ID A0A6J2RF00_COTGO Unreviewed; 1307 AA.
AC A0A6J2RF00;
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 X2 {ECO:0000313|RefSeq:XP_029309453.1};
GN Name=col15a1b {ECO:0000313|RefSeq:XP_029309453.1};
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_029309453.1};
RN [1] {ECO:0000313|RefSeq:XP_029309453.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_029309453.1; XM_029453593.1.
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:SF1106; VIKING, ISOFORM A; 1.
DR Pfam; PF01391; Collagen; 5.
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_029309453.1};
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..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1111
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 341..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..389
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..406
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..469
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..513
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..555
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..608
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..840
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..977
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1019
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1090
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1307 AA; 134086 MW; C63383D8CE285CEB 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 DSVPVRAPPT EAPEVELDEY SGHQTSTEAT EEIRGPHMTE EPGERSGDGH
VRHGLKGERG GPGPRGPPGP PGHPGPTPLP GQAQPGPRGT QGTPGASGSP GLAGRDGQQG
NKGDKGDAGQ RGSQGFPGLA GEAGTKGEKG DQAVGVPGPP GLPGPPGPPR SRSVPYGADA
LGSGFEDLDS DTELIRGHPG LPGPPGPPGP PGPLSDSDED LSTAGAPGTP GKDGLTGKPG
IPGPAGKDGG PGLPGVVGEK GEQGLSGPLG PKGECGSLGT AGSSGPPGPS GPQGKRGPSG
PPGPPGPPGT KFFVEDMEGS GKSDMLIGAG VRGPQGPPGL PGAQGPKGED GATGAPALSV
KGEPGDAGPE GLQGPAGLPG ARGAKGEKGN LGPKGDQGVD GLCIPGPPGP PGPIINLSDL
LLNVTDGIFN FTEIRGPPGS VGPEGLPGRA GFPGPRGPKG DLGPPGVQGP AGFKGEKGEP
GVTIAADGSL LSSPKGPQGP KGIKGDRGFP GSSGLMGPIG PSGQKGEYGF PGRPGRSGLP
GRKGDKADSV GLPGPRGLPG PPGNPGKIIG LKGTVFPVRP RPHCKMGRQS GTWEESVGAK
GDKGDEGIPG EPGTLAPVFP EGFVGARGDQ GYQGQKGEKG DGGLPGPPGL PGRSGLVGPK
GESIVGPQGP VGSVGQPGAP GFGRPGSRGS PGPAGPPGYA PAYGSDVNVP GPPGPPGPTG
SPGYANPVTT YKTSHALSRE TQRAAEGTLA YVSEKGGELY IRARNGWRKI QLGELIHPGP
SSSATSQSLS RTGELSRPQR IHSQELQESS RGYQPSYNVL PQTFNAVPGL HMVALNTPLK
GDMRGIRGAD FQCYQQARSM GLTATYRAFL SSHLQDLATI VRKADRTDMP VVNFRGEVLF
SSWMSIFSGN GGTFNPSTPI YSFDGRNVMT DSAWPEKLVW HGSNTVGIRL TTNYCEAWRT
ADIAVTGQAA LLQTGRLLGQ HTRSCSNHYI VLCIENTYVG NKHQKRT
//
