Equinatoxins, pore-forming proteins from the sea anemone Actinia equina, belong to a multigene family

• Published in: Toxicon (Oxford) Vol. 37; no. 10; pp. 1391 - 1401
• Main Authors: Anderluh, Gregor, Križaj, Igor, Štrukelj, Borut, Gubenšek, Franc, Maček, Peter, Pungerčar, Jože
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Oxford Elsevier Ltd 01-10-1999; Elsevier Science
• Subjects: Actinia equina; Amino Acid Sequence; Animal poisons toxicology. Antivenoms; Animals; Anthozoa; Base Sequence; Biological and medical sciences; Blotting, Southern; Chromatography, High Pressure Liquid; Cloning, Molecular; Cnidarian Venoms - genetics; DNA, Complementary; EqtIV protein; equinatoxin; equinatoxins; Marine; Medical sciences; Molecular Sequence Data; Multigene Family; Protein Isoforms - genetics; Recombinant Proteins - genetics; Sea Anemones - genetics; Sequence Homology, Amino Acid; Toxicology; Nucleotide sequence; Animal origin; Actinia equina; Protein; Toxin; Coelenterata; Gene; Analog; Cnidaria; N terminal-Sequence; Isolation; Multigene family; Invertebrata; Aminoacid sequence; Structural analysis
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/S0041-0101(99)00082-3

The multigene family of equinatoxins, pore-forming proteins from sea anemone
Actinia equina, has been studied at the protein and gene levels. We report the cDNA sequence of a new, sphingomyelin inhibited equinatoxin, EqtIV. The N-terminal sequences of natural Eqt I and III were also determined, confirming two isoforms of EqtI, differing at position 13. The number of Eqt genes determined by Southern blot hybridization was found to be more than five, indicating that Eqts belong to a multigene family.