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Protein

Arylacetamide deacetylase

Gene

Aadac

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly (By similarity). Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity.By similarity2 Publications

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881PROSITE-ProRule annotation
Active sitei342 – 3421By similarity
Active sitei372 – 3721By similarity

GO - Molecular functioni

  • deacetylase activity Source: UniProtKB
  • lipase activity Source: MGI
  • serine hydrolase activity Source: UniProtKB
  • triglyceride lipase activity Source: UniProtKB

GO - Biological processi

  • metabolic process Source: InterPro
  • positive regulation of triglyceride catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiR-MMU-211945. Phase 1 - Functionalization of compounds.
SABIO-RKQ99PG0.

Protein family/group databases

ESTHERimouse-aryla. Hormone-sensitive_lipase_like_1.
MEROPSiS09.991.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylacetamide deacetylase (EC:3.1.1.3)
Gene namesi
Name:Aadac
Synonyms:Aada
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1915008. Aadac.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55CytoplasmicSequence analysis
Transmembranei6 – 2621Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini27 – 398372LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3509583.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Arylacetamide deacetylasePRO_0000071543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi115 ↔ 339By similarity
Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ99PG0.
MaxQBiQ99PG0.
PaxDbiQ99PG0.
PeptideAtlasiQ99PG0.
PRIDEiQ99PG0.

PTM databases

iPTMnetiQ99PG0.
PhosphoSiteiQ99PG0.
SwissPalmiQ99PG0.

Expressioni

Tissue specificityi

Highest levels in liver with lower levels in jejunum and kidney.2 Publications

Gene expression databases

BgeeiQ99PG0.
CleanExiMM_AADAC.
GenevisibleiQ99PG0. MM.

Interactioni

Protein-protein interaction databases

IntActiQ99PG0. 3 interactions.
MINTiMINT-1838544.
STRINGi10090.ENSMUSP00000029325.

Structurei

3D structure databases

ProteinModelPortaliQ99PG0.
SMRiQ99PG0. Positions 69-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi110 – 1123Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1515. Eukaryota.
COG0657. LUCA.
GeneTreeiENSGT00550000074556.
HOGENOMiHOG000033738.
HOVERGENiHBG058974.
InParanoidiQ99PG0.
KOiK13616.
OMAiANDNILH.
OrthoDBiEOG7HB599.
PhylomeDBiQ99PG0.
TreeFamiTF314978.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR002168. Lipase_GDXG_HIS_AS.
IPR033140. Lipase_GDXG_put_SER_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
[Graphical view]
PIRSFiPIRSF037251. Arylacetamide_deacetylase. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99PG0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKTISLLIS VVLVAYYLYI PLPDAIEEPW KVVWETAFVK IGTDLASFGE
60 70 80 90 100
LLGISHFMET IQLLMSFQEV PPTSDEHVTV METAFDSVPV RIYIPKRKSM
110 120 130 140 150
ALRRGLFYIH GGGWCLGSAA HFSYDTLSRW TAHKLDAVVV STDYGLAPKH
160 170 180 190 200
HFPRQFEDVY RSLRWFLQED VLEKYGVDPR RVGVSGDSAG GNLAAAVTQQ
210 220 230 240 250
LIQDPDVKIK LKVQALIYPA LQALDTNVPS QQEGSHFPVL TRSLMVRFWS
260 270 280 290 300
EYFTTDRGLE KAMLLNQHVP MESSHLLQFV NWSSLLPERY KKSPVYKNPT
310 320 330 340 350
PGSSELAQKY PGFIDVKACP LLANDNILHH LPKTYIITCQ YDVLRDDGLM
360 370 380 390
YVKRLQNVGV HVTHHHVEDG FHGTFSFPGL KLSERMKNQY LSWLIKNL
Length:398
Mass (Da):45,250
Last modified:January 23, 2007 - v3
Checksum:i77F62E505B70D208
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011A → T in AAH19999 (PubMed:15489334).Curated
Sequence conflicti101 – 1011A → T in AAH54823 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF306788 Genomic DNA. Translation: AAG60035.1.
BC019999 mRNA. Translation: AAH19999.1.
BC054823 mRNA. Translation: AAH54823.1.
CCDSiCCDS17375.1.
RefSeqiNP_075872.1. NM_023383.1.
UniGeneiMm.24547.

