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Protein

Alpha-toxin OD1

Gene
N/A
Organism
Odontobuthus doriae (Yellow Iranian scorpion)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. Mammalian sodium channels Nav1.7/SCN9A (EC(50)=4.5 nM), Nav1.4/SCN4A (EC(50)=9.6 nM), Nav1.6/SCN8A (EC(50)=30 nM) Nav1.5/SCN5A (only at micromolar concentrations), and insect sodium channel para/tipE (EC(50)=80 nM) are affected by this toxin.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei6Important for toxin potency but not for selectivity for individual Nav channel subtype (Nav1.6 and Nav1.7)1

GO - Molecular functioni

  • sodium channel inhibitor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-toxin OD1
OrganismiOdontobuthus doriae (Yellow Iranian scorpion)
Taxonomic identifieri342590 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeOdontobuthus

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi6Y → F: Decrease in potency of about 10-fold, without affecting the selectivity for Nav1.4, Nav1.6 and Nav1.7. 1 Publication1
Mutagenesisi9 – 11DDK → KPH: Increase in potency for Nav1.4 (1.6-fold) and Nav1.7 (2.3-fold) and decrease in potency for Nav1.6 (fold), resulting in a 40-fold increase of selectivity for Nav1.7 over Nav1.6. No change in potency for Nav1.4 and Nav1.6, and important increase in potency for Nav1.7 (11.7-fold); when associated with A-55. 1 Publication3
Mutagenesisi11K → V: Increase in potency for Nav1.4 (5-fold) and Nav1.6 (7.8-fold) and decrease in potency for Nav1.7 (4.3-fold), resulting in a 5-fold increase of selectivity for Nav1.6 over Nav1.7. Increase in potency for Nav1.6 (16-fold), no change in potency for Nav1.7, and decrease in potency for Nav1.4 (1.6-fold); when associated with A-55. 1 Publication1
Mutagenesisi51K → A: No change in potency for Nav1.4, Nav1.6 and Nav1.7. 1 Publication1
Mutagenesisi55E → A: No change in potency for Nav1.4 and Nav1.7, and important decrease in potency for Nav1.6 (2.3-fold), resulting in a 13-fold increase of selectivity for Nav1.4 and Nav1.7 over Nav1.6. No change in potency for Nav1.4; Nav1.6, and important increase in potency for Nav1.7 (11.7-fold); when associated with 9-K--H-11. Increase in potency for Nav1.6 (16-fold), no change in potency for Nav1.7, and decrease in potency for Nav1.4 (1.6-fold); when associated with V-11. 1 Publication1
Mutagenesisi55E → H: No change in potency for Nav1.4 and Nav1.7, and decrease in potency for Nav1.6 (1.7-fold). 1 Publication1
Mutagenesisi60I → G: No change in potency for Nav1.4, and decrease in potency for Nav1.6 (1.6-fold) and Nav1.7 (2.6-fold). 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000667881 – 65Alpha-toxin OD1Add BLAST65

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi13 ↔ 641 Publication
Disulfide bondi17 ↔ 371 Publication
Disulfide bondi23 ↔ 471 Publication
Disulfide bondi27 ↔ 491 Publication
Modified residuei65Arginine amide1 Publication1

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Structurei

Secondary structure

165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Helixi20 – 29Combined sources10
Beta strandi33 – 39Combined sources7
Helixi41 – 43Combined sources3
Beta strandi45 – 53Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HHFX-ray1.80A1-65[»]
ProteinModelPortaliP84646.
SMRiP84646.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi9 – 11Important for toxin selectivity for individual Nav channel subtype (Nav1.6 and Nav1.7), but not for toxin potency3

Sequence similaritiesi

Family and domain databases

Gene3Di3.30.30.10. 1 hit.
InterProiIPR003614. Scorpion_toxin-like.
IPR018218. Scorpion_toxinL.
IPR002061. Scorpion_toxinL/defensin.
[Graphical view]
PfamiPF00537. Toxin_3. 1 hit.
[Graphical view]
PRINTSiPR00285. SCORPNTOXIN.
SMARTiSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMiSSF57095. SSF57095. 1 hit.

Sequencei

Sequence statusi: Complete.

P84646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GVRDAYIADD KNCVYTCASN GYCNTECTKN GAESGYCQWI GRYGNACWCI
60
KLPDEVPIRI PGKCR
Length:65
Mass (Da):7,215
Last modified:October 11, 2005 - v1
Checksum:iFF76362F0C7ACCE7
GO

Mass spectrometryi

Molecular mass is 7204.8 Da from positions 1 - 65. Determined by MALDI. With amidation.1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HHFX-ray1.80A1-65[»]
ProteinModelPortaliP84646.
SMRiP84646.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.30.10. 1 hit.
InterProiIPR003614. Scorpion_toxin-like.
IPR018218. Scorpion_toxinL.
IPR002061. Scorpion_toxinL/defensin.
[Graphical view]
PfamiPF00537. Toxin_3. 1 hit.
[Graphical view]
PRINTSiPR00285. SCORPNTOXIN.
SMARTiSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMiSSF57095. SSF57095. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSCX1_ODODO
AccessioniPrimary (citable) accession number: P84646
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: November 2, 2016
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Mammalian sodium channels Nav1.2/SCN2A, Nav1.3/SCN3A, and Nav1.8/SCN10A are unaffected by high concentrations (PubMed:16038905 and PubMed:16641312).

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

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.