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Volume 272, Number 16, Issue of April 18, 1997 pp. 10422-10428
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Cloning of a Novel Human Diacylglycerol Kinase (DGKtheta ) Containing Three Cysteine-rich Domains, a Proline-rich Region, and a Pleckstrin Homology Domain with an Overlapping Ras-associating Domain

(Received for publication, December 20, 1996)

Brahim Houssa Dagger , Dick Schaap Dagger , José van der Wal Dagger , Kaoru Goto par , Hisatake Kondo par , Akio Yamakawa ** , Masao Shibata ** , Tadaomi Takenawa ** and Wim J. van Blitterswijk Dagger

From the Dagger  Division of Cellular Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands, the par  Department of Anatomy, Tohoku University School of Medicine, Sendai 980, Japan, and the ** Department of Biochemistry, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan

Diacylglycerol kinase (DGK) attenuates levels of second messenger diacylglycerol in cells and produces another (putative) messenger, phosphatidic acid. We have previously purified a 110-kDa DGK from rat brain (Kato, M., and Takenawa, T. (1990) J. Biol. Chem. 265, 794-800). Here we report the cDNA cloning from human brain and retina cDNA libraries. The cDNA encodes a novel DGK isotype, termed DGKtheta , of 941 amino acids with an apparent molecular mass of 110 kDa. DGKtheta contains a C-terminal putative catalytic domain, which is present in all eukaryotic DGKs. In contrast to other DGK isotypes, DGKtheta contains three cysteine-rich domains instead of two. The third cysteine-rich domain is most homologous to the second one in other DGK isotypes. This particular sequence homology extends C-terminally beyond the typical cysteine/histidine core structure and is DGK-specific. DGKtheta furthermore contains various domains for protein-protein interaction, such as a proline- and glycine-rich domain with a putative SH3 domain-binding site and a pleckstrin homology domain with an overlapping Ras-associating domain. DGKtheta is expressed in the brain and, to a lesser extent, in the small intestine, duodenum, and liver. In situ hybridization of DGKtheta mRNA in adult rat brain reveals high expression in the cerebellar cortex and hippocampus. DGKtheta activity in COS cell lysates is optimal toward diacylglycerols containing an unsaturated fatty acid at the sn-2 position.


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