Coxsackie virus and adenovirus receptor

Coxsackie virus and adenovirus receptor

PDB rendering based on 1eaj.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsCXADR ; CAR; CAR4/6; HCAR
External IDsOMIM: 602621 MGI: 1201679 HomoloGene: 1024 GeneCards: CXADR Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez152513052
EnsemblENSG00000154639ENSMUSG00000022865
UniProtP78310P97792
RefSeq (mRNA)NM_001207063NM_001025192
RefSeq (protein)NP_001193992NP_001020363
Location (UCSC)Chr 21:
18.88 – 18.97 Mb		Chr 16:
78.3 – 78.36 Mb
PubMed search

Coxsackievirus and adenovirus receptor (CAR) is a protein that in humans is encoded by the CXADR gene.[1][2][3] The protein encoded by this gene is a type I membrane receptor for group B coxsackie viruses and subgroup C adenoviruses. The human CAR gene (CXADR) is found on chromosome 21. Alternative splicing is known to produce at least 2 splice variants known as hCAR1 and hCAR2 and are each composed of at least 7 exons. Pseudogenes of this gene are found on chromosomes 15, 18, and 21.[3]

Structure

CAR is a transmembrane bound protein with two Ig-like extracellular domains, a transmembrane domain, and a cytoplasmic domain. The N-terminal segment comprises the two extracellular domains (D1 and D2). D1 is most distal from the membrane and contains a V/Ig-like fold whereas D2 is more proximal and

Expression

The protein is found to be expressed in various regions of the body including the heart, brain, and, more generally, epithelial and endothial cells. Moreover, CAR expression is not found in normal or tumour cell lines. Expression of CAR in endothial cells can be regulated by treatment with drugs. [4] [5]

Function

CAR is strongly expressed in the developing central nervous system where it is thought to mediate neurite outgrowth. In contrast,expression of CAR is undetectable in the adult nervous system. It functions as a homophilic and heterophilic cell adhesion molecule through its interactions with extracellular matrix glycoproteins such as: fibronectin, agrin, laminin-1 and tenascin-R.[6] In addition, it is thought to regulate the cytoskeleton through interactions with actin and microtubules. Moreover, its cytoplasmic domain contains putative phosphorylation sites and a PDZ-interaction motif which suggests a scaffolding role.

References

  1. ↑ Bergelson JM, Cunningham JA, Droguett G, Kurt-Jones EA, Krithivas A, Hong JS, Horwitz MS, Crowell RL, Finberg RW (Mar 1997). "Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5". Science 275 (5304): 1320–3. doi:10.1126/science.275.5304.1320. PMID 9036860.
  2. ↑ Tomko RP, Xu R, Philipson L (May 1997). "HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses". Proc Natl Acad Sci U S A 94 (7): 3352–6. doi:10.1073/pnas.94.7.3352. PMC 20373. PMID 9096397.
  3. ↑ 3.0 3.1 "Entrez Gene: CXADR coxsackie virus and adenovirus receptor".
  4. ↑ Funke C, Farr M, Werner B, Dittmann S, Uberla K, Piper C, Niehaus K, Horstkotte D (Apr 2010). "Antiviral effect of Bosentan and Valsartan during coxsackievirus B3 infection of human endothelial cells.". Journal of General Virology 91 (8): 1959–1570. doi:10.1099/vir.0.020065-0. PMID 20392896.
  5. ↑ Werner B, Dittmann S, Funke C, Überla K, Piper C, Niehaus K, Horstkotte D, Farr M. (Dec 2013). "Effect of lovastatin on coxsackievirus B3 infection in human endothelial cells.". Inflammation Research 63 (4): 267–276. doi:10.1007/s00011-013-0695-z. PMID 24316867.
  6. ↑ Patzke C, Max KE, Behlke J, Schreiber J, Schmidt H, Dorner AA, Kröger S, Henning M, Otto A, Heinemann U, Rathjen FG (Feb 2010). "The Coxsackievirus-Adenovirus Receptor reveals complex homophilic and heterophilic interactions on neural cells". Journal of Neuroscience 30 (8): 2897–2910. doi:10.1523/JNEUROSCI.5725-09.2010. PMID 20181587.

Further reading