IED ID | IndEnz0005000355 |
Enzyme Type ID | lipase000355 |
Protein Name |
Liver carboxylesterase 1F EC 3.1.1.1 Carboxyesterase ES-4 Kidney microsomal carboxylesterase Microsomal palmitoyl-CoA hydrolase |
Gene Name | Ces1f |
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 | MCLSFLFLVSLATCVVYGNPSSPPVVDTTKGKVLGKYVSLEGVTQSVAVFLGVPFAKPPLGSLRFAPPQPAEPWSFVKNTTTYPPMCSQDAAKGQRMNDLLTNRKEKIHLEFSEDCLYLNIYTPADFTKNSRLPVMVWIHGGGMTLGGASTYDGRVLSAYENVVVVAIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALHWVQDNIANFGGDPGSVTIFGESAGGFSVSVLVLSPLTKNLFHRAISESGVVFLPGLLTKDVRPAAKQIADMAGCETTTSAIIVHCLRQKTEEELLEIMKKMNLIKLSSQRDNKESYHFLSTVVDNVVLPKDPKEILAEKNFNTVPYIVGINKQECGWLLPTMMGFVPADVELDKKMAITLLEKFASLYGIPEDIIPVAIEKYRKGSDDSIKIRDGILAFIGDVSFSIPSVMVSRDHRDAGAPTYMYEYQYYPSFSSPQRPKHVVGDHADDLYSVFGAPILRDGASEEEIKLSKMVMKFWANFARNGNPNGRGLPHWPQYDQKEEYLQIGATTQQSQRLKAEEVAFWTQLLAKRQPQPHHNEL |
Enzyme Length | 561 |
Uniprot Accession Number | Q64573 |
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=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:0000269|PubMed:12230550};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000305|PubMed:12230550}; |
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 (PubMed:12230550). 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 (By similarity). {ECO:0000250|UniProtKB:Q91WU0, ECO:0000269|PubMed:12230550}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (2); Glycosylation (1); Motif (1); Sequence conflict (9); Signal peptide (1) |
Keywords | Cytoplasm;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Lipid droplet;Microsome;Reference proteome;Serine esterase;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q91WU0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q91WU0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q91WU0}. Microsome {ECO:0000269|PubMed:12230550}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000250 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 558..561; /note=Prevents secretion from ER; /evidence=ECO:0000255|PROSITE-ProRule:PRU10138 |
Gene Encoded By | |
Mass | 62,308 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for retinyl palmitate {ECO:0000269|PubMed:12230550}; Note=kcat is 0.45 min(-1) with retinyl palmitate as substrate. {ECO:0000269|PubMed:12230550}; |
Metal Binding | |
Rhea ID | RHEA:21164; RHEA:13933; RHEA:13934 |
Cross Reference Brenda | 3.1.1.1; |