SOAT2

Not to be confused with Acetyl-Coenzyme A acetyltransferase.

Sterol O-acyltransferase 2

Identifiers

Symbols

SOAT2; ACACT2; ACAT2; ARGP2; MGC116732

External IDs

OMIM: 601311 MGI: 1332226 HomoloGene: 68355 GeneCards: SOAT2 Gene

EC number

2.3.1.26

Gene Ontology
Molecular function	• fatty-acyl-CoA binding • acyltransferase activity • cholesterol binding • transferase activity • cholesterol O-acyltransferase activity
Cellular component	• membrane fraction • endoplasmic reticulum • endoplasmic reticulum membrane • microsome • brush border • membrane • integral to membrane
Biological process	• response to nutrient • steroid metabolic process • cholesterol metabolic process • macrophage derived foam cell differentiation • intestinal cholesterol absorption • cholesterol efflux • very-low-density lipoprotein particle assembly • cholesterol esterification • cholesterol homeostasis
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
53.5 – 53.52 Mb

Chr 15:
101.98 – 101.99 Mb

PubMed search

[1]

[2]

Sterol O-acyltransferase 2, also known as SOAT2, is an enzyme which in humans is encoded by the SOAT2 gene.^[1]

Function

This gene is a member of a small family of Acyl-CoA:cholesterol acyltransferases. The gene encodes a membrane-bound enzyme localized in the endoplasmic reticulum that produces intracellular cholesterol esters from long-chain fatty acyl CoA and cholesterol. The cholesterol esters are then stored as cytoplasmic lipid droplets inside the cell. The enzyme is implicated in cholesterol absorption in the intestine and in the assembly and secretion of apolipoprotein B-containing lipoproteins such as very low-density lipoprotein (VLDL). Several alternatively spliced transcript variants of this gene have been described, but their full-length nature is not known.^[1]

References

^ ^a ^b "Entrez Gene: SOAT2 sterol O-acyltransferase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8435.

Chang TY, Chang CC, Cheng D; Chang (1997). "Acyl-coenzyme A:cholesterol acyltransferase". Annu. Rev. Biochem. 66: 613–38. doi:10.1146/annurev.biochem.66.1.613. PMID 9242919.
Yang H, Bard M, Bruner DA, et al. (1996). "Sterol esterification in yeast: a two-gene process". Science 272 (5266): 1353–6. doi:10.1126/science.272.5266.1353. PMID 8650549.
Cases S, Novak S, Zheng YW, et al. (1998). "ACAT-2, a second mammalian acyl-CoA:cholesterol acyltransferase. Its cloning, expression, and characterization". J. Biol. Chem. 273 (41): 26755–64. doi:10.1074/jbc.273.41.26755. PMID 9756919.
Oelkers P, Behari A, Cromley D, et al. (1998). "Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes". J. Biol. Chem. 273 (41): 26765–71. doi:10.1074/jbc.273.41.26765. PMID 9756920.
Chang CC, Sakashita N, Ornvold K, et al. (2000). "Immunological quantitation and localization of ACAT-1 and ACAT-2 in human liver and small intestine". J. Biol. Chem. 275 (36): 28083–92. doi:10.1074/jbc.M003927200. PMID 10846185.
Lee H, Choi E, Seomun Y, et al. (2001). "High-Resolution Transcript Map of the Region Spanning D12S1629 and D12S312 at Chromosome 12q13: Triple A Syndrome-Linked Region". Genome Res. 10 (10): 1561–7. doi:10.1101/gr.142100. PMC 310951. PMID 11042153. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310951.
Joyce CW, Shelness GS, Davis MA, et al. (2001). "ACAT1 and ACAT2 Membrane Topology Segregates a Serine Residue Essential for Activity to Opposite Sides of the Endoplasmic Reticulum Membrane". Mol. Biol. Cell 11 (11): 3675–87. PMC 15029. PMID 11071899. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=15029.
Seo T, Oelkers PM, Giattina MR, et al. (2001). "Differential modulation of ACAT1 and ACAT2 transcription and activity by long chain free fatty acids in cultured cells". Biochemistry 40 (15): 4756–62. doi:10.1021/bi0022947. PMID 11294643.
Katsuren K, Tamura T, Arashiro R, et al. (2001). "Structure of the human acyl-CoA:cholesterol acyltransferase-2 (ACAT-2) gene and its relation to dyslipidemia". Biochim. Biophys. Acta 1531 (3): 230–40. doi:10.1016/S1388-1981(01)00106-8. PMID 11325614.
Song BL, Qi W, Yang XY, et al. (2001). "Organization of human ACAT-2 gene and its cell-type-specific promoter activity". Biochem. Biophys. Res. Commun. 282 (2): 580–8. doi:10.1006/bbrc.2001.4612. PMID 11401500.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Katsuren K, Fukuyama S, Takata K, Ohta T (2003). "Effects of a new single-nucleotide polymorphism in the Acyl-CoA:cholesterol acyltransferase-2 gene on plasma lipids and apolipoproteins in patients with hyperlipidemia". J. Atheroscler. Thromb. 10 (1): 32–6. doi:10.5551/jat.10.32. PMID 12621162.
Lin S, Lu X, Chang CC, Chang TY (2004). "Human Acyl-Coenzyme A:Cholesterol Acyltransferase Expressed in Chinese Hamster Ovary Cells: Membrane Topology and Active Site Location". Mol. Biol. Cell 14 (6): 2447–60. doi:10.1091/mbc.E02-11-0725. PMC 194892. PMID 12808042. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=194892.
Sakashita N, Miyazaki A, Chang CC, et al. (2003). "Acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT2) is induced in monocyte-derived macrophages: in vivo and in vitro studies". Lab. Invest. 83 (11): 1569–81. doi:10.1097/01.LAB.0000095687.17383.39. PMID 14615411.
Smith JL, Rangaraj K, Simpson R, et al. (2004). "Quantitative analysis of the expression of ACAT genes in human tissues by real-time PCR". J. Lipid Res. 45 (4): 686–96. doi:10.1194/jlr.M300365-JLR200. PMID 14729857.
Liang JJ, Oelkers P, Guo C, et al. (2004). "Overexpression of human diacylglycerol acyltransferase 1, acyl-coa:cholesterol acyltransferase 1, or acyl-CoA:cholesterol acyltransferase 2 stimulates secretion of apolipoprotein B-containing lipoproteins in McA-RH7777 cells". J. Biol. Chem. 279 (43): 44938–44. doi:10.1074/jbc.M408507200. PMID 15308631.
Parini P, Davis M, Lada AT, et al. (2005). "ACAT2 is localized to hepatocytes and is the major cholesterol-esterifying enzyme in human liver". Circulation 110 (14): 2017–23. doi:10.1161/01.CIR.0000143163.76212.0B. PMID 15451793.
Kim J, Bhinge AA, Morgan XC, Iyer VR (2005). "Mapping DNA-protein interactions in large genomes by sequence tag analysis of genomic enrichment". Nat. Methods 2 (1): 47–53. doi:10.1038/nmeth726. PMID 15782160.
Pramfalk C, Davis MA, Eriksson M, et al. (2005). "Control of ACAT2 liver expression by HNF1". J. Lipid Res. 46 (9): 1868–76. doi:10.1194/jlr.M400450-JLR200. PMID 15961790.

SOAT2

Function

References

Further reading