The domain within your query sequence starts at position 3 and ends at position 58; the E-value for the Arrestin_C domain shown below is 5e-21.

RVQLFEIRLSQGRVVYGPGEPLAGTVHLRLGAPLPFRGSLPAGEHNFPFQFLLPGS

The domain was found using the schnipsel database

Arrestin_C

Arrestin (or S-antigen), C-terminal domain

• SMART accession number: SM01017
• Description: Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes 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).
• 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) ].

There are 9903 Arrestin_C domains in 9566 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Cellular role: signalling

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Hirsch JA, Schubert C, Gurevich VV, Sigler PB
• The 2.8 A crystal structure of visual arrestin: a model for arrestin'sregulation.
• Cell. 1999; 97: 257-69

G protein-coupled signaling is utilized by a wide variety of eukaryotesfor communicating information from the extracellular environment. Signaltermination is achieved by the action of the arrestins, which bind toactivated, phosphorylated G protein-coupled receptors. We describe herecrystallographic studies of visual arrestin in its basal conformation. Thesalient features of the structure are a bipartite molecule with an unusualpolar core. This core is stabilized in part by an extendedcarboxy-terminal tail that locks the molecule into an inactive state. Inaddition, arrestin is found to be a dimer of two asymmetric molecules,suggesting an intrinsic conformational plasticity. In conjunction withbiochemical and mutagenesis data, we propose a molecular mechanism bywhich arrestin is activated for receptor binding.

• Palczewski K
• Structure and functions of arrestins.
• Protein Sci. 1994; 3: 1355-61

Transmembrane signal transductions in a variety of cell types that mediatesignals as diverse as those carried by neurotransmitters, hormones, andsensory signals share basic biochemical mechanisms that include: (1) anextracellular perturbation (neurotransmitter, hormone, odor, light); (2)specific receptors; (3) coupling proteins, such as G proteins; and (4)effector enzymes or ion channels. Parallel to these amplificationreactions, receptors are precisely inactivated by mechanisms that involveprotein kinases and regulatory proteins called arrestins. The structureand functions of arrestins are the focus of this review.

Structure (3D structures containing this domain)

3D Structures of Arrestin_C domains in PDB

PDB code	Title
1ayr	ARRESTIN FROM BOVINE ROD OUTER SEGMENTS
1cf1	ARRESTIN FROM BOVINE ROD OUTER SEGMENTS
1g4m	CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1
1g4r	CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1
1jsy	Crystal structure of bovine arrestin-2
1suj	X-ray crystal structure of ambystoma tigrinum cone arrestin
1zsh	Crystal structure of bovine arrestin-2 in complex with inositol hexakisphosphate (IP6)
2wtr	Full length Arrestin2
3gc3	Crystal Structure of Arrestin2S and Clathrin
3gd1	Structure of an Arrestin/Clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking
3p2d	Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes
3ugu	Crystal Structure of p44 (Splice Variant of Visual Arrestin)
3ugx	Crystal Structure of Visual Arrestin
4j2q	Crystal structure of C-terminally truncated arrestin reveals mechanism of arrestin activation
4jqi	Structure of active beta-arrestin1 bound to a G protein-coupled receptor phosphopeptide
4ll1	The structure of the TRX and TXNIP complex
4ll4	The structure of the TRX and TXNIP complex
4zrg	4ZRG
4zwj	4ZWJ
5dgy	5DGY

Links (links to other resources describing this domain)

• PFAM: Arrestin_C
• INTERPRO: IPR011022