Search Results
Overview
| Uniprot ID | P14555 |
|---|---|
| Protein Name | Phospholipase A2, membrane associated |
| Gene Name | PLA2G2A |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 112 | SQLCECDKAAATCFA |
| 30 | VNFHRMIKLTTGKEA |
| 35 | MIKLTTGKEAALSYG |
| 57 | VGGRGSPKDATDRCC |
Function
Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration (PubMed:10455175, PubMed:10681567, PubMed:2925633). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (PubMed:10455175, PubMed:10681567). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (PubMed:10358193, PubMed:11694541). Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response (PubMed:25082876). Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (PubMed:14998370). Independent of its catalytic activity, acts as a ligand for integrins (PubMed:18635536, PubMed:25398877). Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 (PubMed:18635536, PubMed:25398877). Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:25398877). Induces cell proliferation in an integrin-dependent manner (PubMed:18635536)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005741 | mitochondrial outer membrane |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0030141 | secretory granule |
| Molecular Function | GO:0004623 | A2-type glycerophospholipase activity |
| Molecular Function | GO:0005509 | calcium ion binding |
| Molecular Function | GO:0005543 | phospholipid binding |
| Biological Process | GO:0038166 | angiotensin-activated signaling pathway |
| Biological Process | GO:0050482 | arachidonate secretion |
| Biological Process | GO:0050830 | defense response to Gram-positive bacterium |
| Biological Process | GO:0006954 | inflammatory response |
| Biological Process | GO:0036335 | intestinal stem cell homeostasis |
| Biological Process | GO:0031640 | killing of cells of another organism |
| Biological Process | GO:0016042 | lipid catabolic process |
| Biological Process | GO:0034374 | low-density lipoprotein particle remodeling |
| Biological Process | GO:0042130 | negative regulation of T cell proliferation |
| Biological Process | GO:0046473 | phosphatidic acid metabolic process |
| Biological Process | GO:0046470 | phosphatidylcholine metabolic process |
| Biological Process | GO:0046337 | phosphatidylethanolamine metabolic process |
| Biological Process | GO:0046471 | phosphatidylglycerol metabolic process |
| Biological Process | GO:0006644 | phospholipid metabolic process |
| Biological Process | GO:0070374 | positive regulation of ERK1 and ERK2 cascade |
| Biological Process | GO:0050729 | positive regulation of inflammatory response |
| Biological Process | GO:0010744 | positive regulation of macrophage derived foam cell differentiation |
| Biological Process | GO:1902563 | regulation of neutrophil activation |
Reference
[1] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[2] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.