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Protein Domain : IPR017864

Name  Arrestin, conserved site Short Name  Arrestin_CS
Type  Conserved_site Description  G protein-coupled receptors are a large family of signalling molecules that respond to a wide variety of extracellular stimuli. The receptors relay the information encoded by the ligand through the activation of heterotrimeric G proteins and intracellular effector molecules. To ensure the appropriate regulation of the signalling cascade, it is vital to properly inactivate the receptor. This inactivation is achieved, in part, by the binding of a soluble protein, arrestin, which uncouples the receptor from the downstream G protein after the receptors are phosphorylated by G protein-coupled receptor kinases. In addition to the inactivation of G protein-coupled receptors, arrestins have also been implicated in the endocytosis of receptors and cross talk with other signalling pathways. 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 []. The protein binds calcium, and shows similarity in its C terminus to alpha-transducin and other purine nucleotide-binding proteins. In mammals, arrestin is associated with autoimmune uveitis.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) [], 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 beta-sheets connected through a hinge region and one short alpha-helix on the back of the amino-terminal fold []. The binding region for phosphorylated light-activated rhodopsin is located at the N-terminal domain, as indicated by the docking of the photoreceptor to the three-dimensional structure of arrestin.

Publication Counts Displayer

0 Child Features

0 Contains

1 Cross References

Source . Name

Subject . Primary Identifier
PS00295 PROSITE IPR017864

2 Data Sets

Name URL
TrEMBL data set
InterPro data set  

4 Found In

DB identifier Name Short Name Type
IPR014756 Immunoglobulin E-set Ig_E-set Domain
IPR000698 Arrestin Arrestin Family
IPR011021 Arrestin-like, N-terminal Arrestin-like_N Domain
IPR014753 Arrestin, N-terminal Arrestin_N Domain

0 GO Annotation

0 Ontology Annotations

0 Parent Features

23 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0080583 P15372 Drosophila melanogaster
FBpp0076326 P19107 Drosophila melanogaster
FBpp0085236 Q9V393 Drosophila melanogaster
FBpp0278984 Q29LC9 Drosophila pseudoobscura
FBpp0281954 Q298D4 Drosophila pseudoobscura
FBpp0287160 Q29D09 Drosophila pseudoobscura
FBpp0161631 B4KZ69 Drosophila mojavensis
FBpp0167154 B4KEG0 Drosophila mojavensis
FBpp0172012 B4K866 Drosophila mojavensis
FBpp0226724 B4LEM0 Drosophila virilis
FBpp0232126 B4LSW4 Drosophila virilis
FBpp0237215 B4LY88 Drosophila virilis
FBpp0257819 B4P8N4 Drosophila yakuba
FBpp0268299 B4PP42 Drosophila yakuba
A8X5S0_CAEBR A8X5S0 Caenorhabditis briggsae
K7GVG4_CAEJA K7GVG4 Caenorhabditis japonica
K7GVG3_CAEJA K7GVG3 Caenorhabditis japonica
G0N7N0_CAEBE G0N7N0 Caenorhabditis brenneri
ARRB_CAEEL P51485 Caenorhabditis elegans
Q5BIJ0_DROME Q5BIJ0 Drosophila melanogaster
Q29QY4_DROME Q29QY4 Drosophila melanogaster
B4PFK8_DROYA B4PFK8 Drosophila yakuba
E3MA36_CAERE E3MA36 Caenorhabditis remanei