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P60980

- VSTX1_GRARO

UniProt

P60980 - VSTX1_GRARO

Protein

Kappa-theraphotoxin-Gr3a

Gene
N/A
Organism
Grammostola rosea (Chilean rose tarantula) (Grammostola spatulata)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Inhibits sodium channels Nav1.7/SCN9A and potassium channels Kv11.1/KCNH2. Also binds the voltage-sensor domain of the potassium channel KvAP (from the archaeon Aeropyrum pernix) with very slow apparent binding kinetics and affects channel gating. Reaches its target by dynamically partitioning into anionic or zwitterionic headgroup lipid membranes. May bind to the open state of KvAP.4 Publications

    GO - Molecular functioni

    1. ion channel inhibitor activity Source: InterPro

    GO - Biological processi

    1. pathogenesis Source: InterPro

    Keywords - Molecular functioni

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kappa-theraphotoxin-Gr3a
    Short name:
    Kappa-TRTX-Gr3a
    Alternative name(s):
    Voltage sensor toxin 1
    Short name:
    VsTx1
    OrganismiGrammostola rosea (Chilean rose tarantula) (Grammostola spatulata)
    Taxonomic identifieri432528 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeTheraphosidaeGrammostola

    Organism-specific databases

    ArachnoServeriAS000423. kappa-theraphotoxin-Gr3a.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Peptidei1 – 3434Kappa-theraphotoxin-Gr3aPRO_0000045008Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi2 ↔ 161 Publication
    Disulfide bondi9 ↔ 211 Publication
    Disulfide bondi15 ↔ 281 Publication

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Structurei

    Secondary structure

    1
    34
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 123
    Beta strandi19 – 224
    Turni23 – 264
    Beta strandi27 – 304

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S6XNMR-A1-34[»]
    ProteinModelPortaliP60980.
    SMRiP60980. Positions 1-34.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60980.

    Family & Domainsi

    Domaini

    The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.

    Sequence similaritiesi

    Belongs to the huwentoxin-1 family.Curated

    Keywords - Domaini

    Knottin

    Family and domain databases

    InterProiIPR013140. Huwentoxin_CS1.
    IPR011696. Ion_channel_inhibitory.
    [Graphical view]
    PfamiPF07740. Toxin_12. 1 hit.
    [Graphical view]
    PROSITEiPS60021. HWTX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P60980-1 [UniParc]FASTAAdd to Basket

    « Hide

    ECGKFMWKCK NSNDCCKDLV CSSRWKWCVL ASPF                    34
    Length:34
    Mass (Da):4,004
    Last modified:April 26, 2004 - v1
    Checksum:i800AF52DA953C078
    GO

    Mass spectrometryi

    Molecular mass is 3997.0 Da from positions 1 - 34. 1 Publication

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S6X NMR - A 1-34 [» ]
    ProteinModelPortali P60980.
    SMRi P60980. Positions 1-34.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ArachnoServeri AS000423. kappa-theraphotoxin-Gr3a.

    Miscellaneous databases

    EvolutionaryTracei P60980.

    Family and domain databases

    InterProi IPR013140. Huwentoxin_CS1.
    IPR011696. Ion_channel_inhibitory.
    [Graphical view ]
    Pfami PF07740. Toxin_12. 1 hit.
    [Graphical view ]
    PROSITEi PS60021. HWTX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional analysis of an archaebacterial voltage-dependent K+ channel."
      Ruta V., Jiang Y., Lee A., Chen J., MacKinnon R.
      Nature 422:180-185(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Venom.
    2. "Target promiscuity and heterogeneous effects of tarantula venom peptides affecting Na+ and K+ ion channels."
      Redaelli E., Cassulini R.R., Silva D.F., Clement H., Schiavon E., Zamudio F.Z., Odell G., Arcangeli A., Clare J.J., Alagon A., de la Vega R.C., Possani L.D., Wanke E.
      J. Biol. Chem. 285:4130-4142(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, FUNCTION, TOXIN TARGET.
    3. "A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom."
      Lee S.-Y., MacKinnon R.
      Nature 430:232-235(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "Localization of the voltage-sensor toxin receptor on KvAP."
      Ruta V., MacKinnon R.
      Biochemistry 43:10071-10079(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Tissue: Venom.
    5. "Vstx1, a modifier of Kv channel gating, localizes to the interfacial region of lipid bilayers."
      Bemporad D., Sands Z.A., Wee C.L., Grottesi A., Sansom M.S.
      Biochemistry 45:11844-11855(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel."
      Jung H.J., Lee J.Y., Kim S.H., Eu Y.-J., Shin S.Y., Milescu M., Swartz K.J., Kim J.I.
      Biochemistry 44:6015-6023(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, DISULFIDE BONDS, MEMBRANE-PARTITIONING, SYNTHESIS.

    Entry informationi

    Entry nameiVSTX1_GRARO
    AccessioniPrimary (citable) accession number: P60980
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: April 26, 2004
    Last modified: October 1, 2014
    This is version 46 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Miscellaneous

    Does not inhibit potassium channels Kv1.1/KCNA1 (IC50>200 µM), Kv1.4/KCNA4 (IC50>200 µM), Kv11.2/KCNH6 (IC50=45 µM) and Kv11.3/KCNH7 (IC50=55 µM) and sodium channels Nav1.1/SCN1A, Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.6/SCN8A.1 Publication

    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

    External Data

    Dasty 3