EST1D_MOUSE
ID EST1D_MOUSE Reviewed; 565 AA.
AC Q8VCT4; Q91ZV9; Q924V8; Q9ULY1;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Carboxylesterase 1D {ECO:0000305};
DE AltName: Full=Carboxylesterase 3;
DE EC=3.1.1.1;
DE EC=3.1.1.67;
DE AltName: Full=Fatty acid ethyl ester synthase;
DE Short=FAEE synthase;
DE AltName: Full=Triacylglycerol hydrolase;
DE Short=TGH;
DE Flags: Precursor;
GN Name=Ces1d {ECO:0000312|MGI:MGI:2148202};
GN Synonyms=Ces1 {ECO:0000303|PubMed:15269189}, Ces3;
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] {ECO:0000305, ECO:0000312|EMBL:BAA84996.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10518925; DOI=10.1016/s0014-5793(99)01111-4;
RA Mori M., Hosokawa M., Ogasawara Y., Tsukada E., Chiba K.;
RT "cDNA cloning, characterization and stable expression of novel human brain
RT carboxylesterase.";
RL FEBS Lett. 458:17-22(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK58067.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/J {ECO:0000312|EMBL:AAK58067.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAK58067.1};
RX PubMed=11470237; DOI=10.1016/s1388-1981(01)00133-0;
RA Dolinsky V.W., Sipione S., Lehner R., Vance D.E.;
RT "The cloning and expression of a murine triacylglycerol hydrolase cDNA and
RT the structure of its corresponding gene.";
RL Biochim. Biophys. Acta 1532:162-172(2001).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAB60698.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-38, CATALYTIC ACTIVITY,
RP SUBUNIT, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB60698.1};
RC TISSUE=Liver {ECO:0000312|EMBL:BAB60698.1};
RX PubMed=15269189; DOI=10.1124/dmd.104.000620;
RA Furihata T., Hosokawa M., Koyano N., Nakamura T., Satoh T., Chiba K.;
RT "Identification of di-(2-ethylhexyl) phthalate-induced carboxylesterase 1
RT in C57BL/6 mouse liver microsomes: purification, cDNA cloning, and
RT baculovirus-mediated expression.";
RL Drug Metab. Dispos. 32:1170-1177(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5] {ECO:0000312|EMBL:AAH19198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH19198.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH19198.1};
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 [6]
RP PROTEIN SEQUENCE OF 331-337 AND 390-398, FUNCTION, LIPASE AND NEUTRAL
RP CHOLESTERYL ESTER HYDROLASE ACTIVITIES, AND SUBCELLULAR LOCATION.
RX PubMed=15220344; DOI=10.1074/jbc.m400541200;
RA Soni K.G., Lehner R., Metalnikov P., O'Donnell P., Semache M., Gao W.,
RA Ashman K., Pshezhetsky A.V., Mitchell G.A.;
RT "Carboxylesterase 3 (EC 3.1.1.1) is a major adipocyte lipase.";
RL J. Biol. Chem. 279:40683-40689(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Testis;
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).
RN [8]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-382, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Major lipase in white adipose tissue. Involved in the
CC metabolism of xenobiotics and of natural substrates. Hydrolyzes
CC triacylglycerols and monoacylglycerols, with a preference for
CC monoacylglycerols. The susceptibility of the substrate increases with
CC decreasing acyl chain length of the fatty acid moiety. Catalyzes the
CC synthesis of fatty acid ethyl esters (PubMed:15220344). Hydrolyzes
CC retinyl esters (By similarity). {ECO:0000250|UniProtKB:P16303,
CC ECO:0000269|PubMed:15220344}.
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:15269189};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl ethyl ester + H2O = a long-chain fatty
CC acid + ethanol + H(+); Xref=Rhea:RHEA:16641, ChEBI:CHEBI:13209,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236,
CC ChEBI:CHEBI:57560; EC=3.1.1.67;
CC Evidence={ECO:0000269|PubMed:15269189};
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:P16303};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000250|UniProtKB:P16303};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:15269189}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:15220344}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:15220344}. Lipid droplet
CC {ECO:0000269|PubMed:15220344}. Microsome
CC {ECO:0000250|UniProtKB:P16303}.
CC -!- TISSUE SPECIFICITY: Highest expression occurs in liver with lower
CC levels in adipose tissue, kidney, heart, intestine, lung, testis and
CC thymus. {ECO:0000269|PubMed:11470237, ECO:0000269|PubMed:15269189}.
CC -!- INDUCTION: By di-(2-ethylhexyl) phthalate.
CC {ECO:0000269|PubMed:15269189}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000255}.
CC -!- CAUTION: Was originally thought to originate from human.
CC {ECO:0000305|PubMed:10518925}.
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DR EMBL; AB025028; BAA84996.1; -; mRNA.
DR EMBL; AF378751; AAK58067.1; -; mRNA.
DR EMBL; AB023631; BAB60698.1; -; mRNA.
DR EMBL; AK078879; BAC37439.1; -; mRNA.
DR EMBL; BC019198; AAH19198.1; -; mRNA.
DR CCDS; CCDS22528.1; -.
DR RefSeq; NP_444430.2; NM_053200.2.
