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P13487 (KAX11_LEIQH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Potassium channel toxin alpha-KTx 1.1
Alternative name(s):
ChTX-Lq1
ChTx-a
Charybdotoxin
Short name=ChTX
OrganismLeiurus quinquestriatus hebraeus (Yellow scorpion)
Taxonomic identifier6884 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeLeiurus

Protein attributes

Sequence length59 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Has a pH-specific antimicrobial activity against bacteria (B.subtilis, E.coli and S.aureus) and the fungus C.albicans. Ref.8

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Domain

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

Sequence similarities

Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.2 Ref.3 Ref.4
Chain23 – 5937Potassium channel toxin alpha-KTx 1.1
PRO_0000035307

Regions

Region48 – 558Interaction with Ca(2+)-activated K(+) channels Potential

Sites

Site491Basic residue of the functional dyad By similarity
Site581Aromatic residue of the functional dyad By similarity

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid
Disulfide bond29 ↔ 50 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Disulfide bond35 ↔ 55 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Disulfide bond39 ↔ 57 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Secondary structure

......... 59
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13487 [UniParc].

Last modified November 21, 2003. Version 4.
Checksum: 379227EBBCB21947

FASTA596,674
        10         20         30         40         50 
MKILSVLLLA LIICSIVGWS EAQFTNVSCT TSKECWSVCQ RLHNTSRGKC MNKKCRCYS 

« Hide

References

[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]"Solution synthesis of charybdotoxin (ChTX), a K+ channel blocker."
Lambert P., Kuroda H., Chino N., Watanabe T.X., Kimura T., Sakakibara S.
Biochem. Biophys. Res. Commun. 170:684-690(1990) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA60963. A28202.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAHNMR-A24-59[»]
1CMRNMR-A29-46[»]
2CRDNMR-A24-59[»]
4JTAX-ray2.50Y24-59[»]
4JTCX-ray2.56Y24-59[»]
4JTDX-ray2.54Y24-59[»]
ProteinModelPortalP13487.
SMRP13487. Positions 23-59.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.30.10. 1 hit.
InterProIPR003614. Scorpion_toxin-like.
IPR001947. Scorpion_toxinS_K_inh.
[Graphical view]
PfamPF00451. Toxin_2. 1 hit.
[Graphical view]
PRINTSPR00286. CHARYBDTOXIN.
ProDomPD003586. Scorpion_toxinS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF57095. SSF57095. 1 hit.
PROSITEPS01138. SCORP_SHORT_TOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13487.

Entry information

Entry nameKAX11_LEIQH
AccessionPrimary (citable) accession number: P13487
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 21, 2003
Last modified: October 16, 2013
This is version 113 of the entry and version 4 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

Scorpion potassium channel toxins

Nomenclature of scorpion potassium channel toxins and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references