ID A0A1S3R7I4_SALSA Unreviewed; 776 AA.
AC A0A1S3R7I4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11-like isoform X2 {ECO:0000313|RefSeq:XP_014048325.1};
GN Name=LOC106601009 {ECO:0000313|RefSeq:XP_014048325.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014048325.1};
RN [1] {ECO:0000313|RefSeq:XP_014048325.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014048325.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_014048325.1; XM_014192850.1.
DR AlphaFoldDB; A0A1S3R7I4; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000087266; Chromosome ssa03.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
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 PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF114; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 11; 1.
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; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..776
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010262836"
FT TRANSMEM 742..765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..444
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 450..537
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 681..718
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 196..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 509..529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 708..717
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 776 AA; 85160 MW; 66CEBD013A5E6E51 CRC64;
MLAVWCLVFA AVGERFAVSG RSTLVRDASL WDWFSPEERG DSSDIAAEVT YPKRLVQQLE
SEEEMSHGYL DTRVKNTTGG TSPVHLAQSC FQVETFGHTF TLDLELNHNL LSSDYVERHF
HQDGKPSQSK GGEHCYYQGR LRGLPESWAA LSTCLGLCGM FSDGMFSYGI EPLFDGTNQT
EGAHLVRRMP DVRLSPDCQD CTDDSEGDRA RGNGDEQLKD PRVSEVLRRS KRQLPRRPTV
QSETKYIELM VVNDYEMFVQ LRRSTTQARN FAKAVVNMAD AIYREQLNTR IVLVAMETWS
SANMVPVVTD PLTTLQNFMK YRKDSIKEQS DVVHLFSGRT FQSSRSGTAY TGGVCSLTRG
GGINEYGNVG PMAITLCQSL GQNIGMRWNN IRSSAGDCRC PDSWLGCIME DTGYYLPRKF
SRCSVDEYIQ FLLQGGGSCL FNKPNKLLDP PECGNGFVET GEECDCGSQL ECARSGGACC
KKCTLTHDAM CSSGLCCSGC RYELRGAVCR QAVNDCDIPE SCTGDSSQCP HNVHKLDGYM
CDSSQGRCYS GRCRTLDGQC KGLWGYNSAD RFCYEKLNAE GTEKGNCGRS PEGQGWLQCN
KPDVLCGFLF CINMTVKPKF GDLEGEVTSL TIYHQNKYLD CRGGHVLLED GSDLGYVEDG
TPCGPNMMCL ERHCLPVAAF NLSTCSGSTL GRTCSDHGTC SNEVKCICDR DYTGKDCSVF
DPIPDPTPPA NTEKKGPSGT NIIIGSIAGA ILLAAIVLGG TGWGFKNIRR GRSGGG
//
