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Cloning and characterization of a human GDPD domain-containing protein GDPD5

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Abstract

Glycerophosphodiester phosphodiesterase (GDPD) catalyzes the hydrolysis of deacylated glycerophospholipids to glycerol phosphate and alcohol. GDPD5 has been reported in Mus musculus and Gallus gallus, but not in Homo sapiens. Here we report the cloning and characterization of a novel human GDPD domain-containing gene, GDPD5, isolated from human testis cDNA library, and mapped to 11q13.4–13.5 by searching the UCSC genomic database. The GDPD5 cDNA sequence of 3442 base pairs contains an open reading frame encoding 605 amino acids. The GDPD5 gene consists of 17 exons and encodes a putative protein with six transmembrane regions and a GDPD motif. Subcellular localization of GDPD5 demonstrated that the protein was localized in the cytoplasm when overexpressed in COS-7 cells. RT-PCR analysis showed that GDPD5 was widely expressed in human tissues and the expression levels in kidney and prostate were relatively low.

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Abbreviations

GDE/GDPD:

Glycerophosphodiester phosphodiesterase

MIR16:

Membrane interacting protein of RGS16

RGS16:

G protein signaling 16

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Acknowledgements

This work was supported by the National 973 program of China, 863 projects of China and the National Natural Science foundation of China (30024001).

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Authors and Affiliations

  1. State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Handan Road 220, Shanghai, 200433, P.R. China

    Qingyu Lang, Haoxing Zhang, Jie Li, Hongkun Yin, Yifeng Zhang, Wenwen Tang, Bo Wan & Long Yu

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  1. Qingyu Lang
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  2. Haoxing Zhang
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  8. Long Yu
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Correspondence to Long Yu.

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Lang, Q., Zhang, H., Li, J. et al. Cloning and characterization of a human GDPD domain-containing protein GDPD5. Mol Biol Rep 35, 351–359 (2008). https://doi.org/10.1007/s11033-007-9093-3

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