Characterization of cyclophilin D in freshwater pearl mussel (Hyriopsis schlegelii) |
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Authors: | Xiu-Xiu Liu Cheng-Yuan Wang Chun Luo Jun-Qing Sheng Di Wu Bei-Juan Hu Jun-Hua Wang Yi-Jiang Hong |
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Institution: | 1. School of Life Sciences, Nanchang University, Nanchang Jiangxi 330031, China;2. School of Life Sciences, Nanchang University, Nanchang Jiangxi 330031, China;Key Laboratory of Aquatic Animals Resources and Utilization of Jiangxi, Nanchang University, Nanchang Jiangxi 330031, China |
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Abstract: | Cyclophilin D (referred to as HsCypD) was obtained from the freshwater pearl mussel (Hyriopsis schlegelii).The full-length cDNA was 2 671 bp,encoding a protein consisting of 367 amino acids.HsCypD was determined to be a hydrophilic intracellular protein with 10 phosphorylation sites and four tetratricopeptide repeat (TPR) domains,but no signal peptide.The core sequence region YKGCIFHRIIKDFMVQGG is highly conserved in vertebrates and invertebrates.Phylogenetic tree analysis indicated that CypD from all species had a common origin,and HsCypD had the closest phylogenetic relationship with CypD from Lottia gigantea.The constitutive mRNA expression levels of HsCypD exhibited tissue-specific patterns,with the highest level detected in the intestines,followed by the gonads,and the lowest expression found in the hemocytes. |
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Keywords: | Hyriopsis schlegelii Cyclophilin D Sequence analysis |
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