ID A0A8U0TLS3_SALNM Unreviewed; 1345 AA.
AC A0A8U0TLS3;
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 {ECO:0000313|RefSeq:XP_038820323.1};
GN Name=LOC120020688 {ECO:0000313|RefSeq:XP_038820323.1};
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_038820323.1};
RN [1] {ECO:0000313|RefSeq:XP_038820323.1}
RP IDENTIFICATION.
RC TISSUE=White muscle {ECO:0000313|RefSeq:XP_038820323.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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_038820323.1; XM_038964395.1.
DR GeneID; 120020688; -.
DR KEGG; snh:120020688; -.
DR Proteomes; UP000808372; Chromosome 25.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1118; LAMININ G DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000808372};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1345
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035717210"
FT DOMAIN 113..304
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 70..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..460
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..515
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..909
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..941
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1018
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1047
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1064
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1345 AA; 139202 MW; A74833D4D5001FEB CRC64;
MAVLRLCSLL LLLLMAPVHG QWWSVLWGKA QEMITQPPTT EVLTTTKVFW TMEGTEVGQV
GTQTEVYTTA PVQSTPLQST QEPAGAGTTE IKPKAKKRPL KMWKSRELGS TGHLDLTELI
GVPLPPSISY ITGYEGFRPA YNFGPGANIG RLTKTFMPDP FFRDFAIIVT IRPSSNQGGV
LFAITDAQQR VVQLGLALTA VEDQTQRIQL YYTEGGQGSS HSQQVVSFKV PDMTKKWTIF
TLSVQDQEVC LYMDCDDFQA ETFHRSSRQL SFEPSSGIFV GNAGGTGLER FVGSIQQLVI
KSDPRAAEEQ CEEDDPYASG DGSGAETMDD RETESELMNM KRRKETARPE DMLSGPVRAP
PTESPEVELD EYSGHLTPTE EAHQDMQLRG PHQTEEPEMS GDGGPLSHRL KGERGEPGPI
GPAGPRGPPG PPTLSEGRRS GHRQPGPRGP RGPTGAPGVP GKDGQQGSKG EDGDPGQRGP
QGFPGLAGEV GVKGDKGDPG AGLPGPPGPP GPPGPLRSHS VPYGEDALGS GFGDLDNTEL
IRGPPGPPGQ PGPPGPTSPF NVSEGLFTGQ PGPPGRYGLV GKPGPPGQPG LDGDVGSTGP
KGLKGEQGLV GPKGESGDQG LAGATGLRGP EGKRGDTGPR GLPGLPGPPG AGLFVEDMEG
SGKNDMLLDV GLKGPQGPPG LPGSAGPKGE DGKDGAPGLS VKGEPGAPGP EGLQGLAGLP
GARGLKGDKG DPGPKGECGP DGHSVPGSPG PPGSPGPIIN LQDLLLNDTE GMFNQIRGPP
GLMGPEGEPG RAGFPGPRGP KGDIGLPGLH GPPGMKGAKG DSGVTIAADG TVLTGVRGPQ
GPKGIKGERG FPGVAGIMGP IGPTGQKGEY GFPGRPGRPG MAGKKGDKGD AIGQPGLPGP
PGPPGPPGPV IGLNGTVFPV RPRPFCKTPV NGSRGSSQGS RRGNRGAKGE KGEVGLPGTP
GEPDDVLPEG FVGEKGDMGY EGMKGEKGDA GLPGPPGLPG RSGLVGPKGE SIVGAPGHPG
APGEPGVPGI GRPGTRGPPG PAGPPPVYAS AVSIPGPPGP PGPPGITGYE NLVTTYRNTI
TLMRESHRAA EGSMAYASDK GELYVRARDG WRKVQLGELI PFPAGTPSSA LSQALSRPDR
SRPHRQELVG TSYMPNYNVL PHIVHSVPGL HLVALNAPFS GDMRGIRGAD FQCYQQARAI
GLTATYRAFM SSHLQDLATI VKKGDRYSMP VINLKGEVLY GSWMNIFSGN GGVLDPSIPI
YSFDGRNVMT DPAWPQKLVW HGSSTVGIRM TTNYCEAWRA GDMAVTGQAS LLQTGRLLGQ
HTRSCSNRFV VLCIENSYID HRRSN
//
