ID   A0A250Y4N1_CASCN        Unreviewed;       733 AA.
AC   A0A250Y4N1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   02-JUN-2021, entry version 23.
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|PIRSR:PIRSR001199-2,
CC         ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR001199-2,
CC       ECO:0000256|PROSITE-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}.
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DR   EMBL; GFFV01001353; JAV38592.1; -; Transcribed_RNA.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 3.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 2.60.120.290; -; 3.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR029837; BMP-1.
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; PTHR45645:SF24; PTHR45645:SF24; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 3.
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; SSF49854; SSF49854; 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   Differentiation {ECO:0000256|ARBA:ARBA00022782};
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|ARBA:ARBA00022729, 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   METAL           216
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001199-2"
FT   METAL           216
FT                   /note="Zinc; via tele nitrogen; catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   METAL           220
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001199-2"
FT   METAL           220
FT                   /note="Zinc; via tele nitrogen; catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   METAL           226
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001199-2"
FT   METAL           226
FT                   /note="Zinc; via tele nitrogen; catalytic"
FT                   /evidence="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
//