ID A0A8C2TR22_COTJA Unreviewed; 1369 AA.
AC A0A8C2TR22;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSCJPP00005015418.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSCJPP00005015418.1};
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934 {ECO:0000313|Ensembl:ENSCJPP00005015418.1, ECO:0000313|Proteomes:UP000694412};
RN [1] {ECO:0000313|Ensembl:ENSCJPP00005015418.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG International Coturnix japonica Genome Analysis Consortium;
RA Warren W., Burt D.W., Antin P.B., Lanford R., Gros J., Wilson R.K.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJPP00005015418.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCJPP00005015418.1}
RP IDENTIFICATION.
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; ENSCJPT00005021867.1; ENSCJPP00005015418.1; ENSCJPG00005012784.1.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000694412; Chromosome 7.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
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; 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:SF1060; COLLAGEN ALPHA-1(IV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
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:UP000694412};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1369
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034715740"
FT DOMAIN 35..223
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 84..222
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 223..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..239
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..612
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..719
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..864
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..960
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..977
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1001
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1047
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1369 AA; 140194 MW; 7AE523CECC6C2975 CRC64;
MSPGCAPRRL LLLIGLFVLL LLPAASQEPE NLSTEVSLLE LIGDPPPEEI LKIYGPENNP
GYVFGPNANT GQVARYHLPS PFYRDFSLLF HIQPTTPRAG VLFAITDSSQ SIIYVGVKLS
DLQMGKQQII FYYTEPGSQS SYAAATFTVP TLLNQWTRFA ISVEEDEVVL YLDCEEHERV
RFERSPDEME LEEGSGLFVA QAGGADPDKY QGVIADLRLR GDPRAAEHQC EEEEDDTEAS
GDFGSGAEDR HGHLGKDKGI PGLLDAVPVT SPPVVEGSGT RSSVGSPQQA ERTRVEERLQ
VSTGGTGPKG EKGEKGERGL KGDSGTSGIL GTGNAKGEKG EKGELGIKGS AGFGYPGSKG
QKGEPGEPGP PGPPSQHTDG MSLEQVTGPP GPTGPPGKDG APGRDGEPGD PGEDGKPGEM
GPPGFPGTPG ESGQKGEKGD PGVGPRGPPG PPGPPGPPGP SSRQDGLTFI DMEGSGFGGD
LETLRGPRGP PGPPGPPGVP GLPGEPGRFG MNSTDLPGPP GLPGRDGTPG PPGPEGPLGP
PGKDGMPGPP GPKGERGDVG DLGLPGAPGP KGSKGEAGPV GPPGEPGLAG LPGPVGPRGQ
PGPPGPPGPP GPGYEAGFSD MEGSGLPLAT GSPGPRGPSG PQGMPGLPGI KGEVGSLGHP
GPPGPKGDAG VPGVDGRPGL EGFPGPQGPK GSRGSPGEKG ERGQDGLGLP GPPGPPGPPG
QVIYISSEDR PLAAVPGPEG RAGHAGFPGP VGPKGDPGSP GIQGAPGMKG EKGEPGVIIS
PDGTIVAANV KGQKGEPGLP GPMGPSGPHG RAGMKGEIGF PGRPGRPGMN GLKGEKGDPV
DISSVLNLRG PPGPPGPPGP PGPPGSVVYD SNNGFSDASR PAFPGFHQFP GQKGEKGDVG
APGPPGQFPY DLSRFSASLR GDKGEAGPKG EKGEPGGSAL YGPSVTGPPG PQGYPGPPGP
KGDSIVGPPG PPGPQGPPGI GYEGRQGPPG PPGPPGPPSF PGPHRQGEYL PCVSAPRHRT
SLTISLSFHP AISIPGPPGP PGPPGPPGTS RTSLGLRAMP TYQAMLSAAH ELPEGGLIFL
ADRQELYVRV RGGFRRVLLE EHNLVPGSAL DNEVYDKLPS IHYGGAQQPV HPLRNHNPPP
TARPWRGDEV VANQHRLPQP PLLQQHELLN SYYIHRWPDP TPVAAHVHRD FQPALHLVAL
NTPLSGGMRG IRGADFQCFQ QARQVGLAGT FRAFLSSRLQ DLYSIVRRAD RTTVPIVNLQ
DEMLFSNWEA LFTGSEAPLR AGARILSFDG RDILQDSAWP QKSIWHGSDA KGRRLPESYC
EAWRTEERGT SGQASSLSSG KLLEQSASSC QHAFVVLCIE NSFMTAAKK
//
