P78310 · CXAR_HUMAN

  • Protein
    Coxsackievirus and adenovirus receptor
  • Gene
    CXADR
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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.
(Microbial infection) Acts as a receptor for adenovirus type C.
(Microbial infection) Acts as a receptor for Coxsackievirus B1 to B6.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentacrosomal vesicle
Cellular Componentadherens junction
Cellular Componentapicolateral plasma membrane
Cellular Componentbasolateral plasma membrane
Cellular Componentbicellular tight junction
Cellular Componentcell body
Cellular Componentcell junction
Cellular Componentcell-cell junction
Cellular Componentcytoplasm
Cellular Componentextracellular region
Cellular Componentextracellular space
Cellular Componentfilopodium
Cellular Componentgrowth cone
Cellular Componentintercalated disc
Cellular Componentmembrane raft
Cellular Componentneuromuscular junction
Cellular Componentneuron projection
Cellular Componentnucleoplasm
Cellular Componentplasma membrane
Cellular Componentprotein-containing complex
Molecular Functionbeta-catenin binding
Molecular Functioncell adhesion molecule binding
Molecular Functioncell adhesive protein binding involved in AV node cell-bundle of His cell communication
Molecular Functionconnexin binding
Molecular Functionidentical protein binding
Molecular Functionintegrin binding
Molecular FunctionPDZ domain binding
Molecular Functionsignaling receptor binding
Molecular Functionvirus receptor activity
Biological Processactin cytoskeleton organization
Biological ProcessAV node cell to bundle of His cell communication
Biological ProcessAV node cell-bundle of His cell adhesion involved in cell communication
Biological Processcardiac muscle cell development
Biological Processcell-cell junction organization
Biological Processdefense response to virus
Biological Processepithelial structure maintenance
Biological Processgamma-delta T cell activation
Biological Processgerm cell migration
Biological Processheart development
Biological Processheterophilic cell-cell adhesion via plasma membrane cell adhesion molecules
Biological Processhomotypic cell-cell adhesion
Biological Processmitochondrion organization
Biological Processneutrophil chemotaxis
Biological Processregulation of AV node cell action potential
Biological Processtransepithelial transport

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Coxsackievirus and adenovirus receptor
  • Short names
    CAR; hCAR
  • Alternative names
    • CVB3-binding protein
    • Coxsackievirus B-adenovirus receptor
    • HCVADR

Gene names

    • Name
      CXADR
    • Synonyms
      CAR

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P78310
  • Secondary accessions
    • B2R8V8
    • B7WPI3
    • D3YHP0
    • O00694
    • Q8WWT6

Proteomes

Organism-specific databases

Subcellular Location

Isoform 1

Cell membrane
; Single-pass type I membrane protein
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 (PubMed:12297051).
In airway epithelial cells localized to basolateral membrane but not to apical surface (PubMed:11316797).

Isoform 3

Secreted

Isoform 4

Secreted

Isoform 5

Secreted

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain20-237Extracellular
Transmembrane238-258Helical
Topological domain259-365Cytoplasmic

