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Coxsackievirus and adenovirus receptor (CAR) (hCAR) (CVB3-binding protein) (Coxsackievirus B-adenovirus receptor) (HCVADR)

 CXAR_HUMAN              Reviewed;         365 AA.
P78310; B2R8V8; B7WPI3; D3YHP0; O00694; Q8WWT6; Q8WWT7; Q8WWT8;
Q9UKV4;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
25-OCT-2017, entry version 183.
RecName: Full=Coxsackievirus and adenovirus receptor;
Short=CAR;
Short=hCAR;
AltName: Full=CVB3-binding protein;
AltName: Full=Coxsackievirus B-adenovirus receptor;
AltName: Full=HCVADR;
Flags: Precursor;
Name=CXADR; Synonyms=CAR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS A VIRUS RECEPTOR,
AND TISSUE SPECIFICITY.
PubMed=9096397; DOI=10.1073/pnas.94.7.3352;
Tomko R.P., Xu R., Philipson L.;
"HCAR and MCAR: the human and mouse cellular receptors for subgroup C
adenoviruses and group B coxsackieviruses.";
Proc. Natl. Acad. Sci. U.S.A. 94:3352-3356(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9036860; DOI=10.1126/science.275.5304.1320;
Bergelson J.M., Cunningham J.A., Droguett G., Kurt-Jones E.,
Krithivas A., Hong J.S., Horwitz M.S., Crowell R.L., Finberg R.W.;
"Isolation of a common receptor for Coxsackie B viruses and
adenoviruses 2 and 5.";
Science 275:1320-1323(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10543405; DOI=10.1007/s004399900136;
Bowles K.R., Gibson J., Wu J., Shaffer L.G., Towbin J.A., Bowles N.E.;
"Genomic organization and chromosomal localization of the human
Coxsackievirus B-adenovirus receptor gene.";
Hum. Genet. 105:354-359(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11573093; DOI=10.1038/nsb1001-874;
He Y., Chipman P.R., Howitt J., Bator C.M., Whitt M.A., Baker T.S.,
Kuhn R.J., Anderson C.W., Freimuth P., Rossmann M.G.;
"Interaction of coxsackievirus B3 with the full length coxsackievirus-
adenovirus receptor.";
Nat. Struct. Biol. 8:874-878(2001).
[5]
FUNCTION (MICROBIAL INFECTION), NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS
3; 4 AND 5), INTERACTION WITH COXSACKIEVIRUS TYPE B3, AND SUBCELLULAR
LOCATION.
PubMed=14978041; DOI=10.1074/jbc.M311754200;
Doerner A., Xiong D., Couch K., Yajima T., Knowlton K.U.;
"Alternatively spliced soluble coxsackie-adenovirus receptors inhibit
coxsackievirus infection.";
J. Biol. Chem. 279:18497-18503(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Andersson B., Tomko R.P., Andersson K., Darban H., Oncu D., Mizra M.,
Sollerbrant K., Sonnhammer E., Philipson L.;
"Putative regulatory domains in the human and mouse CAR genes.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
Dietel M.;
"Identification and characterisation of CAR 4/6 as a new splice
variant of the Coxsackie adenovirus receptor (CAR).";
Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cervix;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE
SPECIFICITY.
TISSUE=Liver;
PubMed=10490761; DOI=10.1038/sj.gt.3301030;
Fechner H., Haack A., Wang H., Wang X., Eizema K., Pauschinger M.,
Schoemaker R.G., van Veghel R., Houtsmuller A.B., Schultheiss H.-P.,
Lamers J.M.J., Poller W.;
"Expression of Coxsackie-adenovirus-receptor and alpha v-integrin does
not correlate with adenovector targeting in vivo indicating anatomical
vector barriers.";
Gene Ther. 6:1520-1535(1999).
[15]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ADENOVIRUS
SUBGROUPS A/C/D/E/F FIBER PROTEINS.
