ID   A0A250Y4N1_CASCN        Unreviewed;       733 AA.
AC   A0A250Y4N1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   31-JUL-2019, entry version 15.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha;
OC   Castoridae; 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.,
RA   Engstrom M.D., Dutton C.J., Kerr K.C., Franke M., Rapley W.,
RA   Wintle R.F., Scherer S.W.;
RT   "De Novo Genome and Transcriptome Assembly of the Canadian Beaver
RT   (Castor canadensis).";
RL   G3 (Bethesda) 0-0:755-773(2017).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001199-2,
CC         ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR001199-
CC       2, ECO:0000256|RuleBase:RU361183};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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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:InterPro.
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; IPR013032; EGF-like_CS.
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; 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|SAAS:SAAS00601599};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076,
KW   ECO:0000256|SAAS:SAAS00438935};
KW   Hydrolase {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973787};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001199-2,
KW   ECO:0000256|RuleBase:RU361183, ECO:0000256|SAAS:SAAS00973795};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS01068076};
KW   Protease {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973825};
KW   Repeat {ECO:0000256|SAAS:SAAS00792548};
KW   Signal {ECO:0000256|RuleBase:RU361183};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001199-2, ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973802}.
FT   SIGNAL        1     27       {ECO:0000256|RuleBase:RU361183}.
FT   CHAIN        28    733       Metalloendopeptidase.
FT                                {ECO:0000256|RuleBase:RU361183}.
FT                                /FTId=PRO_5011819595.
FT   DOMAIN      325    437       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      438    550       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      550    591       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      594    706       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   REGION       90    129       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      705    733       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     92    110       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   ACT_SITE    217    217       {ECO:0000256|PIRSR:PIRSR001199-1}.
FT   METAL       216    216       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   METAL       220    220       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   METAL       226    226       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
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
//