ID A0A8C0VIX1_CYACU Unreviewed; 1687 AA.
AC A0A8C0VIX1;
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:ENSCCEP00000022788.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSCCEP00000022788.1};
OS Cyanistes caeruleus (Eurasian blue tit) (Parus caeruleus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Paridae; Cyanistes.
OX NCBI_TaxID=156563 {ECO:0000313|Ensembl:ENSCCEP00000022788.1, ECO:0000313|Proteomes:UP000694410};
RN [1] {ECO:0000313|Ensembl:ENSCCEP00000022788.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCEP00000022788.1}
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; ENSCCET00000034562.1; ENSCCEP00000022788.1; ENSCCEG00000020538.1.
DR Proteomes; UP000694410; Unplaced.
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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; 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:UP000694410};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1687
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034406379"
FT DOMAIN 389..577
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 34..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..56
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..98
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..593
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..640
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..882
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..928
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..954
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..990
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1058
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1687 AA; 173814 MW; 22E58E7DEA4CA465 CRC64;
MAPPRLGFLL LLACCFSCSE TQLLHWVWDS RKTTGSPAAP GEGIPALEPP TSAAAPAPSP
SPGTWGGEVA GNVTTPRRQE PDPATAAPGG EGTAAKTTEQ WDRNAMVEST VWPSIAPPHS
MSPAPGQQAA SSPTDDPRLL GTGTIEHFQI LGSGNTEDPQ LLGTGTIEDL HLLGSGNTEH
LQLLGTGTTE HLQLLSMRTA KEAQFLGSVT SKDAQLLGTR TTEDLQLLES GTTENPQLVR
MGTTEDPQLL GSRTSKDPEL LGSGTTEDLQ LLGLGTTEDP QLLGMISTTE DPQLLGTWTT
EDPQLLGKGT TEDLQLPGML TTENLQLLAM RNTKDTQLLR TVTPEDPELL RTVTTENPEL
LGTGTPTAME TQVSLQRPAG PQPESLSAEV SLLELIGDPP TEEIHRIYGP DNNPGYVFGP
NANTGQVARY HLPSPFYRDF SLLFHIQPTT PRAGVLFAVT DSSQSIIYVG VKLSELRAGQ
QQIIFYYTEP GSPSSYPAAT FTVPTLLNQW TRFAISVEEE EVVLYLDCEE HERVRFERSP
DEMELEEGSG LFVAQAGGAD PDKYQGVIAD LKLRGDPRAA ERQCEEEEDD TEVSGDFGSG
MEGGQKFSGK VEGVPGLVEA VPVTSPPVAG GSGPRSGGGS LQQAERTRVE ETLQVSTGGT
GRKGEKGEKG ERGLKGDSGT DGTIGPGSVK GQKGEKGDLG VKGSAGFGYP GSKGQKGEPG
DPGPPGAPSW HTDGSVVEQV TGPPGPPGKD GAPGRDGEPG EMGPPGFPGL PGEPGLKGEK
GDPGMGPRGP PGPPGPPGPP GPSSKNDKLT FIDMEGSGFG GDLESLRGPQ GPPGPPGPPG
VPGLPGEPGR FGMNRTDLPG PPGLPGRDGI PGPPGPVGPQ GPPGRDGEAG QPGPKGERGD
VGDLGLPGLP GPKGNKGEVG PVGPPGEMGL AGLPGPIGPR GQPGPPGPPG PPGPGYDAGF
GDMEGSGLSF SPGPPGPEGP QGVPGLPGVK GEVGSPGQPG LPGPKGDAGM PGVDGRPGLE
GFPGPQGPKG DKGSAGEKGE RGQDGVGLPG PPGPPGPPGQ VITVSSEDKS LVAFPGPEGR
PGHAGFPGPV GPKGDQGSTG PQGAPGLKGE KGEPGVIISP DGTVVTAKVK GEKGEPGLRG
PMGPSGPPGR AGMKGEIGFP GRPGRPGMNG LKGEKGDPAD VLGLRGPPGL PGPPGPPGPP
GSIVYNNGNT FSDSGHPVFP GFHQFPGQKG EKGDTGPPGP PGQFPYDVSH FSTSLRGDKG
DAGPKGEKGE PGSTPLYGAG VSGLPGPPGP QGYPGLPGPK GDSIVGPPGP PGPQGPPGIG
YEGRQGPPGP PGPPGPPSFP GPHRQAVSIP GPPGPPGPPG PPGTSGMFLG IRAVPTYQAM
LSSAHELPEG SLVFLTDRQE LYVRLRGGFR RVLLEEHNLI PSSALDNEVY DKPPTLRYAG
PQPHGPLHPL RNHVPPATAR PWRGDEVVAN QHRLPEQPLL HHQHELINGY YIHRRPDPVP
VAAHVHQDFQ PALHLVALNT PLSGGMRGIR GADFQCFQQA RQVGLAGTFR AFLSSRLQDL
YSIVRRADRA TVPIVNLRDE VLFNNWEALF MGSGAPLQAG ARILSFDGRD VLRDAGWPQK
SVWHGSDAKG RRLPESYCET WRTEERTVTG QASSLASGKL LEQVASSCQH AFIVLCIENS
FMTSAKK
//