PubMed=9733828;
Roelvink P.W., Lizonova A., Lee J.G.M., Li Y., Bergelson J.M.,
Finberg R.W., Brough D.E., Kovesdi I., Wickham T.J.;
"The coxsackievirus-adenovirus receptor protein can function as a
cellular attachment protein for adenovirus serotypes from subgroups A,
C, D, E, and F.";
J. Virol. 72:7909-7915(1998).
[16]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HUMAN ADENOVIRUS
FIBER PROTEIN, AND MUTAGENESIS OF 70-VAL--ILE-72.
PubMed=10666333; DOI=10.1006/excr.1999.4761;
Tomko R.P., Johansson C.B., Totrov M., Abagyan R., Frisen J.,
Philipson L.;
"Expression of the adenovirus receptor and its interaction with the
fiber knob.";
Exp. Cell Res. 255:47-55(2000).
[17]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS
GROUP B CAPSID PROTEINS.
PubMed=10814575; DOI=10.1006/viro.2000.0324;
Martino T.A., Petric M., Weingartl H., Bergelson J.M., Opavsky M.A.,
Richardson C.D., Modlin J.F., Finberg R.W., Kain K.C., Willis N.,
Gauntt C.J., Liu P.P.;
"The coxsackie-adenovirus receptor (CAR) is used by reference strains
and clinical isolates representing all six serotypes of coxsackievirus
group B and by swine vesicular disease virus.";
Virology 271:99-108(2000).
[18]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=11549277; DOI=10.1006/bbrc.2001.5535;
Thoelen I., Magnusson C., Tagerud S., Polacek C., Lindberg M.,
Van Ranst M.;
"Identification of alternative splice products encoded by the human
coxsackie-adenovirus receptor gene.";
Biochem. Biophys. Res. Commun. 287:216-222(2001).
[19]
TISSUE SPECIFICITY.
PubMed=11457744; DOI=10.1161/01.CIR.104.3.275;
Noutsias M., Fechner H., de Jonge H., Wang X., Dekkers D.,
Houtsmuller A.B., Pauschinger M., Bergelson J.M., Warraich R.,
Yacoub M., Hetzer R., Lamers J.M.J., Schultheiss H.-P., Poller W.;
"Human coxsackie-adenovirus receptor is colocalized with integrins
alpha(v)beta(3) and alpha(v)beta(5) on the cardiomyocyte sarcolemma
and upregulated in dilated cardiomyopathy: implications for
cardiotropic viral infections.";
Circulation 104:275-280(2001).
[20]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-318 AND 345-LEU--MET-348.
PubMed=11316797; DOI=10.1074/jbc.M009531200;
Cohen C.J., Gaetz J., Ohman T., Bergelson J.M.;
"Multiple regions within the coxsackievirus and adenovirus receptor
cytoplasmic domain are required for basolateral sorting.";
J. Biol. Chem. 276:25392-25398(2001).
[21]
SUBCELLULAR LOCATION, INTERACTION WITH TJP1, AND FUNCTION.
PubMed=11734628; DOI=10.1073/pnas.261452898;
Cohen C.J., Shieh J.T.C., Pickles R.J., Okegawa T., Hsieh J.-T.,
Bergelson J.M.;
"The coxsackievirus and adenovirus receptor is a transmembrane
component of the tight junction.";
Proc. Natl. Acad. Sci. U.S.A. 98:15191-15196(2001).
[22]
FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, INTERACTION WITH
CTNNB1, AND INTERACTION WITH HUMAN ADENOVIRUS FIBER PROTEIN.
PubMed=12297051; DOI=10.1016/S0092-8674(02)00912-1;
Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J.,
Welsh M.J.;
"Adenovirus fiber disrupts CAR-mediated intercellular adhesion
allowing virus escape.";
Cell 110:789-799(2002).
[23]
PALMITOYLATION AT CYS-259 AND CYS-260, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 259-CYS-CYS-260.
