The suffix “septine” is derived from the Greek word “sepsis” [σῆψις], which means “decay” or “putrefaction”.
Finally, 6a specifies that this was the sixth Acititoxin of which the full-length amino acid sequence was published and that this is the first isoform.
These toxins can be classified as type I voltage-gated potassium channel inhibiting peptides, based on their size and structure.
[4][6] The residues which are demonstrated to be most essential for potassium channel binding are the adjacent Lys-24 and Tyr-25, which are conserved in all four orthologous peptides.
[4][7] Kaliseptine competitively binds the dendrotoxin (DTXI) receptor domain on the voltage-gated potassium channel KV1.2.
Evidence was provided that DTXI binds in close proximity to the external mouth of the channel, leading to occlusion of the pore.
Kaliseptine is thought to act in conjunction with other neurotoxins present in the snakelocks anemone venom, altogether prolonging the action potential.
[13] When the nematocysts of the snakelocks anemone come into contact with human skin, the venom can cause redness, swelling and pain.