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P01497

- SIX1_ANDAU

UniProt

P01497 - SIX1_ANDAU

Protein

Beta-insect excitatory toxin 1

Gene
N/A
Organism
Androctonus australis (Sahara scorpion)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.

    GO - Molecular functioni

    1. ion channel inhibitor activity Source: InterPro

    GO - Biological processi

    1. defense response Source: InterPro

    Keywords - Molecular functioni

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-insect excitatory toxin 1
    Alternative name(s):
    AaH IT1
    Short name:
    AaH IT
    Short name:
    AaHIT
    Short name:
    AaHIT1
    Short name:
    AaIT1
    OrganismiAndroctonus australis (Sahara scorpion)
    Taxonomic identifieri6858 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeAndroctonus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Toxic dosei

    PD50 is 0.099 ng/mg of insects.1 Publication

    Biotechnological usei

    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).1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18182 PublicationsAdd
    BLAST
    Chaini19 – 8870Beta-insect excitatory toxin 1PRO_0000035187Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 ↔ 551 Publication
    Disulfide bondi40 ↔ 601 Publication
    Disulfide bondi44 ↔ 621 Publication
    Disulfide bondi56 ↔ 821 Publication

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Structurei

    3D structure databases

    ProteinModelPortaliP01497.
    SMRiP01497. Positions 19-88.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P01497-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFLLLFLVV LPIMGVFGKK NGYAVDSSGK APECLLSNYC NNECTKVHYA   50
    DKGYCCLLSC YCFGLNDDKK VLEISDTRKS YCDTTIIN 88
    Length:88
    Mass (Da):9,852
    Last modified:July 21, 1986 - v2
    Checksum:iE6FF097B3277748F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431E → Q AA sequence 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171F → L.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27706 mRNA. Translation: AAA29951.1.
    M27705 mRNA. Translation: AAA29950.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27706 mRNA. Translation: AAA29951.1 .
    M27705 mRNA. Translation: AAA29950.1 .

    3D structure databases

    ProteinModelPortali P01497.
    SMRi P01497. Positions 19-88.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.30.30.10. 1 hit.
    InterProi IPR003614. Scorpion_toxin-like.
    IPR002061. Scorpion_toxinL/defensin.
    [Graphical view ]
    Pfami PF00537. Toxin_3. 1 hit.
    [Graphical view ]
    SMARTi SM00505. Knot1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57095. SSF57095. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiSIX1_ANDAU
    AccessioniPrimary (citable) accession number: P01497
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 90 of the entry and version 2 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