ID A0A8U0QZW8_SALNM Unreviewed; 1226 AA.
AC A0A8U0QZW8;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X1 {ECO:0000313|RefSeq:XP_038853616.1};
GN Name=LOC120051067 {ECO:0000313|RefSeq:XP_038853616.1};
OS Salvelinus namaycush (Lake trout) (Salmo namaycush).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salvelinus.
OX NCBI_TaxID=8040 {ECO:0000313|Proteomes:UP000808372, ECO:0000313|RefSeq:XP_038853616.1};
RN [1] {ECO:0000313|RefSeq:XP_038853616.1}
RP IDENTIFICATION.
RC TISSUE=White muscle {ECO:0000313|RefSeq:XP_038853616.1};
RG RefSeq;
RL Submitted (AUG-2025) 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_038853616.1; XM_038997688.1.
DR AlphaFoldDB; A0A8U0QZW8; -.
DR GeneID; 120051067; -.
DR KEGG; snh:120051067; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000808372; Chromosome 7.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000808372};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1226
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035918592"
FT DOMAIN 37..225
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 223..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..383
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..492
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..980
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 124391 MW; 9F1930405AB90C71 CRC64;
MTSRSLSLWS FGIHLALWYC QLSTAYQLLD ERGSQGQIDL TELIGVPLPP SVSFITGFEG
YPAYSFGPDA NVGRLTKSFI PDPFYRDFAM TVTAKPTTQR GGVLFAITDA YQRVVHLGVA
LSPVEDGSQR VLLYYTDPGD GSTKEAASFK LGDLTGRWAR FTLTVQGAEV RLYMDCEEYH
RVAFQRSPEP LTFEASSGIF VGNAGGTGLD RFVGSIQQLV LKGDPTAPDD QCEEDDPYAS
GYGSGDDSFD DTETMDEVKK VVEEREYIMP EEPMIAPVRA PPTEASPSDD EEDAGESSGQ
EVELTAERGP SQTADAAYRP GSATPSQKGE RGDPGPAGPP GSPGPPGPQS PLGDGSSGEG
EPGPRGPQGP QGPAGTPGAP GNDGQPGSGG KDGDPGENGV QGFPGLPGDP GPKGDKGDPG
VGKPGSPGPP GPPGRPNSSR SLNGVDGSGF GDFDSDTEIM TGPPGPPGPP GLPGPPGSPE
GLSASPGAPG APGKDGEMGK PGLPGVGGHD GDPGPAGERG EKGEPGLSGP PGPKGEPSAA
GFPGLPGSEG PEGKPGLRGP PGPPGPPGRG FSLDLEDIEG SGTLGGFGAV MPRGPQGPIG
KPGPPGQKGK DGQDGLPGVA VKGEPGASGA AGSSGLDGLP GHTGAKGDSG DMGPKGERGQ
DGLSFPGPPG PPGPPGPVIN LQDLLVNDTE GVFNFSGVLE SQGPRGPRGP KGDLGMTGIM
GPPGLKGEKG EPGVMVAADG SMMSGLTGPQ GPKGIKGDCG VPGPAGVMGP IGPEGPKGEY
GYPGRPGRPG ISGHKGDRGD AVVVSGPPGP PGPPGRPGMF NCPKGTVFPI PPRPHCKKAI
NGSKSSTNGG ANCLPTGTKG DRGERGFPGM PAPPLTMLPK GTTGNKGDHG FRGDKGEKGE
AGLPGSPGMP GRSGLVGPKG ETVMGPRGYP GVPGSPGTPG YGRPGPQGLQ GPPGPPGEPS
RFGSAVTIHG PPGPTGPAGP PGTSAMTFPS SEVMMQQTKD SSEGTLSFTT GTGKLYIRVK
QGWKEVLLGD LIPLPINLLL NDEAQPGSGR KYGLKLVALN QPHTGNFGGV YIADKMCYEQ
AKAMGLSAYY RAFLSSPKPR AVNKDLVPQK FRESYPVTNL RGDILFSNYK SIFTGGGGKF
PPNIPIYSFD GRDVLADPFW PKKSIWHGSN TFGNMAVDRS CESWRVNDIS IVGQSSSLSS
GSLIGQQTSS CSNELIILCI ETIEHV
//
