Detail Information for IndEnz0010001322
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