PubMed=12021372; DOI=10.1128/JVI.76.12.6382-6386.2002;
van't Hof W., Crystal R.G.;
"Fatty acid modification of the coxsackievirus and adenovirus
receptor.";
J. Virol. 76:6382-6386(2002).
[24]
INTERACTION WITH LNX.
PubMed=12468544; DOI=10.1074/jbc.M205927200;
Sollerbrant K., Raschperger E., Mirza M., Engstroem U., Philipson L.,
Ljungdahl P.O., Pettersson R.F.;
"The Coxsackievirus and adenovirus receptor (CAR) forms a complex with
the PDZ domain-containing protein ligand-of-numb protein-X (LNX).";
J. Biol. Chem. 278:7439-7444(2003).
[25]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
PubMed=15533241; DOI=10.1186/1471-2121-5-42;
Shaw C.A., Holland P.C., Sinnreich M., Allen C., Sollerbrant K.,
Karpati G., Nalbantoglu J.;
"Isoform-specific expression of the Coxsackie and adenovirus receptor
(CAR) in neuromuscular junction and cardiac intercalated discs.";
BMC Cell Biol. 5:42-42(2004).
[26]
INTERACTION WITH MPDZ, AND SUBCELLULAR LOCATION.
PubMed=15364909; DOI=10.1074/jbc.M409061200;
Coyne C.B., Voelker T., Pichla S.L., Bergelson J.M.;
"The coxsackievirus and adenovirus receptor interacts with the multi-
PDZ domain protein-1 (MUPP-1) within the tight junction.";
J. Biol. Chem. 279:48079-48084(2004).
[27]
INTERACTION WITH BAIAP1; DLG4 AND PRKCABP.
PubMed=15304526; DOI=10.1242/jcs.01300;
Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L.,
Zabner J.;
"A role for the PDZ-binding domain of the coxsackie B virus and
adenovirus receptor (CAR) in cell adhesion and growth.";
J. Cell Sci. 117:4401-4409(2004).
[28]
INTERACTION WITH JAML, DOMAIN, AND FUNCTION.
PubMed=15800062; DOI=10.1091/mbc.E05-01-0036;
Zen K., Liu Y., McCall I.C., Wu T., Lee W., Babbin B.A., Nusrat A.,
Parkos C.A.;
"Neutrophil migration across tight junctions is mediated by adhesive
interactions between epithelial CAR and a JAM-like protein on
neutrophils.";
Mol. Biol. Cell 16:2694-2703(2005).
[29]
FUNCTION IN LEUKOCYTE MIGRATION, AND INTERACTION WITH JAML.
PubMed=19064666; DOI=10.1083/jcb.200805061;
Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O.,
Bourdoulous S.;
"JAM-L-mediated leukocyte adhesion to endothelial cells is regulated
in cis by alpha4beta1 integrin activation.";
J. Cell Biol. 183:1159-1173(2008).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-332, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-323 AND
SER-332, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-144 IN COMPLEX WITH HUMAN
ADENOVIRUS 12 FIBER PROTEIN, AND DISULFIDE BONDS.
PubMed=10567268; DOI=10.1126/science.286.5444.1579;
Bewley M.C., Springer K., Zhang Y.-B., Freimuth P., Flanagan J.M.;
"Structural analysis of the mechanism of adenovirus binding to its
human cellular receptor, CAR.";
Science 286:1579-1583(1999).
[36]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 15-140, DOMAIN, AND DISULFIDE
BOND.
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).
[37]
STRUCTURE BY NMR OF 21-144, AND DISULFIDE BONDS.
PubMed=14967025; DOI=10.1021/bi035490x;
Jiang S., Jacobs A., Laue T.M., Caffrey M.;
"Solution structure of the coxsackievirus and adenovirus receptor
domain 1.";
Biochemistry 43:1847-1853(2004).