Keywords

Disease & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis70-72Abolishes binding to adenovirus type 5.
Mutagenesis259-260Loss of palmitoylation and altered localization.
Mutagenesis318Affects basolateral localization in airway epithelial cells.
Natural variantVAR_049871323in dbSNP:rs34727960
Mutagenesis345-348Affects basolateral localization in airway epithelial cells.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 386 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, lipidation, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
Signal1-19UniProt
ChainPRO_000001473920-365UniProtCoxsackievirus and adenovirus receptor
Disulfide bond41↔120UniProt
Glycosylation106UniProtN-linked (GlcNAc...) asparagine
Disulfide bond162↔212UniProt
Glycosylation201UniProtN-linked (GlcNAc...) asparagine
Lipidation259UniProtS-palmitoyl cysteine
Lipidation260UniProtS-palmitoyl cysteine
Modified residue (large scale data)289PRIDEPhosphoserine
Modified residue (large scale data)290PRIDEPhosphothreonine
Modified residue (large scale data)293PRIDEPhosphoserine
Modified residue297UniProtPhosphoserine
Modified residue304UniProtPhosphoserine
Modified residue (large scale data)304PRIDEPhosphoserine
Modified residue306UniProtPhosphoserine
Modified residue (large scale data)306PRIDEPhosphoserine
Modified residue (large scale data)308PRIDEPhosphoserine
Modified residue (large scale data)313PRIDEPhosphotyrosine
Modified residue (large scale data)314PRIDEPhosphoserine
Modified residue (large scale data)318PRIDEPhosphotyrosine
Modified residue323UniProtPhosphoserine
Modified residue (large scale data)323PRIDEPhosphoserine
Modified residue (large scale data)329PRIDEPhosphothreonine
Modified residue332UniProtPhosphoserine
Modified residue (large scale data)332PRIDEPhosphoserine
Modified residue (large scale data)334PRIDEPhosphothreonine
Modified residue (large scale data)346PRIDEPhosphoserine
Modified residue (large scale data)359PRIDEPhosphoserine
Modified residue363UniProtPhosphoserine

Post-translational modification

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

Keywords

Proteomic databases

PTM databases

Expression

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.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Monomer. May form homodimer. Interacts with LNX, MAGI1, 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.
(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:10567268, PubMed:10666333, PubMed:10814575, PubMed:12297051, PubMed:14978041, PubMed:9733828).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P78310ANKRD46 Q86W74-23EBI-747931, EBI-12109402
BINARY P78310FAM3C Q925203EBI-747931, EBI-2876774
BINARY P78310MAL P211453EBI-747931, EBI-3932027

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, compositional bias, region, motif.

TypeIDPosition(s)Description
Domain20-134Ig-like C2-type 1
Domain141-228Ig-like C2-type 2
Compositional bias269-285Basic and acidic residues
Region269-343Disordered
Compositional bias286-330Polar residues
Motif360-365PDZ-binding

Domain

The Ig-like C2-type 1 domain mediates homodimerization and interaction with JAML.
The PDZ-binding motif mediates interaction with MPDZ and MAGI1.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (7)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 7 isoforms produced by Alternative splicing.

P78310-1

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.

  • Name
    1
  • Synonyms
    SIV
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    365
  • Mass (Da)
    40,030
  • Last updated
    1997-05-01 v1
  • Checksum
    AB01C6346CB7FE64
MALLLCFVLLCGVVDFARSLSITTPEEMIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPADNQKVDQVIILYSGDKIYDDYYPDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKIHLVVLVKPSGARCYVDGSEEIGSDFKIKCEPKEGSLPLQYEWQKLSDSQKMPTSWLAEMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPPSNKAGLIAGAIIGTLLALALIGLIIFCCRKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERTPQSPTLPPAKVAAPNLSRMGAIPVMIPAQSKDGSIV

P78310-2

  • Name
    2
  • Synonyms
    CAR2, HCAR2, TVV
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P78310-3

  • Name
    3
  • Synonyms
    CAR2/7, Gamma
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 71-89: IILYSGDKIYDDYYPDLKG → GRCATSKEPYVHCQKLHRQ
    • 90-365: Missing

P78310-4

  • Name
    4
  • Synonyms
    CAR3/7
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 139-139: V → GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDIPRLSITKYQVKTLNALLRVRLSHLLR
    • 140-365: Missing

P78310-5

  • Name
    5
  • Synonyms
    CAR4/7, Beta
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 191-191: E → GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDIPRLSITKYQVKTLNALLRVRLSHLLR
    • 192-365: Missing

P78310-6

  • Name
    6
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 340-365: VAAPNLSRMGAIPVMIPAQSKDGSIV → FKYPYKTDGITVV

