CDS2

From Wikipedia, the free encyclopedia

CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 2

Identifiers

CDS2; FLJ38111

External IDs

OMIM: 603549 MGI: 1332236 HomoloGene: 37854

Gene ontology
Molecular Function:	• phosphatidate cytidylyltransferase activity • transferase activity
Cellular Component:	• mitochondrial inner membrane • endoplasmic reticulum • membrane • integral to membrane
Biological Process:	• phospholipid biosynthetic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003818 (mRNA)
NP_003809 (protein)

NM_138651 (mRNA)
NP_619592 (protein)

Location

Chr 20: 5.06 - 5.12 Mb

Chr 2: 131.95 - 132 Mb

Pubmed search

[1]

[2]

CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 2, also known as CDS2, 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: CDS2 CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 2.

[edit] Further reading

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.
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.
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.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
Halford S, Inglis S, Gwilliam R, et al. (2002). "Genomic organization of human CDS2 and evaluation as a candidate gene for corneal hereditary endothelial dystrophy 2 on chromosome 20p13.". Exp. Eye Res. 75 (5): 619–23. PMID 12457874.
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.
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.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.