EST1F_MOUSE
ID EST1F_MOUSE Reviewed; 561 AA.
AC Q91WU0; D6RHA4; Q3UWB1;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Carboxylesterase 1F {ECO:0000312|MGI:MGI:2142687};
DE EC=3.1.1.1 {ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:16804080};
DE AltName: Full=Carboxylic ester hydrolase {ECO:0000255|PROSITE-ProRule:PRU10039};
DE AltName: Full=Triacylglycerol hydrolase 2 {ECO:0000303|PubMed:16804080};
DE Short=TGH-2 {ECO:0000303|PubMed:16804080};
DE Flags: Precursor;
GN Name=Ces1f {ECO:0000312|MGI:MGI:2142687};
GN Synonyms=CesML1 {ECO:0000312|MGI:MGI:2142687};
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 {ECO:0000312|EMBL:AAH13479.1};
RN [1] {ECO:0000312|EMBL:BAE23005.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23005.1};
RC TISSUE=Colon {ECO:0000312|EMBL:BAE23005.1};
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 [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAH13479.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH13479.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH13479.1};
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 [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION BY FASTING.
RX PubMed=16804080; DOI=10.2337/db05-0585;
RA Okazaki H., Igarashi M., Nishi M., Tajima M., Sekiya M., Okazaki S.,
RA Yahagi N., Ohashi K., Tsukamoto K., Amemiya-Kudo M., Matsuzaka T.,
RA Shimano H., Yamada N., Aoki J., Morikawa R., Takanezawa Y., Arai H.,
RA Nagai R., Kadowaki T., Osuga J., Ishibashi S.;
RT "Identification of a novel member of the carboxylesterase family that
RT hydrolyzes triacylglycerol: a potential role in adipocyte lipolysis.";
RL Diabetes 55:2091-2097(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Liver;
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 (By
CC similarity). Hydrolyzes p-nitrophenyl butyrate (PNPB), triacylglycerol
CC and monoacylglycerol. Shows higher activity against PNPB, a short-chain
CC fatty acid ester, than against triolein, a long-chain fatty acid ester.
CC Shows no detectable activity against diacylglycerol, cholesterol ester
CC or phospholipids. May play a role in adipocyte lipolysis.
CC {ECO:0000250|UniProtKB:Q64573, ECO:0000269|PubMed:16804080}.
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:16804080};
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:Q64573};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000250|UniProtKB:Q64573};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000305|PubMed:16804080}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:16804080}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:16804080}. Microsome
CC {ECO:0000250|UniProtKB:Q64573}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91WU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91WU0-2; Sequence=VSP_058396, VSP_058397;
CC -!- TISSUE SPECIFICITY: Expressed in liver, white and brown adipose tissue,
CC kidney, intestine, adrenal, heart and ovary. Not detected in muscle,
CC lung, testis, brain and spleen. {ECO:0000269|PubMed:16804080}.
CC -!- INDUCTION: Induced by fasting and repressed by refeeding.
CC {ECO:0000269|PubMed:16804080}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000255, ECO:0000255|RuleBase:RU361235}.
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DR EMBL; AK136491; BAE23005.1; -; mRNA.
DR EMBL; AC162949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013479; AAH13479.1; -; mRNA.
DR CCDS; CCDS22530.1; -. [Q91WU0-1]
DR RefSeq; NP_659179.1; NM_144930.2. [Q91WU0-1]
DR AlphaFoldDB; Q91WU0; -.
DR SMR; Q91WU0; -.
DR STRING; 10090.ENSMUSP00000034178; -.
DR ESTHER; mouse-Ces1f; Carb_B_Chordata.
DR PhosphoSitePlus; Q91WU0; -.
DR SwissPalm; Q91WU0; -.
DR jPOST; Q91WU0; -.
DR MaxQB; Q91WU0; -.
DR PaxDb; Q91WU0; -.
DR PeptideAtlas; Q91WU0; -.
DR PRIDE; Q91WU0; -.
DR ProteomicsDB; 281385; -. [Q91WU0-1]
DR DNASU; 234564; -.
DR Ensembl; ENSMUST00000034178; ENSMUSP00000034178; ENSMUSG00000031725. [Q91WU0-1]
DR Ensembl; ENSMUST00000140026; ENSMUSP00000116525; ENSMUSG00000031725. [Q91WU0-2]
DR GeneID; 234564; -.
DR KEGG; mmu:234564; -.
DR UCSC; uc009mup.2; mouse. [Q91WU0-1]
DR CTD; 234564; -.
DR MGI; MGI:2142687; Ces1f.
DR VEuPathDB; HostDB:ENSMUSG00000031725; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000158564; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; Q91WU0; -.
DR OMA; FDSTHES; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q91WU0; -.
DR TreeFam; TF315470; -.
DR BioGRID-ORCS; 234564; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q91WU0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91WU0; protein.
DR Bgee; ENSMUSG00000031725; Expressed in right kidney and 68 other tissues.
DR Genevisible; Q3UWB1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
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 GO; GO:0019626; P:short-chain fatty acid catabolic process; IDA: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 Alternative splicing; Cytoplasm; Disulfide bond; Endoplasmic reticulum;
KW Hydrolase; Lipid droplet; Microsome; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..561
FT /note="Carboxylesterase 1F"
FT /id="PRO_5006993881"
FT MOTIF 558..561
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
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 DISULFID 87..116
FT /evidence="ECO:0000250|UniProtKB:Q99K10"
FT DISULFID 273..284
FT /evidence="ECO:0000250|UniProtKB:Q99K10"
FT VAR_SEQ 18..50
FT /note="GNPSSPPVVDTAHGKVLGKHVNVEGFSQPVAVF -> EGGEIDKEAVGELEK
FT IVCCSRMEPKEIPLHHLW (in isoform 2)"
FT /id="VSP_058396"
FT VAR_SEQ 51..561
FT /note="Missing (in isoform 2)"
FT /id="VSP_058397"
FT CONFLICT 209
FT /note="G -> D (in Ref. 1; BAE23005)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="K -> R (in Ref. 1; BAE23005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 61612 MW; 100313143A797B68 CRC64;
MFLSTLFLVS LATCVICGNP SSPPVVDTAH GKVLGKHVNV EGFSQPVAVF LGIPFAKPPL
GSLRFAPPQP AEPWSSVKNA TTYPPMCSQD AARGQAVNDL ITNRKEKIHL EFSEDCLYLN
IYTPADFSKN SRLPVMVWIH GGGLKLGGAS SFDGRALSAY ENVVVVAIQY RLSIWGFFST
GDEHSRGNWG HLDQVAALHW VQDNIANFGG DPGSVTIFGE SAGGYSVSIL ILSPLSKNLF
HRAISESGVA FIPGMFTKDV RPITEQIAVT AGCKTTTSAV IVHCMRQKTE EELLEIMHKL
NLYKLSLQGD TKNSDQFVTS VLDGVVLPKD PKEILAEKNF NTVPYIVGIN KQECGWLLPT
MTGFLPADVK LDKKKAIALL EQFASMTGIP EDIIPVAVEK YTKGSDDPDQ IREGVLDAMG
DVAFGVPSVI VSRGHRDTGA PTYMYEYQYY PSFSSPQRPK NVVGDHADDV YSVFGAPILR
EGASEEEINL SKMVMKFWAN FARNGNPNGK GLPHWPKYDQ KEGYLHIGGT TQQAQRLKEE
EVTFWTQSLA KKQPQPYHNE L
