CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020003
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Arylacetamide deacetylase 
Protein Synonyms/Alias
  
Gene Name
 Aadac 
Gene Synonyms/Alias
 Aada 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
149TDYGLAPKHHFPRQFubiquitination[1]
174LQEDVLEKYGVDPRRubiquitination[1]
208LIQDPDVKIKLKVQAubiquitination[1]
297YKKSPVYKNPTPGSSubiquitination[1]
309GSSELAQKYPGFIDVubiquitination[1]
317YPGFIDVKACPLLANubiquitination[1]
333NILHHLPKTYIITCQacetylation[2]
396QYLSWLIKNL*****acetylation[3]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [3] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758
Functional Description
 Arylacetamide deacetylation is an important enzyme activity in the metabolic activation of arylamine substrates to ultimate carcinogens (By similarity). Displays major serine hydrolase activity in liver microsomes. Displays cellular triglyceride lipase activity in liver. Increases intracellular fatty acids derived from hydrolysis of newly formed triglyceride stores. 
Sequence Annotation
 ACT_SITE 110 110 Potential.
 ACT_SITE 188 188 Potential.
 CARBOHYD 281 281 N-linked (GlcNAc...) (Potential).
 DISULFID 115 339 By similarity.  
Keyword
 Complete proteome; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Microsome; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 398 AA 
Protein Sequence
MGKTISLLIS VVLVAYYLYI PLPDAIEEPW KVVWETAFVK IGTDLASFGE LLGISHFMET 60
IQLLMSFQEV PPTSDEHVTV METAFDSVPV RIYIPKRKSM ALRRGLFYIH GGGWCLGSAA 120
HFSYDTLSRW TAHKLDAVVV STDYGLAPKH HFPRQFEDVY RSLRWFLQED VLEKYGVDPR 180
RVGVSGDSAG GNLAAAVTQQ LIQDPDVKIK LKVQALIYPA LQALDTNVPS QQEGSHFPVL 240
TRSLMVRFWS EYFTTDRGLE KAMLLNQHVP MESSHLLQFV NWSSLLPERY KKSPVYKNPT 300
PGSSELAQKY PGFIDVKACP LLANDNILHH LPKTYIITCQ YDVLRDDGLM YVKRLQNVGV 360
HVTHHHVEDG FHGTFSFPGL KLSERMKNQY LSWLIKNL 398 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0004091; F:carboxylesterase activity; IEA:InterPro.
 GO:0019213; F:deacetylase activity; ISS:UniProtKB.
 GO:0050253; F:retinyl-palmitate esterase activity; IEA:EC.
 GO:0017171; F:serine hydrolase activity; IDA:UniProtKB.
 GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
 GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:UniProtKB. 
Interpro
 IPR013094; AB_hydrolase_3.
 IPR017157; Arylacetamide_deacetylase.
 IPR002168; Lipase_GDXG_AS. 
Pfam
 PF07859; Abhydrolase_3 
SMART
  
PROSITE
 PS01173; LIPASE_GDXG_HIS
 PS01174; LIPASE_GDXG_SER 
PRINTS