title: Characterization of VAMP-2 gene from marine teleostean, Lateolabrax japonicus.
abstract: The whole length SPV2 gene of 715 bp, encoding VAMP-2 protein of 110 amino acids from Japanese sea perch, Lateolabrax japonicus, was obtained by using both RT-PCR and anchored PCR strategies while we initiated the structural and functional study on SNARE proteins in marine teleostean. Analysis of the deduced amino acid sequence indicated that SPV2 has its core arginine residue, a potential N-linked glycosylation site near its N-terminal, and one transmembrane domain in its C-terminal. Advanced structural analysis of bioinformatics approach predicts a coiled-coil alpha-helix backbone as the characteristic of SPV2 main conformational structure, identical to the structure of rat VAMP-2 obtained by crystallography. Semi-quantitative RT-PCR revealed that SPV2 was generally expressed in 10 neural and non-neural tissues, with the highest concentration in brain and the least in muscle.
authors.affiliation: College of Marine Life Sciences, Ocean University of China, Qingdao 266003, China.
authors.forename: Kui
authors.initials: K
authors.lastname: Chen
authors.forename: Xiaohang
authors.initials: X
authors.lastname: Huang
authors.forename: Zhenmin
authors.initials: Z
authors.lastname: Bao
authors.forename: Herbert
authors.initials: H
authors.lastname: Gaisano
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001492:Bass / Q000235:genetics*; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D050988:Vesicle-Associated Membrane Protein 2 / Q000737:chemistry* / Q000235:genetics*
chemical_list: D050988:Vesicle-Associated Membrane Protein 2