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Showing Protein 85/88 kDa calcium-independent phospholipase A2 (HMDBP12172)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP12172
Secondary Accession Numbers None
Name 85/88 kDa calcium-independent phospholipase A2
Synonyms
  1. CaI-PLA2
  2. 2-lysophosphatidylcholine acylhydrolase
  3. Group VI phospholipase A2
  4. Intracellular membrane-associated calcium-independent phospholipase A2 beta
  5. Palmitoyl-CoA hydrolase
  6. Patatin-like phospholipase domain-containing protein 9
  7. GVI PLA2
  8. iPLA2-beta
  9. PNPLA9
Gene Name PLA2G6
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Calcium-independent phospholipase involved in phospholipid remodeling with implications in cellular membrane homeostasis, mitochondrial integrity and signal transduction. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity respectively), producing lysophospholipids that are used in deacylation-reacylation cycles (PubMed:18937505). Hydrolyzes both saturated and unsaturated long fatty acyl chains in various glycerophospholipid classes such as phosphatidylcholines, phosphatidylethanolamines and phosphatidates, with a preference for hydrolysis at sn-2 position. Can further hydrolyze lysophospholipids carrying saturated fatty acyl chains (lysophospholipase activity). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (By similarity). Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains from cardiolipins, yielding monolysocardiolipins that can be reacylated with unoxidized fatty acyls to regenerate native cardiolipin species. Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic islets, releasing oxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates (HETEs) (PubMed:24648512). Has thioesterase activity toward fatty-acyl CoA releasing CoA-SH known to facilitate fatty acid transport and beta-oxidation in mitochondria particularly in skeletal muscle (PubMed:18937505). Plays a role in regulation of membrane dynamics and homeostasis. Selectively hydrolyzes sn-2 arachidonoyl group in plasmalogen phospholipids, structural components of lipid rafts and myelin (By similarity). Regulates F-actin polymerization at the pseudopods, which is required for both speed and directionality of MCP1/CCL2-induced monocyte chemotaxis (By similarity). Targets membrane phospholipids to produce potent lipid signaling messengers. Generates lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), which acts via G-protein receptors in various cell types. Has phospholipase A2 activity toward platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role in inactivation of this potent proinflammatory signaling lipid (By similarity). In response to glucose, amplifies calcium influx in pancreatic beta cells to promote INS secretion (PubMed:17895289).
Pathways
  • alpha-Linolenic acid metabolism
  • Arachidonic acid metabolism
  • Ether lipid metabolism
  • Fc gamma R-mediated phagocytosis
  • Glycerophospholipid metabolism
  • Inflammatory mediator regulation of TRP channels
  • Linoleic acid metabolism
  • Ras signaling pathway
  • Vascular smooth muscle contraction
Reactions Not Available
GO Classification
Biological Process
elevation of cytosolic calcium ion concentration
positive regulation of release of cytochrome c from mitochondria
positive regulation of insulin secretion involved in cellular response to glucose stimulus
chemotaxis
phosphatidylcholine catabolic process
cardiolipin acyl-chain remodeling
positive regulation of protein phosphorylation
memory
positive regulation of arachidonic acid secretion
phosphatidylethanolamine catabolic process
negative regulation of synaptic transmission, glutamatergic
cardiolipin biosynthetic process
maternal process involved in female pregnancy
antibacterial humoral response
phosphatidic acid metabolic process
platelet activating factor metabolic process
positive regulation of ceramide biosynthetic process
positive regulation of exocytosis
positive regulation of protein kinase C signaling
regulation of store-operated calcium channel activity
response to endoplasmic reticulum stress
urinary bladder smooth muscle contraction
Cellular Component
cytosol
centriolar satellite
mitochondrion
plasma membrane
extracellular space
pseudopodium
integral to membrane
Molecular Function
protein kinase binding
lysophospholipase activity
serine hydrolase activity
palmitoyl-CoA hydrolase activity
calcium-independent phospholipase A2 activity
1-alkyl-2-acetylglycerophosphocholine esterase activity
ATP-dependent protein binding
identical protein binding
calmodulin binding
phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine)
phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine)
myristoyl-CoA hydrolase activity
phosphatidyl phospholipase B activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 807
Molecular Weight 89559.1
Theoretical pI 7.235
Pfam Domain Function
Signals Not Available
Transmembrane Regions
  • 481-501;512-532;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P97819
UniProtKB/Swiss-Prot Entry Name PLPL9_MOUSE
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [PubMed:21183079 ]
  3. Balboa MA, Balsinde J, Jones SS, Dennis EA: Identity between the Ca2+-independent phospholipase A2 enzymes from P388D1 macrophages and Chinese hamster ovary cells. J Biol Chem. 1997 Mar 28;272(13):8576-80. doi: 10.1074/jbc.272.13.8576. [PubMed:9079688 ]
  4. Chiu CH, Jackowski S: Role of calcium-independent phospholipases (iPLA(2)) in phosphatidylcholine metabolism. Biochem Biophys Res Commun. 2001 Sep 28;287(3):600-6. doi: 10.1006/bbrc.2001.5632. [PubMed:11563837 ]
  5. Bao S, Jacobson DA, Wohltmann M, Bohrer A, Jin W, Philipson LH, Turk J: Glucose homeostasis, insulin secretion, and islet phospholipids in mice that overexpress iPLA2beta in pancreatic beta-cells and in iPLA2beta-null mice. Am J Physiol Endocrinol Metab. 2008 Feb;294(2):E217-29. doi: 10.1152/ajpendo.00474.2007. Epub 2007 Sep 25. [PubMed:17895289 ]
  6. Carper MJ, Zhang S, Turk J, Ramanadham S: Skeletal muscle group VIA phospholipase A2 (iPLA2beta): expression and role in fatty acid oxidation. Biochemistry. 2008 Nov 18;47(46):12241-9. doi: 10.1021/bi800923s. Epub 2008 Oct 21. [PubMed:18937505 ]
  7. Shinzawa K, Sumi H, Ikawa M, Matsuoka Y, Okabe M, Sakoda S, Tsujimoto Y: Neuroaxonal dystrophy caused by group VIA phospholipase A2 deficiency in mice: a model of human neurodegenerative disease. J Neurosci. 2008 Feb 27;28(9):2212-20. doi: 10.1523/JNEUROSCI.4354-07.2008. [PubMed:18305254 ]
  8. Beck G, Sugiura Y, Shinzawa K, Kato S, Setou M, Tsujimoto Y, Sakoda S, Sumi-Akamaru H: Neuroaxonal dystrophy in calcium-independent phospholipase A2beta deficiency results from insufficient remodeling and degeneration of mitochondrial and presynaptic membranes. J Neurosci. 2011 Aug 3;31(31):11411-20. doi: 10.1523/JNEUROSCI.0345-11.2011. [PubMed:21813701 ]
  9. Song H, Wohltmann M, Tan M, Ladenson JH, Turk J: Group VIA phospholipase A2 mitigates palmitate-induced beta-cell mitochondrial injury and apoptosis. J Biol Chem. 2014 May 16;289(20):14194-210. doi: 10.1074/jbc.M114.561910. Epub 2014 Mar 19. [PubMed:24648512 ]