EST1E_RAT
ID EST1E_RAT Reviewed; 561 AA.
AC Q63108;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Carboxylesterase 1E;
DE EC=3.1.1.1;
DE AltName: Full=Carboxyesterase ES-3 {ECO:0000303|PubMed:12230550};
DE AltName: Full=ES-HTEL;
DE AltName: Full=Egasyn;
DE AltName: Full=Liver carboxylesterase 3;
DE AltName: Full=pI 5.5 esterase;
DE Flags: Precursor;
GN Name=Ces1e; Synonyms=Ces1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7945287; DOI=10.1006/bbrc.1994.2341;
RA Robbi M., Beaufay H.;
RT "Cloning and sequencing of rat liver carboxylesterase ES-3 (egasyn).";
RL Biochem. Biophys. Res. Commun. 203:1404-1411(1994).
RN [2]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12230550; DOI=10.1046/j.1432-1033.2002.03121.x;
RA Sanghani S.P., Davis W.I., Dumaual N.G., Mahrenholz A., Bosron W.F.;
RT "Identification of microsomal rat liver carboxylesterases and their
RT activity with retinyl palmitate.";
RL Eur. J. Biochem. 269:4387-4398(2002).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC activation of ester and amide prodrugs. Hydrolyzes retinyl esters
CC (PubMed:12230550). {ECO:0000269|PubMed:12230550}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol +
CC H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616; Evidence={ECO:0000269|PubMed:12230550};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000305|PubMed:12230550};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.89 uM for retinyl palmitate {ECO:0000269|PubMed:12230550};
CC Note=kcat is 0.19 min(-1) with retinyl palmitate as substrate.
CC {ECO:0000269|PubMed:12230550};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Microsome membrane
CC {ECO:0000269|PubMed:7945287}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:12230550}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; X81395; CAA57158.1; -; mRNA.
DR PIR; JC2447; JC2447.
DR AlphaFoldDB; Q63108; -.
DR SMR; Q63108; -.
DR ChEMBL; CHEMBL2771; -.
DR SwissLipids; SLP:000001459; -.
DR ESTHER; ratno-Ces1e; Carb_B_Chordata.
DR GlyGen; Q63108; 3 sites.
DR iPTMnet; Q63108; -.
DR PhosphoSitePlus; Q63108; -.
DR PeptideAtlas; Q63108; -.
DR PRIDE; Q63108; -.
DR RGD; 621508; Ces1e.
DR InParanoid; Q63108; -.
DR PhylomeDB; Q63108; -.
DR BRENDA; 3.1.1.1; 5301.
DR PRO; PR:Q63108; -.
DR Proteomes; UP000002494; 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:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0001523; P:retinoid metabolic process; TAS:UniProtKB.
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 Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Lipid metabolism; Membrane; Microsome; Reference proteome; Serine esterase;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..561
FT /note="Carboxylesterase 1E"
FT /id="PRO_0000008580"
FT MOTIF 558..561
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 221
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 353
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT ACT_SITE 466
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..116
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT DISULFID 273..284
FT /evidence="ECO:0000250|UniProtKB:P23141"
SQ SEQUENCE 561 AA; 61715 MW; 1E14D66DF089B86F CRC64;
MCLYALILVF LAAFTAGGHP SSLPVVDTLQ GKVLGKYVSL EGFTQPVAVF LGVPFAKPPL
GSLRFAPPQP AEPWSFVKNT TSYPPMCSQD PVAGQIVNDL LTNWEENISL QFSEDCLYLN
IYTPADLTKR DRLPVMVWIH GGGLVLGGAS TYDGLALSTH ENVVVVVIQY RLGIWGFFST
GDEHSRGNWG HLDQVAALHW VQDNIDNFGG DPGSVTIFGE SAGGESVSVL VLSPLAKNLF
HKAISESGVA LTAGLVKKNT RPLAEKIAVV SGCKSTTSAS MVHCLRQKTE EELLETTLKL
NLFSLDLHGD SRQSYPFVPT VLDGVVLPKM PEEILAEKDF NTVPYIVGIN KQEFGWILPT
MMNYPPSDMK LDPMTATSLL KKSSFLLNLP EEAIPVAVEK YLRHTDDPDR NKDQLLELIG
DVIFGVPSVI VSRGHRDAGA RTYMYEFQYR PSFSSKMKPS TVVGDHGDEI YSVFGAPILR
GGTSKEEINL SKMMMKFWAN FARNGNPNGQ GLPHWPEYDQ KEGYLQIGAT TQQAQKLKEK
EVAFWSELLA MKPLHAGHTE L
