Function | Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), releasing various unsaturated fatty acids including oleoate, linoleoate, arachidonate, docosahexaenoate and lysophosphatidylethanolamines in preference to lysophosphatidylcholines. In response to high-fat diet, hydrolyzes minor lipoprotein phospholipids including phosphatidylserines, phosphatidylinositols and phosphatidylglycerols, altering lipoprotein composition and fat storage in adipose tissue and liver. May act in an autocrine and paracrine manner. Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria. Acts as a hair follicle phospholipase A2. Selectively releases lysophosphatidylethanolamines (LPE) and various unsaturated fatty acids in skin to regulate hair follicle homeostasis. May regulate the inflammatory response by releasing arachidonate, a precursor of prostaglandins and leukotrienes. Upon allergen exposure, may participate in allergic inflammatory response by enhancing leukotriene C4 synthesis and degranulation in mast cells. |
Protein Name | Group Iie Secretory Phospholipase A2Giie Spla2Spla2-IiePhosphatidylcholine 2-Acylhydrolase 2e |
Database Links | Reactome: R-HSA-1482788Reactome: R-HSA-1482801Reactome: R-HSA-1482839Reactome: R-HSA-1482922Reactome: R-HSA-1482925Reactome: R-HSA-1483166 |
Cellular Localisation | SecretedCytoplasmThrough Binding To Heparan Sulfate ProteoglycanMay Be Localized To Cytoplasmic Compartments Enriched In Anionic Phospholipids |
Alternative Antibody Names | Anti-Group Iie Secretory Phospholipase A2 antibodyAnti-Giie Spla2 antibodyAnti-Spla2-Iie antibodyAnti-Phosphatidylcholine 2-Acylhydrolase 2e antibodyAnti-PLA2G2E antibody |
Information sourced from Uniprot.org