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Identification
HMDB Protein ID HMDBP00060
Secondary Accession Numbers
  • 5289
  • HMDBP07224
Name Cytosolic phospholipase A2
Synonyms
  1. Lysophospholipase
  2. Phosphatidylcholine 2-acylhydrolase
  3. Phospholipase A2
  4. Phospholipase A2 group IVA
  5. cPLA2
Gene Name PLA2G4A
Protein Type Unknown
Biological Properties
General Function Involved in metabolic process
Specific Function Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.
Pathways
  • alpha-Linolenic acid metabolism
  • Arachidonic acid metabolism
  • Ether lipid metabolism
  • Fc Epsilon Receptor I Signaling in Mast Cells
  • Fc epsilon RI signaling pathway
  • Fc gamma R-mediated phagocytosis
  • Glutamatergic synapse
  • Glycerophospholipid metabolism
  • GnRH signaling pathway
  • Linoleic acid metabolism
  • Long-term depression
  • MAPK signaling pathway
  • Serotonergic synapse
  • Vascular smooth muscle contraction
  • VEGF signaling pathway
Reactions
Phosphatidylcholine + Water → 1-acylglycerophosphocholine + a carboxylate details
2-lysophosphatidylcholine + Water → Glycerophosphocholine + a carboxylate details
Phosphatidylcholine + Water → 1-Acyl-sn-glycero-3-phosphocholine + Fatty acid details
Phosphatidylcholine + Water → 1-Acyl-sn-glycero-3-phosphocholine + Arachidonic acid details
Phosphatidylethanolamine + Water → 1-Acyl-sn-glycero-3-phosphoethanolamine + Fatty acid details
Phosphatidylcholine + Water → 1-Acyl-sn-glycero-3-phosphocholine + Linoleic acid details
O-1-Alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + Water → 1-(1-Alkenyl)-sn-glycero-3-phosphoethanolamine + Carboxylate details
1-Radyl-2-acyl-sn-glycero-3-phosphocholine + Water → 1-Organyl-2-lyso-sn-glycero-3-phosphocholine + Carboxylate details
Phosphatidylcholine + Water → 1-Acyl-sn-glycero-3-phosphocholine + alpha-Linolenic acid details
GO Classification
Biological Process
phosphatidylcholine acyl-chain remodeling
phosphatidylethanolamine acyl-chain remodeling
phosphatidylinositol acyl-chain remodeling
positive regulation of bone mineralization
phosphatidylserine acyl-chain remodeling
positive regulation of apoptotic process
platelet activation
positive regulation of cell proliferation
response to heat
response to organic nitrogen
cellular response to antibiotic
response to lipopolysaccharide
response to calcium ion
phospholipid catabolic process
cardiolipin acyl-chain remodeling
arachidonic acid secretion
icosanoid biosynthetic process
icosanoid metabolic process
luteolysis
positive regulation of fever generation
positive regulation of prostaglandin biosynthetic process
positive regulation of vesicle fusion
surfactant homeostasis
response to glucocorticoid stimulus
decidualization
response to vitamin D
arachidonic acid metabolic process
phosphatidic acid biosynthetic process
platelet activating factor biosynthetic process
aging
ovulation from ovarian follicle
phosphatidylglycerol acyl-chain remodeling
response to hydrogen peroxide
response to methylmercury
Cellular Component
endoplasmic reticulum membrane
cytosol
Golgi apparatus
perinuclear region of cytoplasm
nucleus
zymogen granule
mitochondrial inner membrane
Function
hydrolase activity, acting on ester bonds
catalytic activity
hydrolase activity
lipase activity
phospholipase activity
Molecular Function
phospholipase A2 activity
lysophospholipase activity
calcium-dependent phospholipase A2 activity
calcium-dependent phospholipid binding
calcium ion binding
Process
metabolic process
organophosphate metabolic process
phospholipid metabolic process
phospholipid catabolic process
Cellular Location
  1. Cytoplasm
  2. Cytoplasmic vesicle
Gene Properties
Chromosome Location 1
Locus 1q25
SNPs PLA2G4A
Gene Sequence
>2250 bp
ATGTCATTTATAGATCCTTACCAGCACATTATAGTGGAGCACCAGTATTCCCACAAGTTT
ACGGTAGTGGTGTTACGTGCCACCAAAGTGACAAAGGGGGCCTTTGGTGACATGCTTGAT
ACTCCAGATCCCTATGTGGAACTTTTTATCTCTACAACCCCTGACAGCAGGAAGAGAACA
AGACATTTCAATAATGACATAAACCCTGTGTGGAATGAGACCTTTGAATTTATTTTGGAT
CCTAATCAGGAAAATGTTTTGGAGATTACGTTAATGGATGCCAATTATGTCATGGATGAA
ACTCTAGGGACAGCAACATTTACTGTATCTTCTATGAAGGTGGGAGAAAAGAAAGAAGTT
CCTTTTATTTTCAACCAAGTCACTGAAATGGTTCTAGAAATGTCTCTTGAAGTTTGCTCA
TGCCCAGACCTACGATTTAGTATGGCTCTGTGTGATCAGGAGAAGACTTTCAGACAACAG
AGAAAAGAACACATAAGGGAGAGCATGAAGAAACTCTTGGGTCCAAAGAATAGTGAAGGA
TTGCATTCTGCACGTGATGTGCCTGTGGTAGCCATATTGGGTTCAGGTGGGGGTTTCCGA
GCCATGGTGGGATTCTCTGGTGTGATGAAGGCATTATACGAATCAGGAATTCTGGATTGT
GCTACCTACGTTGCTGGTCTTTCTGGCTCCACCTGGTATATGTCAACCTTGTATTCTCAC
CCTGATTTTCCAGAGAAAGGGCCAGAGGAGATTAATGAAGAACTAATGAAAAATGTTAGC
CACAATCCCCTTTTACTTCTCACACCACAGAAAGTTAAAAGATATGTTGAGTCTTTATGG
AAGAAGAAAAGCTCTGGACAACCTGTCACCTTTACTGATATCTTTGGGATGTTAATAGGA
GAAACACTAATTCATAATAGAATGAATACTACTCTGAGCAGTTTGAAGGAAAAAGTTAAT
ACTGCACAATGCCCTTTACCTCTTTTCACCTGTCTTCATGTCAAACCTGACGTTTCAGAG
CTGATGTTTGCAGATTGGGTTGAATTTAGTCCATACGAAATTGGCATGGCTAAATATGGT
ACTTTTATGGCTCCCGACTTATTTGGAAGCAAATTTTTTATGGGAACAGTCGTTAAGAAG
TATGAAGAAAACCCCTTGCATTTCTTAATGGGTGTCTGGGGCAGTGCCTTTTCCATATTG
TTCAACAGAGTTTTGGGCGTTTCTGGTTCACAAAGCAGAGGCTCCACAATGGAGGAAGAA
TTAGAAAATATTACCACAAAGCATATTGTGAGTAATGATAGCTCGGACAGTGATGATGAA
TCACACGAACCCAAAGGCACTGAAAATGAAGATGCTGGAAGTGACTATCAAAGTGATAAT
CAAGCAAGTTGGATTCATCGTATGATAATGGCCTTGGTGAGTGATTCAGCTTTATTCAAT
ACCAGAGAAGGACGTGCTGGGAAGGTACACAACTTCATGCTGGGCTTGAATCTCAATACA
TCTTATCCACTGTCTCCTTTGAGTGACTTTGCCACACAGGACTCCTTTGATGATGATGAA
CTGGATGCAGCTGTAGCAGATCCTGATGAATTTGAGCGAATATATGAGCCTCTGGATGTC
AAAAGTAAAAAGATTCATGTAGTGGACAGTGGGCTCACATTTAACCTGCCGTATCCCTTG
ATACTGAGACCTCAGAGAGGGGTTGATCTCATAATCTCCTTTGACTTTTCTGCAAGGCCA
AGTGACTCTAGTCCTCCGTTCAAGGAACTTCTACTTGCAGAAAAGTGGGCTAAAATGAAC
AAGCTCCCCTTTCCAAAGATTGATCCTTATGTGTTTGATCGGGAAGGGCTGAAGGAGTGC
TATGTCTTTAAACCCAAGAATCCTGATATGGAGAAAGATTGCCCAACCATCATCCACTTT
GTTCTGGCCAACATCAACTTCAGAAAGTACAAGGCTCCAGGTGTTCCAAGGGAAACTGAG
GAAGAGAAAGAAATCGCTGACTTTGATATTTTTGATGACCCAGAATCACCATTTTCAACC
TTCAATTTTCAATATCCAAATCAAGCATTCAAAAGACTACATGATCTTATGCACTTCAAT
ACTCTGAACAACATTGATGTGATAAAAGAAGCCATGGTTGAAAGCATTGAATATAGAAGA
CAGAATCCATCTCGTTGCTCTGTTTCCCTTAGTAATGTTGAGGCAAGAAGATTTTTCAAC
AAGGAGTTTCTAAGTAAACCCAAAGCATAG
Protein Properties
Number of Residues 749
Molecular Weight 85210.19
Theoretical pI 5.376
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Cytosolic phospholipase A2
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P47712
UniProtKB/Swiss-Prot Entry Name PA24A_HUMAN
PDB IDs
GenBank Gene ID M72393
GeneCard ID PLA2G4A
GenAtlas ID PLA2G4A
HGNC ID HGNC:9035
References
General References
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  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  6. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
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  10. Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed:11416127 ]
  11. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974 ]
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  15. Sharp JD, Pickard RT, Chiou XG, Manetta JV, Kovacevic S, Miller JR, Varshavsky AD, Roberts EF, Strifler BA, Brems DN, et al.: Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1994 Sep 16;269(37):23250-4. [PubMed:8083230 ]
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