Venom Protein Card


Accession: Pre05206    Phospholipase A2   [Apis mellifera]

Basic info
Organism Apis mellifera
Taxonomy Insecta > Hymenoptera > Apidae > Apis > Apis mellifera
Protein Description Phospholipase A2
Mass Weight 18486.69 Da
Isoelectric Point 7.18
Expression Highly expressed in venom gland
Annotation
Function PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.Three segments were taken from the known X-ray structure of bovine pancre- atic phospholipase A2 [6] which form the active site and the region which binds the Ca2' ion.
Pfam
PF05826 Phospholip_A2_2
Features
Feature key Position Length
Signal Peptide 1..18 18
Propeptide 19..33 15
Chain 34..167 134
Cross-Reference
NCBI Nucleotide X16709.1
NCBI Protein CAA34681.1
UniProt P00630
Sequence
GGATCCTTGTTCCTTCTCCTCCTCTCTACCTCTCACGGATGGCAAATCAGGGATAGGATCGGGGATAACGAGTTGGAGGAACGGATAATATATCCAGGAACGTTATGGTGCGGGCATGGTAACAAGTCGTCCGGCCCGAACGAGCTAGGTCGGTTCAAGCACACGGATGCATGCTGTCGAACCCACGACATGTGCCCGGACGTTATGTCAGCTGGTGAATCGAAGCACGGCCTGACCAACACGGCCTCCCACACCAGGTTGTCGTGCGACTGCGACGACAAGTTCTATGATTGTCTTAAAAATTCGGCGGACACGATTAGCTCGTATTTCGTAGGGAAGATGTACTTCAATCTGATAGACACGAAGTGTTACAAACTGGAGCATCCTGTCACCGGGTGCGGTGAGAGAACCGAGGGTCGTTGTCTTCACTACACCGTGGACAAAAGCAAACCGAAAGTGTACCAATGGTTCGATCTTCGCAAGTATTGA
GSLFLLLLSTSHGWQIRDRIGDNELEERIIYPGTLWCGHGNKSSGPNELGRFKHTDACCRTHDMCPDVMSAGESKHGLTNTASHTRLSCDCDDKFYDCLKNSADTISSYFVGKMYFNLIDTKCYKLEHPVTGCGERTEGRCLHYTVDKSKPKVYQWFDLRKY

3D Structure
Publication
1. Moreira L.A., Ito J., Ghosh A., Devenport M., Zieler H., Abraham E.G., Crisanti A., Nolan T., Catteruccia F., Jacobs-Lorena M.;
"Bee venom phospholipase inhibits malaria parasite development in transgenic mosquitoes.";
J. Biol. Chem. 277:40839-40843(2002).
2. Valdez-Cruz N.A., Segovia L., Corona M., Possani L.D.;
"Sequence analysis and phylogenetic relationship of genes encoding heterodimeric phospholipases A2 from the venom of the scorpion Anuroctonus phaiodactylus.";
Gene 396:149-158(2007).
3. Kuchler K., Gmachl M., Sippl M.J., Kreil G.;
"Analysis of the cDNA for phospholipase A2 from honeybee venom glands. The deduced amino acid sequence reveals homology to the corresponding vertebrate enzymes.";
Eur. J. Biochem. 184:249-254(1989).
4. Shipolini R.A., Callewaert G.L., Cottrell R.C., Vernon C.A.;
"The amino-acid sequence and carbohydrate content of phospholipase A2 from bee venom.";
Eur. J. Biochem. 48:465-476(1974).
5. Ferreira Junior R.S., Sciani J.M., Marques-Porto R., Junior A.L., Orsi R.D., Barraviera B., Pimenta D.C.;
"Africanized honey bee (Apis mellifera) venom profiling: Seasonal variation of melittin and phospholipase A(2) levels.";
Toxicon 56:355-362(2010).
6. Shipolini R.A., Doonan S., Vernon C.A.;
"The disulphide bridges of phospholipase A2 from bee venom.";
Eur. J. Biochem. 48:477-483(1974).
7. Kubelka V., Altmann F., Staudacher E., Tretter V., Marz L., Hard K., Kamerling J.P., Vliegenthart J.F.;
"Primary structures of the N-linked carbohydrate chains from honeybee venom phospholipase A2.";
Eur. J. Biochem. 213:1193-1204(1993).
8. Scott D.L., Otwinowski Z., Gelb M.H., Sigler P.B.;
"Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue.";
Science 250:1563-1566(1990).