4.5 Article

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

期刊

MOLECULAR BIOLOGY REPORTS
卷 35, 期 3, 页码 351-359

出版社

SPRINGER
DOI: 10.1007/s11033-007-9093-3

关键词

Cytoplasm; GDPD domain; glycerophosphodiester phosphodiesterase; SRE; transmembrane

向作者/读者索取更多资源

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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据