAGQGRCFD ARCKTRDGQC MALWGYSSAD RFCYEKLNSE GTEKGNCGPD PTGQGWVQCT KQDVLCGLLL CNNLTAKPSF GELQGKLTSL TIQHQNRYMD CRGGHAVLDD GLDLGYVEDG TPCGPNMMCL DRRCIPVTTF NLSTCPGSSY SRICSHHGTC SNEMKCICDP DYTGKDCSVF DPIPIPTPLE GPEKYRGPSG TNIIIGSVAG AILLAAIVLG GTGWGFK // ID H2TH60_TAKRU Unreviewed; 722 AA. AC H2TH60; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000024009}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000024009, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000024009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000024009} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000024108; ENSTRUP00000024009; ENSTRUG00000009555. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 688 711 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 190 389 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 395 482 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 626 663 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 454 474 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 653 662 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 722 AA; 80166 MW; 7B73975EB4748D4D CRC64; LVQPKRLLQQ MHGQEELHHN RLDTRIHNQA AGPQNIHLAQ TSFLVEAFET SFILDLELNH NLLSTEYVER HYEEDGRLCE NTGGEHCYYH GHVRGMPQSW AALSTCLGLQ GMFSDGNFSY GIEPIDSDEE KNQHVVYRVP DMDLFSFDCP AGSVILICSD EMPPEQYRIR EALRRPQVRR GQRTVQSETK YIELMVVNDH ELFVQRRRST THTKTFAKSV VNMADAIYKE QLNTRIVLVA METWSSENKI SVGDDVLLTL RDFMKYRKES IKEHCDAVHL FSGRTFMSSR SEAAYFGGIC SLTKGGGINE FGGVGPLAIT LCQSLGQNLG MLRNKEQSAA GDCRCPDPWL GCIMEETSYH LPRKFSRCSV DEYLRFLQQG GGSCLFNKPS KLLDPPECGN GYVELGEECD CGLITECARS GANCCKKCTL THNAMCSNGL CCRDCKYELR GVTCRESVNE CDIPETCTGD SSQCPHNVHK LDGYMCDAGQ GRCFDARCKT RDGQCMALWG YSSADRFCYE KLNSEGTEKG NCGPDPTGQG WVQCTKQDVL CGLLLCNNLT AKPSFGELQG KLTSLTIQHQ NRYMDCRGGH AVLDDGLDLG YVEDGTPCGP NMMCLDRRCI PVTTFNLSTC PGSSYSRICS HHGTCSNEMK CICDPDYTGK DCSVFDPIPI PTPLEGPEKY RGPSGTNIII GSVAGAILLA AIVLGGTGWG FKNIRRGRYD PA // ID H2TH61_TAKRU Unreviewed; 726 AA. AC H2TH61; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000024010}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000024010, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000024010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000024010} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000024109; ENSTRUP00000024010; ENSTRUG00000009555. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 689 712 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 189 388 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 394 481 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 625 662 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 453 473 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 652 661 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 726 AA; 80845 MW; 650F130136E4C854 CRC64; PKRLLQQMHG QEELHHNRLD TRIHNQAAGP QNIHLAQTSF LVEAFETSFI LDLELNHNLL STEYVERHYE EKRPRWQKGG EHCYYHGHVR GMPQSWAALS TCLGLQGMFS DGNFSYGIEP IDSDEASNLS TAQLHSLKRW INDLYSNCLP AFDNQRGTQA STVKETLTRW RRRRRRVRRG QRTVQSETKY IELMVVNDHE LFVQRRRSTT HTKTFAKSVV NMADAIYKEQ LNTRIVLVAM ETWSSENKIS VGDDVLLTLR DFMKYRKESI KEHCDAVHLF SGRTFMSSRS EAAYFGGICS LTKGGGINEF GGVGPLAITL CQSLGQNLGM LRNKEQSAAG DCRCPDPWLG CIMEETSYHL PRKFSRCSVD EYLRFLQQGG GSCLFNKPSK LLDPPECGNG YVELGEECDC GLITECARSG ANCCKKCTLT HNAMCSNGLC CRDCKYELRG VTCRESVNEC DIPETCTGDS SQCPHNVHKL DGYMCDAGQG RCFDARCKTR DGQCMALWGY SSADRFCYEK LNSEGTEKGN CGPDPTGQGW VQCTKQDVLC GLLLCNNLTA KPSFGELQGK LTSLTIQHQN RYMDCRGGHA VLDDGLDLGY VEDGTPCGPN MMCLDRRCIP VTTFNLSTCP GSSYSRICSH HGTCSNEMKC ICDPDYTGKD CSVFDPIPIP TPLEGPENFN PTGPSGTNII IGSVAGAILL AAIVLGGTGW GFKNIRRGRY DPAYES // ID H2TH62_TAKRU Unreviewed; 710 AA. AC H2TH62; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000024011}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000024011, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000024011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000024011} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000024110; ENSTRUP00000024011; ENSTRUG00000009555. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 687 708 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 187 386 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 392 479 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 623 660 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 451 471 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 650 659 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 710 AA; 78987 MW; 9C1C29731B17AEDD CRC64; PKRLLQQMHG QEELHHNRLD TRIHNQAAGP QNIHLAQTSF LVEAFETSFI LDLELNHNLL STEYVERHYE EDGRLCENTG GEHCYYHGHV RGMPQSWAAL STCLGLQGMF SDGNFSYGIE PIDSDENQRG TQASTVKETL TRWRRRRRRR RRRSWFPVTT LLPEVKMSKR SSHYVRRGQR TVQSETKYIE LMVVNDHELF VQRRRSTTHT KTFAKSVVNM ADAIYKEQLN TRIVLVAMET WSSENKISVG DDVLLTLRDF MKYRKESIKE HCDAVHLFSG RTFMSSRSEA AYFGGICSLT KGGGINEFGG VGPLAITLCQ SLGQNLGMLR NKEQSAAGDC RCPDPWLGCI MEETSYHLPR KFSRCSVDEY LRFLQQGGGS CLFNKPSKLL DPPECGNGYV ELGEECDCGL ITECARSGAN CCKKCTLTHN AMCSNGLCCR DCKYELRGVT CRESVNECDI PETCTGDSSQ CPHNVHKLDG YMCDAGQGRC FDARCKTRDG QCMALWGYSS ADRFCYEKLN SEGTEKGNCG PDPTGQGWVQ CTKQDVLCGL LLCNNLTAKP SFGELQGKLT SLTIQHQNRY MDCRGGHAVL DDGLDLGYVE DGTPCGPNMM CLDRRCIPVT TFNLSTCPGS SYSRICSHHG TCSNEMKCIC DPDYTGKDCS VFDPIPIPTP LEGPENFNPT GPSGTNIIIG SVAGAILLAA IVLGGTGWGF // ID H2YZ96_CIOSA Unreviewed; 828 AA. AC H2YZ96; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 23-MAY-2018, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000010658}; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000010658, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000010658} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000010658} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 51511.ENSCSAVP00000010658; -. DR Ensembl; ENSCSAVT00000010788; ENSCSAVP00000010658; ENSCSAVG00000006270. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; H2YZ96; -. DR OMA; PDGCCVE; -. DR OrthoDB; EOG091G01NX; -. DR TreeFam; TF314733; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005794; C:Golgi apparatus; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0017124; F:SH3 domain binding; IEA:InterPro. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR033596; ADAM19. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR PANTHER; PTHR11905:SF19; PTHR11905:SF19; 1. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00276, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DOMAIN 148 350 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 358 445 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 585 617 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 290 290 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 289 289 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 293 293 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 299 299 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 265 345 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 589 599 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 607 616 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 828 AA; 89561 MW; D9A6E7831B1E2F19 CRC64; FSLQFGNRTL ILELKLNDEL LPKDFTTSTY TDNGEIIMEK PKLQDRNHCY YQGKVRNIKG SHVIMSTCNG LRGCITLPND FLLIEPLGAD SSKHVVYRPS DRRLNNIESC GNEEHTDDHF SENVDKFAGM LRGNSPHRHK RQTSTEKKFL ELLIVADKAQ VSRSKHTRIE LDSRVKELVN YLHGFYKKLS IHVVLSHIEV WSSRDKIPLK TNAKEVLNEF LSYRQNKIRT DSVDSPWRYT DNAQLLYGGS FDGTTIGMAS VKTMCSSRSG GVNQDHQSNV FYTAATLAHE MGHNFGMHHD SSECVCAQNA QCIMAASSGF GSTKDWSSCS KDYLAQSIRE GLGNCLLNVP DPSRLYGGPK CGNDIVEMGE ECDCGGIEEC SSLCCNATTC KLNPGAKCET GPCCLSCQYS PPGHVCRGTD NKDCDLAEYC TGFSANCPGN VYMENGSPCN NKQAYCSDGI CLTHDMQCQG VWGDGAVSGV DICYQQVNKL GNWNGNCGKD LNGNFLKCTK ENSKCGKLQC SGGGPRPMVG RDRYSFVNTI GGIHKCKTIS SDDNATDVSD PGLVRDGTAC GTMKTCNDGE CSALPAMTCS ATCNGNGICN NLGNCHCNRG WAPPFCNSEG NGGSINSGPI TNKQSKSLNL YILVMPTKTR CIGSSSYLKV LLHTDTKNRT PIVMSITQPS RPPIVSTNVQ NTPSRPPPPR PLAPPQVSVS VTPIRTAPPP PKPPTVPPPV PSFPPPNVQP PLPPPPPPTV PASKPPVPQP PAPKPSSTPS KPVVTRPPVP SFVSKQPIKP DNPTNNQPPP PPSKPPLPPA GKPPPPVSKK PTPDKVIS // ID H2YZ97_CIOSA Unreviewed; 712 AA. AC H2YZ97; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000010659}; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000010659, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000010659} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000010659} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000010789; ENSCSAVP00000010659; ENSCSAVG00000006270. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00276, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DOMAIN 149 326 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 334 421 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 544 576 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 266 266 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 265 265 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 269 269 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 275 275 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 241 321 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 548 558 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 566 575 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 712 AA; 76932 MW; 494E5FBFDB67A942 CRC64; HAVNTLFSLQ FGNRTLILEL KLNDELLPKD FTTSTYTDNG EIIMEKPKLQ DRNHCYYQGK VRNIKGSHVI MSTCNGLRGC ITLPNDFLLI EPLGADSSKH VVYRPSDRRL NNIESCGNEE HTDDHFSENV DKFAGFLIFS KHTRIELDSR VKELVNYLHG FYKKLSIHVV LSHIEVWSSR DKIPLKTNAK EVLNEFLSYR QNKIRTDSVD SPWRYTDNAQ LLYGGSFDGT TIGMASVKTM CSSRSGGVNQ DHQSNVFYTA ATLAHEMGHN FGMHHDSSEC VCAQNAQCIM AASSGFGSTK DWSSCSKDYL AQSIREGLGN CLLNVPDPSR LYGGPKCGND IVEMGEECDC GGIEECSSLC CNATTCKLNP GAKCETGPCC LSCQYSPPGH VCRGTDNKDC DLAEYCTGFS ANCPGNVYME NGSPCNNKQA YCSDGICLTH DMQCQGVWGD VTGCLLYKVL KCLFIVLIHI NSKCGKLQCS GGGPRPMVGR DRYSFVNTIG GIHKCKTISS DDNATDVSDP GLVRDGTACG TMKTCNDGEC SALPAMTCSA TCNGNGICNN LGNCHCNRGW APPFCNSEGN GGSINSGPIT NKQSKSLNLY ILVMVSVSVT PIRTAPPPPK PPTVPPPVPS FPPPNVQPPL PPPPPPTVPA SKPPVPQPPA PKPSSTPSKP VVTRPPVPSF VSKQPIKPDN PTNNQPPPPP SKPPLPPAGK PP // ID H2YZ98_CIOSA Unreviewed; 809 AA. AC H2YZ98; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 23-MAY-2018, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAVP00000010660}; OS Ciona savignyi (Pacific transparent sea squirt). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000010660, ECO:0000313|Proteomes:UP000007875}; RN [1] {ECO:0000313|Ensembl:ENSCSAVP00000010660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., RA Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., RA David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., RA Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., RA Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., RA Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., RA O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000010660} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAVT00000010790; ENSCSAVP00000010660; ENSCSAVG00000006270. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000007875; Unassembled WGS sequence. DR GO; GO:0005794; C:Golgi apparatus; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0017124; F:SH3 domain binding; IEA:InterPro. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR033596; ADAM19. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR PANTHER; PTHR11905:SF19; PTHR11905:SF19; 1. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007875}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00276, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000007875}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 631 661 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 138 340 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 348 435 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 575 607 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 280 280 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 279 279 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 283 283 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 289 289 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 255 335 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 579 589 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 597 606 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 809 AA; 87969 MW; 2CD7004F8F9E426A CRC64; ILELKLNDEL LPKDFTTSTY TDNGEIIMEK PKLQDRNHCY YQGKVRNIKG SHVIMSTCNG LRGCITLPND FLLIEPLGAD SSKHVVYRPS DRRLNNIESC GNEEHTDDHF SENVDKFAGM LRGNSPHRHK RQTSTEKKFL ELLIVADKAQ VSRSKHTRIE LDSRVKELVN YLHGFYKKLS IHVVLSHIEV WSSRDKIPLK TNAKEVLNEF LSYRQNKIRT DSVDSPWRYT DNAQLLYGGS FDGTTIGMAS VKTMCSSRSG GVNQDHQSNV FYTAATLAHE MGHNFGMHHD SSECVCAQNA QCIMAASSGF GSTKDWSSCS KDYLAQSIRE GLGNCLLNVP DPSRLYGGPK CGNDIVEMGE ECDCGGIEEC SSLCCNATTC KLNPGAKCET GPCCLSCQYS PPGHVCRGTD NKDCDLAEYC TGFSANCPGN VYMENGSPCN NKQAYCSDGI CLTHDMQCQG VWGDGAVSGV DICYQQVNKL GNWNGNCGKD LNGNFLKCTK ENSKCGKLQC SGGGPRPMVG RDRYSFVNTI GGIHKCKTIS SDDNATDVSD PGLVRDGTAC GTMKTCNDGE CSALPAMTCS ATCNGNGICN NLGNCHCNRG WAPPFCNSEG NGGSINSGPI TNKQSKSLNL YILWTLKTIL MLVMFLVVFP IIIGLGLFIW YRYCHGREQN RTPIVMSITQ PSRPPIVSTN VQNTPSRPPP PRPLAPPQVS VSVTPIRTAP PPPKPPTVPP PVPSFPPPNV QPPLPPPPPP TVPASKPPVP QPPAPKPSST PSKPVVTRPP VPSFVSKQPI KPDNPTNNQP PPPPSKPPL // ID H3CD70_TETNG Unreviewed; 872 AA. AC H3CD70; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 23-MAY-2018, entry version 44. DE SubName: Full=ADAM metallopeptidase domain 8a {ECO:0000313|Ensembl:ENSTNIP00000006193}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000006193, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000006193} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000006193} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 99883.ENSTNIP00000006193; -. DR Ensembl; ENSTNIT00000006341; ENSTNIP00000006193; ENSTNIG00000016539. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; H3CD70; -. DR OMA; DENVQGC; -. DR OrthoDB; EOG091G01NX; -. DR TreeFam; TF314733; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0002020; F:protease binding; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 872 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003582174. FT TRANSMEM 679 704 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 205 406 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 414 500 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 634 666 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 340 340 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 339 339 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 343 343 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 349 349 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 472 492 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 638 648 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 656 665 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 872 AA; 94324 MW; DE0BE75FE6A63CA4 CRC64; MADLGHFLFM LLVSWGTTSA EPLPHVKKYQ TVIPQRLEDP SPSDDAAAHR TFPDVLRFSL TITEQNYTLH LEKNKHLVGG SFTVTHFSDQ GARVTTAPDL RDHCYYHGHV VGVEDSSASV GLCSGIRGFV HVHGQIYLIE PLAEAETDGG LHAVYNYKHL RRKRSSCSHG NQTSYYDHVP GPSGLFQLAS LKRRGQSGER VGKPRTVELV VVVDHTEYKK IGSTKMVESR VLEVANHVDK LYRPVGIRVM LVGLEIWSYR DLIDVSSDPE LTLGRFLKWR QWSLLPRTKH DNAQLITGVD FDGSTVGLAN TNTMCTSNSG AVNEDHNKSP VGVASTIAHE MGHNLGLSHD VENCVCGSQT TKRGCIMSES VGEAGLSIQG SSAAGSQQQL STFLEEITPA CLLDSPSTSR IYGGPVCGNA FVEAGEECDC GTAKECRNPC CNATTCKLAA GAQCAAGECC HRCQLKATGS VCRPKSGDCD LEEYCTGFSA SCPRDAFTSN GLACNRGAGY CYNGQCPSHQ QHCRRLWGPE AKMAVEACYL QHGNCRKTLF NQKCSRRDQF CGKLLCSDGW EFPVTSKKFL YPLGNGKQCN EAGMNSEDNY PPDLAMVPTG TKCGPNMVCY NQRCQDMKSV KPYATSDCSS KCNNRGVCNH ENKCHCDPGW APPYCDVLLS ELPRETGSVV LPVSLAVGFL LLLVLVFGGL MCYIKKRPPV KRCLQSASGQ SNPLFRSGSA RGSPRLGPAH IGQPVFVESS ATQACKPLFS SRATTAAPKP SRAAPEPPKN PKPVAQPSQV QQVPRPPSSV GAEVSCCMQS LAPQKKPLPP SRPLPPVASK PVVKSKPPVP PVKPKPSAYA SSLPHTQLLA GRAALMPPNR PR // ID H3CY08_TETNG Unreviewed; 736 AA. AC H3CY08; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTNIP00000013143}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000013143, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000013143} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000013143} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR ProteinModelPortal; H3CY08; -. DR STRING; 99883.ENSTNIP00000013143; -. DR Ensembl; ENSTNIT00000013335; ENSTNIP00000013143; ENSTNIG00000010242. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; H3CY08; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 699 722 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 200 399 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 405 492 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 636 673 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 464 484 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 663 672 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 736 AA; 81085 MW; 86088DA9745B89CF CRC64; SGDGRALVQP KRLLQQMHGR EELPHSRLDT RLQHQAPGPQ NIHLAQSSFL VEAFGTSFIL DLELNHNLLS TEYVERYYDE DGRLSQDTGG EHCYYHGRLR GVPRSWAALS TCHGLQGMFS DGNFSYGIEP IDSDCPPSPS QEKNQHVVYR VPDVDLSPPD CPGVICVLCE GDMGARPERM DFCCLLQVRR GQHTVQTETK YIELMVVNDH ELFVQRRRST TQTKNFAKSV VNMADAIYKE QLNTRIVLVA METWSSENKI SVGDDALLTL RDFMKYRKES IKERCDAVHL FSGRTFMSSR SEAAYIGGIC SLTRGGGINE FGSVGPMAIT LCQSLGQNLG MLRSKERASA GDCRCPDPWL GCIMEDTSYH LPRKFSRCSV DEYLRFLQQG GGSCLFNKPS KLLDAPECGN GYVELGEECD CGLVTECDRS GAICCKKCTL THNAMCSNGL CCRDCKYELR GVTCREAANE CDIPETCTGD SSQCPHNVHK LDGYTCDAGQ GRCFDGRCKT RDGQCMALWG YTSADRFCYE KLNSEGTEKG NCGPDPSGQG WVQCTKQDVL CGLLLCMNLT ARPSFGQLQG KLTSLTIQHQ NRYMDCRGGH AVLDDGLDLG YVEDGTPCGP NMMCLERRCI PVTTFNLSTC PGSSHSRICS HHGTCSNEMK CICDPDYTGK DCSVFDPIPI PTPSEGPEKY RGSPSGTNII IGSVAGAILL AAIVLGGTGW GFKNIRRGRY DPACQS // ID H3DGJ5_TETNG Unreviewed; 870 AA. AC H3DGJ5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 23-MAY-2018, entry version 43. DE SubName: Full=ADAM metallopeptidase domain 8a {ECO:0000313|Ensembl:ENSTNIP00000019639}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000019639, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000019639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000019639} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTNIT00000019869; ENSTNIP00000019639; ENSTNIG00000016539. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 870 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003582310. FT TRANSMEM 679 704 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 205 406 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 414 500 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 634 666 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 340 340 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 339 339 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 343 343 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 349 349 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 472 492 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 638 648 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 656 665 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 870 AA; 94117 MW; 425EC1724A40C824 CRC64; MADLGHFLFM LLVSWGTTSA EPLPHVKKYQ TVIPQRLEDP SPSDDAAAHR TFPDVLRFSL TITEQNYTLH LEKNKHLVGG SFTVTHFSDQ GARVTTAPDL RDHCYYHGHV VGVEDSSASV GLCSGIRGFV HVHGQIYLIE PLAEAETDGG LHAVYNYKHL RRKRSSCSHG NQTSYYDHVP GPSGLFQLAS LKRRGQSGER VGKPRTVELV VVVDHTEYKK IGSTKMVESR VLEVANHVDK LYRPVGIRVM LVGLEIWSYR DLIDVSSDPE LTLGRFLKWR QWSLLPRTKH DNAQLITGVD FDGSTVGLAN TNTMCTSNSG AVNEDHNKSP VGVASTIAHE MGHNLGLSHD VENCVCGSQT TKRGCIMSES VGEAGLSIQG SSAAGSQQQL STFLEEITPA CLLDSPSTSR IYGGPVCGNA FVEAGEECDC GTAKECRNPC CNATTCKLAA GAQCAAGECC HRCQLKATGS VCRPKSGDCD LEEYCTGFSA SCPRDAFTSN GLACNRGAGY CYNGQCPSHQ QHCRRLWGPE AKMAVEACYL QHGNCRKTLF NQKCSRRDQF CGKLLCSDGW EFPVTSKKFL YPLGNGKQCN EAGMNSEDNY PPDLAMVPTG TKCGPNMVCY NQRCQDMKSV KPYATSDCSS KCNNRGVCNH ENKCHCDPGW APPYCDVLLS ELPRETGSVV LPVSLAVGFL LLLVLVFGGL MCYIKKRPPV KRCLQSASGQ SNPLFRSGSA RGSPRLGPAH IGQPVFVESS ATQACKPLFS SRATTAAPKP SRAAPEPPKN PKPVAQPSQV QQVPRPPSSV GAEVSCCMQS LAPQKKPLPP SRPLPPVASK PVVKSKPPVP PVKPKPSAYA SSLPHTQLTS VILKKGPWPS // ID I3JFY7_ORENI Unreviewed; 861 AA. AC I3JFY7; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 43. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSONIP00000007778}; GN Name=adam22 {ECO:0000313|Ensembl:ENSONIP00000007778}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000007778, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000007778} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERX01025210; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01025211; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01025212; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3JFY7; -. DR Ensembl; ENSONIT00000007783; ENSONIP00000007778; ENSONIG00000006173. DR GeneTree; ENSGT00910000144014; -. DR OMA; TRDRQCK; -. DR TreeFam; TF314733; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 861 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003672703. FT TRANSMEM 740 763 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 246 446 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 452 539 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 683 720 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 511 531 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 710 719 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 861 AA; 94548 MW; 9E78D367F04D4D14 CRC64; MVLLMRPRWW ISLLCVCELV HVGHQSSPNA GDGDALSSLK ALRDAGRFVG KEDTVPVRLL YSRHNHSQIT QDELSTRVKA TASSDSTQVN HVAQASFQVD AFGRKFILDV ELNHDLLSSG YVERHLSENG KTVITSGGEH CYYQGKVRNI PHSFVALSTC HGLHGMFFDG NHTYMIEPGG HGGSNGDIRI HMIYKSAGEE AINDLLGGAL PEPPFPSPPF PGSKVVHRRK KRQAPRLSRS VEDETKYIEL MVINDHLMYK KHRLSVGHTN NNAKTVVNIA DMIFREQLNT RIVLVAMETW SADNKFNIDD GDPMVTLKEF MKYRKDFIKE KCDSVHLFAG NRFHSSWGGA SYMGGVCSLT KGGGVNEYGK TNEMAITLAQ SLGQNIGIFS DKKRMLNGEC KCDDRWAGCI MDDIGFYLPK KFSDCNVEEY YNFLNSGGGA CLFNKPLKLL DPPECGNGFV EPGEECDCGS PAECAKEGEN CCKNCTLTQG SVCSNGLCCN NCQMEFKGVV CRDAVNDCDI PEICSGNSSQ CPPNVHKMDG YTCEKDQGRC FGGRCKTKDR QCKFIWGEKA TAADKFCYEK LNIEGTEKGN CGKDKDTWIQ CNKQDVHCGY LLCSNISPAP RLGELQGGLT SFSVAQHSAS LDCSGAHVVI DGDIDLGYVE DGTACGTDSI CFNHKCLPIQ QFNFSTCPGT TDKAICSGNG VCSNELKCVC NRGWTGENCS SMFPVAKPTA SVSGIDSTNI IIGAIAGSIL FLALILAVTA WCYKSYKQKC YVESEVHRRF CRQMPPGDYV TKPGDPDSFY SDMPPGVSTN SGCSSKKRSN GLSHSWSERI PDAKHITDIC ENGRPRSNSW QGKLCFFCFS G // ID I3JFY8_ORENI Unreviewed; 898 AA. AC I3JFY8; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 43. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSONIP00000007779}; GN Name=adam22 {ECO:0000313|Ensembl:ENSONIP00000007779}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000007779, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000007779} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERX01025210; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01025211; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01025212; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3JFY8; -. DR STRING; 8128.ENSONIP00000007779; -. DR Ensembl; ENSONIT00000007784; ENSONIP00000007779; ENSONIG00000006173. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; I3JFY8; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 698 721 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 202 402 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 408 495 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 639 676 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 467 487 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 666 675 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 898 AA; 99104 MW; 8262C3ADB1250751 CRC64; VGKEDTVPVR LLYSRHNHSQ ITQDELSTRV KATASSDSTQ VNHVAQASFQ VDAFGRKFIL DVELNHDLLS SGYVERHLSE NGKTVITSGG EHCYYQGKVR NIPHSFVALS TCHGLHGMFF DGNHTYMIEP GGHGGSNLNS NEKERKHEVK YMLLVLGLPL LYREFPFSWI NSTRIRISQK AFHKRKKRQA PRLSRSVEDE TKYIELMVIN DHLMYKKHRL SVGHTNNNAK TVVNIADMIF REQLNTRIVL VAMETWSADN KFNIDDGDPM VTLKEFMKYR KDFIKEKCDS VHLFAGNRFH SSWGGASYMG GVCSLTKGGG VNEYGKTNEM AITLAQSLGQ NIGIFSDKKR MLNGECKCDD RWAGCIMDDI GFYLPKKFSD CNVEEYYNFL NSGGGACLFN KPLKLLDPPE CGNGFVEPGE ECDCGSPAEC AKEGENCCKN CTLTQGSVCS NGLCCNNCQM EFKGVVCRDA VNDCDIPEIC SGNSSQCPPN VHKMDGYTCE KDQGRCFGGR CKTKDRQCKF IWGEKATAAD KFCYEKLNIE GTEKGNCGKD KDTWIQCNKQ DVHCGYLLCS NISPAPRLGE LQGGLTSFSV AQHSASLDCS GAHVVIDGDI DLGYVEDGTA CGTDSICFNH KCLPIQQFNF STCPGTTDKA ICSGNGVCSN ELKCVCNRGW TGENCSSMFP VAKPTASVSV SGIDSTNIII GAIAGSILFL ALILAVTAWC YKSYKQKWQM PPGDYVTKPG DPDSFYSDMP PGVSTNSGCS SKKRSACLSH LQICTPSFTP SIPSISQNLS QFAFRSNGLS HSWSERIPDA KHITDICENG RPRSNSWQGN LSGNRKKLKG KKFRARSNST ETLSPAKSPT SSTGSIASSR RYPYPMPPLP DDQRKANRQS ARLWETSI // ID I3JT76_ORENI Unreviewed; 801 AA. AC I3JT76; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=ADAM metallopeptidase domain 8a {ECO:0000313|Ensembl:ENSONIP00000012071}; GN Name=adam8 {ECO:0000313|Ensembl:ENSONIP00000012071}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000012071, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000012071} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERX01006355; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSONIT00000012080; ENSONIP00000012071; ENSONIG00000009606. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 801 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003673413. FT TRANSMEM 670 693 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 197 395 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 403 489 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 623 655 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 332 332 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 331 331 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 335 335 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 341 341 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 461 481 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 627 637 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 645 654 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 801 AA; 88260 MW; BC0BE71CE374CA14 CRC64; IWIFFSSWGI ITASVETLPH VIKYQTVIPQ RLKDSSLFND DAAAAATHKK YPDALQYSIW IAGQNHTLHL EKNKNLVGKT FSVTHYSDQG DQISTTPDLS VHCYYHGHIV GVEDSSASIG LCSGIKGFVR LRDQTYLIEP LGTDDEGLHA VYNYKHLRRK RSLCSHGNTT TFYDHVARPS GLFRLASLKA ARTKRPRTVE LVLVVDHREY KKFGSKKTIE ERALEIANHV DKLYRPVGIR VMLVGLDIWS YRDQIQVSTN PEVTLRRFLE WRQQHLLPRT KHDNAQFITA VDFDGSTVGL ANTNAMCTSN SGAVNEDHNT NAIGVASTIA HEMGHNLGLS HDTEDCVCGT SVSKKGCIMS ESVGLKYPEL FSSCSRQQLS KFLEEINPAC LLNTPSTARV YGGPVCGNAF LEPGEECDCG TVKECTNPCC NATTCKLNAG AQCAEGECCH NCQLKPTGSV CRPKAGDCDL AEYCTGFSSV CPTDAYTQNG LLCNHGTGYC YNGMCPSRRD HCKRLWGPDA EVASDACFYQ HEMPRPVCNP KLYNGTDQSC GTLFCSGGWE FPVTSRKSFY KVENGDMCNV ATMNPEDNYP EDLGMVPTGT KCGNNMVCYN QQCQEIKNIK TYGRNDCSAK CNNHGVCNHE SKCHCDPGWA PPFCDVEQSE LPQESGLVKF IVSLVTGLLL LLLVVIGSLM WYVRKRQPAK RAIVHISLQI PPIFRGTVQP VVSVEQRTTQ ASSWISTNQP APQTGALKPS RAAPEPPKKA AAVPQPSVFQ QSKPLPPSRP LPPLTTKPTM KPKPPMPPAK P // ID I3MW56_ICTTR Unreviewed; 771 AA. AC I3MW56; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 43. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSSTOP00000016351}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSSTOP00000016351}; OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) OS (Spermophilus tridecemlineatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; OC Sciuridae; Xerinae; Marmotini; Ictidomys. OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000016351, ECO:0000313|Proteomes:UP000005215}; RN [1] {ECO:0000313|Ensembl:ENSSTOP00000016351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Assembly & Analysis Group; RG Computational R&D Group; RG and Sequencing Platform; RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.; RT "The Draft Genome of Spermophilus tridecemlineatus."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSTOP00000016351} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTP01052403; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005328184.1; XM_005328127.1. DR STRING; 43179.ENSSTOP00000016351; -. DR Ensembl; ENSSTOT00000020353; ENSSTOP00000016351; ENSSTOG00000023746. DR GeneID; 101978297; -. DR CTD; 4185; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; I3MW56; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000005215; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005215}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005215}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 771 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003677534. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 241 440 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 446 533 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 675 712 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 505 525 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 702 711 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 771 AA; 83824 MW; 871738D0463733B1 CRC64; MRRLRRRAIA ALLLLLPLLP APGLGARDPV GALRWRGSPQ VGIVEAPEVT EPSRLVGESS GGEVRKQQLD TRVRQEPPGG PPVHLAQVSF VIPAFNSNFT LDLELNHHLL SSQYVERHFS REGTTQHSTG AGDHCYYQGK LRGSPHSFAA ISTCWGLHGV FSDGNLTYIV EPQEMAGPWG APQGPLPHLI YRTPLLPAPL GCREPGCLFA DPAHSAPPNR PKLRRKRQVR RGHPTVHSET KYVELIVIND HQLFEQMRQS VVLTSNFAKS VVNLADVIYK EQLNTRIVLV AMETWADGNK IQVQDDLLET LARLMVYRRE GLPEPSDATH LFSGRTFQST SSGAAYVGGI CSLSRGGGVN EYGNMGAMAV TLAQTLGQNL GMMWNKHRSS AGDCKCPDIW LGCIMEDTGF YLPRKFSRCS IDEYNQFLQE GGGSCLFNKP LKLLDPPECG NGFVEAGEEC DCGSVQECSR AGGNCCKKCT LTHDAMCSDG LCCRRCKYEP RGVSCREAVN ECDIAETCTG DSSQCPPNLH KLDGYYCDHE QGRCYGGRCK TRDRQCQALW GHVAADRFCY EKLNVEGTER GNCGRKGSGW VQCNKQDVLC GFLLCVNISG APRLGDLGGD ISSVTFYHQG KELDCRGGHV QLADGSDLSY VEDGTACGPN MLCLDHRCLP ASAFNFSTCP GSGERRICSH HGVCSNEGKC ICQPDWTGKD CSIHNPLPTS PPTGETERYK GPSGTNIIIG SIAGAVLVAA IVLGGTGWGF KNIRRGRSGG A // ID J9P0S1_CANLF Unreviewed; 946 AA. AC J9P0S1; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 28-MAR-2018, entry version 38. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSCAFP00000039144}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSCAFP00000039144, GN ECO:0000313|VGNC:VGNC:37580}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000039144, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000039144, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000039144, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000039144} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000039144}; RG Ensembl; RL Submitted (SEP-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEX03009298; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9615.ENSCAFP00000039144; -. DR MEROPS; M12.978; -. DR PaxDb; J9P0S1; -. DR Ensembl; ENSCAFT00000047142; ENSCAFP00000039144; ENSCAFG00000001852. DR VGNC; VGNC:37580; ADAM22. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; J9P0S1; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Reactome; R-CFA-5682910; LGI-ADAM interactions. DR Proteomes; UP000002254; Chromosome 14. DR Bgee; ENSCAFG00000001852; -. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 946 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003825494. FT TRANSMEM 740 763 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 242 441 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 447 534 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 506 526 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 946 AA; 104268 MW; DBBABBE364294C3F CRC64; MQAAAAAAAA SVPFLLLCAL GTCPPARCGR AGDASLTELE RRDENRFLER QSIVPLRLLY RSGGDDETGH DALDTRVRGH AAGGQLTHVD QASFQVDAFG TSFILDIMLN HDLLSSEYIE RHVEHGGKTV EVKGGEHCYY QGHVRGNPDS FVALSTCHGL HGMFYDGNHT YLIEPEENDT SQEDFHFHSV YKSRLFEFPL DDLPSEFQQV HITPPKFTLK PRPKRSKRQL RRHPRNVEEE TKYIELMIVN DHLMFKKHRL SVVHTNTYAK SVVNMADLIY KDQLKTRIVL VAMETWAADN KFAISENPLI TLREFMKYRR DFIKEKSDAV HLFSGSQFES SRSGAAYIGG ICSLLKGGGV NEFGKTDLMA VTLAQSLAHN IGIISDKRKL ASGECKCEDT WSGCIMGDTG YYLPKKFTQC NIEEYHDFLN SGGGACLFNK PSKLLDPPEC GNGFIETGEE CDCGTPAECV LEGAECCKKC TLTQESQCSD GLCCKKCKFQ PMGTVCREAV NDCDIRETCS GNSSQCAPNI HKMDGYSCDG IQGICFGGRC KTRDRQCKYI WGQKVMASDK YCYEKLNIEG TEKGNCGKDK DTWIQCNKRD VLCGYLLCTN IGNIPRLGEL DGEITSTLVV QQGRTLNCSG GHVKLEEDVD LGYVEDGTPC GPQMMCLEHR CLPVASFNFS TCLSNKEGTV CSGNGICSNE LKCVCNRHWI GADCSTYFPH NDDAKTGITL SGNGVAGTNI IIGIIAGTIL VLALILGITA WGYKNYREQR QLPQGDYVKK PGDGDSFYSD IPPGVSTNSA SSSKKRSNGL SHSWSERIPD TKHISDICEN GRPRSNSWQG NLGGNRKKIR GKRFRPRSNS TEREPQAPEP GHSLAQTVPS QGISPGGSDS PQTGSLDHRT LSPAKSPSSS TGSIASSRKY PYPMPPLPDE EKKVNRQSAR LWETSI // ID K7ETS4_PONAB Unreviewed; 943 AA. AC K7ETS4; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 28-MAR-2018, entry version 32. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSPPYP00000023947}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSPPYP00000023947}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000023947, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000023947, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000023947} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGA01257039; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257040; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257041; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257042; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257043; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257044; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257045; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257046; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257047; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01257048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9601.ENSPPYP00000023947; -. DR Ensembl; ENSPPYT00000033211; ENSPPYP00000023947; ENSPPYG00000017839. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; K7ETS4; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000001595; Chromosome 7. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 943 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003900904. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 943 AA; 104298 MW; 9FA6E053580BAE72 CRC64; MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFLERQSI VPLRLIYRSG GEDESRHDAL DTRVRGDPGG RQLTHVDQAS FQVDAFGTSF ILDVMLNHDL LSSEYIERHI ERGGKTVEVK GGEHCYYQGH IRGNPASFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PPKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR FRPRSNSTER EPQAPEPGHS LAQTVPSQGI SLGGSDTPQT GSLDHRTLSP AKSPSSSTGS IASSRKYPYP MPPLPDEDKK VNRQSARLWE TSI // ID K7GNP1_PIG Unreviewed; 835 AA. AC K7GNP1; K9IW78; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 2. DT 23-MAY-2018, entry version 39. DE SubName: Full=ADAM metallopeptidase domain 8 {ECO:0000313|EMBL:JAA53562.1, ECO:0000313|Ensembl:ENSSSCP00000029496}; GN Name=ADAM8 {ECO:0000313|EMBL:JAA53562.1, GN ECO:0000313|Ensembl:ENSSSCP00000029496}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000029496, ECO:0000313|Proteomes:UP000008227}; RN [1] {ECO:0000313|Ensembl:ENSSSCP00000029496, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000029496}; RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSSCP00000029496} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:JAA53562.1} RP NUCLEOTIDE SEQUENCE. RA Dawson H.D., Chen C.T.; RT "Global Gene Expression Profiling of Alveolar Macrophages by Deep RT Sequencing."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEMK02000097; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; GACC01000245; JAA53562.1; -; mRNA. DR RefSeq; XP_013849740.1; XM_013994286.1. DR MEROPS; M12.208; -. DR Ensembl; ENSSSCT00000033889; ENSSSCP00000029496; ENSSSCG00000010772. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Reactome; R-SSC-1474228; Degradation of the extracellular matrix. DR Reactome; R-SSC-6798695; Neutrophil degranulation. DR Proteomes; UP000008227; Chromosome 14. DR Bgee; ENSSSCG00000010772; -. DR GO; GO:0071133; C:alpha9-beta1 integrin-ADAM8 complex; IEA:Ensembl. DR GO; GO:0071065; C:alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0032127; C:dense core granule membrane; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl. DR GO; GO:0032010; C:phagolysosome; IEA:Ensembl. DR GO; GO:0002102; C:podosome; IEA:Ensembl. DR GO; GO:0042581; C:specific granule; IEA:Ensembl. DR GO; GO:0070820; C:tertiary granule; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl. DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl. DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl. DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl. DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEA:Ensembl. DR GO; GO:0048247; P:lymphocyte chemotaxis; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0002675; P:positive regulation of acute inflammatory response; IEA:Ensembl. DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl. DR GO; GO:2000418; P:positive regulation of eosinophil migration; IEA:Ensembl. DR GO; GO:2000415; P:positive regulation of fibronectin-dependent thymocyte migration; IEA:Ensembl. DR GO; GO:0045089; P:positive regulation of innate immune response; IEA:Ensembl. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl. DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl. DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IEA:Ensembl. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl. DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl. DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl. DR GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; IEA:Ensembl. DR GO; GO:2000309; P:positive regulation of tumor necrosis factor (ligand) superfamily member 11 production; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 835 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014580497. FT TRANSMEM 660 682 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 198 398 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 406 492 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 613 645 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 333 333 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 332 332 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 336 336 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 342 342 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 464 484 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 617 627 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 635 644 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 835 AA; 89323 MW; DC9D46B8FE165556 CRC64; MRGLELPLLA SLWLQVVAPR AALPHLEQYE VVWPRRLPGP RARRALPSPS GQYPESVSYV LEARGHAFTV HLRKNRDLVG SGYTETYTAT NGSQVTEQLQ RQDDCFYQGH VEGHQRSAVS LSTCSGLRGF FRAGSAVHLI EPLEGGGEEG RHALYQAEHL QQKARTCGVN DSSLESILGP RISAALRPRN WPLPRETRYV ELFVVTDSTE FRQLGSREAV RRRVLEVVNH VDKLYQELNF RVVLVGLEIW NSGDKIAISS DPDTTLNNFL AWRARDLASR HLHDNAQLIT GVDFTGTTVG LAKVSAMCSR DSGAVNQDHS HNPIGVASTM AHEMGHNLGM DHDENVQGCF CPVPQGGGGC VMAASLGSAF PRMFSQCSRT DLETFLEKPR TACLADAPDP DRLVGGPVCG NRFVERGEQC DCGPPEDCQN RCCNASTCLL AEGAECAHGA CCHECRVQLA GKPCRPPKDE CDLGEFCDGQ QALCPEDAFQ ENGTPCRGGY CYNGDCPTLA QRCQDLWGPG ARVAVEACYA NSISAGCVGG VSRGRTHRCG TLFCEGGQKP LERSSCTLTS HSGTCQALNQ DDSAEYEPVP EGTRCGSEQV CWKGLCQDLH VYRSRNCSAR CNNHGVCNHK DQCHCHPGWA PPHCAELLST AHPASGSLQI GLVVPLVLLG ALVLAVAAVG IYRRTRSPVQ GRNVGPKTAV GLSNPLFPGG HGTPGASKAP APSVCPPELV PASDPSQHPK PTASPLTPKR PPPAPPAAMS SPLFPVPVYA PQAPGQLRPA PPAKPLPVLK PKQVVKPNCA PPMPPVKPGA GGAQPGPPQG AAGPKVALKP PVQRR // ID L5MDT0_MYODS Unreviewed; 1042 AA. AC L5MDT0; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 23-MAY-2018, entry version 31. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 8 {ECO:0000313|EMBL:ELK36784.1}; GN ORFNames=MDA_GLEAN10021254 {ECO:0000313|EMBL:ELK36784.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK36784.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB101169; ELK36784.1; -; Genomic_DNA. DR ProteinModelPortal; L5MDT0; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:ELK36784.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 1042 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003971121. FT TRANSMEM 659 682 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 198 398 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 406 492 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 614 646 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT COILED 989 1016 {ECO:0000256|SAM:Coils}. FT ACT_SITE 333 333 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 332 332 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 336 336 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 342 342 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 464 484 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 618 628 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 636 645 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1042 AA; 112078 MW; 017907D971A1F73F CRC64; MLHLGLWLLG VWWLQVAAPS PPLSHVEQYE VVRPQRLPGP RARRALPSSV GLYPESVSYV LGAPGNTFTL HLRKNRDLVG SGYTETYTAA NGSQVTEQLQ RQDHCFYQGH VEGHPLSAAS LSTCDGLRGF FQAGSAVHLI EPLDGSGEEG QHALYKAQHL QQKAGTCGVS NTSLESMLGP RTLAAFRPRN RPLSRKTRFV ELYVVTDSRE FQKLGSREAV RRRVLEVVNH VDKLYQELKF RVVLVGLDIW NHGDKIQVSS DASVTLDNFL TWRAQNLVGR HPHDNVQLIT GIDFAGSTVG LAKVSAMCSQ NSGAVNQDHS PNPIGVACTL AHEMGHNLGM DHDENVQGCY CPESRTRGGC VMAGSIGSTF PTLFSQCSQD DLETFVEKPR ITCIANAPDP DRLVGGPVCG NGFVEQGEQC DCGYPQDCRD RCCNTTTCQL AEGAECAHGA CCHECRVKPA GKLCRPGKDA CDLDEYCDGQ RPSCPEDAFQ ENGTPCPGGY CYNGACPTRA QRCQDLWGPG TQPARETCYS FNVLPGCQSN ARLGAERAGC ETLFCEGGQK PPERASCTFT YSSAICQALN LDGGSGFERV LEGTRCGNER VCWKGLCQDF HVYRSRNCSA QCNGHGVCNH KGQCHCQPGW APPHCTELLA ELRVASRSLL MGVVVPVVLL VTLALTVLGV VVHRKAGSRI RGRNVAPKTA MGLSNPLFQK RGFGPEKGMA PAPTTHSPEP VTTMSANHSG PLPRPTASAV TPTRPPPAPP ATMSSPLFPV PMYTQQSPAQ LRPAPPTKPL PEQKPRQVIK PTSVPPVPPV KPKAGGANPG TTENFTINLG LLGVSHQEDS TEGDIRKVVA NTPGAIEPIL CALKEKVVDA VREDPPGAGL LVGAFVPQPL KSLQDPGVSG ADADGLWLGL ATTPHAGSTQ TPDVCGKRAA ASRQACGALE FTHLQGRAGV LSSPVPSGVK TLQSQRAEKT GHYACRGRDP AGGPREHLNT GVQQLLEEKE QALAILQETV QVLQMKVIRL EHLVELKDRR ISELTRRGIE PQ // ID M0R5P8_RAT Unreviewed; 775 AA. AC M0R5P8; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 2. DT 23-MAY-2018, entry version 35. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSRNOP00000064723}; GN Name=Adam22 {ECO:0000313|Ensembl:ENSRNOP00000064723, GN ECO:0000313|RGD:1585016}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000064723, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000064723, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000064723, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000213|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., RA Lundby C., Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 RT different rat organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [3] {ECO:0000313|Ensembl:ENSRNOP00000064723} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000064723}; RG Ensembl; RL Submitted (FEB-2013) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABR07059516; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059517; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059518; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059519; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059520; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059521; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059522; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059523; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059524; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07059525; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSRNOT00000073501; ENSRNOP00000064723; ENSRNOG00000042478. DR RGD; 1585016; Adam22. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR Reactome; R-RNO-5682910; LGI-ADAM interactions. DR Proteomes; UP000002494; Chromosome 4. DR Bgee; ENSRNOG00000042478; -. DR ExpressionAtlas; M0R5P8; baseline and differential. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 606 629 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 108 307 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 313 400 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 544 581 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 372 392 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 571 580 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 775 AA; 85695 MW; 5C79086A31B3D0EA CRC64; QGGEHCYYQG QIRGNPASFV ALSTCHGLQM FADCKHDEFS TPQRNTHIQE SQFHSVYKSR LLEFPLDDLP SEFQRINITA PQFTLKPRLK RRKRQLLRFP RNVEEETKYI ELMIVNDHLM FKKHRLSVVY TNTYAKSVVN MADVIYKDQL KTRIVLVAME TWAADNKFAI SENPLVTLRE FMKYRRDFIK EKADAVHLFS GSQFESSRSG AAYIGGICSL LRGGGVNEFG KTDLMAVTLA QSLAHNIGII SDKRKLASGE CKCEDTWSGC IMGDTGYYLP KKFTQCNIEE YHDFLNSGGG ACLFNKPSKL LDPPECGNGF IETGEECDCG TPAECALEGA ECCKKCTLTQ DSQCSDGLCC KKCKFQPLGT VCREAVNDCD IREICSGNSS QCAPNVHKMD GYSCDGTQGI CFGGRCKTRD RQCKYIWGQK VTASDRYCYE KLNIEGTEKG NCGKDKDTWT QCNKRDVLCG FLLCTNIGNI PRLGELDGEI TSTLVVQQGR TLNCSGGHVK LEEDVDLGYV EDGTPCGPQM MCLEHRCLPM ASFNFSTCLS NKAGTVCSGN GVCSNELKCV CNRHWTGADC GTHFPHNDDA KTGITLSGNG VAGTNIIIGI IAGTILVLAL ILGITAWGYK NYREQRQLPQ GDYVKKPGDG DSFYSDFPPG GSADSASSSK KRSNGLSHSW SERIPDTKHI SDICENGRPR SNSWQGNVGG NKKKIRGKRF RPRSNSTETL SPAKSPSSST GSIASSRKYP YPMPPLPDEE KTVNRQSARL WETSI // ID M3W439_FELCA Unreviewed; 872 AA. AC M3W439; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 23-MAY-2018, entry version 40. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSFCAP00000005067}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSFCAP00000005067}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000005067, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000005067, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005067, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000005067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005067}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000005067} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005067}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANG03038167; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AANG03038168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AANG03038169; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AANG03038170; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9685.ENSFCAP00000005067; -. DR Ensembl; ENSFCAT00000005466; ENSFCAP00000005067; ENSFCAG00000005464. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; M3W439; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000011712; Chromosome E1. DR Bgee; ENSFCAG00000005464; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 838 861 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 342 541 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 547 634 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 776 813 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 606 626 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 803 812 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 872 AA; 93781 MW; 1553B2C0670CFE3E CRC64; MAKAGAAXXX XXXXXXXXXA GGREGGTEGA CTHLSPSGPP TAASPLPPAN GLCRSLRVRG GSRDRRAGGK LLAPSPSGSS SAGDQIRPAP RGTPEWGMKC AHPSPKSPAP QWASACSYGL VSSGLGTRGP VGALHWRVSP QLGSPEAPEV TEPSRLVGES SGGEVRKQQL DTRVRQEPPG GPPVHLAQVS FVIPAFNSNF TLDLELNHHL LSSQYVERHF SREGTTQHST GAGDHCYYQG KLRGNPHSFA ALSTCQGLHG VFSDGNFTYI VEPREMARPQ EPPQGPLPHL IYRTPLLPAP LGCREPGCLF AAPAHSAPVN RPRLRRKRQV RRGHPTVHSE TKYVELIVVN DHQLFEQMRQ SVVLTSNFAK SVVNLADVMY KEQLNTRIVL VAMETWADGD KIQVQDDLLE TLARLMVYRR EGLPEPSDAT HLFSGRTFQS TSSGAAYVGG ICSLSRGGGV NEYDNMGAMA VTLAQTLGQN LGMMWNKHRS SAGDCKCPDN WLGCIMEDTG FYLPRKFSRC SIDEYNQFLQ EGGGSCLFNK PLKLLDPPEC GNGFVEAGEE CDCGSVQECS RAGGNCCKKC TLTHDAMCSD GLCCRRCKYE PRGVSCREAV NECDIAETCT GDSSQCPPNL HKLDGYYCDH EQGRCYGGRC KTRDRQCQAL WGHAAADRFC YEKLNVEGTE RGNCGRKGSG WVQCNKQDVL CGFLLCVNIS GAPRLGDLGG DINSVTFYHQ GKELDCRGGH VQLADGSDLS YVEDGTACGP NMLCLDHRCL PASAFNFSTC PGSGERRICS HHGVCSNEGK CICQPDWTGK DCSIHNPLPT SPPTGETERY KGPSGTNIII GSIAGAVLVA AIVLGGTGWG FKNIRRGRSG GA // ID M3WZK6_FELCA Unreviewed; 943 AA. AC M3WZK6; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 23-MAY-2018, entry version 42. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSFCAP00000019797}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSFCAP00000019797}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000019797, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000019797, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000019797, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000019797} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000019797}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000019797} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000019797}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANG03321447; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AANG03321448; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AANG03321449; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AANG03321450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AANG03321451; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AANG03321452; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9685.ENSFCAP00000019797; -. DR Ensembl; ENSFCAT00000027901; ENSFCAP00000019797; ENSFCAG00000025413. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; M3WZK6; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000011712; Chromosome A2. DR Bgee; ENSFCAG00000025413; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 943 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014180020. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 702 711 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 943 AA; 103935 MW; 3E2B9C136F88AFCF CRC64; MQAAAAASVP FLLLCALGTC PPARCGRAGD ASLTELERRN ENRFLERQSI VPLRLLYRSG GEDETGHDAL DTRVRGHPGG GQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYVERYV EHGGKTVEVK GGEHCYYQGR VRGNPASFVA LSTCHGLHGM FYDGNHTYLI EPEENDTSQE DFHFHSVYKS RLFEFPLDDL PSEFQQVHIT PPKFILKPAP KRSKRQLRRH PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWAADNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGIQG ICFGGRCKTR DRQCKYIWGQ KVMASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNVGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SNKEGTVCSG NGVCSNELKC VCNRHWVGAD CSTYFPHNED SKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GISTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNRKKIRGKR FRPRSNSTER EPQAPEPGHS LAQTVPSQGI SPGGSDSPQT GSLDHRTLSP AKSPSSSTGS IASSRKYPYP MPPLPDEEKK VNRQSARLWE TSI // ID M3YCN9_MUSPF Unreviewed; 775 AA. AC M3YCN9; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 23-MAY-2018, entry version 37. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSMPUP00000009096}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSMPUP00000009096}; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000009096, ECO:0000313|Proteomes:UP000000715}; RN [1] {ECO:0000313|Ensembl:ENSMPUP00000009096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000009096}; RA Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S., RA Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E., RA Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J., RA Walker B.J., Young S., Birren B., Lindblad-Toh K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSMPUP00000009096} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYP01079309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_004772576.1; XM_004772519.2. DR STRING; 9669.ENSMPUP00000009096; -. DR MEROPS; M12.976; -. DR Ensembl; ENSMPUT00000009249; ENSMPUP00000009096; ENSMPUG00000009173. DR GeneID; 101674681; -. DR CTD; 4185; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; M3YCN9; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000000715; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000715}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000715}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 741 764 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 245 444 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 450 537 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 679 716 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 509 529 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 706 715 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 775 AA; 84333 MW; E1B362305AB4B989 CRC64; MRWTHPSPKS PAPRWASACS SGLVSPGLGT RGPFGALRWR VSPQLGQPGA PEVTEPSRLV GESSGGEVRK QQLDTRVRQE PPGGPPVHLA QVSFVIPAFN SNFTLDLELN HHLLSSQYVE RHFSREGTTQ HNTGAGDHCY YQGKLRGNPH SFAALSTCQG LHGVFSDGNF TYIVEPREMS RSQEPPQGPL PHLIYRTPLL PAPLGCREPG CLFAAPAHSA PVNRPRLRRK RQVRRGHPTV HSETKYVELI VVNDHQLFEQ MRQSVVLTSN FAKSVVNLAD VMYKEQLNTR IVLVAMETWA DGDKIQVQDD LLETLARLMV YRREGLPEPS DATHLFSGRT FQSASSGAAY VGGICSLSRG GGVNEYDNMG AMAVTLAQTL GQNLGMMWNK HRSSAGDCKC PDNWLGCIME DTGFYLPRKF SRCSIDEYNQ FLQEGGGSCL FNKPLKLLDP PECGNGFVEA GEECDCGSVQ ECSRAGGNCC KKCTLTHDAM CSDGLCCRRC KYEPRGVSCR EAVNECDIAE TCTGDSSQCP PNLHKLDGYY CDHEQGRCYG GRCKTRDRQC QALWGHAAAD RFCYEKLNVE GTERGNCGRK GSGWVQCNKQ DVLCGFLLCV NISGAPRLGD LGGDINSVTF YHQGKELDCR GGHVQLADGS DLSYVEDGTA CGPNMLCLDH RCLPASAFNF STCPGSGERR ICSHHGVCSN EGKCICQPDW TGKDCSIHNP LPTSPPTGET ERYKGPSGTN IIIGSIAGAV LVAAIVLGGT GWGFKNIRRG RSGGA // ID M3Z3N2_MUSPF Unreviewed; 943 AA. AC M3Z3N2; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 23-MAY-2018, entry version 38. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSMPUP00000018194}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSMPUP00000018194}; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000018194, ECO:0000313|Proteomes:UP000000715}; RN [1] {ECO:0000313|Ensembl:ENSMPUP00000018194} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000018194}; RA Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S., RA Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E., RA Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J., RA Walker B.J., Young S., Birren B., Lindblad-Toh K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSMPUP00000018194} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYP01005854; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01005855; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01005856; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01005857; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01005858; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01005859; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01005860; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01005861; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01005862; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9669.ENSMPUP00000018194; -. DR Ensembl; ENSMPUT00000018464; ENSMPUP00000018194; ENSMPUG00000018312. