PLA2G10

Phospholipase A2, group X
PDB rendering based on 1le6.
Available structures PDB 1LE6, 1LE7
Identifiers
Symbols	PLA2G10; GXPLA2; GXSPLA2; MGC119918; MGC119919; MGC133367; SPLA2
External IDs	OMIM: 603603 MGI: 1347522 HomoloGene: 2636 GeneCards: PLA2G10 Gene
EC number	3.1.1.4
Gene Ontology Molecular function • phospholipase activity • phospholipase A2 activity • calcium ion binding • hydrolase activity Cellular component • extracellular region Biological process • phospholipid metabolic process • axon guidance • positive regulation of macrophage derived foam cell differentiation • positive regulation of lipid storage • lipid catabolic process • arachidonic acid metabolic process • positive regulation of cellular protein metabolic process • positive regulation of prostaglandin secretion • cholesterol homeostasis • regulation of macrophage activation • negative regulation of sequence-specific DNA binding transcription factor activity • lysophospholipid transport • positive regulation of arachidonic acid secretion • negative regulation of cholesterol efflux Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8399	26565
Ensembl	ENSG00000069764	ENSMUSG00000022683
UniProt	O15496	Q8C5Y6
RefSeq (mRNA)	NM_003561	NM_011987.2
RefSeq (protein)	NP_003552	NP_036117.1
Location (UCSC)	Chr 16: 14.77 – 14.83 Mb	Chr 16: 13.72 – 13.73 Mb
PubMed search	[1]	[2]

Group 10 secretory phospholipase A2 is an enzyme that in humans is encoded by the PLA2G10 gene.

Further reading

• 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. 
• Sartipy P, Camejo G, Svensson L, Hurt-Camejo E (2003). "Phospholipase A2 modification of lipoproteins: potential effects on atherogenesis.". Adv. Exp. Med. Biol. 507: 3–7. PMID 12664556. 
• Murakami M, Kudo I (2004). "New phospholipase A(2) isozymes with a potential role in atherosclerosis.". Curr. Opin. Lipidol. 14 (5): 431–6. doi:10.1097/01.mol.0000092629.86399.d6. PMID 14501581. 
• Lennon G, Auffray C, Polymeropoulos M, Soares MB (1996). "The I.M.A.G.E. Consortium: an integrated molecular analysis of genomes and their expression.". Genomics 33 (1): 151–2. doi:10.1006/geno.1996.0177. PMID 8617505. 
• 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. 
• Yokota Y, Higashino K, Nakano K, et al. (2000). "Identification of group X secretory phospholipase A(2) as a natural ligand for mouse phospholipase A(2) receptor.". FEBS Lett. 478 (1-2): 187–91. doi:10.1016/S0014-5793(00)01848-2. PMID 10922494. 
• Morioka Y, Saiga A, Yokota Y, et al. (2000). "Mouse group X secretory phospholipase A2 induces a potent release of arachidonic acid from spleen cells and acts as a ligand for the phospholipase A2 receptor.". Arch. Biochem. Biophys. 381 (1): 31–42. doi:10.1006/abbi.2000.1977. PMID 11019817. 
• 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. 
• Hanasaki K, Yamada K, Yamamoto S, et al. (2002). "Potent modification of low density lipoprotein by group X secretory phospholipase A2 is linked to macrophage foam cell formation.". J. Biol. Chem. 277 (32): 29116–24. doi:10.1074/jbc.M202867200. PMID 12021277. 
• Osterström A, Dimberg J, Fransén K, Söderkvist P (2002). "Expression of cytosolic and group X secretory phospholipase A(2) genes in human colorectal adenocarcinomas.". Cancer Lett. 182 (2): 175–82. doi:10.1016/S0304-3835(02)00081-2. PMID 12048163. 
• Pan YH, Yu BZ, Singer AG, et al. (2002). "Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes.". J. Biol. Chem. 277 (32): 29086–93. doi:10.1074/jbc.M202531200. PMID 12161451. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Wooton-Kee CR, Boyanovsky BB, Nasser MS, et al. (2004). "Group V sPLA2 hydrolysis of low-density lipoprotein results in spontaneous particle aggregation and promotes macrophage foam cell formation.". Arterioscler. Thromb. Vasc. Biol. 24 (4): 762–7. doi:10.1161/01.ATV.0000122363.02961.c1. PMID 14962950. 
• Mounier CM, Ghomashchi F, Lindsay MR, et al. (2004). "Arachidonic acid release from mammalian cells transfected with human groups IIA and X secreted phospholipase A(2) occurs predominantly during the secretory process and with the involvement of cytosolic phospholipase A(2)-alpha.". J. Biol. Chem. 279 (24): 25024–38. doi:10.1074/jbc.M313019200. PMID 15007070. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Masuda S, Murakami M, Takanezawa Y, et al. (2005). "Neuronal expression and neuritogenic action of group X secreted phospholipase A2.". J. Biol. Chem. 280 (24): 23203–14. doi:10.1074/jbc.M500985200. PMID 15781456.