ID A0A8C2VH25_CHILA Unreviewed; 1551 AA.
AC A0A8C2VH25;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSCLAP00000013866.1};
OS Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC Chinchillidae; Chinchilla.
OX NCBI_TaxID=34839 {ECO:0000313|Ensembl:ENSCLAP00000013866.1, ECO:0000313|Proteomes:UP000694398};
RN [1] {ECO:0000313|Ensembl:ENSCLAP00000013866.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCLAP00000013866.1}
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; ENSCLAT00000014022.1; ENSCLAP00000013866.1; ENSCLAG00000009590.1.
DR GeneTree; ENSGT00940000158212; -.
DR OMA; VQDQHQN; -.
DR Proteomes; UP000694398; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
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; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
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:UP000694398};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1551
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034234341"
FT DOMAIN 310..427
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 39..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..837
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 325..371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 362..400
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1551 AA; 160148 MW; 8F5E0063FD9433D1 CRC64;
MAPDPSGCLR LLLLACCLAP AWATLLPLDW LWSPKISDST AAPVSRPQGH PSPQPTEAAS
THVASQRGPT EPRTALASTR PASEEQATTW SETPAARVTR TPLAPPAESW DAKEENIAGV
GAKILNVAQG IRNFVQLWDD AAVETPTTST PMDVHPLARP SSDPQDSGAT LRPSHGAPTV
LGTQTAEASA LAVPTQPPPS LGRSLAPLRG SSVSPLSPGR ASLSSAPSRA PPWGQPQDLG
SAAGPRRRHG RPDFRWAPSL VMGAPSALSS GPSAWLSLVA LEPFPGDGGA WVSLVASSNR
SALLGLGPPT PDGRCLPLTP ALPACSRLGI GHSWLPNHLR HRSSEEVQAA AQAWGSLLRA
HCHPFLAWFF CLLLAPPCGP GPPAPLPPCR QFCEAVEDAC WSRLDGARLP VACDTLRAQE
DGLCVLIGPA AESTSQEVGL LQLLGEPLPQ QVTAVSDPEV GPAYVFGPDA NSGQVARHHV
PSPFFRDFSL LLHVRPDTES AGVLLAITDG AQAAVALGVK LSEVQDQHQN ISLLYTEPGT
SQTRTAASFR LPAFVGQWTR FALSVDGGSV ALYVDCEEFQ RLPFARSPRG LELEPGAGLF
VGQAGGADPD KFQGAIAELW VRGDPRVSPV HCVDEEDEDE DGASGDLGSG LEEPRELHRE
DTPGLRPPPP VTSPPLATGG SLEDTRTEEI EAQTTATSLG HEALPGVCEL SVWGIGDVDG
EPVSIPGLGA LSCPADLGFP WVTMMGFSLP QGDPGVGPRG PPGPQGPPGP PGPSFRHDKL
TFIDMEGSGF SGDLETLRGS KGDPGPVGDP GEIGFTGAPG PAGPPGPPGP PGPPGPGPAA
GFQHGPWGVV GWASPAGLLG AAQQVRSPLR SGGEPLWETS EGARGFPGLP GGEGAAGPMV
SDHSWHRSSL ALAGPVSMEP GRKSECLSEV QGYLSPTAPG APPQGDPGKD GVGQPGLPGP
PGPPGPVVYV SDQDVRTCGH GSWSLTSAWS PPQGPAGPKG DEGSKGAQGS PGPKGEKGEP
GDVSLGFGMR VSPAEVGRAL GTGPWPVLRT RPAGLTGSPP DQSSLSPQGM PGPPGPPGPP
GPPGTPIYDS NAFVESGRPG TPGAQGLPGP SGPKGEKGDV GQPGPPGDVP PPHEPVLPQG
EKGERGDAGP KGERGAPGAS GGFFGSSVPG PPGPPGYPGI PGRQGPPGPP GPPGPPSFPG
PHRQSKCGQG AGWLGTALLP GSVSIPGPPG PPGPPGPPGT MGTSSGVRAW ATYETMLEKV
REVPQGWLIF VAEDEELYVR VRDGVRKVLV SSRPTDNEVA ALQPPLVQLH GGGPYPRREH
SSTARPWRAD DILASPPRLP NPQPYPGVPH HHGAYVHLQP TNPTGSAAHP HHDFQPVLHL
VALNSPLPGG MRGIRGADFQ CFQQARAVGL SGTFRAFLSS RLQDLYSIVR RADRGAVPIV
NLKDEMLSPS WEALFSGSRG QLKPGARIFS FDGRDVLRHS AWPQKTVWHG SDPSGRRLTE
SYCETWRTDA AAATGQASSL LAGRLLEQNA ASCHNAYIVL CIENSFMTPS K
//
