ID A0A1S3NWY8_SALSA Unreviewed; 1495 AA.
AC A0A1S3NWY8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Collagen alpha-2(V) chain-like {ECO:0000313|RefSeq:XP_014019899.1};
GN Name=LOC106581929 {ECO:0000313|RefSeq:XP_014019899.1};
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_014019899.1};
RN [1] {ECO:0000313|RefSeq:XP_014019899.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014019899.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014019899.1; XM_014164424.1.
DR STRING; 8030.ENSSSAP00000072165; -.
DR Allergome; 12212; Sal s 6.
DR PaxDb; 8030-ENSSSAP00000072165; -.
DR GeneID; 106581929; -.
DR KEGG; sasa:106581929; -.
DR CTD; 564821; -.
DR OMA; KIECREM; -.
DR OrthoDB; 2970887at2759; -.
DR Proteomes; UP000087266; Chromosome ssa21.
DR Bgee; ENSSSAG00000057090; Expressed in nose and 13 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 6.20.200.20; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 4: Predicted;
KW Collagen {ECO:0000313|RefSeq:XP_014019899.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1495
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010262806"
FT DOMAIN 34..92
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 1263..1495
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 97..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1495 AA; 144687 MW; 5FF91752B7912221 CRC64;
MMSFVHSRIC LFLVVSVAQV LIVKCQDGNS GDDAGCTVDG QVYTNRDIWK PEPCRICVCD
SGSVLCDEIQ CDELSNCEKV TIPEGECCPI CQSEGGSDTS GNVRPDGGRV YRGQKGEPGE
VPQVTGIRGR PGPMGPPGSP GFRGDRGQKG RPGLRGPAGY DGEPGVPGNP GEPGPAGNQG
PPGGLGAQMA GGFGDEKSAG QTAMVPGTSG EAGARGPPGP NGNPGHAGPQ GPPGEVGDPG
HMGTSGQRGP EGPPGKPGED GEGGKSGNPG EMGFPGSAGA RGFPGTPGPP GLKGHRGHTG
PIGLRGETGT VGSKGALGPT GPIGTPGPMG PRGMPGERGR LGANGVPGMK GPPGNIGKSG
PMGPLGINGP PGYPGIPGMK GQPGATGVRG PEGQQGQRGE TGHQGRAGST GQQGPSGTDG
GPGTKGPVGT MGVQGPGGHL GPHGPPGPQG STGQPGIKGQ LGDVGIPGYK GEAGPKGEPG
PPGSQGVIGP QGEEGKRGTR GDSGSLGPPG PVGERGSPGN RGFPGADGLP GPKGAQGDRG
PSGISGPKGS GGDPGRTGEP GLPGARGLTG TPGVQGAEGK PGPLGPAGED GRPGPAGSIG
TRGPAGTMGT PGPKGFNGDP GKTGEQGSLG VAGQRGPPGK DGEVGPAGPA GPLGVAGERG
EQGPPGVNGF QGLPGPPGPP GESGKPGDLG IPGEGGAVGQ IGPRGERGIP GERGELGPHG
LAGAKGIPGA PGPDGPKGSP GPTGSLGDLG PPGLQGMPGE RGISGSPGPK GDRGSGGEKG
SEGTPGNDGA RGLPGPLGPP GPNGPSGEKG EAGPKGPPGP HGSRAMPGPR GEPGPIGPVG
FGGPPGPDGQ PGVKGEPGEP GQKGDAGSPG PQGLAGSHGP PGIVGVAGLK GGRGTQGAPG
PTGFPGSAGR VGPPGSAGPV GEAGPLGSPG KEGPPGLRGE NGSPGRQGER GPPGPAGGSG
DKGDSGEDGP TGPDGPPGPA GTTGQRGIVG LPGQRGERGM LGLPGPAGPP GKQGTAGPGG
DKGPTGPIGS PGANGPRGDP GPDGPAGSDG PPGKDGVIGQ RGDRGDHGPE GLVGTPGQPG
TPGPVGATGG SGKRGDAGSR GPNGPPGSAG KRGLTGPQGP RGDKGDLGDH GERGQKGHRG
FTGLQGLPGP PGTTGEQGAS GIIGPSGQRG PPGPVGPTGK EGYIGQPGPM GPPGTRGISG
EIGPEGPPGE PGPNGPPGPP GPPTAAMDDL FGGMHDYDAG PPPPEFNEDE ALPNSNATQQ
LDPGVQATLK ALSSQIDSMK SPDGSRKHPA RTCEDLKQCY PLKKSGEYWV DPNQGSSEDA
IKVHCNMETG ETCISANPAS IPKKVWWNTS RKKPVWFGAD INRGTQFTYG NKDQPANSVT
VQMTFIRLLS KEASQTITYH CKNTVGYKDE ATGNLKKAVI LKGSNDLELK AEGNNRFRYT
VVEDSCGQSN GKWGKTVFEY RTQKTARLPI MDMAPVDIGG SNQEFGIDIG PVCFL
//
