title: Phosphatidic acid phosphatase from mammalian tissues: discovery of channel-like proteins with unexpected functions.
abstract: Phosphatidic acid phosphatase (PAP) has long been known as a key enzyme involved in both glycerolipid biosynthesis and cellular signal transduction. The cDNA cloning of a plasma membrane-bound type 2 PAP has revealed the existence of a novel glycoprotein with six transmembrane domains. The type 2 PAP now represents an enzyme family consisting of Drosophila Wunen and rat Dri 42, which participate in germ cell migration and epithelial differentiation, respectively. Such novel functions of the type 2 PAP suggest the unexpected importance of lipids and/or their metabolic enzymes.
authors.affiliation: Department of Biochemistry, Sapporo Medical University, School of Medicine, Japan. kanoh@sapmed.ac.jp
authors.forename: H
authors.initials: H
authors.lastname: Kanoh
authors.forename: M
authors.initials: M
authors.lastname: Kai
authors.forename: I
authors.initials: I
authors.lastname: Wada
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D018076:DNA, Complementary; D006023:Glycoproteins / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D010711:Phosphatidate Phosphatase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D018076:DNA, Complementary; D006023:Glycoproteins; D010711:Phosphatidate Phosphatase