P83257 · T3D1B_PIRLC

Function

function

Insecticidal toxin. Binds to site 4 of insect voltage-gated sodium channel (Nav) and inhibits channel inactivation. In vivo, it lethal to lepidopteran larvae. Has no adverse affects when intracerebroventricularly injected in mice at a dose of 0.2 ug, but causes reversible paralysis of legs when injected intracerebroventricularly in mice at a dose of 2.0 ug.

Features

Showing features for site.

1375101520253035
ACVGDGQRCASWSGPYCCDGYYCSCRSMPYCRCRNNS
TypeIDPosition(s)Description
Site8Pharmacophore
Site12Pharmacophore
Site19May be involved in voltage sensor trapping upon activation of sodium channel
Site22Pharmacophore
Site24Pharmacophore
Site26Pharmacophore
Site28Pharmacophore
Site30Pharmacophore
Site32Pharmacophore
Site34Pharmacophore

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 regulator activity
Molecular Functiontoxin activity
Biological Processmodulation of process of another organism

Keywords

Protein family/group databases

    • 8.B.6.1.9the ca2+ channel-targeting spider toxin (cst) family

Names & Taxonomy

Protein names

  • Recommended name
    Delta-amaurobitoxin-Pl1b
  • Short names
    Delta-AMATX-Pl1b
  • Alternative names
    • Delta-palutoxin IT2
      (Delta-paluIT2
      )

Organism names

Accessions

  • Primary accession
    P83257

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Toxic dose

LD50 is 24.2 ng/mg body weight of lepidoptera larvae.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis3No change in binding affinity and in lethal dose.
Mutagenesis5No change in binding affinity and in lethal dose.
Mutagenesis7No change in binding affinity and in lethal dose.
Mutagenesis851-fold decrease in binding affinity and no change in lethal dose.
Mutagenesis8More than 80-fold decrease in binding affinity and 5-fold decrease in toxicity.
Mutagenesis11No change in binding affinity and in lethal dose.
Mutagenesis12More than 160-fold decrease in binding affinity and no change in lethal dose.
Mutagenesis1213.5-fold decrease in binding affinity and more than 8-fold decrease in toxicity.
Mutagenesis13No change in binding affinity and in lethal dose.
Mutagenesis16No change in binding affinity and in lethal dose.
Mutagenesis19No change in binding affinity and 2.9-fold decrease in toxicity.
Mutagenesis21No change in binding affinity and in lethal dose.
Mutagenesis2254-fold decrease in binding affinity and no change in lethal dose.
Mutagenesis2440-fold decrease in binding affinity and no change in lethal dose.
Mutagenesis2616-fold decrease in binding affinity and no change in lethal dose.
Mutagenesis2828-fold decrease in binding affinity and no change in lethal dose.
Mutagenesis3058-fold decrease in binding affinity and 5.1-fold decrease in toxicity.
Mutagenesis3016-fold decrease in binding affinity and no change in lethal dose.
Mutagenesis3224-fold decrease in binding affinity and 2.3-fold decrease in toxicity.
Mutagenesis3418-fold decrease in binding affinity and no change in lethal dose.
Mutagenesis35No change in binding affinity and in lethal dose.
Mutagenesis36No change in binding affinity and in lethal dose.
Mutagenesis37No change in binding affinity and in lethal dose.

PTM/Processing

Features

Showing features for peptide, disulfide bond, modified residue.

TypeIDPosition(s)Description
PeptidePRO_00000449621-37Delta-amaurobitoxin-Pl1b
Disulfide bond2↔18
Disulfide bond9↔23
Disulfide bond17↔33
Disulfide bond25↔31
Modified residue37Serine amide

Keywords

Expression

Tissue specificity

Expressed by the venom gland.

Family & Domains

Domain

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    37
  • Mass (Da)
    4,124
  • Last updated
    2002-03-01 v1
  • Checksum
    861E12C2EB547716
ACVGDGQRCASWSGPYCCDGYYCSCRSMPYCRCRNNS

Mass Spectrometry

Molecular mass is 4,114.6 Da. Determined by MALDI.

Keywords

Similar Proteins

Disclaimer

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