Aliases for PLA2G6 Gene
- Phospholipase A2 Group VI 2 3 5
- Intracellular Membrane-Associated Calcium-Independent Phospholipase A2 Beta 3 4
- Phospholipase A2, Group VI (Cytosolic, Calcium-Independent) 2 3
- Patatin-Like Phospholipase Domain-Containing Protein 9 3 4
- Neurodegeneration With Brain Iron Accumulation 2 2 3
- IPLA2-Beta 3 4
- CaI-PLA2 3 4
- GVI PLA2 3 4
- PNPLA9 3 4
- 85/88 KDa Calcium-Independent Phospholipase A2 3
- 85 KDa Calcium-Independent Phospholipase A2 3
- Group VI Phospholipase A2 4
- EC 184.108.40.206 4
External Ids for PLA2G6 Gene
Previous GeneCards Identifiers for PLA2G6 Gene
The protein encoded by this gene is an A2 phospholipase, a class of enzyme that catalyzes the release of fatty acids from phospholipids. The encoded protein may play a role in phospholipid remodelling, arachidonic acid release, leukotriene and prostaglandin synthesis, fas-mediated apoptosis, and transmembrane ion flux in glucose-stimulated B-cells. Several transcript variants encoding multiple isoforms have been described, but the full-length nature of only three of them have been determined to date. [provided by RefSeq, Dec 2010]
GeneCards Summary for PLA2G6 Gene
PLA2G6 (Phospholipase A2 Group VI) is a Protein Coding gene. Diseases associated with PLA2G6 include Parkinson Disease 14, Autosomal Recessive and Neurodegeneration With Brain Iron Accumulation 2A. Among its related pathways are Metabolism and Ras signaling pathway. Gene Ontology (GO) annotations related to this gene include calmodulin binding and ATP-dependent protein binding. An important paralog of this gene is PNPLA8.
UniProtKB/Swiss-Prot for PLA2G6 Gene
Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods.
Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.
Phospholipases are a group of enzymes that hydrolyze phospholipids into fatty acids and other lipophilic molecules. There are four major classes; phospholipase A, phospholipase B, phosphoinositide-specific phospholipase C and phospholipase D.