GenomeNet

Database: UniProt
Entry: E2RJJ6_CANLF
LinkDB: E2RJJ6_CANLF
Original site: E2RJJ6_CANLF 
ID   E2RJJ6_CANLF            Unreviewed;       988 AA.
AC   E2RJJ6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 2.
DT   05-JUN-2019, entry version 75.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   Name=BMP1 {ECO:0000313|Ensembl:ENSCAFP00000014115,
GN   ECO:0000313|VGNC:VGNC:38475};
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:ENSCAFP00000014115, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000014115, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000014115,
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:ENSCAFP00000014115}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000014115};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
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; AAEX03014378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAEX03014379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; E2RJJ6; -.
DR   STRING; 9612.ENSCAFP00000014115; -.
DR   PaxDb; E2RJJ6; -.
DR   Ensembl; ENSCAFT00000015253; ENSCAFP00000014115; ENSCAFG00000009587.
DR   VGNC; VGNC:38475; BMP1.
DR   eggNOG; KOG3714; Eukaryota.
DR   eggNOG; ENOG410ZPX7; LUCA.
DR   GeneTree; ENSGT00940000157176; -.
DR   InParanoid; E2RJJ6; -.
DR   OMA; KGFEASH; -.
DR   TreeFam; TF314351; -.
DR   Reactome; R-CFA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-CFA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-CFA-2214320; Anchoring fibril formation.
DR   Proteomes; UP000002254; Chromosome 25.
DR   Bgee; ENSCAFG00000009587; Expressed in 3 organ(s), highest expression level in liver.
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:InterPro.
DR   GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl.
DR   CDD; cd00041; CUB; 5.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 2.60.120.290; -; 5.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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; 5.
DR   Pfam; PF07645; EGF_CA; 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; SSF49854; SSF49854; 5.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01180; CUB; 5.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
PE   4: Predicted;
KW   Calcium {ECO:0000256|SAAS:SAAS00909960};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002254};
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   Reference proteome {ECO:0000313|Proteomes:UP000002254};
KW   Repeat {ECO:0000256|SAAS:SAAS00594563};
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     24       {ECO:0000256|RuleBase:RU361183}.
FT   CHAIN        25    988       Metalloendopeptidase.
FT                                {ECO:0000256|RuleBase:RU361183}.
FT                                /FTId=PRO_5005127753.
FT   DOMAIN      324    436       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      437    549       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      549    590       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      593    705       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      705    745       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      749    861       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      862    978       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   REGION       82    127       Disordered. {ECO:0000256|MobiDB-lite:
FT                                E2RJJ6}.
FT   COMPBIAS     82    109       Polar. {ECO:0000256|MobiDB-lite:E2RJJ6}.
FT   ACT_SITE    216    216       {ECO:0000256|PIRSR:PIRSR001199-1}.
FT   METAL       215    215       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   METAL       219    219       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   METAL       225    225       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
SQ   SEQUENCE   988 AA;  111828 MW;  F4004F8C8343B8E8 CRC64;
     MPGVARLPLP LLLWLLLLPR PGRPLELTVY TYDLGEEEDS 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
//
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