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; M3Z3N2; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000000715; Unassembled WGS sequence. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl. DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000715}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000715}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 943 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004045785. FT TRANSMEM 737 760 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 239 438 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 444 531 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 675 712 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 503 523 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 702 711 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 943 AA; 104003 MW; 0CB55726733A60AF CRC64; MQAAAAASVP FLLLCALGTC PPARCGRAGD ALLTELERRN ENRFLERQSI VPLRLLYRSG GEDETGHDAL DTRVRGHHGA GQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYVERHV EHGGKTVEVK GGEHCYYQGH IRGNPASFVA LSTCHGLHGM FYDGNHTYLI EPEENDTSQE DFHFHSVYKS RLFEFPLDDL PSEFQQVHIT PPKFILKPKP KRSKRQLRRH PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWAADNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVMASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG KTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SNKEGTVCSG NGVCSNELKC VCNRHWIGAD CSTYFPHNDD TKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIAP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNRKKIRGKR FRPRSNSTER EPQAPEPGHS LAQTVPSQGI SLGGSDSPQT GSLDHRTLSP AKSPSSSTGS IASSRKYPYP MPPLPDEEKK VNRQSARLWE TSI // ID M3ZXI4_XIPMA Unreviewed; 920 AA. AC M3ZXI4; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 23-MAY-2018, entry version 41. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSXMAP00000006928}; OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Xiphophorus. OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000006928, ECO:0000313|Proteomes:UP000002852}; RN [1] {ECO:0000313|Ensembl:ENSXMAP00000006928} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000006928}; RA Walter R., Schartl M., Warren W.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSXMAP00000006928} RP IDENTIFICATION. RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000006928}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAJ01025744; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGAJ01025745; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGAJ01025746; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGAJ01025747; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGAJ01025748; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGAJ01025749; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005809170.1; XM_005809113.1. DR STRING; 8083.ENSXMAP00000006928; -. DR Ensembl; ENSXMAT00000006936; ENSXMAP00000006928; ENSXMAG00000006881. DR GeneID; 102225300; -. DR KEGG; xma:102225300; -. DR CTD; 53616; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR InParanoid; M3ZXI4; -. DR KO; K16068; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000002852; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002852}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002852}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 920 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004046723. FT TRANSMEM 739 762 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 242 441 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 447 534 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 678 715 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 506 526 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 705 714 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 920 AA; 101581 MW; 2D84ED381DFCCF06 CRC64; MMLRMPWWIS LLCVCGLMHV GHQSSLDASN GDAFSSLKAL RDAGRFVGKE NTVPLRLVYS SQNHSQITHD ELSTRVKASP DSTQMEHVTQ ATFQVDAFGK TFILDVELNH DLLSSGYQER HLSENGKIFV TKGGEHCYYQ GRVRDAPRSF AALSTCHGLQ GMFFDGNHTY TIEPGGQANN SGNLHIHLIY KSAGQEELSD LFGGDLPEPP FPSPPFPESK VVHWRKKRQA PRLSRSVEDE TKYIELMVIN DHVMYKRHRL SVGHTNNNAK TVVNIADMIF REQLNTQIVL VAMETWSVDN KFNIDDDPMV TLKEFMKYRK DFIKEKCDSV HLFSGNQFHS NRGAVSYTGG VCSLTKGGGV NEYGKTNDMA ITLAQALGQN IGIFSDKKRI LNGECKCDDR WAGCIMDDVG FYLPKKFTDC NVEEYHNFLN SGGGACLFNK PMKLLDPPEC GNGILEAGEE CDCGSTEECA KEGENCCKNC TLTKGSNCSN GLCCRNCQME VMGVLCRDAV NDCDIPEKCT GNSSQCPPNV HKMDGYTCEK DQGRCFNGRC KTKDRQCKYI WGEKATAADK FCYEKLNIEG TEKGNCGKEK DTWIQCNKQD VHCGYLLCSN ISPAPRLGDL QGGLTSFSVA QHGAPLDCSG AHVLIDGDTD LGYVEDGTAC GTDSICLDHK CLPIEQFNFS TCPGTTAKTI CSGHGVCSNE LRCVCELGWT GDDCYSRSPF SNLVVGPTAP VSGITSTNII IGAITGSILF LALILAVTAW CYKSYKKRRY AESEVHRRFC RQIPPGDYVT KPGDADSFYS DMPPGVSTNS GCSSKKRSNG LSHSWSERIP DAKHITDICE NGRPRSNSWQ GNLSGNRKKL KGKKFRARSN STETLSPAKS PTSSTGSIAS SRRYPYPMPP LPDDQRKANR QSARLWETSI // ID P70534_RAT Unreviewed; 740 AA. AC P70534; D3ZSV4; DT 01-FEB-1997, integrated into UniProtKB/TrEMBL. DT 01-FEB-1997, sequence version 1. DT 23-MAY-2018, entry version 149. DE SubName: Full=ADAM metallopeptidase domain 3A {ECO:0000313|Ensembl:ENSRNOP00000023756}; DE SubName: Full=ADAM metallopeptidase domain 3A (Cyritestin 1) {ECO:0000313|EMBL:AAH78839.1}; DE SubName: Full=Transmembrane protein tMDC I {ECO:0000313|EMBL:CAA69210.1}; GN Name=Adam3a {ECO:0000313|EMBL:AAH78839.1, GN ECO:0000313|Ensembl:ENSRNOP00000023756, ECO:0000313|RGD:621469}; GN Synonyms=Adam3 {ECO:0000313|RGD:621469}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:CAA69210.1}; RN [1] {ECO:0000313|EMBL:CAA69210.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sprague Dawley {ECO:0000313|EMBL:CAA69210.1}; RC TISSUE=Testis {ECO:0000313|EMBL:CAA69210.1}; RX PubMed=9291465; RX DOI=10.1002/(SICI)1098-2795(199710)48:2<159::AID-MRD3>3.3.CO;2-L; RA Frayne J., Jury J.A., Barker H.L., Hall L.; RT "Rat MDC family of proteins: sequence analysis, tissue distribution, RT and expression in prepubertal and adult rat testis."; RL Mol. Reprod. Dev. 48:159-167(1997). RN [2] {ECO:0000313|EMBL:AAH78839.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis {ECO:0000313|EMBL:AAH78839.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., RA Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., RA Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., RA Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., RA Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., RA Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., RA Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., RA Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., RA Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., RA Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., RA Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., RA Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., RA Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., RA Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., RA Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., RA Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., RA Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., RA Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., RA Makowski K.A., Bosak S., Malek J.; RT "The status, 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] {ECO:0000313|Ensembl:ENSRNOP00000023756, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000023756, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [4] {ECO:0000313|Ensembl:ENSRNOP00000023756} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000023756}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC107411; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC132163; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC078839; AAH78839.1; -; mRNA. DR EMBL; Y07903; CAA69210.1; -; mRNA. DR RefSeq; NP_064698.1; NM_020302.2. DR UniGene; Rn.42918; -. DR STRING; 10116.ENSRNOP00000023756; -. DR MEROPS; M12.951; -. DR Ensembl; ENSRNOT00000023756; ENSRNOP00000023756; ENSRNOG00000017554. DR GeneID; 57021; -. DR KEGG; rno:57021; -. DR UCSC; RGD:621469; rat. DR CTD; 1587; -. DR RGD; 621469; Adam3a. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR HOGENOM; HOG000230883; -. DR HOVERGEN; HBG103628; -. DR Proteomes; UP000002494; Chromosome 16. DR Bgee; ENSRNOG00000017554; -. DR ExpressionAtlas; P70534; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008584; P:male gonad development; IEP:RGD. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 740 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014306651. FT TRANSMEM 691 710 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 187 384 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 395 484 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 620 654 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 340 345 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 456 476 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 644 653 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 740 AA; 82532 MW; C7FE16CB81E028E2 CRC64; MLPLFLVLSC LGQLIAVGKD IETPLIQITV PEKIETNIKD AKESETQVTY VIRIEGKAYT LQLEKQSFLH PHFVTNLHNK LGTLQPYFSL VKSHCFYQGH AVEIPASTVT LSTCSGLRGL LQLENVTYGI EPLESSTTLE HILYEIQNHK IDYSPLKENY TNSQDESGSY RILVKPLKSS NSKLRKRILT VKIIMDKGMF DHVGSEVGVA TQKVVQMFGL INTMFSQLKM TVMLNSLEIW SEENKIETNG DADEVLQRFL LWTHKEMPQT TKEITYLLLY KDHPDYVGAT YHGMACNPKF TAGIALHPKT LGVEGFAIVL SQLLGINLGL TYDDIYNCFC RGSTCIMNPS AIHSEGIKVF SSCSMDEFRQ LASQPDLDCL LKTQETEVVA LPQAAKVCGN YILEPPEQCD CGPAERCSHK KCCKSEDCTL LSDAECGSGA CCDKRTCKIA ERGRLCRKST DQCDFPEFCN GTSEFCVADI KAADLEPCNN ETAYCFKGVC QDRDRQCTDL FGKYAKGPNY VCAQEVNLQN DKFGNCHGRC NYSALFCGKA VCYWSFAELV KTDVFDVQYT YLGGQVCVSA HLRVRNDETK DDTYVRDGTI CGNGQVCYRG ECLRVHVLRG DRECEADDKC QGHGICNNQN NCQCEAGFAP PECDMTPSSP GGSMDDGFWL PLDKSTPLVI KRPGTQYKKG LLISFYVFLP FLIVTAIMVV KQNISKMFGQ GEEEFSEGSI SEEINDSKQS // ID Q7KUY7_DROME Unreviewed; 837 AA. AC Q7KUY7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 2. DT 23-MAY-2018, entry version 130. DE SubName: Full=Mind-meld, isoform B {ECO:0000313|EMBL:AAS65376.2}; DE EC=3.4.24.- {ECO:0000313|EMBL:AAS65376.2}; GN Name=mmd {ECO:0000313|EMBL:AAS65376.2, GN ECO:0000313|FlyBase:FBgn0259110}; GN Synonyms=CG15603 {ECO:0000313|EMBL:AAS65376.2}, GN CG15604 {ECO:0000313|EMBL:AAS65376.2}, GN CG9163 {ECO:0000313|EMBL:AAS65376.2}, GN CT26192 {ECO:0000313|EMBL:AAS65376.2}, GN Dmel\CG42252 {ECO:0000313|EMBL:AAS65376.2}; GN ORFNames=CG42252 {ECO:0000313|EMBL:AAS65376.2, GN ECO:0000313|FlyBase:FBgn0259110}, GN Dmel_CG42252 {ECO:0000313|EMBL:AAS65376.2}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAS65376.2, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAS65376.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX 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., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., 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., 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., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., RA 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] {ECO:0000313|EMBL:AAS65376.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAS65376.2, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; 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., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., 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] {ECO:0000313|EMBL:AAS65376.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AAS65376.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAS65376.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AAS65376.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:AAS65376.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014298; AAS65376.2; -; Genomic_DNA. DR RefSeq; NP_996475.2; NM_206752.3. DR ProteinModelPortal; Q7KUY7; -. DR PRIDE; Q7KUY7; -. DR EnsemblMetazoa; FBtr0299534; FBpp0288809; FBgn0259110. DR EnsemblMetazoa; FBtr0310307; FBpp0301990; FBgn0259110. DR GeneID; 32561; -. DR UCSC; CG42252-RB; d. melanogaster. DR CTD; 23531; -. DR FlyBase; FBgn0259110; mmd. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR OMA; PKKHFHR; -. DR OrthoDB; EOG091G01L9; -. DR Reactome; R-DME-5682910; LGI-ADAM interactions. DR ChiTaRS; mmd; fly. DR GenomeRNAi; 32561; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0259110; -. DR ExpressionAtlas; Q7KUY7; baseline and differential. DR Genevisible; Q7KUY7; DM. DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:FlyBase. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Hydrolase {ECO:0000313|EMBL:AAS65376.2}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 837 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004290900. FT TRANSMEM 794 818 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 270 473 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 479 566 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 718 755 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 407 407 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 411 411 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 417 417 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 538 558 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 745 754 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 837 AA; 93091 MW; C83CCF53D4CD6A3F CRC64; MWINIANLIL IIAQLCVFVT SAGEADYTLD DSFWNEESPV GEVERLLKEY RQNQELVRRI GGHYYQIIYP VQLRHHEKMG ISTREVSLPK PGQRPRPHDD SGFNRGRTKK HFHRTSLLIK AFNHKFRLDL ELNSQLLSPN IQQKHYHVGG YLVDGNRHDI EHCYYHGTVK DYPGASAAFH TCNGVSGVIH IGNETFVIHP FYGGDLSKHP HVIFEARTKA NKGCANSGNL DSWRLSRRTK HLSAGVAGVV EEILQAGVGR NKRDVREATK YIETAIIVDK AMFDKRNGST RAEVIHDAIQ VANIADLYFR TLNTRVSVVY IETWGKNQAV IDGSKDISKA ISNFNDYTSR NLFQIERDTT QLLTGETFAG GEAGMAVPET VCTPRAVGIS VDVNVYEPHL LAGTMAHMIG HNIGMGHDDG REECFCRDWH GCIMAQSIVG QENVQPYKFS ECSKKDYIDA LRTGHGLCLL NKPNEIELRR NCGNKVVEED EECDCGTFEE CALDQCCDGI TCKLKSEAQC ASGACCDQCR LRPKDYICRD SNNECDLPEY CDGEIGQCPS DVFKKNGSPC GLSKTGISGY CFQGYCPTLS LQCEAIWGYG GSAADRQCYE QFNSKGSING HCGRDANEHY IKCEPENVQC GTLQCKDGER QPVNDGIDQL YSRTIISIKG QEFECKATSG QVGSNSYPEH GLVKDGTPCG DNLICLNQTC VSLFPHVDQT KCPANSQGLE CSEHGVCTNT NRCFCDMGWG GNDCSSVVLL TTALPTEALP TPENTIKMEK KETPYENYHG SNTVFLVGVL MSVVGFVFIT FTLMALCYRS VVVHRNFSLC LRLVEKK // ID Q7QI04_ANOGA Unreviewed; 1561 AA. AC Q7QI04; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 4. DT 23-MAY-2018, entry version 123. DE SubName: Full=AGAP000974-PA {ECO:0000313|EMBL:EAA04951.4}; GN Name=1270470 {ECO:0000313|VectorBase:AGAP000974-PA}; GN ORFNames=AgaP_AGAP000974 {ECO:0000313|EMBL:EAA04951.4}; OS Anopheles gambiae (African malaria mosquito). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea; OC Culicidae; Anophelinae; Anopheles. OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA04951.4, ECO:0000313|Proteomes:UP000007062}; RN [1] {ECO:0000313|EMBL:EAA04951.4, ECO:0000313|Proteomes:UP000007062, ECO:0000313|VectorBase:AGAP000974-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEST {ECO:0000313|EMBL:EAA04951.4, RC ECO:0000313|Proteomes:UP000007062}; RX 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.D., 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.D., Kokoza E., RA Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., RA Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., 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.J., Unger M.F., Walenz B., Wang A.H., RA Wang J., 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). RN [2] {ECO:0000313|EMBL:EAA04951.4} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA04951.4}; RG The Anopheles Genome Sequencing Consortium; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EAA04951.4} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA04951.4}; RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003; RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.; RT "The Anopheles gambiae genome: an update."; RL Trends Parasitol. 20:49-52(2004). RN [4] {ECO:0000313|EMBL:EAA04951.4} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA04951.4}; RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5; RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F., RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.; RT "Update of the Anopheles gambiae PEST genome assembly."; RL Genome Biol. 8:R5-R5(2007). RN [5] {ECO:0000313|EMBL:EAA04951.4} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA04951.4}; RG VectorBase; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|VectorBase:AGAP000974-PA} RP IDENTIFICATION. RC STRAIN=PEST {ECO:0000313|VectorBase:AGAP000974-PA}; RG VectorBase; RL Submitted (FEB-2017) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAAB01008811; EAA04951.4; -; Genomic_DNA. DR RefSeq; XP_309168.4; XM_309168.4. DR ProteinModelPortal; Q7QI04; -. DR EnsemblMetazoa; AGAP000974-RA; AGAP000974-PA; AGAP000974. DR GeneID; 1270470; -. DR KEGG; aga:AgaP_AGAP000974; -. DR VectorBase; AGAP000974-RA; AGAP000974-PA; AGAP000974. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR HOGENOM; HOG000082378; -. DR InParanoid; Q7QI04; -. DR OrthoDB; EOG091G01L9; -. DR PhylomeDB; Q7QI04; -. DR Proteomes; UP000007062; Chromosome X. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007062}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000007062}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 1561 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014588530. FT TRANSMEM 778 802 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 250 454 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 460 548 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 701 738 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 388 388 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 392 392 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 398 398 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 520 540 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 728 737 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1561 AA; 170022 MW; F45582CB83A315D6 CRC64; MKLMSPLRAL LLALVMTLAE SAGEADYTLD DSFWNEESPV GEVERLLKEH QQNQELVDKI GSSYYQIIYP VQLRHHEKMG ISTREVNQPK TGKHFHRTSL LIKAFNHKFR LDLELNTQLL APNIVQKHYL PSGFAQDSHR EIEHCYYHGT VKDYPGASAA FHTCNGVSGV IHVGNETFVI HPFYGGDLSK HPHVIFEART KSNKGCANSG NLEWRTRSIR RGSSHHAGLV ELIDRNGAGR YRRDVRETTK YIETALIIDK AMFQKRNGST RTEVVHDAIQ VANIADLYFR TLNTRVSVVY IETWQGQNQA QIDGGKDISK AISNFNDYTS RNLYKIDKDT TQLLTGETFA GGEVGMSVPE TVCTPKAVGI SVDMNPYEPH LLAGTMAHMI GHNIGMGHDD NRDECICRDW HGCIMSQSIV GLENVQPYKF SECSRLDYID ALRIGHGLCL LNKPNEVELR KNCGNGIVED DEECDCGSAL DCDKTDPCCD GITCKLKKES QCATGPCCDK CILKPPGVIC RDAHNECDLP EYCNGESGQC PPDVHKKNGN PCGMNSTGFS TGYCFNGVCP TQAAQCERIW GYSGTGADRV CYEQFNSKGS INGHCGKDAN GNYIKCEPEN IQCGSLQCKD GDRTPVEDCC EHLYSRAIIS IRGTEYECKS ITGASTNSNT PPYGLVRDGT PCGDNLICVN QTCVSIFPYI DQTKCPTNHN NLECSGNGDC TNNNKCFCKF GWTGPDCSIQ AHITTTYPSL ITSTTSESTI IMEKKTTRYA NYHGSNTVFL VGVLMSVVGG VFITFALMAL CYRSKTTRLK YDPPYVKKPM AKYVGGATAA NHHSQDDVSL EGSNKMMFGN QTTQFRDHKA IRRMTGSVSE DDPTHSGEEE TVSFIDLPPN SLLNKQMPEK GILKKHGLGL VLGDGTKDKW HAANDDAQSD NLELIAQQES TIPSSGGQVV VGGGGGVGVG GGVGGGVGGL GGPGVIGGVL GGGVGGGGGI IGSGGLGPGV GGVLGTVSDV ERTMKSLNGY HEDILEALRS AAQAQRSSAN TPSGSISEEL LRKTLAECVT GSQISAASVH PQDREYKRSV SSRTGSRENV CEPQPHVLSD AGQTATLLHH HRQQQQQQQQ QQQHQVQQGL LGDEDDTPSV GPLRIRNLED LIRQLEHHSS RHMSPSGSED IRMSETEADR HYRVDSSAAC SESSHGSNQQ LAQVQKTATI LPPYSSRCRP PRSDDEGRFS YGGAGGPGGG GGGGVMVGAG GGSGTVSGTG RYRHPASIRH QGHQSHSPHS PHSFAHHTHH GHAHGHSSHA GHSSHHSSHT HLHQDEEGIY ESADPVHPHA HPHDRSGLDQ RDTNDSERCL PTPTHPPNPH RHRSRSHRIH SLRLPFSFVR LVPEAKRSFQ TVCSFVVYRL RYHVFSDELF QAQQQLARWA SEDVVSVVVM EQGSDTSHAQ GPSSANTMHG HMQQHPSQQQ PPSHHQPPPQ PSQQQPPLQP PHQLIDSVNG VPVMGSCHSI SSSMNHQLVN NRDYYPSPPS TETESSGSVI QPLRRGPITP GPGPDGNHIM ESTGRYPEYK H // ID Q7TQG7_MOUSE Unreviewed; 778 AA. AC Q7TQG7; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 23-MAY-2018, entry version 133. DE SubName: Full=A disintegrin and metallopeptidase domain 11, isoform CRA_a {ECO:0000313|EMBL:EDL34149.1}; DE SubName: Full=Adam11 protein {ECO:0000313|EMBL:AAH54536.1}; DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11 {ECO:0000313|Ensembl:ENSMUSP00000069466}; GN Name=Adam11 {ECO:0000313|EMBL:AAH54536.1, GN ECO:0000313|Ensembl:ENSMUSP00000069466, ECO:0000313|MGI:MGI:1098667}; GN ORFNames=mCG_7457 {ECO:0000313|EMBL:EDL34149.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH54536.1}; RN [1] {ECO:0000313|EMBL:EDL34149.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mixed {ECO:0000313|EMBL:EDL34149.1}; RX PubMed=12040188; DOI=10.1126/science.1069193; RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R., RA Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A., RA Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W., RA Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K., RA Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J., RA Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R., RA Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H., RA Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A., RA Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A., RA Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C., RA Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C., RA Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B., RA Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E., RA Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R., RA Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C., RA Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L., RA Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S., RA Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L., RA Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R., RA Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R., RA Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J., RA Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L., RA Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C., RA Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A., RA Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H., RA Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L., RA Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M., RA Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K., RA Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S., RA Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J., RA Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G., RA Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.; RT "A comparison of whole-genome shotgun-derived mouse chromosome 16 and RT the human genome."; RL Science 296:1661-1671(2002). RN [2] {ECO:0000313|EMBL:AAH54536.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH54536.1}; RC TISSUE=Brain {ECO:0000313|EMBL:AAH54536.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., RA Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., RA Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., RA Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., RA Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., RA Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., RA Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., RA Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., RA Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., RA Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., RA Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., RA Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., RA Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., RA Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., RA Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., RA Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., RA Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., RA Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., RA Makowski K.A., Bosak S., Malek J.; RT "The status, 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] {ECO:0000313|EMBL:EDL34149.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mixed {ECO:0000313|EMBL:EDL34149.1}; RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSMUSP00000069466, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000069466, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] {ECO:0000313|Ensembl:ENSMUSP00000069466} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000069466}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL929067; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC054536; AAH54536.1; -; mRNA. DR EMBL; CH466558; EDL34149.1; -; Genomic_DNA. DR RefSeq; NP_001104248.1; NM_001110778.2. DR RefSeq; NP_033743.2; NM_009613.3. DR UniGene; Mm.89854; -. DR Ensembl; ENSMUST00000068150; ENSMUSP00000069466; ENSMUSG00000020926. DR GeneID; 11488; -. DR KEGG; mmu:11488; -. DR UCSC; uc007lsj.2; mouse. DR CTD; 4185; -. DR MGI; MGI:1098667; Adam11. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR HOGENOM; HOG000231962; -. DR HOVERGEN; HBG050456; -. DR KO; K16067; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR TreeFam; TF314733; -. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; ENSMUSG00000020926; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:EDL34149.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0000213|MaxQB:Q7TQG7, KW ECO:0000213|PeptideAtlas:Q7TQG7}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 778 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014588654. FT TRANSMEM 739 762 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 243 442 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 448 535 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 677 714 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 507 527 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 704 713 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 778 AA; 84822 MW; C6F1C1C4743F9F01 CRC64; MRRLRRWAIA ALLLLPLLPP PGLGALGPRG ALHWRSSAHV GSPESPEGSE VTEPSRLVRQ SSGGEVRKPQ LDTRVRQDPP RGTPVHLAQV SFVIPAFDSN FTLDLELNHH LLSSQYVERH FSREGTRQHS TGAGDHCYYH GKLRGNPQSF AALSTCQGLH GVFSDGNLTY IVEPKEIAGP WGPPQGPLPH LIYRTPLLPA PLGCREPGCL FAVPAQSALP NWPKLRRKRQ VRRGHPTVHS ETKYVELIVI NDHQLFEQMR QSVVLTSNFA KSVVNLADVI YKEQLNTRIV LVAMETWADG DKIQVQDDLL ETLARLMVYR REGLPEPSDA THLFSGRTFQ STSSGAAYVG GICSLSRGGG VNEYGNMGAM AVTLAQTLGQ NLGMMWNKHR SSAGDCKCPD IWLGCIMEDT GFYLPRKFSR CSIDEYNQFL QEGGGSCLFN KPLKLLDPPE CGNGFVEAGE ECDCGSVQEC SRAGGNCCKK CTLTHDAMCS DGLCCRRCKY EPRGVSCREA VNECDIAETC TGDSSQCPPN LHKLDGYYCD HEQGRCYGGR CKTRDRQCQA LWGHAAADRF CYEKLNVEGT ERGNCGRKGS GWVQCSKQDV LCGFLLCVNI SGAPRLGDLG GDISSVTFYH QGKELDCRGG HVQLADGSDL SYVEDGTACG PNMLCLDHRC LPASAFNFST CPGSGERRIC SHHGVCSNEG KCICQPDWTG KDCSIHNPLP TSPPTGETER YKGPSGTNII IGSIAGAVLV AAIVLGGTGW GFKNIRRGRY DPTQQGAV // ID S7PSR3_MYOBR Unreviewed; 996 AA. AC S7PSR3; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 23-MAY-2018, entry version 27. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 {ECO:0000313|EMBL:EPQ13903.1}; GN ORFNames=D623_10033833 {ECO:0000313|EMBL:EPQ13903.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ13903.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KE163803; EPQ13903.1; -; Genomic_DNA. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:EPQ13903.1}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 996 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004544039. FT TRANSMEM 736 759 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 238 437 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 443 530 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 674 711 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 502 522 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 701 710 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 996 AA; 109420 MW; 7015EF52DB271C38 CRC64; MQAAAASVPI LLLCALGTCP LVRGGRAGDA SLTELERRNE NGFLERQSIV PLRLLYRAGD EDETGHDKLT TRVRGDPRGA QLTHVNQASF QVDAFGTSFI LDVVLNHDLL SSEYIERHIE HGGKTVEVKG GEHCYYQGHI RGNLASFVAL STCHGLHGMF YDGNHTYLIE PEENDTSQED FRFHSVYKSR LFEFPLDDLP SEFQQVNITP PKFILKPRPK RTKRQLHRHP RNVEEETKYI ELMIVNDHLM FKKHRLSVVH TNTYAKSVVN MADLIYKDQL KTRIVLVAME TWAADNKFAI SENPLITLRE FMKYRRDFIK EKSDAVHLFS GSQFESSRSG AAYIGGICSL LKGGGVNEFG KTDLMAVTLA QSLAHNIGII SDKRKLASGE CKCEDTWSGC IMGDTGYYLP KKFTQCNVEE YHDFLNSGGG ACLFNKPSKL LDPPECGNGF IETGEECDCG TPAECVLEGA ECCKKCTLTQ DSQCSDGLCC KKCKFQPMGT VCREAVNDCD IRESCSGNSS QCAPNIHKMD GYSCDGVQGI CFGGRCKTRD RQCKYIWGQK VMASDKYCYE KLNIEGTEKG NCGRDKDTWI QCNKRDVLCG YLLCTNIGNI PRLGELDGEI TSTLVVQQGR TLNCSGGHVK LEEDVDLGYV EDGTPCGPRM MCLEHRCLPV ASFNFSTCLS NKEGIVCSGN GVCSNELKCV CNRHWTGADC STYFPLNDEE KTGITLSGNG VAGTNIIIGI IAGTILVLAL ILGMTAWGYK QLPQGDYVKK PGDGDSFYSD IPPGVSTNSA SSSKKRSNGL SHSWSERIPD TKHTDICENG RPRSNSWQGN VGGNRKKIRG KRFRPRSNST EREPQAPEPG HSLAQTVPSQ GISPGGSDSP QTGSLDHRTL SPAKSPSSST GSIASSRKYP YPMPPLPDEE KKVNRQSARG HHPEGLLSCL QALYAVAAPR GSSNLLTVLL GATVAASRRT YFSAGAHLLV SLWRPVSFTE VHPAET // ID T1G9B8_HELRO Unreviewed; 1002 AA. AC T1G9B8; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 23-MAY-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESN91736.1, ECO:0000313|EnsemblMetazoa:HelroP96397}; GN Name=20217665 {ECO:0000313|EnsemblMetazoa:HelroP96397}; GN ORFNames=HELRODRAFT_96397 {ECO:0000313|EMBL:ESN91736.1}; OS Helobdella robusta (Californian leech). OC Eukaryota; Metazoa; Lophotrochozoa; Annelida; Clitellata; Hirudinea; OC Rhynchobdellida; Glossiphoniidae; Helobdella. OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP96397, ECO:0000313|Proteomes:UP000015101}; RN [1] {ECO:0000313|EnsemblMetazoa:HelroP96397, ECO:0000313|Proteomes:UP000015101} RP NUCLEOTIDE SEQUENCE. RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., RA Otillar R.P., Terry A.Y., Boore J.L., Simakov O., Marletaz F., RA Cho S.-J., Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., RA Lv J., Arendt D., Savage R., Osoegawa K., de Jong P., Lindberg D.R., RA Seaver E.C., Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ESN91736.1, ECO:0000313|EnsemblMetazoa:HelroP96397, ECO:0000313|Proteomes:UP000015101} RP NUCLEOTIDE SEQUENCE. RX PubMed=23254933; DOI=10.1038/nature11696; RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P., RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R., RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., RA Aerts A., Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., RA Lindberg D.R., Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.; RT "Insights into bilaterian evolution from three spiralian genomes."; RL Nature 493:526-531(2013). RN [3] {ECO:0000313|EnsemblMetazoa:HelroP96397} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMQM01002175; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KB097700; ESN91736.1; -; Genomic_DNA. DR RefSeq; XP_009030549.1; XM_009032301.1. DR EnsemblMetazoa; HelroT96397; HelroP96397; HelroG96397. DR GeneID; 20217665; -. DR KEGG; hro:HELRODRAFT_96397; -. DR CTD; 20217665; -. DR KO; K06835; -. DR OMA; NFHSHSL; -. DR OrthoDB; EOG091G01O1; -. DR Proteomes; UP000015101; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000015101}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000015101}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 1002 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5010981191. FT TRANSMEM 729 754 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 231 429 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 436 524 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 679 710 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 368 368 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 367 367 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 371 371 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 377 377 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 384 408 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 386 391 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 496 516 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 700 709 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 1002 AA; 112990 MW; 85924FA6C632BBD3 CRC64; MKFFIKFRFC KIFCILLVLS LKKAVNGNLI VETQILDRYS SYNKTFVQLY DSTGKHIFST YDNQTQCHLR HIYVEFVLEN HKLTLDLQKN DFLFTPGYME RTSSSLLPSN YTSRNCYYIG ALLNDDRQLI PNVHVAVSTC KGLRGCVMLE NDTINIEPAT EDINDVHYFF RDSSRLRKTH HFNHSKLVVD DDDVSDDPHA MMKKKKYNPH RTHRLKKRSK NRPYDSNNET LIVELYVAND QAQFIRQGSN VQATIDRTKD AVNIVNSIYR QLNVYIVLIG VEVWNDIDRI QTTNDPQNLL NNFLKYREDF LNSWTPNDNA QLITGRNLGD GILGKAPVMT MCTWSKSGAI NVDHSLDVAR LAATMAHEIG HNFGLEHDDS VKEVTCPDEK CIMGPQSSEF IPARFSSNSK MVFKDLLDEG MRHCLQNSPH KVFGEGNDCG NGFINKGEDC DCGLPKDCTS KCCDPRTCKF LSRATCATGS CCNLDTCQIK PPMTECRGVQ SECDVGEYCD GESEFCPFDV FKHNGHPCTS FQKGAFCFDG QCRTHDTQCK RLYGVTGQQS ASMCYEQFNI DGSLRGNCGY KWEETKSYIK CNNSDVMCGL LHCQHSSEKM MFWDKTVSKD IIENIIFIQP GNIRYDCKTV MLDIDKDADN PGLVPNGASC GSNKMCMSQR CVDAREFVES LNCPECHNHG VCTNIGQCHC DVGYAPPHCD RSGFGGSLHS NAISDKSKVG ALVGVSIFVF IIFPCILIIA ILLYKRKHLI MKRLGLGKYR SVSRPTLPPR GEPVTNTYPR PPPPSYPQLA PPPPLPSGPP PFTTVPLMSS HSFSRPPNST KPLVNKLQSS KSFSQTSRTK PSIEMVHGNF VRPQPPVRPS RLPASTARSD EDTEVVGAND AGDLRSALTK LQELDFLNPK YTQRHHRETR LPRISKSDDD DESNHDYDHQ NRKHVPFRKA PPPPPQVKDT DMSEDEDCKQ NYQKASQAAK RQPSISKKPS FRPPPPPKPK PI // ID T1IEU1_RHOPR Unreviewed; 991 AA. AC T1IEU1; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 23-MAY-2018, entry version 34. DE SubName: Full=Uncharacterized protein (Fragment) {ECO:0000313|EnsemblMetazoa:RPRC014810-PA}; DE Flags: Fragment; OS Rhodnius prolixus (Triatomid bug). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Paraneoptera; Hemiptera; Heteroptera; OC Panheteroptera; Cimicomorpha; Reduviidae; Triatominae; Rhodnius. OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC014810-PA, ECO:0000313|Proteomes:UP000015103}; RN [1] {ECO:0000313|EnsemblMetazoa:RPRC014810-PA} RP NUCLEOTIDE SEQUENCE. RA Syromyatnikov M.Y., Popov V.N.; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:RPRC014810-PA} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (MAY-2015) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACPB03017714; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACPB03017715; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACPB03017716; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACPB03017717; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EnsemblMetazoa; RPRC014810-RA; RPRC014810-PA; RPRC014810. DR VectorBase; RPRC014810-RA; RPRC014810-PA; RPRC014810. DR OMA; QCFEQFN; -. DR Proteomes; UP000015103; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000015103}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000015103}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 645 669 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 316 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 322 410 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 559 596 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT METAL 250 250 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 254 254 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 260 260 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 382 402 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 586 595 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 991 AA; 108399 MW; FF67CF7846CB4CD1 CRC64; ITSKSFLFQE IEHCYYHGTV KDYPGATAAF HTCNGVSGVI HVGNETFVIQ PFYGGDLSKH PHVIFESRIK TNKGCANAGN LEWRSFRRAK HLSNLVEAAN RRFRRDVAEA TKYIETALVI DKAMFEKRNG STRAEVVHDA IQVANIADLY FRTLNTRVSV VYIETWQGAN QAVIDKTQDI SRALLNFNDY TSRNLFHIDK DTAQLLTGEI FQGGEAGMSV PETVCTPKSV GISVDVNAYE LYLLAGTMAH MIGHNIGMGH DGRREKCVCR DWHGCIMAQS IVGLENVQPY TFSECSRSDY NSALRTGHGI CLLNKPNELE VRRTCGNNVV EEGEDCDCGM IPECQDIDPC CDPYTCKLKK EAECASGPCC VACKLKKGGT VCREASNECD LPEHCTGEHG QCPLDVHKKN GNPCASESGY CFNGICPTLD LQCKQIWGYD GVAGDIECYK QFNSKGSFSG HCGYDSDKKA FIKCDKENSR CGSLQCQRGS SYPLVAGVDQ LYSRTIISTK GVEYECKATS GPVDQPDVPD LGLVRDGTPC GENLICVNQT CTSIFPHMDQ GTCPSNHNKL ECSGNGVCTN VNKCYCFLGW SGPDCSIQVE IIISPSPEAT AYPGSGQSQS DKADIEKQMN KKETPYENSH STNTVFLVGT LMSVVGGVFI VFALSALCYR SVVVHKNFSL CLRRSTVPRM DPPYNKKPIV KGFGTSAQQT PEGAVAMSAP NKLLGFGHIA GQRVLFRPNH MVPGGPASRF QEHKLQQMKR MGVGSGSEDD PGHSGEEETV SFIDLPPNNL SKLPEKGILK KSCPYGGGGG SDDPCHKGSK WLDDTQSDAQ EMLSQSDNNL TAEMISGGPI LEVERNLKTL NGYHEDILEA LRSAASRHHS GGPSSVTASS DDLLRRSLAA AAALEAGYVR GSSQDKLCTD ASKYTVFSKS LVRNEEEDED VPPCGPIRIR NLEDLIRQLE HKTTRHMSPS GSEDIRMSET EADRHYNRLD S // ID U3JVL9_FICAL Unreviewed; 626 AA. AC U3JVL9; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 23-MAY-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFALP00000006823}; OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; OC Ficedula. OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000006823, ECO:0000313|Proteomes:UP000016665}; RN [1] {ECO:0000313|Ensembl:ENSFALP00000006823} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTO01021737; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSFALT00000006852; ENSFALP00000006823; ENSFALG00000006513. DR GeneTree; ENSGT00910000144019; -. DR OMA; PLYLEMH; -. DR OrthoDB; EOG091G02F0; -. DR Proteomes; UP000016665; Unplaced. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016665}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00276, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Reference proteome {ECO:0000313|Proteomes:UP000016665}. FT DOMAIN 144 341 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 351 438 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 578 612 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 297 302 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 602 611 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 626 AA; 68222 MW; C5C2E766EBB5FB9B CRC64; KEAASYLLRI EGRLYTIHLQ QHAFLSDDFQ TYLSSEKGSY PAPAHVEGGC HYWGYIDGFP SSAVSLSTCS GLRGLLQFEN VSYGIQPLGT PPASQHALYR LRDEQMAAAP PAHGPPKARL LSWDVLDTAQ QDDEPLSAAA QSPKYLTVYV VLDKALYSYM GSDPNAATQK IIQAFNLINS MFYPLNVTIV LSSLELWAEG DKVSTAGDIH DLLQRFLHWK ELSLEPQAYN IASLLGYRER GAFLGAAAPG QACQRGAAAT VALYHGNVTL ESFSVLLAQL LGHSLGMSLD SPQGCSCPGR VCTMSPEALH FSGAKAFSNC SIRAFETLLK RGRGACLFQS PRLQRPSRQS GAVCGNRVVE AGEQCDCGTA QECLQDRCCT DRCRLKPKAR CASGLCCKNC QFRRRNSLCR PAADSTCDLP EVCSGSSASC PPDVYLQDGQ DCGRGTGYCY QGRCQSSDLQ CKRFYGRDSK NAPVGCYEEI NAQRDRFGHC GFRDGHNLQP CAWRDLRCGK LICTYPSHKP FSAAAAAVIY AQVRQDLCVS LNYLNVPAWQ DPLLVPPGTK CGSGRLCINY TCHPLSVLGS SCDSKTNCNG HGVCNNKGSC HCHPGWQPPH CRRRGWRRAS SLEGGE // ID U6PSS2_HAECO Unreviewed; 1017 AA. AC U6PSS2; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 22-NOV-2017, entry version 22. DE SubName: Full=Peptidase M12B and Blood coagulation inhibitor and ADAM and EGF domain containing protein {ECO:0000313|EMBL:CDJ94468.1}; GN ORFNames=HCOI_01812200 {ECO:0000313|EMBL:CDJ94468.1}; OS Haemonchus contortus (Barber pole worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Trichostrongyloidea; Haemonchidae; Haemonchinae; OC Haemonchus. OX NCBI_TaxID=6289 {ECO:0000313|EMBL:CDJ94468.1, ECO:0000313|Proteomes:UP000025227}; RN [1] {ECO:0000313|Proteomes:UP000025227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISE/inbred ISE {ECO:0000313|Proteomes:UP000025227}; RX PubMed=23985316; DOI=10.1186/gb-2013-14-8-r88; RA Laing R., Kikuchi T., Martinelli A., Tsai I.J., Beech R.N., Redman E., RA Holroyd N., Bartley D.J., Beasley H., Britton C., Curran D., RA Devaney E., Gilabert A., Hunt M., Jackson F., Johnston S.L., RA Kryukov I., Li K., Morrison A.A., Reid A.J., Sargison N., RA Saunders G.I., Wasmuth J.D., Wolstenholme A., Berriman M., RA Gilleard J.S., Cotton J.A.; RT "The genome and transcriptome of Haemonchus contortus, a key model RT parasite for drug and vaccine discovery."; RL Genome Biol. 14:R88.01-R88.16(2013). RN [2] {ECO:0000313|Proteomes:UP000025227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISE/inbred ISE {ECO:0000313|Proteomes:UP000025227}; RA Huang N.-L., Huang M.-D., Chen T.-L.L., Huang A.H.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CDJ94468.1, ECO:0000313|Proteomes:UP000025227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISE/inbred ISE {ECO:0000313|EMBL:CDJ94468.1, RC ECO:0000313|Proteomes:UP000025227}; RA Laing R., Kikuchi T., Martinelli A., Tsai I.J., Beech R.N., Redman E., RA Holroyd N., Bartley D.J., Beasley H., Britton C., Curran D., RA Devaney E., Gilabert A., Jackson F., Hunt M., Johnston S., Kryukov I., RA Li K., Morrison A.A., Reid A.J., Sargison N., Saunders G., RA Wasmuth J.D., Wolstenholme A., Berriman M., Gilleard J.S., RA Cotton J.A.; RT "The genome and transcriptome of Haemonchus contortus: a key model RT parasite for drug and vaccine discovery."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HF966405; CDJ94468.1; -; Genomic_DNA. DR Proteomes; UP000025227; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000025227}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000025227}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 1017 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004679353. FT TRANSMEM 724 746 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 219 422 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 428 515 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 487 507 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 1017 AA; 112676 MW; BE66FCDCF21990A8 CRC64; MTTRFCYCLL FVVLFHVTYS TARVDFRQSS ANKAFIASIP DGDYEVVHPF QIRDKNERIG IDTRNYFLKA AEHYQHVTIV IRSNAVGRIK LVLERNNFIF LNRTSFHKLD SSGEHGFAQR IENCYYQGTV AGDPSSFVAL SSCNGLRGII AFSNGSTYGV WPLDVGDRGR RHPHILYKTH WTQEAKCGTS VAPIEHTIRR RMSRDHHRRH SRDLSKQTKY IELALVGDHE YVKQHGFSDE DSLTYMLEAV NIADLMFSRD LNVRLSVVYA EIWLDVQRVD LFEDIERTMS GVVDYSTGHI YNIAKDASVM FTGGSFANNE AVNAVFRSIC TARSTTIVKA IDAFAAQWAG QMLAESLGHL FGLEHDTQSC QCETDSSKHR CIMTDRPGMP GAPFSWQFSK CSIARMHGVW QSGHVQCLLN KPFQPSQLRE CGNGVVDGSE ECDCGSRETC TDPCCDPLTC TLRAHAQCAA HHQCCHRCEL RRSGEICRSA RSSCDVAETC DGKSGDCPPD GHLMDGTACG RAGQCWRGNC SDPHQQCQEI WGDSARVAEQ ECFKQNTRGH EYANCGTIDG TGTYRSCQQE HIRCGTLQCQ DGATTPSQSA LRAFTFQFLQ DDKQVQCKSI ADENVGLVKD GSSCGPGRLC VAGSCVEMSS VSTTITCPSN NHALQCSGHG DCTTTAICVC FAGWTGTACD VRSNTTMGKS RGQARTIVNV PSIAGGKTLD TATLLGILLI VGVVLLLLLV CLLFCYRRRS IVEIPTPSDE KLDDSVPDRT QRSIKFGSMP SWRDEKRKRK SNKHVYGALN RITEADERDS SSVKSRESGS QNAGSQLLFE PHQVIPYARS EISFTERVPD HIYESTVIMS NTSPFHIKRP MRSLNSWSQS PSASTEHLAP TPLRLNNIKQ LLRNLQTNDD GADEFRDNCI ELLDTRYALD AYGSSYKPIG EVCGEEELSG VEADHDHGSN TESSRGYDLE TRPPDSRLGV GDGESSPALG RGTCDFRQSP SLFNDSFKLE MSSSIHT // ID W5KLB4_ASTMX Unreviewed; 780 AA. AC W5KLB4; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 23-MAY-2018, entry version 36. DE SubName: Full=ADAM metallopeptidase domain 23 {ECO:0000313|Ensembl:ENSAMXP00000008376}; GN Name=ADAM23 (1 of many) {ECO:0000313|Ensembl:ENSAMXP00000008376}; OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes; OC Characoidei; Characidae; Characidae incertae sedis; Astyanax clade; OC Astyanax. OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000008376, ECO:0000313|Proteomes:UP000018467}; RN [1] {ECO:0000313|Ensembl:ENSAMXP00000008376, ECO:0000313|Proteomes:UP000018467} RP NUCLEOTIDE SEQUENCE. RC STRAIN=female {ECO:0000313|Ensembl:ENSAMXP00000008376}; RA Jeffery W., Warren W., Wilson R.K.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAMXP00000008376} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APWO01111754; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_007258029.1; XM_007257967.2. DR Ensembl; ENSAMXT00000008376; ENSAMXP00000008376; ENSAMXG00000007893. DR GeneID; 103039143; -. DR KEGG; amex:103039143; -. DR GeneTree; ENSGT00910000144014; -. DR KO; K06837; -. DR OMA; MELASWA; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000018467; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018467}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000018467}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 780 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004865209. FT TRANSMEM 743 766 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 250 447 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 453 538 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 682 719 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 510 530 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 709 718 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 780 AA; 85990 MW; 8303E0B8FCFB0B50 CRC64; MWLRFLSHLL VSVLVSGLRS SITTALLVEN EPGGDAVSVR VEQDATAPTH TRNESGQEVE QAITYPSRLI YFLNENSEST YHNLNTWAKT PGHQGQAVHL AQATFQLEAF GSRFILDLTL NNDLLSSDYV EIHYEDGKPI LSKGGEHCYY SGQVRGVEAS RVALSTCNGL HGMFDDGVYV YLIEPLKQTH SFEGAARPHT LRRTPSLLQS NDPQDEGDKV EPLLSELDDM SWLRRRKKRA IPRNVFEEMK YIELMIVSDH NMFKRHKTKQ QTKNFAKSVV NLVDAVFKEH LNTRVVLVAV EIWTDKDQIP ITVYPLEMLR NFSRYRQQHI KQHADAVHLF TNVTFHYHQS SIAFVGGMCS VSHGVGVNEY GSTWTMAVSL SQSLAQNLGI RWDVTSKNKE CGCVDSWVGC IMEDTGVQHP RKFSKCSISD YKEFLLKGGG SCLFNKPTKL FQTTECGNGY VEVGEECDCG VRAECYKECC KKCSLSNGAH CSDGPCCNST CLFYPRGYSC RFAVNDCDIS ETCSGDSGQC PPNLHKQDGH LCHLDQGRCY TGECKTRESQ CKYVWGPKSG SSEKFCYEKL NTEGSEKGNC GENGQKWIQC SKHDVFCGLL MCTNVGQVPR IGVIKGEITP TTFNHQGNLI ECSGGHVLLD DLTDLGYVED GTPCGPSMMC LDRKCLSIQS LNMSACPTGP NGRICSNHGV CNNEATCTCD TTWAGTDCSM ADPPKEPPPS EDDGPKGPSA TNLIIGSIAG AILVGAIVLG GTGWGFKAVK KGRFNENAAI // ID W5MA26_LEPOC Unreviewed; 866 AA. AC W5MA26; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 23-MAY-2018, entry version 32. DE SubName: Full=ADAM metallopeptidase domain 8a {ECO:0000313|Ensembl:ENSLOCP00000005235}; OS Lepisosteus oculatus (Spotted gar). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae; OC Lepisosteus. OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005235, ECO:0000313|Proteomes:UP000018468}; RN [1] {ECO:0000313|Ensembl:ENSLOCP00000005235, ECO:0000313|Proteomes:UP000018468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.; RT "The Draft Genome of Lepisosteus oculatus."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLOCP00000005235} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAT01025211; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_015201918.1; XM_015346432.1. DR Ensembl; ENSLOCT00000005243; ENSLOCP00000005235; ENSLOCG00000004374. DR GeneID; 102690734; -. DR CTD; 101; -. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000018468; Linkage group LG5. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018468}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000018468}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 866 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004865773. FT TRANSMEM 676 701 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 201 400 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 408 494 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 632 664 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 337 337 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 336 336 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 340 340 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 346 346 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 466 486 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 636 646 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 654 663 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 866 AA; 94490 MW; 84E24C7FCD25E12D CRC64; MCGIVLSSFI CISSWALLVN ALSSLPDVEK YEVISPRRLN NAREKRSLST DKRLYSEELR YALTIEGRNY TLHLEKNRNL LGKDYTETHY LKNGTEVTST PNLKDHCYYQ GHIQGMNDSS ASVEVCSGIR GLVRAGQKLF LIEPLGGSAD GEHALYRQEH LRRKRSACRE ANRTVFDKDP KPAGFIRIQS WRSAPVVKGP KYVELFLVVD NTEYKQHNKD MSQIRRRMMD VTNHIDKLYR TINIRVMLVG LEVWTDWDKI DVSTDPDKTL TRFLEWRKNV LLKKKRHDNA HFVTGISFVG STVGLANKFA MCTINSAGVN EDHNPNSIGL ASTIAHEMGH NLGMSHDTES CYCEKSLSPK GCVMAPSVGD VFPQSFSSCS QQELESFLNQ ISSACLNNVP SAGDLFGGPE CGNMFLEPGE ECDCGTVEEC RNPCCNATTC RLTEGAQCAQ GECCQACKLK PAGVVCRKSA GDCDLDDFCS GLSAECPKDD FKMNGLPCEN NQGYCFNGQC PTHLQHCQIL WGPGAQVAPD LCFKNNQQGN LHLFCKKTRY GPQPCAQEDV KCGKIHCTGG SDLPVTQSKY VLTMSWPQLL KCNVAEVTDT EAEDIGLVPT GTKCGDNKVC YGNACKDIAV YGTKGCSEKC NNHGVCNHER KCHCDPGWAP PYCDVKLSEL PQGGSAVVIA VSVVVTILVL LPLIVGGLIC CRRGRKEVYS SKKRAHSASG LSNPLFHGVS TKSSPRCAPP RISTPTFLES SASPLPCAPL RSTVTPSRAP PQPPPKIAAT QSAAKSSPIV KPSQPPPLPP PETVCFQAKP PAPKKPLPDL SVKQVAKPNS APPVPPVKPP GSAPHRKQPQ VAGKPKTALM PPVKPR // ID W5MA38_LEPOC Unreviewed; 875 AA. AC W5MA38; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 23-MAY-2018, entry version 31. DE SubName: Full=ADAM metallopeptidase domain 8a {ECO:0000313|Ensembl:ENSLOCP00000005247}; OS Lepisosteus oculatus (Spotted gar). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae; OC Lepisosteus. OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005247, ECO:0000313|Proteomes:UP000018468}; RN [1] {ECO:0000313|Ensembl:ENSLOCP00000005247, ECO:0000313|Proteomes:UP000018468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.; RT "The Draft Genome of Lepisosteus oculatus."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLOCP00000005247} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAT01025211; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSLOCT00000005255; ENSLOCP00000005247; ENSLOCG00000004374. DR GeneTree; ENSGT00910000144014; -. DR OMA; DENVQGC; -. DR OrthoDB; EOG091G01NX; -. DR Proteomes; UP000018468; Linkage group LG5. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018468}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Reference proteome {ECO:0000313|Proteomes:UP000018468}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT TRANSMEM 677 702 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 202 401 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 409 495 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 633 665 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT ACT_SITE 338 338 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 337 337 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 341 341 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 347 347 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 467 487 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 637 647 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 655 664 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 875 AA; 96160 MW; D3124E5F67CC800F CRC64; ASQNTIQMRI YIFTSLYATN IALSSLPDVE KYEVISPRRL NNAREKRSLS TDKRLYSEEL RYALTIEGRN YTLHLEKNRN LLGKDYTETH YLKNGTEVTS TPNLKDHCYY QGHIQGMNDS SASVEVCSGI RGLVRAGQKL FLIEPLGGSA DGEHALYRQE HLRRKRSACR EANRTVFDKD PKPAGFIRIQ SWRSAPVVKG PKYVELFLVV DNTEYKQHNK DMSQIRRRMM DVTNHIDKLY RTINIRVMLV GLEVWTDWDK IDVSTDPDKT LTRFLEWRKN VLLKKKRHDN AHFVTGISFV GSTVGLANKF AMCTINSAGV NEDHNPNSIG LASTIAHEMG HNLGMSHDTE SCYCEKSLSP KGCVMAPSVG DVFPQSFSSC SQQELESFLN QISSACLNNV PSAGDLFGGP ECGNMFLEPG EECDCGTVEE CRNPCCNATT CRLTEGAQCA QGECCQACKL KPAGVVCRKS AGDCDLDDFC SGLSAECPKD DFKMNGLPCE NNQGYCFNGQ CPTHLQHCQI LWGPGAQVAP DLCFKNNQQG NLHLFCKKTR YGPQPCAQED VKCGKIHCTG GSDLPVTQSK YVLTMSWPQL LKCNVAEVTD TEAEDIGLVP TGTKCGDNKV CYGNACKDIA VYGTKGCSEK CNNHGVCNHE RKCHCDPGWA PPYCDVKLSE LPQGGSAVVI AVSVVVTILV LLPLIVGGLI CCRRGRKEVY SSKKRAHSAS GLSNPLFHGV STKSSPRCAP PRISTPTFLE SSASPLPCAP LRSTVTPSRA PPQIVKPSQP PPLPPPETVC FQVKTHKYLM IKETGVLKIY VLYLFQAKPP APKKPLPDLS VKQVAKPNSA PPVPPVKPPG SAPHRKQPQV AGKPKTALMP PVKPR // ID W5PGS6_SHEEP Unreviewed; 772 AA. AC W5PGS6; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 23-MAY-2018, entry version 32. DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSOARP00000009642}; GN Name=ADAM11 {ECO:0000313|Ensembl:ENSOARP00000009642}; 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 {ECO:0000313|Ensembl:ENSOARP00000009642, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000009642, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000009642}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000009642} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMGL01018764; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSOART00000009781; ENSOARP00000009642; ENSOARG00000008974. DR GeneTree; ENSGT00910000144014; -. DR OMA; ICSHHGV; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000002356; Chromosome 11. