Reviewed, UniProtKB/Swiss-Prot P78310 (CXAR_HUMAN)

Names and origin

Protein names

Recommended name:
    Coxsackievirus and adenovirus receptor
Alternative name(s):
    Coxsackievirus B-adenovirus receptor
    HCVADR
      Short name=hCAR
    CVB3-binding protein

Gene names

Name:	CXADR
Synonyms:	CAR

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the epithelial apical junction complex that is essential for the tight junction integrity. Proposed to function as a homophilic cell adhesion molecule. Recruits MPDZ to intercellular contact sites. Probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN) through adhesive interactions with AMICA1/JAML located in the plasma membrane of PMN. Ref.1 Ref.12 Ref.17 Ref.18 Ref.25
Subunit structure	Monomer. Probably homodimer formed by 2 molecules on adjacent cells. Interacts with LNX, MPDZ, BAIAP1, DLG4, PRKCABP, TJP1 and CTNNB1. Secreted isoform 3, isoform 4 and isoform 5 can interact with the extracellular domain of the receptor. Interacts with adenovirus subgroup A, C, D, E and F fiber proteins as well as coxsackievirus B1, B2, B3, B4, B5 and B6 capsid proteins and acts as a receptor for these viruses. Ref.17 Ref.18 Ref.25 Ref.5 Ref.11 Ref.13 Ref.20 Ref.22 Ref.23
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein. Cell junction › tight junction. Cell junction › adherens junction. Basolateral cell membrane; Single-pass type I membrane protein. Note: In epithelial cells localizes to the apical junction complex composced of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface. Ref.17 Ref.18 Ref.5 Ref.22 Ref.16 Ref.19 Ref.21 Isoform 2: Cell membrane; Single-pass type I membrane protein. Cell junction › tight junction. Cell junction › adherens junction. Basolateral cell membrane; Single-pass membrane protein. Note: In epithelial cells localizes to the apical junction complex composced of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface. Ref.17 Ref.18 Ref.5 Ref.22 Ref.16 Ref.19 Ref.21 Isoform 3: Secreted. Ref.17 Ref.18 Ref.5 Ref.22 Ref.16 Ref.19 Ref.21 Isoform 4: Secreted. Ref.17 Ref.18 Ref.5 Ref.22 Ref.16 Ref.19 Ref.21 Isoform 5: Secreted. Ref.17 Ref.18 Ref.5 Ref.22 Ref.16 Ref.19 Ref.21
Tissue specificity	Expressed in pancreas, brain, heart, small intestine, testis, prostate and at a lower level in liver and lung. Isoform 5 is ubiquitoulsy expressed while 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. Ref.1 Ref.21 Ref.10 Ref.14 Ref.15
Domain	The Ig-like C2-type 1 domain probably mediates homodimerization and interaction with JAML. Ref.25 Ref.28 The PDZ-binding motif mediates interaction with MPDZ and BAIAP1. Ref.25 Ref.28
Post-translational modification	N-glycosylated By similarity. Palmitoylated on Cys-259 and/or Cys-260; required for proper localization to the plasma membrane. Ref.19
Sequence similarities	Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Cell adhesion Host-virus interaction
Cellular component	Cell junction Cell membrane Membrane Secreted Tight junction
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA adherens junction Inferred from electronic annotation. Source: UniProtKB-SubCell basolateral plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc tight junction Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from electronic annotation. Source: UniProtKB-KW receptor activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78310-1) Also known as: SIV; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: In epithelial cells localizes to the apical junction complex composced of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface. Ref.17 Ref.18 Ref.5 Ref.22 Ref.16 Ref.19 Ref.21
Isoform 2 (identifier: P78310-2) Also known as: CAR2; HCAR2; TVV; The sequence of this isoform differs from the canonical sequence as follows:      340-345: VAAPNL → FKYPY      346-365: Missing.
Note: In epithelial cells localizes to the apical junction complex composced of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface. Ref.17 Ref.18 Ref.5 Ref.22 Ref.16 Ref.19 Ref.21
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Sequence conflict	343	1	P → A in AAD31772. Ref.10
Isoform 3 (identifier: P78310-3) Also known as: CAR2/7; Gamma; The sequence of this isoform differs from the canonical sequence as follows:      71-89: IILYSGDKIYDDYYPDLKG → GRCATSKEPYVHCQKLHRQ      90-365: Missing.
Isoform 4 (identifier: P78310-4) Also known as: CAR3/7; The sequence of this isoform differs from the canonical sequence as follows:      139-139: V → GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDIPRLSITKYQVKTLNALLRVRLSHLLR      140-365: Missing.
Isoform 5 (identifier: P78310-5) Also known as: CAR4/7; Beta; The sequence of this isoform differs from the canonical sequence as follows:      191-191: E → GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDIPRLSITKYQVKTLNALLRVRLSHLLR      192-365: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Chain

