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PROSITE documentation PDOC51210 [for PROSITE entry PS51210]

PLA2c domain profile





Description

The PLA2c domain is the catalytic lipase domain in cytosolic phospholipase A2 (cPLA2) (EC 3.1.1.4) and lysophospholipase or phospholipase B (PLB) (EC 3.1.1.5) of vertebrates and fungi. It catalyzes the carboxylic ester hydrolysis of glycerophospholipids or lysophospholipids. The mammalian cPLA2 group IVA enzymes cleave intracellular phospholipid membranes to produce lipid mediators, which also play a role in inflammatory diseases such as asthma and arthritis. This enzyme contains a N-terminal calcium-binding C2 domain (see <PDOC00380>) that presents the catalytic domain to the membrane [1]. Fungal secreted lysophospholipase/PLB can possess three different enzymatic activities, the hydrolase activity of phospholipase, lysophospholipase and a lysophospholipase transacylase activity.

The 3D structure of the PLA2c domain forms a central core of a 10-stranded mixed β sheet surrounded by 9 α helices (see <PDB:1CJY>). This central α/β core resembles the α/β hydrolase fold, but an additional 180-residue patch between strands 9 and 10 forms a catalytic domain 'cap' [2]. Ser 228 and Asp 549 of human cPLA2 α form the potential catalytic dyad. Parts of the cap-region are poorly conserved and are distinct among isoforms [3,4].

Some proteins known to contain a PLA2c domain:

  • Mammalian cytosolic phospholipase A2 (cPLA2) α/group IVA, which releases arachidonic acid from the sn-2 position of membrane glycerophospholipids and initiates the biosynthesis of prostaglandins, leukotrienes and platelet-activating factor.
  • Mammalian cytosolic phospholipase A2 (cPLA2) γ/group IVC, which is implicated in the remodeling of membrane phospholipids.
  • Fungal lysophospholipases/PLB, which are considered to be important for virulence of pathogenic fungi.
  • Yeast sporulation-specific protein 1 (SPO1), which is required for meiosis.

The profile we developed covers the entire PLA2c domain.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

May 2006 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

PLA2C, PS51210; PLA2c domain profile  (MATRIX)


References

1AuthorsNalefski E.A. Sultzman L.A. Martin D.M. Kriz R.W. Towler P.S. Knopf J.L. Clark J.D.
TitleDelineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain.
SourceJ. Biol. Chem. 269:18239-18249(1994)
PubMed ID8027085

2AuthorsDessen A. Tang J. Schmidt H. Stahl M. Clark J.D. Seehra J. Somers W.S.
TitleCrystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism.
SourceCell 97:349-360(1999).
PubMed ID10319815

3AuthorsSong C. Chang X.J. Bean K.M. Proia M.S. Knopf J.L. Kriz R.W.
TitleMolecular characterization of cytosolic phospholipase A2-beta.
SourceJ. Biol. Chem. 274:17063-17067(1999).
PubMed ID10358058

4AuthorsOhto T. Uozumi N. Hirabayashi T. Shimizu T.
TitleIdentification of novel cytosolic phospholipase A(2)s, murine cPLA(2)delta, epsilon, and zeta, which form a gene cluster with cPLA(2)beta.
SourceJ. Biol. Chem. 280:24576-24583(2005).
PubMed ID15866882
DOI10.1074/jbc.M413711200



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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