ID   AAAD_HUMAN              Reviewed;         399 AA.
AC   P22760; A8K3L3; D3DNJ6; Q8N1A9;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 5.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Arylacetamide deacetylase;
DE            EC=3.1.1.3;
GN   Name=AADAC; Synonyms=DAC;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT ILE-281.
RC   TISSUE=Liver;
RX   PubMed=8063807; DOI=10.1016/s0021-9258(17)31855-0;
RA   Probst M.R., Beer M., Beer D., Jenoe P., Meyer U.A., Gasser R.;
RT   "Human liver arylacetamide deacetylase. Molecular cloning of a novel
RT   esterase involved in the metabolic activation of arylamine carcinogens with
RT   high sequence similarity to hormone-sensitive lipase.";
RL   J. Biol. Chem. 269:21650-21656(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-281.
RC   TISSUE=Heart;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-281.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   TISSUE=Liver;
RX   PubMed=2043131; DOI=10.1016/0006-291x(91)92005-5;
RA   Probst M.R., Jenoe P., Meyer U.A.;
RT   "Purification and characterization of a human liver arylacetamide
RT   deacetylase.";
RL   Biochem. Biophys. Res. Commun. 177:453-459(1991).
RN   [7]
RP   FUNCTION.
RX   PubMed=17936933; DOI=10.1002/jbt.20178;
RA   Ross M.K., Crow J.A.;
RT   "Human carboxylesterases and their role in xenobiotic and endobiotic
RT   metabolism.";
RL   J. Biochem. Mol. Toxicol. 21:187-196(2007).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=19339378; DOI=10.1124/dmd.109.026567;
RA   Watanabe A., Fukami T., Nakajima M., Takamiya M., Aoki Y., Yokoi T.;
RT   "Human arylacetamide deacetylase is a principal enzyme in flutamide
RT   hydrolysis.";
RL   Drug Metab. Dispos. 37:1513-1520(2009).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78 AND ASN-282.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [10]
RP   BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=22207054; DOI=10.1124/dmd.111.043067;
RA   Kobayashi Y., Fukami T., Nakajima A., Watanabe A., Nakajima M., Yokoi T.;
RT   "Species differences in tissue distribution and enzyme activities of
RT   arylacetamide deacetylase in human, rat, and mouse.";
RL   Drug Metab. Dispos. 40:671-679(2012).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, VARIANTS ILE-281 AND GLN-399 EXT, AND CHARACTERIZATION OF
RP   VARIANTS ILE-281 AND GLN-399 EXT.
RX   PubMed=22415931; DOI=10.1124/dmd.112.044883;
RA   Shimizu M., Fukami T., Kobayashi Y., Takamiya M., Aoki Y., Nakajima M.,
RA   Yokoi T.;
RT   "A novel polymorphic allele of human arylacetamide deacetylase leads to
RT   decreased enzyme activity.";
RL   Drug Metab. Dispos. 40:1183-1190(2012).
RN   [12]
RP   BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION AT ASN-78 AND ASN-282, AND
RP   MUTAGENESIS OF ASN-78 AND ASN-282.
RX   PubMed=24125761; DOI=10.1016/j.bcp.2013.10.001;
RA   Muta K., Fukami T., Nakajima M., Yokoi T.;
RT   "N-Glycosylation during translation is essential for human arylacetamide
RT   deacetylase enzyme activity.";
RL   Biochem. Pharmacol. 87:352-359(2014).
RN   [13]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=23542347; DOI=10.1016/j.jhep.2013.03.022;
RA   Nourbakhsh M., Douglas D.N., Pu C.H., Lewis J.T., Kawahara T., Lisboa L.F.,
RA   Wei E., Asthana S., Quiroga A.D., Law L.M., Chen C., Addison W.R.,
RA   Nelson R., Houghton M., Lehner R., Kneteman N.M.;
RT   "Arylacetamide deacetylase: a novel host factor with important roles in the
RT   lipolysis of cellular triacylglycerol stores, VLDL assembly and HCV
RT   production.";
RL   J. Hepatol. 59:336-343(2013).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   VARIANT ILE-281.
