ID A0A8V0YMR9_CHICK Unreviewed; 1317 AA.
AC A0A8V0YMR9;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE SubName: Full=Collagen, type XVIII, alpha 1 {ECO:0000313|Ensembl:ENSGALP00010020013.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSGALP00010020013.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010020013.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010020013.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Broiler {ECO:0000313|Ensembl:ENSGALP00010020013.1};
RA Warren W., Formenti G., Fedrigo O., Haase B., Mountcastle J., Balacco J.,
RA Tracey A., Schneider V., Okimoto R., Cheng H., Hawken R., Howe K.,
RA Jarvis E.D.;
RT "Gallus gallus (Chicken) genome, bGalGal1, GRCg7b, maternal haplotype
RT autosomes + Z & W.";
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGALP00010020013.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010020013.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGALP00010020013.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010020013.1};
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; ENSGALT00010034050.1; ENSGALP00010020013.1; ENSGALG00010014162.1.
DR GeneTree; ENSGT00940000158212; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000000539; Chromosome 7.
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; 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; 5.
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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A8V0YMR9};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1317
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036486717"
FT DOMAIN 34..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 83..221
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 222..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..512
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..564
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..836
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..932
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..949
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..973
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..995
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1317 AA; 134544 MW; 649584DA83CA6223 CRC64;
MRPGCAPRRL LLLGLFVLLL LPAASQEPEN LSTEVSLLEL IGDPPPEEIL KIYGPDNNPG
YVFGPSANTG QVARYHLPSP FYRDFSLLFH IQPTTPRAGM LFAITDSTQS IIYVGVKLSD
LQMGKQQIIF YYTEPGSQSS YAAATFTVPT LLNQWTRFAI SVEEDEVILY LDCEEHERVR
FERSPDEMEL EEGSGLFVAQ AGGADPDKYQ GVIADLRLRG DPRAAEHQCE EEEDDAEASG
DFGSGAEDRH HPSGKDKGIP GLLDAVPVTS PPVVEGSGTR SSAGSPQQAE RTRVEERLQV
STGGTGPKGE KGEKGERGPK GDSGTSGILG TGATKGEKGS AGFGYPGSKG QKGEPGEPGP
PGPLSRHTDS MSLEQVTGPP GPTGPPGKDG APGRDGEPGD PGEDGKPGEM GPQGFPGTPG
ESGQKGEKGD PGVGPRGPPG PPGPPGPPGR SSKQDGLGPR GPPGPPGPPG VPGLPGEPGR
FGMNSTDLPG PPGLPGRDGT PGAPGPEGPL GPPGKDGMPG PPGPKGERGD VGDLGLPGAP
GPKGSKGEAG PAGPPGETGL AGLPGPVGPR GPPGPPGPPG PPGPGYEAGF GDMEGSGLPL
ATGSPGPRGP SGPQGVPGLP GIKGEVGSLG QPGPPGPKGD AGVPGVDGRP GLEGFPGPQG
PKGNRGSPGE KGERGQDGVG LPGPPGPPGP PGQVIYMSSE DRPLVALPGP EGRSGHAGFP
GPVGPKGDPG SPGIQGAPGI KGEKGEPGVI ISPDGTIVAA NVKGQKGEPG LPGPMGPSGP
HGRAGMKGEI GFPGRPGRPG MNGLKGEKGD PVDISSVLSL RGPPGPPGPP GPPGPPGSVV
YDSNNGFSDA SRPAFPGFHQ FPGQKGEKGD VGAPGPPGQF PYDLSRFSAS LRGDKGEAGP
KGEKGEPGSS TLYGPSVTGP PGPQGYPGPP GPKGDSIVGP PGPPGPQGPP GIGYEGRQGP
PGPPGPPGPP SFPGPHRQAI SIPGPPGPPG PPGPPGTSGT SLGLRTMPTY QAMLSAAHEL
PEGGLIFLAD RQELYIRLRG GFRRVLLEEH TLVPSSALDN EVYDKLPSIH YGGAQQPVHP
LRNHNPPPTA RPWRGDEVVA NQHHLPQPPL LQQHELLNSY YIHRWPDPAP VAAHVHQDFQ
PALHLVALNT PLSGGMRGIR GADFQCFQQA RQVGLAGTFR AFLSSRLQDL YSIVRRADRT
AVPIVNLRDE VLFSNWEALF TGSEAPLRAG ARILSFDGRD ILQDSAWPQK SIWHGSDAKG
RRLPESYCEA WRTDERGTSG QASSLSSGKL LEQSASSCQH AFVVLCIENS FMTAAKK
//
