P51972 · PA2B1_AGKPI

Function

function

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 per subunit.

Features

Showing features for binding site, active site.

1123102030405060708090100110120
TypeIDPosition(s)Description
Binding site27Ca2+ (UniProtKB | ChEBI)
Binding site29Ca2+ (UniProtKB | ChEBI)
Binding site31Ca2+ (UniProtKB | ChEBI)
Active site47
Binding site48Ca2+ (UniProtKB | ChEBI)
Active site89

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent phospholipase A2 activity
Molecular Functionphospholipid binding
Biological Processarachidonic acid secretion
Biological Processlipid catabolic process
Biological Processnegative regulation of T cell proliferation
Biological Processphospholipid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Basic phospholipase A2 APP-D49
  • EC number
  • Short names
    svPLA2
  • Alternative names
    • App-dimer
    • AppP3
    • Phosphatidylcholine 2-acylhydrolase

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Agkistrodon

Accessions

  • Primary accession
    P51972

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis675% decrease in catalytic efficiency.
Mutagenesis795% decrease in catalytic efficiency. 500-fold decrease in catalytic efficiency; when associated with E-10.
Mutagenesis1095% decrease in catalytic efficiency. 500-fold decrease in catalytic efficiency; when associated with E-7.
Mutagenesis1175% decrease in catalytic efficiency.
Mutagenesis1560% decrease in catalytic efficiency.
Mutagenesis53No effect on catalytic efficiency.
Mutagenesis60No effect on catalytic efficiency.

PTM/Processing

Features

Showing features for chain, lipidation, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00001616051-123Basic phospholipase A2 APP-D49
Lipidation7N6-palmitoyl lysine
Lipidation10N6-palmitoyl lysine
Disulfide bond26↔116
Disulfide bond28↔44
Disulfide bond43↔95
Disulfide bond49↔123
Disulfide bond50↔88
Disulfide bond57↔81
Disulfide bond75↔86

Post-translational modification

Acylation causes dimerization.

Keywords

Expression

Tissue specificity

Expressed by the venom gland.

Interaction

Subunit

Monomer or homodimer.

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    123
  • Mass (Da)
    13,989
  • Last updated
    1998-07-15 v2
  • Checksum
    C39986552D990D72
NLFQFEKLIKKMTGKSGMLWYSAYGCYCGWGGQGRPKDATDRCCFVHDCCYGKVTGCNPKMDIYTYSVDNGNIVCGGTNPCKKQICECDRAAAICFRDNLKTYDSKTYWKYPKKNCKEESEPC

Mass Spectrometry

Molecular mass is 13,988.67 Da. Determined by Electrospray.

Keywords

Sequence databases

Similar Proteins

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