ID A0AA97IXT6_EUBMA Unreviewed; 1578 AA.
AC A0AA97IXT6;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X2 {ECO:0000313|RefSeq:XP_054827516.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_054827516.1};
OS Eublepharis macularius (Leopard gecko) (Cyrtodactylus macularius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Gekkota; Eublepharidae; Eublepharinae;
OC Eublepharis.
OX NCBI_TaxID=481883 {ECO:0000313|Proteomes:UP001190640, ECO:0000313|RefSeq:XP_054827516.1};
RN [1] {ECO:0000313|RefSeq:XP_054827516.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_054827516.1};
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_054827516.1; XM_054971541.1.
DR GeneID; 129324335; -.
DR CTD; 80781; -.
DR Proteomes; UP001190640; Chromosome 2.
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; 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; IPR050938; Collagen_Structural_Proteins.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR010363; DUF959_COL18_N.
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; PF06121; DUF959; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_054827516.1};
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:UP001190640};
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..1578
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041708288"
FT DOMAIN 220..408
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 87..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..98
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..702
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..746
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..770
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..921
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1010
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1068
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1578 AA; 162174 MW; 3A2AB8EC4ECA5E3F CRC64;
MARAVQNIGL LLLLSCSISN AQGWTSWLWR SSEKTTLPPT KAVDTEDQTT HQLATSEATT
LNIPPESTTR QTGRVWNIFT LKRPDLTTDT TVPTTATASP SELGGREGNI AGVGAEILNV
AEGIRNLVQQ WDKTATKGTE RTEAPPVTAG VLEASPLHAV ELVAIQNVTA NLTDNMQILL
ETQQPQLALS VTTKPNFLLN KTQVLLKKPE TPLPENFSTE VGLLELIGDP PPDQITKIYG
PDNSPGYVFG LDANTGQVAR YHLPSPFYRD FSLLFHIQPT SDKAGVLFAI TDASQSIIYV
GVKLSEVKDG KQKIIFYYTE PGSQNSYAAA TFIVPSLVNQ WTRFAISVEE EEVVLYMDCE
EFERVHFERS PDEMDLEEGS GLFVAQAGGA DPDKYQGVIA ELKVKGDPRA ADVHCEDEED
DSDMMSGDGG SGAEEKPQPS EKERGIPVPL SLPEPPPVTS PPTDKKPVQP EEKPGLQTEL
TKPEERPPFA SGVGAKGEKG DPGEKGERGP KGDSRVGGVL PAGGAKGEKG EKGELGVKGN
AGFGYPGSKG QKGEPGAKGS PGPAGPPGPP GTIVQGPDGS VIEQVTGPPG PTGPPGLPGK
DGVPGKDGEP GDPGEDGKPG DVGPQGFPGT PGESGQKGEK GDPGVGSQGP PGPPGPPGLP
GFSSKLDKLT FIDMEGSGFG GDLESLRGPR GPPGPPGPPG VPGLPGQPGR FGMNGTDLPG
PPGLPGVPGR DGSPGLPGPP GPPGPPGKDG IPGLPGASGA NGEPGELGLP GAPGPKGSKG
DAGLPGTPGE TGLAGLPGPM GPRGQPGPPG PPGPGFAPGI DDMEGSGLPF VSALPGARGP
EGPQGPPGLP GLKGDAGNPG LPGEKGEKGD AGLPGLDGRP GLEGFPGPQG AKGDKGNSGD
KGEQGQDGVG FPGPPGPPGP PGQVVYLTSD DRSLSSVPGP EGKQGHAGFP GPVGPKGDTG
APGFQGSVGP KGEKGEPGVI IGPDGTIIAA QTKGEKGEPG PRGPAGPAGP PGRYGQKGEI
GFPGRPGRPG MNGLKGEKGD PADSSGGLGL MGLPGLPGPP GPPGPPGSVV PVYDNNAFSE
MGPPGPPGLP GYHGAPGQKG EKGEMGAPGL PGQFPYDLSR FGSPVTGEKG DQGDSGAKGE
KGEPGGGGFF GSSVAGSPGP PGYPGLPGPK GDSIRGPPGP PGPQGPPGTG SEGRPGATGP
PGPPGPPGPP SFPGPHRQSV SIPGPPGPPG PPGPPGIGDA SSGLRILPTY QSMMTRAHEM
PEGQLFFIRD REELYIRVRN GIRRVLLEER VSISGPGLDN EVYDRPPRNH YPQSGGIASS
GSQRPFQQHL PLHPHREYSV YSTAKPWRGD ESVANQHRLP EQPVIHQPHQ GAQQEQVNAF
FHNSRQSETL PSAVHMHHDF QPALHLIALN TPLSGSMRGI RGADFQCFQQ AREVGLTGTF
RAFLSSRLQD LYSIVRRADR STVPIVNLRD EVLFTNWEYL FSGSEAPFRT GVPILSFDGR
DVLRDSAWPQ KSVWHGSDSK GRRLTESYCE TWRTDDTVVT GQAASLASGK LLEQKSSSCR
NAFIVLCIEN SFMTSSQK
//
