| IED ID | IndEnz0005000495 |
| Enzyme Type ID | lipase000495 |
| Protein Name |
Carboxylesterase 1C EC 3.1.1.1 Carboxyesterase ES-1 E1 ES-THET Esterase-2 Liver carboxylesterase 1 Neutral retinyl ester hydrolase NREH Retinyl ester hydrolase REH |
| Gene Name | Ces1c Es2 |
| 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 | MWLCALVWASLAVCPIWGHPSSPPVVDTTKGKVLGKYVSLEGFTQPVAVFLGVPFAKPPLGSLRFAPPEPAEPWSFVKNTTTYPPMCSQDGVVGKLLADMLSTGKESIPLEFSEDCLYLNIYSPADLTKNSRLPVMVWIHGGGLIIGGASPYSGLALSAHENVVVVTIQYRLGIWGLFSTGDEHSRGNWAHLDQLAALRWVQDNIANFGGNPDSVTIFGESAGGVSVSALVLSPLAKNLFHRAISESGVVLTTNLDKKNTQAVAQMIATLSGCNNTSSAAMVQCLRQKTEAELLELTVKLDNTSMSTVIDGVVLPKTPEEILTEKSFNTVPYIVGFNKQEFGWIIPTMMGNLLSEGRMNEKMASSFLKRFSPNLNISESVIPAIIEKYLRGTDDPAKKKELLLDMFSDVFFGIPAVLMSRSLRDAGAPTYMYEFQYRPSFVSDQRPQTVQGDHGDEIFSVFGTPFLKEGASEEETNLSKLVMKFWANFARNGNPNGEGLPHWPKYDQKEGYLQIGATTQQAQKLKGEEVAFWTELLAKNPPQTEHTEHT |
| Enzyme Length | 549 |
| Uniprot Accession Number | P10959 |
| Absorption | |
| Active Site | ACT_SITE 221; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 340; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 453; /note=Charge relay system; /evidence=ECO:0000250 |
| 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:9305911}; |
| 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. Involved in the extracellular metabolism of lung surfactant (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Active from pH 4.0-8.0. {ECO:0000269|PubMed:9305911}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Glycosylation (6); Modified residue (1); Motif (1); Natural variant (1); Sequence conflict (15); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Phosphoprotein;Reference proteome;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Microsomal membrane, lumen of endoplasmic reticulum. |
| Modified Residue | MOD_RES 471; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:3235453 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 546..549; /note=Prevents secretion from ER; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 60,175 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=69 uM for retinyl palmitate {ECO:0000269|PubMed:9305911}; Vmax=3.1 nmol/min/mg enzyme with retinyl palmitate as substrate {ECO:0000269|PubMed:9305911}; |
| Metal Binding | |
| Rhea ID | RHEA:21164 |
| Cross Reference Brenda | 3.1.1.1; |