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 733 756 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 237 436 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 442 529 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 671 708 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 501 521 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 698 707 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 772 AA; 83466 MW; EDC3F7DC28AEFD28 CRC64; HRWASVCSHG LLSPGVGTGG PAGALRWRVS PHLGGPEAPE VTEPSRLVGE SSGGEVRKQQ LDTRVRQEPP GGPPVHLAQV SFVIPAFNSN FTLDLELNHH LLSSQYVERH FSREGPTQHS TGAGDHCYYQ GKLRGNPHSF AALSTCQGLH GVFSDGNFTY IVEPREMAGP RENAQGPLPH LIYRTPLLIF SLPGPAGTLP PGCLFAAPDH PAPPNRPRLR RKRQVRRGHP TVHSETKYVE LIVINDHQLF GQMRQSVVLT SNFAKSVVNL ADVMYKEQLN TRIVLVAMET WADGDKIQVQ DDLLETLARL MVYRREGLPE ASDATHLFSG RTFQSTSSGA AYVGGICSLS RGGGVNEYDN MGAMAVTLAQ TLGQNLGMMW NKHRSSAGDC KCPDNWLGCI MEDTGFYLPR KFSRCSIDEY NQFLQEGGGS CLFNKPLKLL DPPECGGGGR GGGCEGGSGV PQECSRAGGN CCKKCTLTHD AMCSDGLCCR RCKYEPRGVS CREAVNECDI AETCTGDSSQ CPPNLHKLDG YYCDHEQGRC YGGRCKTRDR QCQALWGHAA ADRFCYEKLN VEGTERGNCG RKGSGWVQCN KQDVLCGFLL CVNISGAPRL GDLGGDISSV TFYHQGKELD CRGGHVQLAD GSDLSYVEDG TACGPNMLCL DHRCLPASAF NFSTCPGSGE RRICSHHGVC SNEGKCICQP DWTGKDCSIH NPLPTSPPTG ETERYKGPSG TNIIIGSIAG AVLVAAIVLG GTGWGFKNIR RGRYDPTQQG AV // ID W5PP68_SHEEP Unreviewed; 903 AA. AC W5PP68; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 23-MAY-2018, entry version 35. DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSOARP00000012244}; GN Name=ADAM22 {ECO:0000313|Ensembl:ENSOARP00000012244}; 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 {ECO:0000313|Ensembl:ENSOARP00000012244, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000012244, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000012244}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000012244} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMGL01088037; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01088038; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01088039; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01088040; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01088041; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01088042; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01088043; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSOART00000012420; ENSOARP00000012244; ENSOARG00000011416. DR GeneTree; ENSGT00910000144014; -. DR OMA; TRDRQCK; -. DR OrthoDB; EOG091G010C; -. DR Proteomes; UP000002356; Chromosome 4. DR ExpressionAtlas; W5PP68; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 734 757 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 236 435 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 441 528 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 672 709 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 500 520 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 699 708 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 903 AA; 100123 MW; 84A0C70BBA6509B3 CRC64; MDECPSGSLF SPFLPNSSFP SFLPEGDASL TELERRNENR FLERQSIVPL RLIYSSGGED ETGHDALDTR VRGDPSSGQL THVDQASFQL DAFGTSFILD VLLNHDLLSS EYVERHIEHG GKTVEVKGGE HCYYQGHIRG NPASFVALST CHGLHGMFYD GNHTYLIEPE GNDTSQEDFH VHSVYKSRLF EFPLDDLPSE FQQVNITPPK FILKPRPKRS KRQLRRYPRN VEEEIKYIEL MIVNDHLMFK KHRLSVVLTN TYAKSVVNMA DLIYKDQLKT RIVLVAMETW AADNKFAISE NPLITLREFM KYRRDFIKEK SDAVHLFSGS QFESSRSGAA YIGGICSLLK GGGVNEFGKT DLMAVTLAQS LAHNIGIISD KRKLASGECK CEDTWSGCIM GDTGYYLPKK FTQCNIEEYH DFLNSGGGAC LFNKPSKLLD PPECGNGFIE TGEECDCGTP AECVLEGAEC CKKCTLTQDS QCSDGLCCKK CKFQPMGTVC REAVNDCDIR ETCSGNSSQC APNIHKMDGY SCDGVQGICF GGRCKTRDRQ CKYIWGQNVM SSDKYCYEKL NIEGTEKGNC GRDKDTWIQC NKRDVLCGYL LCTNIGNIPR LGELDGEITS TLVVQQGRTL NCSGGHVKLD EDVDLGYVED GTPCGPKMMC LEHRCLPVAS FNFSTCLSNK EGTICSGNGV CSNELKCVCN RHWVGEDCST YFPYNDDAKA GITLSGNGVA GTNIIIGIIA GTILVLALIL GITAWGYKNY REQRQLPQGD YVKKPGDGDS FYSDIPPGVS TNSASSSKKR SNGLSHSWSE RIPDTKHISD ICENGRPRSN SWQGNLGGNR KKIRGKRFRP RSNSTETLSP AKSPSSSTGS IASSRKYPYP MPPLPDEEKK VNRQSARLWE TSI // ID A0A016SNK5_9BILA Unreviewed; 608 AA. AC A0A016SNK5; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 23-MAY-2018, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EYB92278.1}; GN Name=Acey_s0196.g1545 {ECO:0000313|EMBL:EYB92278.1}; GN ORFNames=Y032_0196g1545 {ECO:0000313|EMBL:EYB92278.1}; OS Ancylostoma ceylanicum. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; OC Ancylostoma. OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB92278.1, ECO:0000313|Proteomes:UP000024635}; RN [1] {ECO:0000313|Proteomes:UP000024635} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635}; RX PubMed=25730766; DOI=10.1038/ng.3237; RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W., RA Aroian R.V.; RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma RT ceylanicum identify infection-specific gene families."; RL Nat. Genet. 47:416-422(2015). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYB92278.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JARK01001532; EYB92278.1; -; Genomic_DNA. DR Proteomes; UP000024635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000024635}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000024635}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 339 360 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 43 130 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 283 315 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 102 122 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 287 297 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 305 314 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 608 AA; 67213 MW; E3C2CF00F52650AA CRC64; MGNQLKASPP SFWSDCSLRY LYNSFNRGVD LCLKNPPEKT IGGAKCGNGI VEPGEECDCG REQCSHSCCD GKTCRLAGDA ECADGDCCDF LTCKPKPRAT MCRAPVGICD LPEYCNGDTP DCPADFFIQN GDVCPGRKNE YCYEGQCGSR PDQCVSIWGP TGKEGDRACF QQNTNGIIQG NCGFDVHTRM FTRCLADDIM CGRLQCGTQA ERPIFGDPTT VTSAYTYVRV GTETHQCHVI KTTYVVGQKN KPDPGMVLDG SECGDNKICV NAKCKPLSEV SKTVSKCNDH CHYRGVCNNV GNCHCENGFG GIACEIPGFG GSVNSNPSST SRGITPSTVL LVLLAISSLA LILICSYYWF MKKRNLAGEF WEYMRKTLKL HGVLVPVRKA PPPPRRHMKR ESLNAMWGDG SVTYSVNERP PTLVPPAIPL MSVNAGTASP KPRSPDHLLA RVPSACNGTN NKATFTRMPS VRPKEPPPVI PSRPRDSKLE ELYKERGEEM GIKSIRRWYI DRYYPQACPG FWESPCHHGF RKSAARAGDV ATLLFPSNKY QWSFIHEKDL SIRLISGIPI GLGLGNKLHR KSQWFLVFIF TLTKTMPGQC LHNLRRYF // ID A0A016SPM3_9BILA Unreviewed; 606 AA. AC A0A016SPM3; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 23-MAY-2018, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EYB92279.1}; GN Name=Acey_s0196.g1545 {ECO:0000313|EMBL:EYB92279.1}; GN ORFNames=Y032_0196g1545 {ECO:0000313|EMBL:EYB92279.1}; OS Ancylostoma ceylanicum. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; OC Ancylostoma. OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB92279.1, ECO:0000313|Proteomes:UP000024635}; RN [1] {ECO:0000313|Proteomes:UP000024635} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635}; RX PubMed=25730766; DOI=10.1038/ng.3237; RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W., RA Aroian R.V.; RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma RT ceylanicum identify infection-specific gene families."; RL Nat. Genet. 47:416-422(2015). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYB92279.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JARK01001532; EYB92279.1; -; Genomic_DNA. DR Proteomes; UP000024635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000024635}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000024635}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 339 360 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 43 130 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 283 315 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 102 122 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 287 297 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 305 314 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 606 AA; 67013 MW; C63B41DD8E102745 CRC64; MGNQLKASPP SFWSDCSLRY LYNSFNRGVD LCLKNPPEKT IGGAKCGNGI VEPGEECDCG REQCSHSCCD GKTCRLAGDA ECADGDCCDF LTCKPKPRAT MCRAPVGICD LPEYCNGDTP DCPADFFIQN GDVCPGRKNE YCYEGQCGSR PDQCVSIWGP TGKEGDRACF QQNTNGIIQG NCGFDVHTRM FTRCLADDIM CGRLQCGTQA ERPIFGDPTT VTSAYTYVRV GTETHQCHVI KTTYVVGQKN KPDPGMVLDG SECGDNKICV NAKCKPLSEV SKTVSKCNDH CHYRGVCNNV GNCHCENGFG GIACEIPGFG GSVNSNPSST SRGITPSTVL LVLLAISSLA LILICSYYWF MKKRNLAGEF WEYMRKTLKL HGVLVPVRKA PPPPRRHMKR ESLNAMWGDG SVTYSVNERP PTLVPPAIPL MSVNAGTASP KPRSPDHLLA RVPSACNGTN NKATFTRMPS VRPKEPPPVI PSRPRDSKLE ELYKERGEEM GIKRRWYIDR YYPQACPGFW ESPCHHGFRK SAARAGDVAT LLFPSNKYQW SFIHEKDLSI RLISGIPIGL GLGNKLHRKS QWFLVFIFTL TKTMPGQCLH NLRRYF // ID A0A087TES2_9ARAC Unreviewed; 67 AA. AC A0A087TES2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 25-OCT-2017, entry version 11. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KFM63611.1}; DE Flags: Fragment; GN ORFNames=X975_19948 {ECO:0000313|EMBL:KFM63611.1}; OS Stegodyphus mimosarum. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Araneae; Araneomorphae; Entelegynae; Eresoidea; Eresidae; Stegodyphus. OX NCBI_TaxID=407821 {ECO:0000313|EMBL:KFM63611.1, ECO:0000313|Proteomes:UP000054359}; RN [1] {ECO:0000313|EMBL:KFM63611.1, ECO:0000313|Proteomes:UP000054359} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Bechsgaard J.; RT "Genome sequencing of Stegodyphus mimosarum."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK114886; KFM63611.1; -; Genomic_DNA. DR EnsemblMetazoa; KFM63611; KFM63611; X975_19948. DR Proteomes; UP000054359; Unassembled WGS sequence. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054359}; KW Integrin {ECO:0000313|EMBL:KFM63611.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000054359}. FT DOMAIN 1 35 Disintegrin. {ECO:0000259|SMART:SM00050}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFM63611.1}. FT NON_TER 67 67 {ECO:0000313|EMBL:KFM63611.1}. SQ SEQUENCE 67 AA; 7403 MW; D4EC497BDA5CB18E CRC64; QLRPSGHLCR PALTECDIPE FCDGKSGQCP TDLYRKNASP CNNGEGFCYH GDCPTPDSQC EYLWGYG // ID A0A087XX15_POEFO Unreviewed; 249 AA. AC A0A087XX15; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 2. DT 28-MAR-2018, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000010318}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000010318, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000010318, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000010318}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000010318} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYCK01001150; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000010333; ENSPFOP00000010318; ENSPFOG00000010357. DR GeneTree; ENSGT00910000144571; -. DR OMA; SHEECAL; -. DR OrthoDB; EOG091G01NX; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}. FT DOMAIN 50 136 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 108 128 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 249 AA; 26664 MW; BB19DC1F163A2AB7 CRC64; RLSRSISLTR RYPFPTVFSS CSKKDLMASF EKGVGMCLFN MPELKVLYGG QKCGNGYVEE GEECDCGEVE ECMNPCCNAT TCTLKGDAVC AHGHCCQDCQ LKPAGTPCRE PSNSCDLPEF CTGGSPHCPA NVYLHDGHSC LNVDGYCYNG ICQTHEQQCI TLWGQGAKPA PGICFERVNS AGDPYGNCGK DSKGSFAKCE ARDAKCGKIQ CQGGANRPVI GTNAVSIETN IPLQEGGRIL CRGTHVYLG // ID A0A091GQ46_BUCRH Unreviewed; 465 AA. AC A0A091GQ46; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 23-MAY-2018, entry version 20. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:KFO85289.1}; DE Flags: Fragment; GN ORFNames=N320_11262 {ECO:0000313|EMBL:KFO85289.1}; OS Buceros rhinoceros silvestris. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros. OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO85289.1, ECO:0000313|Proteomes:UP000054064}; RN [1] {ECO:0000313|EMBL:KFO85289.1, ECO:0000313|Proteomes:UP000054064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO85289.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL507355; KFO85289.1; -; Genomic_DNA. DR Proteomes; UP000054064; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054064}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KFO85289.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000054064}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 285 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 66 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 212 244 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 38 58 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 216 226 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 234 243 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFO85289.1}. FT NON_TER 465 465 {ECO:0000313|EMBL:KFO85289.1}. SQ SEQUENCE 465 AA; 50225 MW; 524431E81AEAC3AA CRC64; ECTNRCCNAT TCTLKPGAVC AHGLCCEDCQ LKPAGISCRE SSNSCDLPEF CTGASPHCPA NVYLHDGHAC HRVDGYCYNG ICQTHEQQCI TLWGQGAKPA PGICFERVNS AGDPYGNCGK DSKSSFAKCE PRDAKCGKIQ CQGGANRPVI GTNAVSIETN IPLQEGGKIL CRGTHVYLGD DMPDPGLVLS GTKCEDGKIC LNRRCQNTSV FGVHKCATKC HGRGVCNNKK NCHCEADWAP PYCDKPGFGG SVDSGPIRQA DNKSLTVGVL ITTLCLIFAG SVMYLKRKTF MRWLFTSKKT TIEKLRSVSP ARPSSSSEPH HVHTTSLSKN LIVKPQNINT PKRDGPRRPL PYQIIDISNP VKTRDLPQLK TPQRVLPPLP QLPCHQAGPE RPLPANPSLR FAQENHKPNP PRKPLPADPL TKARCHGAGT AAPGHTKPLP HVTPIRPAPK HPPQVSRSSN TADAK // ID A0A091NLX8_APAVI Unreviewed; 524 AA. AC A0A091NLX8; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 23-MAY-2018, entry version 25. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:KFP90758.1}; DE Flags: Fragment; GN ORFNames=N311_04769 {ECO:0000313|EMBL:KFP90758.1}; OS Apaloderma vittatum (Bar-tailed trogon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; OC Apaloderma. OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP90758.1, ECO:0000313|Proteomes:UP000054244}; RN [1] {ECO:0000313|EMBL:KFP90758.1, ECO:0000313|Proteomes:UP000054244} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP90758.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL388516; KFP90758.1; -; Genomic_DNA. DR RefSeq; XP_009871579.1; XM_009873277.1. DR GeneID; 104276828; -. DR CTD; 8038; -. DR Proteomes; UP000054244; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054244}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KFP90758.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000054244}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 324 344 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 39 125 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 271 303 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 97 117 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 275 285 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 293 302 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFP90758.1}. FT NON_TER 524 524 {ECO:0000313|EMBL:KFP90758.1}. SQ SEQUENCE 524 AA; 56512 MW; F34F04421A5F493A CRC64; YPFPMVFSSC SRKDLENSLE KGVGMCLFNL PEVKESFGGQ KCGNGYVEDG EECDCGEPDE CTNRCCNATT CALKPGAVCA HGLCCEDCQL KPAGISCRES SNSCDLPEFC TGASPHCPAN VYLHDGHGCH GGDGYCYNGI CQTHEQQCIT LWGQGAKPAP GICFERVNSA GDPYGNCGKD SKSSFAKCEP RDAKCGKIQC QGGASRPVIG TNAVSIETNI PLQEGGKILC RGTHVYLGDD MPDPGLVLSG TKCEDGKICL NRRCQNTSVF GVHKCATKCH GRGVCNNKKN CHCEADWAPP YCDKPGFGGS VDSGPIRQAD NKSLTVGVLI TILCLIFAGS IMYLKRKTFM KWLFTSKKTT IEKLRSVTPA RPSSSSEPNP VHTTSLSKNL ILKPQNTNVQ KRDSPRRPLP YQIIDISNPV KRHDLPQLKT PQRVLPPLPQ LPCHQAVPER PLPAHPSLRF AQENHKPNPP RKPLPADPLT KARCNGAAAA APAHAKALPH VTPVRPAPKH PPQVSRSSNT ADVK // ID A0A091TRN6_PHALP Unreviewed; 508 AA. AC A0A091TRN6; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 23-MAY-2018, entry version 21. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 19 {ECO:0000313|EMBL:KFQ80155.1}; GN ORFNames=N335_06177 {ECO:0000313|EMBL:KFQ80155.1}; OS Phaethon lepturus (White-tailed tropicbird). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Phaethontidae; OC Phaethon. OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ80155.1, ECO:0000313|Proteomes:UP000053638}; RN [1] {ECO:0000313|EMBL:KFQ80155.1, ECO:0000313|Proteomes:UP000053638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ80155.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK462747; KFQ80155.1; -; Genomic_DNA. DR PhylomeDB; A0A091TRN6; -. DR Proteomes; UP000053638; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR008979; Galactose-bd-like_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053638}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KFQ80155.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053638}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 268 292 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 68 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 216 248 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 40 60 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 220 230 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 238 247 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 508 AA; 55138 MW; 22E31CA1C53A1EB3 CRC64; MQECTNPCCN AHNCTLKEGA QCAHGDCCQS CKLKVAGTTC REAAGSCDLP EYCTGASPYC PANVYLLDGS SCAYGEAYCN NGMCMTHHQQ CVQLWGPGAW PAPDACFQDV NMAGNTYGNC GKDSQGRYVK CDKRDAMCGK IQCQSSAKKP QGTNTVSIDT TIRFNGREVK CRGTYMYTAK DDEEDLSDPG LVMTGTKCGD GMVCKDRRCQ NASLFELEKC VSRCNGHGVC NSNKNCHCDA GWAPPYCEKP GLGGSVDSGP VQRDNHEAIL ITLLLIFLLF LPALMMGVYF WYRRENSLLN KWIKEMRRRS QETCSRKSTG GHSKAAFTLR NISTSSHTNK APRAAFLPKP SAHQPGSQPV NIVHPLRPGP HSIPLRPRDP KPARPPPPAS KSPMGPTKTV VSQAKLPPPK KPLPCSPVRT PLGVVSLHTL CVIPKHQPPR RPLPGSPLLA KELPSAHGQT LLVMVPPTNF KASGTSAMSR PTRPLKPMPP QRPVPAIKVQ STSFPLKK // ID A0A091U7T3_PHALP Unreviewed; 527 AA. AC A0A091U7T3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 23-MAY-2018, entry version 25. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:KFQ70118.1}; DE Flags: Fragment; GN ORFNames=N335_12668 {ECO:0000313|EMBL:KFQ70118.1}; OS Phaethon lepturus (White-tailed tropicbird). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Phaethontidae; OC Phaethon. OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ70118.1, ECO:0000313|Proteomes:UP000053638}; RN [1] {ECO:0000313|EMBL:KFQ70118.1, ECO:0000313|Proteomes:UP000053638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ70118.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK440771; KFQ70118.1; -; Genomic_DNA. DR PhylomeDB; A0A091U7T3; -. DR Proteomes; UP000053638; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053638}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KFQ70118.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053638}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 327 347 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 42 128 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 274 306 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 100 120 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 278 288 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 296 305 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFQ70118.1}. FT NON_TER 527 527 {ECO:0000313|EMBL:KFQ70118.1}. SQ SEQUENCE 527 AA; 56939 MW; 303B920466DD0DEE CRC64; SSSYPFPMVF SSCSRKDLEN SLEKGVGMCL FNLPEVKESF GGQKCGNGYV EDGEECDCGE PDECTNRCCN ATTCTLKLGA VCAHGLCCED CQLKPAGISC RESSNSCDLP EFCTGASPHC PANVYLHDGH ACHGVDGYCY NGICQTHEQQ CITLWGQGAK PAPGICFERV NSAGDPYGNC GKDSKSSFAK CEPRDAKCGK IQCQGGANRP VIGTNAVSIE TNIPLQEGGK ILCRGTHVYL GDDMPDPGLV LSGTKCEDGK ICLNRQCQNT SVFGVHKCAT KCHGRGVCNN KKNCHCEADW APPYCDKPGF GGSMDSGPIR QADNKSLTVG VLITILCLIF AGSIMYLKRK TFMRWLFTSK KTTIEKLRSV SPARPSSSSE PNHVHTTSLS KNLIMKPQNK NIQKKDGPRR PLPYQIIDIS NPVKTHDLPQ LKTPQRVLPP LPQLPCHQAV PERPLPANPS LRFAQENHKP NPPRKPLPAD PLTKVRYTGA CPAAPGLAKA LPHVTPVRPA PKQPPQVSRS GNTADVK // ID A0A093DMS8_9AVES Unreviewed; 464 AA. AC A0A093DMS8; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 23-MAY-2018, entry version 23. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:KFV03289.1}; DE Flags: Fragment; GN ORFNames=N339_04467 {ECO:0000313|EMBL:KFV03289.1}; OS Pterocles gutturalis (yellow-throated sandgrouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; OC Pterocles. OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV03289.1, ECO:0000313|Proteomes:UP000053149}; RN [1] {ECO:0000313|EMBL:KFV03289.1, ECO:0000313|Proteomes:UP000053149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV03289.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL227035; KFV03289.1; -; Genomic_DNA. DR Proteomes; UP000053149; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053149}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KFV03289.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053149}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 326 346 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 41 127 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 273 305 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 99 119 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 277 287 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 295 304 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFV03289.1}. FT NON_TER 464 464 {ECO:0000313|EMBL:KFV03289.1}. SQ SEQUENCE 464 AA; 50210 MW; 43BDC5FFDEC00648 CRC64; TSYPFPMVFS SCSRKDLENS LEKGVGMCLF NLPEVKESFG GQKCGNGYVE DGEECDCGEP DECTNRCCNA TTCALKPGAV CAHGLCCEDC QLKPAGISCR ESSNSCDLPE FCTGASPHCP ANVYLHDGHA CHGVDGYCYN GICQTHEQQC ITLWGQGAKP APGICFERVN SAGDPYGNCG KDSKSSFAKC EPRDAKCGKI QCQGGANRPV IGTNAVSIET NIPLQEGGKI LCRGTHVYLG DDMPDPGLVL SGTKCEDGKI CLNRRCQNTS VFGVHKCATK CHGRGVCNNK KNCHCEADWA PPYCDQPGFG GSVDSGPVRQ ADNKSLTVGV LITILCLIFA GSIMYLKRKT FMRWLFTSKK TTIEKLRSVS PARPSSSSEP NHVHTTSLSK NLIVKPQNTN IQKRDAPRRP LPYQIIDISN PVKTQDLPPL KTPQRVLPPL PQPPCHQAVP ERPLPANPSL RFAQ // ID A0A093IHS5_FULGA Unreviewed; 465 AA. AC A0A093IHS5; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 23-MAY-2018, entry version 23. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:KFW02270.1}; DE Flags: Fragment; GN ORFNames=N327_02980 {ECO:0000313|EMBL:KFW02270.1}; OS Fulmarus glacialis (Northern fulmar). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae; OC Fulmarus. OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW02270.1, ECO:0000313|Proteomes:UP000053806}; RN [1] {ECO:0000313|EMBL:KFW02270.1, ECO:0000313|Proteomes:UP000053806} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW02270.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK594419; KFW02270.1; -; Genomic_DNA. DR RefSeq; XP_009573073.1; XM_009574778.1. DR GeneID; 104074608; -. DR CTD; 8038; -. DR Proteomes; UP000053806; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053806}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KFW02270.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053806}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 285 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 66 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 212 244 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 38 58 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 216 226 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 234 243 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFW02270.1}. FT NON_TER 465 465 {ECO:0000313|EMBL:KFW02270.1}. SQ SEQUENCE 465 AA; 50415 MW; 945F47E7226DFDC8 CRC64; ECTNRCCNAT TCTLKPGAVC AHGLCCEDCQ LKPAGISCRE SSNSCDLPEF CTGASPHCPA NVYLHDGHAC HRVDGYCYNG ICQTHEQQCI TLWGQGAKPA PGICFERVNS AGDPYGNCGK DSKSSFAKCE PRDAKCGKIQ CQGGANRPVI GTNAVSIETN IPLQEGGKIL CRGTHVYLGD DMPDPGLVLS GTKCEDGKIC LNRQCQNTSV FGVHKCATKC HGRGVCNNKK NCHCEADWAP PYCDKPGFGG SVDSGPIRQA DNKSLTIGVL ITILCLIFAG SIMYLKRKTF MRWLFTSKKT TIEKLRSVTP ARPSSSSEPN HVHTTSLSKN LIMKPQNTNI QKRDGPRRPL PYQIIDISNP VKTHDLPQLK TPQRVLPPLP QLPCHHAVPE RPLPANPSLR FAQENSKPNP PRKPLPADPL NKARYNSACT AVPGHTKALP HVTPVRPAPK HPPQVSRSSN TADVK // ID A0A094LPG7_9AVES Unreviewed; 465 AA. AC A0A094LPG7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 23-MAY-2018, entry version 20. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:KFZ65584.1}; DE Flags: Fragment; GN ORFNames=N338_02545 {ECO:0000313|EMBL:KFZ65584.1}; OS Podiceps cristatus (great crested grebe). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Podicipediformes; Podicipedidae; OC Podiceps. OX NCBI_TaxID=345573 {ECO:0000313|EMBL:KFZ65584.1, ECO:0000313|Proteomes:UP000053854}; RN [1] {ECO:0000313|EMBL:KFZ65584.1, ECO:0000313|Proteomes:UP000053854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N338 {ECO:0000313|EMBL:KFZ65584.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL274538; KFZ65584.1; -; Genomic_DNA. DR Proteomes; UP000053854; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053854}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:KFZ65584.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053854}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 285 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 66 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 212 244 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 38 58 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 216 226 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 234 243 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFZ65584.1}. FT NON_TER 465 465 {ECO:0000313|EMBL:KFZ65584.1}. SQ SEQUENCE 465 AA; 50334 MW; F7410D854B1C6D02 CRC64; ECTNRCCNAT TCTLKPGAVC AHGLCCEDCK LKPAGISCRE SSNSCDLPEF CTGASPHCPA NVYLHDGHAC HRVDGYCYNG ICQTHEQQCI TLWGQGAKPA PGICFERVNS AGDPYGNCGK DSKSSFAKCE PRDAKCGKIQ CQGGANRPVI GTNAVSIETN IPLQEGGKIL CRGTHVYLGD DMPDPGLVLS GTKCEDGKIC LNRRCQNTSV FGVHKCATKC HGRGVCNNKK NCHCEADWAP PYCDKPGFGG SMDSGPIRQA DNKSLTIGVL ITVLCLIFAG SIMYLKRKTF MRWLFTSKKT TIEKLRSVSP ARPSSSAEPN RVHTTSLSKN LIMKPQNTNI QKRDGPRRPL PYQIIDISNP VKTHDLPQLK TPQRVLPPLP QLPCHQAVPE RPLPAKPSLR FAQETPKPNP PRKPLPADPL NKARYSGAST PAPGHAKAPP HVTPLRPAPK HPPHVSRPGN TADVK // ID A0A0C2FGJ4_9BILA Unreviewed; 138 AA. AC A0A0C2FGJ4; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 25-OCT-2017, entry version 13. DE SubName: Full=Disintegrin {ECO:0000313|EMBL:KIH47715.1}; DE Flags: Fragment; GN ORFNames=ANCDUO_22221 {ECO:0000313|EMBL:KIH47715.1}; OS Ancylostoma duodenale. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; OC Ancylostoma. OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH47715.1, ECO:0000313|Proteomes:UP000054047}; RN [1] {ECO:0000313|EMBL:KIH47715.1, ECO:0000313|Proteomes:UP000054047} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH47715.1, RC ECO:0000313|Proteomes:UP000054047}; RA Mitreva M.; RT "Draft genome of the parsitic nematode Ancylostoma duodenale."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KN766838; KIH47715.1; -; Genomic_DNA. DR Proteomes; UP000054047; Unassembled WGS sequence. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054047}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW Integrin {ECO:0000313|EMBL:KIH47715.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000054047}. FT DOMAIN 4 91 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 63 83 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT NON_TER 1 1 {ECO:0000313|EMBL:KIH47715.1}. SQ SEQUENCE 138 AA; 14946 MW; C8DF498C3A4C5E0D CRC64; PSQLRECGNG VVDGSEECDC GTRETCTDPC CDPLTCTLRA HAQCAAHHQC CHRCELRKAG EVCRSARSAC DVAETCNGKS GDCPPDGHLV DGTACGRDGQ CWRGNCSDPH NQCQTIWGDV SELTQAKIRD KCLALRYR // ID A0A0N4T906_BRUPA Unreviewed; 298 AA. AC A0A0N4T906; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 28-FEB-2018, entry version 10. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:BPAG_0000469301-mRNA-1}; OS Brugia pahangi (Filarial nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Spiruromorpha; Filarioidea; Onchocercidae; Brugia. OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000469301-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000469301-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:BPAG_0000469301-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; BPAG_0000469301-mRNA-1; BPAG_0000469301-mRNA-1; BPAG_0000469301. DR Proteomes; UP000038020; Genome Assembly. