Aadac
entrez
57300
canonical
uniprot
Q9QZH8
canonical
ensembl
ENSRNOG00000013950
resolver
ensp
ENSRNOP00000018761
resolver
genesymbol
Aadac
resolver
genesymbol_syn
Aada
resolver
uniprot_entry
AAAD_RAT
resolver
amino_acid_sequence
MGRTIFLLISVVLVAYYIYIPLPDDIEEPWKIILGNTLLKLGGDLASFGELLGLNHFMDTVQLFMRFQVVPPTSDENVTVMETDFNSVPVRIYIPKRKSTTLRRGLFFIHGGGWCLGSAAYFMYDTLSRRTAHRLDAVVVSTDYGLAPKYHFPKQFEDVYHSLRWFLQEDILEKYGVDPRRVGVSGDSAGGNLTAAVTQQILQDPDVKIKLKVQALIYPALQALDMNVPSQQENSQYPLLTRSLLIRFWSEYFTTDRDLEKAMLLNQHVPVEFSHLLQFVNWSSLLPQRYKKGYFYKTPTPGSLELAQKYPGFTDVKACPLLANDSILHHLPMTYIITCQYDVLRDDGLMYVKRLQNTGVHVTHHHIEDGFHGALTLPGLKITYRMQNQYLNWLHKNL
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 (By similarity) (PubMed:22207054, PubMed:37002641). Prefers compounds with relatively small acyl groups, especially compounds with acetyl group (By similarity). 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:22207054). Participates in the hydrolysis of carcinogen such as 2-acetylaminofluorene (AAF) and propanil (By similarity). 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 (By similarity). Can also catalyzes the deacetylation of cholesterol acetate (By similarity). 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:0000250|UniProtKB:P22760, ECO:0000250|UniProtKB:Q99PG0, ECO:0000269|PubMed:22207054, ECO:0000269|PubMed:37002641}.
uniprot
proteins
mass_dalton
45693
uniprot
proteins
post_translational_modification
PTM: Glycosylation is required for enzyme activity. {ECO:0000250|UniProtKB:P22760}.
uniprot
proteins
protein_family
'GDXG' lipolytic enzyme family
uniprot
proteins
pubmed
11481320
uniprot
proteins
pubmed
22207054
uniprot
proteins
pubmed
37002641
uniprot
proteins
sequence_length
398
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22760}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P22760}. Microsome membrane {ECO:0000250|UniProtKB:P22760}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P22760}.
uniprot
proteins
transmembrane_region
TRANSMEM 6..26; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins