SMART: Arrestin_C domain annotation

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):	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 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)].
Family alignment:	View or

There are 1068 Arrestin_C domains in 1050 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with Arrestin_C domain is also avaliable.

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Go to specific node: Anopheles gambiae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
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
- Display abstract
- 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
- Display abstract
- 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)

Links (links to other resources describing this domain)
PFAM Arrestin_C
INTERPRO IPR011022

PDB code	Main view	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

PFAM	Arrestin_C
INTERPRO	IPR011022

Arrestin_C

3D Structures of Arrestin_C domains in PDB