The carboxyl-terminal anchorage domain of the turkey beta 1-adrenergic receptor is encoded by an alternatively spliced exon.

The originally described cDNA of the turkey beta 1-adrenergic receptor encodes a receptor with a carboxyl-terminal, 59-amino acid extension that was not found in several mammalian beta 1-adrenergic receptors. This extension blocks agonist-promoted endocytosis and down-regulation of the receptor. This carboxyl-terminal domain is encoded by an exon distinct from that which encodes the body of the receptor, and the originally described cDNA results from removal of an 849-nucleotide intron. Unspliced mRNA encodes a shorter open reading frame whose translated carboxyl terminus is identical with that of the mammalian beta 1-adrenergic receptors. There is no evidence for other introns in the coding region. Splicing of the intron to produce the non-endocytosing receptor is highest in fetal blood cells, is appreciable in adult brain and heart, and is detectable in other tissues. Thus, different tissues use alternative splicing to express beta-adrenergic receptors that either do or do not endocytose and down-regulate in response to agonist.