20 – 365

346

Coxsackievirus and adenovirus receptor

PRO_0000014739

Regions

Topological domain

20 – 237

218

Extracellular Potential

Transmembrane

238 – 258

21

Potential

Topological domain

259 – 365

107

Cytoplasmic Potential

Domain

20 – 134

115

Ig-like C2-type 1

Domain

141 – 228

88

Ig-like C2-type 2

Motif

360 – 365

6

PDZ-binding

Amino acid modifications

Modified residue

293

1

Phosphoserine By similarity

Modified residue

300

1

Phosphoserine By similarity

Modified residue

306

1

Phosphoserine Ref.26

Modified residue

323

1

Phosphoserine By similarity

Modified residue

332

1

Phosphoserine Ref.26 Ref.24

Lipidation

259

1

S-palmitoyl cysteine Probable

Lipidation

260

1

S-palmitoyl cysteine Probable

Glycosylation

106

1

N-linked (GlcNAc...) Potential

Glycosylation

201

1

N-linked (GlcNAc...) Potential

Disulfide bond

41 ↔ 120

Disulfide bond

162 ↔ 212

By similarity

Natural variations

Alternative sequence

71 – 89

19

IILYS…PDLKG → GRCATSKEPYVHCQKLHRQ in isoform 3.

VSP_014819

Alternative sequence

90 – 365

276

Missing in isoform 3.

VSP_014820

Alternative sequence

139

1

V → GKMCHLQRAVRPLPEATSAV IIHPWGPCLLPTWKDIPRLS ITKYQVKTLNALLRVRLSHL LR in isoform 4.

VSP_014821

Alternative sequence

140 – 365

226

Missing in isoform 4.

VSP_014822

Alternative sequence

191

1

E → GKMCHLQRAVRPLPEATSAV IIHPWGPCLLPTWKDIPRLS ITKYQVKTLNALLRVRLSHL LR in isoform 5.

VSP_014823

Alternative sequence

192 – 365

174

Missing in isoform 5.

VSP_014824

Alternative sequence

340 – 345

6

VAAPNL → FKYPY in isoform 2.

VSP_014825

Alternative sequence

346 – 365

20

Missing in isoform 2.

VSP_014826

Natural variant

323

1

S → R: dbSNP rs34727960.

VAR_049871

Experimental info

Mutagenesis

70 – 72

3

VII → AID: Abolishes binding to adenovirus type 5. Ref.12 Ref.19

Mutagenesis

259 – 260

2

CC → AA: Loss of palmitoylation and altered localization. Ref.19

Mutagenesis

318

1

Y → A: Affects basolateral localization in airway epithelial cells. Ref.16 Ref.19

Mutagenesis

345 – 348

4

LSRM → AAAA: Affects basolateral localization in airway epithelial cells. Ref.16 Ref.19

Secondary structure

1

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365

Helix Strand Turn

Details...