P78310-7

  • Name
    7
  • Synonyms
    CAR 4/6
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 191-232: EMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPP → A

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_01481971-89in isoform 3
Alternative sequenceVSP_01482090-365in isoform 3
Alternative sequenceVSP_014821139in isoform 4
Alternative sequenceVSP_014822140-365in isoform 4
Alternative sequenceVSP_014823191in isoform 5
Alternative sequenceVSP_047729191-232in isoform 7
Alternative sequenceVSP_014824192-365in isoform 5
Compositional bias269-285Basic and acidic residues
Compositional bias286-330Polar residues
Alternative sequenceVSP_014825340-345in isoform 2
Alternative sequenceVSP_047357340-365in isoform 6
Sequence conflict343In isoform P78310-2; in Ref. 14; AAD31772
Alternative sequenceVSP_014826346-365in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U90716
EMBL· GenBank· DDBJ
AAC51234.1
EMBL· GenBank· DDBJ
mRNA
Y07593
EMBL· GenBank· DDBJ
CAA68868.1
EMBL· GenBank· DDBJ
mRNA
AF169366
EMBL· GenBank· DDBJ
AAF05908.1
EMBL· GenBank· DDBJ
Genomic DNA
AF169360
EMBL· GenBank· DDBJ
AAF05908.1
EMBL· GenBank· DDBJ
Genomic DNA
AF169361
EMBL· GenBank· DDBJ
AAF05908.1
EMBL· GenBank· DDBJ
Genomic DNA
AF169362
EMBL· GenBank· DDBJ
AAF05908.1
EMBL· GenBank· DDBJ
Genomic DNA
AF169363
EMBL· GenBank· DDBJ
AAF05908.1
EMBL· GenBank· DDBJ
Genomic DNA
AF169364
EMBL· GenBank· DDBJ
AAF05908.1
EMBL· GenBank· DDBJ
Genomic DNA
AF169365
EMBL· GenBank· DDBJ
AAF05908.1
EMBL· GenBank· DDBJ
Genomic DNA
AF200465
EMBL· GenBank· DDBJ
AAF24344.1
EMBL· GenBank· DDBJ
Genomic DNA
AY072910
EMBL· GenBank· DDBJ
AAL68878.1
EMBL· GenBank· DDBJ
mRNA
AY072911
EMBL· GenBank· DDBJ
AAL68879.1
EMBL· GenBank· DDBJ
mRNA
AY072912
EMBL· GenBank· DDBJ
AAL68880.1
EMBL· GenBank· DDBJ
mRNA
AF242865
EMBL· GenBank· DDBJ
AAG01088.1
EMBL· GenBank· DDBJ
Genomic DNA
AF242862
EMBL· GenBank· DDBJ
AAG01088.1
EMBL· GenBank· DDBJ
Genomic DNA
AF242864
EMBL· GenBank· DDBJ
AAG01088.1
EMBL· GenBank· DDBJ
Genomic DNA
GU474812
EMBL· GenBank· DDBJ
ADC84500.1
EMBL· GenBank· DDBJ
mRNA
CR617256
EMBL· GenBank· DDBJ
-mRNA No translation available.
BT019876
EMBL· GenBank· DDBJ
AAV38679.1
EMBL· GenBank· DDBJ
mRNA
AK313526
EMBL· GenBank· DDBJ
BAG36305.1
EMBL· GenBank· DDBJ
mRNA
AP000963
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AP000967
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471079
EMBL· GenBank· DDBJ
EAX10031.1
EMBL· GenBank· DDBJ
Genomic DNA
BC003684
EMBL· GenBank· DDBJ
AAH03684.1
EMBL· GenBank· DDBJ
mRNA
BC010536
EMBL· GenBank· DDBJ
AAH10536.1
EMBL· GenBank· DDBJ
mRNA
AF124598
EMBL· GenBank· DDBJ
AAD31772.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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