CAR protein is expressed in several tissues, including heart, brain, and, more generally, epithelial and endothelial cells.

The cytoplasmic tail of CAR contains the amino acids G S I V, which is characterized as a class 1 PDZ-binding motif for interacting with proteins containing PDZ domains.

[11] The protein is found to be expressed in various regions of the body including the heart, brain, and, more generally, epithelial and endothelial cells.

[15] Knocking out CAR is embryonic lethal in mice by day 11.5, coordinate with severe cardiac muscle abnormalities including left ventricular hyperplasia, sinuatrial valve abnormalities, pericardial edema, thoracic hemorrhaging, myocardial wall degeneration, regional apoptosis, reduced density and disorganization of myofibrils, and enlarged mitochondria.

[22] In patients with myocarditis or dilated cardiomyopathy, elevated Coxsackie B2 viral nucleic acids have been detected in myocardial biopsy samples.

[23] Adenoviral genomic DNA has also been detected in myocardial biopsies of patients with idiopathic cardiomyopathy, or impaired left ventricular function of unknown origin.

[24] Patients exhibiting sudden death from acute myocardial infarction had a higher proportion of active coxsackie B virus infection relative to matched controls, which was coordinate with disrupted sarcolemmal localization of dystrophin, suggesting that enteroviral infection may worsen the outcome of patients with acute myocardial infarction.

[25] A role for CAR in arrhythmia susceptibility and ventricular fibrillation after myocardial infarction was shown in that CXADR lies near the 21q21 locus, which is strongly associated with these insults.