ID A0A1S3PSZ4_SALSA Unreviewed; 810 AA.
AC A0A1S3PSZ4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 isoform X2 {ECO:0000313|RefSeq:XP_014030339.1};
GN Name=adam9 {ECO:0000313|RefSeq:XP_014030339.1};
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_014030339.1};
RN [1] {ECO:0000313|RefSeq:XP_014030339.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014030339.1};
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_014030339.1; XM_014174864.1.
DR AlphaFoldDB; A0A1S3PSZ4; -.
DR GeneID; 106587024; -.
DR CTD; 8754; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000087266; Chromosome ssa26.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
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:SF136; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 9; 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; 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|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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
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}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..810
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010255552"
FT TRANSMEM 704..723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 217..411
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 419..506
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 645..679
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 175..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..810
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 370..375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 478..498
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 669..678
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 810 AA; 89354 MW; 18034F7EAA911583 CRC64;
MGMPLLSHPC FKAICVIALL NGLGDCSEGS ASHQTSQFSS YEVTIPKRFG KQRRDMDSSD
SNQVSYIISA MGKEHVVVLE KNDLLLPEDF TVYTHAKDGS LITNRPPMQD HCHYRGYVED
VEGSSVAMSI CFGLRGVLRM DNSSYGIEPL VSSSDFQHLV YRLEDVVSEP LVCGTPHTEQ
LAPSEQDHSD HQTHSDTHKQ PVSHLLRRKR AVLLQPHYVE LLLVVDNERF TYMHRNETAV
RDEMIHLANY IDSMYVELNI RVVLVGLDIW ANGNPISMEG SAGEVLSRFV QWREKELVPR
RRHDSAQLIL KKSFGGTAGM AFVSTVCSRS HGGGINAFTN NNIPSFASIV AHELGHNLGM
NHDDGRNCHC GVTSCIMNSG ATGSRNFSSC SADDFEKMIL NTGGSCLLNI PRPEEAYSAP
YCGNKLVDMG EECDCGSDKE CEKDPCCEAK TCKLKGGAQC AYGVCCKNCQ YLPGGSVCRG
SNDECDLSEY CNGSSALCPS DVFKQNGHPC KVDKAYCYNG KCQHYDGQCR AIFGPKAKAA
PEVCFKDVNS KGDRFGNCGY QNYGYKKCES RNAMCGKLQC ENVQSVTVFG IEPSIIQTPI
AGIKCWGVDF LLGSDVPDPG MVNEGTKCGE NKVCLNYDCR SADVLNYDCD IQKKCHSHGV
CNSNRNCHCE NGWAPPYCEA KGYGGSVDSG PTWNDKDTST RDGLLVFFFL VLPLMALGFF
VFFRRNELQR RFCRRKRSQG YEADSRPQAN TSRGPPPRAN PNIIVKDRVV QTSRTVSVPS
YVVRPPPPYS RPTPAATQLV PQRPAPPPPV
//
