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Q10726

- KAX61_PANIM

UniProt

Q10726 - KAX61_PANIM

Protein

Potassium channel toxin alpha-KTx 6.1

Gene
N/A
Organism
Pandinus imperator (Emperor scorpion)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Potently and reversibly inhibits the insect voltage-gated Shaker (Sh) potassium channel (isoform alpha (B)), the mammalian voltage-gated potassium channels Kv1.2/KCNA2. Its effect on Kv1.3/KCNA3 is controversial, since this channel is voltage-independently inhibited in PubMed:9464266, but is not affected in PubMed:10931199. Furthermore, this toxin competes with apamin (a small conductance calcium-activated potassium channel inhibitor) for binding onto rat brain synaptosomes.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei5 – 51Part of the basic ring which may anchor to the external vestibule of the K(+) channel
    Sitei12 – 121Part of the basic ring which may anchor to the external vestibule of the K(+) channel
    Sitei24 – 241Basic residue of the functional dyad
    Sitei28 – 281Part of the basic ring which may anchor to the external vestibule of the K(+) channel
    Sitei31 – 311Part of the basic ring which may anchor to the external vestibule of the K(+) channel
    Sitei33 – 331Aromatic residue of the functional dyad

    GO - Molecular functioni

    1. ion channel inhibitor activity Source: InterPro

    GO - Biological processi

    1. defense response Source: InterPro
    2. pathogenesis Source: InterPro

    Keywords - Molecular functioni

    Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Potassium channel toxin alpha-KTx 6.1
    Alternative name(s):
    PiTX-K-gamma
    Potassium channel-blocking toxin 1
    Short name:
    Pi-1
    Short name:
    Pi1
    OrganismiPandinus imperator (Emperor scorpion)
    Taxonomic identifieri55084 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesIuridaScorpionoideaScorpionidaeScorpioninaePandinus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Toxic dosei

    LD50 is 10 µg/kg by intraperitoneal injection into mice.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi5 – 51R → A: 51-fold decrease in inhibiting Kv1.2/KCNA2 channels; when associated with A-12. 479-fold decrease in inhibiting Kv1.2/KCNA2 channels; when associated with A-31. 1 Publication
    Mutagenesisi12 – 121R → A: 51-fold decrease in inhibiting Kv1.2/KCNA2 channels; when associated with A-5. 1 Publication
    Mutagenesisi24 – 241K → A: 500-fold decrease in LD(50), 600-fold decrease of potency in competition assay with apamin, and 17000-fold decrease in inhibiting Kv1.2/KCNA2 channels; when associated with A-33. 1 Publication
    Mutagenesisi31 – 311K → A: 294-fold decrease in inhibiting Kv1.2/KCNA2 channels. 479-fold decrease in inhibiting Kv1.2/KCNA2 channels; when associated with A-5. 1 Publication
    Mutagenesisi33 – 331Y → A: 500-fold decrease in LD(50), 600-fold decrease of potency in competition assay with apamin, and 17,000-fold decrease in inhibiting Kv1.2/KCNA2 channels; when associated with A-24. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Peptidei1 – 3535Potassium channel toxin alpha-KTx 6.1PRO_0000044912Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi4 ↔ 251 Publication
    Disulfide bondi10 ↔ 301 Publication
    Disulfide bondi14 ↔ 321 Publication
    Disulfide bondi20 ↔ 351 Publication

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Structurei

    Secondary structure

    1
    35
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni6 – 105
    Helixi11 – 177
    Beta strandi24 – 263
    Beta strandi29 – 313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WZ5NMR-A1-35[»]
    ProteinModelPortaliQ10726.
    SMRiQ10726. Positions 1-34.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ10726.

    Family & Domainsi

    Domaini

    Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).
    The alpha-helical domain may play a key role in the recognition of SK channels.
    The beta-sheet structure may be involved in bioactivity on Kv channels.

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.30.30.10. 1 hit.
    InterProiIPR003614. Scorpion_toxin-like.
    IPR001947. Scorpion_toxinS_K_inh.
    [Graphical view]
    PfamiPF00451. Toxin_2. 1 hit.
    [Graphical view]
    ProDomiPD003586. Scorpion_toxinS. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF57095. SSF57095. 1 hit.
    PROSITEiPS01138. SCORP_SHORT_TOXIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q10726-1 [UniParc]FASTAAdd to Basket

    « Hide

    LVKCRGTSDC GRPCQQQTGC PNSKCINRMC KCYGC                   35
    Length:35
    Mass (Da):3,843
    Last modified:October 1, 1996 - v1
    Checksum:i208001C82B2C9800
    GO

    Sequence databases

    PIRiS69599.

