Hmdb loader
Identification
HMDB Protein ID HMDBP12432
Secondary Accession Numbers None
Name Acidic phospholipase A2 CM-II
Synonyms
  1. CM 2
  2. svPLA2
  3. Acidic phospholipase A2 1
  4. NnkPLA-I
  5. Phosphatidylcholine 2-acylhydrolase
Gene Name Not Available
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable). Is able to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis neurons (IC(50)=37 nM) and to compete with alpha-bungarotoxin for binding to muscle- and alpha-7 neuronal nAChR types, as well as to AChBPs (PubMed:25522251). In inhibition of alpha-bungarotoxin binding, this toxin is similarly active against T.californica nAChR (IC(50)=1.2 uM), human alpha-7 nAChR (IC(50)=3.2 uM), and L.stagnalis AChBP (IC(50)=1.0 uM), whereas it is not active against A.californica AChBP (IC(50)>100 uM) (PubMed:25522251).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
phospholipid metabolic process
lipid catabolic process
arachidonic acid secretion
Cellular Component
extracellular region
Molecular Function
calcium ion binding
phospholipase A2 activity
toxin activity
phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine)
phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine)
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues Not Available
Molecular Weight 16271.225
Theoretical pI Not Available
Pfam Domain Function
Signals
  • 1-21;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P00596
UniProtKB/Swiss-Prot Entry Name PA2A1_NAJKA
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Vulfius CA, Kasheverov IE, Starkov VG, Osipov AV, Andreeva TV, Filkin SY, Gorbacheva EV, Astashev ME, Tsetlin VI, Utkin YN: Inhibition of nicotinic acetylcholine receptors, a novel facet in the pleiotropic activities of snake venom phospholipases A2. PLoS One. 2014 Dec 18;9(12):e115428. doi: 10.1371/journal.pone.0115428. eCollection 2014. [PubMed:25522251 ]
  2. Chuman Y, Nobuhisa I, Ogawa T, Deshimaru M, Chijiwa T, Tan NH, Fukumaki Y, Shimohigashi Y, Ducancel F, Boulain JC, Menez A, Ohno M: Regional and accelerated molecular evolution in group I snake venom gland phospholipase A2 isozymes. Toxicon. 2000 Mar;38(3):449-62. doi: 10.1016/s0041-0101(99)00165-8. [PubMed:10669032 ]
  3. Joubert FJ, Taljaard N: Purification, some properties and amino-acid sequences of two phospholipases A (CM-II and CM-III) from Naja naja kaouthia venom. Eur J Biochem. 1980 Dec;112(3):493-9. doi: 10.1111/j.1432-1033.1980.tb06112.x. [PubMed:7460933 ]
  4. Osipov AV, Filkin SY, Makarova YV, Tsetlin VI, Utkin YN: A new type of thrombin inhibitor, noncytotoxic phospholipase A2, from the Naja haje cobra venom. Toxicon. 2010 Feb-Mar;55(2-3):186-94. doi: 10.1016/j.toxicon.2009.07.011. Epub 2009 Jul 19. [PubMed:19622365 ]