-!- FUNCTION: Component of the epithelial apical junction complex that
may function as a homophilic cell adhesion molecule and is
essential for tight junction integrity. Also involved in
transepithelial migration of leukocytes through adhesive
interactions with JAML a transmembrane protein of the plasma
membrane of leukocytes. The interaction between both receptors
also mediates the activation of gamma-delta T-cells, a
subpopulation of T-cells residing in epithelia and involved in
tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML
induces downstream cell signaling events in gamma-delta T-cells
through PI3-kinase and MAP kinases. It results in proliferation
and production of cytokines and growth factors by T-cells that in
turn stimulate epithelial tissues repair.
{ECO:0000269|PubMed:11734628, ECO:0000269|PubMed:12297051,
ECO:0000269|PubMed:15800062, ECO:0000269|PubMed:19064666,
ECO:0000269|PubMed:9096397}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for adenovirus
type C (PubMed:9733828, PubMed:10666333, PubMed:12297051,
PubMed:10567268). Acts as a receptor for Coxsackievirus B1 to B6
(PubMed:14978041, PubMed:10814575). {ECO:0000269|PubMed:10567268,
ECO:0000269|PubMed:10666333, ECO:0000269|PubMed:10814575,
ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:14978041,
ECO:0000269|PubMed:9733828}.
-!- SUBUNIT: Monomer. May form homodimer. Interacts with LNX, BAIAP1,
DLG4, PRKCABP, TJP1 and CTNNB1. Interacts with MPDZ; recruits MPDZ
to intercellular contact sites. Interacts with JAML (homodimeric
form). Secreted isoform 3, isoform 4 and isoform 5 can interact
with the extracellular domain of the receptor.
{ECO:0000269|PubMed:11734628, ECO:0000269|PubMed:12468544,
ECO:0000269|PubMed:15304526, ECO:0000269|PubMed:15364909,
ECO:0000269|PubMed:15800062, ECO:0000269|PubMed:19064666}.
-!- SUBUNIT: (Microbial infection) Interacts with adenovirus subgroups
A, C, D, E and F fiber proteins as well as coxsackievirus B1, B2,
B3, B4, B5 and B6 capsid proteins (PubMed:14978041,
PubMed:9733828, PubMed:10666333, PubMed:10814575, PubMed:12297051,
PubMed:10567268). {ECO:0000269|PubMed:10567268,
ECO:0000269|PubMed:10666333, ECO:0000269|PubMed:10814575,
ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:14978041,
ECO:0000269|PubMed:9733828}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:15533241}; Single-pass type I membrane protein
{ECO:0000255}. Basolateral cell membrane
{ECO:0000269|PubMed:11316797, ECO:0000269|PubMed:12021372,
ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:15364909}; Single-
pass type I membrane protein {ECO:0000255}. Cell junction, tight
junction {ECO:0000269|PubMed:11734628,
ECO:0000269|PubMed:12297051}. Cell junction, adherens junction
{ECO:0000269|PubMed:12297051}. Note=In epithelial cells localizes
to the apical junction complex composed of tight and adherens
junctions (PubMed:12297051). In airway epithelial cells localized
to basolateral membrane but not to apical surface
(PubMed:11316797). {ECO:0000269|PubMed:11316797,
ECO:0000269|PubMed:12297051}.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted
{ECO:0000269|PubMed:14978041}.
-!- SUBCELLULAR LOCATION: Isoform 4: Secreted
{ECO:0000269|PubMed:14978041}.
