| pubmed-article:9237689 | pubmed:abstractText | Clavanins are a family of alpha-helical antimicrobial peptides found in hemocytes of the tunicate, Styela clava. We examined a cDNA library prepared from pharyngeal tissues of S. clava and sequenced 24 clones that encoded prepropeptides of Clavanins A, C, D or E. These sequences indicated that Clavanins are synthesized as 9.2 kDa prepropeptides which contain a 19-residue signal peptide, followed in turn by a highly polar 'pro' region (LEERKSEEEK) with five glutamic acid residues, the 23 residues of the mature Clavanin peptide, the glycine residue needed for its amidation and a 27-residue polar C-terminal extension that is removed in later processing. Although the signal sequence and anionic propiece of Clavanin precursors share features with corresponding regions in precursors of the certain frog peptides, including ranalexin, gaegurins, dermaseptins and deltorphins, their unique multipartite structure suggests that they are not actually homologues of these amphibian peptides. | lld:pubmed |
