EST2E_MOUSE
ID EST2E_MOUSE Reviewed; 559 AA.
AC Q8BK48; Q8BM97; Q8VC02;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Pyrethroid hydrolase Ces2e;
DE EC=3.1.1.88;
DE AltName: Full=Carboxylic ester hydrolase {ECO:0000255|RuleBase:RU361235};
DE EC=3.1.1.- {ECO:0000255|RuleBase:RU361235};
DE AltName: Full=carboxylesterase 2E;
DE Flags: Precursor;
GN Name=Ces2e {ECO:0000312|MGI:MGI:2443170}; Synonyms=Ces5;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, Ovary, and Uterus;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and 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 [5]
RP PROTEIN SEQUENCE OF 97-108; 475-481 AND 535-540, PROTEIN SEQUENCE OF
RP N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=15123619; DOI=10.1074/jbc.m403673200;
RA Stok J.E., Huang H., Jones P.D., Wheelock C.E., Morisseau C., Hammock B.D.;
RT "Identification, expression, and purification of a pyrethroid-hydrolyzing
RT carboxylesterase from mouse liver microsomes.";
RL J. Biol. Chem. 279:29863-29869(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Carboxylesterase that catalyzes the hydrolysis of pyrethroids
CC pesticides. Hydrolyzes trans-permethrin at a rate about 22-fold higher
CC than cis-permethrin. Also hydrolyzes trans-cypermethrin. Hydrolyzes
CC retinyl esters (By similarity). {ECO:0000250|UniProtKB:G3V7J5,
CC ECO:0000269|PubMed:15123619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-trans-permethrin + H2O = (1S,3R)-3-(2,2-dichlorovinyl)-
CC 2,2-dimethylcyclopropanecarboxylate + (3-phenoxyphenyl)methanol +
CC H(+); Xref=Rhea:RHEA:30283, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:62523, ChEBI:CHEBI:62527, ChEBI:CHEBI:62531; EC=3.1.1.88;
CC Evidence={ECO:0000269|PubMed:15123619};
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:G3V7J5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000250|UniProtKB:G3V7J5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=286 uM for p-Nitrophenyl acetate {ECO:0000269|PubMed:15123619};
CC KM=0.5 uM for cypermethrin {ECO:0000269|PubMed:15123619};
CC KM=2.2 uM for (R/S)-alpha-cyano(6-methoxy-2-naphthyl)-methyl-(R/S)-
CC trans/cis-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropane carboxylate
CC {ECO:0000269|PubMed:15123619};
CC KM=0.89 uM for (R/S)-alpha-cyano(6-methoxy-2-naphthyl)-methyl-(R)-
CC (-)-2-(4-chlorophenyl)-3-methyl butanoate ((alphaR/S)(2R)-A3)
CC {ECO:0000269|PubMed:15123619};
CC KM=0.96 uM for chrysanthemic acid {ECO:0000269|PubMed:15123619};
CC Note=kcat is 94 sec(-1) with p-Nitrophenyl acetate as substrate. kcat
CC is 0.12 sec(-1) with cypermethrin as substrate. kcat is 0.11 sec(-1)
CC with (R/S)-alpha-cyano(6-methoxy-2-naphthyl)-methyl-(R/S)-trans/cis-
CC 3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropane carboxylate as
CC substrate. kcat is 0.067 sec(-1) with (R/S)-alpha-cyano(6-methoxy-2-
CC naphthyl)-methyl-(R)-(-)-2-(4-chlorophenyl)-3-methyl butanoate
CC ((alphaR/S)(2R)-A3) as substrate. kcat is 0.099 sec(-1) with
CC chrysanthemic acid as substrate.;
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:15123619}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15123619}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; AK033563; BAC28361.1; -; mRNA.
DR EMBL; AK077248; BAC36707.1; -; mRNA.
DR EMBL; AC166833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11239.1; -; Genomic_DNA.
DR EMBL; BC022148; AAH22148.1; -; mRNA.
