| Primary Identifier | IPR000848 | Type | Domain |
| Short Name | GPCR_cAMP |
| description | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].It has been suggested that the cAMP receptors coordinate aggregation ofindividual cells into a multicellular organism, and regulate the expressionof a large number of developmentally-regulated genes [, , ]. The amino acidsequences of the receptors contain high proportions of hydrophobic residuesgrouped into 7 domains, in a manner reminiscent of the rhodopsins and otherreceptors believed to interact with G-proteins. However, while a similar3D framework has been proposed to account for this, there is no significantsequence similarity between these families: the cAMP receptors thus beartheir own unique '7TM' signature. |
