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Protein

Potassium channel toxin alpha-KTx 1.13

Gene
N/A
Organism
Leiurus quinquestriatus hebraeus (Yellow scorpion)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Potent selective inhibitor of high conductance (maxi-K), different medium and small conductance calcium-activated potassium channels (KCa1.1/KCNMA1 and others), as well as a voltage-dependent potassium channel (Kv1.3/KCNA3>Kv1.2/KCNA2>Kv1.6/KCNA3>>Shaker/Sh). It blocks channel activity by a simple bimolecular inhibition process.By similarity
Has a pH-specific antimicrobial activity against bacteria (B.subtilis, E.coli and S.aureus) and the fungus C.albicans.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei27 – 271Basic residue of the functional dyadBy similarity
Sitei36 – 361Aromatic residue of the functional dyadBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Calcium-activated potassium channel impairing toxin, Fungicide, Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium channel toxin alpha-KTx 1.13
Alternative name(s):
Charybdotoxin c1 Publication
Short name:
ChTx-c1 Publication
OrganismiLeiurus quinquestriatus hebraeus (Yellow scorpion)
Taxonomic identifieri6884 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeLeiurus

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3737Potassium channel toxin alpha-KTx 1.13PRO_0000044892Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acidBy similarity
Disulfide bondi7 ↔ 28By similarity
Disulfide bondi13 ↔ 33By similarity
Disulfide bondi17 ↔ 35By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Expressed by the venom gland.Curated

Structurei

3D structure databases

ProteinModelPortaliP59944.
SMRiP59944. Positions 1-37.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 338Interaction with Ca(2+)-activated K(+) channelsSequence analysis

Domaini

Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).By similarity

Sequence similaritiesi

Family and domain databases

Gene3Di3.30.30.10. 1 hit.
InterProiIPR003614. Scorpion_toxin-like.
IPR001947. Scorpion_toxinS_K_inh.
[Graphical view]
PfamiPF00451. Toxin_2. 1 hit.
[Graphical view]
PRINTSiPR00286. CHARYBDTOXIN.
ProDomiPD003586. Scorpion_toxinS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57095. SSF57095. 1 hit.
PROSITEiPS01138. SCORP_SHORT_TOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P59944-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
QFTNVSCTTS KECWSVCEKL YNTSRGKCMN KKCRCYS
Length:37
Mass (Da):4,318
Last modified:October 31, 2003 - v1
Checksum:i29319BCB43994EE2
GO

Cross-referencesi

3D structure databases

ProteinModelPortaliP59944.
SMRiP59944. Positions 1-37.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.30.10. 1 hit.
InterProiIPR003614. Scorpion_toxin-like.
IPR001947. Scorpion_toxinS_K_inh.
[Graphical view]
PfamiPF00451. Toxin_2. 1 hit.
[Graphical view]
PRINTSiPR00286. CHARYBDTOXIN.
ProDomiPD003586. Scorpion_toxinS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57095. SSF57095. 1 hit.
PROSITEiPS01138. SCORP_SHORT_TOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Dynamic diversification from a putative common ancestor of scorpion toxins affecting sodium, potassium, and chloride channels."
    Froy O., Sagiv T., Poreh M., Urbach D., Zilberberg N., Gurevitz M.
    J. Mol. Evol. 48:187-196(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Venom.

Entry informationi

Entry nameiKAX1D_LEIQH
AccessioniPrimary (citable) accession number: P59944
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 31, 2003
Last modified: January 20, 2016
This is version 47 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

Direct protein sequencing

Documents

  1. Scorpion potassium channel toxins
    Nomenclature of scorpion potassium channel toxins and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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.