Sequence diversity of Vipera lebetina snake venom gland serine proteinase homologs--result of alternative-splicing or genome alteration.
Four clones encoding homologous protein(ase)s were isolated from the Vipera lebetina (snake) venom gland cDNA library. One of them represented DNA encoding factor V activating enzyme (Siigur et al., 1999), the other is homologous to VLFVA but has two principal discrepancies in the translated protein sequence in comparison with snake venom serine proteinase structures: in the active site triad Ser195 is replaced by Asn195 and His57 by Arg57. The third and the fourth clone represent combinations of the first two clones. The possibilities of generation of such clones via trans-splicing of the primary gene transcript, by exon shuffling or by unequal crossing-over on the genome level are discussed.
National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia.
E
E
Siigur
A
A
Aaspõllu
J
J
Siigur
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D019143:Evolution, Molecular; D014644:Genetic Variation; D016678:Genome; D008969:Molecular Sequence Data; D020033:Protein Isoforms; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics*; D014757:Viper Venoms / Q000737:chemistry* / Q000235:genetics*; D017819:Viperidae / Q000235:genetics
D018076:DNA, Complementary; D020033:Protein Isoforms; D014757:Viper Venoms; C423570:Vipera lebetina protein 2; D012697:Serine Endopeptidases