Human Metabolome Database Version 3.5

Showing Protein Phospholipase A2, membrane associated (HMDBP00072)

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
  • Glycerophospholipid metabolism
  • Ether lipid metabolism
  • Arachidonic acid metabolism
  • Linoleic acid metabolism
  • alpha-Linolenic acid metabolism
  • Vascular smooth muscle contraction
  • Pancreatic secretion
  • Fat digestion and absorption
Reactions
Phosphatidylcholine + Water unknown 1-acylglycerophosphocholine + a carboxylate details
Phosphatidylcholine + Water unknown 1-Acyl-sn-glycero-3-phosphocholine + Fatty acid details
Phosphatidylcholine + Water unknown 1-Acyl-sn-glycero-3-phosphocholine + Arachidonic acid details
Phosphatidylethanolamine + Water unknown 1-Acyl-sn-glycero-3-phosphoethanolamine + Fatty acid details
Phosphatidylcholine + Water unknown 1-Acyl-sn-glycero-3-phosphocholine + Linoleic acid details
O-1-Alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + Water unknown 1-(1-Alkenyl)-sn-glycero-3-phosphoethanolamine + Carboxylate details
1-Radyl-2-acyl-sn-glycero-3-phosphocholine + Water unknown 1-Organyl-2-lyso-sn-glycero-3-phosphocholine + Carboxylate details
Phosphatidylcholine + Water unknown 1-Acyl-sn-glycero-3-phosphocholine + Alpha-Linolenic acid details
GO Classification
Function
ion binding
cation binding
metal ion binding
hydrolase activity, acting on ester bonds
binding
catalytic activity
hydrolase activity
Process
metabolic process
primary metabolic process
lipid metabolic process
Function
calcium ion binding
carboxylesterase activity
phospholipase a2 activity
Process
lipid catabolic process
organophosphate metabolic process
phospholipid metabolic process
Cellular Component
endoplasmic reticulum membrane
Biological Process
phosphatidic acid biosynthetic process
Cellular Component
extracellular space
Molecular Function
calcium ion binding
Cellular Component
secretory granule
Molecular Function
phospholipid binding
Biological Process
phosphatidylglycerol acyl-chain remodeling
lipid catabolic process
phosphatidylcholine acyl-chain remodeling
phosphatidylethanolamine acyl-chain remodeling
phosphatidylinositol acyl-chain remodeling
phosphatidylserine acyl-chain remodeling
positive regulation of inflammatory response
low-density lipoprotein particle remodeling
positive regulation of macrophage derived foam cell differentiation
Molecular Function
calcium-dependent phospholipase A2 activity
Biological Process
defense response to Gram-positive bacterium
Cellular Location
  1. Membrane
  2. Peripheral membrane protein
Gene Properties
Chromosome Location 1
Locus 1p35
SNPs PLA2G2A Link_out
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 Link_out
UniProtKB/Swiss-Prot Entry Name PA2GA_HUMAN Link_out
PDB IDs
GenBank Gene ID M22430 Link_out
GeneCard ID PLA2G2A Link_out
GenAtlas ID PLA2G2A Link_out
HGNC ID HGNC:9031 Link_out
References
General References
  1. Seilhamer JJ, Pruzanski W, Vadas P, Plant S, Miller JA, Kloss J, Johnson LK: Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid. J Biol Chem. 1989 Apr 5;264(10):5335-8. Pubmed: 2925608 Link_out
  2. Kramer RM, Hession C, Johansen B, Hayes G, McGray P, Chow EP, Tizard R, Pepinsky RB: Structure and properties of a human non-pancreatic phospholipase A2. J Biol Chem. 1989 Apr 5;264(10):5768-75. Pubmed: 2925633 Link_out
  3. 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 Link_out
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  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 Link_out
  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 Link_out
  9. Lai CY, Wada K: Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme. Biochem Biophys Res Commun. 1988 Dec 15;157(2):488-93. Pubmed: 3202859 Link_out
  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 Link_out
  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 Link_out
  12. Scott DL, White SP, Browning JL, Rosa JJ, Gelb MH, Sigler PB: Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate. Science. 1991 Nov 15;254(5034):1007-10. Pubmed: 1948070 Link_out
  13. Schevitz RW, Bach NJ, Carlson DG, Chirgadze NY, Clawson DK, Dillard RD, Draheim SE, Hartley LW, Jones ND, Mihelich ED, et al.: Structure-based design of the first potent and selective inhibitor of human non-pancreatic secretory phospholipase A2. Nat Struct Biol. 1995 Jun;2(6):458-65. Pubmed: 7664108 Link_out
  14. Kitadokoro K, Hagishita S, Sato T, Ohtani M, Miki K: Crystal structure of human secretory phospholipase A2-IIA complex with the potent indolizine inhibitor 120-1032. J Biochem (Tokyo). 1998 Apr;123(4):619-23. Pubmed: 9538252 Link_out