EST1_PIG
ID EST1_PIG Reviewed; 566 AA.
AC Q29550; O97582; P82128;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Liver carboxylesterase;
DE EC=3.1.1.1;
DE AltName: Full=Proline-beta-naphthylamidase;
DE AltName: Full=Retinyl ester hydrolase;
DE Short=REH;
DE Flags: Precursor;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1959668; DOI=10.1016/0014-5793(91)81147-z;
RA Matsushima M., Inoue H., Ichinose M., Tsukada S., Miki K., Kurokawa K.,
RA Takahashi T., Takahashi K.;
RT "The nucleotide and deduced amino acid sequences of porcine liver proline-
RT beta-naphthylamidase. Evidence for the identity with carboxylesterase.";
RL FEBS Lett. 293:37-41(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-44, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Intestinal mucosa;
RX PubMed=9799112; DOI=10.1046/j.1432-1327.1998.2570142.x;
RA David L., Guo X.-J., Villard C., Moulin A., Puigserver A.;
RT "Purification and molecular cloning of porcine intestinal glycerol-ester
RT hydrolase -- evidence for its identity with carboxylesterase.";
RL Eur. J. Biochem. 257:142-148(1998).
RN [3]
RP PROTEIN SEQUENCE OF 19-29; 66-79; 84-90; 314-326; 384-401 AND 438-452,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC TISSUE=Liver;
RX PubMed=9490062; DOI=10.1046/j.1432-1327.1998.2510863.x;
RA Schindler R., Mentlein R., Feldheim W.;
RT "Purification and characterization of retinyl ester hydrolase as a member
RT of the non-specific carboxylesterase supergene family.";
RL Eur. J. Biochem. 251:863-873(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16223870; DOI=10.1124/jpet.105.092726;
RA Landowski C.P., Lorenzi P.L., Song X., Amidon G.L.;
RT "Nucleoside ester prodrug substrate specificity of liver
RT carboxylesterase.";
RL J. Pharmacol. Exp. Ther. 316:572-580(2006).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC activation of ester and amide prodrugs. Active towards
CC triacylglycerides containing short-chain fatty acids from C2 to C6, and
CC 1(3)-monoacylglycerols containing fatty acids from C2 to C12. Inactive
CC on long-chain triacylglycerols and diacylglycerol. Hydrolyzes aromatic
CC and alkyl esters and vitamin A acetate. The hydrolysis rate depends
CC upon the amino acid promoiety and the esterification site of the
CC prodrug. Aromatic promoieties are favored, highest rates are observed
CC with phenylalanyl progdrugs, hydrolysis of valyl and isoleucyl prodrugs
CC is less efficient. With floxuridine prodrugs, activity is higher on 5'
CC monoesters than on 3' monoesters. With gemcitabine prodrugs, activity
CC is higher on 3' monoesters than on 5' monoesters.
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10039,
CC ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC -!- ACTIVITY REGULATION: Activated by CHAPS at concentrations of up to 130
CC mM, higher concentrations reduce activity. In the presence of CHAPS,
CC activity is stimulated by non-ionic detergents. Inhibited by the
CC esterase inhibitors diisopropylfluorophosphate and phenylmethylsulfonyl
CC fluoride. {ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.5 uM for retinyl palmitate {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.46 mM for 5'-L-phenylalanyl-floxuridine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=0.44 mM for 5'-D-phenylalanyl-floxuridine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=1.40 mM for 3'-D-phenylalanyl-floxuridine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=0.74 mM for 3'-L-phenylalanyl-floxuridine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=1.87 mM for 5'-L-prolyl-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.97 mM for 5'-L-leucyl-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=4.85 mM for 3'-L-prolyl-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=1.46 mM for 3'-L-leucyl-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=3.08 mM for 3'-L-lysyl-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=6.25 mM for 5'-L-lysyl-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=1.11 mM for 3'-L-isoleucyl-floxuridine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=3.00 mM for 5'-L-aspartyl-floxuridine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=0.93 mM for 3'-L-aspartyl-floxuridine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=4.12 mM for 5'-D-valyl-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=2.87 mM for 3'-L-valyl-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=3.58 mM for 5'-L-valyl-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=2.94 mM for 5'-L-isoleucyl-floxuridine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=11.23 mM for 3'-D-valyl-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.51 mM for 3'-L-phenylalanyl-gemcitabine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=0.97 mM for 3'-D-phenylalanyl-gemcitabine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=0.17 mM for 5'-L-phenylalanyl-gemcitabine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=0.22 mM for 5'-D-phenylalanyl-gemcitabine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=0.90 mM for 3'-L-valyl-gemcitabine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.94 mM for 3'-L-isoleucyl-gemcitabine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=1.43 mM for 3'-D-valyl-gemcitabine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.85 mM for 5'-L-isoleucyl-gemcitabine
