Q1RP79 · PA2B1_VIPNI

Function

function

Heterodimer: shows the same activities as the monomer, but with a lower potency.
Monomer: snake venom phospholipase A2 (PLA2) that shows presynaptic neurotoxicity, anticoagulant activity and that weakly inhibits ADP-induced platelet aggregation (PubMed:18083205).
Inhibits exocytosis in pancreatic beta cells, confirming it can act presynaptically in inhibiting the exocytosis of neurotransmitters in neurons (PubMed:19500614).
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides

Catalytic activity

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion.

Activity regulation

Enzymatic activity and neurotoxicity are inhibited by Triton X-100, which has been determined to be located in the center of the hydrophobic channel of the enzyme.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site43Ca2+ (UniProtKB | ChEBI)
Binding site45Ca2+ (UniProtKB | ChEBI)
Binding site47Ca2+ (UniProtKB | ChEBI)
Active site63
Binding site64Ca2+ (UniProtKB | ChEBI)
Active site105

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent phospholipase A2 activity
Molecular Functionphospholipid binding
Molecular Functiontoxin activity
Biological Processarachidonic acid secretion
Biological Processlipid catabolic process
Biological Processphospholipid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Basic phospholipase A2 chain HDP-1P
  • EC number
  • Short names
    svPLA2
  • Alternative names
    • Heterodimeric neurotoxic phospholipases A2 basic subunit 1
    • Phosphatidylcholine 2-acylhydrolase

Organism names

Accessions

  • Primary accession
    Q1RP79

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-16
ChainPRO_500007975217-138Basic phospholipase A2 chain HDP-1P
Disulfide bond42↔131
Disulfide bond44↔60
Disulfide bond59↔111
Disulfide bond65↔138
Disulfide bond66↔104
Disulfide bond73↔97
Disulfide bond91↔102

Keywords

Expression

Tissue specificity

Expressed by the venom gland.

Interaction

Subunit

Heterodimer; non-covalently linked. The toxic basic protein has phospholipase A2 activity (chain HDP-1P) and the non-toxic acidic protein functions as its inhibitor (chain HPD-1I (AC A4VBF0)).

Family & Domains

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    138
  • Mass (Da)
    15,566
  • Last updated
    2006-05-16 v1
  • Checksum
    72D55BD516C3E5D9
MRILWIVAVCLIGVEGNLFQFAKMINGKLGAFSVWNYISYGCYCGWGGQGTPKDATDRCCFVHDCCYGRVRGCNPKLAIYAYSFKKGNIVCGKNNGCLRDICECDRVAANCFHQNQNTYNKNYKFLSSSRCRQTSEQC

Mass Spectrometry

Molecular mass is 13,798 Da. Determined by MALDI.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AM238698
EMBL· GenBank· DDBJ
CAJ87658.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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