Organization and alternative splicing of the murine phospholipase D2 gene.
Phospholipase D (PLD) catalyses the hydrolysis of phosphatidylcholine, generating phosphatidic acid and choline. Mammalian PLD activity derives from a family of membrane-associated enzymes that are activated by a wide variety of signal transduction events. cDNA species encoding human, mouse and rat PLD1 and PLD2 have recently been reported. In this study we undertook to determine the organization of the mouse PLD2 gene. We report that the gene spans 17.1 kb and contains 25 exons. Mouse PLD2 is notable for a relatively GC-rich and large 5' untranslated region. Proximal promoter sequences upstream of the first exon contain several consensus SP1 sequences (GGGCGG) but lack TATA and CAAT boxes. Finally, alternatively spliced cDNA species identified for PLD1 and PLD2 are discussed in the context of the PLD2 genomic organization.
Redina
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OE
Department of Pharmacological Sciences, and The Institute for Cell and Developmental Biology, State University of New York, Stony Brook, New York 11794-8651, USA.
Frohman
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MA
D017398:Alternative Splicing / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D051379:Mice; D008969:Molecular Sequence Data; D010739:Phospholipase D / Q000737:chemistry / Q000235:genetics*; D011401:Promoter Regions, Genetic / Q000235:genetics; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid
C105606:phospholipase D2; D010739:Phospholipase D; C106801:phospholipase D1