RX   PubMed=12721789; DOI=10.1007/s10038-003-0021-7;
RA   Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C.,
RA   Nakamura Y.;
RT   "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine
RT   esterase genes, and two other genes in the Japanese population.";
RL   J. Hum. Genet. 48:249-270(2003).
CC   -!- FUNCTION: Displays cellular triglyceride lipase activity in liver,
CC       increases the levels of intracellular fatty acids derived from the
CC       hydrolysis of newly formed triglyceride stores and plays a role in very
CC       low-density lipoprotein assembly. Displays serine esterase activity in
CC       liver. Deacetylates a variety of arylacetamide substrates, including
CC       xenobiotic compounds and procarcinogens, converting them to the primary
CC       arylamide compounds and increasing their toxicity.
CC       {ECO:0000269|PubMed:17936933, ECO:0000269|PubMed:19339378,
CC       ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931,
CC       ECO:0000269|PubMed:23542347}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.8 mM for flutamide {ECO:0000269|PubMed:19339378,
CC         ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931,
CC         ECO:0000269|PubMed:24125761};
CC         KM=0.6 mM for flutamide {ECO:0000269|PubMed:19339378,
CC         ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931,
CC         ECO:0000269|PubMed:24125761};
CC         KM=0.472 mM for flutamide {ECO:0000269|PubMed:19339378,
CC         ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931,
CC         ECO:0000269|PubMed:24125761};
CC         KM=3.05 mM for phenacetin {ECO:0000269|PubMed:19339378,
CC         ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931,
CC         ECO:0000269|PubMed:24125761};
CC         KM=1.8 mM for phenacetin {ECO:0000269|PubMed:19339378,
CC         ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931,
CC         ECO:0000269|PubMed:24125761};
CC         KM=1.42 mM for phenacetin {ECO:0000269|PubMed:19339378,
CC         ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931,
CC         ECO:0000269|PubMed:24125761};
CC         KM=0.2 mM for rifampicin {ECO:0000269|PubMed:19339378,
CC         ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931,
CC         ECO:0000269|PubMed:24125761};
CC         KM=0.154 mM for rifampicin {ECO:0000269|PubMed:19339378,
CC         ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931,
CC         ECO:0000269|PubMed:24125761};
CC         Vmax=1.1 nmol/min/mg enzyme toward flutamide
CC         {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054,
CC         ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761};
CC         Vmax=0.617 nmol/min/mg enzyme toward flutamide
CC         {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054,
CC         ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761};
CC         Vmax=1.34 nmol/min/mg enzyme toward phenacetin
CC         {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054,
CC         ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761};
CC         Vmax=6.4 nmol/min/mg enzyme toward phenacetin
CC         {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054,
CC         ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761};
CC         Vmax=1.42 nmol/min/mg enzyme toward phenacetin
CC         {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054,
CC         ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761};
CC         Vmax=0.149 nmol/min/mg enzyme toward rifampicin
CC         {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054,
CC         ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761};
CC         Vmax=0.06 nmol/min/mg enzyme toward rifampicin
CC         {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054,
CC         ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:24125761};
CC   -!- INTERACTION:
CC       P22760; Q92624: APPBP2; NbExp=3; IntAct=EBI-13217105, EBI-743771;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC       II membrane protein. Microsome membrane; Single-pass type II membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Detected in liver (at protein level). Mainly
CC       expressed in liver, small intestine, colon, adrenal gland and bladder.
CC       {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054,
CC       ECO:0000269|PubMed:22415931}.
CC   -!- INDUCTION: Down-regulated following infection with hepatis C virus
CC       which results in impaired triacylglycerol lipolysis and impaired
CC       assembly of very low density lipoproteins. This may represent a
CC       cellular adaptation to infection that is aimed at limiting viral
CC       production. {ECO:0000269|PubMed:23542347}.
CC   -!- PTM: Glycosylation is required for enzyme activity.
