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Characterization of cyclophilin D in freshwater pearl mussel (Hyriopsis schlegelii).

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.

SUBMITTER: Liu XX

PROVIDER: S-EPMC5396027 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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Characterization of cyclophilin D in freshwater pearl mussel (Hyriopsis schlegelii).

Liu Xiu-Xiu XX Wang Cheng-Yuan CY Luo Chun C Sheng Jun-Qing JQ Wu Di D Hu Bei-Juan BJ Wang Jun-Hua JH Hong Yi-Jiang YJ

Zoological research 20170301 2

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 in ...[more]

PMID: 28409506

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