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Protein

Arylacetamide deacetylase

Gene

Aadac

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 similarity1 Publication

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

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

GO - Molecular functioni

GO - Biological processi

  • lipid metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

SABIO-RKQ9QZH8.

Protein family/group databases

ESTHERiratno-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi631440. 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

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3509586.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Arylacetamide deacetylasePRO_0000071545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence analysis
Disulfide bondi115 ↔ 339By similarity
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence analysis
Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9QZH8.
PRIDEiQ9QZH8.

Expressioni

Tissue specificityi

Highest levels in liver with lower levels in jejunum, kidney and testis.1 Publication

Interactioni

Protein-protein interaction databases

MINTiMINT-4568634.
STRINGi10116.ENSRNOP00000064056.

Structurei

3D structure databases

ProteinModelPortaliQ9QZH8.
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.
HOGENOMiHOG000033738.
HOVERGENiHBG058974.
InParanoidiQ9QZH8.
KOiK13616.
PhylomeDBiQ9QZH8.

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. 1 hit.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QZH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRTIFLLIS VVLVAYYIYI PLPDDIEEPW KIILGNTLLK LGGDLASFGE
60 70 80 90 100
LLGLNHFMDT VQLFMRFQVV PPTSDENVTV METDFNSVPV RIYIPKRKST
110 120 130 140 150
TLRRGLFFIH GGGWCLGSAA YFMYDTLSRR TAHRLDAVVV STDYGLAPKY
160 170 180 190 200
HFPKQFEDVY HSLRWFLQED ILEKYGVDPR RVGVSGDSAG GNLTAAVTQQ
210 220 230 240 250
ILQDPDVKIK LKVQALIYPA LQALDMNVPS QQENSQYPLL TRSLLIRFWS
260 270 280 290 300
EYFTTDRDLE KAMLLNQHVP VEFSHLLQFV NWSSLLPQRY KKGYFYKTPT
310 320 330 340 350
PGSLELAQKY PGFTDVKACP LLANDSILHH LPMTYIITCQ YDVLRDDGLM
360 370 380 390
YVKRLQNTGV HVTHHHIEDG FHGALTLPGL KITYRMQNQY LNWLHKNL
Length:398
Mass (Da):45,693
Last modified:January 23, 2007 - v3
Checksum:i7DDFBC7BDDEC228E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182426 mRNA. Translation: AAD56394.1.
AF264017 Genomic DNA. Translation: AAF74757.1.
RefSeqiNP_065413.1. NM_020538.1.
UniGeneiRn.48732.

Genome annotation databases

GeneIDi57300.
KEGGirno:57300.
UCSCiRGD:631440. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182426 mRNA. Translation: AAD56394.1.
AF264017 Genomic DNA. Translation: AAF74757.1.
RefSeqiNP_065413.1. NM_020538.1.
UniGeneiRn.48732.

3D structure databases

ProteinModelPortaliQ9QZH8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4568634.
STRINGi10116.ENSRNOP00000064056.

Chemistry

ChEMBLiCHEMBL3509586.

Protein family/group databases

ESTHERiratno-aryla. Hormone-sensitive_lipase_like_1.
MEROPSiS09.991.

Proteomic databases

PaxDbiQ9QZH8.
PRIDEiQ9QZH8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi57300.
KEGGirno:57300.
UCSCiRGD:631440. rat.

Organism-specific databases

CTDi13.
RGDi631440. Aadac.

Phylogenomic databases

eggNOGiKOG1515. Eukaryota.
COG0657. LUCA.
HOGENOMiHOG000033738.
HOVERGENiHBG058974.
InParanoidiQ9QZH8.
KOiK13616.
PhylomeDBiQ9QZH8.

Enzyme and pathway databases

SABIO-RKQ9QZH8.

Miscellaneous databases

PROiQ9QZH8.

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. 1 hit.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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 / MRNA].
    Strain: Brown Norway and Sprague-Dawley.
    Tissue: Brain.
  2. "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_RAT
AccessioniPrimary (citable) accession number: Q9QZH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 100 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. 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.