ID A0A1S3NVB5_SALSA Unreviewed; 1476 AA.
AC A0A1S3NVB5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 36.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X2 {ECO:0000313|RefSeq:XP_014019358.1};
GN Name=LOC106581675 {ECO:0000313|RefSeq:XP_014019358.1};
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:UP001652741, ECO:0000313|RefSeq:XP_014019358.1};
RN [1] {ECO:0000313|RefSeq:XP_014019358.1}
RP IDENTIFICATION.
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}.
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DR RefSeq; XP_014019358.1; XM_014163883.2.
DR STRING; 8030.ENSSSAP00000054996; -.
DR PaxDb; 8030-ENSSSAP00000054996; -.
DR GeneID; 106581675; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP001652741; Chromosome ssa21.
DR Bgee; ENSSSAG00000053453; Expressed in mesonephros and 23 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF4; COLLAGEN ALPHA-1(XXIII) CHAIN; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 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 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_014019358.1};
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:UP001652741};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1476
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010259150"
FT DOMAIN 125..314
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..382
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..610
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..693
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..712
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..813
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..950
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1083
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1476 AA; 152257 MW; D9901F45FC41A4D3 CRC64;
MDCKIGFHLS VSLLVVVLVG RCEAFWFSWG GTDGTTEAPS LDNEGSLNPV TSNESPMPEN
IEEVGADLID IASGIHTFVQ TWNQNAKATD APKLTTVRSK ARNERPMEKV AGRPTSRGSK
PDEIGVSLLH LIGDPPPEEI TKIYGPDNSP GYVFGPDANT GQLARAHLPS PFYRDFSLLF
NLKPQSTKGG VIFSVTDASQ KIMYVGVKLS PVKASKQNVI FYYTEPDSQV SYVAATFPVH
NLADQWNRFS ISVLDDKVTF YINCDDQPQV VRFERSPDEM ELEPGAGVFV GQAGGADPDK
FLGVIGELRV VGNPRAAERQ CEEEGDDSDV ASGDGGSGDV EGKLDGKKKG PGTFKWDAEV
QKYVWVEDDR PTVTTTPPSS RPIQQPPVTR QQPEVSPKKE TGPGGSRGEK GDRGEKGDRG
PFGPKGDSGS ESGTRGGAHG EKGVPGEKGI KGKAGFGYPG SKGDPGPAGP PGPPGSPGPV
AEVVSRGDSS VIQTVAGPRG PAGTPGPAGP EGPAGADGEP GDPGEDGSQG LVGPPGFPGT
PGDSGLKGEK GDRGEGQPGP SGPPGPPGLP APSSHNRPTF VDMEGSGFPD LETLRGLPGL
PGPPGLPGAP GPAVVGTGLS SSFGPQGPPG QDGAPGQPGL PGPPGTDGRP AVAGARGEKG
DPGELGLLGA VGAKGAQGLT GIPGQPGQGG LAGLPGPMGP VGQPGPPGPP GPSYHAGFDD
MEGSGVGVAN GVPGARGPDG RQGTTGIPGL PGKPGFPGAP GEKGSEGLQG RDGRPGLDGF
PGPNGQKGDR GERGETGRDG NGQPGPPGPP GPPGQIIYQT SSSGGTGLPG QAGFPGPIGP
KGDMGDPGQP GYGVKGEKGE PGLIIGPDGS PLYLGELSGE KGDRGPAGPV GPPGQYGPSG
IKGEFGMPGR PGRPGVNGYK GEKGEPSTGA GFGYPGVPGP PGPPGPPGPA VPVDRFNGYD
ASRIYPATKG EKGDHGAQGL PGTPGVASNL DIFTFKNDLK GERGDSGVKG EKGEPSGGYY
DPRFRGQQGP PGPPGNPGLM GPKGDSIMGL PGPQGPPGSP GIGYDGRPGI PGPPGPPGPP
GSPSLPGAYR PNHSINIPGP PGPAGPPGTP GHTSGVTVLR SYDTMIATAR RQSEGTLIYI
VDKTDLYIRV RDGFKQVLLG DYSPFYRDLD NEVAAVQPPP VVNYPQSQDH SANNGAEHFS
QGGSAIHHIK PPPRKPVEIP RPAKPENRNP DPRYPPQYDP RYPPQTDAKY PPQTDGRYSH
VQPENRYPTQ PESRFPVTPQ RRPIPLPVPQ PAGHLHTSGP GLHLIALNMP QVGNMRGIRG
SDFLCFQQAR AVGLKGTFRA FLSSKLQDLY SIVRKSDRDS LPIINLRDQV LFNSWESMFS
KTGGRMKENA PIYSFDGRDI LRDSAWPEKM VWHGSSNEGH RQTDNYCETW RAGDRAVTGL
ASSLQSGQLL QQLPSSCSSS YIVLCIENSY LSHSKK
//
