serine/threonine protein phosphatase 2A regulatory subunit B" subunit alpha
Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This group contains protein phosphatase subunit PR130 (also known as protein phosphatase 2A regulatory subunit B'' subunit alpha, PR72, or PPP2R3) that is encoded by the PPP2R3A gene. PR130 and PR72 subunits are derived from the same gene through differential splicing; they harbor specific N-terminal domains of different lengths that are encoded by alternatively spliced exons and have identical C-termini. The common C-terminus contains a two-domain elongated structure with two calcium EF-hands which mediate Ca2+-dependent changes in phosphatase activity. The PR130 subunit has been shown to interact with the LIM domain of lipoma-preferred partner (LPP) through a conserved Zn2+-finger-like motif in the N-terminus of PR130.