| CDIPT | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | CDIPT, PIS, PIS1, CDP-diacylglycerol--inositol 3-phosphatidyltransferase | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 605893 MGI: 105491 HomoloGene: 7159 GeneCards: CDIPT | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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CDP-diacylglycerol—inositol 3-phosphatidyltransferase is an enzyme that in humans is encoded by the CDIPT gene.[5][6]
Phosphatidylinositol breakdown products are ubiquitous second messengers that function downstream of multiple G protein-coupled receptors and tyrosine kinases regulating cell growth, calcium metabolism, and protein kinase C activity. Two enzymes, CDP-diacylglycerol synthase and phosphatidylinositol synthase, are involved in the biosynthesis of phosphatidylinositol. Phosphatidylinositol synthase, a member of the CDP-alcohol phosphatidyl transferase class-I family, is an integral membrane protein found on the cytoplasmic side of the endoplasmic reticulum and the Golgi apparatus.[6]
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000103502 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030682 - Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Lykidis A, Jackson PD, Rock CO, Jackowski S (Jan 1998). "The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content". J Biol Chem. 272 (52): 33402–9. doi:10.1074/jbc.272.52.33402. PMID 9407135.
- 1 2 "Entrez Gene: CDIPT CDP-diacylglycerol--inositol 3-phosphatidyltransferase (phosphatidylinositol synthase)".
External links
- Human CDIPT genome location and CDIPT gene details page in the UCSC Genome Browser.
Further reading
- Antonsson B (1997). "Phosphatidylinositol synthase from mammalian tissues". Biochim. Biophys. Acta. 1348 (1–2): 179–86. doi:10.1016/s0005-2760(97)00105-7. PMID 9370331.
- Antonsson BE (1994). "Purification and characterization of phosphatidylinositol synthase from human placenta". Biochem. J. 297 (Pt 3): 517–22. doi:10.1042/bj2970517. PMC 1137864. PMID 8110188.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- de Serres FJ, Luisetti M, Ferrarotti I, et al. (2005). "Alpha-1 antitrypsin deficiency in Italy: regional differences of the PIS and PIZ deficiency alleles". Monaldi Archives for Chest Disease. 63 (3): 133–41. doi:10.4081/monaldi.2005.630. PMID 16312203.
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