ID   AAAD_BOVIN              Reviewed;         399 AA.
AC   Q0P5B7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Arylacetamide deacetylase;
DE            EC=3.1.1.3;
GN   Name=AADAC;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; BC120261; AAI20262.1; -; mRNA.
DR   RefSeq; NP_001069259.1; NM_001075791.2.
DR   AlphaFoldDB; Q0P5B7; -.
DR   SMR; Q0P5B7; -.
DR   STRING; 9913.ENSBTAP00000015373; -.
DR   ESTHER; bovin-aaad; Arylacetamide_deacetylase.
DR   PaxDb; Q0P5B7; -.
DR   PeptideAtlas; Q0P5B7; -.
DR   PRIDE; Q0P5B7; -.
DR   GeneID; 519557; -.
DR   KEGG; bta:519557; -.
DR   CTD; 13; -.
DR   eggNOG; KOG1515; Eukaryota.
DR   InParanoid; Q0P5B7; -.
DR   OrthoDB; 1263520at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017171; F:serine hydrolase activity; IBA:GO_Central.
DR   GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IBA:GO_Central.
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   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..399
FT                   /note="Arylacetamide deacetylase"
FT                   /id="PRO_0000269569"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..25
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..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:0000255|PROSITE-ProRule:PRU10038"
FT   ACT_SITE        343
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        373
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        116..340
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   399 AA;  45604 MW;  B18B0BB5BFC0126C CRC64;
     MRKKYFGFLI LGVLLAGYIY VPLPDNVEEP WKIMLLNTFL KTSSYLALFG EILGLNHFMK
     SMALFSRIQG FPPTSDENII VKDTTFNDIP VRIYVPQQKT KSLRRGLFYI HGGGWCFGSN
     DYYSYDLLSR WTAERLDAVV ISTNYRLAPK YHFPVQFEDV YTALKWFLDP QNLESYGVDP
     GRIGISGDSA GGNLAAAVAQ QLLEDPDVKI KLKVQTLIYP ALQNFDFDLP SYRENAHYPV
     LSKSLMVRFW SEYFTTDRSL KKAMLSNQHI PLESSNLFKF VNWSSLLPEK FKKGHIYKTP
     THGSSELAKK YPGILDVKAS PLLADDSKLR GLPLTYVITC QYDVLRDDGL MYVTRLQKSG
     VQVIHNHVEG AFHGTLAFLF TKVGYRAANQ YINWLHENL