EST1E_MOUSE
ID EST1E_MOUSE Reviewed; 562 AA.
AC Q64176;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Carboxylesterase 1E {ECO:0000305};
DE EC=3.1.1.1 {ECO:0000255|PROSITE-ProRule:PRU10039};
DE AltName: Full=Egasyn;
DE AltName: Full=Liver carboxylesterase 22;
DE Short=Es-22;
DE Short=Esterase-22;
DE Flags: Precursor;
GN Name=Ces1e {ECO:0000312|MGI:MGI:95432}; Synonyms=Es22;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1783403; DOI=10.1016/0888-7543(91)90020-f;
RA Ovnic M., Swank R.T., Fletcher C., Zhen L., Novak E.K., Baumann H.,
RA Heintz N., Ganschow R.E.;
RT "Characterization and functional expression of a cDNA encoding egasyn
RT (esterase-22): the endoplasmic reticulum-targeting protein of beta-
RT glucuronidase.";
RL Genomics 11:956-967(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC activation of ester and amide prodrugs. Hydrolyzes retinyl esters.
CC {ECO:0000250|UniProtKB:Q63108}.
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:0000250|UniProtKB:Q63108};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000250|UniProtKB:Q63108};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q63108}. Microsome membrane
CC {ECO:0000250|UniProtKB:Q63108}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; S80191; AAB21335.1; -; mRNA.
DR EMBL; BC019208; AAH19208.1; -; mRNA.
DR CCDS; CCDS22529.1; -.
DR PIR; A55281; A55281.
DR RefSeq; NP_598421.1; NM_133660.3.
DR AlphaFoldDB; Q64176; -.
DR SMR; Q64176; -.
DR CORUM; Q64176; -.
DR IntAct; Q64176; 1.
DR STRING; 10090.ENSMUSP00000034173; -.
DR ESTHER; mouse-Ces1e; Carb_B_Chordata.
DR GlyGen; Q64176; 3 sites.
DR iPTMnet; Q64176; -.
DR PhosphoSitePlus; Q64176; -.
DR jPOST; Q64176; -.
DR MaxQB; Q64176; -.
DR PaxDb; Q64176; -.
DR PRIDE; Q64176; -.
DR ProteomicsDB; 275784; -.
DR DNASU; 13897; -.
DR Ensembl; ENSMUST00000034173; ENSMUSP00000034173; ENSMUSG00000061959.
DR GeneID; 13897; -.
DR KEGG; mmu:13897; -.
DR UCSC; uc009muo.2; mouse.
DR CTD; 13897; -.
DR MGI; MGI:95432; Ces1e.
DR VEuPathDB; HostDB:ENSMUSG00000061959; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000158564; -.
DR InParanoid; Q64176; -.
DR OMA; FSEGKMD; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q64176; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.1; 3474.
DR BioGRID-ORCS; 13897; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ces1e; mouse.
DR PRO; PR:Q64176; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q64176; protein.
DR Bgee; ENSMUSG00000061959; Expressed in left lobe of liver and 63 other tissues.
DR ExpressionAtlas; Q64176; baseline and differential.
DR Genevisible; Q64176; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
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:MGI.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; ISO:MGI.
DR GO; GO:0004771; F:sterol esterase activity; ISO:MGI.
DR GO; GO:0071397; P:cellular response to cholesterol; ISO:MGI.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISO:MGI.
DR GO; GO:0006695; P:cholesterol biosynthetic process; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; ISO:MGI.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; ISO:MGI.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:MGI.
DR GO; GO:0090205; P:positive regulation of cholesterol metabolic process; ISO:MGI.
DR GO; GO:0070857; P:regulation of bile acid biosynthetic process; ISO:MGI.
DR GO; GO:0120188; P:regulation of bile acid secretion; ISO:MGI.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:MGI.
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 Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Membrane; Microsome; Reference proteome;
KW Serine esterase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..562
FT /note="Carboxylesterase 1E"
FT /id="PRO_0000008576"
FT MOTIF 559..562
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|UniProtKB:P23141"
FT ACT_SITE 467
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..117
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT DISULFID 274..285
FT /evidence="ECO:0000250|UniProtKB:P23141"
SQ SEQUENCE 562 AA; 61582 MW; FB1A4367A0CCB2E3 CRC64;
MCLSALILVS LAAFTAGAGH PSSPPMVDTV QGKVLGKYIS LEGFTQPVAV FLGVPFAKPP
LGSLRFAPPQ PAEPWSSVKN ATSYPPMCFQ DPVTGQIVND LLTNRKEKIP LQFSEDCLYL
NIYTPADLTK SDRLPVMVWI HGGGLVLGGA STYDGLVLST HENVVVVVIQ YRLGIWGFFS
TGDEHSRGNW GHLDQVAALH WVQDNIAKFG GDPGSVTIFG ESAGGESVSV LVLSPLAKNL
FQRAISESGV ALTAGLVKKN TRPLAEKIAV ISGCKNTTSA AMVHCLRQKT EEELLGTTLK
LNLFKLDLHG DSRQSHPFVP TVLDGVLLPK MPEEILAEKN FNTVPYIVGI NKQEFGWILP
TMMNYPPSDV KLDQMTAMSL LKKSSFLLNL PEDAIAVAIE KYLRDKDYTG RNKDQLLELI
GDVVFGVPSV IVSRGHRDAG APTYMYEFQY SPSFSSEMKP DTVVGDHGDE IYSVFGAPIL
RGGTSEEEIN LSKMMMKFWA NFARNGNPNG QGLPHWPEYD QKEGYLQIGA TTQQAQKLKE
KEVAFWTELL AKKQLPTEHT EL
