SOAT2

Not to be confused with Acetyl-Coenzyme A acetyltransferase.

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

SOAT2
Identifiers
Aliases	SOAT2, ACACT2, ACAT2, ARGP2, sterol O-acyltransferase 2
External IDs	OMIM: 601311; MGI: 1332226; HomoloGene: 68355; GeneCards: SOAT2; OMA:SOAT2 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) Band 12q13.13 Start 53,103,486 bp End 53,124,535 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15 F2|15 57.33 cM Start 102,058,961 bp End 102,071,904 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa testicle gonad duodenum spleen right lobe of liver gastric mucosa tibial nerve thoracic aorta ascending aorta Top expressed in yolk sac jejunum intestinal villus Ileal epithelium duodenum left lobe of liver perirhinal cortex entorhinal cortex choroid plexus of fourth ventricle primitive streak More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity cholesterol binding O-acyltransferase activity fatty-acyl-CoA binding sterol O-acyltransferase activity acyltransferase activity 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: 102.06 – 102.07 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

See also: Long-chain fatty acid and Fatty acyl-CoA esters

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.

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.{{cite journal}}: 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. S2CID 45308699.
• 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. S2CID 11543738.
• 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. S2CID 36046291.
• 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. S2CID 23331466.
• 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. S2CID 35044397.
• 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. S2CID 6338679.
• 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. S2CID 6135437.
• 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. S2CID 21852000.