Arrestin C-terminal-like domain (IPR011022)

Short name: Arrestin_C-like

Overlapping homologous superfamilies


Domain relationships



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 [PMID: 15335861]. 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) [PMID: 7720881], 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 [PMID: 8452755, PMID: 1517224, PMID: 2158671]. The crystal structure of bovine retinal arrestin comprises two domains of antiparallel beta-sheets connected through a hinge region and one short alpha-helix on the back of the amino-terminal fold [PMID: 9495348].

This C-terminal domain consists of an immunoglobulin-like beta-sandwich structure. This domain is found in arrestins and in other proteins including arrestin domain-containing proteins, protein ROD1 [PMID: 8621680] and ROG3 [PMID: 12163175] and thioredoxin-interacting protein [PMID: 17603038].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.