ID A0A803T999_ANOCA Unreviewed; 1885 AA.
AC A0A803T999;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=col18a1 {ECO:0000313|Ensembl:ENSACAP00000031789.1};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000031789.1, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000031789.1, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000031789.1,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000031789.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSACAP00000031789.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: May regulate extracellular matrix-dependent motility and
CC morphogenesis of endothelial and non-endothelial cells; the function
CC requires homotrimerization and implicates MAPK signaling.
CC {ECO:0000256|ARBA:ARBA00053766}.
CC -!- FUNCTION: Probably plays a major role in determining the retinal
CC structure as well as in the closure of the neural tube.
CC {ECO:0000256|ARBA:ARBA00054383}.
CC -!- SUBUNIT: Forms homotrimers. Recombinant non-collagenous domain 1 has
CC stronger affinity to NID1, HSPG2 and laminin-1:NID1 complex and lower
CC affinity to FBLN1 and FBLN2 than endostatin.
CC {ECO:0000256|ARBA:ARBA00065165}.
CC -!- SUBUNIT: Monomeric. Interacts with KDR/VEGFR2. Interacts with the
CC ITGA5:ITGB1 complex. Interacts with NID1, HSPG2, laminin-1:NID1
CC complex, FBLN1 and FBLN2. {ECO:0000256|ARBA:ARBA00064471}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR Ensembl; ENSACAT00000041236.1; ENSACAP00000031789.1; ENSACAG00000010273.3.
DR GeneTree; ENSGT00940000158212; -.
DR InParanoid; A0A803T999; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000001646; Chromosome 1.
DR Bgee; ENSACAG00000010273; Expressed in forelimb bud and 12 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 1.10.2000.10:FF:000017; Alpha 1 type XVIII collagen; 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; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR010363; DUF959_COL18_N.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
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; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 3: Inferred from homology;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1885
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032439260"
FT DOMAIN 407..525
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 31..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..163
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..738
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..840
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1014
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1030
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1046
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1057
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1230
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1465
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1495
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1555
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 422..468
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 459..497
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1885 AA; 195604 MW; 09141E382C5BF359 CRC64;
MARAELSIGL LLLLTCGFSN AQGWRSWFWG PEQTTIPPSE APSPKEQTEE TEWTTQHLAK
PEPTTTSSIP LESSTQQKGT VWTISTLKRP NFTATTSIPA VTSPSQLDSK EGDIAGVGAE
ILNVAEGIRN LVQLWDEKTT ETTKTTKAPA TTEAPATTET PTTVDLLKSS PTPGTEPGST
LNTTANSTGD AQPLLETGQP KEVTLVTTKP TLLWNKTRVL LKKPAFPLPG SSSFSFSPDD
YVSGTMVAFQ ESTRAGQEST TSSETRATWG ASSDKQGVLP GANVSELQEP RANHSSRVDG
GITSKVVGAL DNWLLHSIAN PNQSLSKGNR AHLHLKNHPF FNYSGIVVAD ATKNHSRDSV
SHSNATNVMD FSSGNTSDSL EFLLTYTVQH FSNSSTGLPS FFPGLTPTAG HCLPLPTKLS
YCNNLGMKHF RVPNYLHLGS EEEIQAALHE WEGLLKSRCH RYLEWFFCLL LVPGCNASLP
ITPPPCRGFC EALKDLCWIH LKEGQLPISC NSLPEEDGVY SCVFVNVSAE NLSTEVGLIE
LIGDPPPEQI TKVYGPDNSP GYVFGQDANT GQVARYHLPS PFYRDFSLLF HVQPTTEKPG
VLFAITDSSQ SIIYVGVKLS EVKDGKQQII FYYTEPGSQN SYAAATFLVP SMVNRWTRFA
ISVEDEEVVL YVDCEEFERV HFERSPDEME LEDGSGLFVA QAGGADHDKY QGVIAELKVK
GDARAAELQC EEDEDDSDMM SGDGGSGIEE KPRLPEKARV TPVVSGLPVP PPVTSPPIAK
TPTEQEEKPH LHTDIAEPKE KSPSAAGVGA KGEKGDSGEK GERGPKGDSG LGGVVSTGGA
KGEKGEKGDL GVKGNAGFGY PGSKGQKGEP GAEGSPGPTG PPGPPGTIVK HSDGSVIEQV
AGQPGPTGPP GSPGKDGLPG KDGEPGDPGE DGKPGDVGPQ GFPGTPGEPG QKGEKGDPGV
GARGPPGPPG PPGFSSKLDK LTFIDMEGSG FGSDLENLRG PRGPPGPPGP PGVPGLPGQP
GRFGTNGTDL PGPPGLPGVT GRDGSPGLPG PPGPPGLPGR DGISGQPGLN GARGEPGEIG
LPGAPGPKGD VGLPGEPGQI GLAGLPGPMG PRGQPGPPGP PGPGFVAGFD DMEGSGLPFV
SAVPGARGPE GPQGPPGLPG PMGDPGTIGL PGIPGPKGPS GLPGLDGHPG SAGFPGPQGE
KGDKGDPGTK GEPGQDGIGL PGPPGLPGPP GQIIHLSGDN TNVPLLPGPE GKQGHAGFPG
PVGPKGDIGS PGFPGSPGLK GDKGEPGVII GPDGTVIATN SKGEKGEGGP RGPVGPLGPP
GRPGQKGEIG FPGRPGRPGM NGLKGEKGDP ADPSGGLGVR GPPGIPGPPG PPGPPGTVVP
VYDNNAFGDV GPPGPPGLPG YHGAPGQKGD KGDVGPPGPP GQFPYDFSTF DSPFWGERAE
KGESGEKGEK GEPGGGGLFG PGAAGLPGHP GYPGPPGPKG DSVRGPPGPP GPQGPPGAGF
EGRPGPPGPP GSPGPPGPPS FPGPHRQAIS IPGPPGPPGP PGPPGSNDAS SPSGPQILPT
YQSMMSRSHE VPEGQLIFIR DREELYIRVR NGFRKILLEE RISLSGPGLD NEVYDRPSSV
HHSHGDTASS GSQRTFQQHL PVHSQYSTYS TAKPWRGDEG AINQHRLPEQ PAIQQPHHGA
HHQQEPLNAF FHQPEPAPSA VHTHHDFQPA LHLIALNTPL SGSMRGIRGA DFQCFQQARE
VGLTGTFRAF LSSRLQDLYS IVRRADRSTV PIVNLRDEVL FNNWENLFSG SEASFRTGVR
ILSFDGRDVL RNPAWPQKYV WHGSDSKGRR LTENYCETWR TDDTVVTGQA SSLASGKLLE
QKSSNCKNAY IVLCIENSFM TSSKK
//
