ID A0A8C0Z504_CANLF Unreviewed; 988 AA. AC A0A8C0Z504; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 24-JUL-2024, entry version 13. DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183}; DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183}; GN Name=BMP1 {ECO:0000313|Ensembl:ENSCAFP00000046623.2, GN ECO:0000313|VGNC:VGNC:38475}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00040037346.1, ECO:0000313|Proteomes:UP000694542}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000046623.2, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000046623.2}; 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., Mauceli E., RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., RA Searle S.M.J., 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., Bachantsang P., RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., RA Naylor J., 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., Osman S., RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., RA 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:ENSCAFP00040037346.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. 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 Ensembl; ENSCAFT00000063173.2; ENSCAFP00000046623.2; ENSCAFG00000009587.8. DR Ensembl; ENSCAFT00040042812.1; ENSCAFP00040037346.1; ENSCAFG00040022949.1. DR VGNC; VGNC:38475; BMP1. DR Proteomes; UP000002254; Chromosome 25. DR Proteomes; UP000694542; Chromosome 25. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00041; CUB; 5. 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; 2. DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5. DR InterPro; IPR015446; BMP_1/tolloid-like. DR InterPro; IPR000859; CUB_dom. DR InterPro; IPR050841; Dev_metalloprotease_endo_rcpt. 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; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR049883; NOTCH1_EGF-like. 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; PTHR24251:SF42; BONE MORPHOGENETIC PROTEIN 1; 1. DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1. DR Pfam; PF01400; Astacin; 1. DR Pfam; PF00431; CUB; 5. DR Pfam; PF07645; EGF_CA; 1. DR Pfam; PF14670; FXa_inhibition; 1. DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1. DR PRINTS; PR00480; ASTACIN. DR SMART; SM00042; CUB; 5. DR SMART; SM00181; EGF; 2. DR SMART; SM00179; EGF_CA; 2. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 5. DR PROSITE; PS51864; ASTACIN; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 1. DR PROSITE; PS01180; CUB; 5. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS01187; EGF_CA; 2. PE 4: Predicted; KW Developmental protein {ECO:0000256|ARBA:ARBA00022473}; 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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211, KW ECO:0000256|RuleBase:RU361183}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR001199-2}; 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..24 FT /evidence="ECO:0000256|RuleBase:RU361183" FT CHAIN 25..988 FT /note="Metalloendopeptidase" FT /evidence="ECO:0000256|RuleBase:RU361183" FT /id="PRO_5041764737" FT DOMAIN 123..322 FT /note="Peptidase M12A" FT /evidence="ECO:0000259|PROSITE:PS51864" FT DOMAIN 324..436 FT /note="CUB" FT /evidence="ECO:0000259|PROSITE:PS01180" FT DOMAIN 437..549 FT /note="CUB" FT /evidence="ECO:0000259|PROSITE:PS01180" FT DOMAIN 549..590 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 593..705 FT /note="CUB" FT /evidence="ECO:0000259|PROSITE:PS01180" FT DOMAIN 749..861 FT /note="CUB" FT /evidence="ECO:0000259|PROSITE:PS01180" FT DOMAIN 862..978 FT /note="CUB" FT /evidence="ECO:0000259|PROSITE:PS01180" FT REGION 82..127 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 82..109 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 216 FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1, FT ECO:0000256|PROSITE-ProRule:PRU01211" FT BINDING 215 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 219 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 225 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 185..207 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" FT DISULFID 187..188 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211" SQ SEQUENCE 988 AA; 111786 MW; DD17B0E27441EA88 CRC64; MPGVARLPLP LLLWLLLLPR PGRPLDLADY TYDLGEEDDS EPVNYKDPCK AAAFLGDIAL DEEDLTAFQV QQVADLRQRT THRSSIKTAA PGNSSAFNCQ STSGQLQRRS RGRWRSRSRS RRAATSRPER VWPDGVIPFV IGGNFTGSQR AVFRQAMRHW EKHTCVTFLE RTDEDSYIVF TYRPCGCCSY VGRRGGGPQA ISIGKNCDKF GIVVHELGHV IGFWHEHTRP DRDRHVSIVR ENIQPGQEYN FLKMELQEVE SLGETYDFDS IMHYARNTFS RGIFLDTIVP KYEVNGVKPP IGQRTRLSKG DIAQARKLYK CPACGETLQD STGNFSSPEY PNGYSAHMHC VWRISVTPGE KIILNFTSMD LYRSRLCWYD YVEVRDGFWR KAPLRGRFCG GKLPEPIVST DSRLWVEFRS SSNWVGKGFF AVYEAICGGD VKKDNGHIQS PNYPDDYRPS KVCIWRIQVS EGFHVGLTFQ SFEIERHDSC AYDYLEVRDG HSETSTLIGR YCGYEKPDDI KSTSSRLWLK FVSDGSINKA GFAVNFFKEV DECSRPNRGG CEQRCLNTLG SYKCSCDPGY ELAPDKRRCE AACGGFLTKL NGSITSPGWP KEYPPNKNCI WQLVAPTQYR ISLQFDFFET EGNDVCKYDF VEVRSGLTAD SKLHGKFCGS EKPEVITSQY NNMRVEFKSD NTVSKKGFKA HFFSDKDECS KDNGGCQQDC VNTFGSYECQ CRSGFVLHDN KHDCKEAGCD HKVTSTSGTI TSPNWPDKYP SKKECTWAIS STPGHRVKLT FMEMDIESQP ECAYDHLEVY DGRDAKAPVL GRFCGSKKPE PVLATGSRMF LRFYSDNSVQ RKGFQASHST ECGGQVRAEV KTKDLYSHAQ FGDNNYPGGV DCEWVIVAEE GYGVELVFQT FEVEEETDCG YDYMELFDGY DSTAPRLGRY CGSGPPEEVY SAGDSVLVKF HSDDTITKKG FHLRYTSTKF QDTLHSRK //