ID A0A8I3PHE2_CANLF Unreviewed; 1717 AA.
AC A0A8I3PHE2;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSCAFP00845032029.1};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00845032029.1, ECO:0000313|Proteomes:UP000805418};
RN [1] {ECO:0000313|Ensembl:ENSCAFP00845032029.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Labrador retriever {ECO:0000313|Ensembl:ENSCAFP00845032029.1};
RA Eory L., Zhang W., Schoenebeck J.;
RT "Long-read based genome assembly of a Labrador retriever dog.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCAFP00845032029.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845032029.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCAFP00845032029.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845032029.1};
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 Ensembl; ENSCAFT00845040900.1; ENSCAFP00845032029.1; ENSCAFG00845022231.1.
DR GeneTree; ENSGT00940000158212; -.
DR OrthoDB; 5983381at2759; -.
DR Reactome; R-CFA-1442490; Collagen degradation.
DR Reactome; R-CFA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-CFA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-CFA-216083; Integrin cell surface interactions.
DR Reactome; R-CFA-8948216; Collagen chain trimerization.
DR Proteomes; UP000805418; Chromosome 31.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
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; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR37456:SF4; COLLAGEN ALPHA-1(XXIII) CHAIN; 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; 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:UP000805418};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1717
FT /note="Collagen alpha-1(XVIII) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035269071"
FT DOMAIN 328..445
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 39..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..237
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..771
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..875
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..903
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..919
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..951
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..981
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1087
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1326
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1394
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 343..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 380..418
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1717 AA; 174015 MW; 1232238CB2628B48 CRC64;
MARHPGRCLL LLLLLTCCPA AAQVDLLSLN WLWSTRTAGP TAEPVSEAPG SPHVQPRDET
GTPVTPQPGP TEQGNAPASP EPPLRGLETD EHAASAAPSA PPAGPDPKEE KEENIAGVGA
KILNVAQGIR SFVQLWDDTT RPESSSTAGT PAPVTPTSPL ALPGPSRPPP ENGTALWLGS
TDAPRVEAST LPAPTRLPPS LDRPRAALRE PSGPPPSPGR ASLSSAPRGA PPGGIQPSPG
PPQDLDGEGL RPGLQHRLPG LRGRSPHLLP LVMGALGADA APSALSSDPP ALLPGTPLSA
VTGGRGAWAA PAADSLGPGP ANNSAPLTPA GRCLPLPPAL PVCGRLGIGR AWLPNHLQHA
SRDEVRAAAR AWGGLLRTRC HRFLARFVCL LLAPPCRSGP PPAPPPCRQF CEALEDACWS
HLPGAGLPVP CASLPAQEDG LCVFIGPGAE SRGSEVGLLQ LLGEPPPQQV TQVDDPDVGP
AFVFGPDANS GQVARYHVPS PFFRDFSLLM HVRPATEGPG VLFAITDAAQ AVVSVGVKLS
GVRDGQQHVQ LLYTEPGAAR TRTAASFRLP AFTGQWTRLA LSVDGATVAL FVDCELFQRV
PLERSPGGLQ LEPGAGLFVA QAGGADPDKF QGMIAELRVR GDPHVSPLHC LEEDDDDSGG
VSGDFGSGLE DDREPSGLLP KAELPEAPPV TSPPLTGGRD VEDSRMEEIE EEATASPLGA
RTLPGSATVT AESAQRLGGS LQEAPTGPAA HNPEAWPGPG PQGPPGPPGP PGKDGTPGRD
GEPGDPGEDG RPGDPGPQGF PGTPGDVGPK GEKGDPGVGP RGPPGPQGPP GPPGPSFRHD
KLTFIDMEGS GFGGDLESLR GPRGFPGPPG PPGVPGLPGE PGRFGMNSSD VPGPAGLPGV
PGRDGPPGLP GAPGPPGPPG KEGGPGKPGP KGSPGDAGAP GPKGSKGDPG PIGVPGESGL
AGPPGPAGPP GPPGPPGPPG PGLAAGFVDM EGSGEPFWST AHGASGPQGP PGLPGVKGDP
GIVGPPGAKG EVGADGPPGF PGLPGREGTA GAQGPKGEKG TQGEKGEPGR DGVGQPGLPG
PPGPPGPVVY VSEQERAATG VPGPEGRPGH AGFPGPAGPK GDLGSKGQRG PPGPKGEKGE
PGPAFSPDGS MLAPAQKGAK GEPGFRGPPG PYGRPGHKGE IGFPGRPGRP GMNGLKGEKG
EPGQASAGFG MTGPPGPPGP PGPPGPPGTP VYDSNAFMEP GHPGPPGLPG HQGPSGPKGD
KGDVGPPGPP GQFPFDLLQL GAEMKGEKGD RGDAGQKGER GEPGGGGFFG SSVPGPPGPP
GYPGIPGPKG ESVQGHPGPP GPQGPPGIGH EGRRGPPGPP GPPGPPGPPS FPGPYRQTIS
VPGPPGPPGP PGPPGTMGTS SGVRIWATYQ TMLDKVPDVP EGWLMFVAER EELYVRVRNG
FRKVLLEARV PLPRGTDNEV AALQPPVVQL HEGNPYPRRE PTHATARPWR ADDILASPPR
LLDPQPYPGA PHHGSYVHFQ PARPTGGPVH THTHTHQDFQ PVLHLVALNS PQPGGMRGIR
GADFQCFQQA RAAGLAGTFR AFLSSRLQDL YSIVRRADRT GVPVVNLRDE VLFPSWEALF
SGSEGQLKPG ARIFSFDGRD VLQHPAWPRK SVWHGSDPSG RRLTDSYCET WRTEAPAATG
QASSLLAGRL LEQEAASCRH AFVVLCIENS VMTSFSK
//
