4.6.1.14	malfunction	loss of GPI-phospholipase C polypeptide is associated with sustained replication of nascent procyclics	
4.6.1.14	physiological function	in monomorphic ILTat 1.3 strain, total GPI-phospholipase C polypeptide enzyme activity (per cell) remains constant for 72 h after initiation of transformation. GPI-phospholipase C polypeptide remains in AnTat 1.1 through differentiation, when variant surface glycoprotein is lost and procyclin is expressed on the cell surface	
4.6.1.14	physiological function	glycosylphosphatidylinositol-specific phospholipase D (GPI-PLD) specifically cleaves glycosylphosphatidylinositol-anchored proteins from cell membranes. Reduction of GPI-anchored proteins on cell membranes by over expression of GPI-PLD results in significant inhibition of intracellular Ca2+ mobilization and ERK1/2 phosphorylation in response to oscillatory fluid flow	
4.6.1.14	physiological function	glycosylphosphatidylinositol phospholipase C is a virulence factor that releases variant surface glycoprotein from dying cells	
4.6.1.14	physiological function	GDE3 cleaves and releases urokinase receptor from its glycosylphosphatidylinositol-anchor with consequent loss of function. GDE3 overexpression depletes urokinase receptor uPAR from distinct basolateral membrane domains in breast cancer cells, resulting in a less transformed phenotype, it slows tumor growth in a xenograft model and correlates with prolonged survival in patients