Detail Information for IndEnz0010000068
IED ID IndEnz0010000068
Enzyme Type ID esterase000068
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;