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Protein

Potassium channel toxin alpha-KTx 1.1

Gene
N/A
Organism
Leiurus quinquestriatus hebraeus (Yellow scorpion)
Status
Reviewed-Annotation score: Annotation score: 5 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 (KCa/KCNM), as well as a voltage-dependent potassium channel (Kv1.3/KCNA3). It appears to block channel activity by a simple bimolecular inhibition process.1 Publication
Has a pH-specific antimicrobial activity against bacteria (B.subtilis, E.coli and S.aureus) and the fungus C.albicans.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei49 – 491Basic residue of the functional dyadBy similarity
Sitei58 – 581Aromatic residue of the functional dyadBy similarity

GO - Molecular functioni

  1. ion channel inhibitor activity Source: InterPro

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB-KW
  2. defense response to fungus Source: UniProtKB-KW
  3. killing of cells of other organism Source: UniProtKB-KW
  4. pathogenesis Source: InterPro
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 1.1
Alternative name(s):
ChTX-Lq1
ChTx-a
Charybdotoxin
Short name:
ChTX
OrganismiLeiurus quinquestriatus hebraeus (Yellow scorpion)
Taxonomic identifieri6884 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeLeiurus

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
Signal peptidei1 – 22223 PublicationsAdd
BLAST
Chaini23 – 5937Potassium channel toxin alpha-KTx 1.1PRO_0000035307Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Pyrrolidone carboxylic acid
Disulfide bondi29 ↔ 50
Disulfide bondi35 ↔ 55
Disulfide bondi39 ↔ 57

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1
59
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 343Combined sources
Helixi36 – 427Combined sources
Beta strandi48 – 503Combined sources
Beta strandi52 – 554Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAHNMR-A24-59[»]
1CMRNMR-A29-59[»]
2A9HNMR-E24-59[»]
2CRDNMR-A24-59[»]
4JTAX-ray2.50Y23-59[»]
4JTCX-ray2.56Y23-59[»]
4JTDX-ray2.54Y23-59[»]
ProteinModelPortaliP13487.
SMRiP13487. Positions 23-59.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13487.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 558Interaction 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).

Sequence similaritiesi

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13487-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKILSVLLLA LIICSIVGWS EAQFTNVSCT TSKECWSVCQ RLHNTSRGKC

MNKKCRCYS
Length:59
Mass (Da):6,674
Last modified:November 21, 2003 - v4
Checksum:i379227EBBCB21947
GO

Sequence databases

PIRiA28202. A60963.

Cross-referencesi

Sequence databases

PIRiA28202. A60963.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAHNMR-A24-59[»]
1CMRNMR-A29-59[»]
2A9HNMR-E24-59[»]
2CRDNMR-A24-59[»]
4JTAX-ray2.50Y23-59[»]
4JTCX-ray2.56Y23-59[»]
4JTDX-ray2.54Y23-59[»]
ProteinModelPortaliP13487.
SMRiP13487. Positions 23-59.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP13487.

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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Single abdominal segment.
  2. "Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels."
    Gimenez-Gallego G., Navia M.A., Reuben J.P., Katz G.M., Kaczorowski G.J., Garcia M.L.
    Proc. Natl. Acad. Sci. U.S.A. 85:3329-3333(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-59.
  3. "Charybdotoxin is a new member of the K+ channel toxin family that includes dendrotoxin I and mast cell degranulating peptide."
    Schweitz H., Bidard J.-N., Maes P., Lazdunski M.
    Biochemistry 28:9708-9714(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-59.
  4. "Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2+-activated K+ channels."
    Lucchesi K., Ravindran A., Young H., Moczydlowski E.
    J. Membr. Biol. 109:269-281(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-59.
    Tissue: Venom.
  5. Cited for: SYNTHESIS OF 23-59.
  6. "Synthesis and structural characterization of charybdotoxin, a potent peptidyl inhibitor of the high conductance Ca2(+)-activated K+ channel."
    Sugg E.E., Garcia M.L., Reuben J.P., Patchett A.A., Kaczorowski G.J.
    J. Biol. Chem. 265:18745-18748(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 23-59, DISULFIDE BONDS.
  7. "Moving pieces in a taxonomic puzzle: venom 2D-LC/MS and data clustering analyses to infer phylogenetic relationships in some scorpions from the Buthidae family (Scorpiones)."
    Nascimento D.G., Rates B., Santos D.M., Verano-Braga T., Barbosa-Silva A., Dutra A.A.A., Biondi I., Martin-Eauclaire M.-F., De Lima M.E., Pimenta A.M.C.
    Toxicon 47:628-639(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Multidimensional signatures in antimicrobial peptides."
    Yount N.Y., Yeaman M.R.
    Proc. Natl. Acad. Sci. U.S.A. 101:7363-7368(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Molecular structure of charybdotoxin, a pore-directed inhibitor of potassium ion channels."
    Massefski W. Jr., Redfield A.G., Hare D.R., Miller C.
    Science 249:521-524(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-59, DISULFIDE BONDS.
  10. "Three-dimensional structure of natural charybdotoxin in aqueous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins."
    Bontems F., Roumestand C., Boyot P., Gilquin B., Doljansky Y.
    Eur. J. Biochem. 196:19-28(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-59, DISULFIDE BONDS.
  11. "Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins."
    Bontems F., Roumestand C., Gilquin B., Menez A., Toma F.
    Science 254:1521-1523(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-59, DISULFIDE BONDS.
  12. "Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications."
    Bontems F., Gilquin B., Roumestand C., Menez A., Toma F.
    Biochemistry 31:7756-7764(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-59, DISULFIDE BONDS.
  13. "Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects."
    Bonmatin J.-M., Genest M., Petit M.-C., Gincel E., Simorre J.-P., Cornet B., Gallet X., Caille A., Labbe H., Vovelle F., Ptak M.
    Biochimie 74:825-836(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-59, DISULFIDE BONDS.
  14. "NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing."
    Song J., Gilquin B., Jamin N., Drakopoulou E., Guenneugues M., Dauplais M., Vita C., Menez A.
    Biochemistry 36:3760-3766(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-59, DISULFIDE BONDS.

Entry informationi

Entry nameiKAX11_LEIQH
AccessioniPrimary (citable) accession number: P13487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 21, 2003
Last modified: January 7, 2015
This is version 119 of the entry and version 4 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. Scorpion potassium channel toxins
    Nomenclature of scorpion potassium channel toxins and list of entries
  3. 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.