ID A0A4W2F292_BOBOX Unreviewed; 1761 AA.
AC A0A4W2F292;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSBIXP00000043506.1};
OS Bos indicus x Bos taurus (Hybrid cattle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=30522 {ECO:0000313|Ensembl:ENSBIXP00000043506.1, ECO:0000313|Proteomes:UP000314981};
RN [1] {ECO:0000313|Ensembl:ENSBIXP00000043506.1, ECO:0000313|Proteomes:UP000314981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Low W.Y., Tearle R., Bickhart D.M., Rosen B.D., Koren S., Rhie A.,
RA Hiendleder S., Phillippy A.M., Smith T.P.L., Williams J.L.;
RT "Haplotype-resolved cattle genomes.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBIXP00000043506.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSBIXP00000043506.1}
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 STRING; 30522.A0A4W2F292; -.
DR Ensembl; ENSBIXT00000052279.1; ENSBIXP00000043506.1; ENSBIXG00000005802.1.
DR OMA; WWKVSAS; -.
DR Proteomes; UP000314981; Chromosome 1.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; 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; 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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 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 SMART; SM00063; FRI; 1.
DR SMART; SM00282; LamG; 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:UP000314981};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1761
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021459539"
FT DOMAIN 346..463
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 44..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..185
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..681
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..819
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..884
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..923
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..951
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1012
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1029
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1100
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1162
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1182
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1277
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1361
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1420
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 361..407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 398..436
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1761 AA; 179801 MW; C96CC23646548A95 CRC64;
MAPDPSSGRG HHGLLLLACC LSAAQADLFS WIWSGNSAWP IAAPASKPPD SSPVWPTEDT
TTHVAPRDAP TDWWKVSASP TAPLGRPEVG QGQTPTGPTA STVSLDPKEE NIAGVGAKIL
NVAQGIRSFV QLWDNAKDTT PAESSAGAET PPPTDTMDDL STPGPSITPQ DSGTTLQLST
TALSSPDTQR TEAGTLPMPT QPPPSPGRPW FRESLVSPTP GRSSLSSVPA PAPPRGSQLP
LGRPLQLDGE GLLLAAARPG QQHADDRRPM PPLPPLVTGS LGKHTALWAL SSDPPAKLSH
VAVSALTVDS GAWAPHVANS AGPGLANKST LLGAAELAAT EQPVPTTAGR CLPLLPSLAL
CGHLGIRRSW WPNHLHHTSR EEVQAAVPAW GALLRTHCHR FLAWFFCLLL APPCGPGLPP
GLPPCRQFCE ALEDACWSHL DGRGLPLPCA SLPAREDGHC VFIGPPADEE VVEVGLQQLL
GEPPPWQVAM VHDPDVGSAY EFGEDGSGGG QAARRLLPGT FFQDFSLLVR VRPASARAGV
LFAVTDPAQA VVSVGVKLTA ARGGRQHMQL LYTEPGATHT RTAASFELPA LDGRWTRLAL
SVDGAYARLF VDCKEVQGQP LAHSLHDLQL EPDARLFVAQ AGGADPEKFQ GLISELRLRR
DPQVSPRQCQ DEDEDDDDDG ASGDLGSGLV ETQEHLREEL GAPLGPRLPE APPVTSPPLA
GVGNEEDLRT EEVEESTTAS SLGAQTLPSL GTVGTWDESV WSPGSSVKER GLKGQKGEPG
AQGPPGPIGP QGPAGPAIDS HEAQPVSGPQ GPPGPPGPPG KDGTPGRDGE PGDPGEDGKP
GDTGPQGFPG TPGDVGPKGE KGDPGVGPRG PPGPQGPPGP PGPSFKPDRL TFIDMEGSGF
GGDLESLRGP RGFPGPPGPP GVPGLPGEPG RFGMNSSDVP GPAGLPGVPG RDGPPGRPGP
PGPPGTPGKD GQPGLTGQKG SLGEAGAPGP KGSKGDPGPV GAPGEHGLAG APGPAGPPGP
PGPPGPPGPG FAAGFDDMEG SGSPLWSTAR GAEGLQGPPG TPGVKGDPGA VGPPGSKGEV
GADGAPGLPG LPGREGAAGP QGPKGEKGTQ GEKGDPGKDG VGQPGLPGPP GPPGPVVYVS
EQDRVLASVP GPEGRAGFAG FPGPAGPKGD LGAKGQQGIP GPKGEKGEPG TFFGPDGRAL
TPAQKGAKGE PGFRGPPGPY GRPGHKGEIG FPGRPGRPGM NGLKGEKGEP GDASVGFGMR
GPAGPPGPPG PPGPPGTPVY DSNAFVDSGR PGPPGLPGHQ GPSGLKGDKG DVGPPGPPGQ
FPFDLLQLGA EMKGEKGDRG AAGQKGERGE PGGGGFFGSG VPGPPGPPGY PGIPGPKGDS
IRGQPGPPGP QGPPGIGYEG PQGPPGPPGP PGPPGPPSFP GPYRQTISVP GPPGPPGPPG
PPGSMGTSSG VRVWATYQML VDQVPQVPEG WLIYVADREE LYVRVRNGFR KVLLEAHVPL
PHGTDNEVAV LQPPLVQLHE GNPYPRREVP HPTARSWRAD DILASPPRRP HPQPYPGAPH
HGAYAHLRPV PPTASPSHTH HDFQPVLHLV ALNSPQSGGL RGIRGADFQC FQQARAAGLA
GTFRAFLSSR LQDLYSIVRR ADRATLPVVN LRDEVLFPSW EALFSGSEGQ LKPGARIFSF
DGRDVLQHPT WPQKSVWHGS DPSGRRLTES YCETWRTDSR AATGQASSLL AGRLLEQKAA
GCHNAFIVLC IENSFMTSSS K
//