Genome annotation databases

EnsembliENSMUST00000029325; ENSMUSP00000029325; ENSMUSG00000027761.
GeneIDi67758.
KEGGimmu:67758.
UCSCiuc008piz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF306788 Genomic DNA. Translation: AAG60035.1.
BC019999 mRNA. Translation: AAH19999.1.
BC054823 mRNA. Translation: AAH54823.1.
CCDSiCCDS17375.1.
RefSeqiNP_075872.1. NM_023383.1.
UniGeneiMm.24547.

3D structure databases

ProteinModelPortaliQ99PG0.
SMRiQ99PG0. Positions 69-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99PG0. 3 interactions.
MINTiMINT-1838544.
STRINGi10090.ENSMUSP00000029325.

Chemistry

ChEMBLiCHEMBL3509583.

Protein family/group databases

ESTHERimouse-aryla. Hormone-sensitive_lipase_like_1.
MEROPSiS09.991.

PTM databases

iPTMnetiQ99PG0.
PhosphoSiteiQ99PG0.
SwissPalmiQ99PG0.

Proteomic databases

EPDiQ99PG0.
MaxQBiQ99PG0.
PaxDbiQ99PG0.
PeptideAtlasiQ99PG0.
PRIDEiQ99PG0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029325; ENSMUSP00000029325; ENSMUSG00000027761.
GeneIDi67758.
KEGGimmu:67758.
UCSCiuc008piz.1. mouse.

Organism-specific databases

CTDi13.
MGIiMGI:1915008. Aadac.

Phylogenomic databases

eggNOGiKOG1515. Eukaryota.
COG0657. LUCA.
GeneTreeiENSGT00550000074556.
HOGENOMiHOG000033738.
HOVERGENiHBG058974.
InParanoidiQ99PG0.
KOiK13616.
OMAiANDNILH.
OrthoDBiEOG7HB599.
PhylomeDBiQ99PG0.
TreeFamiTF314978.

Enzyme and pathway databases

ReactomeiR-MMU-211945. Phase 1 - Functionalization of compounds.
SABIO-RKQ99PG0.

Miscellaneous databases

PROiQ99PG0.
SOURCEiSearch...

Gene expression databases

BgeeiQ99PG0.
CleanExiMM_AADAC.
GenevisibleiQ99PG0. MM.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR002168. Lipase_GDXG_HIS_AS.
IPR033140. Lipase_GDXG_put_SER_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
[Graphical view]
PIRSFiPIRSF037251. Arylacetamide_deacetylase. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the rodent genes for arylacetamide deacetylase, a putative microsomal lipase, and evidence for transcriptional regulation."
    Trickett J.I., Patel D.D., Knight B.L., Saggerson E.D., Gibbons G.F., Pease R.J.
    J. Biol. Chem. 276:39522-39532(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvEvTacfBr.
    Tissue: Spleen.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.
  4. "Arylacetamide deacetylase attenuates fatty-acid-induced triacylglycerol accumulation in rat hepatoma cells."
    Lo V., Erickson B., Thomason-Hughes M., Ko K.W., Dolinsky V.W., Nelson R., Lehner R.
    J. Lipid Res. 51:368-377(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
  5. "Species differences in tissue distribution and enzyme activities of arylacetamide deacetylase in human, rat, and mouse."
    Kobayashi Y., Fukami T., Nakajima A., Watanabe A., Nakajima M., Yokoi T.
    Drug Metab. Dispos. 40:671-679(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiAAAD_MOUSE
AccessioniPrimary (citable) accession number: Q99PG0
Secondary accession number(s): Q8VCF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.