Beta strand

21 – 32

12

Beta strand

37 – 39

3

Beta strand

42 – 44

3

Beta strand

53 – 61

9

Beta strand

68 – 75

8

Beta strand

78 – 80

3

Turn

86 – 90

5

Beta strand

91 – 93

3

Helix

98 – 100

3

Beta strand

105 – 107

3

Helix

112 – 114

3

Beta strand

116 – 124

9

Beta strand

127 – 138

12

Beta strand

145 – 148

4

Beta strand

156 – 163

8

Beta strand

166 – 168

3

Beta strand

171 – 178

8

Helix

185 – 192

8

Beta strand

195 – 201

7

Beta strand

208 – 215

8

Beta strand

221 – 227

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SIV) [UniParc]. Last modified May 1, 1997. Version 1. Checksum: AB01C6346CB7FE64	FASTA	365	40,030
	10 20 30 40 50 60 MALLLCFVLL CGVVDFARSL SITTPEEMIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS 70 80 90 100 110 120 PADNQKVDQV IILYSGDKIY DDYYPDLKGR VHFTSNDLKS GDASINVTNL QLSDIGTYQC 130 140 150 160 170 180 KVKKAPGVAN KKIHLVVLVK PSGARCYVDG SEEIGSDFKI KCEPKEGSLP LQYEWQKLSD 190 200 210 220 230 240 SQKMPTSWLA EMTSSVISVK NASSEYSGTY SCTVRNRVGS DQCLLRLNVV PPSNKAGLIA 250 260 270 280 290 300 GAIIGTLLAL ALIGLIIFCC RKKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS 310 320 330 340 350 360 SLGSMSPSNM EGYSKTQYNQ VPSEDFERTP QSPTLPPAKV AAPNLSRMGA IPVMIPAQSK DGSIV
	Isoform 2 (CAR2) (HCAR2) (TVV). Checksum: EEE9C22E96C697AA	FASTA	344	38,124
	10 20 30 40 50 60 MALLLCFVLL CGVVDFARSL SITTPEEMIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS 70 80 90 100 110 120 PADNQKVDQV IILYSGDKIY DDYYPDLKGR VHFTSNDLKS GDASINVTNL QLSDIGTYQC 130 140 150 160 170 180 KVKKAPGVAN KKIHLVVLVK PSGARCYVDG SEEIGSDFKI KCEPKEGSLP LQYEWQKLSD 190 200 210 220 230 240 SQKMPTSWLA EMTSSVISVK NASSEYSGTY SCTVRNRVGS DQCLLRLNVV PPSNKAGLIA 250 260 270 280 290 300 GAIIGTLLAL ALIGLIIFCC RKKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS 310 320 330 340 SLGSMSPSNM EGYSKTQYNQ VPSEDFERTP QSPTLPPAKF KYPY
	Isoform 3 (CAR2/7) (Gamma). Checksum: 50951EAAC77CAE36	FASTA	89	9,967
	10 20 30 40 50 60 MALLLCFVLL CGVVDFARSL SITTPEEMIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS 70 80 PADNQKVDQV GRCATSKEPY VHCQKLHRQ
	Isoform 4 (CAR3/7). Checksum: 43FDB19DF6A7FEB8	FASTA	200	22,370
	10 20 30 40 50 60 MALLLCFVLL CGVVDFARSL SITTPEEMIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS 70 80 90 100 110 120 PADNQKVDQV IILYSGDKIY DDYYPDLKGR VHFTSNDLKS GDASINVTNL QLSDIGTYQC 130 140 150 160 170 180 KVKKAPGVAN KKIHLVVLGK MCHLQRAVRP LPEATSAVII HPWGPCLLPT WKDIPRLSIT 190 200 KYQVKTLNAL LRVRLSHLLR
	Isoform 5 (CAR4/7) (Beta). Checksum: 4532559D01AB67E2	FASTA	252	28,201
	10 20 30 40 50 60 MALLLCFVLL CGVVDFARSL SITTPEEMIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS 70 80 90 100 110 120 PADNQKVDQV IILYSGDKIY DDYYPDLKGR VHFTSNDLKS GDASINVTNL QLSDIGTYQC 130 140 150 160 170 180 KVKKAPGVAN KKIHLVVLVK PSGARCYVDG SEEIGSDFKI KCEPKEGSLP LQYEWQKLSD 190 200 210 220 230 240 SQKMPTSWLA GKMCHLQRAV RPLPEATSAV IIHPWGPCLL PTWKDIPRLS ITKYQVKTLN 250 ALLRVRLSHL LR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses." Tomko R.P., Xu R., Philipson L. Proc. Natl. Acad. Sci. U.S.A. 94:3352-3356(1997) [PubMed: 9096397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS A VIRUS RECEPTOR, TISSUE SPECIFICITY.
[2]	"Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5." 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. Science 275:1320-1323(1997) [PubMed: 9036860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Genomic organization and chromosomal localization of the human Coxsackievirus B-adenovirus receptor gene." Bowles K.R., Gibson J., Wu J., Shaffer L.G., Towbin J.A., Bowles N.E. Hum. Genet. 105:354-359(1999) [PubMed: 10543405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor." 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. Nat. Struct. Biol. 8:874-878(2001) [PubMed: 11573093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Alternatively spliced soluble coxsackie-adenovirus receptors inhibit coxsackievirus infection." Doerner A., Xiong D., Couch K., Yajima T., Knowlton K.U. J. Biol. Chem. 279:18497-18503(2004) [PubMed: 14978041] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), INTERACTION WITH COXSACKIEVIRUS TYPE B3, SUBCELLULAR LOCATION.
[6]	"Putative regulatory domains in the human and mouse CAR genes." Andersson B., Tomko R.P., Andersson K., Darban H., Oncu D., Mizra M., Sollerbrant K., Sonnhammer E., Philipson L. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Cervix.
[8]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Cervix.
[10]	"Expression of Coxsackie-adenovirus-receptor and alpha v-integrin does not correlate with adenovector targeting in vivo indicating anatomical vector barriers." 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. Gene Ther. 6:1520-1535(1999) [PubMed: 10490761] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. Tissue: Liver.
[11]	"The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F." 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. J. Virol. 72:7909-7915(1998) [PubMed: 9733828] [Abstract] Cited for: INTERACTION WITH ADENOVIRUS SUBGROUP A, C, D, E, F FIBER PROTEINS.
[12]	"Expression of the adenovirus receptor and its interaction with the fiber knob." Tomko R.P., Johansson C.B., Totrov M., Abagyan R., Frisen J., Philipson L. Exp. Cell Res. 255:47-55(2000) [PubMed: 10666333] [Abstract] Cited for: FUNCTION IN VIRAL BINDING, MUTAGENESIS OF 70-VAL--ILE-72.
