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P78310 (CXAR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coxsackievirus and adenovirus receptor

Short name=CAR
Short name=hCAR
Alternative name(s):
CVB3-binding protein
Coxsackievirus B-adenovirus receptor
HCVADR
Gene names
Name:CXADR
Synonyms:CAR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the epithelial apical junction complex that may function as an homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with AMICA1/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, AMICA1 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. Ref.1 Ref.21 Ref.22 Ref.28 Ref.29

Subunit structure

Monomer. May form homodimer. Interacts with LNX, BAIAP1, DLG4, PRKCABP, TJP1 and CTNNB1. Interacts with MPDZ; recruits MPDZ to intercellular contact sites. Interacts with AMICA1 (homodimeric form). Secreted isoform 3, isoform 4 and isoform 5 can interact with the extracellular domain of the receptor. 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 and acts as a receptor for these viruses. Ref.5 Ref.15 Ref.16 Ref.17 Ref.21 Ref.22 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein. Cell junctiontight junction. Cell junctionadherens junction. Basolateral cell membrane; Single-pass type I membrane protein. Note: In epithelial cells localizes to the apical junction complex composed of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface. Ref.5 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26

Isoform 2: Cell membrane; Single-pass type I membrane protein. Cell junctiontight junction. Cell junctionadherens 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.5 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26

Isoform 3: Secreted Ref.5 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26.

Isoform 4: Secreted Ref.5 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26.

Isoform 5: Secreted Ref.5 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26.

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. Ref.1 Ref.14 Ref.18 Ref.19 Ref.25

Domain

The Ig-like C2-type 1 domain mediates homodimerization and interaction with AMICA1. Ref.28 Ref.34

The PDZ-binding motif mediates interaction with MPDZ and BAIAP1. Ref.28 Ref.34

Post-translational modification

N-glycosylated By similarity.

Palmitoylated on Cys-259 and/or Cys-260; required for proper localization to the plasma membrane. Ref.23

Sequence similarities

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processCell adhesion
Host-virus interaction
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
Tight junction
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHost cell receptor for virus entry
Receptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processAV node cell to bundle of His cell communication

Inferred from sequence or structural similarity. Source: UniProtKB

actin cytoskeleton reorganization

Inferred from direct assay PubMed 17675666. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cardiac muscle fiber development

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell junction organization

Inferred from sequence or structural similarity. Source: UniProtKB

defense response to virus

Inferred from direct assay Ref.5. Source: UniProtKB

epithelial structure maintenance

Inferred from mutant phenotype Ref.27. Source: UniProtKB

gamma-delta T cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

germ cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

heart development

Inferred from sequence or structural similarity. Source: UniProtKB

heterophilic cell-cell adhesion

Inferred from direct assay PubMed 12869515Ref.28. Source: UniProtKB

homotypic cell-cell adhesion

Inferred from direct assay Ref.21. Source: UniProtKB

leukocyte migration

Traceable author statement. Source: Reactome

mitochondrion organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

neutrophil chemotaxis

Inferred from mutant phenotype Ref.28. Source: UniProtKB

regulation of immune response

Traceable author statement. Source: Reactome

single organismal cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

transepithelial transport

Inferred from mutant phenotype Ref.28. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentacrosomal vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

adherens junction

Inferred from direct assay Ref.22. Source: UniProtKB

apicolateral plasma membrane

Inferred from direct assay Ref.26. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay PubMed 20361046Ref.20. Source: UniProtKB

cell body

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from direct assay. Source: HPA

cell-cell junction

Inferred from direct assay PubMed 17675666PubMed 20235596. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from direct assay Ref.5. Source: UniProtKB

filopodium

Inferred from sequence or structural similarity. Source: UniProtKB

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Non-traceable author statement Ref.1. Source: UniProtKB

intercalated disc

Inferred from direct assay Ref.25. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 17675666. Source: UniProtKB

neuromuscular junction

Inferred from direct assay Ref.25. Source: UniProtKB

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay PubMed 16780588Ref.1. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 17675666. Source: UniProtKB

tight junction

Inferred from direct assay Ref.28Ref.21. Source: UniProtKB

   Molecular_functionPDZ domain binding

Inferred from physical interaction Ref.26. Source: UniProtKB

beta-catenin binding

Inferred from physical interaction Ref.22. Source: UniProtKB

cell adhesion molecule binding

Inferred from physical interaction PubMed 12869515Ref.28. Source: UniProtKB

connexin binding

Inferred from sequence or structural similarity. Source: UniProtKB

identical protein binding

Inferred from direct assay Ref.5. Source: UniProtKB

integrin binding

Inferred from physical interaction PubMed 12869515. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.21PubMed 17675666. Source: UniProtKB

receptor binding

Inferred from physical interaction Ref.5. Source: UniProtKB

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 7 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.
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.
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.
Isoform 6 (identifier: P78310-6)

The sequence of this isoform differs from the canonical sequence as follows:
     340-365: VAAPNLSRMGAIPVMIPAQSKDGSIV → FKYPYKTDGITVV
Note: Gene prediction based on EST data.
Isoform 7 (identifier: P78310-7)