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC KM=1.16 mM for 5'-D-valyl-gemcitabine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.96 mM for 5'-L-valyl-gemcitabine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.91 mM for 5'-L-phenylalanyl-BDCRB {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.90 mM for 5'-D-phenylalanyl-BDCRB {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.14 mM for pNPB {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.52 mM for pNPA {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=1.18 mM for PHEE {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.08 mM for PHBE {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.40 mM for AcPHEE {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=0.63 mM for 5' cinn-floxuridine {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=4.21 mM for CPT-11 {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC KM=8.81 mM for VACV {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC Vmax=530 nmol/h/mg enzyme with retinyl palmitate as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=1.82 nmol/min/ug enzyme with 5'-L-phenylalanyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=1.63 nmol/min/ug enzyme with 5'-D-phenylalanyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=4.05 nmol/min/ug enzyme with 3'-D-phenylalanyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=1.55 nmol/min/ug enzyme with 3'-L-phenylalanyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=1.97 nmol/min/ug enzyme with 5'-L-prolyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.92 nmol/min/ug enzyme with 5'-L-leucyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=4.53 nmol/min/ug enzyme with 3'-L-prolyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.70 nmol/min/ug enzyme with 3'-L-leucyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.59 nmol/min/ug enzyme with 3'-L-lysyl-floxuridine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=1.11 nmol/min/ug enzyme with 5'-L-lysyl-floxuridine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.16 nmol/min/ug enzyme with 3'-L-isoleucyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.33 nmol/min/ug enzyme with 5'-L-aspartyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.10 nmol/min/ug enzyme with 3'-L-aspartyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.30 nmol/min/ug enzyme with 5'-D-valyl-floxuridine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.19 nmol/min/ug enzyme with 3'-L-valyl-floxuridine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.21 nmol/min/ug enzyme with 5'-L-valyl-floxuridine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.15 nmol/min/ug enzyme with 5'-L-isoleucyl-floxuridine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.27 nmol/min/ug enzyme with 3'-D-valyl-floxuridine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=283.52 nmol/min/ug enzyme with 3'-L-phenylalanyl-gemcitabine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=406.92 nmol/min/ug enzyme with 3'-D-phenylalanyl-gemcitabine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=3.25 nmol/min/ug enzyme with 5'-L-phenylalanyl-gemcitabine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=3.19 nmol/min/ug enzyme with 5'-D-phenylalanyl-gemcitabine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.35 nmol/min/ug enzyme with 3'-L-valyl-gemcitabine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.24 nmol/min/ug enzyme with 3'-L-isoleucyl-gemcitabine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.32 nmol/min/ug enzyme with 3'-D-valyl-gemcitabine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.09 nmol/min/ug enzyme with 5'-L-isoleucyl-gemcitabine as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.13 nmol/min/ug enzyme with 5'-D-valyl-gemcitabine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.12 nmol/min/ug enzyme with 5'-L-valyl-gemcitabine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=2.33 nmol/min/ug enzyme with 5'-L-phenylalanyl-BDCRB as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=1.60 nmol/min/ug enzyme with 5'-D-phenylalanyl-BDCRB as
CC substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=82.25 nmol/min/ug enzyme with pNPB as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=60.45 nmol/min/ug enzyme with pNPA as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=11859.78 nmol/min/ug enzyme with PHEE as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=7.24 nmol/min/ug enzyme with PHBE as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=1.29 nmol/min/ug enzyme with AcPHEE as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=4.00 nmol/min/ug enzyme with 5' cinn-floxuridine as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC Vmax=0.03 nmol/min/ug enzyme with CPT-11 as substrate
CC {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062,
CC ECO:0000269|PubMed:9799112};
CC pH dependence:
CC Optimum pH is 8.0 with tributylglycerol as substrate, and 8.2 with
CC retinyl palmitate as substrate. Active from pH 4.5-9.5 with retinyl
CC palmitate as substrate. {ECO:0000269|PubMed:16223870,
CC ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; X63323; CAA44929.1; -; mRNA.
