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Protein

Kappa-theraphotoxin-Gr3a

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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 123Combined sources
Beta strandi19 – 224Combined sources
Turni23 – 264Combined sources
Beta strandi27 – 304Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S6XNMR-A1-34[»]
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

        10         20         30 
ECGKFMWKCK NSNDCCKDLV CSSRWKWCVL ASPF
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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S6XNMR-A1-34[»]
SMRiP60980. Positions 1-34.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ArachnoServeriAS000423. kappa-theraphotoxin-Gr3a.

Miscellaneous databases

EvolutionaryTraceiP60980.

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]
ProtoNetiSearch...

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: April 1, 2015
This is version 49 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.