AADAC
entrez
13
canonical
uniprot
P22760
canonical
ensembl
ENSG00000114771
resolver
ensp
ENSP00000232892
resolver
ensp
ENSP00000524513
resolver
ensp
ENSP00000524514
resolver
ensp
ENSP00000524515
resolver
enst
ENST00000232892
resolver
enst
ENST00000854454
resolver
enst
ENST00000854455
resolver
genesymbol
AADAC
resolver
genesymbol_syn
DAC
resolver
hgnc
HGNC:17
resolver
uniprot
A8K3L3
resolver
uniprot
D3DNJ6
resolver
uniprot
Q8N1A9
resolver
uniprot_entry
AAAD_HUMAN
resolver
uniprot_sec
A8K3L3
resolver
uniprot_sec
D3DNJ6
resolver
uniprot_sec
Q8N1A9
resolver
activity_regulation
ACTIVITY REGULATION: Arylacetamide deacetylase activity is inhibited by bis(p-nitrophenyl)phosphate (BPNPP) (non competitive type inhibition), diisopropylphosphorofluoride (DFP), eserine and vinblastine (PubMed:19339378, PubMed:24464802, PubMed:27422753, PubMed:8063807). Arylacetamide deacetylase is moderately inhibited by sodium fluoride, phenylmethylsulfonyl fluoride (PMSF), and disulfiram (PubMed:19339378). Arylalkyl acylamidase activity is inhibited by eserine in a dose-dependent manner (PubMed:37002641). Acetylesterase activity is potently inhibited by diisopropylphosphorofluoride (DFP), vinblastine, and epigallocatechin gallate (EGCg) and orlistat (PubMed:34450168). Acetylesterase activity is moderately inhibited by bis(p-nitrophenyl)phosphate (BPNPP) and phenylmethylsulfonyl fluoride (PMSF) as well as digitonin and telmisartan (PubMed:34450168). {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:24464802, ECO:0000269|PubMed:27422753, ECO:0000269|PubMed:34450168, ECO:0000269|PubMed:37002641, ECO:0000269|PubMed:8063807}.
uniprot
proteins
amino_acid_sequence
MGRKSLYLLIVGILIAYYIYTPLPDNVEEPWRMMWINAHLKTIQNLATFVELLGLHHFMDSFKVVGSFDEVPPTSDENVTVTETKFNNILVRVYVPKRKSEALRRGLFYIHGGGWCVGSAALSGYDLLSRWTADRLDAVVVSTNYRLAPKYHFPIQFEDVYNALRWFLRKKVLAKYGVNPERIGISGDSAGGNLAAAVTQQLLDDPDVKIKLKIQSLIYPALQPLDVDLPSYQENSNFLFLSKSLMVRFWSEYFTTDRSLEKAMLSRQHVPVESSHLFKFVNWSSLLPERFIKGHVYNNPNYGSSELAKKYPGFLDVRAAPLLADDNKLRGLPLTYVITCQYDLLRDDGLMYVTRLRNTGVQVTHNHVEDGFHGAFSFLGLKISHRLINQYIEWLKENL
uniprot
proteins
ec_number
3.-.-.-
uniprot
proteins
ec_number
3.1.1.6
uniprot
proteins
ec_number
3.1.1.79
uniprot
proteins
ec_number
3.5.1.76
uniprot
proteins
function
FUNCTION: Catalyzes the hydrolysis of ester and amide bonds and is largely involved in prodrugs activation, xenobiotic detoxification or toxicity, and, in some contexts, lipid and indole metabolism (PubMed:17936933, PubMed:18034159, PubMed:19339378, PubMed:2043131, PubMed:21856291, PubMed:22207054, PubMed:22415931, PubMed:23542347, PubMed:24125761, PubMed:24464802, PubMed:26164127, PubMed:27422753, PubMed:33446525, PubMed:34450168, PubMed:37002641, PubMed:8063807). Prefers compounds with relatively small acyl groups, especially compounds with acetyl group (PubMed:26164127). Participates in the hydrolysis of clinical drugs including acetyl esters compounds such as eslicarbazepine, abiraterone and rifamycins (rifampicin, rifabutin, and rifapentine) and N-acetylarylamine compounds such as flutamide, N-monoacetyldapsone, and phenacetin (PubMed:19339378, PubMed:21856291, PubMed:22207054, PubMed:22415931, PubMed:24125761, PubMed:24464802, PubMed:26164127, PubMed:27422753). Participates in the hydrolysis of carcinogen such as 2-acetylaminofluorene (AAF) and propanil (PubMed:2043131, PubMed:26164127, PubMed:8063807). In addition, plays a role in lipid metabolism by hydrolyzing newly synthesized diacylglycerol, so limiting triacylglycerol synthesis for cytoplasmic storage droplet formation and for VLDL assembly (PubMed:23542347). Can also catalyzes the deacetylation of cholesterol acetate (PubMed:18034159). Moreover can play a role in metabolism of pineal indoles by catalyzing the deacetylation of N-acetylarylalkylamine compounds including N-acetylserotonin (NAS), melatonin and N-acetyltryptamine, NAS conversion being the most efficient reaction (PubMed:37002641). {ECO:0000269|PubMed:17936933, ECO:0000269|PubMed:18034159, ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:2043131, ECO:0000269|PubMed:21856291, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:22415931, ECO:0000269|PubMed:23542347, ECO:0000269|PubMed:24125761, ECO:0000269|PubMed:24464802, ECO:0000269|PubMed:26164127, ECO:0000269|PubMed:27422753, ECO:0000269|PubMed:33446525, ECO:0000269|PubMed:34450168, ECO:0000269|PubMed:37002641, ECO:0000269|PubMed:8063807}.
uniprot
proteins
mass_dalton
45734
uniprot
proteins
mutagenesis
MUTAGEN 78; /note="N->Q: Abolishes glycosylation at this site and causes moderate decrease in activity."; /evidence="ECO:0000269|PubMed:24125761"; MUTAGEN 282; /note="N->Q: Abolishes glycosylation at this site and causes substantial decrease in activity and reduced substrate affinity."; /evidence="ECO:0000269|PubMed:24125761
uniprot
proteins
post_translational_modification
PTM: Glycosylation is required for enzyme activity. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24125761}.
uniprot
proteins
protein_family
'GDXG' lipolytic enzyme family
uniprot
proteins
pubmed
12721789
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17936933
uniprot
proteins
pubmed
18034159
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19339378
uniprot
proteins
pubmed
2043131
uniprot
proteins
pubmed
21856291
uniprot
proteins
pubmed
22207054
uniprot
proteins
pubmed
22415931
uniprot
proteins
pubmed
23542347
uniprot
proteins
pubmed
24125761
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24464802
uniprot
proteins
pubmed
26164127
uniprot
proteins
pubmed
27422753
uniprot
proteins
pubmed
33446525
uniprot
proteins
pubmed
34450168
uniprot
proteins
pubmed
37002641
uniprot
proteins
pubmed
8063807
uniprot
proteins
sequence_length
399
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19339378}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q7M370}. Microsome membrane {ECO:0000269|PubMed:19339378, ECO:0000269|PubMed:22207054}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q7M370}.
uniprot
proteins
transmembrane_region
TRANSMEM 6..23; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins