ID A0A6J2RJC2_COTGO Unreviewed; 1296 AA.
AC A0A6J2RJC2;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Collagen, type XV, alpha 1b isoform X4 {ECO:0000313|RefSeq:XP_029309455.1};
GN Name=col15a1b {ECO:0000313|RefSeq:XP_029309455.1};
OS Cottoperca gobio (Frogmouth) (Aphritis gobio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Bovichtidae; Cottoperca.
OX NCBI_TaxID=56716 {ECO:0000313|Proteomes:UP000504630, ECO:0000313|RefSeq:XP_029309455.1};
RN [1] {ECO:0000313|RefSeq:XP_029309455.1}
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_029309455.1; XM_029453595.1.
DR GeneID; 115022564; -.
DR CTD; 558137; -.
DR Proteomes; UP000504630; Chromosome 17.
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; 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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 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 ECO:0000313|RefSeq:XP_029309455.1};
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:UP000504630};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 74..263
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..294
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..470
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..514
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..556
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..609
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..829
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..966
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1008
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1079
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1296 AA; 133079 MW; 20254A697F5E0047 CRC64;
MVKGDRVTEN APEDSTLTEG SVLAPTPSPV SIFDHSTEEQ GTSPPEDNAG GGSKHRVQYK
PLKHWKSERG SGDHLDLTEL IGVPLPPFVS FTPGHESFPA YNFGPDANIG RLTKTFVPGS
FYRDFAIIVT VRPATQRGGV LFAITDALQK VVELGLALTP VRGGLQSILL YYTDREQASH
SHKAASFSVP DMTEQWTRFT LVVEHDEVRL YMDCGEAERT TFHRSAERLN FSHNSGIFVA
NAGGTGLDKF VGSLQQLVIK DDPRAAEEQC EDDDPYASGY TSGDDALDDR ETEEEIMKNT
HERKHGTAQE EDSVPVRAPP TEAPEVELDE YSGHQTSTEA TEEIRGPHMT EEPGERSGDG
HVRHGLKGER GGPGPRGPPG PPGHPGPTPL PGQAQPGPRG TQGTPGASGS PGLAGRDGQQ
GNKGDKGDAG QRGSQGFPGL AGEAGTKGEK GDQAVGVPGP PGLPGPPGPP RSRSVPYGAD
ALGSGFEDLD SDTELIRGHP GLPGPPGPPG PPGPLSDSDE DLSTAGAPGT PGKDGLTGKP
GIPGPAGKDG GPGLPGVVGE KGEQGLSGPL GPKGECGSLG TAGSSGPPGP SGPQGKRGPS
GPPGPPGPPG TKFFVEDMEG SGKSDMLIGA GVRGPQGPPG LPGAQGPKGE DGATGAPALS
VKGEPGDAGP EGLQGPAGLP GARGAKGEKG NLGPKGDQGV DGLCIPGPPG PPGPIINLSD
LLLNVTDGIF NFTEIRGPPG SVGPRGPKGD LGPPGVQGPA GFKGEKGEPG VTIAADGSLL
SSPKGPQGPK GIKGDRGFPG SSGLMGPIGP SGQKGEYGFP GRPGRSGLPG RKGDKADSVG
LPGPRGLPGP PGNPGKIIGL KGTVFPVRPR PHCKMGRQSG TWEESVGAKG DKGDEGIPGE
PGTLAPVFPE GFVGARGDQG YQGQKGEKGD GGLPGPPGLP GRSGLVGPKG ESIVGPQGPV
GSVGQPGAPG FGRPGSRGSP GPAGPPGYAP AYGSDVNVPG PPGPPGPTGS PGYANPVTTY
KTSHALSRET QRAAEGTLAY VSEKGGELYI RARNGWRKIQ LGELIHPGPS SSATSQSLSR
TGELSRPQRI HSQELQESSR GYQPSYNVLP QTFNAVPGLH MVALNTPLKG DMRGIRGADF
QCYQQARSMG LTATYRAFLS SHLQDLATIV RKADRTDMPV VNFRGEVLFS SWMSIFSGNG
GTFNPSTPIY SFDGRNVMTD SAWPEKLVWH GSNTVGIRLT TNYCEAWRTA DIAVTGQAAL
LQTGRLLGQH TRSCSNHYIV LCIENTYVGN KHQKRT
//
