CDIPT (original) (raw)

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Protein-coding gene in humans

CDIPT
Identifiers
Aliases	CDIPT, PIS, PIS1, CDP-diacylglycerol--inositol 3-phosphatidyltransferase
External IDs	OMIM: 605893; MGI: 105491; HomoloGene: 7159; GeneCards: CDIPT; OMA:CDIPT - orthologs
Gene location (Human)Chr.Chromosome 16 (human)[1]Band16p11.2Start29,858,357 bp[1]End29,863,414 bp[1]
Gene location (Mouse)Chr.Chromosome 7 (mouse)[2]Band7 F3|7 69.26 cMStart126,575,086 bp[2]End126,579,673 bp[2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inparotid glandendothelial cellBrodmann area 23spermmiddle temporal gyruspancreatic ductal cellgerminal epitheliumvisceral pleuraparietal pleuragingival epitheliumTop expressed inPaneth cellmotor neuronsubstantia nigraretinal pigment epitheliumbarrel cortexseminal vesiculaendocardial cushionfossafacial motor nucleusmedullary collecting ductMore reference expression dataBioGPSMore reference expression data
Gene ontologyMolecular function transferase activity phosphotransferase activity, for other substituted phosphate groups manganese ion binding alcohol binding CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity protein binding diacylglycerol binding carbohydrate binding Cellular component integral component of membrane Golgi apparatus endoplasmic reticulum membrane membrane Golgi membrane plasma membrane endoplasmic reticulum Biological process lipid metabolism CDP-diacylglycerol metabolic process phospholipid biosynthetic process phosphatidylinositol biosynthetic process Sources:Amigo / QuickGO
OrthologsSpeciesHuman MouseEntrez1042352858EnsemblENSG00000103502ENSMUSG00000030682UniProtO14735Q8VDP6RefSeq (mRNA)NM_001286585NM_001286586NM_006319NM_145752NM_026638NM_001347656NM_001379260RefSeq (protein)NP_001273514NP_001273515NP_006310NP_001273514.1NP_001273515.1NP_006310.1NP_001334585NP_080914NP_001366189Location (UCSC)Chr 16: 29.86 – 29.86 MbChr 7: 126.58 – 126.58 MbPubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000103502 – Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030682 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ 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.
6. ^ a b "Entrez Gene: CDIPT CDP-diacylglycerol--inositol 3-phosphatidyltransferase (phosphatidylinositol synthase)".

• Human CDIPT genome location and CDIPT gene details page in the UCSC Genome Browser.

• 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.