ID A0A8C7J0H7_ONCKI Unreviewed; 1329 AA.
AC A0A8C7J0H7;
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 XV, alpha 1b {ECO:0000313|Ensembl:ENSOKIP00005079307.1};
GN Name=col15a1 {ECO:0000313|Ensembl:ENSOKIP00005079307.1};
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:ENSOKIP00005079307.1, ECO:0000313|Proteomes:UP000694557};
RN [1] {ECO:0000313|Ensembl:ENSOKIP00005079307.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOKIP00005079307.1}
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 RefSeq; XP_031666160.1; XM_031810300.1.
DR Ensembl; ENSOKIT00005084494.1; ENSOKIP00005079307.1; ENSOKIG00005034193.1.
DR GeneID; 109874915; -.
DR GeneTree; ENSGT00940000164061; -.
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; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1329
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034305760"
FT DOMAIN 110..300
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 159..299
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 301..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..687
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..924
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1027
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1044
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1329 AA; 137477 MW; 799B99FADBA3BC51 CRC64;
MALLCLYSLL LLMAPVHGQW WSAFLGKSQE MTTQPLTTVP TTTQVLWTTE GTEVGQVGTQ
TEVFTTAPVQ STPLQSIQEP AGDGTTEIKP KAKKISLKMW KSRERGSTGH LDLTELIGVP
LPPSVSFITG YEGFPAYGFG PDANIGRLTK TFMPDPFFRD FAIIVTIRPS SKQGGVLFAI
TDAQQKVVQL GLALTPVEDE TQRIQLYYTE GGEESSHSQQ VASFKLPDMR NKWTRFTLSV
QDQEVRLYMD CDDFQAETFH RSSRQLSFEP SSGIFVGNAG GTGLEKFVGS IQQLVIKPDP
RAAEEQCEED DPYASGDGSG DDTLHDRETD DKLMNTERKK ETARPEDMLS VPVRAPPTES
PELELDEYTV HLTPTNQAHQ EMLLEVSHQT EEPGERSGDG RPLSYGQKGE QGEPGPMGPA
GPRGPPGPST PSEDRSGHGQ PGPRGPQGPS GAPGVPGKDG QPGRKGEDGD PGQRGPHGFP
GLAGEVGVKG DKGDTGVGLP GPPGPPGPLK SHSVPYGEDA LGSGFGDLDD TEFIRGSPGP
PGPPGQPGPP GPTRFFEASE GLFPGQPGSP GPPGRDGLVG KHGPPGPTGL DGDAGVTGPT
GLKGEQGLAG PNGPMGVSGD PGLTGATGPR GLEGKTGDPG PRGLPGPPGP PGGRFFVEDV
EGSGKNDMVL GTELKGPQGP PGLPGPAGPK GEDGKDGASG LSVKGEPGAS GPEGLQGLAG
LPGARGLKGD KGDPGPKGEC GPDGHNVPGP PGPPGPPGPI INLQDLLLNN TESMFNITEI
RGPPGPMGPR GPKGDSGLPG FQGPPGMKGA KGEAGVTIAA DGTVMTSVRG PRGPKGIKGE
RGFPGAYGVM GPIGPTGQKG EYGFPGRPGR PGMAGKKGDQ GDAIGQPGLP GPPGPPGPPG
PVTGLNGVNG SKGSSQGGRR NGGAKGEKGE VGLPGMPGEP DDILPEGVVG EKGDMGYEGM
KGDQGEPGLP GPPGLPGRSG LVGPKGESVI GTVGHPGAPG EPGVLGIGRP GSRGPPGPAG
PPGPPPVYGS AVSIPGPPGP PGPPGITGYE NPVSTYRNTN SLMRESHRAA EGSMAYVSDK
GELYVRTRDG WRKVQLGELI LVPAESPSSA VSQALSRPGD RTRPHRPHSQ ELVGTSYVPN
YNVLPHTVHS VPALHLVALN APFSGDMRGI RGADFQCYQQ ARAMGLTATY RAFLSSHLQD
LATIVKKGDR YNMPVINLKG EVIYSSWMNI FSGNGGVFDP SIPIYSFEGR NVMTDPTWPQ
KLVWHGSSTV GIRMTTNYCE AWRAGDMAVT GQASLLQTGR LLGQHTRSCS NHFIVLCIEN
SYIDHRRSN
//
