Phospholipase C Delta 1 (PLCd1)

By screening a human aortic smooth muscle cDNA library with a probe derived from a rat C6 glioma cell PLC-delta-1 cDNA, Cheng et al. (1995) cloned a PLCD1 cDNA. The deduced 756-amino acid protein shares 95% sequence homology with the rat protein. It contains a pleckstrin homology (PH) domain and the conserved X and Y domains of PLC proteins. It is distinguished from PLC-gamma by lack of the SH2 and SH3 domains that are essential for activation of PLC-gamma by tyrosine protein kinases, and from PLC-beta by lack of the C-terminal region of PLC-beta that is responsible for binding and activation by G proteins. Northern blot analysis detected ubiquitous expression of a 3.8-kb transcript, with highest expression in lung, heart, pancreas, skeletal muscle, and kidney.