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P16341 (KAX51_LEIQH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. 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 5.1
Alternative name(s):
Leiurotoxin I
Short name=LeTx I
Leiurotoxin-1
Scyllatoxin
Short name=ScyTx
OrganismLeiurus quinquestriatus hebraeus (Yellow scorpion)
Taxonomic identifier6884 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeLeiurus

Protein attributes

Sequence length31 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Blocker for the small conductance calcium-activated potassium channels (SK-Ca); also known as apamine-sensitive potassium channel.

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 5 subfamily.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionIon channel impairing toxin
Neurotoxin
Potassium channel inhibitor
Toxin
   PTMAmidation
Disulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: InterPro

   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 – 3131Potassium channel toxin alpha-KTx 5.1
PRO_0000044924

Amino acid modifications

Modified residue311Histidine amide Ref.1
Disulfide bond3 ↔ 21 Ref.2 Ref.4
Disulfide bond8 ↔ 26 Ref.2 Ref.4
Disulfide bond12 ↔ 28 Ref.2 Ref.4

Secondary structure

....... 31
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16341 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: BB3183DC5CEA53A7

FASTA313,430
        10         20         30 
AFCNLRMCQL SCRSLGLLGK CIGDKCECVK H 

« Hide

References

[1]"Purification and characterization of a unique, potent inhibitor of apamin binding from Leiurus quinquestriatus hebraeus venom."
Chicci G.G., Gimenez-Gallego G., Ber E., Garcia M.L., Winquist R., Cascieri M.A.
J. Biol. Chem. 263:10192-10197(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Leiurotoxin I (scyllatoxin), a peptide ligand for Ca2(+)-activated K+ channels. Chemical synthesis, radiolabeling, and receptor characterization."
Auguste P., Hugues M., Grave B., Gesquiere J.C., Maes P., Tartar A., Romey G., Schweitz H., Lazdunski M.
J. Biol. Chem. 265:4753-4759(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS.
[3]"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.
[4]"Solution conformation of leiurotoxin I (scyllatoxin) by 1H nuclear magnetic resonance. Resonance assignment and secondary structure."
Martins J.C., Zhang W., Tartar A., Lazdunski M., Borremans F.A.M.
FEBS Lett. 260:249-253(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA28805.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCYNMR-A1-31[»]
ProteinModelPortalP16341.
SMRP16341. Positions 2-31.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR003614. Scorpion_toxin-like.
IPR001947. Scorpion_toxinS_K_inh.
[Graphical view]
PfamPF00451. Toxin_2. 1 hit.
[Graphical view]
SUPFAMSSF57095. SSF57095. 1 hit.
PROSITEPS01138. SCORP_SHORT_TOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16341.

Entry information

Entry nameKAX51_LEIQH
AccessionPrimary (citable) accession number: P16341
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

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

SIMILARITY comments

Index of protein domains and families