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Reviewed, UniProtKB/Swiss-Prot P58498 (KAX64_PANIM)

Last modified June 16, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Potassium channel toxin alpha-KTx 6.4
Alternative name(s):
    Potassium channel-blocking toxin 4
      Short name=Pi-4
      Short name=Pi4
OrganismPandinus imperator (Emperor scorpion)
Taxonomic identifier55084 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaChelicerataArachnidaScorpionesIuridaScorpionoideaScorpionidaeScorpioninaePandinus

Protein attributes

Sequence length38 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Potently blocks voltage-gated potassium channel Kv1.2 (KCNA2) and Shaker B (Sh) (complete and reversible), whereas has no effect on voltage-gated potassium channel Kv1.1 (KCNA1) and Kv1.3 (KCNA3). Also blocks small conductance calcium-activated potassium channel (KCNN). Ref.2

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Toxic dose

LD50 is 10 µg/kg by intracerebroventricular injection into mice. Ref.2

Sequence similarities

Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 6 subfamily.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionIonic channel inhibitor
Potassium channel inhibitor
Toxin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpotassium channel inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 3838Potassium channel toxin alpha-KTx 6.4
PRO_0000044913

Sites

Site101Important for the interaction with KCNA2 channel
Site191Important for the interaction with KCNA2 channel
Site261Important for the interaction with KCNA2 channel
Site281Important for the interaction with KCNA2 channel
Site301Important for the interaction with KCNA2 channel
Site331Important for the interaction with KCNA2 channel
Site351Important for the interaction with KCNA2 channel

Amino acid modifications

Disulfide bond6 ↔ 27 Ref.2 Ref.3
Disulfide bond12 ↔ 32 Ref.2 Ref.3
Disulfide bond16 ↔ 34 Ref.2 Ref.3
Disulfide bond22 ↔ 37 Ref.2 Ref.3

Secondary structure

....... 38
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P58498-1 [UniParc].

Last modified December 19, 2001. Version 1.
Checksum: 1C1F402B8DF2EEFF

FASTA384,188
        10         20         30 
IEAIRCGGSR DCYRPCQKRT GCPNAKCINK TCKCYGCS 

« Hide

References

[1]"Two similar peptides from the venom of the scorpion Pandinus imperator, one highly effective blocker and the other inactive on K+ channels."
Olamendi-Portugal T., Gomez-Lagunas F., Gurrola G.B., Possani L.D.
Toxicon 36:759-770(1998) [PubMed: 9655636] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Synthesis and characterization of Pi4, a scorpion toxin from Pandinus imperator that acts on K+ channels."
M'Barek S., Mosbah A., Sandoz G., Fajloun Z., Olamendi-Portugal T., Rochat H., Sampieri F., Guijarro J.I., Mansuelle P., Delepierre M., De Waard M., Sabatier J.-M.
Eur. J. Biochem. 270:3583-3592(2003) [PubMed: 12919322] [Abstract]
Cited for: FUNCTION, LETHAL DOSE, DISULFIDE BONDS, SYNTHESIS.
[3]"Solution structure of Pi4, a short four-disulfide-bridged scorpion toxin specific of potassium channels."
Guijarro J.I., M'Barek S., Gomez-Lagunas F., Garnier D., Rochat H., Sabatier J.-M., Possani L.D., Delepierre M.
Protein Sci. 12:1844-1854(2003) [PubMed: 12930984] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BONDS, SYNTHESIS.
[4]Erratum
Guijarro J.I., M'Barek S., Gomez-Lagunas F., Garnier D., Rochat H., Sabatier J.-M., Possani L., Delepierre M.
Protein Sci. 12:2651-2651(2003)

Cross-references

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1N8MNMR-A1-38[»]
ModBaseSearch...

Family and domain databases

InterProIPR001947. Scorpion_toxinS.
[Graphical view]
PfamPF00451. Toxin_2. 1 hit.
[Graphical view]
ProDomPD003586. Scorpion_toxinS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS01138. SCORP_SHORT_TOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAX64_PANIM
AccessionPrimary (citable) accession number: P58498
Entry history
Integrated into UniProtKB/Swiss-Prot: December 19, 2001
Last sequence update: December 19, 2001
Last modified: June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Scorpion potassium channel toxins

Nomenclature of scorpion potassium channel toxins and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents