GenomeNet

Database: UniProt
Entry: A0A0F8C7J9_LARCR
LinkDB: A0A0F8C7J9_LARCR
Original site: A0A0F8C7J9_LARCR 
ID   A0A0F8C7J9_LARCR        Unreviewed;       815 AA.
AC   A0A0F8C7J9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUN-2019, entry version 30.
DE   SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 {ECO:0000313|EMBL:KKF12729.1};
GN   ORFNames=EH28_12585 {ECO:0000313|EMBL:KKF12729.1};
OS   Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Larimichthys.
OX   NCBI_TaxID=215358 {ECO:0000313|EMBL:KKF12729.1};
RN   [1] {ECO:0000313|EMBL:KKF12729.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSNF {ECO:0000313|EMBL:KKF12729.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:KKF12729.1};
RX   PubMed=25835551;
RA   Ao J., Mu Y., Xiang L.X., Fan D., Feng M., Zhang S., Shi Q., Zhu L.Y.,
RA   Li T., Ding Y., Nie L., Li Q., Dong W.R., Jiang L., Sun B., Zhang X.,
RA   Li M., Zhang H.Q., Xie S., Zhu Y., Jiang X., Wang X., Mu P., Chen W.,
RA   Yue Z., Wang Z., Wang J., Shao J.Z., Chen X.;
RT   "Genome Sequencing of the Perciform Fish Larimichthys crocea Provides
RT   Insights into Molecular and Genetic Mechanisms of Stress Adaptation.";
RL   PLoS Genet. 11:E1005118-E1005118(2015).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KQ042638; KKF12729.1; -; Genomic_DNA.
DR   RefSeq; XP_010739201.2; XM_010740899.2.
DR   STRING; 215358.XP_010739201.1; -.
DR   GeneID; 104926903; -.
DR   KEGG; lco:104926903; -.
DR   KO; K06834; -.
DR   OrthoDB; 162519at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068,
KW   ECO:0000256|SAAS:SAAS00117091};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Integrin {ECO:0000313|EMBL:KKF12729.1};
KW   Membrane {ECO:0000256|SAAS:SAAS01078504, ECO:0000256|SAM:Phobius};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAAS:SAAS01078486,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS01078482,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    815       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002527995.
FT   TRANSMEM    694    716       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      207    403       Peptidase M12B. {ECO:0000259|PROSITE:
FT                                PS50215}.
FT   DOMAIN      411    497       Disintegrin. {ECO:0000259|PROSITE:
FT                                PS50214}.
FT   DOMAIN      637    671       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   REGION      731    773       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0F8C7J9}.
FT   REGION      787    815       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0F8C7J9}.
FT   COMPBIAS    734    752       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0F8C7J9}.
FT   COMPBIAS    753    767       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A0F8C7J9}.
FT   COMPBIAS    791    815       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A0F8C7J9}.
FT   DISULFID    469    489       {ECO:0000256|PROSITE-ProRule:PRU00068}.
FT   DISULFID    661    670       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   815 AA;  88966 MW;  C73E238C0A789545 CRC64;
     MVRKYILFAV FLLFDVSGGD SEDNFNGFAL KLPKYSIVNP QAIHRWTRSI NNQSKQKSEE
     DMITYALNID NRKHFLHLQK NKDFLHPNFV QYSHDATGNH KSTYPKQHVH CYYHGEVEGY
     ENSVVVLSTC SGLRGVILLE NETYGLEPVP RSTTNEHLLY LLKDLQSDHV TCGVIGEAAS
     TQKHEPFEPG QSLTSLLRRK RNLPQTSYVE LVLVVDNLRY NFKKQNETAV RDEMVEMANL
     LDGYYKQLNI RIVLVGLEIF KDVNPFSVDG SAGDVLGRFV KWRKASLLPR IRHDIGQLIV
     GRPNPYDGGV LGMAFVGTVC SVATSGGINV LSDDSLAYVS TVVAHEMGHN MGMHHDDTRC
     KCDGGSCIMA ATAGGSTTFS TCSGEDFEAL IIRGGGVCLK NQPSPSDVIG TAQCGNGRMD
     EGEQCDCGTP EECNNKCCDA ATCTFTSGSA CAQGDCCDNC QIRVAGTPCR NSVNICDLPE
     YCNGKTASCP EDFYIMDGLP CQDAYCYEGR CQTYDFQCKQ LFAPDPATKA DNICFEYANT
     RGNLFGNCGI TSSGGHIKCS VADSMCGKVQ CTNVDLSTIP SGAHVSIQMV QGSTCINADF
     NLGTDVLDPA YVNPGSPCDK GKTCLDFKCV NASALLPDLD CDAQTTCNNR GVCNDQGHCH
     CDNGWAPPNC DKSGRGGSID SGPAQIDYSL RNGLLIFFLL VVPLLVLLIL ALLYIFRRDT
     LDSCLKRSRL KSRHTQNVNN QSNNNVQTSV TTLPPAQPPP ERPAYPPATS VPISGFRYGE
     LDYWNTEPIT APEQPPAPRQ GPGVPKPIAP KQPPN
//
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