Also known as: CAR 4/6;

The sequence of this isoform differs from the canonical sequence as follows:
     191-232: EMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPP → A

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 365346Coxsackievirus and adenovirus receptor
PRO_0000014739

Regions

Topological domain20 – 237218Extracellular Potential
Transmembrane238 – 25821Helical; Potential
Topological domain259 – 365107Cytoplasmic Potential
Domain20 – 134115Ig-like C2-type 1
Domain141 – 22888Ig-like C2-type 2
Motif360 – 3656PDZ-binding

Amino acid modifications

Modified residue3061Phosphoserine Ref.30
Modified residue3231Phosphoserine By similarity
Modified residue3321Phosphoserine Ref.30
Lipidation2591S-palmitoyl cysteine Probable
Lipidation2601S-palmitoyl cysteine Probable
Glycosylation1061N-linked (GlcNAc...) Potential
Glycosylation2011N-linked (GlcNAc...) Potential
Disulfide bond41 ↔ 120
Disulfide bond162 ↔ 212 By similarity

Natural variations

Alternative sequence71 – 8919IILYS…PDLKG → GRCATSKEPYVHCQKLHRQ in isoform 3.
VSP_014819
Alternative sequence90 – 365276Missing in isoform 3.
VSP_014820
Alternative sequence1391V → GKMCHLQRAVRPLPEATSAV IIHPWGPCLLPTWKDIPRLS ITKYQVKTLNALLRVRLSHL LR in isoform 4.
VSP_014821
Alternative sequence140 – 365226Missing in isoform 4.
VSP_014822
Alternative sequence191 – 23242EMTSS…NVVPP → A in isoform 7.
VSP_047729
Alternative sequence1911E → GKMCHLQRAVRPLPEATSAV IIHPWGPCLLPTWKDIPRLS ITKYQVKTLNALLRVRLSHL LR in isoform 5.
VSP_014823
Alternative sequence192 – 365174Missing in isoform 5.
VSP_014824
Alternative sequence340 – 36526VAAPN…DGSIV → FKYPYKTDGITVV in isoform 6.
VSP_047357
Alternative sequence340 – 3456VAAPNL → FKYPY in isoform 2.
VSP_014825
Alternative sequence346 – 36520Missing in isoform 2.
VSP_014826
Natural variant3231S → R.
Corresponds to variant rs34727960 [ dbSNP | Ensembl ].
VAR_049871

Experimental info

Mutagenesis70 – 723VII → AID: Abolishes binding to adenovirus type 5. Ref.16 Ref.23
Mutagenesis259 – 2602CC → AA: Loss of palmitoylation and altered localization. Ref.23
Mutagenesis3181Y → A: Affects basolateral localization in airway epithelial cells. Ref.20 Ref.23
Mutagenesis345 – 3484LSRM → AAAA: Affects basolateral localization in airway epithelial cells. Ref.20 Ref.23
Isoform 2:
Sequence conflict3431P → A in AAD31772. Ref.14

Secondary structure

........................................... 365
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SIV) [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: AB01C6346CB7FE64

FASTA36540,030
        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 

« Hide

Isoform 2 (CAR2) (HCAR2) (TVV) [UniParc].

Checksum: EEE9C22E96C697AA
Show »

FASTA34438,124
Isoform 3 (CAR2/7) (Gamma) [UniParc].

Checksum: 50951EAAC77CAE36
Show »

FASTA899,967
Isoform 4 (CAR3/7) [UniParc].

Checksum: 43FDB19DF6A7FEB8
Show »

FASTA20022,370
Isoform 5 (CAR4/7) (Beta) [UniParc].

Checksum: 4532559D01AB67E2
Show »

FASTA25228,201
Isoform 6 [UniParc].

Checksum: 0D7C56FEBE6BD653
Show »

FASTA35238,938
Isoform 7 (CAR 4/6) [UniParc].

Checksum: 97915CFCAF43B698
Show »

