GPLD1 hydrolyses GPI-anchors from proteins

Stable Identifier
Reaction [transition]
Homo sapiens
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Some proteins function at the cell's surface, attached to the plasma membrane via GPI (glycosylphosphatidylinositol) anchors and include enzymes, receptors, cell adhesion molecules and antigens. These GPI-anchored proteins participate in many important cellular functions including immune recognition, complement regulation and intracellular signaling. Phosphatidylinositol-glycan-specific phospholipase D (GPLD1) (Schofield et al. 2000) is a secreted protein that specifically cleaves GPI-anchored proteins by cleaving the linkage between the phosphate and inositol in GPI (Davitz et al. 1987, Low & Prasad 1988). In addition, it also localises to the ER where it can cleave GPI anchor intermediates transiting to the plasma membrane (not shown here). GPLD1 may play a role in the regulation of GPI-anchored proteins on (intra)cellular membranes.
Literature References
PubMed ID Title Journal Year
11072085 Structure and expression of the human glycosylphosphatidylinositol phospholipase D1 (GPLD1) gene

Schofield, JN, Rademacher, TW

Biochim. Biophys. Acta 2000
2443973 A glycan-phosphatidylinositol-specific phospholipase D in human serum

Nussenzweig, V, Englund, PT, Shak, S, Davitz, MA, Krakow, J, Hereld, D

Science 1987
3422494 A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma

Prasad, AR, Low, MG

Proc. Natl. Acad. Sci. U.S.A. 1988
Catalyst Activity

glycosylphosphatidylinositol phospholipase D activity of GPLD1 [extracellular region]

Orthologous Events
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