ID A0A250Y4N1_CASCN Unreviewed; 733 AA. AC A0A250Y4N1; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 08-NOV-2023, entry version 32. DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183}; DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183}; GN Name=BMP1 {ECO:0000313|EMBL:JAV38592.1}; OS Castor canadensis (American beaver). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Castoridae; OC Castor. OX NCBI_TaxID=51338 {ECO:0000313|EMBL:JAV38592.1}; RN [1] {ECO:0000313|EMBL:JAV38592.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ROM106880 {ECO:0000313|EMBL:JAV38592.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:JAV38592.1}; RX PubMed=28087693; DOI=10.1534/g3.116.038208; RA Lok S., Paton T.A., Wang Z., Kaur G., Walker S., Yuen R.K., Sung W.W., RA Whitney J., Buchanan J.A., Trost B., Singh N., Apresto B., Chen N., RA Coole M., Dawson T.J., Ho K.Y., Hu Z., Pullenayegum S., Samler K., RA Shipstone A., Tsoi F., Wang T., Pereira S.L., Rostami P., Ryan C.A., RA Tong A.H., Ng K., Sundaravadanam Y., Simpson J.T., Lim B.K., Engstrom M.D., RA Dutton C.J., Kerr K.C., Franke M., Rapley W., Wintle R.F., Scherer S.W.; RT "De Novo Genome and Transcriptome Assembly of the Canadian Beaver (Castor RT canadensis)."; RL G3 (Bethesda) 7:755-773(2017). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211, CC ECO:0000256|RuleBase:RU361183}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE- CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}; CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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 (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GFFV01001353; JAV38592.1; -; Transcribed_RNA. DR AlphaFoldDB; A0A250Y4N1; -. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00041; CUB; 3. DR CDD; cd00054; EGF_CA; 1. DR CDD; cd04281; ZnMc_BMP1_TLD; 1. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR Gene3D; 2.10.25.10; Laminin; 1. DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 3. DR InterPro; IPR015446; BMP_1/tolloid-like. DR InterPro; IPR000859; CUB_dom. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001506; Peptidase_M12A. DR InterPro; IPR006026; Peptidase_Metallo. DR InterPro; IPR035914; Sperma_CUB_dom_sf. DR InterPro; IPR034036; ZnMP_TLD/BMP1. DR PANTHER; PTHR10127:SF863; BONE MORPHOGENETIC PROTEIN 1; 1. DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1. DR Pfam; PF01400; Astacin; 1. DR Pfam; PF00431; CUB; 3. DR Pfam; PF14670; FXa_inhibition; 1. DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1. DR PRINTS; PR00480; ASTACIN. DR SMART; SM00042; CUB; 3. DR SMART; SM00181; EGF; 1. DR SMART; SM00179; EGF_CA; 1. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 3. DR PROSITE; PS51864; ASTACIN; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 1. DR PROSITE; PS01180; CUB; 3. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS01187; EGF_CA; 1. PE 4: Predicted; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU01211}; KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE- KW ProRule:PRU00076}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211, KW ECO:0000256|RuleBase:RU361183}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001199-2, ECO:0000256|PROSITE- KW ProRule:PRU01211}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE- KW ProRule:PRU01211}; KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211, KW ECO:0000256|RuleBase:RU361183}; Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|RuleBase:RU361183}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001199-2}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|RuleBase:RU361183" FT CHAIN 28..733 FT /note="Metalloendopeptidase" FT /evidence="ECO:0000256|RuleBase:RU361183" FT /id="PRO_5011819595" FT DOMAIN 124..323 FT /note="Peptidase M12A" FT /evidence="ECO:0000259|PROSITE:PS51864" FT DOMAIN 325..437 FT /note="CUB" FT /evidence="ECO:0000259|PROSITE:PS01180" FT DOMAIN 438..550 FT /note="CUB" FT /evidence="ECO:0000259|PROSITE:PS01180" FT DOMAIN 550..591 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 594..706 FT /note="CUB" FT /evidence="ECO:0000259|PROSITE:PS01180" FT REGION 90..129 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 705..733 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 92..110 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 217 FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1, FT ECO:0000256|PROSITE-ProRule:PRU01211" FT BINDING 216 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2, FT ECO:0000256|PROSITE-ProRule:PRU01211" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2, FT ECO:0000256|PROSITE-ProRule:PRU01211" FT BINDING 226 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2, FT ECO:0000256|PROSITE-ProRule:PRU01211" FT DISULFID 186..208 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" FT DISULFID 188..189 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" SQ SEQUENCE 733 AA; 83236 MW; 985DCC6104511FCE CRC64; MPGVARPPLP LLLRLLLLLL LPRPGRPLDL ADYTYDLGEE DASEPLNYKD PCKAAAFLGD IALDEEDLRA FQVQQAGDLR QRAACRSPIK AAGNSSAPSC QSTSGQSQRE TRGRWRGRPR SRRAATSRPE RVWPDGVIPF VIGGNFTGSQ RAVFRQAMRH WEKHTCVTFL ERTDEDSYIV FTYRPCGCCS YVGRRGGGPQ AISIGKNCDK FGIVVHELGH VIGFWHEHTR PDRDRHVSIV RENIQPGQEY NFLKMEIQEV ESLGETYDFD SIMHYARNTF SRGIFLDTIV PKYEVNGVKP PIGQRTRLSK GDIAQARKLY KCPACGETLQ DSTGNFSSPE YPNGYSAHMH CVWRISVTPG EKIILNFTSM DLYRSRLCWY DYVEVRDGFW RKAPLRGRFC GGKLPEPIVS TDSRLWVEFR SSSNWVGKGF FAVYEAICGG DVKKDNGHIQ SPNYPDDYRP NKVCIWRIQV SEGFHVGLTF QSFEIERHDS CAYDYLEVRD GHSESSSLIG RYCGYEKPDD IKSTSSRLWL KFVSDGSINK AGFAVNFFKE VDECSRPNRG GCEQRCLNTL GSYKCSCDPG YELAPDKRHC EAACGGFLTK LNGSITSPGW PKEYPPNKNC IWQLVAPTQY RISLQFDFFE TEGNDVCKYD FVEVRSGLTA DSKLHGKFCG SEKPEVITSQ YNNMRVEFKS DNTVSKKGFK AHFFSEKRPT LQPPRGRPQQ VKFRVQKRNR TPQ //