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P82228

- TJT1C_HADVE

UniProt

P82228 - TJT1C_HADVE

Protein

Kappa-hexatoxin-Hv1c

Gene
N/A
Organism
Hadronyche versuta (Blue mountains funnel-web spider) (Atrax versutus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    This excitatory toxin inhibits insect calcium-activated potassium channels (Slo-type). Pan-neuronal expression in Drosophila is lethal but flies engineered to express the toxin only in clock neurons have defects in circadian rhythm but a normal lifespan.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei2 – 21Important for the neurotoxic activity
    Sitei8 – 81Critical for the neurotoxic activity
    Sitei9 – 91Critical for the neurotoxic activity
    Sitei13 – 131Critical for the neurotoxic activity
    Sitei14 – 141Critical for the neurotoxic activity
    Sitei29 – 291Important for the neurotoxic activity
    Sitei31 – 311Critical for the neurotoxic activity

    GO - Biological processi

    1. pathogenesis Source: InterPro

    Keywords - Molecular functioni

    Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kappa-hexatoxin-Hv1c
    Short name:
    Kappa-HXTX-Hv1c
    Alternative name(s):
    Janus-atracotoxin-Hv1c
    Short name:
    Janus-AcTx-Hv1c
    Kappa-atracotoxin-Hv1c
    Short name:
    Kappa-AcTx-Hv1c
    OrganismiHadronyche versuta (Blue mountains funnel-web spider) (Atrax versutus)
    Taxonomic identifieri6904 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeHexathelidaeHadronyche

    Organism-specific databases

    ArachnoServeriAS000174. kappa-hexatoxin-Hv1c.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Toxic dosei

    LD50 of recombinant toxin is 320 +-20 pmol/g (according to PubMed:11937509) or 91 +-5 pmol/g (according to PubMed:12220722) when injected into house flies (Musca domestica).2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 22Missing: 73-fold decrease in toxicity to flies. 1 Publication
    Mutagenesisi1 – 11Missing: No change in toxicity. 1 Publication
    Mutagenesisi2 – 21I → A: 7-fold decrease in toxicity to flies. 1 Publication
    Mutagenesisi8 – 81R → A: 98-fold decrease in toxicity to flies. 1 Publication
    Mutagenesisi8 – 81R → E: 270-fold decrease in toxicity to flies. 1 Publication
    Mutagenesisi9 – 91P → A: 269-fold decrease in toxicity to flies. 1 Publication
    Mutagenesisi13 – 142CC → SS: 423-fold decrease in toxicity to flies.
    Mutagenesisi29 – 291V → A: 13-fold decrease in toxicity to flies. 1 Publication
    Mutagenesisi31 – 311Y → A: 162-fold decrease in toxicity to flies. 1 Publication
    Mutagenesisi31 – 311Y → F: 1.8-fold decrease in toxicity to flies. 1 Publication
    Mutagenesisi35 – 373Missing: No change in toxicity to flies.
    Mutagenesisi36 – 372Missing: No change in toxicity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Peptidei1 – 3737Kappa-hexatoxin-Hv1cPRO_0000044998Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi3 ↔ 17
    Disulfide bondi10 ↔ 22
    Disulfide bondi13 ↔ 14
    Disulfide bondi16 ↔ 32

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Structurei

    Secondary structure

    1
    37
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 245
    Beta strandi30 – 345

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DL0NMR-A1-37[»]
    ProteinModelPortaliP82228.
    SMRiP82228. Positions 1-37.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP82228.

    Family & Domainsi

    Domaini

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

    Sequence similaritiesi

    Belongs to the janus-atracotoxin family.Curated

    Keywords - Domaini

    Knottin

    Family and domain databases

    InterProiIPR012499. Toxin_16.
    [Graphical view]
    PfamiPF07945. Toxin_16. 1 hit.
    [Graphical view]
    PROSITEiPS60020. J_ACTX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P82228-1 [UniParc]FASTAAdd to Basket

    « Hide

    AICTGADRPC AACCPCCPGT SCKAESNGVS YCRKDEP                 37
    Length:37
    Mass (Da):3,768
    Last modified:May 30, 2000 - v1
    Checksum:iE4DDF046CC750FFC
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DL0 NMR - A 1-37 [» ]
    ProteinModelPortali P82228.
    SMRi P82228. Positions 1-37.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ArachnoServeri AS000174. kappa-hexatoxin-Hv1c.

    Miscellaneous databases

    EvolutionaryTracei P82228.

    Family and domain databases

    InterProi IPR012499. Toxin_16.
    [Graphical view ]
    Pfami PF07945. Toxin_16. 1 hit.
    [Graphical view ]
    PROSITEi PS60020. J_ACTX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge."
      Wang X.-H., Connor M., Smith R., Maciejewski M.W., Howden M.E.H., Nicholson G.M., Christie M.J., King G.F.
      Nat. Struct. Biol. 7:505-513(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, STRUCTURE BY NMR.
      Tissue: Venom.
    2. "Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function."
      Maggio F., King G.F.
      J. Biol. Chem. 277:22806-22813(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ILE-2; ARG-8; PRO-9; 13-CYS-CYS-14; VAL-29 AND TYR-31, LETHAL DOSE.
    3. "Role of the structurally disordered N- and C-terminal residues in the Janus-faced atracotoxins."
      Maggio F., King G.F.
      Toxicon 40:1355-1361(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ALA-1; 1-ALA-ILE-2 AND 36-GLU-PRO-37, LETHAL DOSE.
    4. "A model genetic system for testing the in vivo function of peptide toxins."
      Tedford H.W., Maggio F., Reenan R.A., King G.
      Peptides 28:51-56(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Phase coupling of a circadian neuropeptide with rest/activity rhythms detected using a membrane-tethered spider toxin."
      Wu Y., Cao G., Pavlicek B., Luo X., Nitabach M.N.
      PLoS Biol. 6:E273-E273(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels."
      Gunning S.J., Maggio F., Windley M.J., Valenzuela S.M., King G.F., Nicholson G.M.
      FEBS J. 275:4045-4059(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiTJT1C_HADVE
    AccessioniPrimary (citable) accession number: P82228
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 60 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

    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