SMART: Pfam domain Arrestin

The domain within your query sequence starts at position 125 and ends at position 210; the E-value for the Arrestin_C domain shown below is 1.6e-8.

KTGNVVLTASTDLRGYVVGQVLRLQADIENQSGKDTSPVVASLLQKVSYKAKRWIYDVRT
IAEVEGTGVKAWRRAQWQEQILVPAL

Arrestin_C

PFAM accession number:	PF02752
Interpro abstract (IPR011022):	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 [ (PUBMED:8621680) ] and ROG3 [ (PUBMED:12163175) ] and thioredoxin-interacting protein [ (PUBMED:17603038) ]. 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 [ (PUBMED: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) [ (PUBMED: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 [ (PUBMED:8452755) (PUBMED:1517224) (PUBMED: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 [ (PUBMED:9495348) ].

PFAM accession number:

PF02752

Interpro abstract (IPR011022):

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 [ (PUBMED:8621680) ] and ROG3 [ (PUBMED:12163175) ] and thioredoxin-interacting protein [ (PUBMED:17603038) ].

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 [ (PUBMED: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) [ (PUBMED: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 [ (PUBMED:8452755) (PUBMED:1517224) (PUBMED: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 [ (PUBMED:9495348) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Arrestin_C