DR AlphaFoldDB; Q8VCT4; -.
DR SMR; Q8VCT4; -.
DR IntAct; Q8VCT4; 1.
DR STRING; 10090.ENSMUSP00000034172; -.
DR BindingDB; Q8VCT4; -.
DR ChEMBL; CHEMBL3137293; -.
DR ESTHER; mouse-Ces1d; Carb_B_Chordata.
DR MEROPS; S09.983; -.
DR CarbonylDB; Q8VCT4; -.
DR GlyGen; Q8VCT4; 2 sites.
DR iPTMnet; Q8VCT4; -.
DR PhosphoSitePlus; Q8VCT4; -.
DR SwissPalm; Q8VCT4; -.
DR CPTAC; non-CPTAC-3408; -.
DR jPOST; Q8VCT4; -.
DR MaxQB; Q8VCT4; -.
DR PaxDb; Q8VCT4; -.
DR PeptideAtlas; Q8VCT4; -.
DR PRIDE; Q8VCT4; -.
DR ProteomicsDB; 281592; -.
DR DNASU; 104158; -.
DR Ensembl; ENSMUST00000034172; ENSMUSP00000034172; ENSMUSG00000056973.
DR GeneID; 104158; -.
DR KEGG; mmu:104158; -.
DR UCSC; uc009mun.1; mouse.
DR CTD; 104158; -.
DR MGI; MGI:2148202; Ces1d.
DR VEuPathDB; HostDB:ENSMUSG00000056973; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000154623; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; Q8VCT4; -.
DR OMA; WYNGTDW; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q8VCT4; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.1; 3474.
DR Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR BioGRID-ORCS; 104158; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ces1d; mouse.
DR PRO; PR:Q8VCT4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8VCT4; protein.
DR Bgee; ENSMUSG00000056973; Expressed in gonadal fat pad and 168 other tissues.
DR Genevisible; Q8VCT4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
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:0030339; F:fatty-acyl-ethyl-ester synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004771; F:sterol esterase activity; IDA:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; TAS:ProtInc.
DR GO; GO:0046464; P:acylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0071397; P:cellular response to cholesterol; ISO:MGI.
DR GO; GO:0070417; P:cellular response to cold; IMP: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:0060086; P:circadian temperature homeostasis; IMP:MGI.
DR GO; GO:0106106; P:cold-induced thermogenesis; IMP:MGI.
DR GO; GO:0061725; P:cytosolic lipolysis; IMP:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IDA:MGI.
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:0061411; P:positive regulation of transcription from RNA polymerase II promoter in response to cold; IMP: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:0009636; P:response to toxic substance; TAS:ProtInc.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:MGI.
DR GO; GO:0019626; P:short-chain fatty acid catabolic process; IDA:MGI.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP: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 Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid droplet; Lipid metabolism; Microsome; Reference proteome;
KW Serine esterase; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:15269189"
FT CHAIN 19..565
FT /note="Carboxylesterase 1D"
FT /id="PRO_0000008583"
FT MOTIF 562..565
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 221
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P22303,
FT ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 353
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P22303"
FT ACT_SITE 466
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P22303"
FT MOD_RES 382
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P23141"
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"
FT CONFLICT 2
FT /note="G -> R (in Ref. 1; BAA84996 and 2; AAK58067)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="V -> F (in Ref. 1; BAA84996)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="G -> W (in Ref. 1; BAA84996)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="D -> H (in Ref. 3; BAB60698)"
FT /evidence="ECO:0000305"
FT CONFLICT 456..458
FT /note="AMR -> RHED (in Ref. 1; BAA84996)"
FT /evidence="ECO:0000305"
FT CONFLICT 517..520
FT /note="EYDQ -> RNMTK (in Ref. 1; BAA84996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 61788 MW; E85A9976F9916B34 CRC64;
MGLYPLIWLS LAACTAWGYP SSPPVVNTVK GKVLGKYVNL EGFTQPVAVF LGVPFAKPPL
GSLRFAPPQP AEPWSFVKNT TSYPPMCSQD AVGGQVLSEL FTNRKENIPL QFSEDCLYLN
IYTPADLTKN SRLPVMVWIH GGGLVVGGAS TYDGLALSAH ENVVVVTIQY RLGIWGFFST
GDEHSRGNWG HLDQVAALRW VQDNIANFGG NPGSVTIFGE SAGGFSVSVL VLSPLAKNLF
HRAISESGVS LTAALITTDV KPIAGLVATL SGCKTTTSAV MVHCLRQKTE DELLETSLKL
NLFKLDLLGN PKESYPFLPT VIDGVVLPKA PEEILAEKSF STVPYIVGIN KQEFGWIIPT
LMGYPLAEGK LDQKTANSLL WKSYPTLKIS ENMIPVVAEK YLGGTDDLTK KKDLFQDLMA
DVVFGVPSVI VSRSHRDAGA STYMYEFEYR PSFVSAMRPK AVIGDHGDEI FSVFGSPFLK
DGASEEETNL SKMVMKFWAN FARNGNPNGG GLPHWPEYDQ KEGYLKIGAS TQAAQRLKDK
EVSFWAELRA KESAQRPSHR EHVEL
