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P60980 (VSTX1_GRARO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kappa-theraphotoxin-Gr3a

Short name=Kappa-TRTX-Gr3a
Alternative name(s):
Voltage sensor toxin 1
Short name=VsTx1
OrganismGrammostola rosea (Chilean rose tarantula) (Grammostola spatulata)
Taxonomic identifier432528 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeTheraphosidaeGrammostola

Protein attributes

Sequence length34 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.3 Ref.4 Ref.5

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Domain

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

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 (Ref.2).

Sequence similarities

Belongs to the huwentoxin-1 family.

Mass spectrometry

Molecular mass is 3997.0 Da from positions 1 - 34. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 3434Kappa-theraphotoxin-Gr3a
PRO_0000045008

Amino acid modifications

Disulfide bond2 ↔ 16 Ref.6
Disulfide bond9 ↔ 21 Ref.6
Disulfide bond15 ↔ 28 Ref.6

Secondary structure

....... 34
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60980 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: 800AF52DA953C078

FASTA344,004
        10         20         30 
ECGKFMWKCK NSNDCCKDLV CSSRWKWCVL ASPF 

« Hide

References

[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.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S6XNMR-A1-34[»]
ProteinModelPortalP60980.
SMRP60980. Positions 1-34.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ArachnoServerAS000423. kappa-theraphotoxin-Gr3a.

Family and domain databases

InterProIPR013140. Huwentoxin_CS1.
IPR011696. Ion_channel_inhibitory.
[Graphical view]
PfamPF07740. Toxin_12. 1 hit.
[Graphical view]
PROSITEPS60021. HWTX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60980.

Entry information

Entry nameVSTX1_GRARO
AccessionPrimary (citable) accession number: P60980
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: April 16, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references