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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 (KCa1.1/KCNMA1 and others), as well as a voltage-dependent potassium channel (Kv1.3/KCNA3>Kv1.2/KCNA2>Kv1.6/KCNA3>>Shaker/Sh) (PubMed:2477548, PubMed:8204618, PubMed:7517498, PubMed:20007782). It blocks channel activity by a simple bimolecular inhibition process.4 Publications
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

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 1.1
Alternative name(s):
ChTX-Lq11 Publication
ChTx-a
Charybdotoxin
Short name:
CTX1 Publication
Short name:
ChTX
OrganismiLeiurus quinquestriatus hebraeus (Yellow scorpion)
Taxonomic identifieri6884 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeLeiurus

Subcellular locationi

GO - Cellular componenti

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 1.13 PublicationsPRO_0000035307Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Pyrrolidone carboxylic acid2 Publications
Disulfide bondi29 ↔ 507 Publications
Disulfide bondi35 ↔ 557 Publications
Disulfide bondi39 ↔ 577 Publications

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, PYROGLUTAMATE FORMATION AT GLN-23.
  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, PYROGLUTAMATE FORMATION AT GLN-23.
  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, FUNCTION, ACTIVITY PROFILE.
    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. "Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom."
    Garcia M.L., Garcia-Calvo M., Hidalgo P., Lee A., Mackinnon R.
    Biochemistry 33:6834-6839(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ACTIVITY PROFILE.
  8. "Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines."
    Grissmer S., Nguyen A.N., Aiyar J., Hanson D.C., Mather R.J., Gutman G.A., Karmilowicz M.J., Auperin D.D., Chandy K.G.
    Mol. Pharmacol. 45:1227-1234(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ACTIVITY PROFILE.
  9. "BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1."
    Zhang M., Korolkova Y.V., Liu J., Jiang M., Grishin E.V., Tseng G.N.
    Biophys. J. 84:3022-3036(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVITY PROFILE.
  10. "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.
  11. Cited for: FUNCTION, ACTIVITY PROFILE.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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: December 9, 2015
This is version 122 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Shows very little or no activity on Kv1.1/KCNA1 (Ki=1500 nM), Kv1.5/KCNA5 (Kd>100 nM), Kv2.1/KCNB1 (Ki= >2000 nM), Kv3.1/KCNC1 (Kd>1000 nM) and Kv11.1/KCNH2/ERG1.3 Publications

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

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.