CDS1 (gene)

From Wikipedia, the free encyclopedia

CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 1

Identifiers

External IDs

OMIM: 603548 MGI: 1921846 HomoloGene: 68173

Gene ontology
Molecular Function:	• magnesium ion binding • diacylglycerol cholinephosphotransferase activity • phosphatidate cytidylyltransferase activity • transferase activity
Cellular Component:	• endoplasmic reticulum • membrane • integral to membrane
Biological Process:	• lipid metabolic process • signal transduction • visual perception • phospholipid biosynthetic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001263 (mRNA)
NP_001254 (protein)

NM_173370 (mRNA)
NP_775546 (protein)

Location

Chr 4: 85.72 - 85.79 Mb

Chr 5: 102.01 - 102.06 Mb

Pubmed search

[1]

[2]

CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 1, also known as CDS1, is a human gene.^[1]

Breakdown products of phosphoinositides 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. This gene encodes an enzyme which regulates the amount of phosphatidylinositol available for signaling by catalyzing the conversion of phosphatidic acid to CDP-diacylglycerol. This enzyme is an integral membrane protein localized to two subcellular domains, the matrix side of the inner mitochondrial membrane where it is thought to be involved in the synthesis of phosphatidylglycerol and cardiolipin and the cytoplasmic side of the endoplasmic reticulum where it functions in phosphatidylinositol biosynthesis. Two genes encoding this enzyme have been identified in humans, one mapping to human chromosome 4q21 and a second to 20p13.^[1]

[edit] References

^ ^a ^b Entrez Gene: CDS1 CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 1.

[edit] Further reading

Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
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.
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.
Liu Y, Virshup DM, White RL, Hsu LC (2002). "Regulation of BRCA1 phosphorylation by interaction with protein phosphatase 1alpha.". Cancer Res. 62 (22): 6357–61. PMID 12438214.
Volta M, Bulfone A, Gattuso C, et al. (1999). "Identification and characterization of CDS2, a mammalian homolog of the Drosophila CDP-diacylglycerol synthase gene.". Genomics 55 (1): 68–77. doi:10.1006/geno.1998.5610. PMID 9889000.
Halford S, Dulai KS, Daw SC, et al. (1999). "Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes.". Genomics 54 (1): 140–4. doi:10.1006/geno.1998.5547. PMID 9806839.
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.
Weeks R, Dowhan W, Shen H, et al. (1997). "Isolation and expression of an isoform of human CDP-diacylglycerol synthase cDNA.". DNA Cell Biol. 16 (3): 281–9. PMID 9115637.
Heacock AM, Uhler MD, Agranoff BW (1996). "Cloning of CDP-diacylglycerol synthase from a human neuronal cell line.". J. Neurochem. 67 (5): 2200–3. PMID 8863531.