P01482 · SCX5_ANDMA

Function

function

Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission.

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 Functionsodium channel inhibitor activity
Molecular Functiontoxin activity
Biological Processdefense response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-toxin Amm5
  • Alternative names
    • Amm V (AmmV)
    • Neurotoxin 5
    • Neurotoxin V

Organism names

Accessions

  • Primary accession
    P01482

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, disulfide bond, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000667231-64Alpha-toxin Amm5
Disulfide bond12↔63
Disulfide bond16↔36
Disulfide bond22↔46
Disulfide bond26↔48
Modified residue64Asparagine amide

Keywords

Expression

Tissue specificity

Expressed by the venom gland.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-64LCN-type CS-alpha/beta

Domain

Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    64
  • Mass (Da)
    7,301
  • Last updated
    1986-07-21 v1
  • Checksum
    3D03A733534CD866
LKDGYIIDDLNCTFFCGRNAYCDDECKKKGGESGYCQWASPYGNACWCYKLPDRVSIKEKGRCN

Mass Spectrometry

Molecular mass is 7,280 Da. Determined by MALDI.

Keywords

Sequence databases

Similar Proteins

Disclaimer

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