Detail Information for IndEnz0010000270
IED ID IndEnz0010000270
Enzyme Type ID esterase000270
Protein Name Arylacetamide deacetylase
EC 3.1.1.3
Gene Name Aadac Aada
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MGKTISLLISVVLVAYYLYIPLPDAIEEPWKVVWETAFVKIGTDLASFGELLGISHFMETIQLLMSFQEVPPTSDEHVTVMETAFDSVPVRIYIPKRKSMALRRGLFYIHGGGWCLGSAAHFSYDTLSRWTAHKLDAVVVSTDYGLAPKHHFPRQFEDVYRSLRWFLQEDVLEKYGVDPRRVGVSGDSAGGNLAAAVTQQLIQDPDVKIKLKVQALIYPALQALDTNVPSQQEGSHFPVLTRSLMVRFWSEYFTTDRGLEKAMLLNQHVPMESSHLLQFVNWSSLLPERYKKSPVYKNPTPGSSELAQKYPGFIDVKACPLLANDNILHHLPKTYIITCQYDVLRDDGLMYVKRLQNVGVHVTHHHVEDGFHGTFSFPGLKLSERMKNQYLSWLIKNL
Enzyme Length 398
Uniprot Accession Number Q99PG0
Absorption
Active Site ACT_SITE 188; /evidence=ECO:0000255|PROSITE-ProRule:PRU10038; ACT_SITE 342; /evidence=ECO:0000250|UniProtKB:Q5NUF3; ACT_SITE 372; /evidence=ECO:0000250|UniProtKB:Q5NUF3
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:19654421};
DNA Binding
EC Number 3.1.1.3
Enzyme Function FUNCTION: 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. {ECO:0000250, ECO:0000269|PubMed:19654421, ECO:0000269|PubMed:22207054}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (1); Glycosylation (1); Motif (1); Sequence conflict (2); Topological domain (2); Transmembrane (1)
Keywords Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Lipid metabolism;Membrane;Microsome;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19654421}; Single-pass type II membrane protein {ECO:0000269|PubMed:19654421}. Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: N-glycosylated. {ECO:0000269|PubMed:19654421}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 14681479; 19334288; 21267068; 21386911; 21491542; 21677750; 34450168; 34798123;
Motif MOTIF 110..112; /note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole; /evidence=ECO:0000250|UniProtKB:Q5NUF3
Gene Encoded By
Mass 45,250
Kinetics
Metal Binding
Rhea ID RHEA:12044
Cross Reference Brenda