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000038020}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW Reference proteome {ECO:0000313|Proteomes:UP000038020}. FT DOMAIN 1 70 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 42 62 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 298 AA; 32546 MW; 05D9B1DE0DA507B5 CRC64; MRDQCFDPCC DPLTCTLRVH AHCASHQACC HRCQLRPIGH VCRPARSVCD VAEVCTGDDG DCPEDGYLID GTVCGISGQC WKGNCSDVEQ QCRDLWGSDA STADEHCYER NGLGLEYGNC GTDRDGIFRK CAVENVHCGT LHCRGGSQTP LNLKFNSFNL QFLHETKQIQ CKMVTNLDIG MVMDGSSCGS GKVCVQGICS PLVQVSPPVH CPSNNLAYQC SGHGDCTTTR RCLCYNGWMG TACDTKTNIT HSTTIAPSDV SHFSDIFIPS FAGKLFHLFF CDFDDPYEFA NAISSIEN // ID A0A0N4UXF8_ENTVE Unreviewed; 745 AA. AC A0A0N4UXF8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 28-MAR-2018, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:EVEC_0000221701-mRNA-1}; OS Enterobius vermicularis (Human pinworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Oxyurida; OC Oxyuroidea; Oxyuridae; Enterobius. OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000221701-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000221701-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:EVEC_0000221701-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; EVEC_0000221701-mRNA-1; EVEC_0000221701-mRNA-1; EVEC_0000221701. DR Proteomes; UP000038041; Genome Assembly. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000038041}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000038041}. FT DOMAIN 58 145 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 117 137 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 745 AA; 81776 MW; 5A089084AD4EF7FD CRC64; MAVSAYVYNV SMIELIGKVR NSSFTWKMSQ CSIDQLHNNL KLGHLQCLLN KPRQESSLQL CGNGVVDKGE ECDCGSRESC MDECCDPLTC TLRSEAQCAS HQICCKQCKV LSKGYICRAK RSSCDVEEKC DGEKGDCPPD GYLVDGTHCG INGQCWKGNC SDNESRCKAL WGSNASVAED RCFERNEMGI EDGNCGVEAD NRFRKCSPED ARCGLLHCQG GSSAPLQKNF DSYTAQFHYD GRTVNQSMVG MVADGSSCGM RKVCFEGRCL LLDDVSQPVL CPTTNVALPC SGHGRILSQW NSTLEFSTPE LLLEMCSEVS NCQKTTAASQ VFSAVTSVIT DTHFPSLCEK AGFLFVMCIY VQHCTTSLTC ICFTGWGGTA CNIRLSTPAN VLSTTTTVDE EFVPPLAAGR TLNTTTLLAI LLFVGIVLLM LRRSGNELLD GPLDEKMNES IPENADRIIK FGNMPSYREE KRKRKKNKRV YDALHRINEA SDERDSVSLK SRESGGKGSA VGSTNGSAVG CPEPVVGFGV EDNRVFNRIV NGSTSSILKN GNANRRLLNE GEIYSRSPCS EILGSPSRYT AVGRNGVRYD KNRSGYATDT ELGASPYAPH YVETLSMTRV DISPTLSDGS VTRLAPTPLK LNNIGMLLKQ LRYNDTMASE AELSTVEADN LDHIEPDPNI ETSRGFEVRE PVKLRKNESW SEGEKPKDSD YRSESRIKQL PLKSIQAGEV EQNPSLFSDS FRLEL // ID A0A0N5DPF8_TRIMR Unreviewed; 442 AA. AC A0A0N5DPF8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 28-MAR-2018, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:TMUE_s0038002500}; OS Trichuris muris (Mouse whipworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichinellida; Trichuridae; Trichuris. OX NCBI_TaxID=70415 {ECO:0000313|Proteomes:UP000046395, ECO:0000313|WBParaSite:TMUE_s0038002500}; RN [1] {ECO:0000313|Proteomes:UP000046395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Edinburgh {ECO:0000313|Proteomes:UP000046395}; RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D., RA Schwartz K.J., Yoon K.; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000046395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Edinburgh {ECO:0000313|Proteomes:UP000046395}; RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A., RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z., RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.; RT "The whipworm genome and dual-species transcriptomics of an intimate RT host-pathogen interaction."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|WBParaSite:TMUE_s0038002500} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Edinburgh {ECO:0000313|WBParaSite:TMUE_s0038002500}; RG Helminth Genomes Consortium; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|WBParaSite:TMUE_s0038002500} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; TMUE_s0038002500; TMUE_s0038002500; TMUE_s0038002500. DR Proteomes; UP000046395; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000046395}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000046395}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 358 380 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 50 138 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. SQ SEQUENCE 442 AA; 49026 MW; 2C0B91D912BC9158 CRC64; MGNPSRSSLE SRKHRPVYKF SERSRKTLQA LLNSYQGLCL AGEITQGHIL HTCGNKVVET GEQCDCGTWQ ECESVDPCCM PLTCRLKEWA QCSNGSCCDK CKFTEGNICR SSRDAECDIP EYCSAASEQC PADLYSYDGM PCGPDREGYC YGGRCHFAAE ECQKAYGNES AVSTEHCFVE LKSLTNFIQC GVNERGRPIV RTDTNFLNGV LFCQGGVKRQ AQGVQSKLDE QPYMRAYGKL SKCRLLIDKI VPLNSSSFRD DGRCTSGIET LRANCEKCTK DRRLPRCSGH GTWTKVNGCL CDDGWRGADC SLRKSMANVV KKVICVGNRT HAENSTLAEN RTCSAMFGIR FGRFSMDIYS LLLAGGCILL GVICCVQMIA LCFSNHSSCW IAIAEALHIR SRRARLPAAW IAGYIFRVSN RKEALVELAN AMIVRRGNEN LT // ID A0A0R3X8K3_HYDTA Unreviewed; 218 AA. AC A0A0R3X8K3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 25-OCT-2017, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:TTAC_0000987801-mRNA-1}; OS Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis). OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Taeniidae; Hydatigera. OX NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000987801-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000987801-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:TTAC_0000987801-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; TTAC_0000987801-mRNA-1; TTAC_0000987801-mRNA-1; TTAC_0000987801. DR Proteomes; UP000046396; Genome Assembly. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000046396}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000046396}. FT DOMAIN 1 64 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 36 56 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 218 AA; 24033 MW; 130584DE7538FB63 CRC64; LLAGAECATG PCCDIQSTFG DPSRTTCKLK QSGSVCREAG NSCDLPEYCS GESEWCPADV FKTDGEVCYT REGYKSHCIR GGCNAPDEWC RVLWGPTGLA AGPDCVAHNM IRDANNAIDK VANCGRLRPR GDERWREMDQ WPSKACNDWR VPFAISHHIY SAIFACNGTV CLSCSKTVVG KSDHSFSYLK LISYLNGLLK RQEETLNYLL LSLDRDGL // ID A0A158QCK9_HYMDI Unreviewed; 441 AA. AC A0A158QCK9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 28-MAR-2018, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:HDID_0000164001-mRNA-1}; OS Hymenolepis diminuta (Rat tapeworm). OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Hymenolepididae; Hymenolepis. OX NCBI_TaxID=6216 {ECO:0000313|WBParaSite:HDID_0000164001-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000164001-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:HDID_0000164001-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (APR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; HDID_0000164001-mRNA-1; HDID_0000164001-mRNA-1; HDID_0000164001. DR Proteomes; UP000046397; Genome Assembly. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000046397}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW Reference proteome {ECO:0000313|Proteomes:UP000046397}. FT DOMAIN 75 175 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 147 167 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 441 AA; 48383 MW; B54A78878DD9A2E0 CRC64; MEWSPCSIRD MPNLLRFGMG ACLHDIPVQS HTSLLPRQLR LIDVNGPSSI HTYTVINTQR GTPELLQSTP LSLKMSLCGN GKLDPGEECD CGTRETCPKE VRACCDVTTC KFREGAECAS GPCCDIQTVS GDPSKTICKL KASGTVCRDV GNSCDLPEYC DGQSEWCPAD VFKTDGETCY TKEGYRATYG VDGFDFILSA ELVVYYINGI PLYKISNCIR GGCNAPDEWC RVLWGPTGTA AGPGCIGYNL IRDPNSQSID EVANCGRLRP RSDERWKEID QWPSKPCYDW PDAECGRLWC MHRNEKAMLL GWQESQRRVD PHTQRTCVAL VYDPLDPLQH AEITSQTGFP GPGWDHTASV TQDAGMTPDG TPCQRGVCNN LGHCHCNIGY APPDCVKKGN GGSIDSGPPP PCKLKVILVH LSGIALNNHL RWVLYVDTLA I // ID A0A183KCJ3_9TREM Unreviewed; 386 AA. AC A0A183KCJ3; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 25-OCT-2017, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:SCUD_0001273601-mRNA-1}; OS Schistosoma curassoni. OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida; OC Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0001273601-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0001273601-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:SCUD_0001273601-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (JUN-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; SCUD_0001273601-mRNA-1; SCUD_0001273601-mRNA-1; SCUD_0001273601. DR Proteomes; UP000050789; Genome assembly. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050789}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000050789}. FT DOMAIN 70 164 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 136 156 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 386 AA; 42212 MW; 334CF13659EE1D52 CRC64; MDYHVSRLIS LAIAEILGIK SFPCPPLYSC YSFDLFSDGD NSRLRLALSS GMADCLLQNI AVTKDSKSFI DTCGNGQIDR GEECDPVVRR SLSYSSNFTN PMSCCNLETC LASVWAVCTH GPCCHQCRLK QKGSVCRPAF DQCDLPEFCT GTHPSCPLDL YLENGSPCLT QSTQSLIGIV SASSTSSSAL SSSSTTIITT TTSTTVVQKN NNSSSSQLNY LVENHKSLCY QGRCPTRHSQ CEMIWGEQAT EASDYCFHLH NTKTDGACGV QGQHCTIEHA KCGLLQCQGG RPRPVSLEAQ SGQPFVTYTE HQGRQFECKY LSHTSKVRFV PEGASCAPDR YCFHQECVLP HVVFQSICPT GPVNKQLENG HIIYKNVTCS DHGVSE // ID A0A183LJM8_9TREM Unreviewed; 361 AA. AC A0A183LJM8; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 25-OCT-2017, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:SMRZ_0000400201-mRNA-1}; OS Schistosoma margrebowiei. OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida; OC Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=48269 {ECO:0000313|Proteomes:UP000050790, ECO:0000313|WBParaSite:SMRZ_0000400201-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050790, ECO:0000313|WBParaSite:SMRZ_0000400201-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:SMRZ_0000400201-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (JUN-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; SMRZ_0000400201-mRNA-1; SMRZ_0000400201-mRNA-1; SMRZ_0000400201. DR Proteomes; UP000050790; Genome assembly. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050790}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000050790}. FT DOMAIN 70 164 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 136 156 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 361 AA; 39576 MW; 8BA54AA12972077B CRC64; MDYHVSRLIS LAIAEILGIK SFPCPPLYSC YSFDLFSDGD NSRLRLALSS GMADCLLQNI AVTKDSKSFI DTCGNGQIDR GEECDPVVRR SLSYSSNFTN PMSCCNLDTC LASVWAVCTH GPCCHQCRLK QKGSVCRPAF DQCDLPEFCT GTHPSCPLDL YLENGSPCLT QSTQSLIGIV SASSTSSSAL SSSSTTTITT TASTTVVQKN NNSSSSQLNY LVENHKSLCY QGRCPTRHSQ CEMIWGEQAT EASDYCFHLH NTKTDGACGV QGQHCTIEHA KCGLLQCQGG RPRPVSLEAQ SGQPFVTYTE HQGRQFECNV YLNLVYHMCV CSVYAITTNR NKRELCGIVY HITIGYNNIE L // ID A0A183QXF5_9TREM Unreviewed; 598 AA. AC A0A183QXF5; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 25-OCT-2017, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:SROB_0000837101-mRNA-1}; OS Schistosoma rodhaini. OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida; OC Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6188 {ECO:0000313|Proteomes:UP000050792, ECO:0000313|WBParaSite:SROB_0000837101-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050792, ECO:0000313|WBParaSite:SROB_0000837101-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:SROB_0000837101-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (JUN-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; SROB_0000837101-mRNA-1; SROB_0000837101-mRNA-1; SROB_0000837101. DR Proteomes; UP000050792; Genome assembly. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050792}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW Reference proteome {ECO:0000313|Proteomes:UP000050792}. FT DOMAIN 158 252 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 224 244 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 598 AA; 66541 MW; 32BFAAAB2AAA1226 CRC64; MIIISVNNTD MDYHVSRLIS LAIAEILGIK SFPCPPLYSC YSFDLFSDGD NSRLRLALSS GMADCLLQNI AVTKENSLEL EIQISRFRLR DLMVKRPLRD LRYWSPCASL VCNQGFPTPL GELSVSTNPV EAPDICFSSS QFRKQHPWCE KSDSKSFIDT CGNGQIDRGE ECDPIVRRTL SYSSNFTNPM SCCNLDTCLA SVWAVCTHGP CCHQCRLKQK GSLCRPAFDQ CDLPEFCTGT HPSCPLDLYL ENGSPCLTQS TQSLLGTVSA SSTSLSALSS SSTTTTSTTV VQKSNNSSSS QLNYLVENHK SLCYQGRCPT RHSQCEMIWG EQATEASDYC FHLHNTKTDG ACGVQGQHCT IEHAKCGLLQ CQGGRPRPVS LEAQSGQPFV TYTEHQGRQF ECKNKRELCG IVCHIANGYN NIELSKFRQG ASCAPDRYCF HQECVLPHVV FQSNCPTGPI NKQLENGHII YQNVTCSDHG LCTNAGFCLC HPEWTGNACE LPLVITNQSN NITNDQNDIL SNSSLSSIVS SQSTIIMNPL SSEVIHWIWD YLKQMQKSYG NSRNFQLKRF SMFVLFFIHV YSQLPYVFSS IGKVCVYI // ID A0A183TFK3_SCHSO Unreviewed; 545 AA. AC A0A183TFK3; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 22-NOV-2017, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:SSLN_0001582201-mRNA-1}; OS Schistocephalus solidus (Tapeworm). OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Diphyllobothriidea; Diphyllobothriidae; Schistocephalus. OX NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001582201-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001582201-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:SSLN_0001582201-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (JUN-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; SSLN_0001582201-mRNA-1; SSLN_0001582201-mRNA-1; SSLN_0001582201. DR Proteomes; UP000050788; Genome assembly. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050788}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000050788}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 164 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 226 336 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 308 328 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 545 AA; 59084 MW; 63BE8B3927E1CBD4 CRC64; LSSSLSRPTR DLTDVNKSTV PRSISPLAAA AASAADMDPG FEGERFQQSR PVDSRRDVVV LLTTTNFDEG AGSMAIPASI CTPRATAVLK ENTSNPELDT ARVLSRAIAE ILGIHSFPCP SMYNSAFTLM HPAFLLLLLL LLLLFFFFFF FFFFFFFFFF FLFLPDSLTL ITENFTHIHY SVFIPKCVDQ EAFSAGDLSR LRLALLSGMS SCLRPFASTE RQTLRQDTCG NGVVDRGEEC DPQHGVNLLS PRDAAAAAAA TANGSTPASL SASGGCCDPR TCLASIDAVC VDGACCRGCQ LVPRGRLCRP NRDQCDLPEF CSGTEPHCPS DLYLENGMPC RAKPRGSAAA DGSAEGSEAA SGEQEEEEEE ETALCYEGRC PTRSSQCRNL WGPLSQVSDK YCFETLNKNI ESACGPSTKC KPENAMCGLL HCRGGQSLPL PREARSAQVF NVRTHRSMQP IECKYLQSVS KFSYVPEGAS CDVDHFCFRN RCVKPGLSVH SKCPVGPFSV SSHTNPDGTQ AFIHPAVRYN LPTGTANVTC SGRGV // ID A7SGQ4_NEMVE Unreviewed; 161 AA. AC A7SGQ4; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 25-OCT-2017, entry version 51. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO37131.1}; DE Flags: Fragment; GN ORFNames=v1g16735 {ECO:0000313|EMBL:EDO37131.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO37131.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS469654; EDO37131.1; -; Genomic_DNA. DR RefSeq; XP_001629194.1; XM_001629144.1. DR STRING; 45351.NEMVEDRAFT_v1g16735-PA; -. DR EnsemblMetazoa; EDO37131; EDO37131; NEMVEDRAFT_v1g16735. DR GeneID; 5508616; -. DR KEGG; nve:NEMVE_v1g16735; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR HOGENOM; HOG000198860; -. DR InParanoid; A7SGQ4; -. DR OMA; PCGINKS; -. DR OrthoDB; EOG091G01L9; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}. FT DOMAIN 1 85 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 57 77 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT NON_TER 1 1 {ECO:0000313|EMBL:EDO37131.1}. FT NON_TER 161 161 {ECO:0000313|EMBL:EDO37131.1}. SQ SEQUENCE 161 AA; 17276 MW; 2E055FA8EEC2E30D CRC64; ICGNGFKEEG EECDCGTAER YSDDCCNSTT CKLTAGSECM DGPCCFKCKL SPAGKECREK VSECDLPEVC DGKSELCPAN RYVYNGKSCG DGKGFCFNGV CPTLDNQCET LWGLGVTSGP EVCYTINMKG TYSGSCAKLQ NGSFVGCKYE DIYCGMLHCT D // ID B3LW18_DROAN Unreviewed; 498 AA. AC B3LW18; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 2. DT 23-MAY-2018, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV41551.2}; DE EC=3.4.24.- {ECO:0000313|EMBL:EDV41551.2}; GN Name=Dana\GF17537 {ECO:0000313|EMBL:EDV41551.2}; GN ORFNames=Dana_GF17537 {ECO:0000313|EMBL:EDV41551.2}, GN GF17537 {ECO:0000313|FlyBase:FBgn0094555}; OS Drosophila ananassae (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV41551.2, ECO:0000313|Proteomes:UP000007801}; RN [1] {ECO:0000313|EMBL:EDV41551.2, ECO:0000313|Proteomes:UP000007801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH902617; EDV41551.2; -; Genomic_DNA. DR RefSeq; XP_001952968.2; XM_001952933.2. DR EnsemblMetazoa; FBtr0383205; FBpp0343356; FBgn0094555. DR GeneID; 6500321; -. DR KEGG; dan:Dana_GF17537; -. DR FlyBase; FBgn0094555; Dana\GF17537. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR InParanoid; B3LW18; -. DR OrthoDB; EOG091G01O1; -. DR Proteomes; UP000007801; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR008979; Galactose-bd-like_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007801}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Hydrolase {ECO:0000313|EMBL:EDV41551.2}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007801}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 498 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006454360. FT TRANSMEM 294 316 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 37 90 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 240 272 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 62 82 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 244 254 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 262 271 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 498 AA; 53238 MW; C60C50B1BFF8FECE CRC64; MSRRSRLHLH LPLVLLLVLQ STCLLPAEAA AEGGGGKPRA SCATGECCDL ATCRPKMAGS ACREAENECD LPEYCTGESE YCPADVFRRD TEPCDGGQAY CFHGNCRSHS NQCRILWGST GENSEHCYDK NMSGDRMGNC GYNRLNKTYV RCEAEHVKCG MLHCIHLNER LEFGMESAAV LSHSYVSHDR KIVACRTAVV DLGLQSTDPG LTPNGAKCGE DKMCVNQKCL PVSTVRSTGM GKACPDDCNG NGICNSMGHC HCDVGFGGES CGKAGSGGSP DSGPATDPNG SPGLKRFLCV LFFFVLPVVG ICWLLYQCHK NGLFASGKLK DNMYVSTTSS ISSSASQGSS SPDSSTITSS PPVKRPAPTA PLINTLPLPA PTVLVTNTAP ATITNTHTLS RHKSNPDAVH HVHIQPPQVP KSQSYEMPPR KLSTVPASSS YSNYKNIDTE PQITDNSTLR RKLDITAPRL HATTNPLALT EGAQFIQSGP ARCAPSKK // ID C3YIZ0_BRAFL Unreviewed; 302 AA. AC C3YIZ0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 28-MAR-2018, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN59864.1}; GN ORFNames=BRAFLDRAFT_240345 {ECO:0000313|EMBL:EEN59864.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN59864.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN59864.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN59864.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666516; EEN59864.1; -; Genomic_DNA. DR RefSeq; XP_002603853.1; XM_002603807.1. DR ProteinModelPortal; C3YIZ0; -. DR STRING; 7739.JGI240345; -. DR GeneID; 7253735; -. DR KEGG; bfo:BRAFLDRAFT_240345; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR InParanoid; C3YIZ0; -. DR KO; K06835; -. DR OMA; SHEECAL; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}. FT DOMAIN 42 128 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 100 120 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 302 AA; 32078 MW; D7EF3B909676A9F9 CRC64; MSRSQPAAVF SSCSSTDLQN ALLKGVGACL YNLPDPDRLY GGPVCGNGYL EEGEDCDCGT VDECTSPCCD PSTCTLHENA TCAIGLCCEG CQLVSAGNPC RDDLGDCDLP EYCTGTSPHC PPNVFIQDGY DCLYEEGYCF NGACLTHEAQ CKETWGEGKK VAEDVCYSLI NTKGDVYGNC GKDENDQYIP CSEIDIKCGK LQCQGGTVYP IIGSNAATIE SKIPWEGEMI TCRGAYIDLG DDMPDPGLVL TGTKCGEGKI CYNRQCQEMR IVDIGIKPCN CSGHGVSHTG AVLNPATVVT MG // ID E2R8B8_CANLF Unreviewed; 404 AA. AC E2R8B8; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 2. DT 23-MAY-2018, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCAFP00000032023}; GN Name=LOC482849 {ECO:0000313|Ensembl:ENSCAFP00000032023}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000032023, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000032023, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000032023, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000032023} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000032023}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEX03010385; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCAFT00000036620; ENSCAFP00000032023; ENSCAFG00000005832. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR Proteomes; UP000002254; Chromosome 16. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 349 366 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 44 132 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 280 313 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 104 124 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 303 312 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 404 AA; 44800 MW; 6935BF24EA6AD6DD CRC64; RQSGGVKEFS TCNLDDFKYL ASHSGFECLR NILPEIPVYK QRQRRVCGNG KLEEGEQCDC GTIETCTHKA CCDPRSCVIK TGKQCGSGEC CTPDCKLRPG GIPCRKSLDE CDFTEYCNGV SSHCVPDTYA RNGQSCESGD AFCYEGQCRT ASKQCKQLIG GASRGGSFAC YDEINSRADR YGNCGRDFCS FSNLLCGKLV CAWPHKALVS RANLSVIYSH VREEMCVSTY RSKEKAIKNT WTTYETPEDR DDTFVQDGTV CGPAMYCINF SCVEIQYQIN TQQCNSSYCN SHGVCNNLHH CHCEQGFAPP TCLEKKGEFG SIDDGHKAPS GKSNLREGNT TLSKHQFQLI FYISLPVLII TAVVLIKHKK IRELCYRGET ESERSVSEES SSNSKLSPSI SQLL // ID F1PN80_CANLF Unreviewed; 529 AA. AC F1PN80; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 2. DT 23-MAY-2018, entry version 51. DE SubName: Full=ADAM metallopeptidase domain 33 {ECO:0000313|Ensembl:ENSCAFP00000034408}; GN Name=ADAM33 {ECO:0000313|Ensembl:ENSCAFP00000034408, GN ECO:0000313|VGNC:VGNC:37585}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000034408, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000034408, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000034408, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000034408} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000034408}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEX03013827; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAEX03013828; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAEX03013829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAEX03013830; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCAFT00000038664; ENSCAFP00000034408; ENSCAFG00000006234. DR VGNC; VGNC:37585; ADAM33. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000002254; Chromosome 24. DR Bgee; ENSCAFG00000006234; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 442 462 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 157 243 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 389 421 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 215 235 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 393 403 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 411 420 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 529 AA; 56228 MW; 9F55494888C6CF85 CRC64; MLRRRKLGKS GFPKVYGLLP EHSSEDSPPP GVTAPRSRFA LLGSLVLASH PPTAGSPRDF AQVTCPLWAL PRGDPGRLSL RRCPRIQGLG GRAQRVVVGE GRGEVAVPAR PTPLPPRRHP FPRVFSACSR RQLRAFFRKG GGACLSNAPD SRLLVPRARC GNGLVEEGEE CDCGASQECQ DACCLAHNCS LRAGAQCSHG DCCARCLLKP AGVPCRRAVG DCDLPEFCTG ASPYCPPDIY LLDGSPCASG RGYCWDGACP TLEEQCQQLW GPGSSPAPEL CFQIVNSAGD AHGNCGQDGK GGFVPCAPRD AQCGKLQCLG GEQHPLPPHT VPVDSSVGLG REEVTCRGVF LLPGVQLDLL DLGLVEPGTP CGPRMVCQNR RCQNTTFLEL EQCLTTCHGH GVCNSNKNCH CAPGWAPPSC DKPGFGGSVD SGPMQPENHK TFLLGVILSF LLPLLPGAGL AWCCCRQPRS GLQQCLWGLR RDPSCSRPKD GPNRDRPSSS IHPMELGPAA TGEPQPLDLE NSARAQEPP // ID F1RZL9_PIG Unreviewed; 741 AA. AC F1RZL9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 3. DT 23-MAY-2018, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSSCP00000016750}; GN Name=ADAM2 {ECO:0000313|Ensembl:ENSSSCP00000016750}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000016750, ECO:0000313|Proteomes:UP000008227}; RN [1] {ECO:0000313|Ensembl:ENSSSCP00000016750, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000016750}; RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSSCP00000016750} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEMK02000099; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PaxDb; F1RZL9; -. DR PRIDE; F1RZL9; -. DR Ensembl; ENSSSCT00000017211; ENSSSCP00000016750; ENSSSCG00000034623. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR InParanoid; F1RZL9; -. DR OrthoDB; EOG091G0VW4; -. DR TreeFam; TF343636; -. DR ChiTaRS; ADAM2; pig. DR Proteomes; UP000008227; Chromosome 15. DR Bgee; ENSSSCG00000030223; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00517240}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAAS:SAAS00781361, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00781361, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 741 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5012632882. FT TRANSMEM 704 723 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 194 392 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 402 491 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 630 664 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 348 353 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 463 483 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 654 663 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 741 AA; 82643 MW; 61354C64592A1113 CRC64; MARPAGHAML SVLLILSGLG QLTSAGRHSV TSLLQITVPQ KIVKDTKDGR ASDTNVTYAI KINRKTFTLH LEKQSFLDSG FLVYSYNKSG ILHPDSSFIK GHCFYQGYAK EIPNSVVTVS TCSGLRGLLQ LENISYGIEP LESSATYEHM IYQIKDNKSD FPPIVKNHST TQFPDQPFKI LVKSEKKSDV LLKRILKIQV IIDKALYDYM GSEVALASEK VVYIFSLINN MFSQLKMTIM LTSLELWSDK NKILTNGDAN EMLQKFVSWK EKKLFQRSHD MAYLLIYRDH PNYIGATYHG MACNPKFAAG IALYPKMISL EAFSVILAQL IGINLGLTYK SDIYNCDCPG NICIMNPEAI RSRGVKFFSS CSIDEFKSTV SQPEFECLQN QIISKVVSQG QVASCGNGVL DAGEQCDCGD AERCSHKKCC NPKTCELITN AECGTGICCD KETCQIAERG TLCRRSTDVC DFPEYCNGIT EFCVPDVKSA DLETCNNKTA FCFQGLCRDP DKQCAELFGK FARGGSDLCS QHVNGQTDNF GNCRGRFCRY RDLGCGKIVC TWMRSEVVPF KNFDTQYTYY KGLLCVSAQL RNSTPVNLPE DFTYTWDGTM CGPKQFCMRG SCTNISDYVQ RPNCNSTARC RGHGVCNTQL NCHCDAGYAP PACEPSPSSP GGSIDDGFWI LEDEDVKYTK LLLKRPRASQ KKGLLISFYI FLPLLILIAL ITLKCNKKKI FQDKEGTVSE E // ID F6WQG6_CALJA Unreviewed; 521 AA. AC F6WQG6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 42. DE SubName: Full=ADAM metallopeptidase domain 15 {ECO:0000313|Ensembl:ENSCJAP00000016867}; GN Name=ADAM15 {ECO:0000313|Ensembl:ENSCJAP00000016867}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000016867, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000016867, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000016867} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01121905; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01121906; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01121907; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01121908; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCJAT00000017835; ENSCJAP00000016867; ENSCJAG00000009075. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000008225; Chromosome 18. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR033605; ADAM15. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR PANTHER; PTHR11905:SF130; PTHR11905:SF130; 2. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 15 {ECO:0000256|SAM:SignalP}. FT CHAIN 16 521 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5013107671. FT TRANSMEM 401 424 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 215 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 360 392 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 187 207 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 364 374 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 382 391 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 521 AA; 55641 MW; 588CCF7EE535E174 CRC64; MRLALLWALE RLLGAGSPWP SWPLPNXGGT KEQQARSEKS PSGPLEPQVL QDDLPNSLEE VLQSSLPEPL RIKLELDGDS HILELLQNRY FLPGLNFSNC SRQALEKALL DGMGSCLFER LPSLPSMAAF CGNMFVESGE QCDCGFPDDC TDPCCDSSTC KLRPGAQCAS DGPCCQNCQL HPSGWQCRPT RGECDLPEFC LGNSSQCPPD VSLGDGEPCA GGQAVCMHGR CASYAQQCQS LWGPGAQPAA PLCLQTANTR GNAFGSCGRS PSGSYESCSP RDAICGQLQC QTDRTQPLLG SVHALIWEMI DVNGTGLNCS WVHLDLGNDV AQPLLTLPGT ACGPGLVCID HRCQPVDLLG AQECRSKCHG HGVCDSNRHC HCEEGWAPPD CTTQLKATSS LTTGLLLSLL VLLVLVMLGA SYWYRVRLHQ RLCQLKGPTC QYRAAQSGPP ERPGPPQRAL LARGTKSQGP AKPPPPRKPL PADPQGRCPS GDLSGPEAGI PPLVVPSRPA PPPPTMSSLY L // ID F7IQ95_CALJA Unreviewed; 512 AA. AC F7IQ95; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 23-MAY-2018, entry version 42. DE SubName: Full=ADAM metallopeptidase domain 19 {ECO:0000313|Ensembl:ENSCJAP00000035211}; GN Name=ADAM19 {ECO:0000313|Ensembl:ENSCJAP00000035211}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000035211, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000035211, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000035211} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFV01083077; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01083078; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01083079; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01083080; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01083081; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01083082; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01083083; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACFV01083084; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCJAT00000037179; ENSCJAP00000035211; ENSCJAG00000018932. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR Proteomes; UP000008225; Chromosome 2. DR GO; GO:0005794; C:Golgi apparatus; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0017124; F:SH3 domain binding; IEA:InterPro. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:InterPro. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR033596; ADAM19. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR PANTHER; PTHR11905:SF19; PTHR11905:SF19; 1. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 297 318 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 10 96 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 244 276 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 68 88 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 248 258 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 266 275 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 512 AA; 55462 MW; AF977CA1F9F7E7EB CRC64; MPDTRTLYGG RRCGNGYLED GEECDCGEEE ECNNPCCNAS NCTLKQGAEC AHGSCCHECK LLAPGTLCRE QARQCDLPEF CTGKSPHCPT NFYQMDGTPC EGGQAYCYNG MCLTYQEQCQ QLWGPGARPA PDLCFEKVNV AGDTFGNCGK DMNGEHRKCN MRDAKCGKIQ CQSSEARPLE SNAVPIDTTI IMNGRQIQCR GTHVYRGPEE ESDMLDPGLV MTGTKCGYNH ICFEGQCRNT SFFETEGCGK KCNGHGVCNN NQNCHCLPGW APPFCNTPGQ GGSIDSGPMP PESVGPVVAG VLAAIFVLVV LLLIYYCCRQ NKKLGQLKPS ALPSKLRQQF SCPFRVSQNS GTGHANPTFK LQTPQGKRKV INTPEILRKP SQPPPRPPPD YLRGGSPPAL LPAHLSRAAR NSPAPASQIE RTESSRRPPP SRPVPPAPHC ILSQDFSRPR PPQKALPANP VPGRRALPRP GGASTLWPPG ASPRQSQPVA APAPKEIYAQ CCCLSGEEYR SQ // ID G3HFT4_CRIGR Unreviewed; 402 AA. AC G3HFT4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 37. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 19 {ECO:0000313|EMBL:EGW01403.1}; GN ORFNames=I79_009449 {ECO:0000313|EMBL:EGW01403.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW01403.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH000335; EGW01403.1; -; Genomic_DNA. DR ProteinModelPortal; G3HFT4; -. DR PRIDE; G3HFT4; -. DR InParanoid; G3HFT4; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0005794; C:Golgi apparatus; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0017124; F:SH3 domain binding; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:InterPro. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR033596; ADAM19. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR PANTHER; PTHR11905:SF19; PTHR11905:SF19; 1. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:EGW01403.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 300 321 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 10 96 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 247 279 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 68 88 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 251 261 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 269 278 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 402 AA; 43788 MW; 43660833BC18B765 CRC64; MPDTRTLYGG RRCGNGYLED GEECDCGEEE ECNNPCCNAS NCTLKGKAEC AHGSCCHQCK LVAPGTLCRE QVRQCDLPEF CTGKSPHCPT NFYQMDGTPC EGGQAYCYNG MCLTYKEQCQ QLWGPGARPA LDLCFERVNA AGDTYGNCGK GLNGKYRKCS PRDAKCGKIQ CQSTQARPLE SNAVSIDTTI TLNGRRIHCR GTHVYRGPEE EEGEGDMLDP GLVMTGTKCG HNHICFEGQC RNTSFFETEG CGKKCNGHGV CNNNQNCHCF HGWAPPFCNT PGDGGSIDSA PLPPKSVGPV IAGVFSAFFV LAVLVLLFHC YRQSHKLGKP SALPFKLRQQ FSCPFRVSQS GGTGHANPTF KLQTPQGKRK VANTPETLRK PSHPPPXXXC TLNPHLHCCQ HI // ID G5B7E5_HETGA Unreviewed; 366 AA. AC G5B7E5; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 25-OCT-2017, entry version 23. DE SubName: Full=Putative disintegrin and metalloproteinase domain-containing protein 5 {ECO:0000313|EMBL:EHB05206.1}; GN ORFNames=GW7_19427 {ECO:0000313|EMBL:EHB05206.1}; OS Heterocephalus glaber (Naked mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Heterocephalus. OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB05206.1, ECO:0000313|Proteomes:UP000006813}; RN [1] {ECO:0000313|EMBL:EHB05206.1, ECO:0000313|Proteomes:UP000006813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993625; DOI=10.1038/nature10533; RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L., RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X., RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A., RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., RA Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L., RA Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.; RT "Genome sequencing reveals insights into physiology and longevity of RT the naked mole rat."; RL Nature 479:223-227(2011). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH168777; EHB05206.1; -; Genomic_DNA. DR InParanoid; G5B7E5; -. DR Proteomes; UP000006813; Unassembled WGS sequence. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006813}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00028283}; KW Integrin {ECO:0000313|EMBL:EHB05206.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006813}. FT DOMAIN 127 195 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. SQ SEQUENCE 366 AA; 40938 MW; AC4F79F3A7E9F024 CRC64; MFLLVVLLTG VGGLYAGHNH FYLQLLLFIH MTKTAPNILS LCYLRGVMRI ENISYGIEPL EAVSGFMHMI YEENNDDTHV SLFGENDTFT WLNNTENQVR SSLHKTEFTK LFPRYIEMYI VVDKNLNCTH VRCCDPTSCK KKGSVKCGSG ECCTTNCQLK KANTLCRSSI DTECDFNEYC NGNEGDCVPD TYARDGSHCD SGEGYCFGGI CRTFDRQCEA LFGKGSKGAP FACFDEINSR GDRFGNCGRY HCEIQHALCG KLVCTWPHKT LISRENLSVI YTHVRDDICV AGAKTDGKII RTTSFTTYLE PTDRDETFVE DGTICGPGMI CNNFQNCHCN KGFSPLECQL KKGEFGSIDD GHMTKG // ID G7P8Z0_MACFA Unreviewed; 331 AA. AC G7P8Z0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 23-MAY-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHH63942.1}; GN ORFNames=EGM_17022 {ECO:0000313|EMBL:EHH63942.1}; 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 {ECO:0000313|Proteomes:UP000009130}; RN [1] {ECO:0000313|EMBL:EHH63942.1, ECO:0000313|Proteomes:UP000009130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH63942.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001282; EHH63942.1; -; Genomic_DNA. DR Proteomes; UP000009130; Chromosome 7. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009130}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000009130}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 290 308 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 3 89 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 229 262 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 61 81 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 252 261 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 331 AA; 36708 MW; AED39CC3C0826A7D CRC64; MTTVLCGNLI VEGKEECDCG SFKQCYASHC CQSDCHFTPG SICHLGDCCT NCSFSPLGTL CRPIQNICDL PEYCHGTTLT CPPDLYLQDG TPCTEEGYCY HGNCTDRNVL CKAIFGVSAE DAPEDCYDIN LENHRFGHCT RARTAIAYEA CALIDKFCGR LQCTNVTHLP RLQEHVSFHH SIRRGFQCFG LDEHRATDTT DVGHVIDGTP CADGIFCNNS QCNATITSLG YDCHPEKCSH RGVCNNRRNC HCHIGWDPPR CLRRGIGGSV DSGPPPRRTR SVKQSQQSVL YLRVVFGRIY TFIIALLFGM ATNARILRTT TVEKVTVTEP E // ID H0YBG8_HUMAN Unreviewed; 387 AA. AC H0YBG8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 23-MAY-2018, entry version 51. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|Ensembl:ENSP00000429484}; DE Flags: Fragment; GN Name=ADAM28 {ECO:0000313|Ensembl:ENSP00000429484}; 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 {ECO:0000313|Ensembl:ENSP00000429484, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000429484, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Glockner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000429484} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC044891; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC120193; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0YBG8; -. DR PeptideAtlas; H0YBG8; -. DR PRIDE; H0YBG8; -. DR Ensembl; ENST00000521629; ENSP00000429484; ENSG00000042980. DR UCSC; uc064lgl.1; human. DR EuPathDB; HostDB:ENSG00000042980.12; -. DR HGNC; HGNC:206; ADAM28. DR OpenTargets; ENSG00000042980; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR ChiTaRS; ADAM28; human. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000042980; -. DR ExpressionAtlas; H0YBG8; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0000213|EPD:H0YBG8, KW ECO:0000213|PeptideAtlas:H0YBG8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 295 319 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 40 126 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 258 290 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 98 118 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 262 272 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 280 289 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000429484}. SQ SEQUENCE 387 AA; 42812 MW; 5F3946DFF923DE35 CRC64; XFYIPTDFSS CSRLSYDKFF EDKLSNCLFN APLPTDIIST PICGNQLVEM GEDCDCGTSE ECTNICCDAK TCKIKATFQC ALGECCEKCQ FKKAGMVCRP AKDECDLPEM CNGKSGNCPD DRFQVNGFPC HHGKGHCLMG TCPTLQEQCT ELWGPGTEVA DKSCYNRNEG GSKYGYCRRV DDTLIPCKAN DTMCGKLFCQ GGSDNLPWKG RIVTFLTCKT FDPEDTSQEI GMVANGTKCG DNKVCINAEC VDIEKAYKST NCSSKCKGHA VCDHELQCQC EEGWIPPDCD DSSVVFHFSI VVGVLFPMAV IFVVVAMVIR HQSSREKQKK DQRPLSTTGT RPHKQKRKPQ MVKAVQPQEM SQMKPHVYDL PVEGNEPPAS FDSNPKA // ID H0YC66_HUMAN Unreviewed; 489 AA. AC H0YC66; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 19 {ECO:0000313|Ensembl:ENSP00000431027}; DE Flags: Fragment; GN Name=ADAM19 {ECO:0000313|Ensembl:ENSP00000431027}; 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 {ECO:0000313|Ensembl:ENSP00000431027, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000431027, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000431027} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC008676; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC008694; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC106801; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0YC66; -. DR MaxQB; H0YC66; -. DR PeptideAtlas; H0YC66; -. DR PRIDE; H0YC66; -. DR Ensembl; ENST00000517374; ENSP00000431027; ENSG00000135074. DR UCSC; uc063jdp.1; human. DR EuPathDB; HostDB:ENSG00000135074.15; -. DR HGNC; HGNC:197; ADAM19. DR OpenTargets; ENSG00000135074; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144014; -. DR ChiTaRS; ADAM19; human. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000135074; -. DR ExpressionAtlas; H0YC66; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0017124; F:SH3 domain binding; IEA:InterPro. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:InterPro. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR033596; ADAM19. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR PANTHER; PTHR11905:SF19; PTHR11905:SF19; 1. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0000213|MaxQB:H0YC66, KW ECO:0000213|PeptideAtlas:H0YC66}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 295 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 73 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 221 253 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 45 65 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 225 235 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 243 252 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000431027}. SQ SEQUENCE 489 AA; 52833 MW; EC838622DC272CEC CRC64; XDCGEEEECN NPCCNASNCT LRPGAECAHG SCCHQCKLLA PGTLCREQAR QCDLPEFCTG KSPHCPTNFY QMDGTPCEGG QAYCYNGMCL TYQEQCQQLW GPGARPAPDL CFEKVNVAGD TFGNCGKDMN GEHRKCNMRD AKCGKIQCQS SEARPLESNA VPIDTTIIMN GRQIQCRGTH VYRGPEEEGD MLDPGLVMTG TKCGYNHICF EGQCRNTSFF ETEGCGKKCN GHGVCNNNQN CHCLPGWAPP FCNTPGHGGS IDSGPMPPES VGPVVAGVLV AILVLAVLML MYYCCRQNNK LGQLKPSALP SKLRQQFSCP FRVSQNSGTG HANPTFKLQT PQGKRKVINT PEILRKPSQP PPRPPPDYLR GGSPPAPLPA HLSRAARNSP GPGSQIERTE SSRRPPPSRP IPPAPNCIVS QDFSRPRPPQ KALPANPVPG RRSLPRPGGA SPLRPPGAGP QQSRPLAALA PKRVWKTCNL KTGDQFQSQ // ID H3EC61_PRIPA Unreviewed; 308 AA. AC H3EC61; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:PPA07309}; OS Pristionchus pacificus (Parasitic nematode). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Diplogasterida; OC Neodiplogasteridae; Pristionchus. OX NCBI_TaxID=54126 {ECO:0000313|EnsemblMetazoa:PPA07309, ECO:0000313|Proteomes:UP000005239}; RN [1] {ECO:0000313|EnsemblMetazoa:PPA07309, ECO:0000313|Proteomes:UP000005239} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PS312 {ECO:0000313|EnsemblMetazoa:PPA07309, RC ECO:0000313|Proteomes:UP000005239}; RX PubMed=18806794; DOI=10.1038/ng.227; RA Dieterich C., Clifton S.W., Schuster L.N., Chinwalla A., RA Delehaunty K., Dinkelacker I., Fulton L., Fulton R., Godfrey J., RA Minx P., Mitreva M., Roeseler W., Tian H., Witte H., Yang S.P., RA Wilson R.K., Sommer R.J.; RT "The Pristionchus pacificus genome provides a unique perspective on RT nematode lifestyle and parasitism."; RL Nat. Genet. 40:1193-1198(2008). RN [2] {ECO:0000313|EnsemblMetazoa:PPA07309} RP IDENTIFICATION. RC STRAIN=PS312 {ECO:0000313|EnsemblMetazoa:PPA07309}; RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 54126.PPA07309; -. DR EnsemblMetazoa; PPA07309; PPA07309; PPA07309. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR InParanoid; H3EC61; -. DR OrthoDB; EOG091G01O1; -. DR Proteomes; UP000005239; Unassembled WGS sequence. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005239}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000005239}. FT DOMAIN 61 151 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 123 143 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 308 AA; 33861 MW; EA8FCB83DC123B39 CRC64; MSHCIMNPSE IKTKDPTDAG TTSQHLQYWS SCSLAELEQL YSTGADYCLW DEPGMTIEED EAVCGNGIVE DGEECDCGQL VRGCITHTCC DATTCKLRAG AQCASGACCD MKTCLAAPTT RMCRDAKNTC DVPEYCDGVN AECTVDQHLP DGLTCPDDEN AICYGGRCGS RLLQCKEIWG EQARPSADSC YKDGNLCKIP RSEGMFAGSG EEVKVKVTRD HLCKEKDKMC GMLRCSVGDF DEAKGHITGW HYTFSTKEQC KVMFTEYQRD YKPHYFMGMT PDGAACGDGK VDDIRFLIPK YEMGTSSL // ID K7EXD6_PELSI Unreviewed; 416 AA. AC K7EXD6; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 23-MAY-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPSIP00000000446}; OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudines; Cryptodira; Trionychia; Trionychidae; OC Pelodiscus. OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000000446, ECO:0000313|Proteomes:UP000007267}; RN [1] {ECO:0000313|Ensembl:ENSPSIP00000000446} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17381049; DOI=10.1080/10425170600760091; RA Jung S.-O., Lee Y.-M., Kartavtsev Y., Park I.-S., Kim D.S., Lee J.-S.; RT "The complete mitochondrial genome of the Korean soft-shelled turtle RT Pelodiscus sinensis (Testudines, Trionychidae)."; RL DNA Seq. 17:471-483(2006). RN [2] {ECO:0000313|Proteomes:UP000007267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267}; RG Soft-shell Turtle Genome Consortium; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSPSIP00000000446} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCU01134828; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; K7EXD6; -. DR Ensembl; ENSPSIT00000000446; ENSPSIP00000000446; ENSPSIG00000000447. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00910000144019; -. DR OMA; LYSTHEL; -. DR TreeFam; TF314733; -. DR Proteomes; UP000007267; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.390.10; -; 1. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007267}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007267}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 336 362 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 50 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 58 144 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 285 318 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 10 15 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 116 136 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 308 317 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 416 AA; 45620 MW; 9867A01DF1E25B55 CRC64; MFHDEKYCHC PRRQCIMAAL HSVTDLFSNC SYNYYYNQMI SSAGCLLKPP ASKEVYTRKY CGNQMVESGE QCDCGSKYNC RKDPCCQSNC TLSAGATCAF GECCEDCQIL PAGTLCRKSN NKCDLPEYCN GTSQWCQKDV YVQDGAPCEK GAYCYGGNCS SHDQQCKMIF GKEAIVAPLA CFQKLNMHGD RFGNCGITRE MNAKYKKCQA DDILCGRVQC ENKKIIPSLQ DHSTILQTPV DSNWCWGTDY HHGMEIDDIG AVRDGASCGP DKICVNMSCV NLSLLNNDCN ATKCHKRGIC NSHKNCHCDY GWAPPYCQDK GYGGSIDSGP PPRVKALGGG AIATLILLAA AAALGIGFGV YYKTALMGWF RRSMARFHAT QQTGASSQGV HASSHVKPAT MSKPRLESMQ EALDFM // ID L5JPX7_PTEAL Unreviewed; 340 AA. AC L5JPX7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 23-MAY-2018, entry version 26. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 29 {ECO:0000313|EMBL:ELK01390.1}; GN ORFNames=PAL_GLEAN10000079 {ECO:0000313|EMBL:ELK01390.1}; OS Pteropus alecto (Black flying fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; OC Pteropodidae; Pteropodinae; Pteropus. OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK01390.1, ECO:0000313|Proteomes:UP000010552}; RN [1] {ECO:0000313|Proteomes:UP000010552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB094354; ELK01390.1; -; Genomic_DNA. DR InParanoid; L5JPX7; -. DR Proteomes; UP000010552; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010552}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:ELK01390.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000010552}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 300 320 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 13 99 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 239 272 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 71 91 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 262 271 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 340 AA; 37216 MW; 24E3A510F1EA44BA CRC64; MTDIVYTNRT YSVARCGDNV VDETEQCDCG SFKRCYNDPC CKSDCTFPRG SSCDTGRCCV NCTQAAPGVL CRPIQNICDL PEYCTGSGFQ CPDDFYLQDG TPCTEEGYCY HGNCTDRTMH CQEIFGEGAL KGPDSCYSIN ERGHRFGHCR RAAMLFQPEA CGPSDVQCGR LQCTNVTHLP QLQEHVGFHQ SLISGVLCFG VDLHRATETT DVGLVRSGTP CGRGKFCLNT YCNGSISAIV YDCYPSKCSH RGVCNNAKNC HCHVGWDPPS CLHRGAGGSI NSGPPPSKMR RVSQNIETVV YLRVVFGRLY AFLAAILFGV ATNVRTIKTT VVNVETAEEK // ID L5JTB2_PTEAL Unreviewed; 357 AA. AC L5JTB2; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 20. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 21 {ECO:0000313|EMBL:ELK02232.1}; GN ORFNames=PAL_GLEAN10005134 {ECO:0000313|EMBL:ELK02232.1}; OS Pteropus alecto (Black flying fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; OC Pteropodidae; Pteropodinae; Pteropus. OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK02232.1, ECO:0000313|Proteomes:UP000010552}; RN [1] {ECO:0000313|Proteomes:UP000010552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB031146; ELK02232.1; -; Genomic_DNA. DR InParanoid; L5JTB2; -. DR Proteomes; UP000010552; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010552}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW Integrin {ECO:0000313|EMBL:ELK02232.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000010552}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 318 342 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 42 128 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 100 120 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 357 AA; 39126 MW; D04D5D42A31098F9 CRC64; MNAVRVPAER FTNCSYADFA KTTLNQGSCL HTPPSLGEVL MLKRCGDGVV EGEEECDCGS VKQCEQDPCC LSNCTLRPGA ACAFGLCCKD CKFMPSGALC RHEVNECDLP EWCNATGHQC PEDGYVQDGV PCSDEAYCYQ KRCNNHDEMS REIFGEGAKS ASQNCYQEIN SQGNRFGHCG INGTTYLKCN TADIFCGRVQ CENVVAIPHL RDRSALQHIH RNGVTCWGIA YHLGMDIPDV GEVKDGTMCG SGKICIHKKC VSLSHPSQIC LPETCNMKGI CNNKHHCHCG YGWSPPYCLH RGYGGNVDSG PPSARRGAFF PLVMILSLSV LILLVTTVFM YLQKHFAPKE TEAHPSD // ID L5KMM6_PTEAL Unreviewed; 580 AA. AC L5KMM6; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 23-MAY-2018, entry version 31. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:ELK11828.1}; GN ORFNames=PAL_GLEAN10008989 {ECO:0000313|EMBL:ELK11828.1}; OS Pteropus alecto (Black flying fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; OC Pteropodidae; Pteropodinae; Pteropus. OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK11828.1, ECO:0000313|Proteomes:UP000010552}; RN [1] {ECO:0000313|Proteomes:UP000010552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB030668; ELK11828.1; -; Genomic_DNA. DR ProteinModelPortal; L5KMM6; -. DR InParanoid; L5KMM6; -. DR Proteomes; UP000010552; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010552}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:ELK11828.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000010552}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 379 400 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 95 181 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 327 359 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 153 173 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 331 341 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 349 358 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 580 AA; 62136 MW; E8D16CD815941610 CRC64; MPRVLMSFLC MQLSESHGDL SNHCADGSCP WIPDIVLGKG FRALLMECRH VSRADPYPFP MLFSSCSRKD LEASLEKGVG VCLFNLPEVR QSSGGRKCGN GYVEEGEQCD CGEPEECTSL CCNATTCTLK PDAVCAHGLC CEDCQLKPAG TACRDPSNSC DLPEFCSGSS PHCPANVYLH DGHPCQGLDG YCYNGVCQTH EQQCVTLWGP GAKPAPGICF ERVNSAGDPY GNCGKSSKGS FAKCELRDAK CGKIQCQGGA SRPVIGTNAV SIETNIPLQE GGRILCRGTH VYLGDDMPDP GLVLAGTKCA DGKICLNRRC QNISVFGVHE CAKQCHGRGV CNNRRNCHCE AHWAPPLCDK SGFGGSTDSG PIRRADNQGV TIGLLVTVLC LLAAGFVVYL KRKTLIPLLF TDKKSAIEKL RCVRPPRPSS GSHPGQAHLT HLGKGLLRKP PHSSAPRDNP KRPLQCLNVD ISRPLKALDF PQPHPPPRVL PPLHQAPRAP GVPARPLPAN PAPRQAQGTR KPDPPQKPLP ANPLSKTTRL ASALARTPEQ QASGLRLVPL RAAPECPRPG PRATHVAYAK // ID L5M161_MYODS Unreviewed; 385 AA. AC L5M161; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 23-MAY-2018, entry version 27. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 29 {ECO:0000313|EMBL:ELK32042.1}; GN ORFNames=MDA_GLEAN10000485 {ECO:0000313|EMBL:ELK32042.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK32042.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB105679; ELK32042.1; -; Genomic_DNA. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR001590; Peptidase_M12B. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:ELK32042.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 344 366 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 47 Peptidase M12B. FT {ECO:0000259|PROSITE:PS50215}. FT DOMAIN 59 145 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 284 317 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 117 137 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 307 316 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 385 AA; 42069 MW; AA16203B7E9D8A4C CRC64; MDCVCQRRAT CIMYRYPVLT DSFSNCSFVH TQHVLNNNIQ RCLFKERGPL AYSNSSLTSI RCGNSVVEDK EQCDCGTFKQ CYSNTCCESD CRFSPGSICN RETCCANCTH SPAGTLCRPI QNICDLPEYC LGKDTRCPSD FYLQDGTPCT EDGYCYQGNC TDRSMHCKEI FGEGALSAPD VCYSINKKGH RFGHCKVTDE YQPKGCADAD VMCGRLQCVN VTHLPRLQEH VGFHHSIIGG SLCFGVGAHR ATDTTDVGAV RPGTPCGGGN FCLQGFCNAT LAAIDYNCPP SKCNYRGVCN NNRNCHCHVG WDPPLCINHG AGGSVDSGPP PRRRRSVRAG GMSLVYLRVV FGRMLALIAA LLFGVATNVR TIQTTTVTEV KVRGK // ID L5MEW7_MYODS Unreviewed; 465 AA. AC L5MEW7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 23-MAY-2018, entry version 25. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:ELK36815.1}; GN ORFNames=MDA_GLEAN10021310 {ECO:0000313|EMBL:ELK36815.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK36815.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB101169; ELK36815.1; -; Genomic_DNA. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076, KW ECO:0000256|SAAS:SAAS00877335}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:ELK36815.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 297 318 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 15 99 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 245 277 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 249 259 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 267 276 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 465 AA; 49283 MW; 8FD67523084C50BE CRC64; MCLFNLPEVR PAFGGRKCGD GYVEEGEECD CGEPEECPSR CCNASTCTLT PGAVCAHGLC CEHCQVSPGR PRGASNACDL PEFCSGASPH CPANVYLHDG HPCQGVDGYC YNGICQTHEQ QCVTLWGPGA KPAPGICFER VNSAGDPYGN CGKDAKSSFA KCETRDAKCG KIQCQGGASR PVIGTNAVSI ETNIPLQEGG RILCRGTHVY LGDDMPDPGL VLAGTKCADG KICLNRRCQN ISVFGVHECA RQCHGRGVCN NRKNCHCEAH WAPPFCDKVG FGGSTDSGPI RQAGHRGLTA GVLASILCLL AAGLVVYLKR KTLVRLLFTD KKTLEKLRCV RPARPPGGCQ PSQAPLPPVS DNPKRPLQCQ NVAISRPLQA LGRPRPPSPQ RVLPTLHQAP RTPSVPARPL PATPALRQAQ GTRKPSAPQK PLPAVPLSKT ARLAPDPTST PGPESGLRLA PLRLV // ID L8Y408_TUPCH Unreviewed; 329 AA. AC L8Y408; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 23-MAY-2018, entry version 26. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 30 {ECO:0000313|EMBL:ELV10977.1}; GN ORFNames=TREES_T100010249 {ECO:0000313|EMBL:ELV10977.1}; OS Tupaia chinensis (Chinese tree shrew). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia. OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV10977.1, ECO:0000313|Proteomes:UP000011518}; RN [1] {ECO:0000313|Proteomes:UP000011518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Zhang G., Fan Y., Yao Y., Huang Z.; RT "Genome of the Chinese tree shrew, a rising model animal genetically RT related to primates."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB366175; ELV10977.1; -; Genomic_DNA. DR InParanoid; L8Y408; -. DR Proteomes; UP000011518; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR033959; ADAM4. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR PANTHER; PTHR11905:SF167; PTHR11905:SF167; 1. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011518}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:ELV10977.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000011518}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 289 310 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 6 80 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 225 258 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 52 72 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 248 257 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 329 AA; 35939 MW; D7EE168D548EAF01 CRC64; MPGLLEECDC GSFKECADDQ CCETTCALSL GSICDVGSCC VRCKYARPGM ICRDTLGICD LPEYCDGKSE QCPEDLYIQD GTPCSAVAVC IAGNCSDRDM QCQALFGYRV KDASPACYNK LNTKGDRFGN CGVKLQRGGS KPFKCEEDDV LCGLLHCDGI DHIPGGGEHT TFRSILVQDV SEVKCFGYDA HHGTELPEMG LVVDGATCGP GRYCYRQNCT FYDDLGFDCD VKKCNFRGVC NNKKNCHCVR GWKPPLCEER GSGGSENSGP PADRDVGIRA KILVNVNKFL LFLLLRLAFL LFALLLGGLF KAKEVIEEKI YEDDISGKN // ID S9WI59_CAMFR Unreviewed; 686 AA. AC S9WI59; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 28-MAR-2018, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPY78217.1}; GN ORFNames=CB1_001111034 {ECO:0000313|EMBL:EPY78217.1}; OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Tylopoda; OC Camelidae; Camelus. OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY78217.1, ECO:0000313|Proteomes:UP000030684}; RN [1] {ECO:0000313|EMBL:EPY78217.1, ECO:0000313|Proteomes:UP000030684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684}; RX PubMed=23149746; RG Bactrian Camels Genome Sequencing and Analysis Consortium; RA Jirimutu null, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., RA Wang L., Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., RA Zhang W., Batmunkh M., Ts B., Narenbatu null, Unierhu null, RA Bat-Ireedui S., Gao H., Baysgalan B., Li Q., Jia Z., RA Turigenbayila null, Subudenggerile null, Narenmanduhu null, Wang Z., RA Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt null, Erdemt null, RA Altansha null, Altansukh null, Liu T., Cao M., Aruuntsever null, RA Bayart null, Hosblig null, He F., Zha-ti A., Zheng G., Qiu F., Sun Z., RA Zhao L., Zhao W., Liu B., Li C., Chen Y., Tang X., Guo C., Liu W., RA Ming L., Temuulen null, Cui A., Li Y., Gao J., Li J., Wurentaodi null, RA Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T., Bayaer T., RA Li Y., Meng H.; RT "Genome sequences of wild and domestic bactrian camels."; RL Nat. Commun. 3:1202-1202(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB017334; EPY78217.1; -; Genomic_DNA. DR Proteomes; UP000030684; Unassembled WGS sequence. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030684}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000030684}. FT DOMAIN 159 245 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 217 237 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 686 AA; 72773 MW; 227E8D7613D16698 CRC64; MAAGDRKDER KEQSLNYLQP EVTLIPSSLL IPSPRMITQP TEVQGAGTAP PGHGEGSVNF AGKLAHPATS LCSPGFSRQE QDLPSDRLCS HRAVLGEDSN LPVTGPNSGV GQPRPLARIV YPFPVLFSSC SRRDLEASLE KGVGMCLFNL PEVRQAFGGR KCGNGYVEEG EECDCGEPEE CLNSCCNATT CTLKPDAVCA HGLCCDACRL KPAGTACREP SNSCDLPEFC TGASPHCPAN VYLHDGHPCQ GVDGYCYNGI CQTHEQQCVT LWGPGAKPAP GICFERVNSA GDPYGNCGKN SKSSFAKCEL RDAKCGKIQC QGGASRPVIG TNAVSIETNI PLQEGGRILC RGTHVYLGDD MPDPGLVLAG TKCADGKICL NRRCQNVSVF GVHECAVQCH SRGVLTCFDA VKLRPSVSPQ YFVLKVCNNR KNCHCEAHWA PPFCDKFGFG GSTDSGPIRQ AARDAPLAEV ILRQTAKWVC APSPAIQRSP ARAGPPRPPQ QRPADKTATF QHIEGTQMAQ FPGGPLGLPP KQAPDAGPLL NETVITTVTL GSDPTGQHQE IAAVSERGHQ QTPQSPGCSS AQFFSAGAPA PAPGSSCALR PRQTPAGQPC AQTGPDPLSK TTRLSGASAR PLGQRESGLR LAPIRASPRL HRDSPWLTMR PKTHLDPGSL GHSTPVPLRR LLITQC // ID S9X4A6_CAMFR Unreviewed; 486 AA. AC S9X4A6; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPY82294.1}; GN ORFNames=CB1_000667004 {ECO:0000313|EMBL:EPY82294.1}; OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Tylopoda; OC Camelidae; Camelus. OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY82294.1, ECO:0000313|Proteomes:UP000030684}; RN [1] {ECO:0000313|EMBL:EPY82294.1, ECO:0000313|Proteomes:UP000030684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684}; RX PubMed=23149746; RG Bactrian Camels Genome Sequencing and Analysis Consortium; RA Jirimutu null, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., RA Wang L., Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., RA Zhang W., Batmunkh M., Ts B., Narenbatu null, Unierhu null, RA Bat-Ireedui S., Gao H., Baysgalan B., Li Q., Jia Z., RA Turigenbayila null, Subudenggerile null, Narenmanduhu null, Wang Z., RA Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt null, Erdemt null, RA Altansha null, Altansukh null, Liu T., Cao M., Aruuntsever null, RA Bayart null, Hosblig null, He F., Zha-ti A., Zheng G., Qiu F., Sun Z., RA Zhao L., Zhao W., Liu B., Li C., Chen Y., Tang X., Guo C., Liu W., RA Ming L., Temuulen null, Cui A., Li Y., Gao J., Li J., Wurentaodi null, RA Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T., Bayaer T., RA Li Y., Meng H.; RT "Genome sequences of wild and domestic bactrian camels."; RL Nat. Commun. 3:1202-1202(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB016936; EPY82294.1; -; Genomic_DNA. DR Proteomes; UP000030684; Unassembled WGS sequence. DR GO; GO:0007338; P:single fertilization; IEA:InterPro. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR033958; ADAM2. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR PANTHER; PTHR11905:SF108; PTHR11905:SF108; 3. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030684}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000030684}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 486 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004559511. FT DOMAIN 263 336 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 308 328 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 486 AA; 51867 MW; D3E8BCD8B1B15493 CRC64; MLSLLLLLSG LGRLTTTSHQ PALVQGPAGG EPSVGSEPAQ VLGLLVGGLR ANITSTNYSG EKTGSNSSAG GDSETQLYQE DSYRQGSIDY EAGEDEGRYG SVECGEVPMA LLIAPVSERT PRRCASQASE CGEKVLLAAA PGSVRGPEGS PRAPNCPPPS PTATTRAGIR DVKPCCAFCF CSLGSSGSRQ TTVSYKIVIE GKTYTVNLMQ KGLLQFENVS YGIEPLEPSI GFEHVIYQVK HRNAGISLYA EKETESREMP YKIQSVEECE ALPQVCCNRA TCQLSGNSVC DTGPCCEACA YKLSGEMCRP ASNECDLPEF CNGSSASCQD DFYVQNGHPC EDNQWICLEG NCMSGAIQCT HIFGEGSSFA GQECYEDLNS KGDQSGNCGA TASGYTKCEP KDLKCGKLIC TYDKTELINI PSATIVYANI KGHLCVALDY AFGDKASDNM WVCKNKTCVD SAFLNYDCTP EKCNNQGVSI STVQQE // ID T0MG67_CAMFR Unreviewed; 467 AA. AC T0MG67; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 23-MAY-2018, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EQB77385.1}; GN ORFNames=CB1_000340047 {ECO:0000313|EMBL:EQB77385.1}; OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Tylopoda; OC Camelidae; Camelus. OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EQB77385.1, ECO:0000313|Proteomes:UP000030684}; RN [1] {ECO:0000313|EMBL:EQB77385.1, ECO:0000313|Proteomes:UP000030684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684}; RX PubMed=23149746; RG Bactrian Camels Genome Sequencing and Analysis Consortium; RA Jirimutu null, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., RA Wang L., Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., RA Zhang W., Batmunkh M., Ts B., Narenbatu null, Unierhu null, RA Bat-Ireedui S., Gao H., Baysgalan B., Li Q., Jia Z., RA Turigenbayila null, Subudenggerile null, Narenmanduhu null, Wang Z., RA Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt null, Erdemt null, RA Altansha null, Altansukh null, Liu T., Cao M., Aruuntsever null, RA Bayart null, Hosblig null, He F., Zha-ti A., Zheng G., Qiu F., Sun Z., RA Zhao L., Zhao W., Liu B., Li C., Chen Y., Tang X., Guo C., Liu W., RA Ming L., Temuulen null, Cui A., Li Y., Gao J., Li J., Wurentaodi null, RA Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T., Bayaer T., RA Li Y., Meng H.; RT "Genome sequences of wild and domestic bactrian camels."; RL Nat. Commun. 3:1202-1202(2012). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB016630; EQB77385.1; -; Genomic_DNA. DR Proteomes; UP000030684; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030684}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000030684}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 392 414 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 89 174 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 315 349 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT COILED 438 466 {ECO:0000256|SAM:Coils}. FT DISULFID 146 166 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 339 348 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 467 AA; 51161 MW; 9DF03996060CDBBB CRC64; MKGLRPALLP EASRVMSGIM LVLVLVFLPS LYGDLGSVYY SSYEIVIPKS LTVEGREDPV EKVSYMLFMQ GQKQLIHLTP GHKGRLQRDV QCGNGIVDET EQCDCGSECD NHPCCDETCR LKEKAVCNPG PCCNNSCQYE KIGSTCRPAV GECDLPEYCL GDSGECPPDR YKQDGTSCQK VHYCFEGRCR TADNQCLDIF GYPAKSAPEE CYRSLNKKGN RFGNCGSPTN SNPEYVQCED NNLFCGKVVC TNVKQLPDIR PQHTVLQVPH ENDYCWVMDA YDTTDIPDEG TSWGGSTCGD NSVCMNHICS DHSVLGYDCK PEEMCNGKGV CNNLKHCHCV GGFAPPDCNT AGNGGSVDSG PPGMSEGPEP PAGGGSQNTT GSKKEELLDT AIILFIILFL IILAIIMCCI FCLCKREKEK EAAPPPEEGP PAEAAPPVEA PEEEEEEEEE EEEEEEEEEE EEEESEP // ID T1EDV3_HELRO Unreviewed; 336 AA. AC T1EDV3; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESO12677.1, ECO:0000313|EnsemblMetazoa:HelroP105476}; GN Name=20194755 {ECO:0000313|EnsemblMetazoa:HelroP105476}; GN ORFNames=HELRODRAFT_105476 {ECO:0000313|EMBL:ESO12677.1}; OS Helobdella robusta (Californian leech). OC Eukaryota; Metazoa; Lophotrochozoa; Annelida; Clitellata; Hirudinea; OC Rhynchobdellida; Glossiphoniidae; Helobdella. OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP105476, ECO:0000313|Proteomes:UP000015101}; RN [1] {ECO:0000313|EnsemblMetazoa:HelroP105476, ECO:0000313|Proteomes:UP000015101} RP NUCLEOTIDE SEQUENCE. RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., RA Otillar R.P., Terry A.Y., Boore J.L., Simakov O., Marletaz F., RA Cho S.-J., Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., RA Lv J., Arendt D., Savage R., Osoegawa K., de Jong P., Lindberg D.R., RA Seaver E.C., Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ESO12677.1, ECO:0000313|EnsemblMetazoa:HelroP105476, ECO:0000313|Proteomes:UP000015101} RP NUCLEOTIDE SEQUENCE. RX PubMed=23254933; DOI=10.1038/nature11696; RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P., RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R., RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., RA Aerts A., Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., RA Lindberg D.R., Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.; RT "Insights into bilaterian evolution from three spiralian genomes."; RL Nature 493:526-531(2013). RN [3] {ECO:0000313|EnsemblMetazoa:HelroP105476} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMQM01000213; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KB095811; ESO12677.1; -; Genomic_DNA. DR RefSeq; XP_009009397.1; XM_009011149.1. DR EnsemblMetazoa; HelroT105476; HelroP105476; HelroG105476. DR GeneID; 20194755; -. DR KEGG; hro:HELRODRAFT_105476; -. DR CTD; 20194755; -. DR KO; K08610; -. DR OrthoDB; EOG093704ZC; -. DR Proteomes; UP000015101; Unassembled WGS sequence. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000015101}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000015101}. FT DOMAIN 54 143 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 115 135 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 336 AA; 37749 MW; 84C488734CBE48C6 CRC64; MNSGLKKKIV PSYGFSTCSR KHFRKVIQRG LAPCLEQRYL VEPSQLPTLP SHEEPVCGNG IVEEEEDYDC LGKHLQFCNT SCYDAHCKLY DGNSCASGLC CDLNTCQIKT KGTTCRYKKS DCDVTESCDG ISPKCPPDQH VHDGTKCLRN NYCISGKCGD KTKTCALLWG AGVKESSEWC YKVNEKANSA GHCGVYMDRT GLHYRKCLSG SYLCGRLWCQ ALATYRRFSN KMESSVHFQS SSQLNNQLKN ATFCVAVDYH YGKTQTSPGL VPDGAACGHN MLCFKQVCRP RSYILSEMHV SEKVQRWNIA RNSSHTKALM LGWLIVFFIK FIHKQI // ID T1EKQ5_HELRO Unreviewed; 120 AA. AC T1EKQ5; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESO12673.1, ECO:0000313|EnsemblMetazoa:HelroP152299}; GN Name=20197155 {ECO:0000313|EnsemblMetazoa:HelroP152299}; GN ORFNames=HELRODRAFT_152299 {ECO:0000313|EMBL:ESO12673.1}; OS Helobdella robusta (Californian leech). OC Eukaryota; Metazoa; Lophotrochozoa; Annelida; Clitellata; Hirudinea; OC Rhynchobdellida; Glossiphoniidae; Helobdella. OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP152299, ECO:0000313|Proteomes:UP000015101}; RN [1] {ECO:0000313|EnsemblMetazoa:HelroP152299, ECO:0000313|Proteomes:UP000015101} RP NUCLEOTIDE SEQUENCE. RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., RA Otillar R.P., Terry A.Y., Boore J.L., Simakov O., Marletaz F., RA Cho S.-J., Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., RA Lv J., Arendt D., Savage R., Osoegawa K., de Jong P., Lindberg D.R., RA Seaver E.C., Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ESO12673.1, ECO:0000313|EnsemblMetazoa:HelroP152299, ECO:0000313|Proteomes:UP000015101} RP NUCLEOTIDE SEQUENCE. RX PubMed=23254933; DOI=10.1038/nature11696; RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P., RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R., RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., RA Aerts A., Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., RA Lindberg D.R., Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.; RT "Insights into bilaterian evolution from three spiralian genomes."; RL Nature 493:526-531(2013). RN [3] {ECO:0000313|EnsemblMetazoa:HelroP152299} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMQM01000213; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KB095811; ESO12673.1; -; Genomic_DNA. DR RefSeq; XP_009009393.1; XM_009011145.1. DR EnsemblMetazoa; HelroT152299; HelroP152299; HelroG152299. DR GeneID; 20197155; -. DR KEGG; hro:HELRODRAFT_152299; -. DR CTD; 20197155; -. DR Proteomes; UP000015101; Unassembled WGS sequence. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000015101}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000015101}. FT DOMAIN 1 68 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 40 60 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT NON_TER 1 1 {ECO:0000313|EMBL:ESO12673.1}. FT NON_TER 120 120 {ECO:0000313|EMBL:ESO12673.1}. SQ SEQUENCE 120 AA; 13071 MW; 51D1E6C717093F0B CRC64; QRCSIKCCDK NTCKFTRNAK CASGLCCNLN TCQLKKNSLC REAAGECDVE EVCDGASNHC PVDRHVNNTT PCQVGGGGFC FDGECNSHDK ACQALYGNKS ISAPEQCYQM NMNATKFYNC // ID T1G9U8_HELRO Unreviewed; 236 AA. AC T1G9U8; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESO03887.1, ECO:0000313|EnsemblMetazoa:HelroP99723}; GN Name=20217844 {ECO:0000313|EnsemblMetazoa:HelroP99723}; GN ORFNames=HELRODRAFT_99723 {ECO:0000313|EMBL:ESO03887.1}; OS Helobdella robusta (Californian leech). OC Eukaryota; Metazoa; Lophotrochozoa; Annelida; Clitellata; Hirudinea; OC Rhynchobdellida; Glossiphoniidae; Helobdella. OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP99723, ECO:0000313|Proteomes:UP000015101}; RN [1] {ECO:0000313|EnsemblMetazoa:HelroP99723, ECO:0000313|Proteomes:UP000015101} RP NUCLEOTIDE SEQUENCE. RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., RA Otillar R.P., Terry A.Y., Boore J.L., Simakov O., Marletaz F., RA Cho S.-J., Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., RA Lv J., Arendt D., Savage R., Osoegawa K., de Jong P., Lindberg D.R., RA Seaver E.C., Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ESO03887.1, ECO:0000313|EnsemblMetazoa:HelroP99723, ECO:0000313|Proteomes:UP000015101} RP NUCLEOTIDE SEQUENCE. RX PubMed=23254933; DOI=10.1038/nature11696; RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P., RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R., RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., RA Aerts A., Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., RA Lindberg D.R., Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.; RT "Insights into bilaterian evolution from three spiralian genomes."; RL Nature 493:526-531(2013). RN [3] {ECO:0000313|EnsemblMetazoa:HelroP99723} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMQM01004401; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KB096551; ESO03887.1; -; Genomic_DNA. DR RefSeq; XP_009017823.1; XM_009019575.1. DR EnsemblMetazoa; HelroT99723; HelroP99723; HelroG99723. DR GeneID; 20217844; -. DR KEGG; hro:HELRODRAFT_99723; -. DR CTD; 20217844; -. DR OMA; CELATCN; -. DR OrthoDB; EOG093704ZC; -. DR Proteomes; UP000015101; Unassembled WGS sequence. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000015101}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000015101}. FT DOMAIN 6 96 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 68 88 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 236 AA; 25855 MW; 3C923BDE1AC2C393 CRC64; MSNVTAANCG NGFLEPGEEC DCGSFPDEVC SKACCNGTTC KLRPTAKCAS GLCCELATCN MKSVEMVCRP VEDDCDVEDH CDGNSSLCGD DVKPDGSMCT DRQYCYNGKC QPRNAQYSQL WLDESVVSAG ERCYSHTTVE DSNCFYCDYN VSSKTSIPCK QKDVLCGSLL CDLRQIHPDL KSLHDRCQLG LECVCAVYKV DRRNSHATFV NDGTSCGRSL VTSLYLVISN CQNNFK // ID T1KPL9_TETUR Unreviewed; 437 AA. AC T1KPL9; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 23-MAY-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:tetur17g00960.1}; GN Name=107366038 {ECO:0000313|EnsemblMetazoa:tetur17g00960.1}; OS Tetranychus urticae (Two-spotted spider mite). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Acari; Acariformes; Trombidiformes; Prostigmata; Eleutherengona; OC Raphignathae; Tetranychoidea; Tetranychidae; Tetranychus. OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur17g00960.1, ECO:0000313|Proteomes:UP000015104}; RN [1] {ECO:0000313|EnsemblMetazoa:tetur17g00960.1, ECO:0000313|Proteomes:UP000015104} RP NUCLEOTIDE SEQUENCE. RC STRAIN=London {ECO:0000313|EnsemblMetazoa:tetur17g00960.1}; RA Rombauts S.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:tetur17g00960.1} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAEY01000333; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_015789100.1; XM_015933614.1. DR EnsemblMetazoa; tetur17g00960.1; tetur17g00960.1; tetur17g00960. DR GeneID; 107366038; -. DR KEGG; tut:107366038; -. DR Proteomes; UP000015104; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000015104}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000015104}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 377 400 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 56 144 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DOMAIN 294 326 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DISULFID 116 136 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT DISULFID 298 308 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 316 325 {ECO:0000256|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 437 AA; 46964 MW; 73D799957CB48BE6 CRC64; MKNKLVNPKS IVLVSIFICF HLISNVTSSL SLDELSLDEN NEITYLKDKP LALQSTKTCG NRIIEPDEQC DCGRPDCGSC CDGKTCMLNS TACCGSGPCC NPKTCFPYAR IDNVVCKKAV DECDLPEYCD GLSEFCPEDR YKPNGIPCNK SQFNARCYAG RCANHAIQCG KLWGPNIIQS HESCYQAKLM GKTTFPCKLE GPMNKTEQQC TIDDTTCGLL YCNAPANTKL VYEQPFAGSK KHNIINGTHQ CLALEGSLSS LNPGMVPDGS PCGTTISGMC VGVKCVLVDT VLKKIKACPK NCSGHGICNN AGACHCDPLY TSSDCSVEIS KNMSKPMNGS TASLIFKPTS KQIAECRDKL RIFTTSASSQ PVNLSTFTLA IIIGFLLSVL VSVAVLWNLY HRYGSSNTED NRPGTAPKPP ATPATPATPA TPAIPPN // ID V3YWR7_LOTGI Unreviewed; 144 AA. AC V3YWR7; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 25-OCT-2017, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESO82478.1}; DE Flags: Fragment; GN ORFNames=LOTGIDRAFT_134520 {ECO:0000313|EMBL:ESO82478.1}; OS Lottia gigantea (Giant owl limpet). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda; OC Patellogastropoda; Lottioidea; Lottiidae; Lottia. OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO82478.1, ECO:0000313|Proteomes:UP000030746}; RN [1] {ECO:0000313|EMBL:ESO82478.1, ECO:0000313|Proteomes:UP000030746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23254933; DOI=10.1038/nature11696; RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P., RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R., RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., RA Aerts A., Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., RA Lindberg D.R., Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.; RT "Insights into bilaterian evolution from three spiralian genomes."; RL Nature 493:526-531(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB203888; ESO82478.1; -; Genomic_DNA. DR RefSeq; XP_009066831.1; XM_009068583.1. DR EnsemblMetazoa; LotgiT134520; LotgiP134520; LotgiG134520. DR GeneID; 20233568; -. DR KEGG; lgi:LOTGIDRAFT_134520; -. DR CTD; 20233568; -. DR OMA; PCGINKS; -. DR OrthoDB; EOG091G01L9; -. DR Proteomes; UP000030746; Unassembled WGS sequence. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030746}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW Reference proteome {ECO:0000313|Proteomes:UP000030746}. FT DOMAIN 1 77 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 49 69 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT NON_TER 1 1 {ECO:0000313|EMBL:ESO82478.1}. SQ SEQUENCE 144 AA; 15710 MW; 0E20CCBC308CBF13 CRC64; EECDCGSEEE CMKKDPCCDP TTCLLKSWAQ CRSGQCCHNC TVLPSTVKCR DKKSDCDVPE YCDGIQGECP SNNYLQDGHP CNNDAGYCMG GICPSTQQQC QQIWGADSKG GEEQCFERFN PTGNFNGHCG KDKTTGTFAK CSAE // ID V8N6T1_OPHHA Unreviewed; 386 AA. AC V8N6T1; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 23-MAY-2018, entry version 23. DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 21 {ECO:0000313|EMBL:ETE57272.1}; DE Flags: Fragment; GN Name=Adam21 {ECO:0000313|EMBL:ETE57272.1}; GN ORFNames=L345_17015 {ECO:0000313|EMBL:ETE57272.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE57272.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE57272.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE57272.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE57272.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZIM01008978; ETE57272.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR Pfam; PF08516; ADAM_CR; 2. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 2. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00028283}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Integrin {ECO:0000313|EMBL:ETE57272.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}. FT DOMAIN 97 130 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DOMAIN 162 224 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 120 129 {ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 196 216 {ECO:0000256|PROSITE-ProRule:PRU00068}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE57272.1}. FT NON_TER 386 386 {ECO:0000313|EMBL:ETE57272.1}. SQ SEQUENCE 386 AA; 42469 MW; 28EA66AB1E96D5E4 CRC64; INNKGDRFGN CGLKHDIYKK CYTADSLCGR IQCKNIQMPS LEDHSTIIHT STGVNQCWGT DYHTGMKVND IGAVRDGTPC GNSMLCIEGS CVDVSILKYD CNVTMCHNRG VCNTLKHCHC DVGWAPPDCR NKGYGGSIDS GPPPVTDTNK TLAIVYPNIS LSDPCCQANC MLCPAAVCAF GLCCANCQYR QHGTVCREKI SSCDLPEYCN GTSEHCPEDM RVQDGAVCND GVYCYHENCM THAVQNDVRQ VNNKGDRFGN CGLKHGIYMK CDTGDSLYGR IQCKNIQMPC LEDHSTIIYT STRVNQCWGT DYHMGMNIND IEAVRDGTPC GSNMMCIEGS CVDVSILKYD CNDAMCHSRE VCNTHRHCHC DVGLHCDVQT AEIKAT // ID W4YXH9_STRPU Unreviewed; 489 AA. AC W4YXH9; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 25-OCT-2017, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:SPU_020547-tr}; OS Strongylocentrotus purpuratus (Purple sea urchin). OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; OC Echinoidea; Euechinoidea; Echinacea; Echinoida; Strongylocentrotidae; OC Strongylocentrotus. OX NCBI_TaxID=7668 {ECO:0000313|EnsemblMetazoa:SPU_020547-tr, ECO:0000313|Proteomes:UP000007110}; RN [1] {ECO:0000313|EnsemblMetazoa:SPU_020547-tr} RP NUCLEOTIDE SEQUENCE. RA Murali S., Liu Y., Vee V., English A., Wang M., Skinner E., Han Y., RA Muzny D.M., Worley K.C., Gibbs R.A.; RT "Genome sequencing for Strongylocentrotus purpuratus."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:SPU_020547-tr} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAGJ04077380; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGJ04077381; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGJ04077382; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGJ04077383; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 7668.SPU_020547tr; -. DR EnsemblMetazoa; SPU_020547-tr; SPU_020547-tr; SPU_020547. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR OrthoDB; EOG091G01NX; -. DR Proteomes; UP000007110; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR013032; EGF-like_CS. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS01186; EGF_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007110}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007110}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 292 315 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 47 113 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 85 105 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 489 AA; 52829 MW; 2D333EC7A63CD12C CRC64; MAKSVTIGPH DPLFLMLIER NLFRKRYVET HITEDGHVVT KLPHKHECDT KCCVPETCRF HVNATCAEGE CCDSECQMLS AGTLCRDKYN PCDLPEYCTG TSAECPGNVY LQNGEKCDRR NSDSLCYDGQ CHSYQQQCEE VWGIQRSPVR AGVDECYALN EQGSHFGSCG ETDVRPCPTS NMRCGRLMCE NVPARPVLSS IATIAPARVY DSNNQVHICK TVSLNFGADV LDPGYVAEGT SCAEGKVCNS KSHCHCNQGW APPLCNTVGY GGSIDSGPAL PRDNIGVSTG TVAALLVLFI VIFPLLTVCG VVIYCKRQRL RQMLNKSREA RTGHQSFRNS PGSNGATRKT VTVTRTPSVR ASPPTIEHIP NKSTGNVVHD VYPLIPTGPS VSYKPDRPPA RPSSPPPGQT SRPPPLPSAA PTRPSQTPAK PTAPPSRPTV PKFKPTARSQ SFNFPAKSEP GSGASLGESK NTSKKCVAAI SIVRVMSLI // ID W5NPV3_SHEEP Unreviewed; 190 AA. AC W5NPV3; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 23-MAY-2018, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOARP00000000193}; 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 {ECO:0000313|Ensembl:ENSOARP00000000193, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Proteomes:UP000002356}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000000193} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSOART00000000219; ENSOARP00000000193; ENSOARG00000000210. DR GeneTree; ENSGT00900000141298; -. DR OMA; HICTSAY; -. DR OrthoDB; EOG091G0D6R; -. DR Proteomes; UP000002356; Unplaced. DR Gene3D; 4.10.70.10; -; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068, KW ECO:0000256|SAAS:SAAS00877335}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}. FT DOMAIN 1 70 Disintegrin. FT {ECO:0000259|PROSITE:PS50214}. FT DISULFID 42 62 {ECO:0000256|PROSITE-ProRule:PRU00068}. SQ SEQUENCE 190 AA; 21374 MW; A9ECF41B4FDFEDAB CRC64; FQTCEYSKCC DPLNCVLKGK AECGSGPCCG KNTCKCNRGR ECRKSTDPCD FPEFCNGLSE FCAPDMRAAD LQMCNNKSSY CFKGICQDRT MQCTNLFGKY AKEASYQCAE EVNYQGDVFG NCLGKPWFFL HHLCGKLVCH WTHSLIVSRN DIHVQYTYLG GHICTSAYLR TRKFPDPTIS SNGSMCDEDK //