The function of ENSG00000130055 (GDPD2, glycerophosphodiester phosphodiesterase domain containing 2) is as follows. 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 (PubMed:28849762, PubMed:32629025, PubMed:32917725). 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 (PubMed:28849762). 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 (PubMed:35182431). 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 (PubMed:32629025, PubMed:32917725). 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). {ECO:0000250|UniProtKB:Q9ESM6, ECO:0000269|PubMed:28849762, ECO:0000269|PubMed:32629025, ECO:0000269|PubMed:32917725, ECO:0000269|PubMed:35182431}.