PLA2G10

PLA2G10
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1LE6, 1LE7, 4UY1
Identifiers
Aliases	PLA2G10, GXPLA2, GXSPLA2, SPLA2, sPLA2-X, phospholipase A2 group X
External IDs	OMIM: 603603 MGI: 1347522 HomoloGene: 2636 GeneCards: PLA2G10
Gene location (Human)
Chr.	Chromosome 16 (human)[1]
End	14,694,669 bp[1]
Gene location (Mouse)
Chr.	Chromosome 16 (mouse)[2]
End	13,730,983 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• calcium ion binding; • phospholipase A2 activity; • phospholipase activity; • metal ion binding; • hydrolase activity; • phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); • phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); • phospholipid binding; • calcium-dependent phospholipase A2 activity;
Cellular component	• extracellular region; • extracellular;
Biological process	• phosphatidic acid biosynthetic process; • positive regulation of cellular protein metabolic process; • phosphatidylserine acyl-chain remodeling; • phosphatidylethanolamine acyl-chain remodeling; • lysophospholipid transport; • lipid metabolism; • positive regulation of lipid storage; • phosphatidylinositol acyl-chain remodeling; • negative regulation of sequence-specific DNA binding transcription factor activity; • axon guidance; • lipid catabolic process; • positive regulation of prostaglandin secretion; • positive regulation of macrophage derived foam cell differentiation; • positive regulation of arachidonic acid secretion; • phosphatidylglycerol acyl-chain remodeling; • negative regulation of cholesterol efflux; • cholesterol homeostasis; • arachidonic acid metabolic process; • phosphatidylcholine acyl-chain remodeling; • regulation of macrophage activation; • phospholipid metabolic process; • arachidonic acid secretion; • cellular response to leukemia inhibitory factor;
	Sources:Amigo / QuickGO
Orthologs
	8399
	26565
	ENSG00000276870; ENSG00000069764
	ENSMUSG00000022683
	O15496
	Q9QXX3
	NM_003561
	NM_001291009; NM_011987
	NP_003552
	NP_001277938; NP_036117
	Wikidata
View/Edit Human	View/Edit Mouse

Group 10 secretory phospholipase A2 is an enzyme that in humans is encoded by the PLA2G10 gene.[5][6]

References

ENSG00000069764 GRCh38: Ensembl release 89: ENSG00000276870, ENSG00000069764 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000022683 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G (Jul 1997). "Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2". J Biol Chem. 272 (25): 15745–52. doi:10.1074/jbc.272.25.15745. PMID 9188469.
"Entrez Gene: PLA2G10 phospholipase A2, group X".

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. Advances in Experimental Medicine and Biology. 507. pp. 3–7. doi:10.1007/978-1-4615-0193-0_1. ISBN 978-1-4613-4960-0. 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:10.1097/00041433-200310000-00003. 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.
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" (PDF). 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.
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.

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[refGRCh38Ensembl-1] ENSG00000069764 GRCh38: Ensembl release 89: ENSG00000276870, ENSG00000069764 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000022683 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9188469-5] Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G (Jul 1997). "Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2". J Biol Chem. 272 (25): 15745–52. doi:10.1074/jbc.272.25.15745. PMID 9188469.

[entrez-6] "Entrez Gene: PLA2G10 phospholipase A2, group X".

PLA2G10

References

Further reading