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
- GVI PLA2 3 4
- CaI-PLA2 3 4
- PNPLA9 3 4
- 85 KDa Calcium-Independent Phospholipase A2 3
- Group VI Phospholipase A2 4
- EC 126.96.36.199 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 Infantile Neuroaxonal Dystrophy 1. Among its related pathways are Golgi-to-ER retrograde transport and Regulation of actin dynamics for phagocytic cup formation. 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.