P00618 · PA2B2_BUNMU
- ProteinBasic phospholipase A2 beta-bungarotoxin A2 chain
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids145 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
Cofactor
Note: Binds 1 Ca2+ ion.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent phospholipase A2 activity | |
Molecular Function | phospholipid binding | |
Molecular Function | toxin activity | |
Biological Process | arachidonic acid secretion | |
Biological Process | lipid catabolic process | |
Biological Process | phospholipid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBasic phospholipase A2 beta-bungarotoxin A2 chain
- EC number
- Short namesBeta-BuTX A2 chain; svPLA2
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Elapidae > Bungarinae > Bungarus
Accessions
- Primary accessionP00618
Subcellular Location
Phenotypes & Variants
Toxic dose
LD50 is 0.066 mg/kg by intraperitoneal injection in beta-3 bungarotoxin and 0.073 mg/kg in beta-4.
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MLIFLWCGAVCVSLLGA | ||||||
Propeptide | PRO_0000022837 | 18-25 | ||||
Sequence: ANIPPHPL | ||||||
Chain | PRO_0000022838 | 26-145 | Basic phospholipase A2 beta-bungarotoxin A2 chain | |||
Sequence: NLINFMEMIRYTIPCEKTWGEYADYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAEKKHKCNPKTQSYSYKLTKRTIICYGAAGTCARIVCDCDRTAALCFGNSEYIERHKNIDTKRHCR | ||||||
Disulfide bond | 40 | Interchain (with a B chain) | ||||
Sequence: C | ||||||
Disulfide bond | 52↔144 | |||||
Sequence: CYCGAGGSGRPIDALDRCCYVHDNCYGDAEKKHKCNPKTQSYSYKLTKRTIICYGAAGTCARIVCDCDRTAALCFGNSEYIERHKNIDTKRHC | ||||||
Disulfide bond | 54↔70 | |||||
Sequence: CGAGGSGRPIDALDRCC | ||||||
Disulfide bond | 69↔125 | |||||
Sequence: CCYVHDNCYGDAEKKHKCNPKTQSYSYKLTKRTIICYGAAGTCARIVCDCDRTAALC | ||||||
Disulfide bond | 76↔118 | |||||
Sequence: CYGDAEKKHKCNPKTQSYSYKLTKRTIICYGAAGTCARIVCDC | ||||||
Disulfide bond | 86↔111 | |||||
Sequence: CNPKTQSYSYKLTKRTIICYGAAGTC | ||||||
Disulfide bond | 104↔116 | |||||
Sequence: CYGAAGTCARIVC |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Heterodimer; disulfide-linked. The A chains have phospholipase A2 activity and the B chains show homology with the basic protease inhibitors. The A2 chain is found in beta-3 and beta-4 bungarotoxins.
Structure
Family & Domains
Sequence similarities
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length145
- Mass (Da)16,296
- Last updated1990-11-01 v2
- Checksum08CD9D0E84E57581
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 91-92 | in Ref. 2; AA sequence | ||||
Sequence: QS → SQ | ||||||
Sequence conflict | 128 | in Ref. 2; AA sequence | ||||
Sequence: N → Q | ||||||
Sequence conflict | 130 | in Ref. 2; AA sequence | ||||
Sequence: E → D |
Keywords
- Technical term