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Sequence Analysis of the Full-length cDNA and Protein Structure Homology Modeling of FABP2 from Paralichthys Olivaceus
Author(s) -
Xiaowu Chen,
Zhiyi Shi
Publication year - 2009
Publication title -
bioinformatics and biology insights
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 23
ISSN - 1177-9322
DOI - 10.4137/bbi.s2287
Subject(s) - genbank , paralichthys , complementary dna , danio , open reading frame , biology , homology modeling , uniprot , gene , microbiology and biotechnology , olive flounder , genetics , peptide sequence , zebrafish , biochemistry , fish <actinopterygii> , fishery , enzyme
Using zebrafish intestinal fatty acid-binding protein 2 (FABP2) mRNA sequence as the initial query probe, four highly homologous Paralichthys olivaceus EST sequences were retrieved from Genbank database. The assembled full-length cDNA contains the open reading frame of P. olivaceus FABP2 gene, which was validated by subsequent RT-PCR cloning. In the coding region, the average GC content is 56%, but it would reach 76.8% if only counting for the third base of the codons. The deduced P. olivaceus FABP2 polypeptide contains 132 amino acids (aa), with a predicted molecular size of 15.3 kD and pI at 6.74. This protein multiple-alignment has shown that this peptide is 75.7% identical to the corresponding homologous protein in Danio rerio. Among the 7 aa that are essential for FABP2 function, 3 were found to be conserved among P. olivaceus, Danio rerio, Tetraodon nigroviridi, Rattus norvegicus, and Homo sapiens. The study provides essential information on molecular evolution and function of FABP family.

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