Phosphatidylinositol glycan anchor biosynthesis class V protein (PIGV)

Phosphatidylinositol glycan anchor biosynthesis class V protein (PIGV) is a mannosyltransferase enzyme localized in the endoplasmic reticulum. It catalyzes the transfer of the second mannose moiety onto a glycosylphosphatidylinositol (GPI) anchor precursor, a critical step during GPI anchor biosynthesis. GPI anchors are glycolipids that attach certain proteins to the cell membrane surface, especially on the extracellular face. Mutations in PIGV are causally linked to Mabry syndrome, a genetic disorder with intellectual disability, distinctive facial features, elevated blood alkaline phosphatase (hyperphosphatasia), and other systemic effects due to defective GPI-anchoring of proteins. The enzyme's activity is crucial for proper localization of many cell-surface proteins and the disruption of PIGV function mainly results in a loss of GPI-anchored proteins from the membrane, rather than being a current target for small molecule drugs or classic receptor blockade[1][2][3][4][7][9].

Other names

GPI mannosyltransferase 2GPI-MT-IIGPI mannosyltransferase IIdol-P-Man dependent GPI mannosyltransferase IIphosphatidylinositol glycan anchor biosynthesis, class VHPMRS1PIG-VFLJ20477PIGV_HUMAN