CXAR_DANRE
ID CXAR_DANRE Reviewed; 372 AA.
AC Q90Y50; Q804R4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Coxsackievirus and adenovirus receptor homolog;
DE Short=CAR;
DE Flags: Precursor;
GN Name=cxadr;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11080637; DOI=10.1016/s0969-2126(00)00528-1;
RA van Raaij M.J., Chouin E., van der Zandt H., Bergelson J.M., Cusack S.;
RT "Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain
RT at 1.7 A resolution.";
RL Structure 8:1147-1155(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 75-372.
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4]
RP IDENTIFICATION.
RX PubMed=12239327; DOI=10.1128/jvi.76.20.10503-10506.2002;
RA Petrella J., Cohen C.J., Gaetz J., Bergelson J.M.;
RT "A zebrafish coxsackievirus and adenovirus receptor homologue interacts
RT with coxsackie B virus and adenovirus.";
RL J. Virol. 76:10503-10506(2002).
CC -!- FUNCTION: May function as a homophilic cell adhesion molecule and be
CC essential for tight junction integrity. May also be involved in
CC transepithelial migration of leukocytes through adhesive interactions
CC with jaml. The interaction between both receptors may also mediate the
CC activation of gamma-delta T-cells, a subpopulation of T-cells residing
CC in epithelia and involved in tissue homeostasis and repair (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Probably homodimer formed by 2 molecules on adjacent
CC cells (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P78310};
CC Single-pass type I membrane protein {ECO:0000255}. Basolateral cell
CC membrane {ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane
CC protein {ECO:0000255}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P78310}.
CC -!- DOMAIN: The Ig-like C2-type 1 domain may mediate homodimerization.
CC {ECO:0000250}.
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DR EMBL; AF268197; AAK58592.1; -; mRNA.
DR EMBL; BC045286; AAH45286.1; -; mRNA.
DR EMBL; AL732562; CAD61163.1; -; Genomic_DNA.
DR RefSeq; NP_694480.1; NM_152948.1.
DR AlphaFoldDB; Q90Y50; -.
DR SMR; Q90Y50; -.
DR STRING; 7955.ENSDARP00000064106; -.
DR PaxDb; Q90Y50; -.
DR PeptideAtlas; Q90Y50; -.
DR Ensembl; ENSDART00000064107; ENSDARP00000064106; ENSDARG00000043658.
DR Ensembl; ENSDART00000159751; ENSDARP00000141108; ENSDARG00000043658.
DR GeneID; 791793; -.
DR KEGG; dre:791793; -.
DR CTD; 1525; -.
DR ZFIN; ZDB-GENE-020814-2; cxadr.
DR eggNOG; ENOG502QSG0; Eukaryota.
DR GeneTree; ENSGT00940000154829; -.
DR HOGENOM; CLU_040549_0_0_1; -.
DR InParanoid; Q90Y50; -.
DR OMA; CQFTLAP; -.
DR OrthoDB; 896005at2759; -.
DR PhylomeDB; Q90Y50; -.
DR TreeFam; TF330875; -.
DR Reactome; R-DRE-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-DRE-202733; Cell surface interactions at the vascular wall.
DR PRO; PR:Q90Y50; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000043658; Expressed in liver and 21 other tissues.
DR ExpressionAtlas; Q90Y50; baseline.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IDA:ZFIN.
DR GO; GO:0009986; C:cell surface; IDA:ZFIN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014704; C:intercalated disc; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; IDA:ZFIN.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IMP:ZFIN.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..372
FT /note="Coxsackievirus and adenovirus receptor homolog"
FT /id="PRO_0000014743"
FT TOPO_DOM 23..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..140
FT /note="Ig-like C2-type 1"
FT DOMAIN 130..234
FT /note="Ig-like C2-type 2"
FT REGION 286..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 150..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 166..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 372 AA; 40664 MW; C363B71E7601C73A CRC64;
MDMRTSFLCV TYVILLTGSA CGLQITSTGQ TSIEKASGES VKLDCQFTLA SDDSGPLDIE
WSLQPSDNQK EEKVVIVYSG DRAFEHYYDP LKGRVHFNSP DPKNGDASMN IMGLKATDTG
TYQCKIKKVP GIASRKYLLT VMVRPSKPKC SAEGQTYVGK NMVLKCSSVE GTQPMEYIWE
RTSGNKLLPP LAILDKVTGT MTLKNATGDA SGTYRCQAKN RVGTEECVVE VTITQPPNTA
GIIAGVIICI LLLLILLALI LFCCCRARHK KKYEKEIAYE IREDVPPPKS RVSTARSFTS
VGSQRSSLGS MSPSNLHEYS KPQYDKIPSE EYDRPPSHAP IPPPSRMAGP NLSRMGAIPV
MIPAQNKDGS IV
