P0C1B6 (BEST_PARTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 25.
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: Bestoxin |
| Organism | Parabuthus transvaalicus (South African fattail scorpion) |
| Taxonomic identifier | 170972 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Chelicerata › Arachnida › Scorpiones › Buthida › Buthoidea › Buthidae › Parabuthus![]() |
Protein attributes
| Sequence length | 58 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing By similarity. In mice, causes intense writhing. |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Sequence similarities | Belongs to the long (3 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily. |
| Mass spectrometry | Molecular mass is 6603.6 Da from positions 1 - 58. Determined by ESI. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Ion channel impairing toxin Neurotoxin Sodium channel inhibitor Toxin |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | defense response Inferred from electronic annotation. Source: InterPro |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | sodium channel inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Three structurally related, highly potent, peptides from the venom of Parabuthus transvaalicus possess divergent biological activity." Inceoglu A.B., Lango J., Pessah I.N., Hammock B.D. Toxicon 45:727-733(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY. Tissue: Venom. |
Cross-references
3D structure databases | |
|---|---|
| ProteinModelPortal | P0C1B6. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.30.30.10. 1 hit. |
| InterPro | IPR003614. Scorpion_toxin-like. IPR002061. Scorpion_toxinL/defesin. [Graphical view] |
| Pfam | PF00537. Toxin_3. 1 hit. [Graphical view] |
| SMART | SM00505. Knot1. 1 hit. [Graphical view] |
| SUPFAM | SSF57095. SSF57095. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | BEST_PARTR | ||||||||
| Accession | Primary (citable) accession number: P0C1B6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Animal Toxin Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
