AAAD_MOUSE
ID AAAD_MOUSE Reviewed; 398 AA.
AC Q99PG0; Q8VCF2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Arylacetamide deacetylase;
DE EC=3.1.1.3;
GN Name=Aadac; Synonyms=Aada;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvEvTacfBr; TISSUE=Spleen;
RX PubMed=11481320; DOI=10.1074/jbc.m101764200;
RA Trickett J.I., Patel D.D., Knight B.L., Saggerson E.D., Gibbons G.F.,
RA Pease R.J.;
RT "Characterization of the rodent genes for arylacetamide deacetylase, a
RT putative microsomal lipase, and evidence for transcriptional regulation.";
RL J. Biol. Chem. 276:39522-39532(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RX PubMed=19654421; DOI=10.1194/jlr.m000596;
RA Lo V., Erickson B., Thomason-Hughes M., Ko K.W., Dolinsky V.W., Nelson R.,
RA Lehner R.;
RT "Arylacetamide deacetylase attenuates fatty-acid-induced triacylglycerol
RT accumulation in rat hepatoma cells.";
RL J. Lipid Res. 51:368-377(2010).
RN [5]
RP 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).
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 (By similarity). Displays serine
CC esterase activity in liver. Deacetylates a variety of arylacetamide
CC substrates, including xenobiotic compounds and procarcinogens,
CC converting them to the primary arylamide compounds and increasing their
CC toxicity. {ECO:0000250, ECO:0000269|PubMed:19654421,
CC ECO:0000269|PubMed:22207054}.
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 Evidence={ECO:0000269|PubMed:19654421};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19654421}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:19654421}. Microsome membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest levels in liver with lower levels in
CC jejunum and kidney. {ECO:0000269|PubMed:19654421,
CC ECO:0000269|PubMed:22207054}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19654421}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF306788; AAG60035.1; -; Genomic_DNA.
DR EMBL; BC019999; AAH19999.1; -; mRNA.
DR EMBL; BC054823; AAH54823.1; -; mRNA.
DR CCDS; CCDS17375.1; -.
DR RefSeq; NP_075872.1; NM_023383.1.
DR AlphaFoldDB; Q99PG0; -.
DR SMR; Q99PG0; -.
DR STRING; 10090.ENSMUSP00000029325; -.
DR ChEMBL; CHEMBL3509583; -.
DR ESTHER; mouse-aryla; Arylacetamide_deacetylase.
DR MEROPS; S09.991; -.
DR GlyGen; Q99PG0; 1 site.
DR iPTMnet; Q99PG0; -.
DR PhosphoSitePlus; Q99PG0; -.
DR SwissPalm; Q99PG0; -.
DR jPOST; Q99PG0; -.
DR MaxQB; Q99PG0; -.
DR PaxDb; Q99PG0; -.
DR PeptideAtlas; Q99PG0; -.
DR PRIDE; Q99PG0; -.
DR ProteomicsDB; 296430; -.
DR Antibodypedia; 1182; 208 antibodies from 27 providers.
DR DNASU; 67758; -.
DR Ensembl; ENSMUST00000029325; ENSMUSP00000029325; ENSMUSG00000027761.
DR GeneID; 67758; -.
DR KEGG; mmu:67758; -.
DR UCSC; uc008piz.1; mouse.
DR CTD; 13; -.
DR MGI; MGI:1915008; Aadac.
DR VEuPathDB; HostDB:ENSMUSG00000027761; -.
DR eggNOG; KOG1515; Eukaryota.
DR GeneTree; ENSGT00940000155975; -.
DR HOGENOM; CLU_012494_12_0_1; -.
DR InParanoid; Q99PG0; -.
DR OMA; PKHMARW; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q99PG0; -.
DR TreeFam; TF314978; -.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR SABIO-RK; Q99PG0; -.
DR BioGRID-ORCS; 67758; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Aadac; mouse.
DR PRO; PR:Q99PG0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99PG0; protein.
DR Bgee; ENSMUSG00000027761; Expressed in left lobe of liver and 112 other tissues.
DR Genevisible; Q99PG0; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB.
DR GO; GO:0016298; F:lipase activity; TAS:MGI.
DR GO; GO:0017171; F:serine hydrolase activity; IDA:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR017157; Arylacetamide_deacetylase.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Lipid metabolism; Membrane; Microsome; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="Arylacetamide deacetylase"
FT /id="PRO_0000071543"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 110..112
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 188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 342
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 372
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..339
FT /evidence="ECO:0000250"
FT CONFLICT 101
FT /note="A -> T (in Ref. 2; AAH19999/AAH54823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45250 MW; 77F62E505B70D208 CRC64;
MGKTISLLIS VVLVAYYLYI PLPDAIEEPW KVVWETAFVK IGTDLASFGE LLGISHFMET
IQLLMSFQEV PPTSDEHVTV METAFDSVPV RIYIPKRKSM ALRRGLFYIH GGGWCLGSAA
HFSYDTLSRW TAHKLDAVVV STDYGLAPKH HFPRQFEDVY RSLRWFLQED VLEKYGVDPR
RVGVSGDSAG GNLAAAVTQQ LIQDPDVKIK LKVQALIYPA LQALDTNVPS QQEGSHFPVL
TRSLMVRFWS EYFTTDRGLE KAMLLNQHVP MESSHLLQFV NWSSLLPERY KKSPVYKNPT
PGSSELAQKY PGFIDVKACP LLANDNILHH LPKTYIITCQ YDVLRDDGLM YVKRLQNVGV
HVTHHHVEDG FHGTFSFPGL KLSERMKNQY LSWLIKNL
