ID A0A6P8TC76_GYMAC Unreviewed; 1426 AA.
AC A0A6P8TC76;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen, type XV, alpha 1b isoform X1 {ECO:0000313|RefSeq:XP_034054970.1};
GN Name=col15a1b {ECO:0000313|RefSeq:XP_034054970.1};
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_034054970.1};
RN [1] {ECO:0000313|RefSeq:XP_034054970.1}
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_034054970.1; XM_034199079.1.
DR GeneID; 117534843; -.
DR KEGG; gacu:117534843; -.
DR CTD; 558137; -.
DR InParanoid; A0A6P8TC76; -.
DR OrthoDB; 10060752at2759; -.
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_034054970.1};
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..1426
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027970475"
FT DOMAIN 139..328
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 329..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1233
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..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..478
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..629
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..726
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..833
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..960
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1096
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1128
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1209
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1426 AA; 146169 MW; DE0A0C5BA2CD62F4 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 GTEKEEGSVP VRAPPTEAPE VELEEFSGQQ TTTEATEDML LKGPHMTQEP
GEEPRDGHVR HGIKGERGSP GPRGPPGHPG PTPLPGQAQP GPRGTQGPAG APGSPGQQGR
DGQAGHKGDK GDAGQRGTQG LSGSDGEAGS KGEKGDQGVG APGLPGPPGP PRSHSVSYGA
DALGSGFEDL DSDTELIRGH PGLPGPPGPP GPPGPLPSSS AEGFSSGYAG LPGKDGPQGK
PGLPMYEDWF SGSGSDASGL SSEFSSDLGS GFSSGFSSDP GFASGSGLDF GSAWGSGEGL
AGRNGSPGLS GALGEKGEQG LAGQPGPKGE CGSLGTNGSS GAPGPSGPPG KRGPSGPPGP
PGPPWPTKFF VEDMEGSGKS DMLIGTGVRG TQGPPGIHGP TGPKGEDGAT GAPGLSVKGE
PGGKGPEGRQ GPAGLPGARG AKGEKGNLGS KGDRGVDGLS IPGAPGPPGP PGPTINLPDL
LLNMTDGIFN FTDIRGPPGA VGPEGLPGRA GFPGPRGPKG DVGPAGVQGP LGLKGEKGEP
GVTIAADGSL ISAPRGPQGP KGLKGDRGFS GPAGLMGPIG PNGQKGEYGF PGRPGRSGMP
GRKGDKGDAV GLSGPPGPPG QPGLPGRVVG LKGTVFPVRP RPHCKMGRQS GTARDSVGAK
GNKGDIGIPG EPGTPAPEFP DGVVGARGDK GYQGQKGDKG EGLPGPPGLP GRSGLVGPKG
ESIVGPHGPV GPVGEPGAPG FGRPGPRGPP GPAGPPGPAS GYGSGASVPG PPGPQGPTGS
PGNANAMTVY KTSNALGRET HRVAEGTLAY VSEKGGELFI RARNGWRKIQ LGELIQSGPS
SSVTSQSLSR TAERSRPHRI HSQELQESSR GYQPSYNVLP QTFNAVPGLH LVALNAPLKG
DMRGIRGADF QCYQQARSMG LTTTYRAFLS SHLQDLATIV RKADRTDMPV VNLRGEVLFS
SWMSIFSGNG GTFTPSTPIY SFDGRNVMTD SAWPEKQVWH GSNTVGIRLT SNYCEAWRTG
DMAVTGQAAL LQTGRLLGQH TRSCSNHYIV LCIENTYVGN THQKRT
//
