ID A0A6P8UXP3_GYMAC Unreviewed; 1430 AA.
AC A0A6P8UXP3;
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 XVIII alpha 1 chain a isoform X2 {ECO:0000313|RefSeq:XP_034077360.1};
GN Name=col18a1a {ECO:0000313|RefSeq:XP_034077360.1};
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_034077360.1};
RN [1] {ECO:0000313|RefSeq:XP_034077360.1}
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_034077360.1; XM_034221469.1.
DR GeneID; 117549491; -.
DR CTD; 564123; -.
DR Proteomes; UP000515161; Unplaced.
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:0032836; P:glomerular basement membrane development; 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; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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_034077360.1};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1430
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027807453"
FT DOMAIN 120..309
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 35..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..54
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..111
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..407
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..492
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..597
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..649
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..663
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..728
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..860
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..918
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..932
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1042
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1063
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1086
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1430 AA; 146901 MW; C39C6B7716E4CD00 CRC64;
MAKIRTSFGV LFLLTLLVVY SDAWFWDWTG TTTMPPTVDH EGSGSSEGSG EPSSENIAMV
RSEMIDEGQG IQKVVPTWDQ TTEGLRLTTV EPTTEPESGG TSEKGTEGIS SHIRKPEESG
VTLLQLIGDP PPSTITQVFG PDSSPGYVFG PDANSGQLAR TYLPSPFYRD FALIFNLKPT
SERGGTIFSI TDAAQQIMYV GVKLSAVQGG NQYVILYYTE PDSQQSYEAA RFLAPSMKDT
WTRFAIAVRD DKVMFYLNCD TDPQVMRLER SPDEMELEAG AGVFVGQAGG ADPEKFLGVI
GELRIVGDPR AAERHCEEDG DDSDMASGDG SGDEERNSRP AGETLRWTTT PPSSRPIQQP
PLSKKDEMLT ERDTGAKGEK GSQGNSGLKG DRGPIGPKGE TTSSSGSGSR GGSRGEKGEL
GEKGLKGSAG FGYIGKKGEP GPAGPVGPPG PPGAATEVTV GGDGSVASRA PAPRGPAGPP
GTSGPEGPPG TDGEPGDPGE DGKTGLEGPP GFPGTPGDPG LKGDKGDRGD GQPGPRGPPG
LPGPGIRSTF VDMEGSGFPD LESVRGLPGL QGPPGPPGAP GPSTTGTASS SGAFGPPGKD
GAAGQPGLPG IPGTDGSPGA SAPKGENGDA GELGLPGAIG QKGSGGDPGV QGDPGETGLA
GLPGPLGPVG KPGPPGPPGS SYRVGFDDME ASGGGFNNGL PGARGPEGRQ GSSGLPGLPG
KSGLPGIPGQ KGSEGSLGRD GQPGLDGFPG PQGPKGDGGD KGDRGEPGRD GSGLTGPPGP
PGPPGQIIYQ TDGNAGGVAG DVGRTGENGL PGQAGFPGPI GPRGNRGEPG VPGYGVKGEK
GEPGLVIGPD GSLLHLDGLS GQKGDIGPPG SVGLAGPYGP SGIKGEFGMP GRPGRPGVNG
YKGEKGDTSG GSGYGYPGVP GQPGPPGPPG PTSPFDRFNR YDDTSRNYPA TKGDKGEQGD
HGLPGIPGTA PNFDIYAFKN ELKGERGDVG VKGEKGEQSG GYYDQRFGGV QGQPGPPGKP
GLEGPKGDSV MGPPGPQGPP GTPGIGYDGR PGVPGPPGPP GLPTLPETYR PNNPVSIPGP
PGPPGQPGSS ALSSGVTVLR SYETMVATAR RQSEGSLIYI LDKADLYLRV RDGLRQVMLG
DYNPFFRDLA NEVAEVQPPP VIVYPDTQDQ SQNNGAGHYS HGGPVIRPIE PSSQPPVNPR
YPPQYDPRFP DPRQTGHTDG RFVPHQTDNR YSVTPRRPSP PIPQPAVPAE PSASGLHIIA
LNAPQTGNMR GIRGADFLCF QQARAVGLKG TFRAFLSSKL QDLYTIVRRA DRDNFSIVNL
KDQVLFDSWE SMFGDNTNKM RENVPIYSFD GRDTLRDSAW PEKMVWHGSN NKGHRQTDHY
CETWRTGDHA VSGLASSLQS GQLLQQSSSS CSGSYIVLCI ENAFTTHSKK
//