DR EMBL; AF064741; AAC70013.1; -; mRNA.
DR PIR; S19307; S19307.
DR RefSeq; NP_001302695.1; NM_001315766.1.
DR RefSeq; XP_013850047.1; XM_013994593.1.
DR PDB; 5FV4; X-ray; 2.40 A; A/B/C/D/E/F=19-562.
DR PDBsum; 5FV4; -.
DR AlphaFoldDB; Q29550; -.
DR SMR; Q29550; -.
DR STRING; 9823.ENSSSCP00000003045; -.
DR BindingDB; Q29550; -.
DR ChEMBL; CHEMBL3383; -.
DR DrugCentral; Q29550; -.
DR ESTHER; pig-EST1; Carb_B_Chordata.
DR MEROPS; S09.981; -.
DR PaxDb; Q29550; -.
DR PeptideAtlas; Q29550; -.
DR PRIDE; Q29550; -.
DR GeneID; 100736962; -.
DR KEGG; ssc:100736962; -.
DR eggNOG; KOG1516; Eukaryota.
DR OrthoDB; 754103at2759; -.
DR SABIO-RK; Q29550; -.
DR PRO; PR:Q29550; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Phosphoprotein;
KW Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..566
FT /note="Liver carboxylesterase"
FT /id="PRO_0000008577"
FT MOTIF 563..566
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 222
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 354
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 467
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..117
FT /evidence="ECO:0000250"
FT DISULFID 274..285
FT /evidence="ECO:0000250"
FT CONFLICT 18
FT /note="Missing (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="P -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..95
FT /note="VE -> AG (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..111
FT /note="TL -> IP (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="K -> R (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="L -> V (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 151..152
FT /note="PM -> ST (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..157
FT /note="VV -> LA (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="P -> T (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 254..255
FT /note="VA -> AG (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="F -> L (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="Q -> P (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 320..321
FT /note="PT -> AF (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="V -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="S -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="Y -> F (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="A -> T (in Ref. 2; AAC70013)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="T -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:5FV4"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 211..221
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:5FV4"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 395..403
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 409..424
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 426..438
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 469..474
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 486..505
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 524..531
FT /evidence="ECO:0007829|PDB:5FV4"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:5FV4"
FT HELIX 540..549
FT /evidence="ECO:0007829|PDB:5FV4"
SQ SEQUENCE 566 AA; 62016 MW; BE046545307DEDE5 CRC64;
MWLLPLVLTS LASSATWAGQ PASPPVVDTA QGRVLGKYVS LEGLAQPVAV FLGVPFAKPP
LGSLRFAPPQ PAEPWSFVKN TTSYPPMCCQ DPVVEQMTSD LFTNGKERLT LEFSEDCLYL
NIYTPADLTK RGRLPVMVWI HGGGLVLGGA PMYDGVVLAA HENVVVVAIQ YRLGIWGFFS
TGDEHSRGNW GHLDQVAALH WVQENIANFG GDPGSVTIFG ESAGGESVSV LVLSPLAKNL
FHRAISESGV ALTVALVRKD MKAAAKQIAV LAGCKTTTSA VFVHCLRQKS EDELLDLTLK
MKFLTLDFHG DQRESHPFLP TVVDGVLLPK MPEEILAEKD FNTVPYIVGI NKQEFGWLLP
TMMGFPLSEG KLDQKTATSL LWKSYPIANI PEELTPVATD KYLGGTDDPV KKKDLFLDLM
GDVVFGVPSV TVARQHRDAG APTYMYEFQY RPSFSSDKKP KTVIGDHGDE IFSVFGFPLL
KGDAPEEEVS LSKTVMKFWA NFARSGNPNG EGLPHWPMYD QEEGYLQIGV NTQAAKRLKG
EEVAFWNDLL SKEAAKKPPK IKHAEL
