EST2E_RAT
ID EST2E_RAT Reviewed; 567 AA.
AC G3V7J5; O35535;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Pyrethroid hydrolase Ces2e {ECO:0000250|UniProtKB:Q8BK48};
DE EC=3.1.1.88 {ECO:0000250|UniProtKB:Q8BK48};
DE AltName: Full=Carboxylic ester hydrolase {ECO:0000255|RuleBase:RU361235};
DE EC=3.1.1.- {ECO:0000255|RuleBase:RU361235};
DE Flags: Precursor;
GN Name=Ces2e {ECO:0000312|RGD:621563};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|EMBL:BAA23607.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-567.
RC STRAIN=Wistar {ECO:0000312|EMBL:BAA23607.1};
RC TISSUE=Liver {ECO:0000312|EMBL:BAA23607.1};
RA Sone T., Sawada T., Takabatake E., Wang C., Isobe M.;
RT "Molecular cloning of a rat liver cDNA encoding a novel phenobarbital-
RT inducible carboxylesterase.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12230550; DOI=10.1046/j.1432-1033.2002.03121.x;
RA Sanghani S.P., Davis W.I., Dumaual N.G., Mahrenholz A., Bosron W.F.;
RT "Identification of microsomal rat liver carboxylesterases and their
RT activity with retinyl palmitate.";
RL Eur. J. Biochem. 269:4387-4398(2002).
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 (By
CC similarity). Hydrolyzes retinyl esters (PubMed:12230550).
CC {ECO:0000250|UniProtKB:Q8BK48, ECO:0000269|PubMed:12230550}.
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:0000269|PubMed:12230550};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000305|PubMed:12230550};
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:0000250|UniProtKB:Q8BK48};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 0.27 min(-1) with retinyl palmitate as substrate.
CC {ECO:0000269|PubMed:12230550};
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:12230550}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:12230550}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; AABR07042570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07042571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D50580; BAA23607.1; -; mRNA.
DR AlphaFoldDB; G3V7J5; -.
DR SMR; G3V7J5; -.
DR STRING; 10116.ENSRNOP00000015724; -.
DR SwissLipids; SLP:000001985; -.
DR ESTHER; ratno-phebest; Carb_B_Chordata.
DR MEROPS; S09.970; -.
DR iPTMnet; O35535; -.
DR PaxDb; G3V7J5; -.
DR PRIDE; G3V7J5; -.
DR Ensembl; ENSRNOT00000015724; ENSRNOP00000015724; ENSRNOG00000011635.
DR RGD; 621563; Ces2e.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000153793; -.
DR HOGENOM; CLU_006586_13_2_1; -.
DR InParanoid; G3V7J5; -.
DR OMA; NKVPIMT; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.1; 5301.
DR PRO; PR:G3V7J5; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000011635; Expressed in liver and 3 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; 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:0102209; F:trans-permethrin hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0001523; P:retinoid metabolic process; TAS:UniProtKB.
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 Disulfide bond; Endoplasmic reticulum; Hydrolase; Microsome;
KW Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255|RuleBase:RU361235"
FT CHAIN 37..567
FT /note="Pyrethroid hydrolase Ces2e"
FT /evidence="ECO:0000255|RuleBase:RU361235"
FT /id="PRO_5005132000"
FT ACT_SITE 237
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 465
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT MOD_RES 37
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P14943"
FT DISULFID 105..132
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT DISULFID 289..300
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT CONFLICT 398
FT /note="M -> T (in Ref. 2; BAA23607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 63583 MW; F6C77AD97FA55C6E CRC64;
MAQTRAWKSI MPLESLPGWL NAVVWGLLLL FCQVQGQDSA SPIRNTHTGQ VRGSFVHVKD
TKSGVHTFLG IPFAKPPIGP LRFAPPEPPE PWSGVRDGTS HPAMCLQNID GLNLENLKIK
MSRSPVSMSE DCLYLSIYTP AHTHKDSNLP VMVWIHGGGL CWGMASTYDG SMLAAIEDVV
VVTIQYRLGI LGFFSTGDEH ARGNWGYLDQ VAALRWVQQN IVHFGGNPDR VTIFGESAGG
ISVSSHVVSP MSQGLFHGAI MESGVALLPN LISNTSEVIY TMVANLSGCE PVDSEALMSC
LREKSEEEML AINNIVRTIS GVVDGKFLPR HPLELLASVD FHPVPSIIGI NSDEYGWIIP
MLHPDSTMKE INRETMRAVL KNTAVQMMLP PECSDLLMEE YMGDTEDSKT LQIQFNEMMG
DFIFVIPALQ VAHFQRSHAP VYFYEFQHQS NFLKDIRPPH VKADHGDELP YVIGYLFWDM
KFVFTEEEKL LSRKMIKYWA NFARHGNPNS EGLPYWPALD HDEQYLQLDI QPVVGRALKA
RRLKFWTKTL PQKIQELKGS QDNHTEL