DR EMBL; BC055062; AAH55062.1; -; mRNA.
DR CCDS; CCDS22588.1; -.
DR RefSeq; NP_001157228.1; NM_001163756.1.
DR RefSeq; NP_766347.1; NM_172759.3.
DR AlphaFoldDB; Q8BK48; -.
DR SMR; Q8BK48; -.
DR IntAct; Q8BK48; 1.
DR STRING; 10090.ENSMUSP00000034355; -.
DR ESTHER; mouse-Ces2e; Carb_B_Chordata.
DR MEROPS; S09.998; -.
DR GlyGen; Q8BK48; 1 site.
DR iPTMnet; Q8BK48; -.
DR PhosphoSitePlus; Q8BK48; -.
DR jPOST; Q8BK48; -.
DR MaxQB; Q8BK48; -.
DR PaxDb; Q8BK48; -.
DR PeptideAtlas; Q8BK48; -.
DR PRIDE; Q8BK48; -.
DR ProteomicsDB; 275892; -.
DR DNASU; 234673; -.
DR Ensembl; ENSMUST00000034355; ENSMUSP00000034355; ENSMUSG00000031886.
DR Ensembl; ENSMUST00000109410; ENSMUSP00000105037; ENSMUSG00000031886.
DR GeneID; 234673; -.
DR KEGG; mmu:234673; -.
DR UCSC; uc009nbg.2; mouse.
DR CTD; 234673; -.
DR MGI; MGI:2443170; Ces2e.
DR VEuPathDB; HostDB:ENSMUSG00000031886; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000153793; -.
DR HOGENOM; CLU_006586_13_2_1; -.
DR InParanoid; Q8BK48; -.
DR OMA; AFMEPPE; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q8BK48; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.1; 3474.
DR BioGRID-ORCS; 234673; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ces2e; mouse.
DR PRO; PR:Q8BK48; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BK48; protein.
DR Bgee; ENSMUSG00000031886; Expressed in small intestine Peyer's patch and 43 other tissues.
DR Genevisible; Q8BK48; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0102209; F:trans-permethrin hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006693; P:prostaglandin metabolic process; 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; Microsome; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:15123619"
FT CHAIN 27..559
FT /note="Pyrethroid hydrolase Ces2e"
FT /id="PRO_0000424211"
FT ACT_SITE 228
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT ACT_SITE 457
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT MOD_RES 27
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P14943"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..123
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT DISULFID 280..291
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT CONFLICT 102
FT /note="M -> F (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="I -> M (in Ref. 1; BAC28361)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="W -> R (in Ref. 1; BAC28361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 62318 MW; CC14C61034A122C3 CRC64;
MPLYKLLGWL NAVACGVLLL VLHVQGQDSA SPIRNTHTGQ VRGSLVHVKD TDIAVHTFLG
IPFAKPPVGP LRFAPPEAPE PWSGVRDGTS HPNMCLQNDN LMGSEDLKMM NLILPPISMS
EDCLYLNIYV PAHAHEGSNL PVMVWIHGGA LTVGMASMYD GSMLAATEDV VVVAIQYRLG
VLGFFSTGDQ HAKGNWGYLD QVAALRWVQQ NIVHFGGNPD RVTIFGESAG GTSVSSHVVS
PMSQGLFHGA IMESGVAVLP DLISSSSEMV HRIVANLSGC AAVNSETLMC CLRGKNEAEM
LAINKVFKII PGVVDGEFLP KHPQELMASK DFHPVPSIIG INNDEYGWIL PTIMDPAQKI
EEITRKTLPA VLKSTALKMM LPPECGDLLM EEYMGDTEDP ETLQAQFREM KGDFMFVIPA
LQVAHFQRSH APVYFYEFQH RPSFFKDFRP PYVKADHGDE IFLVFGYQFG NIKLPYTEEE
EQLSRRIMKY WANFARHGNP NSEGLPYWPV MDHDEQYLQL DIQPSVGRAL KARRLQFWTK
TLPQKIQELK GSQERHKEL
