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InterPro: IPR016090 Phospholipase A2

Protein matchesHelp
UniProtKB
Matches:
1269 proteins
AccessionHelp IPR016090 Phospholipase_A2
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR001211 Phospholipase A2, eukaryotic
IPR008774 Phospholipase A2, metazoa
IPR010711 Phospholipase A2, group XII secretory
IPR015141 Phospholipase A2, prokaryotic/fungal
Contains IPR013090 Phospholipase A2, active site
InterPro annotation
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AbstractHelp

This entry represents eukaryotic and prokaryotic phospholipase A2 enzymes (PLA2; EC:3.1.1.4), small lipolytic enzymes that releases fatty acids from the second carbon group of glycerol. These enzymes enable the of fatty acids and lysophospholipid by hydrolysing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides.

The phospholipase domain adopts an alpha-helical secondary structure, consisting of five alpha-helices and two helical segments [1, 2]. In eukaryotes, PLAS plays a pivotal role in the biosynthesis of prostaglandin and other mediators of inflammation.

Structural linksHelp
PDB - click here
CATH: 1.20.90.10
Database linksHelp
Enzyme: EC:3.1.1.4

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR016090 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. Matoba Y, Katsube Y, Sugiyama M.
The crystal structure of prokaryotic phospholipase A2.
J. Biol. Chem. 277 20059-69 2002 [PubMed: 11897785]
http://dx.doi.org/10.1074/jbc.M200263200
2. Pan YH, Yu BZ, Singer AG, Ghomashchi F, Lambeau G, Gelb MH, Jain MK, Bahnson BJ.
Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes.
J. Biol. Chem. 277 29086-93 2002 [PubMed: 12161451]
http://dx.doi.org/10.1074/jbc.M202531200

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]
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