P0DM51 · PA2B1_BOTPA
- ProteinBasic phospholipase A2 BnpTX-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Snake venom phospholipase A2 (PLA2). In vitro, shows anticoagulant activity and induces cytotoxicity when tested on C2C12 myoblasts/myotubes. In vivo, when tested on mice, induces myotoxicity (intramuscular injection), edema (injection in the subplantar region) and lethality. Also induces neurotoxic effect on mouse neuromuscular preparations and has bactericidal activity on the Gram-negative bacteria E.coli (ATCC29648) and the Gram-positive S.aureus (ATCC 25923). The catalytic and anticoagulant activities of BnpTX-I are higher than those of BnpTX-II. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Miscellaneous
Has a pI of approximately 7.8 and about 121 amino acids.
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.
Activity regulation
P-bromophenacyl bromide (BPB) completely inhibit the catalytic activity whereas it only partially reduces the toxic activities. EDTA and magnesium ions partially inhibit the catalytic activity and partially reduce the toxic activities.
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 | defense response to bacterium | |
Biological Process | lipid catabolic process | |
Biological Process | negative regulation of T cell proliferation | |
Biological Process | phospholipid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBasic phospholipase A2 BnpTX-1
- EC number
- Short namesBnPTx-I; svPLA2
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Bothrops
Accessions
- Primary accessionP0DM51
Subcellular Location
Phenotypes & Variants
Toxic dose
LD50 is 5.1 +/- 1.3 mg/kg by intraperitoneal injection into mice.
LD50 is 2.3 +/- 0.8 mg/kg by intravenous injection into mice.
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000423032 | 1-50 | Basic phospholipase A2 BnpTX-1 | |||
Sequence: DLWQFGKMILKVAGKLPFPYYGAYGCYCGWGGRGKPKDPTDRCCFVHDCC | ||||||
Disulfide bond | 26↔? | |||||
Sequence: DLWQFGKMILKVAGKLPFPYYGAYG | ||||||
Disulfide bond | 28↔44 | |||||
Sequence: CGWGGRGKPKDPTDRCC | ||||||
Disulfide bond | 43↔? | |||||
Sequence: DLWQFGKMILKVAGKLPFPYYGAYGCYCGWGGRGKPKDPTDR | ||||||
Disulfide bond | 49↔? | |||||
Sequence: DLWQFGKMILKVAGKLPFPYYGAYGCYCGWGGRGKPKDPTDRCCFVHD | ||||||
Disulfide bond | 50↔? | |||||
Sequence: DLWQFGKMILKVAGKLPFPYYGAYGCYCGWGGRGKPKDPTDRCCFVHDC |
Post-translational modification
Contains 7 disulfide bonds.
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Dimer.
Structure
Family & Domains
Sequence similarities
Family and domain databases
Sequence
- Sequence statusFragment
- Length50
- Mass (Da)5,653
- Last updated2013-07-24 v1
- Checksum220BFE9682613497
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 50 | |||||
Sequence: C |
Keywords
- Technical term