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P80670 (KAX83_LEIQH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 8.3
Alternative name(s):
Gating modifier of anion channels 2
Leiuropeptide II
Short name=LpII
Leiuropeptide-2
Toxin GaTx2
OrganismLeiurus quinquestriatus hebraeus (Yellow scorpion)
Taxonomic identifier6884 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeLeiurus

Protein attributes

Sequence length29 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specific and potent inhibitor of ClC-2/CLCN2 chloride channel. It slows ClC-2/CLCN2 activation by increasing the latency to first opening by nearly 8-fold but is unable to inhibit open channels, suggesting that this toxin inhibits channel activation gating. Ref.2 Ref.3

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Miscellaneous

Does not inhibit ClC-0, ClC-1/CLCN1, ClC-3/CLCN3, ClC-4/CLCN4, CFTR chloride channel, GABRR, Cl(Ca), Shaker, and Kv1.2/KCNA2.

Sequence similarities

Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 8 subfamily.

Caution

Has sequence similarities with potassium channel inhibitors, but inhibits chloride channels. It is why the systematic name 'Potassium channel toxin alpha-KTx 8.3' has been moved as alternative name.

Mass spectrometry

Molecular mass is 3191.29 Da from positions 1 - 29. Determined by MALDI. Ref.2

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionChloride channel inhibitor
Ion channel impairing toxin
Toxin
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processdefense response

Inferred from electronic annotation. Source: InterPro

pathogenesis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchloride 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 – 2929Potassium channel toxin alpha-KTx 8.3
PRO_0000044542

Amino acid modifications

Disulfide bond3 ↔ 19 Ref.1
Disulfide bond6 ↔ 24 Ref.1
Disulfide bond10 ↔ 26 Ref.1

Sequences

Sequence LengthMass (Da)Tools
P80670 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: BC5F650C196C15B8

FASTA293,199
        10         20 
VSCEDCPDHC STQKARAKCD NDKCVCEPI 

« Hide

References

[1]"Characterization of a new family of toxin-like peptides from the venom of the scorpion Leiurus quinquestriatus hebraeus. 1H-NMR structure of leiuropeptide II."
Buisine E., Wieruszeski J.-M., Lippens G., Wouters D., Tartar A., Sautiere P.
J. Pept. Res. 49:545-555(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, STRUCTURE BY NMR, DISULFIDE BONDS.
Tissue: Venom.
[2]"Isolation and characterization of a high affinity peptide inhibitor of ClC-2 chloride channels."
Thompson C.H., Olivetti P.R., Fuller M.D., Freeman C.S., McMaster D., French R.J., Pohl J., Kubanek J., McCarty N.A.
J. Biol. Chem. 284:26051-26062(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, TOXIN TARGET, MASS SPECTROMETRY.
Tissue: Venom.
[3]"Inhibition of ClC-2 chloride channels by a peptide component or components of scorpion venom."
Thompson C.H., Fields D.M., Olivetti P.R., Fuller M.D., Zhang Z.R., Kubanek J., McCarty N.A.
J. Membr. Biol. 208:65-76(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"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.

Cross-references

3D structure databases

ProteinModelPortalP80670.
SMRP80670. Positions 1-29.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR003614. Scorpion_toxin-like.
IPR008911. Toxin_6.
[Graphical view]
PfamPF05453. Toxin_6. 1 hit.
[Graphical view]
SUPFAMSSF57095. SSF57095. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKAX83_LEIQH
AccessionPrimary (citable) accession number: P80670
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 53 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