IED ID | IndEnz0010001322 |
Enzyme Type ID | esterase001322 |
Protein Name |
Carboxylesterase 1F EC 3.1.1.1 Carboxylic ester hydrolase Triacylglycerol hydrolase 2 TGH-2 |
Gene Name | Ces1f CesML1 |
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 | MFLSTLFLVSLATCVICGNPSSPPVVDTAHGKVLGKHVNVEGFSQPVAVFLGIPFAKPPLGSLRFAPPQPAEPWSSVKNATTYPPMCSQDAARGQAVNDLITNRKEKIHLEFSEDCLYLNIYTPADFSKNSRLPVMVWIHGGGLKLGGASSFDGRALSAYENVVVVAIQYRLSIWGFFSTGDEHSRGNWGHLDQVAALHWVQDNIANFGGDPGSVTIFGESAGGYSVSILILSPLSKNLFHRAISESGVAFIPGMFTKDVRPITEQIAVTAGCKTTTSAVIVHCMRQKTEEELLEIMHKLNLYKLSLQGDTKNSDQFVTSVLDGVVLPKDPKEILAEKNFNTVPYIVGINKQECGWLLPTMTGFLPADVKLDKKKAIALLEQFASMTGIPEDIIPVAVEKYTKGSDDPDQIREGVLDAMGDVAFGVPSVIVSRGHRDTGAPTYMYEYQYYPSFSSPQRPKNVVGDHADDVYSVFGAPILREGASEEEINLSKMVMKFWANFARNGNPNGKGLPHWPKYDQKEGYLHIGGTTQQAQRLKEEEVTFWTQSLAKKQPQPYHNEL |
Enzyme Length | 561 |
Uniprot Accession Number | Q91WU0 |
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, ECO:0000269|PubMed:16804080}; CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000250|UniProtKB:Q64573};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000250|UniProtKB:Q64573}; |
DNA Binding | |
EC Number | 3.1.1.1 |
Enzyme Function | FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes retinyl esters (By similarity). Hydrolyzes p-nitrophenyl butyrate (PNPB), triacylglycerol and monoacylglycerol. Shows higher activity against PNPB, a short-chain fatty acid ester, than against triolein, a long-chain fatty acid ester. Shows no detectable activity against diacylglycerol, cholesterol ester or phospholipids. May play a role in adipocyte lipolysis. {ECO:0000250|UniProtKB:Q64573, ECO:0000269|PubMed:16804080}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (2); Motif (1); Sequence conflict (2); Signal peptide (1) |
Keywords | Alternative splicing;Cytoplasm;Disulfide bond;Endoplasmic reticulum;Hydrolase;Lipid droplet;Microsome;Reference proteome;Signal |
Interact With | |
Induction | INDUCTION: Induced by fasting and repressed by refeeding. {ECO:0000269|PubMed:16804080}. |
Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000305|PubMed:16804080}. Cytoplasm, cytosol {ECO:0000269|PubMed:16804080}. Endoplasmic reticulum {ECO:0000269|PubMed:16804080}. Microsome {ECO:0000250|UniProtKB:Q64573}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10725249; 20931200; 21677750; |
Motif | MOTIF 558..561; /note=Prevents secretion from ER; /evidence=ECO:0000255|PROSITE-ProRule:PRU10138 |
Gene Encoded By | |
Mass | 61,612 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:21164; RHEA:13933; RHEA:13934 |
Cross Reference Brenda |