GDPD2

Calcium-dependent ecto-phospholipase C that cleaves the phosphodiester bond between the glycerol backbone and phosphate group of glycerophospholipids at the cell surface, regulating multiple signaling pathways. Substrates include GPI-anchored proteins, which are released from the membrane upon cleavage of the inositol-phosphate linkage. For example, cleavage and release of UPAR/PLAUR regulates cell-matrix adhesion and extracellular matrix remodeling. Also cleaves the glycosylphosphatidylinositol (GPI) anchor of metalloproteases TRABD2A and TRABD2B, releasing them from the plasma membrane. This release modulates their regulation of Wnt signaling. Also hydrolyzes lysophosphatidylinositol (LPI) to monoacylglycerol and inositol-1-phosphate. Converts 2-arachidonoyl-LPI, the endogenous GPR55 agonist, into 2-arachidonoylglycerol (2-AG), an endocannabinoid that activates CNR1/CNR2. Thereby, acts as a switch redirecting signaling from GPR55 to CNR1/CNR2 within the endocannabinoid system that could alternatively regulate osteoblast proliferation and differentiation. Can also cleave glycerophosphoinositol to glycerol and inositol-1-phosphate in vitro (By similarity). May also play a role in remodeling of the actin cytoskeleton (By similarity)..

Function from UniProtKB (Q9HCC8), read 2026-09-23. CC BY 4.0.