| IED ID | IndEnz0005000484 |
| Enzyme Type ID | lipase000484 |
| Protein Name |
Liver carboxylesterase 1 EC 3.1.1.1 Acyl-coenzyme A:cholesterol acyltransferase Carboxylesterase 1G Cholesteryl ester hydrolase CEH EC 3.1.1.13 ES-x |
| Gene Name | Ces1 Ces1g |
| 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 | MWLCALSLISLTACLSLGHPSLPPVVHTVHGKVLGKYVTLEGFSQPVAVFLGVPFAKPPLGSLRFAPPEPAEPWSFVKHTTSYPPLCYQNPEAALRLAELFTNQRKIIPHKFSEDCLYLNIYTPADLTQNSRLPVMVWIHGGGLVIDGASTYDGVPLAVHENVVVVVIQYRLGIWGFFSTEDEHSRGNWGHLDQVAALHWVQDNIANFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAIAQSSVIFNPCLFGRAARPLAKKIAALAGCKTTTSAAMVHCLRQKTEDELLEVSLKMKFGTVDFLGDPRESYPFLPTVIDGVLLPKAPEEILAEKSFNTVPYMVGINKHEFGWIIPMFLDFPLSERKLDQKTAASILWQAYPILNISEKLIPAAIEKYLGGTEDPATMTDLFLDLIGDIMFGVPSVIVSRSHRDAGAPTYMYEYQYRPSFVSDDRPQELLGDHADELFSVWGAPFLKEGASEEEINLSKMVMKFWANFARNGNPNGEGLPHWPEYDQKEGYLQIGVPAQAAHRLKDKEVDFWTELRAKETAERSSHREHVEL |
| Enzyme Length | 565 |
| Uniprot Accession Number | Q8VCC2 |
| Absorption | |
| Active Site | ACT_SITE 221; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 353; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141; ACT_SITE 466; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10039}; CATALYTIC ACTIVITY: Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate + cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823, ChEBI:CHEBI:46898; Evidence={ECO:0000250|UniProtKB:P23141};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876; Evidence={ECO:0000250|UniProtKB:P23141}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000250|UniProtKB:P23141};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000250|UniProtKB:P23141}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin E2 1-glyceryl ester = glycerol + H(+) + prostaglandin E2; Xref=Rhea:RHEA:48296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:90230, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:P23141};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48297; Evidence={ECO:0000250|UniProtKB:P23141}; CATALYTIC ACTIVITY: Reaction=a cholesterol ester + H2O = a fatty acid + cholesterol + H(+); Xref=Rhea:RHEA:36403, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:28868; EC=3.1.1.13; Evidence={ECO:0000250|UniProtKB:P23141};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36404; Evidence={ECO:0000250|UniProtKB:P23141}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin F2alpha 1-glyceryl ester = glycerol + H(+) + prostaglandin F2alpha; Xref=Rhea:RHEA:48300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57404, ChEBI:CHEBI:90233; Evidence={ECO:0000250|UniProtKB:P23141};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48301; Evidence={ECO:0000250|UniProtKB:P23141}; |
| DNA Binding | |
| EC Number | 3.1.1.1; 3.1.1.13 |
| Enzyme Function | FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate. Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins. Hydrolyzes cellular cholesteryl esters to free cholesterols and promotes reverse cholesterol transport (RCT) by facilitating both the initial and final steps in the process. First of all, allows free cholesterol efflux from macrophages to extracellular cholesterol acceptors and secondly, releases free cholesterol from lipoprotein-delivered cholesteryl esters in the liver for bile acid synthesis or direct secretion into the bile. {ECO:0000250|UniProtKB:P23141}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Glycosylation (2); Modified residue (1); Sequence conflict (3); Signal peptide (1) |
| Keywords | Cytoplasm;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Lipid droplet;Lipid metabolism;Phosphoprotein;Reference proteome;Serine esterase;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated in liver upon feeding a diet enriched in cholestyramine or cholate. {ECO:0000269|PubMed:9565681}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P23141}. Cytoplasm {ECO:0000250|UniProtKB:P23141}. Lipid droplet {ECO:0000250|UniProtKB:P23141}. Note=Moves from cytoplasm to lipid droplets upon lipid loading. Associates with lipid droplets independently of triglycerides (TG) content of the droplets and hydrolyzes cholesteryl esters more efficiently from mixed droplets. {ECO:0000250|UniProtKB:P23141}. |
| Modified Residue | MOD_RES 378; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P23141 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11981826; 16141072; 19651238; 20931200; 21267068; 21677750; 22806626; 23012479; 23145182; 24038130; 24194565; 25356765; 26976727; 27881673; 29259301; 9069116; |
| Motif | |
| Gene Encoded By | |
| Mass | 62,680 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21164; RHEA:33875; RHEA:33876; RHEA:26132; RHEA:26133; RHEA:48296; RHEA:48297; RHEA:36403; RHEA:36404; RHEA:48300; RHEA:48301 |
| Cross Reference Brenda | 3.1.1.1; |