PLA2G5

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2GHN

Identifiers

Aliases

PLA2G5, FRFB, GV-PLA2, PLA2-10, hVPLA(2), phospholipase A2 group V

External IDs

MGI: 101899 HomoloGene: 716 GeneCards: PLA2G5

Gene ontology
Molecular function	• calcium ion binding • heparin binding • calcium-dependent phospholipase A2 activity • metal ion binding • hydrolase activity • phospholipase A2 activity
Cellular component	• Golgi apparatus • plasma membrane • extracellular region • perinuclear region of cytoplasm
Biological process	• phosphatidic acid biosynthetic process • response to cytokine • phosphatidylserine acyl-chain remodeling • phosphatidylethanolamine acyl-chain remodeling • lipid metabolic process • platelet activating factor biosynthetic process • phosphatidylinositol acyl-chain remodeling • lipid catabolic process • positive regulation of phospholipase activity • phosphatidylglycerol acyl-chain remodeling • positive regulation of ERK1 and ERK2 cascade • phospholipid metabolic process • response to cAMP • leukotriene biosynthetic process • phosphatidylcholine acyl-chain remodeling • arachidonic acid secretion
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


5322


18784

Ensembl


ENSG00000127472


ENSMUSG00000041193

UniProt


P39877


P97391

RefSeq (mRNA)


NM_000929


NM_001122954 NM_011110

RefSeq (protein)


NP_000920.1


NP_001116426.1 NP_035240.3

Location (UCSC)

Chr 1: 20.03 – 20.09 Mb

Chr 4: 138.8 – 138.86 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Calcium-dependent phospholipase A2 is an enzyme that in humans is encoded by the PLA2G5 gene.^[3]^[4]^[5]

This gene is a member of the secretory phospholipase A2 family. It is located in a tightly-linked cluster of secretory phospholipase A2 genes on chromosome 1. The encoded enzyme catalyzes the hydrolysis of membrane phospholipids to generate lysophospholipids and free fatty acids including arachidonic acid. It preferentially hydrolyzes linoleoyl-containing phosphatidylcholine substrates. Secretion of this enzyme is thought to induce inflammatory responses in neighboring cells. Alternatively spliced transcript variants have been found, but their full-length nature has not been determined.^[5]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Tischfield JA, Xia YR, Shih DM, Klisak I, Chen J, Engle SJ, Siakotos AN, Winstead MV, Seilhamer JJ, Allamand V, Gyapay G, Lusis AJ (Feb 1997). "Low-molecular-weight, calcium-dependent phospholipase A2 genes are linked and map to homologous chromosome regions in mouse and human". Genomics. 32 (3): 328–33. doi:10.1006/geno.1996.0126. PMID 8838795.
↑ Chen J, Engle SJ, Seilhamer JJ, Tischfield JA (Mar 1994). "Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2". J Biol Chem. 269 (4): 2365–8. PMID 8300559.
1 2 "Entrez Gene: PLA2G5 phospholipase A2, group V".

Schröder HC, Perovic S, Kavsan V, et al. (1998). "Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death.". Neurotoxicology. 19 (4-5): 683–8. PMID 9745929.
Cho W (2001). "Structure, function, and regulation of group V phospholipase A(2).". Biochim. Biophys. Acta. 1488 (1-2): 48–58. doi:10.1016/s1388-1981(00)00109-8. PMID 11080676.
de Beer FC, Webb NR (2006). "Inflammation and atherosclerosis: Group IIa and Group V sPLA2 are not redundant.". Arterioscler. Thromb. Vasc. Biol. 26 (7): 1421–2. doi:10.1161/01.ATV.0000227561.89488.9a. PMID 16794232.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Mavoungou E, Georges-Courbot MC, Poaty-Mavoungou V, et al. (1997). "HIV and SIV envelope glycoproteins induce phospholipase A2 activation in human and macaque lymphocytes.". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 16 (1): 1–9. doi:10.1097/00042560-199709010-00001. PMID 9377118.
Chen Y, Dennis EA (1998). "Expression and characterization of human group V phospholipase A2.". Biochim. Biophys. Acta. 1394 (1): 57–64. doi:10.1016/s0005-2760(98)00098-8. PMID 9767110.
Bingham CO, Fijneman RJ, Friend DS, et al. (1999). "Low molecular weight group IIA and group V phospholipase A(2) enzymes have different intracellular locations in mouse bone marrow-derived mast cells.". J. Biol. Chem. 274 (44): 31476–84. doi:10.1074/jbc.274.44.31476. PMID 10531350.
Johansen B, Rakkestad K, Balboa MA, Dennis EA (2000). "Expression of cytosolic and secreted forms of phospholipase A(2) and cyclooxygenases in human placenta, fetal membranes, and chorionic cell lines.". Prostaglandins Other Lipid Mediat. 60 (4-6): 119–25. doi:10.1016/S0090-6980(99)00057-X. PMID 10751642.
Kim KP, Han SK, Hong M, Cho W (2000). "The molecular basis of phosphatidylcholine preference of human group-V phospholipase A2.". Biochem. J. 348. Pt 3 (3): 643–7. doi:10.1042/0264-6021:3480643. PMC 1221108. PMID 10839997.
Seeds MC, Jones KA, Duncan Hite R, et al. (2000). "Cell-specific expression of group X and group V secretory phospholipases A(2) in human lung airway epithelial cells.". Am. J. Respir. Cell Mol. Biol. 23 (1): 37–44. doi:10.1165/ajrcmb.23.1.4034. PMID 10873151.
Bernatchez PN, Winstead MV, Dennis EA, Sirois MG (2001). "VEGF stimulation of endothelial cell PAF synthesis is mediated by group V 14 kDa secretory phospholipase A2.". Br. J. Pharmacol. 134 (1): 197–205. doi:10.1038/sj.bjp.0704215. PMC 1572915. PMID 11522612.
Degousee N, Ghomashchi F, Stefanski E, et al. (2002). "Groups IV, V, and X phospholipases A2s in human neutrophils: role in eicosanoid production and gram-negative bacterial phospholipid hydrolysis.". J. Biol. Chem. 277 (7): 5061–73. doi:10.1074/jbc.M109083200. PMID 11741884.
Kim YJ, Kim KP, Han SK, et al. (2002). "Group V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2.". J. Biol. Chem. 277 (39): 36479–88. doi:10.1074/jbc.M205399200. PMID 12124392.
Hichami A, Joshi B, Simonin AM, Khan NA (2003). "Role of three isoforms of phospholipase A2 in capacitative calcium influx in human T-cells.". Eur. J. Biochem. 269 (22): 5557–63. doi:10.1046/j.1432-1033.2002.03261.x. PMID 12423354.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Muñoz NM, Kim YJ, Meliton AY, et al. (2003). "Human group V phospholipase A2 induces group IVA phospholipase A2-independent cysteinyl leukotriene synthesis in human eosinophils.". J. Biol. Chem. 278 (40): 38813–20. doi:10.1074/jbc.M302476200. PMID 12796497.

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PLA2G5

References

Further reading