Protein Domain : Arrestin-like, C-terminal IPR014752

Type	Homologous_superfamily
Description	Arrestins comprise a family of closely-related proteins. In addition to the inactivation of G protein-coupled receptors, arrestins have been implicated in the endocytosis of receptors and cross talk with other signalling pathways. S-Arrestin (retinal S-antigen) is a major protein of the retinal rod outer segments. It interacts with photo-activated phosphorylated rhodopsin, inhibiting or 'arresting' its ability to interact with transducin [ ]. Beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X) [], which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction [, , ]. The crystal structure of bovine retinal arrestin comprises two domains of antiparallel β-sheets connected through a hinge region and one short α-helix on the back of the amino-terminal fold []. This superfamily represents the C-terminal domain of arrestin, and Vacuolar protein sorting protein 26 (VPS26), consisting of an immunoglobulin-like β-sandwich structure.VPS26 assembles into a multimeric complex with other vacuolar protein sorting proteins (VPSs) and plays a role in vesicular protein sorting [ ].
Short Name	Arrestin-like_C