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Protein

Potassium channel toxin kappa-KTx 1.1

Gene
N/A
Organism
Heterometrus fulvipes (Indian black scorpion)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Slows the activation kinetics of Kv1.3/KCNA3 currents, and blocks Kv1.3/KCNA3 and Kv1.2/KCNA2 potassium channels. This block is dose-dependent, voltage-independent, and reversible.1 Publication

Miscellaneous

This toxin does not have effect on Kv1.1/KCNA1 currents.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei5Aromatic residue of the functional dyad1 Publication1
Sitei19Basic residue of the functional dyad1 Publication1

GO - Biological processi

Keywordsi

Molecular functionIon channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin

Protein family/group databases

TCDBi8.B.2.1.1. the short scorpion toxin (s-st) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium channel toxin kappa-KTx 1.11 Publication
Alternative name(s):
Kappa-hefutoxin-11 Publication
Short name:
Kappa-HfTx11 Publication
OrganismiHeterometrus fulvipes (Indian black scorpion)
Taxonomic identifieri141248 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesIuridaScorpionoideaScorpionidaeScorpioninaeHeterometrus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi5Y → A: Loss of ability to block potassium channels. Same effect observed; when associated with A-19. 1 Publication1
Mutagenesisi19K → A: Loss of ability to block potassium channels. Same effect observed; when associated with A-5. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00000445441 – 22Potassium channel toxin kappa-KTx 1.11 PublicationAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi4 ↔ 221 Publication
Disulfide bondi8 ↔ 181 Publication
Modified residuei22Cysteine amide1 Publication1

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Structurei

Secondary structure

122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 6Combined sources3
Helixi7 – 12Combined sources6
Helixi17 – 21Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HP9NMR-A1-22[»]
SMRiP82850.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP82850.

Family & Domainsi

Domaini

Has the structural arrangement of two alpha-helices stabilized by two disulfide bonds (CSalpha/alpha 2(S-S)).1 Publication

Sequence similaritiesi

Family and domain databases

InterProiView protein in InterPro
IPR012630. Toxin_25.
PfamiView protein in Pfam
PF08095. Toxin_25. 1 hit.

Sequencei

Sequence statusi: Complete.

P82850-1 [UniParc]FASTAAdd to basket

« Hide

        10         20 
GHACYRNCWR EGNDEETCKE RC
Length:22
Mass (Da):2,660
Last modified:March 1, 2001 - v1
Checksum:i8FB555EB877C6E98
GO

Mass spectrometryi

Molecular mass is 2655.4±0.2 Da from positions 1 - 22. Determined by ESI. 1 Publication

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 one 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.

Entry informationi

Entry nameiKKX11_HETFU
AccessioniPrimary (citable) accession number: P82850
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: March 1, 2001
Last modified: July 5, 2017
This is version 69 of the entry and version 1 of the sequence. See 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. Scorpion potassium channel toxins
    Nomenclature of scorpion potassium channel toxins and list of entries
  3. SIMILARITY comments
    Index of protein domains and families