Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0C1B6 (BEST_PARTR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Bestoxin
OrganismParabuthus transvaalicus (South African fattail scorpion)
Taxonomic identifier170972 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeParabuthus

Protein attributes

Sequence length58 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Secreted.

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 componentSecreted
   Molecular functionIon channel impairing toxin
Neurotoxin
Toxin
Voltage-gated sodium channel impairing toxin
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processdefense response

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionion channel inhibitor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5858Bestoxin
PRO_0000233629

Amino acid modifications

Disulfide bond18 ↔ 41 By similarity
Disulfide bond27 ↔ 46 By similarity
Disulfide bond31 ↔ 48 By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C1B6 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: A5FD4ED9FC7794C2

FASTA586,607
        10         20         30         40         50 
ADVPGNYPLD KDGNTYTCLE LGENKDCQKV CKLHGVQYGY CYAFSCWCKE YLDDKDSV 

« Hide

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

ProteinModelPortalP0C1B6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.30.10. 1 hit.
InterProIPR003614. Scorpion_toxin-like.
IPR002061. Scorpion_toxinL/defensin.
[Graphical view]
PfamPF00537. Toxin_3. 1 hit.
[Graphical view]
SMARTSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMSSF57095. SSF57095. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBEST_PARTR
AccessionPrimary (citable) accession number: P0C1B6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: March 19, 2014
This is version 28 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