Cavia porcellus      (pS/pT)/Arrestin


※ Arrestin family introduction

    Arrestins comprise a family of four known members in mammals: two visual arrestins, 1 and 4, found in the rod and cone cells of the retina, and two nonvisual arrestins, 2 and 3, which are found in most other tissues of the body. The current model of arrestin-mediated interactions with ligand-occupied GPCRs holds that, after ligand occupancy, cytoplasmic regions of the receptor are phosphorylated at serine and threonine residues by a member of the family of G protein-coupled receptor kinases. Upon arrestin binding, these phosphorylated residues disrupt arrestin's polar core, inducing a conformational change within the molecule that allows it to interact further with the receptor. Recent study examined the interactions between members of the arrestin family with the phosphorylated carboxyl-terminal domain of the FPR using a bead-based, cell-free assay (1).

Reference
1. Potter, R.M. (2002) Arrestin variants display differential binding characteristics for the phosphorylated N-formyl peptide receptor carboxyl terminus . Curr Protein Pept Sci, 12, 3-11. PMID: 11777932


There are 4 genes.  Reviewed (0 or Unreviewed (4

No.StatusiEKPD IDEnsemble Gene IDUniProt AccessionGene Name
1
iEKPD-Cap-0651
ENSCPOG00000000209.4
A0A286XHI0
ARRB1
2
iEKPD-Cap-0652
ENSCPOG00000032406.1
A0A286Y5D3
ARRB2
3
iEKPD-Cap-0654
ENSCPOG00000002749.4
H0UZ97
ARRDC3
4
iEKPD-Cap-0653
ENSCPOG00000013680.4
A4L9L4
Sag; SAG