-!- SUBCELLULAR LOCATION: Isoform 5: Secreted
{ECO:0000269|PubMed:14978041}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=SIV;
IsoId=P78310-1; Sequence=Displayed;
Name=2; Synonyms=CAR2, HCAR2, TVV;
IsoId=P78310-2; Sequence=VSP_014825, VSP_014826;
Note=Ref.14 (AAD31772) sequence is in conflict in position:
343:P->A. {ECO:0000305};
Name=3; Synonyms=CAR2/7, Gamma;
IsoId=P78310-3; Sequence=VSP_014819, VSP_014820;
Name=4; Synonyms=CAR3/7;
IsoId=P78310-4; Sequence=VSP_014821, VSP_014822;
Name=5; Synonyms=CAR4/7, Beta;
IsoId=P78310-5; Sequence=VSP_014823, VSP_014824;
Name=6;
IsoId=P78310-6; Sequence=VSP_047357;
Note=Gene prediction based on EST data.;
Name=7; Synonyms=CAR 4/6;
IsoId=P78310-7; Sequence=VSP_047729;
-!- TISSUE SPECIFICITY: Expressed in pancreas, brain, heart, small
intestine, testis, prostate and at a lower level in liver and
lung. Isoform 5 is ubiquitously expressed. Isoform 3 is expressed
in heart, lung and pancreas. In skeletal muscle, isoform 1 is
found at the neuromuscular junction and isoform 2 is found in
blood vessels. In cardiac muscle, isoform 1 and isoform 2 are
found at intercalated disks. In heart expressed in subendothelial
layers of the vessel wall but not in the luminal endothelial
surface. Expression is elevated in hearts with dilated
cardiomyopathy. {ECO:0000269|PubMed:10490761,
ECO:0000269|PubMed:11457744, ECO:0000269|PubMed:11549277,
ECO:0000269|PubMed:9096397}.
-!- DOMAIN: The Ig-like C2-type 1 domain mediates homodimerization and
interaction with JAML.
-!- DOMAIN: The PDZ-binding motif mediates interaction with MPDZ and
BAIAP1.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: Palmitoylated on Cys-259 and/or Cys-260; required for proper
localization to the plasma membrane.
{ECO:0000269|PubMed:12021372}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U90716; AAC51234.1; -; mRNA.
EMBL; Y07593; CAA68868.1; -; mRNA.
EMBL; AF169366; AAF05908.1; -; Genomic_DNA.
EMBL; AF169360; AAF05908.1; JOINED; Genomic_DNA.
EMBL; AF169361; AAF05908.1; JOINED; Genomic_DNA.
EMBL; AF169362; AAF05908.1; JOINED; Genomic_DNA.
EMBL; AF169363; AAF05908.1; JOINED; Genomic_DNA.
EMBL; AF169364; AAF05908.1; JOINED; Genomic_DNA.
EMBL; AF169365; AAF05908.1; JOINED; Genomic_DNA.
EMBL; AF200465; AAF24344.1; -; Genomic_DNA.
EMBL; AY072910; AAL68878.1; -; mRNA.
EMBL; AY072911; AAL68879.1; -; mRNA.
EMBL; AY072912; AAL68880.1; -; mRNA.
EMBL; AF242865; AAG01088.1; -; Genomic_DNA.
EMBL; AF242862; AAG01088.1; JOINED; Genomic_DNA.
EMBL; AF242864; AAG01088.1; JOINED; Genomic_DNA.
EMBL; GU474812; ADC84500.1; -; mRNA.
EMBL; CR617256; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BT019876; AAV38679.1; -; mRNA.
EMBL; AK313526; BAG36305.1; -; mRNA.
EMBL; AP000963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX10031.1; -; Genomic_DNA.
EMBL; BC003684; AAH03684.1; -; mRNA.
EMBL; BC010536; AAH10536.1; -; mRNA.
EMBL; AF124598; AAD31772.1; -; mRNA.
