| Identification |
| HMDB Protein ID
| HMDBP12432 |
| Secondary Accession Numbers
| None |
| Name
| Acidic phospholipase A2 CM-II |
| Synonyms
|
- CM 2
- svPLA2
- Acidic phospholipase A2 1
- NnkPLA-I
- 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
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
| 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
| - 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 ]
- 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 ]
- 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 ]
- 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 ]
|