AAAD_RAT
ID AAAD_RAT Reviewed; 398 AA.
AC Q9QZH8;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Arylacetamide deacetylase;
DE EC=3.1.1.3;
GN Name=Aadac; Synonyms=Aada;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Brown Norway, and Sprague-Dawley; TISSUE=Brain;
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 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: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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}. Microsome membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest levels in liver with lower levels in
CC jejunum, kidney and testis. {ECO:0000269|PubMed:22207054}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF182426; AAD56394.1; -; mRNA.
DR EMBL; AF264017; AAF74757.1; -; Genomic_DNA.
DR RefSeq; NP_065413.1; NM_020538.1.
DR AlphaFoldDB; Q9QZH8; -.
DR SMR; Q9QZH8; -.
DR STRING; 10116.ENSRNOP00000064056; -.
DR ChEMBL; CHEMBL3509586; -.
DR ESTHER; ratno-aryla; Arylacetamide_deacetylase.
DR MEROPS; S09.991; -.
DR GlyGen; Q9QZH8; 4 sites.
DR PaxDb; Q9QZH8; -.
DR GeneID; 57300; -.
DR KEGG; rno:57300; -.
DR UCSC; RGD:631440; rat.
DR CTD; 13; -.
DR RGD; 631440; Aadac.
DR eggNOG; KOG1515; Eukaryota.
DR InParanoid; Q9QZH8; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q9QZH8; -.
DR Reactome; R-RNO-211945; Phase I - Functionalization of compounds.
DR SABIO-RK; Q9QZH8; -.
DR PRO; PR:Q9QZH8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS: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:0017171; F:serine hydrolase activity; ISO:RGD.
DR GO; GO:0004806; F:triglyceride lipase activity; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; NAS:RGD.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISO:RGD.
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 2: Evidence at transcript 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_0000071545"
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:0000250|UniProtKB:Q8BLF1,
FT ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 342
FT /evidence="ECO:0000250|UniProtKB:Q8BLF1"
FT ACT_SITE 372
FT /evidence="ECO:0000250|UniProtKB:Q8BLF1"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..339
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 45693 MW; 7DDFBC7BDDEC228E CRC64;
MGRTIFLLIS VVLVAYYIYI PLPDDIEEPW KIILGNTLLK LGGDLASFGE LLGLNHFMDT
VQLFMRFQVV PPTSDENVTV METDFNSVPV RIYIPKRKST TLRRGLFFIH GGGWCLGSAA
YFMYDTLSRR TAHRLDAVVV STDYGLAPKY HFPKQFEDVY HSLRWFLQED ILEKYGVDPR
RVGVSGDSAG GNLTAAVTQQ ILQDPDVKIK LKVQALIYPA LQALDMNVPS QQENSQYPLL
TRSLLIRFWS EYFTTDRDLE KAMLLNQHVP VEFSHLLQFV NWSSLLPQRY KKGYFYKTPT
PGSLELAQKY PGFTDVKACP LLANDSILHH LPMTYIITCQ YDVLRDDGLM YVKRLQNTGV
HVTHHHIEDG FHGALTLPGL KITYRMQNQY LNWLHKNL
