ID A0A8C8FXV2_ONCTS Unreviewed; 1827 AA.
AC A0A8C8FXV2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 2.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=LOC112225087 {ECO:0000313|Ensembl:ENSOTSP00005040597.2};
OS Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=74940 {ECO:0000313|Ensembl:ENSOTSP00005040597.2, ECO:0000313|Proteomes:UP000694402};
RN [1] {ECO:0000313|Ensembl:ENSOTSP00005040597.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOTSP00005040597.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: May regulate extracellular matrix-dependent motility and
CC morphogenesis of endothelial and non-endothelial cells; the function
CC requires homotrimerization and implicates MAPK signaling.
CC {ECO:0000256|ARBA:ARBA00053766}.
CC -!- FUNCTION: Probably plays a major role in determining the retinal
CC structure as well as in the closure of the neural tube.
CC {ECO:0000256|ARBA:ARBA00054383}.
CC -!- SUBUNIT: Forms homotrimers. Recombinant non-collagenous domain 1 has
CC stronger affinity to NID1, HSPG2 and laminin-1:NID1 complex and lower
CC affinity to FBLN1 and FBLN2 than endostatin.
CC {ECO:0000256|ARBA:ARBA00065165}.
CC -!- SUBUNIT: Monomeric. Interacts with KDR/VEGFR2. Interacts with the
CC ITGA5:ITGB1 complex. Interacts with NID1, HSPG2, laminin-1:NID1
CC complex, FBLN1 and FBLN2. {ECO:0000256|ARBA:ARBA00064471}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR AlphaFoldDB; A0A8C8FXV2; -.
DR Ensembl; ENSOTST00005044185.2; ENSOTSP00005040597.2; ENSOTSG00005019363.2.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000694402; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR CDD; cd07455; CRD_Collagen_XVIII; 1.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 1.10.2000.10:FF:000017; Alpha 1 type XVIII collagen; 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; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR035523; Collagen_XVIII_Fz.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 3: Inferred from homology;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000694402};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1827
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044325751"
FT DOMAIN 340..457
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 33..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..58
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 158..168
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..205
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..722
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..817
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..910
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..950
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1033
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1052
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1434
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1594
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 355..401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1827 AA; 190232 MW; 242273C84F80CEB4 CRC64;
MDCKIGFQLS ISLLVVVLVG RCEALWFSWG STDGTTEAPS LDNEGSGNPV TSNESPTPEN
IEEVGADIID IESGIHKFAQ TWNQNAKATE APKLTTVRSK ARNERPMEKG AGRPTSRGSK
PGNDMSTVQG MGSGLWEWLG VGSGSGFGSW SGFGSGSEFG SRSGFESESS SEFDSESEIR
HGSQIRPVSG IEFGSQSGSS IESGSKPGAS MWDSQEGTVL PTDLTGLAEN VNVLAGKENE
MLGIVKVDLA ERVLDKHNRT AEWNATVFPI DSQPVPSVNV SLETTPSNRS SNRVIDSSSS
WNANNFNSTE YSDEYTVSGD FLTPFDSNHS LLATSETPAP ESPRCWPIDF HLPFCKSMGG
DSFVLPNYFN HSSVKEVQAV LGSWAWLLRS RCHHSLEWFF CLLLLPRCPR GLPPPLPCRS
FCEVLQDSCW TVLDEGSLPM ECHSLPDEDD GYQCLSVSNQ KDEIGVSLLQ LIGDPPPDEI
TKIYGPDNSP GYVFGPDANT GQLARAHLPS PFYRDFSLLF NLKPQSTKGG VIFSVTDASQ
KIMYVGVKLS PVKANKQNVI FYYTEPDSQV SYVAATFPVH NLADQWNRFS ISVLDDKITF
YINCDDQPQV VRFERSPDEM ALEAGAGVFV GQAGGADPDK FLGVIGELRV VGNPRAAERQ
CEEEGDDSDV ASGDGGSGDV EGKLDGKKKG SGTFKWDAEV QKNVWVEDDR PTVTTTPPSS
RPIQQPPVTR QQPEVSPKKE TGPGGSRGEK GDRGEKGDRG PFGPKGDSGS ESGTRGGARG
EKGVPGEKGM KGKAGFGYPG SKGDPGPAGP PGPPGSPGPA AEVVSRGDSS VIQTVAGPRG
PAGTPGPAGP EGPAGADGEP GDPGEDGSQG LVGPPGFPGT PGDSGLKGEK GDRGEGQPGP
SGPPGPPGLP APSSHDRPTF VDMEGSGFPD LEALRGLPGL PGPPGLPGAP GPSVVGTGLS
SSFGPQGPPG QDGAPGQPGL PGPPGTDGRP AVAGARGEKG DPGELGLPGA VGAKGAQGLT
GIPGQPGLGG LAGLPGPMGP VGQPGPPGPP GPSYHAGFDD MEGSGVGVAN GVPGARGPDG
RQGTTGIPGL PGKPGFPGAP GEMGNEGLQG RDGRPGLDGF PGPNGQKGDR GERGETGRDG
NGQPGPPGPP GPPGQIIYQT SSSYDGVVGG AGPQGETGLP GQAGFPGPIG SKGDKGDPGQ
PGYGVKGEKG EPGLIIGPDG SPLYLRELSG EKGDRGPAGP VGPPGQYGPS GIKGEFGMPG
RPGRPGVNGY KGEKGEPSTG AGFGYPGVPG PPGPPGPPGP AVPVDRFNGY DASRNYPATK
GEKGDRGAQG LPGTPGVASN LDIFTFKNDL KGERGDSGMK GEKGEPSGGY YDPRFRGQQG
PPGPPGNPGL MGPKGDSIMG LPGPQGPPGS PGIGYDGRPG IPGPPGPPGP PGSPSLPGAY
RPNHSINIPG PPGPAGPPGT PGHTSGVTVL RSYDTMIATA RRQSEGTLIY IVDKTDLYIR
VRNGFKQVLL GDYSPFYRDL DNEVAAVQPP PVVNYPQSQD HSANNGAEHF SQGGTATLPI
KPPPHKPVEI PRPARPDNRN PDPRYPPQYD PRYPPQTDAR YPPQTDGRYS HVQPENRYPN
QPESRFPVTP QRRPVPLPVP QPGGHLHTSG PGLHLIALNM PQVGNMRGIR GSDFLCFQQA
RAVGLKGTFR AFLSSKLQDL YSIVRKSDRD SLPIINLKDQ VLFNSWESMF SKTGGRMKEN
VPIYSFDGRD ILRDSAWPEK MVWHGSSNEG HRQTDNYCET WRAGDHEVTG LASSLQTGQL
LQQLPSSCSS SYIVLCIENS SLSHSKK
//
