ID A0A8I6GLR1_RAT Unreviewed; 1785 AA.
AC A0A8I6GLR1;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-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:ENSRNOP00000096747.1,
GN ECO:0000313|RGD:70936};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000096747.1, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000096747.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000096747.1};
RA Doris P.A., Kalbfleisch T., Li K., Howe K., Wood J.;
RT "GRCr8: a new rat reference genome assembly contstructed from accurate long
RT reads and long range scaffolding.";
RL Submitted (JAN-2024) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000096747.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000096747.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000096747.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000096747.1};
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 AlphaFoldDB; A0A8I6GLR1; -.
DR FunCoup; A0A8I6GLR1; 244.
DR GlyGen; A0A8I6GLR1; 2 sites.
DR Ensembl; ENSRNOT00000116507.2; ENSRNOP00000096747.1; ENSRNOG00000001229.8.
DR AGR; RGD:70936; -.
DR RGD; 70936; Col18a1.
DR GeneTree; ENSGT00940000158212; -.
DR OMA; VQDQHQN; -.
DR Reactome; R-RNO-1442490; Collagen degradation.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-8948216; Collagen chain trimerization.
DR Proteomes; UP000002494; Chromosome 20.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0030938; C:collagen type XVIII trimer; TAS:RGD.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001886; P:endothelial cell morphogenesis; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:RGD.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:RGD.
DR GO; GO:0051599; P:response to hydrostatic pressure; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR CDD; cd07455; CRD_Collagen_XVIII; 1.
DR CDD; cd00247; Endostatin-like; 1.
DR CDD; cd00110; LamG; 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; IPR035523; Collagen_XVIII_Fz.
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; IPR001791; Laminin_G.
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; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF13385; Laminin_G_3; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A8I6GLR1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1785
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035234149"
FT DOMAIN 371..488
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 56..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1537..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..69
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..124
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..795
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..830
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..942
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..970
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..986
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1045
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1316
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1457
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1588
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 386..432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 423..461
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1785 AA; 184051 MW; 341BB6415E19381C CRC64;
MAPDPSRRFC LLLLLLLLLL LSCCLVPTSA DGNSLNPLNP LEWLWFAKTT DSLEARVSQP
QISSPVQSPE NPTTHVVPQD GLTEQQTTSA NPKLSPEEDR EAGQGGTPAS PVVPIPLVAP
AASPDTKEEN VAGVGAKILN VAQGIRSFVQ LWDEDSTTEH YPGIEASDSP VPTVLPTLAE
PSSAPQGSET TLLLSSGIPS SPDSQTTEAG TLAVPTQPTP FQSSLQAPLG RPSVPPPSPG
RAFLSSARIR APPWGSQEPL RQPQHLEGKG LLPMATRSSR QHRHSDTHGH IPLLPLVTGP
LVTGPLVTGP LVTASLSVHG LLSVPSSDPS AQLSQVAALP GFPGAWVSHV APSSGSELSN
DSALVGNDSL TSPSRCLPLP PTLAICSHLG IGHFWLPNHL RHADSAEVEA TARAWGHLLH
TNCHPFLSWF FCLLLAPSCG PGPPPALPPC RQFCEALEDA CWNYLAGDRL PVVCASLPSQ
EDGYCVFIGP AAENVAEDVG LLQLLGDPLP QKISQVEDPH VGLAYVFGPY SKSSQMAQYH
FPKLFFRDFS LLFEVRPTTE AAGVLFAITD AAQVVVSLGV KLSEVRDGQQ NISLLYTEPG
ASQTQTGASF RLPAFVGQWT HFALSVDGSS VALYVDCEEF QRVPFARSPH GLELERGAGL
FVGQAGAADP DKFQGMISEL RVRKTPRVSP VHCLDEEDDD DDRASGDFGS GLEESSNLHR
QETYLRPGLP QPPPVTSPPL AGGSATEDSR TEEKEEEATV DSKGADTLPV TDSSGVWDGD
VQNPGGGLIK GGLKGQKGEP GAQGPPGPAG PQGPAGPAVQ SPSSQPVPGA QGPPGPQGPP
GKDGIPGRDG EPGDPGEDGR PGDTGPQGFP GTPGDVGPKG EKGDPGIGPR GPPGPPGPPG
PSFRQDKLTF IDMEGSGGFS GDLESLRGPR GFPGPPGPPG VPGLPGEPGR FGVNSSYAPG
PAGLPGVPGK EGPPGFPGPP GPPGKEGPPG VAGQKGSVGD AGSPGPKGSK GDLGPIGMPG
KSGLPGLPGP VGPPGPPGPP GPPGPGFAAG FDDMEGSGTP LWSTARSSDG LQGLPGLPGI
KGDPGVTGPP GAKGEVGADG VQGIPGLPGR EGVAGPPGPK GEKGTQGEKG NPGKDGVGRP
GLPGPPGPPG PVIYVSNEDR AVVSTPGPEG KPGYAGFPGP AGPKGDLGSK GEQGLPGPKG
EKGEPGSIFS PDGTALGQAQ KGAKGEPGFR GPPGPYGRPG YKGEIGFPGR PGRPGTNGLK
GEKGEPGEAS LGFSMRGLPG PPGPPGPPGP PGVPVYDSNA FVESGRPGLP GQQGVQGPPG
PKGDKGEVGP PGPPGQFPID LFHLEAEMKG DKGDRGDAGR KGERGEPGAP GGGFFSSSVP
GPPGPPGYPG IPGPKGESIR GPPGPPGPQG PPGIGYEGRQ GPPGPPGPPG PPSFPGPHRQ
TVSVPGPPGP PGPPGPPGAM GASAGQVRIW ATYQTMLDKI REVPEGWLIF VAEREELYVR
VRNGFRKVLL EARTALPHGT DNEVAALQPP LVQLHEGSSY TRREHSYPTA RPWRADDILA
NPPRLPDRQP YPGVPHHHHH HHHHHSSHEH RPPAHPSPSP AHTHQDFHPV LHLVALNTPL
SGGMRGIRGA DFQCFQQARA VGLSGTFRAF LSSRLQDLYS IVRRADRSSV PIVNLKDEVL
SPSWDTLFSG SQGQLHSGAR IFSFDGRDVL RHPAWPQKSV WHGSDPSGRR LMESYCETWR
TEATGVTGQA SSLLSGRLLE QKAESCHNSY IVLCIENSFM TSFSK
//
