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AADAC
Identifiers
Aliases	AADAC, CES5A1, DAC, arylacetamide deacetylase
External IDs	OMIM: 600338; MGI: 1915008; HomoloGene: 37436; GeneCards: AADAC; OMA:AADAC - orthologs
EC number	3.1.1.3
Gene location (Human) Chr. Chromosome 3 (human) Band 3q25.1 Start 151,814,073 bp End 151,828,488 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 D Start 59,933,138 bp End 59,947,581 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa right adrenal gland right adrenal cortex left adrenal gland left adrenal cortex right lobe of liver duodenum mucosa of ileum body of pancreas gallbladder Top expressed in left lobe of liver right kidney proximal tubule duodenum human kidney precursor cell migratory enteric neural crest cell fetal liver hematopoietic progenitor cell gallbladder jejunum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function serine hydrolase activity carboxylic ester hydrolase activity catalytic activity hydrolase activity lipase activity deacetylase activity triglyceride lipase activity Cellular component organelle membrane integral component of membrane endoplasmic reticulum membrane endoplasmic reticulum membrane intracellular membrane-bounded organelle Biological process xenobiotic metabolic process metabolism positive regulation of triglyceride catabolic process catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 13 67758 Ensembl ENSG00000114771 ENSMUSG00000027761 UniProt P22760 Q99PG0 RefSeq (mRNA) NM_001086 NM_023383 RefSeq (protein) NP_001077 NP_075872 Location (UCSC) Chr 3: 151.81 – 151.83 Mb Chr 3: 59.93 – 59.95 Mb PubMed search
Wikidata
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Arylacetamide deacetylase is an enzyme that in humans is encoded by the AADAC gene.

Microsomal arylacetamide deacetylase competes against the activity of cytosolic arylamine N-acetyltransferase, which catalyzes one of the initial biotransformation pathways for arylamine and heterocyclic amine carcinogens.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000114771 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000027761 – 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. Probst MR, Beer M, Beer D, Jeno P, Meyer UA, Gasser R (Sep 1994). "Human liver arylacetamide deacetylase. Molecular cloning of a novel esterase involved in the metabolic activation of arylamine carcinogens with high sequence similarity to hormone-sensitive lipase". J Biol Chem. 269 (34): 21650–6. doi:10.1016/S0021-9258(17)31855-0. PMID 8063807.
6. ^ "Entrez Gene: AADAC arylacetamide deacetylase (esterase)".

Further reading

• Probst MR, Jenö P, Meyer UA (1991). "Purification and characterization of a human liver arylacetamide deacetylase". Biochem. Biophys. Res. Commun. 177 (1): 453–9. doi:10.1016/0006-291X(91)92005-5. PMID 2043131.
• Yamazaki K, Kusano K, Tadano K, Tanaka I (1997). "Radiation hybrid mapping of human arylacetamide deacetylase (AADAC) locus to chromosome 3". Genomics. 44 (2): 248–50. doi:10.1006/geno.1997.4879. PMID 9299245.
• Ozols J (1998). "Determination of lumenal orientation of microsomal 50-kDa esterase/N-deacetylase". Biochemistry. 37 (28): 10336–44. doi:10.1021/bi9807916. PMID 9665742.
• Mziaut H, Korza G, Hand AR, et al. (1999). "Targeting proteins to the lumen of endoplasmic reticulum using N-terminal domains of 11beta-hydroxysteroid dehydrogenase and the 50-kDa esterase". J. Biol. Chem. 274 (20): 14122–9. doi:10.1074/jbc.274.20.14122. PMID 10318829.
• Trickett JI, Patel DD, Knight BL, et al. (2001). "Characterization of the rodent genes for arylacetamide deacetylase, a putative microsomal lipase, and evidence for transcriptional regulation". J. Biol. Chem. 276 (43): 39522–32. doi:10.1074/jbc.M101764200. PMID 11481320.
• 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.
• Saito S, Iida A, Sekine A, et al. (2003). "Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population". J. Hum. Genet. 48 (5): 249–70. doi:10.1007/s10038-003-0021-7. PMID 12721789.
• Frick C, Atanasov AG, Arnold P, et al. (2004). "Appropriate function of 11beta-hydroxysteroid dehydrogenase type 1 in the endoplasmic reticulum lumen is dependent on its N-terminal region sharing similar topological determinants with 50-kDa esterase". J. Biol. Chem. 279 (30): 31131–8. doi:10.1074/jbc.M313666200. PMID 15152005.
• 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. PMC 528928. PMID 15489334.

External links

• AADAC human gene location in the UCSC Genome Browser.
• AADAC human gene details in the UCSC Genome Browser.

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