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Protein

Delta-amaurobitoxin-Pl1b

Gene
N/A
Organism
Pireneitega luctuosa (Tangled nest spider) (Paracoelotes luctuosus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Insecticidal toxin. Lethal to lepidopteran larvae. No adverse affects when intracerebroventricularly injected in mice at a dose of 0.2 µg but causes reversible paralysis of legs when injected intracerebroventricularly in mice at a dose of 2.0 µg. Binds to site 4 of insect voltage-gated sodium channel (Nav) and inhibits channel inactivation.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei8Pharmacophore1
Sitei12Pharmacophore1
Sitei19May be involved in voltage sensor trapping upon activation of sodium channel1 Publication1
Sitei22Pharmacophore1
Sitei24Pharmacophore1
Sitei26Pharmacophore1
Sitei28Pharmacophore1
Sitei30Pharmacophore1
Sitei32Pharmacophore1
Sitei34Pharmacophore1

GO - Molecular functioni

  • sodium channel inhibitor activity Source: UniProtKB
  • toxin activity Source: InterPro

GO - Biological processi

  • pathogenesis Source: UniProtKB

Keywordsi

Molecular functionIon channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-amaurobitoxin-Pl1b
Short name:
Delta-AMATX-Pl1b
Alternative name(s):
Delta-palutoxin IT21 Publication
Short name:
Delta-paluIT21 Publication
OrganismiPireneitega luctuosa (Tangled nest spider) (Paracoelotes luctuosus)
Taxonomic identifieri185217 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeAraneomorphaeEntelegynaeAmaurobiidaePireneitega

Organism-specific databases

ArachnoServeriAS000302. delta-Amaurobitoxin-Pl1b.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 24.2 ng/mg body weight of lepidoptera larvae.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3V → A: Nonsignificant differences nor in binding affinity neither in lethal dose. 1 Publication1
Mutagenesisi5D → A: Nonsignificant differences nor in binding affinity neither in lethal dose. 1 Publication1
Mutagenesisi7Q → A: Nonsignificant differences nor in binding affinity neither in lethal dose. 1 Publication1
Mutagenesisi8R → A: 51-fold decrease in binding affinity and nonsignificant differences in lethal dose. 1 Publication1
Mutagenesisi8R → D: More than 80-fold decrease in binding affinity and 5-fold decrease in toxicity. 1 Publication1
Mutagenesisi11S → A: Nonsignificant differences nor in binding affinity neither in lethal dose. 1 Publication1
Mutagenesisi12W → A: More than 160-fold decrease in binding affinity and nonsignificant differences in lethal dose. 1 Publication1
Mutagenesisi12W → F: 13.5-fold decrease in binding affinity and more than 8-fold decrease in toxicity. 1 Publication1
Mutagenesisi13S → A: Nonsignificant differences nor in binding affinity neither in lethal dose. 1 Publication1
Mutagenesisi16Y → A: Nonsignificant differences nor in binding affinity neither in lethal dose. 1 Publication1
Mutagenesisi19D → A: Nonsignificant differences in binding affinity and 2.9-fold decrease in toxicity. 1 Publication1
Mutagenesisi21Y → A: Nonsignificant differences nor in binding affinity neither in lethal dose. 1 Publication1
Mutagenesisi22Y → A: 54-fold decrease in binding affinity and nonsignificant differences in lethal dose. 1 Publication1
Mutagenesisi24S → A: 40-fold decrease in binding affinity and nonsignificant differences in lethal dose. 1 Publication1
Mutagenesisi26R → A: 16-fold decrease in binding affinity and nonsignificant differences in lethal dose. 1 Publication1
Mutagenesisi28M → A: 28-fold decrease in binding affinity and nonsignificant differences in lethal dose. 1 Publication1
Mutagenesisi30Y → A: 58-fold decrease in binding affinity and 5.1-fold decrease in toxicity. 1 Publication1
Mutagenesisi30Y → F: 16-fold decrease in binding affinity and nonsignificant differences in lethal dose. 1 Publication1
Mutagenesisi32R → A: 24-fold decrease in binding affinity and 2.3-fold decrease in toxicity. 1 Publication1
Mutagenesisi34R → A: 18-fold decrease in binding affinity and nonsignificant differences in lethal dose. 1 Publication1
Mutagenesisi35N → A: Nonsignificant differences nor in binding affinity neither in lethal dose. 1 Publication1
Mutagenesisi36N → A: Nonsignificant differences nor in binding affinity neither in lethal dose. 1 Publication1
Mutagenesisi37S → A: Nonsignificant differences nor in binding affinity neither in lethal dose. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00000449621 – 37Delta-amaurobitoxin-Pl1bAdd BLAST37

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi2 ↔ 181 Publication
Disulfide bondi9 ↔ 231 Publication
Disulfide bondi17 ↔ 331 Publication
Disulfide bondi25 ↔ 311 Publication
Modified residuei37Serine amide1 Publication1

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Structurei

Secondary structure

137
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Turni11 – 13Combined sources3
Beta strandi22 – 24Combined sources3
Beta strandi27 – 30Combined sources4
Beta strandi32 – 34Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V91NMR-A1-37[»]
ProteinModelPortaliP83257.
SMRiP83257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83257.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Knottin

Family and domain databases

InterProiView protein in InterPro
IPR016328. Beta/delta-agatoxin_fam.
PIRSFiPIRSF001882. Curtatoxin. 1 hit.
PROSITEiView protein in PROSITE
PS60015. MU_AGATOXIN. 1 hit.

Sequencei

Sequence statusi: Complete.

P83257-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
ACVGDGQRCA SWSGPYCCDG YYCSCRSMPY CRCRNNS
Length:37
Mass (Da):4,124
Last modified:March 1, 2002 - v1
Checksum:i861E12C2EB547716
GO

Mass spectrometryi

Molecular mass is 4114.6 Da from positions 1 - 37. Determined by MALDI. 1 Publication

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiT3D1B_PIRLC
AccessioniPrimary (citable) accession number: P83257
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: March 1, 2002
Last modified: July 5, 2017
This is version 70 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families