CCDS; CCDS33519.1; -. [P78310-1]
CCDS; CCDS56204.1; -. [P78310-6]
CCDS; CCDS56205.1; -. [P78310-5]
CCDS; CCDS56206.1; -. [P78310-4]
CCDS; CCDS56207.1; -. [P78310-3]
RefSeq; NP_001193992.1; NM_001207063.1. [P78310-5]
RefSeq; NP_001193993.1; NM_001207064.1. [P78310-4]
RefSeq; NP_001193994.1; NM_001207065.1. [P78310-3]
RefSeq; NP_001193995.1; NM_001207066.1. [P78310-6]
RefSeq; NP_001329.1; NM_001338.4. [P78310-1]
RefSeq; XP_011527781.1; XM_011529479.1. [P78310-5]
UniGene; Hs.627078; -.
PDB; 1EAJ; X-ray; 1.35 A; A/B=15-140.
PDB; 1F5W; X-ray; 1.70 A; A/B=15-140.
PDB; 1JEW; EM; 22.00 A; R=21-140.
PDB; 1KAC; X-ray; 2.60 A; B=22-144.
PDB; 1P69; X-ray; 3.10 A; B=22-144.
PDB; 1P6A; X-ray; 2.90 A; B=22-144.
PDB; 1RSF; NMR; -; A=21-144.
PDB; 2J12; X-ray; 1.50 A; B=15-140.
PDB; 2J1K; X-ray; 2.30 A; A/B/G/J/K/O/P/T/V/X/Y/Z=15-140.
PDB; 2NPL; NMR; -; X=142-235.
PDB; 2W9L; X-ray; 2.91 A; A/B/G/J/K/O/P/T/V/X/Y/Z=16-139.
PDB; 2WBW; X-ray; 1.55 A; B=15-138.
PDB; 3J6L; EM; 9.00 A; B=15-140.
PDB; 3J6M; EM; 9.00 A; B=22-144.
PDB; 3J6N; EM; 9.00 A; K=20-233.
PDB; 3J6O; EM; 9.00 A; S=20-236.
PDBsum; 1EAJ; -.
PDBsum; 1F5W; -.
PDBsum; 1JEW; -.
PDBsum; 1KAC; -.
PDBsum; 1P69; -.
PDBsum; 1P6A; -.
PDBsum; 1RSF; -.
PDBsum; 2J12; -.
PDBsum; 2J1K; -.
PDBsum; 2NPL; -.
PDBsum; 2W9L; -.
PDBsum; 2WBW; -.
PDBsum; 3J6L; -.
PDBsum; 3J6M; -.
PDBsum; 3J6N; -.
PDBsum; 3J6O; -.
ProteinModelPortal; P78310; -.
SMR; P78310; -.
BioGrid; 107905; 18.
IntAct; P78310; 6.
MINT; MINT-111007; -.
STRING; 9606.ENSP00000284878; -.
iPTMnet; P78310; -.
PhosphoSitePlus; P78310; -.
SwissPalm; P78310; -.
BioMuta; CXADR; -.
DMDM; 6685351; -.
EPD; P78310; -.
MaxQB; P78310; -.
PaxDb; P78310; -.
PeptideAtlas; P78310; -.
PRIDE; P78310; -.
DNASU; 1525; -.
Ensembl; ENST00000284878; ENSP00000284878; ENSG00000154639. [P78310-1]
Ensembl; ENST00000356275; ENSP00000348620; ENSG00000154639. [P78310-3]
Ensembl; ENST00000400165; ENSP00000383029; ENSG00000154639. [P78310-4]
Ensembl; ENST00000400166; ENSP00000383030; ENSG00000154639. [P78310-5]
Ensembl; ENST00000400169; ENSP00000383033; ENSG00000154639. [P78310-6]
GeneID; 1525; -.
KEGG; hsa:1525; -.
UCSC; uc002ykh.3; human. [P78310-1]
CTD; 1525; -.
DisGeNET; 1525; -.
EuPathDB; HostDB:ENSG00000154639.18; -.
GeneCards; CXADR; -.
HGNC; HGNC:2559; CXADR.
HPA; CAB005103; -.
HPA; HPA003342; -.
HPA; HPA030411; -.
HPA; HPA030412; -.
MIM; 602621; gene.
neXtProt; NX_P78310; -.
OpenTargets; ENSG00000154639; -.
PharmGKB; PA27055; -.
eggNOG; ENOG410IGDG; Eukaryota.
eggNOG; ENOG4110WP1; LUCA.
GeneTree; ENSGT00760000119145; -.
HOGENOM; HOG000111222; -.
HOVERGEN; HBG105787; -.
InParanoid; P78310; -.
KO; K06788; -.
OMA; VGNKKIQ; -.
OrthoDB; EOG091G05PI; -.
PhylomeDB; P78310; -.
TreeFam; TF330875; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
ChiTaRS; CXADR; human.
EvolutionaryTrace; P78310; -.
GeneWiki; Coxsackie_virus_and_adenovirus_receptor; -.
GenomeRNAi; 1525; -.
PRO; PR:P78310; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000154639; -.
CleanEx; HS_CXADR; -.
Genevisible; P78310; HS.
GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0044297; C:cell body; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:CACAO.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:UniProtKB.
GO; GO:0086082; F:cell adhesive protein binding involved in AV node cell-bundle of His cell communication; IC:BHF-UCL.
GO; GO:0071253; F:connexin binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0086067; P:AV node cell to bundle of His cell communication; ISS:UniProtKB.
GO; GO:0086072; P:AV node cell-bundle of His cell adhesion involved in cell communication; ISS:BHF-UCL.
GO; GO:0048739; P:cardiac muscle fiber development; ISS:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0010669; P:epithelial structure maintenance; IMP:UniProtKB.
GO; GO:0046629; P:gamma-delta T cell activation; ISS:UniProtKB.
GO; GO:0008354; P:germ cell migration; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; IMP:UniProtKB.
GO; GO:0098904; P:regulation of AV node cell action potential; ISS:BHF-UCL.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0070633; P:transepithelial transport; IMP:UniProtKB.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
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.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF00047; ig; 1.
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.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction;
Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Secreted; Signal; Tight junction; Transmembrane; Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 365 Coxsackievirus and adenovirus receptor.
/FTId=PRO_0000014739.
TOPO_DOM 20 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TOPO_DOM 259 365 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 134 Ig-like C2-type 1.
DOMAIN 141 228 Ig-like C2-type 2.
MOTIF 360 365 PDZ-binding.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:P97792}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000250|UniProtKB:P97792}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000250|UniProtKB:P97792}.
LIPID 259 259 S-palmitoyl cysteine.
{ECO:0000305|PubMed:12021372}.
LIPID 260 260 S-palmitoyl cysteine.
{ECO:0000305|PubMed:12021372}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 120 {ECO:0000269|PubMed:10567268,
ECO:0000269|PubMed:11080637,
ECO:0000269|PubMed:14967025}.
DISULFID 162 212 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:14967025}.
VAR_SEQ 71 89 IILYSGDKIYDDYYPDLKG -> GRCATSKEPYVHCQKLHR
Q (in isoform 3).
{ECO:0000303|PubMed:14978041}.
/FTId=VSP_014819.
VAR_SEQ 90 365 Missing (in isoform 3).
{ECO:0000303|PubMed:14978041}.
/FTId=VSP_014820.
VAR_SEQ 139 139 V -> GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDI
PRLSITKYQVKTLNALLRVRLSHLLR (in isoform
4). {ECO:0000303|PubMed:14978041}.
/FTId=VSP_014821.
VAR_SEQ 140 365 Missing (in isoform 4).
{ECO:0000303|PubMed:14978041}.
/FTId=VSP_014822.
VAR_SEQ 191 232 EMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVP
P -> A (in isoform 7).
{ECO:0000303|Ref.7}.
/FTId=VSP_047729.
VAR_SEQ 191 191 E -> GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDI
PRLSITKYQVKTLNALLRVRLSHLLR (in isoform
5). {ECO:0000303|PubMed:14978041}.
