Reviewed,
UniProtKB/Swiss-Prot P78310 (CXAR_HUMAN)
Last modified
June 16, 2009.
Version 97.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 |
| ||||
| 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
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 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||
| 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
| ||||||||||||||||||||||||||||||||||||||||||
References
| « Hide '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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| U90716 mRNA. Translation: AAC51234.1. Y07593 mRNA. Translation: CAA68868.1. AF169366 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 Q9UKV4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 21 Human chromosome 21: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


