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Identification
HMDB Protein ID HMDBP00072
Secondary Accession Numbers
  • 5301
Name Phospholipase A2, membrane associated
Synonyms
  1. GIIC sPLA2
  2. Group IIA phospholipase A2
  3. NPS-PLA2
  4. Non-pancreatic secretory phospholipase A2
  5. Phosphatidylcholine 2-acylhydrolase 2A
Gene Name PLA2G2A
Protein Type Unknown
Biological Properties
General Function Involved in phospholipase A2 activity
Specific Function Thought to participate in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Pathways
  • alpha-Linolenic acid metabolism
  • Arachidonic acid metabolism
  • Ether lipid metabolism
  • Fat digestion and absorption
  • Glycerophospholipid metabolism
  • Linoleic acid metabolism
  • Pancreatic secretion
  • Vascular smooth muscle contraction
Reactions
Phosphatidylcholine + Water → 1-acylglycerophosphocholine + 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
phosphatidylserine acyl-chain remodeling
positive regulation of inflammatory response
lipid catabolic process
low-density lipoprotein particle remodeling
positive regulation of macrophage derived foam cell differentiation
defense response to Gram-positive bacterium
phosphatidic acid biosynthetic process
phosphatidylglycerol acyl-chain remodeling
Cellular Component
endoplasmic reticulum membrane
secretory granule
extracellular space
Function
ion binding
cation binding
metal ion binding
hydrolase activity, acting on ester bonds
binding
catalytic activity
hydrolase activity
calcium ion binding
carboxylesterase activity
phospholipase a2 activity
Molecular Function
phospholipid binding
calcium-dependent phospholipase A2 activity
calcium ion binding
Process
metabolic process
primary metabolic process
lipid metabolic process
lipid catabolic process
organophosphate metabolic process
phospholipid metabolic process
Cellular Location
  1. Peripheral membrane protein
  2. Membrane
Gene Properties
Chromosome Location 1
Locus 1p35
SNPs PLA2G2A
Gene Sequence
>435 bp
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
Protein Properties
Number of Residues 144
Molecular Weight 16082.525
Theoretical pI 9.235
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Phospholipase A2, membrane associated
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P14555
UniProtKB/Swiss-Prot Entry Name PA2GA_HUMAN
PDB IDs
GenBank Gene ID M22430
GeneCard ID PLA2G2A
GenAtlas ID PLA2G2A
HGNC ID HGNC:9031
References
General References
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  6. Kramer RM, Johansen B, Hession C, Pepinsky RB: Structure and properties of a secretable phospholipase A2 from human platelets. Adv Exp Med Biol. 1990;275:35-53. Pubmed: 2239446
  7. Kanda A, Ono T, Yoshida N, Tojo H, Okamoto M: The primary structure of a membrane-associated phospholipase A2 from human spleen. Biochem Biophys Res Commun. 1989 Aug 30;163(1):42-8. Pubmed: 2775276
  8. Hara S, Kudo I, Matsuta K, Miyamoto T, Inoue K: Amino acid composition and NH2-terminal amino acid sequence of human phospholipase A2 purified from rheumatoid synovial fluid. J Biochem (Tokyo). 1988 Sep;104(3):326-8. Pubmed: 3240982
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  10. Minami T, Tojo H, Shinomura Y, Matsuzawa Y, Okamoto M: Purification and characterization of a phospholipase A2 from human ileal mucosa. Biochim Biophys Acta. 1993 Oct 13;1170(2):125-30. Pubmed: 8399335
  11. Wery JP, Schevitz RW, Clawson DK, Bobbitt JL, Dow ER, Gamboa G, Goodson T Jr, Hermann RB, Kramer RM, McClure DB, et al.: Structure of recombinant human rheumatoid arthritic synovial fluid phospholipase A2 at 2.2 A resolution. Nature. 1991 Jul 4;352(6330):79-82. Pubmed: 2062381
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