FASTA32435,570

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]"Identification and characterisation of CAR 4/6 as a new splice variant of the Coxsackie adenovirus receptor (CAR)."
Dietel M.
Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
[8]"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.
[9]"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).
[10]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[11]"The DNA sequence of human chromosome 21."
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. expand/collapse author list , 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.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cervix.
[14]"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] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Tissue: Liver.
[15]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS SUBGROUPS A/C/D/E/F FIBER PROTEINS.
[16]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS FIBER PROTEIN, MUTAGENESIS OF 70-VAL--ILE-72.
[17]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUS GROUP B CAPSID PROTEINS.
[18]"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] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[19]"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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[20]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-318 AND 345-LEU--MET-348.
[21]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TJP1, FUNCTION.
[22]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1, INTERACTION WITH HUMAN ADENOVIRUS FIBER PROTEIN, FUNCTION.
[23]"Fatty acid modification of the coxsackievirus and adenovirus receptor."
van't Hof W., Crystal R.G.
J. Virol. 76:6382-6386(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-259 AND CYS-260, SUBCELLULAR LOCATION, MUTAGENESIS OF 259-CYS-CYS-260.
[24]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LNX.
[25]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
[26]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPDZ, SUBCELLULAR LOCATION.
[27]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAIAP1; DLG4 AND PRKCABP.
[28]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AMICA1, DOMAIN, FUNCTION.
[29]"JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis by alpha4beta1 integrin activation."
Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O., Bourdoulous S.
J. Cell Biol. 183:1159-1173(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LEUKOCYTE MIGRATION, INTERACTION WITH AMICA1.
[30]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-144 IN COMPLEX WITH HUMAN ADENOVIRUS 12 FIBER PROTEIN.
[34]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 15-140, DOMAIN.
[35]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 21-144.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U90716 mRNA. Translation: AAC51234.1.
Y07593 mRNA. Translation: CAA68868.1.
AF169366 expand/collapse EMBL AC list , 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.
GU474812 mRNA. Translation: ADC84500.1.
CR617256 mRNA. No translation available.
BT019876 mRNA. Translation: AAV38679.1.
AK313526 mRNA. Translation: BAG36305.1.
AP000963 Genomic DNA. No translation available.
AP000967 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX10031.1.
BC003684 mRNA. Translation: AAH03684.1.
BC010536 mRNA. Translation: AAH10536.1.
AF124598 mRNA. Translation: AAD31772.1.
CCDSCCDS33519.1. [P78310-1]
CCDS56204.1. [P78310-6]
CCDS56205.1. [P78310-5]
CCDS56206.1. [P78310-4]
CCDS56207.1. [P78310-3]
RefSeqNP_001193992.1. NM_001207063.1. [P78310-5]
NP_001193993.1. NM_001207064.1. [P78310-4]
NP_001193994.1. NM_001207065.1. [P78310-3]
NP_001193995.1. NM_001207066.1. [P78310-6]
NP_001329.1. NM_001338.4. [P78310-1]
UniGeneHs.627078.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EAJX-ray1.35A/B15-140[»]
1F5WX-ray1.70A/B15-140[»]
1JEWelectron microscopy22.00R21-140[»]
1KACX-ray2.60B22-144[»]
1P69X-ray3.10B22-144[»]
1P6AX-ray2.90B22-144[»]
1RSFNMR-A21-144[»]
2J12X-ray1.50B15-140[»]
2J1KX-ray2.30A/B/G/J/K/O/P/T/V/X/Y/Z15-140[»]
2NPLNMR-X142-235[»]
2W9LX-ray2.91A/B/G/J/K/O/P/T/V/X/Y/Z16-139[»]
2WBWX-ray1.55B15-138[»]
3J6Lelectron microscopy9.00B15-140[»]
3J6Melectron microscopy9.00B22-144[»]
3J6Nelectron microscopy9.00K20-233[»]
3J6Oelectron microscopy9.00S20-236[»]
ProteinModelPortalP78310.
SMRP78310. Positions 16-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107905. 12 interactions.
IntActP78310. 3 interactions.
MINTMINT-111007.
STRING9606.ENSP00000284878.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteP78310.

Polymorphism databases

DMDM6685351.

Proteomic databases

MaxQBP78310.
PaxDbP78310.
PRIDEP78310.

Protocols and materials databases

DNASU1525.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284878; ENSP00000284878; ENSG00000154639. [P78310-1]
ENST00000306618; ENSP00000303395; ENSG00000154639. [P78310-7]
ENST00000356275; ENSP00000348620; ENSG00000154639. [P78310-3]
ENST00000400165; ENSP00000383029; ENSG00000154639. [P78310-4]
ENST00000400166; ENSP00000383030; ENSG00000154639. [P78310-5]
ENST00000400169; ENSP00000383033; ENSG00000154639. [P78310-6]
GeneID1525.
KEGGhsa:1525.
UCSCuc002ykh.2. human. [P78310-5]
uc002yki.3. human. [P78310-1]
uc010gld.2. human. [P78310-4]
uc010gle.2. human. [P78310-3]

Organism-specific databases

CTD1525.
GeneCardsGC21P018884.
HGNCHGNC:2559. CXADR.
HPACAB005103.
HPA003342.
HPA030411.
HPA030412.
MIM602621. gene.
neXtProtNX_P78310.
PharmGKBPA27055.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83644.
HOGENOMHOG000111222.
HOVERGENHBG105787.
InParanoidP78310.
KOK06788.
OMATEYSGTY.
OrthoDBEOG7MH0Z1.
PhylomeDBP78310.
TreeFamTF330875.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP78310.
BgeeP78310.
CleanExHS_CXADR.
GenevestigatorP78310.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamPF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCXADR. human.
EvolutionaryTraceP78310.
GeneWikiCoxsackie_virus_and_adenovirus_receptor.
GenomeRNAi1525.
NextBio35491112.
PROP78310.
SOURCESearch...

Entry information

Entry nameCXAR_HUMAN
AccessionPrimary (citable) accession number: P78310
Secondary accession number(s): B2R8V8 expand/collapse secondary AC list , B7WPI3, D3YHP0, O00694, Q8WWT6, Q8WWT7, Q8WWT8, Q9UKV4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM