ID K1PLE9_CRAGI Unreviewed; 1163 AA.
AC K1PLE9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=CGI_10008190 {ECO:0000313|EMBL:EKC19594.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC19594.1};
RN [1] {ECO:0000313|EMBL:EKC19594.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC19594.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
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}.
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DR EMBL; JH815853; EKC19594.1; -; Genomic_DNA.
DR RefSeq; XP_011436127.2; XM_011437825.2.
DR AlphaFoldDB; K1PLE9; -.
DR HOGENOM; CLU_274989_0_0_1; -.
DR InParanoid; K1PLE9; -.
DR OrthoDB; 2958715at2759; -.
DR GO; GO:0016020; C:membrane; 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; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00108; KR; 4.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 5.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR000998; MAM_dom.
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 PANTHER; PTHR24261:SF7; KRINGLE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00051; Kringle; 5.
DR Pfam; PF00629; MAM; 1.
DR PRINTS; PR00480; ASTACIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00130; KR; 5.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57440; Kringle-like; 5.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS00021; KRINGLE_1; 4.
DR PROSITE; PS50070; KRINGLE_2; 5.
DR PROSITE; PS50060; MAM_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT ACT_SITE 264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 360..370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 384..393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 534..544
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 539..556
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 558..567
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 862..885
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 990..999
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1053..1076
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1135..1158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 1163 AA; 131086 MW; C642C52A3EAC0D62 CRC64;
MAVNNLSGLD PSIPVNDSDT IYTGVFLAPP DTQFEYDGRN NVVVAILSDN SNFERWLTLK
LGCVQLSFGS PEYGGLLFTS DSPRVLSLEA TTGHIPLDID PDDPDMRLFL SMGVGVDGAV
KHSKGLHPEN SKRLQARRLD KPDDSEKKTE NKRKPSRKPK RRRKRNFGPN WGKWPKGIVP
YVFDASLDVN RGYFLQAIEL FNNFTCVRWK PKSPEVAAEV GHEGYVLVRS GTSCSSGVGF
NGDGEHIINF KEPGCGWVDV AVHEMLHRIG QRHEHARSDR DRYVKINWDN IHISGRYNYY
RLNTYNRNPY DIGSVMHYGY SSSETADIEL KDKNLNFLEF PGSQIFSYYD LKDVIDQYQC
AAHCISPPVC QNGGYVNANC QCTCPEGFSG VSCDTVVTDP DCGGYVHLKE NDLVLEREKV
AFITSPNYPG PIGLGKICRW AVTVPVGYII KMTIDDLHMA YNPDTLRCYH WLEIQYNLPG
QHGIRRCGDI VGETFLSSID SPTLMIITMD TKLAGGRVTK KGFKLHVEKE REVCRDSPCV
FGICVPTERK SYEYKCVCQP GYTGDKCDQV VDGAKLKCSF ERFEKCFFDN VQEGDEFEWG
PGFRHTISEW TGPEDAFRGE RFIFAEMSLP RVPGDKAILQ TTVALPEQAG CLSFAYNMFG
STVYKLTLYA EGTNSPKYVL WSKEGNQGSD WLTAKVDVPA IQGLKLSFEA VTGDSWDSDI
ALDEITWETG QCGPDTFNDC LRVGKEYGGT RNYTKRGVTC QAWSSNTPHT PGSQYAYLAS
DSNYCRIADE PDPWCYTTDA GTRWDWCSIP YCFATECAYT PTGMDYMGTV SHTKTGIPCQ
RWDSQSPHPH SYGYLSKDEN YCRNTDGSEG PWCYTQDPDI RYELCDVPVC EKIEQECLMT
SRGLDYAGKQ SVTNTGKTCE HWTDEQMSED ENYCRNPDQS VKPWCYVQSG TGLVKEYCDI
PSCADSPCFP NPCKNRGECS VEGASYSCTC LNGFSGDNCE TQELGNQEDC KRSSNGWDYS
GNRNVTQSGR TCQVWSAQSP HSHGYTSYPE NYCRNPDGEP SPWCYTTDPY KRWELCDIPD
CVSPPLECLP NSDLRGRQYY GTQSVTETGD TCQRWDSQSP FTHSFSYLGD QENYCRNPDS
DLKPWCFTTN VNRRYGYCNV PYC
//
