EST2A_MOUSE
ID EST2A_MOUSE Reviewed; 558 AA.
AC Q8QZR3; E9Q3D0; Q3TMR2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Pyrethroid hydrolase Ces2a {ECO:0000305};
DE EC=3.1.1.88 {ECO:0000269|PubMed:15123619};
DE AltName: Full=Carboxylic ester hydrolase 2A {ECO:0000305};
DE EC=3.1.1.-;
DE AltName: Full=carboxylesterase 2A;
DE Flags: Precursor;
GN Name=Ces2a {ECO:0000312|MGI:MGI:2142491}; Synonyms=Ces6;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cecum, and Intestinal mucosa;
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] (ISOFORM 1).
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 FUNCTION.
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 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).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-209 AND LYS-296, AND
RP IDENTIFICATION BY MASS 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: Carboxylesterases that catalyzes the hydrolysis of
CC pyrethroids pesticides. Hydrolyzes permethrin faster than cypermethrin.
CC Hydrolyzes retinyl esters (By similarity).
CC {ECO:0000250|UniProtKB:Q8K3R0, 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:Q8K3R0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000250|UniProtKB:Q8K3R0};
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000250|UniProtKB:Q8K3R0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8QZR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8QZR3-2; Sequence=VSP_053352;
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; AK078953; BAC37476.1; -; mRNA.
DR EMBL; AK165784; BAE38379.1; -; mRNA.
DR EMBL; AC156564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11232.1; -; Genomic_DNA.
DR EMBL; BC024082; AAH24082.1; -; mRNA.
DR EMBL; BC024491; AAH24491.1; -; mRNA.
DR EMBL; BC024517; AAH24517.1; -; mRNA.
DR EMBL; BC025537; AAH25537.1; -; mRNA.
DR EMBL; BC025812; AAH25812.1; -; mRNA.
DR EMBL; BC026643; AAH26643.1; -; mRNA.
DR EMBL; BC031295; AAH31295.1; -; mRNA.
DR CCDS; CCDS22585.1; -. [Q8QZR3-1]
DR CCDS; CCDS52650.1; -. [Q8QZR3-2]
DR RefSeq; NP_001177259.1; NM_001190330.1. [Q8QZR3-2]
DR RefSeq; NP_598721.1; NM_133960.5. [Q8QZR3-1]
DR AlphaFoldDB; Q8QZR3; -.
DR SMR; Q8QZR3; -.
DR IntAct; Q8QZR3; 1.
DR STRING; 10090.ENSMUSP00000034346; -.
DR ESTHER; mouse-Ces2a; Carb_B_Chordata.
DR MEROPS; S09.997; -.
DR GlyGen; Q8QZR3; 2 sites.
DR iPTMnet; Q8QZR3; -.
DR PhosphoSitePlus; Q8QZR3; -.
DR jPOST; Q8QZR3; -.
DR MaxQB; Q8QZR3; -.
DR PaxDb; Q8QZR3; -.
DR PeptideAtlas; Q8QZR3; -.
DR PRIDE; Q8QZR3; -.
DR ProteomicsDB; 275480; -. [Q8QZR3-1]
DR ProteomicsDB; 275481; -. [Q8QZR3-2]
DR DNASU; 102022; -.
DR Ensembl; ENSMUST00000034346; ENSMUSP00000034346; ENSMUSG00000055730. [Q8QZR3-1]
DR Ensembl; ENSMUST00000164182; ENSMUSP00000127346; ENSMUSG00000055730. [Q8QZR3-2]
DR GeneID; 102022; -.
DR KEGG; mmu:102022; -.
DR UCSC; uc009nbc.2; mouse. [Q8QZR3-1]
DR UCSC; uc012giz.1; mouse. [Q8QZR3-2]
DR CTD; 102022; -.
DR MGI; MGI:2142491; Ces2a.
DR VEuPathDB; HostDB:ENSMUSG00000055730; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000153793; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; Q8QZR3; -.
DR OMA; LANICPQ; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q8QZR3; -.
DR TreeFam; TF315470; -.
DR BioGRID-ORCS; 102022; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q8QZR3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8QZR3; protein.
DR Bgee; ENSMUSG00000055730; Expressed in small intestine Peyer's patch and 33 other tissues.
DR ExpressionAtlas; Q8QZR3; baseline and differential.
DR Genevisible; Q8QZR3; 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 GO; GO:0006486; P:protein glycosylation; 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; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Microsome; Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..558
FT /note="Pyrethroid hydrolase Ces2a"
FT /id="PRO_0000424210"
FT ACT_SITE 227
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 344
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT ACT_SITE 456
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT MOD_RES 209
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 296
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..122
FT /evidence="ECO:0000250|UniProtKB:Q99K10"
FT DISULFID 279..290
FT /evidence="ECO:0000250|UniProtKB:Q99K10"
FT VAR_SEQ 272..304
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053352"
FT CONFLICT 200
FT /note="Q -> K (in Ref. 1; BAE38379)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="I -> V (in Ref. 1; BAE38379)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..373
FT /note="LKN -> VKD (in Ref. 1; BAE38379)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 61940 MW; 961AD6BDC892E3FD CRC64;
MPLARLPGWL CVVACGLLLL LQHVHGQDSA SPIRNTHRGQ VRGSFVHVKD TKSGVHAFLG
IPFAKPPVGL LRFAPPEDPE PWSGVRDGTS QPAMCLQPDI MNLEDAKEMN LILPPISMSE
DCLYLNIYTP THAQEGSNLP VMVWIHGGGL VVGSASMNDV SKLAATEEIV IVAIQYRLGV
LGFFSTGDQH ARGNWGYLDQ VAALRWVQKN IAYFGGNRDR VTIFGVSAGG TSVSSHILSP
MSKGLFHGAI MQSGVALLPD LISDTSEVVY KTVANLSGCE ATDSEALIHC LRAKSKQEIL
AINQVFKMIP AVVDGEFLPK HPQELLTSMD FHPVPSIIGV NTDECGWGVP MFMGLDHIIK
NITRETLPAV LKNTAARMML PPECSHLLVE EYMGDTEDPE TLQAQFREML GDFMFVIPAL
QVAHFQRSQA PVYFYEFQHL SSFIKHVRPS HVKADHGDDV AFVFGSYLWD MNLDLTEEEE
LLKRMMMKYW ANFARNGNPN SEGLPSWPVL DHDEQYLQLD TQPAVGRALK ARRLQFWTKT
LPQKIQELKG SQDKHAEL
