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InterPro: IPR013090 Phospholipase A2, active site

Protein matchesHelp
UniProtKB
Matches:
1030 proteins
AccessionHelp IPR013090 Phospholipase_A2_AS
SecondaryHelp IPR001211
TypeHelp Active_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR001211 Phospholipase A2, eukaryotic
IPR008774 Phospholipase A2, metazoa
IPR016090 Phospholipase A2
GO Term annotationHelp
Process GO:0006644 phospholipid metabolic process
GO:0016042 lipid catabolic process
Function GO:0004623 phospholipase A2 activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Phospholipase A2 (EC:3.1.1.4) (PLA2) is a small lipolytic enzyme that releases fatty acids from the second carbon group of glycerol. It is involved in a number of physiologically important cellular processes, such as the liberation of arachidonic acid from membrane phospholipids [1]. It plays a pivotal role in the biosynthesis of prostaglandin and other mediators of inflammation. PLA2 has four to seven disulphide bonds and binds a calcium ion that is essential for activity. Within the active enzyme, the alpha amino group is involved in a conserved hydrogen-bonding network linking the N-terminal region to the active site. The side chains of two conserved residues, His and Asp, participate in the catalytic network [2].

Many PLA2's are widely distributed in snakes, lizards, bees and mammals. In mammals there are at least four forms: pancreatic, membrane-associated as well as two less well characterised forms. The venom of most snakes contains multiple forms of PLA2. Some of them are presynaptic neurotoxins which inhibit neuromuscular transmission by blocking acetylcholine release from the nerve termini.

Some of the proteins containing these active sites are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.

The allergens in this family include allergens with the following designations: Api m 1.

Structural linksHelp
PDB - click here
CATH: 1.20.90.10
Database linksHelp
PDBe-motif: PS00118 , PS00119
Enzyme: EC:3.1.1.4
PROSITE doc: PDOC00109
Blocks: IPB013090

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR013090 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A4FS04 Phospholipase A2 natratoxin

O15496 Group 10 secretory phospholipase A2

P31482 Phospholipase A2, membrane associated

Q9U256 Phospholipase A2-like protein Y52B11A.8

Q9XG81 Probable phospholipase A2 homolog 2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR016090 Phospholipase A2
IPR013090 Phospholipase A2, active site
IPR001211 Phospholipase A2, eukaryotic
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. van den Berg B, Tessari M, Boelens R, Dijkman R, de Haas GH, Kaptein R, Verheij HM.
NMR structures of phospholipase A2 reveal conformational changes during interfacial activation.
Nat. Struct. Biol. 2 402-6 1995 [PubMed: 7664098]
http://dx.doi.org/10.1038/nsb0595-402
2. Gomez F, Vandermeers A, Vandermeers-Piret MC, Herzog R, Rathe J, Stievenart M, Winand J, Christophe J.
Purification and characterization of five variants of phospholipase A2 and complete primary structure of the main phospholipase A2 variant in Heloderma suspectum (Gila monster) venom.
Eur. J. Biochem. 186 23-33 1989 [PubMed: 2480893]
http://dx.doi.org/10.1111/j.1432-1033.1989.tb15172.x

Additional ReadingHelp
Marchi-Salvador DP, Correa LC, Magro AJ, Oliveira CZ, Soares AM, Fontes MR.
Insights into the role of oligomeric state on the biological activities of crotoxin: crystal structure of a tetrameric phospholipase A2 formed by two isoforms of crotoxin B from Crotalus durissus terrificus venom.
Proteins 72 2008 883-91 [PubMed: 18275084]
http://dx.doi.org/10.1002/prot.21980
Murakami MT, Kuch U, Betzel C, Mebs D, Arni RK.
Crystal structure of a novel myotoxic Arg49 phospholipase A2 homolog (zhaoermiatoxin) from Zhaoermia mangshanensis snake venom: insights into Arg49 coordination and the role of Lys122 in the polarization of the C-terminus.
Toxicon 51 2008 723-35 [PubMed: 18295812]
http://dx.doi.org/10.1016/j.toxicon.2007.11.018
Hu P, Sun L, Zhu ZQ, Hou XW, Wang S, Yu SS, Wang HL, Zhang P, Wang M, Niu LW, Teng MK, Ruan DY.
Crystal structure of Natratoxin, a novel snake secreted phospholipaseA2 neurotoxin from Naja atra venom inhibiting A-type K+ currents.
Proteins 72 2008 673-83 [PubMed: 18247353]
http://dx.doi.org/10.1002/prot.21964
Correa LC, Marchi-Salvador DP, Cintra AC, Sampaio SV, Soares AM, Fontes MR.
Crystal structure of a myotoxic Asp49-phospholipase A2 with low catalytic activity: Insights into Ca2+-independent catalytic mechanism.
Biochim. Biophys. Acta 1784 2008 591-9 [PubMed: 18261474]
Davidson FF, Dennis EA.
Evolutionary relationships and implications for the regulation of phospholipase A2 from snake venom to human secreted forms.
J. Mol. Evol. 31 1990 228-38 [PubMed: 2120459]
http://dx.doi.org/10.1007/BF02109500
Zhou X, Tan TC, Valiyaveettil S, Go ML, Kini RM, Velazquez-Campoy A, Sivaraman J.
Structural characterization of myotoxic ecarpholin S from Echis carinatus venom.
Biophys. J. 95 2008 3366-80 [PubMed: 18586854]
http://dx.doi.org/10.1529/biophysj.107.117747
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InterPro 23.1