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P01497 (SIX1_ANDAU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-insect excitatory toxin 1
Alternative name(s):
AaH IT1
Short name=AaH IT
Short name=AaHIT
Short name=AaHIT1
Short name=AaIT1
OrganismAndroctonus australis (Sahara scorpion)
Taxonomic identifier6858 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeAndroctonus

Protein attributes

Sequence length88 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Excitatory insect beta-toxins induce a spastic paralysis. They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active only on insects.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Toxic dose

PD50 is 0.099 ng/mg of insects. Ref.2

Biotechnological use

Could be used to reinforce the natural insecticidal ability of baculoviruses. The insertion of the gene coding for AaHIT causes a higher killing speed of insects by the baculovirus (particularly against lepidopterans). Ref.4

Sequence similarities

Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionIon channel impairing toxin
Neurotoxin
Toxin
Voltage-gated sodium channel impairing toxin
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processdefense response

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionion channel inhibitor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.2 Ref.3
Chain19 – 8870Beta-insect excitatory toxin 1
PRO_0000035187

Amino acid modifications

Disulfide bond34 ↔ 55 Ref.5
Disulfide bond40 ↔ 60 Ref.5
Disulfide bond44 ↔ 62 Ref.5
Disulfide bond56 ↔ 82 Ref.5

Natural variations

Natural variant171F → L.

Experimental info

Sequence conflict431E → Q AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P01497 [UniParc].

Last modified July 21, 1986. Version 2.
Checksum: E6FF097B3277748F

FASTA889,852
        10         20         30         40         50         60 
MKFLLLFLVV LPIMGVFGKK NGYAVDSSGK APECLLSNYC NNECTKVHYA DKGYCCLLSC 

        70         80 
YCFGLNDDKK VLEISDTRKS YCDTTIIN 

« Hide

References

[1]"Precursors of Androctonus australis scorpion neurotoxins. Structures of precursors, processing outcomes, and expression of a functional recombinant toxin II."
Bougis P.E., Rochat H., Smith L.A.
J. Biol. Chem. 264:19259-19265(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Hector.
[2]"Neurotoxins active on insects: amino acid sequences, chemical modifications, and secondary structure estimation by circular dichroism of toxins from the scorpion Androctonus australis hector."
Loret E.P., Mansuelle P., Rochat H., Granier C.
Biochemistry 29:1492-1501(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-88, PARALYTIC DOSE.
Strain: Hector.
Tissue: Venom.
[3]"Covalent structure of the insect toxin of Androctonus australis hector."
Darbon H., Rochat H., Kopeyan C., van Rietschoten J., Zlotkin E.
Toxicon 20:64-64(1982)
Cited for: PROTEIN SEQUENCE OF 19-88.
Strain: Hector.
Tissue: Venom.
[4]"AaIT: from neurotoxin to insecticide."
Zlotkin E., Fishman Y., Elazar M.
Biochimie 82:869-881(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOTECHNOLOGY, REVIEW.
[5]"Two-dimensional 1H nuclear magnetic resonance study of AaH IT, an anti-insect toxin from the scorpion Androctonus australis hector. Sequential resonance assignments and folding of the polypeptide chain."
Darbon H., Weber C., Braun W.
Biochemistry 30:1836-1845(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.
Strain: Hector.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27706 mRNA. Translation: AAA29951.1.
M27705 mRNA. Translation: AAA29950.1.

3D structure databases

ProteinModelPortalP01497.
SMRP01497. Positions 19-88.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.30.10. 1 hit.
InterProIPR003614. Scorpion_toxin-like.
IPR002061. Scorpion_toxinL/defensin.
[Graphical view]
PfamPF00537. Toxin_3. 1 hit.
[Graphical view]
SMARTSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMSSF57095. SSF57095. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSIX1_ANDAU
AccessionPrimary (citable) accession number: P01497
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 19, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families