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Publication : Organization and alternative splicing of the murine phospholipase D2 gene.

First Author  Redina OE Year  1998
Journal  Biochem J Volume  331 ( Pt 3)
Pages  845-51 PubMed ID  9560313
Mgi Jnum  J:48095 Mgi Id  MGI:1261742
Doi  10.1042/bj3310845 Citation  Redina OE, et al. (1998) Organization and alternative splicing of the murine phospholipase D2 gene. Biochem J 331(Pt 3):845-51
abstractText  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.
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