<unk>  I<unk>  I consists of 47 amino acids. The determined molecular mass appears to be approximately 5 kDa. It is classified into Type I voltage-gated sodium channel neurotoxins. As reported by Norton et al., this group consists of polypeptide neurotoxins with an average of 46-49 amino acids and 27 residues that are highly conserved.<unk>  I shares 21 of the 27 conserved residues with the representatives of Type I polypeptide toxins from sea anemone.<unk>  II & III<unk>  II and<unk>  III have not yet been categorized since their structure does not correspond to any known polypeptide neurotoxins from sea anemone.<unk>  II is composed of 59 amino acid residues and has a molecular mass of 6506 Da.<unk>  III has the same number of amino acid residues and a molecular mass of 6558 Da.<unk>  II and III are highly homologous with a similarity percentage of 94.9%. Both<unk>  II and III show sequence similarities to the neurotoxin TxI isolated from Phoneutria nigriventer, an aggressive Brazilian spider. These similarities concern the position of 7 half-cystine (oxidized cysteine) residues in both<unk>  II and III, consistent with the conserved half-cystine residues throughout the P. nigriventer neurotoxins. The amino acid sequence of<unk>  I differs from the amino acid sequences of<unk>  II and III.<unk>  I is rich in the amino acids asparagine and aspartic acid and has no lysine while<unk>  II and III both have a high number of half-cystines. All three polypeptides have in common that glycine is the most abundant amino acid.<unk>  K<unk>  K is a member of the Type I potassium channel toxin family. However, in contrast to the other members of this family which have 35-37 amino acid residues,<unk>  K consists of 83 amino acid residues; it has a molecular mass of 3999.3 Da. It shares six conserved Cys residues with the other members of Type I potassium channel toxins.
AETX
KHAT
SFHAM
IOMAI
DESMOND 
NRX
DHIS
ROHHAD