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Database: UniProt
Entry: A0A1S3PM83_SALSA
LinkDB: A0A1S3PM83_SALSA
Original site: A0A1S3PM83_SALSA 
ID   A0A1S3PM83_SALSA        Unreviewed;       785 AA.
AC   A0A1S3PM83;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   05-JUN-2019, entry version 17.
DE   SubName: Full=disintegrin and metalloproteinase domain-containing protein 23-like isoform X1 {ECO:0000313|RefSeq:XP_014028803.1};
GN   Name=LOC106586256 {ECO:0000313|RefSeq:XP_014028803.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
OC   Salmoniformes; Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014028803.1};
RN   [1] {ECO:0000313|RefSeq:XP_014028803.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014028803.1};
RG   RefSeq;
RL   Submitted (JUN-2017) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   RefSeq; XP_014028803.1; XM_014173328.1.
DR   GeneID; 106586256; -.
DR   KEGG; sasa:106586256; -.
DR   KO; K06837; -.
DR   OrthoDB; 162519at2759; -.
DR   Proteomes; UP000087266; Genome assembly.
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; 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   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000087266};
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|RefSeq:XP_014028803.1};
KW   Membrane {ECO:0000256|SAAS:SAAS01078504, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
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     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    785       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010262812.
FT   TRANSMEM    747    770       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      254    451       Peptidase M12B. {ECO:0000259|PROSITE:
FT                                PS50215}.
FT   DOMAIN      457    542       Disintegrin. {ECO:0000259|PROSITE:
FT                                PS50214}.
FT   DOMAIN      686    723       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   REGION      722    743       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1S3PM83}.
FT   COILED      214    234       {ECO:0000256|SAM:Coils}.
FT   DISULFID    514    534       {ECO:0000256|PROSITE-ProRule:PRU00068}.
FT   DISULFID    713    722       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   785 AA;  86744 MW;  442682AB2705E437 CRC64;
     MHLIFLANLL VSILASWLHP SIAAIVSQGG ENEVVERDAV SLLLEREATA ATATDNTSHH
     AAEHVITYPS RLIYYLNEDS ESTYHDLDTR ARNQATEGHD QAVHLAQASF QLEAFGSRFV
     LDLTLNNDLL SSDYVEIHYE GGKPVLSKGG EHCYYHGQVR GEDDSNVALS TCNGLHGMFD
     DGLYVYLIEP LQQTHSIDTA ARPHSLRRRP TLQRNNDQEE LVEEEQLLSE LDDMSWLKRR
     KKRAMPRNVF EEMKYLEIMI VSDHNMYKRH KTKQHTRNFA KSVVNFVDAI FKEHLHTRVV
     LVAVEIWTDK DHIPISVKPL DMLKDFSKYR AQSIKQHADS VHLFTNVTFH YRRSSAAYFG
     GMCSVSRGVG VNEYGTTWTM ASSLSQSLAQ NLGIQWDPAA KRKECGCADS WVGCIMEDTG
     VQHPRMFSKC SISDYKEFLL KGGGSCLFNR PNKLFESTEC GNGYIEVGEE CDCGARSECY
     KECCKKCSLA NGAHCADGPC CNNTCLFYPR GYSCRYAVND CDISETCSGD SGQCPPNLHK
     QDGYHCQVDQ GRCYGGECKT RGNQCKYLWG SKAGGSEKFC YEKLNTEGTE KGNCGKDGEK
     WLQCSKHDVF CGSLLCSNIG RNPRIGMMKG DITPTSFNHQ GRLVDCSGGH VLLDDETDLG
     YVEDGTPCGP SMMCLDRKCL PIQSLNMSAC PSGPNSQVCS AHGVCNNEAS CTCDTTWAGT
     DCSMPDPPKE PAPAEDEGPK GPSATNLIIG SIAGAILVAA IVLGGTGWGF KNVKKRRYDP
     NASAI
//
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