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P58498 (KAX64_PANIM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 63. 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 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 lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesIuridaScorpionoideaScorpionidaeScorpioninaePandinus

Protein attributes

Sequence length38 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potently, completely and reversibly blocks voltage-gated potassium channel Kv1.2/KCNA2 and Shaker B (Sh). Also blocks small conductance (SK) calcium-activated potassium channel (KCNN). Ref.2

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).

Toxic dose

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

Miscellaneous

This toxin has no effect on voltage-gated potassium channel Kv1.1/KCNA1 and Kv1.3/KCNA3 (Ref.2).

Sequence similarities

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

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 Kv1.2/KCNA2 channel
Site191Important for the interaction with Kv1.2/KCNA2 channel
Site261Basic residue of the functional dyad, important for the interaction with Kv1.2/KCNA2 channel
Site281Important for the interaction with Kv1.2/KCNA2 channel
Site301Important for the interaction with Kv1.2/KCNA2 channel
Site331Important for the interaction with Kv1.2/KCNA2 channel
Site351Aromatic residue of the functional dyad, important for the interaction with Kv1.2/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 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, TOXIN TARGET, 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] [Europe PMC] [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

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N8MNMR-A1-38[»]
ProteinModelPortalP58498.
SMRP58498. Positions 1-38.
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]
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

EvolutionaryTraceP58498.

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: October 16, 2013
This is version 63 of the entry and version 1 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