CC       {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24125761}.
CC   -!- POLYMORPHISM: Three alleles are known: AADAC*1, AADAC*2 and AADAC*3.
CC       The sequence shown is that of AADAC*1 which is found in European
CC       American, African American, Japanese and Korean populations at allelic
CC       frequencies of 39.3 to 47.4%. The AADAC*2 allele is found in European
CC       American, African American, Korean, and Japanese populations at allelic
CC       frequencies of 52.6 to 63.5% whereas the AADAC*3 allele is found in
CC       European American (1.3%) and African American (2.0%) samples but not in
CC       Japanese or Korean samples. {ECO:0000269|PubMed:22415931}.
CC   -!- MISCELLANEOUS: Can hydrolyze a number of clinical drugs such as
CC       flutamide, an antiandrogen drug used for the treatment of prostate
CC       cancer; phenacetin, an analgesic antipyretic which has been withdrawn
CC       from the market due to its links with renal failure; and rifamycins
CC       which have been used as antituberculosis drugs.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA35551.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L32179; AAA35551.1; ALT_FRAME; mRNA.
DR   EMBL; AK290628; BAF83317.1; -; mRNA.
DR   EMBL; AC068647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW78791.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78792.1; -; Genomic_DNA.
DR   EMBL; BC032309; AAH32309.1; -; mRNA.
DR   CCDS; CCDS33877.1; -.
DR   PIR; A53856; A53856.
DR   RefSeq; NP_001077.2; NM_001086.2.
DR   AlphaFoldDB; P22760; -.
DR   SMR; P22760; -.
DR   BioGRID; 106531; 1.
DR   IntAct; P22760; 1.
DR   STRING; 9606.ENSP00000232892; -.
DR   BindingDB; P22760; -.
DR   ChEMBL; CHEMBL3509584; -.
DR   DrugBank; DB16349; Vicagrel.
DR   ESTHER; human-AADAC; Arylacetamide_deacetylase.
DR   MEROPS; S09.991; -.
DR   GlyCosmos; P22760; 2 sites, No reported glycans.
DR   GlyGen; P22760; 2 sites.
DR   iPTMnet; P22760; -.
DR   PhosphoSitePlus; P22760; -.
DR   BioMuta; AADAC; -.
DR   DMDM; 317373587; -.
DR   MassIVE; P22760; -.
DR   PaxDb; 9606-ENSP00000232892; -.
DR   PeptideAtlas; P22760; -.
DR   ProteomicsDB; 54037; -.
DR   Antibodypedia; 1182; 237 antibodies from 27 providers.
DR   DNASU; 13; -.
DR   Ensembl; ENST00000232892.12; ENSP00000232892.6; ENSG00000114771.14.
DR   GeneID; 13; -.
DR   KEGG; hsa:13; -.
DR   MANE-Select; ENST00000232892.12; ENSP00000232892.6; NM_001086.3; NP_001077.2.
DR   UCSC; uc003eze.4; human.
DR   AGR; HGNC:17; -.
DR   CTD; 13; -.
DR   DisGeNET; 13; -.
DR   GeneCards; AADAC; -.
DR   HGNC; HGNC:17; AADAC.
DR   HPA; ENSG00000114771; Tissue enhanced (adrenal gland, intestine, liver).
DR   MIM; 600338; gene.
DR   neXtProt; NX_P22760; -.
DR   OpenTargets; ENSG00000114771; -.
DR   PharmGKB; PA24363; -.
DR   VEuPathDB; HostDB:ENSG00000114771; -.
DR   eggNOG; KOG1515; Eukaryota.
DR   GeneTree; ENSGT00940000155975; -.
DR   HOGENOM; CLU_012494_12_0_1; -.
DR   InParanoid; P22760; -.
DR   OMA; QNQYMPI; -.
DR   OrthoDB; 1144477at2759; -.
DR   PhylomeDB; P22760; -.
DR   TreeFam; TF314978; -.
DR   PathwayCommons; P22760; -.
DR   Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR   SABIO-RK; P22760; -.
DR   SignaLink; P22760; -.
DR   BioGRID-ORCS; 13; 6 hits in 1160 CRISPR screens.
DR   GeneWiki; AADAC; -.
DR   GenomeRNAi; 13; -.
DR   Pharos; P22760; Tchem.
DR   PRO; PR:P22760; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P22760; Protein.
DR   Bgee; ENSG00000114771; Expressed in jejunal mucosa and 121 other cell types or tissues.
DR   ExpressionAtlas; P22760; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
DR   GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0016298; F:lipase activity; TAS:UniProtKB.
DR   GO; GO:0017171; F:serine hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR017157; Arylacetamide_deacetylase.
DR   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   PANTHER; PTHR23024; ARYLACETAMIDE DEACETYLASE; 1.
DR   PANTHER; PTHR23024:SF222; ARYLACETAMIDE DEACETYLASE; 1.
DR   Pfam; PF07859; Abhydrolase_3; 2.
DR   PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
DR   Genevisible; P22760; HS.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Hydrolase; Lipid metabolism; Membrane; Microsome;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..399
FT                   /note="Arylacetamide deacetylase"
FT                   /id="PRO_0000071542"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..23
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..399
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           111..113
FT                   /note="Involved in the stabilization of the negatively
FT                   charged intermediate by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000250|UniProtKB:Q8BLF1,
FT                   ECO:0000255|PROSITE-ProRule:PRU10038"
FT   ACT_SITE        343
FT                   /evidence="ECO:0000250|UniProtKB:Q8BLF1"
FT   ACT_SITE        373
FT                   /evidence="ECO:0000250|UniProtKB:Q8BLF1"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:24125761"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:24125761"
FT   DISULFID        116..340
FT                   /evidence="ECO:0000250"
FT   VARIANT         281
FT                   /note="V -> I (in alleles AADAC*2 and AADAC*3; mildly
FT                   decreased enzyme activity; dbSNP:rs1803155)"
FT                   /evidence="ECO:0000269|PubMed:12721789,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:22415931,
FT                   ECO:0000269|PubMed:8063807, ECO:0000269|Ref.4"
FT                   /id="VAR_014798"
FT   VARIANT         399
FT                   /note="L -> LQ (in allele AADAC*3; decreased enzyme
FT                   activity)"
FT                   /evidence="ECO:0000269|PubMed:22415931"
FT                   /id="VAR_070543"
FT   MUTAGEN         78
FT                   /note="N->Q: Abolishes glycosylation at this site and
FT                   causes moderate decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:24125761"
FT   MUTAGEN         282
FT                   /note="N->Q: Abolishes glycosylation at this site and
FT                   causes substantial decrease in activity and reduced
FT                   substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:24125761"
FT   CONFLICT        3
FT                   /note="R -> M (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55..57
FT                   /note="LHH -> VHI (in Ref. 1; AAA35551)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   399 AA;  45734 MW;  34F9CB717DD7417A CRC64;
     MGRKSLYLLI VGILIAYYIY TPLPDNVEEP WRMMWINAHL KTIQNLATFV ELLGLHHFMD
     SFKVVGSFDE VPPTSDENVT VTETKFNNIL VRVYVPKRKS EALRRGLFYI HGGGWCVGSA
     ALSGYDLLSR WTADRLDAVV VSTNYRLAPK YHFPIQFEDV YNALRWFLRK KVLAKYGVNP
     ERIGISGDSA GGNLAAAVTQ QLLDDPDVKI KLKIQSLIYP ALQPLDVDLP SYQENSNFLF
     LSKSLMVRFW SEYFTTDRSL EKAMLSRQHV PVESSHLFKF VNWSSLLPER FIKGHVYNNP
     NYGSSELAKK YPGFLDVRAA PLLADDNKLR GLPLTYVITC QYDLLRDDGL MYVTRLRNTG
     VQVTHNHVED GFHGAFSFLG LKISHRLINQ YIEWLKENL
//