Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:12200442, PubMed:23949095). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (Probable). By controlling the levels of diacylglycerol, regulates for instance the PKC and EGF receptor signaling pathways and plays a crucial role during development (By similarity). May also regulate clathrin-dependent endocytosis (PubMed:17880279). a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+) 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) Lipid metabolism; glycerolipid metabolism. Homooligomer (PubMed:12200442, PubMed:12084710). Monomer (PubMed:12084710). Interacts with AP2A2; regulates clathrin-dependent endocytosis (PubMed:17880279). Isoform 1 translocation from cytoplasm to the plasma membrane is induced by phorbol esters (PubMed:12200442). Phorbol esters induce the conversion into the monomeric form which can translocate to the plasma membrane (PubMed:12084710). Widely expressed. Only detected in ovary, and to a lesser extent in spleen. Up-regulated by phorbol esters and EGF. Down-regulated by phorbol esters. The SAM domain mediates homooligomerization. The PH domain mediates association with membranes. Phosphorylated (PubMed:12084710). Phosphorylation by PKC induced by phorbol esters prevents homooligomerization and promotes association with membranes (PubMed:12084710). Belongs to the eukaryotic diacylglycerol kinase family.