/FTId=VSP_014823.
VAR_SEQ 192 365 Missing (in isoform 5).
{ECO:0000303|PubMed:14978041}.
/FTId=VSP_014824.
VAR_SEQ 340 365 VAAPNLSRMGAIPVMIPAQSKDGSIV -> FKYPYKTDGIT
VV (in isoform 6). {ECO:0000305}.
/FTId=VSP_047357.
VAR_SEQ 340 345 VAAPNL -> FKYPY (in isoform 2).
{ECO:0000303|Ref.8}.
/FTId=VSP_014825.
VAR_SEQ 346 365 Missing (in isoform 2).
{ECO:0000303|Ref.8}.
/FTId=VSP_014826.
VARIANT 323 323 S -> R (in dbSNP:rs34727960).
/FTId=VAR_049871.
MUTAGEN 70 72 VII->AID: Abolishes binding to adenovirus
type 5. {ECO:0000269|PubMed:10666333}.
MUTAGEN 259 260 CC->AA: Loss of palmitoylation and
altered localization.
{ECO:0000269|PubMed:12021372}.
MUTAGEN 318 318 Y->A: Affects basolateral localization in
airway epithelial cells.
{ECO:0000269|PubMed:11316797}.
MUTAGEN 345 348 LSRM->AAAA: Affects basolateral
localization in airway epithelial cells.
{ECO:0000269|PubMed:11316797}.
STRAND 21 32 {ECO:0000244|PDB:1EAJ}.
STRAND 37 39 {ECO:0000244|PDB:1EAJ}.
STRAND 42 44 {ECO:0000244|PDB:1EAJ}.
STRAND 53 61 {ECO:0000244|PDB:1EAJ}.
STRAND 62 65 {ECO:0000244|PDB:1RSF}.
STRAND 68 75 {ECO:0000244|PDB:1EAJ}.
STRAND 78 80 {ECO:0000244|PDB:1EAJ}.
TURN 86 90 {ECO:0000244|PDB:1EAJ}.
STRAND 91 93 {ECO:0000244|PDB:1EAJ}.
HELIX 98 100 {ECO:0000244|PDB:1EAJ}.
STRAND 105 107 {ECO:0000244|PDB:1EAJ}.
HELIX 112 114 {ECO:0000244|PDB:1EAJ}.
STRAND 116 124 {ECO:0000244|PDB:1EAJ}.
STRAND 127 138 {ECO:0000244|PDB:1EAJ}.
STRAND 145 148 {ECO:0000244|PDB:2NPL}.
STRAND 156 163 {ECO:0000244|PDB:2NPL}.
STRAND 166 168 {ECO:0000244|PDB:2NPL}.
STRAND 171 178 {ECO:0000244|PDB:2NPL}.
HELIX 185 192 {ECO:0000244|PDB:2NPL}.
STRAND 195 201 {ECO:0000244|PDB:2NPL}.
STRAND 208 215 {ECO:0000244|PDB:2NPL}.
STRAND 221 227 {ECO:0000244|PDB:2NPL}.
SEQUENCE 365 AA; 40030 MW; AB01C6346CB7FE64 CRC64;
MALLLCFVLL CGVVDFARSL SITTPEEMIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS
PADNQKVDQV IILYSGDKIY DDYYPDLKGR VHFTSNDLKS GDASINVTNL QLSDIGTYQC
KVKKAPGVAN KKIHLVVLVK PSGARCYVDG SEEIGSDFKI KCEPKEGSLP LQYEWQKLSD
SQKMPTSWLA EMTSSVISVK NASSEYSGTY SCTVRNRVGS DQCLLRLNVV PPSNKAGLIA
GAIIGTLLAL ALIGLIIFCC RKKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
SLGSMSPSNM EGYSKTQYNQ VPSEDFERTP QSPTLPPAKV AAPNLSRMGA IPVMIPAQSK
DGSIV


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