The amino acid sequence of toxin RpIII from the sea anemone, Radianthus paumotensis

FEBS Lett. 1987 Jun 22;218(1):59-62. doi: 10.1016/0014-5793(87)81018-9.

Abstract

The amino acid sequence of the sodium channel toxin RpIII from the sea anemone Radianthus paumotensis has been determined. The protein is homologous with five analogous toxins from three anemone species, and is most similar to a less toxic protein, RpII, from the same organism. Twelve residues are conserved in all six toxins, one of which is an arginine residue thought to be essential for toxicity. The others (Cys, Gly, Pro and Trp) tend to be conserved in other sets of homologous proteins to maintain functional folds. Comparisons of the sequences suggest the existence of two separate but related classes of toxins cumon the three species of anemone.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cnidaria / analysis*
  • Cnidarian Venoms / analysis*
  • Cnidarian Venoms / genetics
  • Marine Toxins / analysis
  • Marine Toxins / genetics
  • Protein Conformation
  • Sea Anemones / analysis*
  • Sea Anemones / genetics
  • Sequence Homology, Nucleic Acid
  • Species Specificity

Substances

  • Cnidarian Venoms
  • Marine Toxins
  • RpIII toxin (Radianthus)