ID A0A8I3S2Z1_CANLF Unreviewed; 1354 AA.
AC A0A8I3S2Z1;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSCAFP00845030728.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSCAFP00845030728.1};
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:ENSCAFP00845030728.1, ECO:0000313|Proteomes:UP000805418};
RN [1] {ECO:0000313|Ensembl:ENSCAFP00845030728.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Labrador retriever {ECO:0000313|Ensembl:ENSCAFP00845030728.1};
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:ENSCAFP00845030728.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845030728.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCAFP00845030728.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845030728.1};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR Ensembl; ENSCAFT00845039233.1; ENSCAFP00845030728.1; ENSCAFG00845022231.1.
DR GeneTree; ENSGT00940000158212; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000805418; Chromosome 31.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 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; 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; 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; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
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}.
FT DOMAIN 63..251
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..511
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..527
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..559
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..589
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..740
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..866
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..963
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1009
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1031
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1354 AA; 136870 MW; FF88FDB1530D750F CRC64;
MARSCGEARG GGGLGRAGGA RGGLTRGRWP GARRWRPLDV LAPLVLLLGA RAASADPESR
GSEVGLLQLL GEPPPQQVTQ VDDPDVGPAF VFGPDANSGQ VARYHVPSPF FRDFSLLMHV
RPATEGPGVL FAITDAAQAV VSVGVKLSGV RDGQQHVQLL YTEPGAARTR TAASFRLPAF
TGQWTRLALS VDGATVALFV DCELFQRVPL ERSPGGLQLE PGAGLFVAQA GGADPDKFQG
MIAELRVRGD PHVSPLHCLE EDDDDSGGVS GDFGSGLEDD REPSGLLPKA ELPEAPPVTS
PPLTGGRDVE DSRMEEIEEE ATASPLGART LPGSATVTAE SAQRLGGSLQ EAPTGPAAHN
PEAWPGPGPQ GPPGPPGPPG KDGTPGRDGE PGDPGEDGRP GDPGPQGFPG TPGDVGPKGE
KGDPGVGPRG PPGPQGPPGP PGPSFRHDKL TFIDMEGSGF GGDLESLRGP RGFPGPPGPP
GVPGLPGEPG RFGMNSSDVP GPAGLPGVPG RDGPPGLPGA PGPPGPPGKE GGPGKPGPKG
SPGDAGAPGP KGSKGDPGPI GVPGESGLAG PPGPAGPPGP PGPPGPPGPG LAAGFVDMEG
SGEPFWSTAH GASGPQGPPG LPGVKGDPGI VGPPGAKGEV GADGPPGFPG LPGREGTAGA
QGPKGEKGTQ GEKGEPGRDG VGQPGLPGPP GPPGPVVYVS EQERAATGVP GPEVGAAARG
HPARAPHPAP RTPRPDPPLS PQGRPGHAGF PGPAGPKGDL GSKGQRGPPG PKGEKGEPGP
AFSPDGSMLA PAQKGAKGEP GFRGPPGPYG RPGHKGEIGF PGRPGRPGMN GLKGEKGEPG
QASAGFGMTG PPGPPGPPGP PGPPGTPVYD SNAFMEPGHP GPPGLPGHQG PSGPKGDKGD
VGPPGPPGQF PFDLLQLGAE MKGEKGDRGD AGQKGERGEP GGGGFFGSSV PGPPGPPGYP
GIPGPKGESV QGHPGPPGPQ GPPGIGHEGR RGPPGPPGPP GPPGPPSFPG PYRQTISVPG
PPGPPGPPGP PGTMGTSSGV RIWATYQTML DKVPDVPEGW LMFVAEREEL YVRVRNGFRK
VLLEARVPLP RGTDNEVAAL QPPVVQLHEG NPYPRREPTH ATARPWRADD ILASPPRLLD
PQPYPGAPHH GSYVHFQPAR PTGGPVHTHT HTHQDFQPVL HLVALNSPQP GGMRGIRGAD
FQCFQQARAA GLAGTFRAFL SSRLQDLYSI VRRADRTGVP VVNLRDEVLF PSWEALFSGS
EGQLKPGARI FSFDGRDVLQ HPAWPRKSVW HGSDPSGRRL TDSYCETWRT EAPAATGQAS
SLLAGRLLEQ EAASCRHAFV VLCIENSVMT SFSK
//