[13]	"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." 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. Virology 271:99-108(2000) [PubMed: 10814575] [Abstract] Cited for: INTERACTION WITH COXSACKIEVIRUS GROUP B CAPSID PROTEINS.
[14]	"Identification of alternative splice products encoded by the human coxsackie-adenovirus receptor gene." Thoelen I., Magnusson C., Tagerud S., Polacek C., Lindberg M., Van Ranst M. Biochem. Biophys. Res. Commun. 287:216-222(2001) [PubMed: 11549277] [Abstract] Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[15]	"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." 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. Circulation 104:275-280(2001) [PubMed: 11457744] [Abstract] Cited for: TISSUE SPECIFICITY.
[16]	"Multiple regions within the coxsackievirus and adenovirus receptor cytoplasmic domain are required for basolateral sorting." Cohen C.J., Gaetz J., Ohman T., Bergelson J.M. J. Biol. Chem. 276:25392-25398(2001) [PubMed: 11316797] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-318 AND 345-LEU--MET-348.
[17]	"The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction." Cohen C.J., Shieh J.T.C., Pickles R.J., Okegawa T., Hsieh J.-T., Bergelson J.M. Proc. Natl. Acad. Sci. U.S.A. 98:15191-15196(2001) [PubMed: 11734628] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TJP1, FUNCTION.
[18]	"Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape." Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J., Welsh M.J. Cell 110:789-799(2002) [PubMed: 12297051] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1, FUNCTION.
[19]	"Fatty acid modification of the coxsackievirus and adenovirus receptor." van't Hof W., Crystal R.G. J. Virol. 76:6382-6386(2002) [PubMed: 12021372] [Abstract] Cited for: PALMITOYLATION AT CYS-259 AND CYS-260, SUBCELLULAR LOCATION, MUTAGENESIS OF 259-CYS-CYS-260.
[20]	"The Coxsackievirus and adenovirus receptor (CAR) forms a complex with the PDZ domain-containing protein ligand-of-numb protein-X (LNX)." Sollerbrant K., Raschperger E., Mirza M., Engstroem U., Philipson L., Ljungdahl P.O., Pettersson R.F. J. Biol. Chem. 278:7439-7444(2003) [PubMed: 12468544] [Abstract] Cited for: INTERACTION WITH LNX.
[21]	"Isoform-specific expression of the Coxsackie and adenovirus receptor (CAR) in neuromuscular junction and cardiac intercalated discs." Shaw C.A., Holland P.C., Sinnreich M., Allen C., Sollerbrant K., Karpati G., Nalbantoglu J. BMC Cell Biol. 5:42-42(2004) [PubMed: 15533241] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
[22]	"The coxsackievirus and adenovirus receptor interacts with the multi-PDZ domain protein-1 (MUPP-1) within the tight junction." Coyne C.B., Voelker T., Pichla S.L., Bergelson J.M. J. Biol. Chem. 279:48079-48084(2004) [PubMed: 15364909] [Abstract] Cited for: INTERACTION WITH MPDZ, SUBCELLULAR LOCATION.
[23]	"A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth." Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L., Zabner J. J. Cell Sci. 117:4401-4409(2004) [PubMed: 15304526] [Abstract] Cited for: INTERACTION WITH BAIAP1; DLG4 AND PRKCABP.
[24]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, MASS SPECTROMETRY. Tissue: Epithelium.
[25]	"Neutrophil migration across tight junctions is mediated by adhesive interactions between epithelial CAR and a JAM-like protein on neutrophils." Zen K., Liu Y., McCall I.C., Wu T., Lee W., Babbin B.A., Nusrat A., Parkos C.A. Mol. Biol. Cell 16:2694-2703(2005) [PubMed: 15800062] [Abstract] Cited for: INTERACTION WITH AMICA1, DOMAIN, FUNCTION.
[26]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-332, MASS SPECTROMETRY.
[27]	"Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR." Bewley M.C., Springer K., Zhang Y.-B., Freimuth P., Flanagan J.M. Science 286:1579-1583(1999) [PubMed: 10567268] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-144 IN COMPLEX WITH ADENOVIRUS 12 FIBER PROTEIN.
[28]	"Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution." van Raaij M.J., Chouin E., van der Zandt H., Bergelson J.M., Cusack S. Structure 8:1147-1155(2000) [PubMed: 11080637] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 15-140, DOMAIN.
[29]	"Solution structure of the coxsackievirus and adenovirus receptor domain 1." Jiang S., Jacobs A., Laue T.M., Caffrey M. Biochemistry 43:1847-1853(2004) [PubMed: 14967025] [Abstract] Cited for: STRUCTURE BY NMR OF 21-144.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U90716 mRNA. Translation: AAC51234.1.
Y07593 mRNA. Translation: CAA68868.1.
AF169366 , AF169360, AF169361, AF169362, AF169363, AF169364, AF169365 Genomic DNA. Translation: AAF05908.1.
AF200465 Genomic DNA. Translation: AAF24344.1.
AY072910 mRNA. Translation: AAL68878.1.
AY072911 mRNA. Translation: AAL68879.1.
AY072912 mRNA. Translation: AAL68880.1.
AF242865, AF242862, AF242864 Genomic DNA. Translation: AAG01088.1.
CR617256 mRNA. No translation available.
BT019876 mRNA. Translation: AAV38679.1.
BC003684 mRNA. Translation: AAH03684.1.
BC010536 mRNA. Translation: AAH10536.1.
AF124598 mRNA. Translation: AAD31772.1.

