Phospholipase D family (IPR015679)

Short name: PLipase_D_fam

Overlapping homologous superfamilies


Family relationships


Phospholipase D (PLD) catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free head group. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals [PMID: 15052340]. In higher organisms, PLD specifically catalyzes the hydrolysis of phosphatidylcholine (PC) to phosphatidic acid (PA) and choline and is activated in response to stimulators of vesicle transport, endocytosis, exocytosis, cell migration, and mitosis.

There are two mammalian phospholipase D genes whose products (PLD1 and PLD2) are alternatively spliced. Both forms have two highly conserved HKD motifs that are essential for catalysis and dimerisation [PMID: 10818442]. It has now been observed that there are abnormalities in PLD expression and activity in many human cancers [PMID: 14517341].

Most bacteria use an enzyme belonging to the phospholipase D family as cardiolipin synthase. In contrast, eukaryotes and most actinobacteria use a cardiolipin synthase of the CDP-alcohol phosphatidyltransferase family [PMID: 19439403].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.