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Coxsackievirus and adenovirus receptor homolog (CAR)

 CXAR_DANRE              Reviewed;         372 AA.
Q90Y50; Q804R4;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 118.
RecName: Full=Coxsackievirus and adenovirus receptor homolog;
Short=CAR;
Flags: Precursor;
Name=cxadr;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11080637; DOI=10.1016/S0969-2126(00)00528-1;
van Raaij M.J., Chouin E., van der Zandt H., Bergelson J.M.,
Cusack S.;
"Dimeric structure of the coxsackievirus and adenovirus receptor D1
domain at 1.7 A resolution.";
Structure 8:1147-1155(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=AB; TISSUE=Embryo;
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 75-372.
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[4]
IDENTIFICATION.
PubMed=12239327; DOI=10.1128/JVI.76.20.10503-10506.2002;
Petrella J., Cohen C.J., Gaetz J., Bergelson J.M.;
"A zebrafish coxsackievirus and adenovirus receptor homologue
interacts with coxsackie B virus and adenovirus.";
J. Virol. 76:10503-10506(2002).
-!- FUNCTION: May function as a homophilic cell adhesion molecule and
be essential for tight junction integrity. May also be involved in
transepithelial migration of leukocytes through adhesive
interactions with jaml. The interaction between both receptors may
also mediate the activation of gamma-delta T-cells, a
subpopulation of T-cells residing in epithelia and involved in
tissue homeostasis and repair (By similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer. Probably homodimer formed by 2 molecules on
adjacent cells (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane
protein {ECO:0000255}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane
protein {ECO:0000255}. Cell junction, tight junction
{ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:P78310}.
-!- DOMAIN: The Ig-like C2-type 1 domain may mediate homodimerization.
{ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AF268197; AAK58592.1; -; mRNA.
EMBL; BC045286; AAH45286.1; -; mRNA.
EMBL; AL732562; CAD61163.1; -; Genomic_DNA.
RefSeq; NP_694480.1; NM_152948.1.
UniGene; Dr.11571; -.
ProteinModelPortal; Q90Y50; -.
SMR; Q90Y50; -.
STRING; 7955.ENSDARP00000064106; -.
PaxDb; Q90Y50; -.
PeptideAtlas; Q90Y50; -.
Ensembl; ENSDART00000064107; ENSDARP00000064106; ENSDARG00000043658.
Ensembl; ENSDART00000159751; ENSDARP00000141108; ENSDARG00000043658.
GeneID; 791793; -.
KEGG; dre:791793; -.
CTD; 1525; -.
ZFIN; ZDB-GENE-020814-2; cxadr.
eggNOG; ENOG410IGDG; Eukaryota.
eggNOG; ENOG4110WP1; LUCA.
GeneTree; ENSGT00760000119145; -.
HOGENOM; HOG000111222; -.
HOVERGEN; HBG105787; -.
InParanoid; Q90Y50; -.
KO; K06788; -.
OMA; VGNKKIQ; -.
OrthoDB; EOG091G05PI; -.
PhylomeDB; Q90Y50; -.
TreeFam; TF330875; -.
PRO; PR:Q90Y50; -.
Proteomes; UP000000437; Chromosome 10.
Bgee; ENSDARG00000043658; Expressed in 23 organ(s), highest expression level in liver.
ExpressionAtlas; Q90Y50; baseline.
GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005923; C:bicellular tight junction; IDA:ZFIN.
GO; GO:0009986; C:cell surface; IDA:ZFIN.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0001618; F:virus receptor activity; IDA:ZFIN.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0001822; P:kidney development; IMP:ZFIN.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
2: Evidence at transcript level;
Cell adhesion; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
Receptor; Reference proteome; Repeat; Signal; Tight junction;
Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 372 Coxsackievirus and adenovirus receptor
homolog.
/FTId=PRO_0000014743.
TOPO_DOM 23 241 Extracellular. {ECO:0000255}.
TRANSMEM 242 262 Helical. {ECO:0000255}.
TOPO_DOM 263 372 Cytoplasmic. {ECO:0000255}.
DOMAIN 23 140 Ig-like C2-type 1.
DOMAIN 130 234 Ig-like C2-type 2.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 45 124 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 150 227 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 166 216 {ECO:0000255|PROSITE-ProRule:PRU00114}.
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


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