IPI

IPI00019146.
IPI00103422.
IPI00103423.
IPI00383114.
IPI00607658.

RefSeq

NP_001329.1.

UniGene

Hs.705503

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EAJ	X-ray	1.35	A/B	15-140	[»]
1F5W	X-ray	1.70	A/B	15-140	[»]
1JEW	electron microscopy	22.00	R	21-140	[»]
1KAC	X-ray	2.60	B	22-144	[»]
1P69	X-ray	3.10	B	22-144	[»]
1P6A	X-ray	2.90	B	22-144	[»]
1RSF	NMR	-	A	21-144	[»]
2J12	X-ray	1.50	B	15-140	[»]
2J1K	X-ray	2.30	A/B/G/J/K/O/P/T/V/X/Y/Z	15-140	[»]
2NPL	NMR	-	X	142-235	[»]
2W9L	X-ray	2.91	A/B/G/J/K/O/P/T/V/X/Y/Z	16-139	[»]
2WBW	X-ray	1.55	B	15-138	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P78310. 2 interactions.

PTM databases

PhosphoSite

P78310.

Proteomic databases

PRIDE

P78310.

Genome annotation databases

Ensembl

ENSG00000154639. Homo sapiens. [Contig view]

GeneID

1525.

KEGG

hsa:1525.

Organism-specific databases

GeneCards

GC21P017807.

H-InvDB

HIX0016031.

HGNC

HGNC:2559. CXADR.

HPA

CAB005103.
HPA003342.

MIM

602621. gene.

PharmGKB

PA27055.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P78310.

HOVERGEN

P78310.

OMA

P78310. CLLRLDV.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

P78310.

Bgee

P78310.

CleanEx

HS_CXADR.

GermOnline

ENSG00000154639. Homo sapiens.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 2 hits.

Pfam

PF07679. I-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

6315.

SOURCE

Search...

Entry information

Entry name

CXAR_HUMAN

Accession

Primary (citable) accession number: P78310
Secondary accession number(s): O00694 , Q8WWT6, Q8WWT7, Q8WWT8, Q9UKV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1997
Last modified:	June 16, 2009
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)