AAAD_RABIT
ID AAAD_RABIT Reviewed; 398 AA.
AC Q7M370;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Arylacetamide deacetylase;
DE EC=3.1.1.3;
DE AltName: Full=50 kDa microsomal esterase/N-deacetylase;
GN Name=AADAC {ECO:0000250|UniProtKB:P22760};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1] {ECO:0000305, ECO:0000312|PIR:A58922}
RP PROTEIN SEQUENCE, ENZYME ACTIVITY, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY,
RP DISULFIDE BOND, ACTIVE SITE, AND GLYCOSYLATION AT ASN-77 AND ASN-281.
RC STRAIN=New Zealand {ECO:0000269|PubMed:9665742};
RC TISSUE=Liver {ECO:0000269|PubMed:9665742};
RX PubMed=9665742; DOI=10.1021/bi9807916;
RA Ozols J.;
RT "Determination of lumenal orientation of microsomal 50-kDa esterase/N-
RT deacetylase.";
RL Biochemistry 37:10336-10344(1998).
RN [2] {ECO:0000305}
RP TOPOLOGY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-3.
RX PubMed=10318829; DOI=10.1074/jbc.274.20.14122;
RA Mziaut H., Korza G., Hand A.R., Gerard C., Ozols J.;
RT "Targeting proteins to the lumen of endoplasmic reticulum using N-terminal
RT domains of 11beta-hydroxysteroid dehydrogenase and the 50-kDa esterase.";
RL J. Biol. Chem. 274:14122-14129(1999).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, AND MUTAGENESIS OF LYS-3; ASP-24
RP AND 27-GLU-GLU-28.
RX PubMed=15152005; DOI=10.1074/jbc.m313666200;
RA Frick C., Atanasov A.G., Arnold P., Ozols J., Odermatt A.;
RT "Appropriate function of 11beta-hydroxysteroid dehydrogenase type 1 in the
RT endoplasmic reticulum lumen is dependent on its N-terminal region sharing
RT similar topological determinants with 50-kDa esterase.";
RL J. Biol. Chem. 279:31131-31138(2004).
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 (By similarity).
CC {ECO:0000250}.
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:9665742};
CC -!- ACTIVITY REGULATION: Inhibited by diisopropylphosphofluoridate (DFP).
CC {ECO:0000269|PubMed:9665742}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein. Microsome membrane; Single-pass type II membrane
CC protein.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:9665742}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR PIR; A58922; A58922.
DR AlphaFoldDB; Q7M370; -.
DR SMR; Q7M370; -.
DR STRING; 9986.ENSOCUP00000020824; -.
DR ESTHER; rabit-Q7M370; Arylacetamide_deacetylase.
DR iPTMnet; Q7M370; -.
DR eggNOG; KOG1515; Eukaryota.
DR InParanoid; Q7M370; -.
DR Proteomes; UP000001811; Unplaced.
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; IDA:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; 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; PS01174; LIPASE_GDXG_SER; 1.
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..398
FT /note="Arylacetamide deacetylase"
FT /id="PRO_0000071544"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..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 ECO:0000269|PubMed:9665742"
FT ACT_SITE 342
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 372
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000303|PubMed:9665742"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000303|PubMed:9665742"
FT DISULFID 115..339
FT /evidence="ECO:0000269|PubMed:9665742"
FT MUTAGEN 3
FT /note="K->I: No effect on membrane topology. Inverted
FT topology; when associated with N-24; Q-27 and Q-28, or with
FT N-24; K-27 and K-28."
FT /evidence="ECO:0000269|PubMed:10318829,
FT ECO:0000269|PubMed:15152005"
FT MUTAGEN 24
FT /note="D->K: Inverted topology; when associated with I-3;
FT Q-27 and Q-28, or with I-3; K-27 and K-28."
FT /evidence="ECO:0000269|PubMed:15152005"
FT MUTAGEN 27..28
FT /note="EE->KK,QQ: No effect on topology; when associated
FT with K-24. Inverted topology; when associated with I-3 and
FT K-24."
FT /evidence="ECO:0000269|PubMed:15152005"
SQ SEQUENCE 398 AA; 45329 MW; 3478177212F30591 CRC64;
GVKTVLLLIV GVLGAYYVYT PLPDNIEEPW RLLWVNAHMK TLTNLALFAE YLGSNIFMNT
VKFLTSFQEV PPTSDENVTV TETTFNNVPV RVYVPKRKSK TLRRGLFYIH GGGWCVGSAA
LSGYDLLSRR TADRLDVVVV STNYRLAPEY HFPIQFEDVY DALKWFLRQD VLEKYGVDPE
RVGVSGDSAG GNLAAAVAQQ LIKDPDVKIK LKTQSLIYPA LQTLDMDLPS YRENAQFPIL
SKSFMVRLWS EYFTSDRSLE KAMLLNQHVP VESSHLFKFT NWSSLLPEKF KKGHVYNTPT
YGSSELARKY PGFLDVRAAP LLADDAQLRG FPLTYVITCQ YDVLRDDGVM YVTRLRNAGV
QVTHNHIEDG FHGALSYNGF KTGYRVEKQY FEWLRENV