    Cross-referencesi

    Sequence databases

    PIRi S69599.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WZ5 NMR - A 1-35 [» ]
    ProteinModelPortali Q10726.
    SMRi Q10726. Positions 1-34.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q10726.

    Family and domain databases

    Gene3Di 3.30.30.10. 1 hit.
    InterProi IPR003614. Scorpion_toxin-like.
    IPR001947. Scorpion_toxinS_K_inh.
    [Graphical view ]
    Pfami PF00451. Toxin_2. 1 hit.
    [Graphical view ]
    ProDomi PD003586. Scorpion_toxinS. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF57095. SSF57095. 1 hit.
    PROSITEi PS01138. SCORP_SHORT_TOXIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel structural class of K+-channel blocking toxin from the scorpion Pandinus imperator."
      Olamendi-Portugal T., Gomez-Lagunas F., Gurrola G.B., Possani L.D.
      Biochem. J. 315:977-981(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, TOXIN TARGET, DISULFIDE BONDS.
      Tissue: Venom.
    2. "Three new toxins from the scorpion Pandinus imperator selectively block certain voltage-gated K+ channels."
      Rogowski R.S., Collins J.H., O'Neill T.J., Gustafson T.A., Werkman T.R., Rogawski M.A., Tenenholz T.C., Weber D.J., Blaustein M.P.
      Mol. Pharmacol. 50:1167-1177(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Venom.
    3. "Block of ShakerB K+ channels by Pi1, a novel class of scorpion toxin."
      Gomez-Lagunas F., Olamendi-Portugal T., Possani L.D.
      FEBS Lett. 400:197-200(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TOXIN TARGET.
    4. "Pandinus imperator scorpion venom blocks voltage-gated K+ channels in human lymphocytes."
      Peter M. Jr., Varga Z., Panyi G., Bene L., Damjanovich S., Pieri C., Possani L.D., Gaspar R. Jr.
      Biochem. Biophys. Res. Commun. 242:621-625(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TOXIN TARGET.
    5. "Chemical synthesis and characterization of Pi1, a scorpion toxin from Pandinus imperator active on K+ channels."
      Fajloun Z., Carlier E., Lecomte C., Geib S., Di Luccio E., Bichet D., Mabrouk K., Rochat H., De Waard M., Sabatier J.M.
      Eur. J. Biochem. 267:5149-5155(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TOXIN TARGET, LETHAL DOSE, SYNTHESIS.
    6. "The 'functional' dyad of scorpion toxin Pi1 is not itself a prerequisite for toxin binding to the voltage-gated Kv1.2 potassium channels."
      Mouhat S., Mosbah A., Visan V., Wulff H., Delepierre M., Darbon H., Grissmer S., De Waard M., Sabatier J.M.
      Biochem. J. 377:25-36(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-5; ARG-12; LYS-24; LYS-31 AND TYR-33, SITES.
    7. "A novel potassium channel blocking toxin from the scorpion Pandinus imperator: a 1H NMR analysis using a nano-NMR probe."
      Delepierre M., Prochnicka-Chalufour A., Possani L.D.
      Biochemistry 36:2649-2658(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.
    8. "The impact of the fourth disulfide bridge in scorpion toxins of the alpha-KTx6 subfamily."
      Carrega L., Mosbah A., Ferrat G., Beeton C., Andreotti N., Mansuelle P., Darbon H., De Waard M., Sabatier J.M.
      Proteins 61:1010-1023(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

    Entry informationi

    Entry nameiKAX61_PANIM
    AccessioniPrimary (citable) accession number: Q10726
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Miscellaneous

    Pi1 analog that is synthesized with a phosphorylation at Tyr-33 (P-Pi1) suffers a 200-fold decrease in LD50, a 200-fold decrease of potency in competition assay with apamin, and a 58-fold decrease in inhibiting Kv1.2/KCNA2 channels.
    This toxin has no effect on Kv1.1/KCNA1.1 Publication

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Scorpion potassium channel toxins
      Nomenclature of scorpion potassium channel toxins and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3