SOAT2

Sterol O-acyltransferase 2, also known as SOAT2, is an enzyme that in humans is encoded by the SOAT2 gene.[5]

SOAT2
Identifiers
Aliases	SOAT2, ACACT2, ACAT2, ARGP2, sterol O-acyltransferase 2
External IDs	OMIM: 601311 MGI: 1332226 HomoloGene: 68355 GeneCards: SOAT2
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q13.13 Start 53,103,486 bp[1] End 53,124,535 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15 F2|15 57.33 cM Start 102,150,526 bp[2] End 102,163,469 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • cholesterol binding • O-acyltransferase activity • fatty-acyl-CoA binding • sterol O-acyltransferase activity • transferase activity, transferring acyl groups • cholesterol O-acyltransferase activity Cellular component • membrane • integral component of membrane • brush border • endoplasmic reticulum • endoplasmic reticulum membrane Biological process • very-low-density lipoprotein particle assembly • steroid metabolic process • macrophage derived foam cell differentiation • intestinal cholesterol absorption • cholesterol efflux • lipid metabolism • cholesterol esterification • cholesterol homeostasis • cholesterol metabolic process • low-density lipoprotein particle clearance Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8435	223920
Ensembl	ENSG00000167780	ENSMUSG00000023045
UniProt	O75908	O88908
RefSeq (mRNA)	NM_003578	NM_146064
RefSeq (protein)	NP_003569	NP_666176
Location (UCSC)	Chr 12: 53.1 – 53.12 Mb	Chr 15: 102.15 – 102.16 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000167780 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000023045 - 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. "Entrez Gene: SOAT2 sterol O-acyltransferase 2".

Further reading

• Chang TY, Chang CC, Cheng D; Chang (1997). "Acyl-coenzyme A:cholesterol acyltransferase". Annu. Rev. Biochem. 66: 613–38. CiteSeerX 10.1.1.319.6184. doi:10.1146/annurev.biochem.66.1.613. PMID 9242919.CS1 maint: multiple names: authors list (link)
• Yang H, Bard M, Bruner DA, et al. (1996). "Sterol esterification in yeast: a two-gene process". Science. 272 (5266): 1353–6. Bibcode:1996Sci...272.1353Y. 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.
• 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. doi:10.1091/mbc.11.11.3675. PMC 15029. PMID 11071899.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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.
• 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.