ID A0A8C7F132_ONCKI Unreviewed; 1372 AA.
AC A0A8C7F132;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE SubName: Full=Collagen type XVIII alpha 1 chain a {ECO:0000313|Ensembl:ENSOKIP00005005353.1};
GN Name=LOC109865460 {ECO:0000313|Ensembl:ENSOKIP00005005353.1};
OS Oncorhynchus kisutch (Coho salmon) (Salmo kisutch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8019 {ECO:0000313|Ensembl:ENSOKIP00005005353.1, ECO:0000313|Proteomes:UP000694557};
RN [1] {ECO:0000313|Ensembl:ENSOKIP00005005353.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOKIP00005005353.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSOKIT00005005713.1; ENSOKIP00005005353.1; ENSOKIG00005002438.1.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000694557; Unassembled WGS sequence.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 4.
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 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:UP000694557};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1372
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034235763"
FT DOMAIN 37..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 227..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..428
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..552
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..583
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..602
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..644
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..706
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..848
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..957
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..977
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1007
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1123
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1372 AA; 142054 MW; 3C0A3E4285B2DA4C CRC64;
MHNVLPRCRC SSWLETLVCS VLVLLTPAAS QWPDESSVSL LQLIGDPPPA EITKVYGPDN
SPGYVFGPDA NTGQLARAHL PSPFYRDFSL LFNLKPQSTN GGVIFSVTDP LQQIMYVGVK
LSPVKANRQN VIFYYTEPDS QESYVAATFP VHNLADQWNR FSISVLDDKV TFYINCDDQP
QVVRFERSPD EMELESGAGV FVGQAGGADP NKFLGVIGEL RVVGDPRAAE RQCEEEGDDS
DAASGDDGSG DERIPDGEKK GSGTSIWDAK IQKYVWVEDV RLTVTTTPTS SRPIQQPPVT
RKQSEVSPKK ERDQGGSRGE KGDRGEKGDR GPIGSKGDSG SESGTRGGAR GEKGVLGEKG
MKGKAGFGYP GSKGDPGPAG PPGPPGLPGP AAEVVSRGDG SVVQTVAGPR GPAGPPGASG
PEGPAGADGE PGDPGEDGSQ GPVGPPGFPG IPGDPGFKGE KGDRGEGQPG PRGPPGPPGQ
PAPTRHDRPT FADMEGSGFP DLETLRGLPG LPGPPGLPGA PGTSVVGTGV SGLFGPKGPP
GQDGAPGQPG DPGELGLPGA VGAKGAQGLN GIPGQPGQGG LAGLPGPMGP LGQPGPPGPP
GPSYRVGFDD MEGSGVGVAN GVPGSRGPEG QQGPPGIPGL PGRSGFPGIP GEKGSEGPQG
SDGRPGLDGF PGPNGQKGDS GDRGERGESG RDGNGQPGPP GPPGPPGQII YQTSSSYDGV
VGVAGPQGQA GFPGPIGPKG DMGDPGQPSY GVKGEKGEPG SIIGPDGNTL YLGRLSGEKG
DRGPAGPVGP PGQYGSPGIK GEFGMPGRPG RPGVNGYKGE KGEPSTGAGF SYPGVPGPPG
PPGPPGPAVP VDRFNGYDAS RNYPVTKGEK GDFGAQGLPG TPGVASNFDI FTFKNDLKGE
RGDTGVKGEK GEPSGGYYDP RFGRQQGPPG PPGNPGLMGP KGDSITGPPG PQGPPGSPGI
GYDGRPGNPG PPGPPGPTGS HSLPGAYRPT HPISIPGPPG PAGPPGIPGH TSGVTVLRSY
DTMIATARRQ SEGTLIYIVD KTDLYIRVRN GFRQIMLSDY SPFYRDLDNE VAAVQPPPVV
NYPQSQDHSA NNGAEQFSQG GAATHPIVPP PRQPIEIPRP AQPNNRDPRD PPQYDHRYPS
QTDPRYPPQT DGRYSPVQPE NRYPTQPERQ YHITPQRQPV PPPVPQPAGH VHTSGPGLHL
IALNTPQVGN IRGIRGADFL CFQQARAVGL KGTFRAFLSS KLQDLYSIVR KSDRDSLPIL
NLKDHVLFNS WESLFRKTEG RMEENAPIYS FDGRDILRDS AWPEKMVWHG SSIEGHRQTD
NYCETWRAAD RAVTGLASSL QTGQLLQQLP SSCSSSYIVL CIENSYLSHS KK
//
