Scorpion long chain toxin (IPR018218)

Short name: Scorpion_toxinL

Overlapping homologous superfamilies

Family relationships


Scorpion toxins, which may be mammal or insect specific, bind to sodium channels, inhibiting the inactivation of activated channels and blocking neuronal transmission. The complete covalent structure of the toxins has been deduced: it comprises around 66 amino acid residues and is cross-linked by four disulphide bridges [PMID: 2311768, PMID: 6845379]. An anti-epilepsy peptide isolated from scorpion venom [PMID: 2930463] shows similarity to both scorpion neurotoxins and anti-insect toxins.

This entry contains alpha toxins as well as beta-insect depressant toxins, and other toxins. Alpha toxins are highly toxic both to mammals and insects. Depressant insect beta-toxins cause a transient contraction paralysis followed by a slow flaccid paralysis. They bind voltage-independently at site-4 of sodium channels and block action potentials, primarily by depolarising the axonal membrane and suppressing the sodium current. This depressant toxin is active only on insects. It is found in a relatively small amount in the venom.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0090729 toxin activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.