| IED ID | IndEnz0005000415 |
| Enzyme Type ID | lipase000415 |
| Protein Name |
Arylacetamide deacetylase EC 3.1.1.3 |
| Gene Name | Aadac Aada |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MGRTIFLLISVVLVAYYIYIPLPDDIEEPWKIILGNTLLKLGGDLASFGELLGLNHFMDTVQLFMRFQVVPPTSDENVTVMETDFNSVPVRIYIPKRKSTTLRRGLFFIHGGGWCLGSAAYFMYDTLSRRTAHRLDAVVVSTDYGLAPKYHFPKQFEDVYHSLRWFLQEDILEKYGVDPRRVGVSGDSAGGNLTAAVTQQILQDPDVKIKLKVQALIYPALQALDMNVPSQQENSQYPLLTRSLLIRFWSEYFTTDRDLEKAMLLNQHVPVEFSHLLQFVNWSSLLPQRYKKGYFYKTPTPGSLELAQKYPGFTDVKACPLLANDSILHHLPMTYIITCQYDVLRDDGLMYVKRLQNTGVHVTHHHIEDGFHGALTLPGLKITYRMQNQYLNWLHKNL |
| Enzyme Length | 398 |
| Uniprot Accession Number | Q9QZH8 |
| Absorption | |
| Active Site | ACT_SITE 188; /evidence="ECO:0000250|UniProtKB:Q8BLF1, ECO:0000255|PROSITE-ProRule:PRU10038"; ACT_SITE 342; /evidence="ECO:0000250|UniProtKB:Q8BLF1"; ACT_SITE 372; /evidence="ECO:0000250|UniProtKB:Q8BLF1" |
| 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; |
| 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:22207054}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (1); Glycosylation (4); Motif (1); 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:0000250}; Single-pass type II membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| 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 | 45,693 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |