having a novel domain, proline rich and containing a PEST sequence characteristic of proteins that are rapidly degraded by the calpain family of proteases
catalyze the hydrolysis of the D-4 position phosphoester of the PI3K generated lipid second messenger, phosphatidylinositol 3,4-bisphosphate (Shearn 2001)
generates and terminates phosphoinositide 3-kinase signals at distinct subcellular locations (Ivetac 2005)