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Beschreibung

Diacylglycerol kinase alpha (UniProt: P23743, also known as EC:2.7.1.107, DAG kinase alpha, 80 kDa diacylglycerol kinase, Diglyceride kinase alpha, DGK-alpha) is encoded by the DGKA (also known as DAGK, DAGK1) gene (Gene ID: 1606) in human. Diacylglycerol kinase is a lipid kinase that converts diacylglycerol to phosphatidic acid, and regulates the activity of many enzymes including protein kinase C, phosphatidylinositol 4-phosphate 5-kinase, and mTOR. Thus far ten mammalian subtypes of DAG kinase have been reported. All DAG kinase with the exception of beta isoform are localized in cytoplasm in several cells, but some translocate to the plasma membrane upon activation. DAG kinase acts as a modulator, which competes with protein kinase C for diacylglycerol in intracellular signaling pathways. DAG kinase also plays a role in the resynthesis of phosphatidylinositols and phosphorylating diacylglycerol to phosphatidic acid. Most DAG kinases, with the exception of theta, contain two cysteine-rich regions (C1A and C1B domains) in the regulatory domain of the N-terminal half of the molecule. In DAK kinase alpha the C1 domain closest to the catalytic domain has an extended region of fifteen amino acids that is not present in C1 domains of other DAG kinases. DAG kinase alpha can be activated by the phosphorylation of Tyr335, which occurs during T cell activation or following exposure of cells to hepatocyte growth factor.