P16341 (KAX51_LEIQH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 81.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Potassium channel toxin alpha-KTx 5.1 Alternative name(s): Leiurotoxin I Short name=LeTx I Leiurotoxin-1 Scyllatoxin Short name=ScyTx |
| Organism | Leiurus quinquestriatus hebraeus (Yellow scorpion) |
| Taxonomic identifier | 6884 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Chelicerata › Arachnida › Scorpiones › Buthida › Buthoidea › Buthidae › Leiurus › ![]() |
Protein attributes
| Sequence length | 31 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 | |
| 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 component | Secreted |
| Molecular function | Ion channel impairing toxin Neurotoxin Potassium channel inhibitor Toxin |
| PTM | Amidation Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | pathogenesis Inferred from electronic annotation. Source: InterPro |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | potassium channel inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||
Molecule processing | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Peptide | 1 – 31 | 31 | Potassium channel toxin alpha-KTx 5.1 | PRO_0000044924 | |||||||||||
Amino acid modifications | |||||||||||||||
| Modified residue | 31 | 1 | Histidine amide Ref.1 | ||||||||||||
| Disulfide bond | 3 ↔ 21 | Ref.2 Ref.4 | |||||||||||||
| Disulfide bond | 8 ↔ 26 | Ref.2 Ref.4 | |||||||||||||
| Disulfide bond | 12 ↔ 28 | Ref.2 Ref.4 | |||||||||||||
Secondary structure | |||||||||||||||
Helix Strand Turn | |||||||||||||||
| Helix | 5 – 14 | 10 | |||||||||||||
| Beta strand | 18 – 21 | 4 | |||||||||||||
| Beta strand | 23 – 29 | 7 | |||||||||||||
Sequences
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 | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | A28805. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P16341. | ||||||||||||
| SMR | P16341. Positions 2-31. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR003614. Scorpion_toxin-like. IPR001947. Scorpion_toxinS_K_inh. [Graphical view] | ||||||||||||
| Pfam | PF00451. Toxin_2. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF57095. SSF57095. 1 hit. | ||||||||||||
| PROSITE | PS01138. SCORP_SHORT_TOXIN. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P16341. | ||||||||||||
Entry information
| Entry name | KAX51_LEIQH | ||||||||
| Accession | Primary (citable) accession number: P16341 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Animal 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 |

Clusters with
