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Protein

Alpha-insect toxin BotIT1

Gene
N/A
Organism
Buthus occitanus tunetanus (Common European scorpion)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This contractive toxin is highly toxic to insects and barely toxic to mammals.

GO - Molecular functioni

  1. ATP-activated nucleotide receptor activity Source: BHF-UCL
  2. ion channel inhibitor activity Source: InterPro

GO - Biological processi

  1. adenosine receptor signaling pathway Source: GOC
  2. defense response Source: InterPro
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-insect toxin BotIT1
OrganismiButhus occitanus tunetanus (Common European scorpion)
Taxonomic identifieri6871 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeButhus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 50 µg/kg in mouse by intracerebroventricular injection and 600 ng/g in Blattella germanica.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6565Alpha-insect toxin BotIT1PRO_0000066713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi12 ↔ 63By similarity
Disulfide bondi16 ↔ 36By similarity
Disulfide bondi22 ↔ 46By similarity
Disulfide bondi26 ↔ 48By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

3D structure databases

ProteinModelPortaliP55902.
SMRiP55902. Positions 1-64.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.

P55902-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VRDAYIAQNY NCVYFCMKDD YCNDLCTKNG ASSGYCQWAG KYGNACWCYA
60
LPDNVPIRIP GKCHS
Length:65
Mass (Da):7,343
Last modified:October 31, 1997 - v1
Checksum:i93A1371D877D7123
GO

Mass spectrometryi

Molecular mass is 7334.93±0.23 Da from positions 1 - 65. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

ProteinModelPortaliP55902.
SMRiP55902. Positions 1-64.
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...

Publicationsi

  1. "Purification, structure and activity of three insect toxins from Buthus occitanus tunetanus venom."
    Borchani L., Stankiewicz M., Kopeyan C., Mansuelle P., Kharrat R., Cestele S., Karoui H., Rochat H., Pelhate M., el Ayeb M.
    Toxicon 35:365-382(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, LETHAL DOSE, MASS SPECTROMETRY.
    Tissue: Venom.

Entry informationi

Entry nameiSIX1_BUTOC
AccessioniPrimary (citable) accession number: P55902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: October 31, 1997
Last modified: January 6, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.