ID A0A6P8T7T6_GYMAC Unreviewed; 1425 AA.
AC A0A6P8T7T6;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Collagen, type XV, alpha 1b isoform X3 {ECO:0000313|RefSeq:XP_034054972.1};
GN Name=col15a1b {ECO:0000313|RefSeq:XP_034054972.1};
OS Gymnodraco acuticeps (Antarctic dragonfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Bathydraconidae; Gymnodraco.
OX NCBI_TaxID=8218 {ECO:0000313|Proteomes:UP000515161, ECO:0000313|RefSeq:XP_034054972.1};
RN [1] {ECO:0000313|RefSeq:XP_034054972.1}
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_034054972.1; XM_034199081.1.
DR GeneID; 117534843; -.
DR CTD; 558137; -.
DR Proteomes; UP000515161; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 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; 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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 3.
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_034054972.1};
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:UP000515161};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1425
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028304904"
FT DOMAIN 139..328
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 329..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..359
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..453
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..477
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..628
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..725
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..832
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..959
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1095
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1127
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1208
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1425 AA; 146040 MW; F864F1ABB9169FF7 CRC64;
MGALRLSFAL FFLSFSPAQA QWWSFIWAKP KTTTISMTSP IPSYITSPSI TSLGSSDIPG
TAEWMLKEDR VTEKAPEIST LTEGSVLPPT PTPGVEIFGQ STAVPGTLPP KENAGAGSKA
RAQCKLLKHW KSERGSGGHL DLTELIGVPL PPSVSFTPGH EGFPAYNLGP DANIGRLTKT
FVPGSFYRDF AIIVTVRPAS QRGGVLFAIT DARQKVVELG LALTPVRGGL QSILLYYTDE
EQASHSHKAA SFSVPDMTEQ WTRFTVVVEQ DEVRLYMDCG EAERTTFHRR PKRLNFSHNS
GVFVANAGGT GLDKFVGSIQ QLVIKDDPRA AEEQCEDDDP YASGFTSGDD ALDDRESEEE
MMKNTHERKQ GTEKEGSVPV RAPPTEAPEV ELEEFSGQQT TTEATEDMLL KGPHMTQEPG
EEPRDGHVRH GIKGERGSPG PRGPPGHPGP TPLPGQAQPG PRGTQGPAGA PGSPGQQGRD
GQAGHKGDKG DAGQRGTQGL SGSDGEAGSK GEKGDQGVGA PGLPGPPGPP RSHSVSYGAD
ALGSGFEDLD SDTELIRGHP GLPGPPGPPG PPGPLPSSSA EGFSSGYAGL PGKDGPQGKP
GLPMYEDWFS GSGSDASGLS SEFSSDLGSG FSSGFSSDPG FASGSGLDFG SAWGSGEGLA
GRNGSPGLSG ALGEKGEQGL AGQPGPKGEC GSLGTNGSSG APGPSGPPGK RGPSGPPGPP
GPPWPTKFFV EDMEGSGKSD MLIGTGVRGT QGPPGIHGPT GPKGEDGATG APGLSVKGEP
GGKGPEGRQG PAGLPGARGA KGEKGNLGSK GDRGVDGLSI PGAPGPPGPP GPTINLPDLL
LNMTDGIFNF TDIRGPPGAV GPEGLPGRAG FPGPRGPKGD VGPAGVQGPL GLKGEKGEPG
VTIAADGSLI SAPRGPQGPK GLKGDRGFSG PAGLMGPIGP NGQKGEYGFP GRPGRSGMPG
RKGDKGDAVG LSGPPGPPGQ PGLPGRVVGL KGTVFPVRPR PHCKMGRQSG TARDSVGAKG
NKGDIGIPGE PGTPAPEFPD GVVGARGDKG YQGQKGDKGE GLPGPPGLPG RSGLVGPKGE
SIVGPHGPVG PVGEPGAPGF GRPGPRGPPG PAGPPGPASG YGSGASVPGP PGPQGPTGSP
GNANAMTVYK TSNALGRETH RVAEGTLAYV SEKGGELFIR ARNGWRKIQL GELIQSGPSS
SVTSQSLSRT AERSRPHRIH SQELQESSRG YQPSYNVLPQ TFNAVPGLHL VALNAPLKGD
MRGIRGADFQ CYQQARSMGL TTTYRAFLSS HLQDLATIVR KADRTDMPVV NLRGEVLFSS
WMSIFSGNGG TFTPSTPIYS FDGRNVMTDS AWPEKQVWHG SNTVGIRLTS NYCEAWRTGD
MAVTGQAALL QTGRLLGQHT RSCSNHYIVL CIENTYVGNT HQKRT
//
