Summary: Phospholipase A2
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Phospholipase A2 Provide feedback
This family consists of several phospholipase A2 like proteins mostly from insects .
Moreira LA, Ito J, Ghosh A, Devenport M, Zieler H, Abraham EG, Crisanti A, Nolan T, Catteruccia F, Jacobs-Lorena M; , J Biol Chem 2002;277:40839-40843.: Bee venom phospholipase inhibits malaria parasite development in transgenic mosquitoes. PUBMED:12167627 EPMC:12167627
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001211
Phospholipase A2 (EC) (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 [PUBMED:7664098]. 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.
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 in this family 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.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||calcium ion binding (GO:0005509)|
|phospholipase A2 activity (GO:0004623)|
|Biological process||lipid catabolic process (GO:0016042)|
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_7918 (release 8.0)|
|Number in seed:||23|
|Number in full:||357|
|Average length of the domain:||92.80 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||37.16 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Phospholip_A2_2 domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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