CDIPT

From Wikipedia, the free encyclopedia

CDP-diacylglycerol--inositol 3-phosphatidyltransferase (phosphatidylinositol synthase)

Identifiers

CDIPT; MGC1328; PIS; PIS1

External IDs

OMIM: 605893 MGI: 105491 HomoloGene: 7159

Gene ontology
Molecular Function:	• magnesium ion binding • CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity • phosphatidylinositol transporter activity • transferase activity • manganese ion binding
Cellular Component:	• endoplasmic reticulum • membrane • integral to membrane
Biological Process:	• phospholipid biosynthetic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_145752 (mRNA)
NP_665695 (protein)

NM_026638 (mRNA)
NP_080914 (protein)

Location

Chr 16: 29.78 - 29.78 Mb

Chr 7: 126.77 - 126.77 Mb

Pubmed search

[1]

[2]

CDP-diacylglycerol--inositol 3-phosphatidyltransferase (phosphatidylinositol synthase), also known as CDIPT, is a human gene.^[1]

Phosphatidylinositol breakdown products are ubiquitous second messengers that function downstream of many 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.^[1]

[edit] References

^ ^a ^b Entrez Gene: CDIPT CDP-diacylglycerol--inositol 3-phosphatidyltransferase (phosphatidylinositol synthase).

[edit] Further reading

Antonsson B (1997). "Phosphatidylinositol synthase from mammalian tissues.". Biochim. Biophys. Acta 1348 (1-2): 179–86. PMID 9370331.
Antonsson BE (1994). "Purification and characterization of phosphatidylinositol synthase from human placenta.". Biochem. J. 297 ( Pt 3): 517–22. 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. 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. PMID 9373149.
Lykidis A, Jackson PD, Rock CO, Jackowski S (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. PMID 9407135.
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. doi:10.1073/pnas.242603899. 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.
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. 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 = Archivio Monaldi per le malattie del torace / Fondazione clinica del lavoro, IRCCS [and] Istituto di clinica tisiologica e malattie apparato respiratorio, Università di Napoli, Secondo ateneo 63 (3): 133–41. PMID 16312203.