EST2_HUMAN
ID EST2_HUMAN Reviewed; 559 AA.
AC O00748; A0A024R6X1; A8K367; Q16859; Q5MAB8; Q7Z366; Q8IUP4; Q8TCP8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cocaine esterase {ECO:0000305};
DE EC=3.1.1.84 {ECO:0000269|PubMed:9169443};
DE AltName: Full=Carboxylesterase 2;
DE Short=CE-2;
DE Short=hCE-2;
DE EC=3.1.1.1 {ECO:0000269|PubMed:9169443};
DE AltName: Full=Methylumbelliferyl-acetate deacetylase 2;
DE EC=3.1.1.56;
DE Flags: Precursor;
GN Name=CES2 {ECO:0000312|HGNC:HGNC:1864}; Synonyms=ICE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Small intestine;
RX PubMed=9144407; DOI=10.1006/bbrc.1997.6413;
RA Schwer H., Langmann T., Daig R., Becker A., Aslanidis C., Schmitz G.;
RT "Molecular cloning and characterization of a novel putative
RT carboxylesterase, present in human intestine and liver.";
RL Biochem. Biophys. Res. Commun. 233:117-120(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 27-34; 57-70;
RP 227-235; 300-305; 346-351; 447-454; 458-466; 535-540 AND 546-551, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, GLYCOSYLATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC TISSUE=Liver;
RX PubMed=9169443; DOI=10.1074/jbc.272.23.14769;
RA Pindel E.V., Kedishvili N.Y., Abraham T.L., Brzezinski M.R., Zhang J.,
RA Dean R.A., Bosron W.F.;
RT "Purification and cloning of a broad substrate specificity human liver
RT carboxylesterase that catalyzes the hydrolysis of cocaine and heroin.";
RL J. Biol. Chem. 272:14769-14775(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Sone T., Ishida Y., Takabatake E., Wang C., Pohl L., Isobe M.;
RT "Molecular cloning and expression of a human liver cDNA encoding a novel
RT carboxylesterase.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Endometrial adenocarcinoma, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RC TISSUE=Macrophage;
RX PubMed=21049984; DOI=10.1021/tx1002194;
RA Xie S., Borazjani A., Hatfield M.J., Edwards C.C., Potter P.M., Ross M.K.;
RT "Inactivation of lipid glyceryl ester metabolism in human THP1
RT monocytes/macrophages by activated organophosphorus insecticides: role of
RT carboxylesterases 1 and 2.";
RL Chem. Res. Toxicol. 23:1890-1904(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=22446793; DOI=10.1007/s00253-012-3994-3;
RA Lamego J., Cunha B., Peixoto C., Sousa M.F., Alves P.M., Simplicio A.L.,
RA Coroadinha A.S.;
RT "Carboxylesterase 2 production and characterization in human cells: new
RT insights into enzyme oligomerization and activity.";
RL Appl. Microbiol. Biotechnol. 97:1161-1173(2013).
RN [13]
RP REVIEW, AND ALTERNATIVE INITIATION (ISOFORMS 3 AND 4).
RX PubMed=28677105; DOI=10.1007/s13238-017-0437-z;
RA Lian J., Nelson R., Lehner R.;
RT "Carboxylesterases in lipid metabolism: from mouse to human.";
RL Protein Cell 9:178-195(2018).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP VARIANT HIS-206.
RX PubMed=12721789; DOI=10.1007/s10038-003-0021-7;
RA Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C.,
RA Nakamura Y.;
RT "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine
RT esterase genes, and two other genes in the Japanese population.";
RL J. Hum. Genet. 48:249-270(2003).
RN [17]
RP VARIANT TRP-34.
RX PubMed=15618752; DOI=10.2133/dmpk.18.327;
RA Kim S.-R., Nakamura T., Saito Y., Sai K., Nakajima T., Saito H., Shirao K.,
RA Minami H., Ohtsu A., Yoshida T., Saijo N., Ozawa S., Sawada J.;
RT "Twelve novel single nucleotide polymorphisms in the CES2 gene encoding
RT human carboxylesterase 2 (hCE-2).";
RL Drug Metab. Pharmacokinet. 18:327-332(2003).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC activation of ester and amide prodrugs (PubMed:9169443). Shows high
CC catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl
CC acetate, heroin and 6-monoacetylmorphine (PubMed:9169443). Hydrolyzes
CC aspirin, substrates with large alcohol group and small acyl group and
CC endogenous lipids such as triacylglycerol (PubMed:28677105). Converts
CC monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-
CC arachidonoylglycerol and prostaglandins (PubMed:21049984).
CC {ECO:0000269|PubMed:21049984, ECO:0000269|PubMed:9169443,
CC ECO:0000303|PubMed:28677105}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cocaine + H2O = benzoate + ecgonine methyl ester + H(+);
CC Xref=Rhea:RHEA:27506, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:59908, ChEBI:CHEBI:60056; EC=3.1.1.84;
CC Evidence={ECO:0000269|PubMed:9169443};
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:9169443};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone +
CC acetate + H(+); Xref=Rhea:RHEA:12208, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17224, ChEBI:CHEBI:17763,
CC ChEBI:CHEBI:30089; EC=3.1.1.56;
CC Evidence={ECO:0000269|PubMed:9169443};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000269|PubMed:21049984};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC Evidence={ECO:0000305|PubMed:21049984};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin E2 1-glyceryl ester = glycerol + H(+) +
CC prostaglandin E2; Xref=Rhea:RHEA:48296, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:90230,
CC ChEBI:CHEBI:606564; Evidence={ECO:0000269|PubMed:21049984};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48297;
CC Evidence={ECO:0000305|PubMed:21049984};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin F2alpha 1-glyceryl ester = glycerol + H(+)
CC + prostaglandin F2alpha; Xref=Rhea:RHEA:48300, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:90233; Evidence={ECO:0000269|PubMed:21049984};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48301;
CC Evidence={ECO:0000305|PubMed:21049984};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.39 mM for cocaine {ECO:0000269|PubMed:9169443};
CC KM=0.15 mM for 4-methylumbelliferyl acetate
CC {ECO:0000269|PubMed:9169443};
CC KM=6.8 mM for heroin {ECO:0000269|PubMed:9169443};
CC KM=46 uM for 2-arachidonoylglycerol {ECO:0000269|PubMed:21049984};
CC KM=750 uM for prostaglandin E2 1-glyceryl ester
CC {ECO:0000269|PubMed:21049984};
CC KM=35 uM for prostaglandin F2alpha 1-glyceryl ester
CC {ECO:0000269|PubMed:21049984};
CC KM=0.13 mM for 6-monoacetylmorphine {ECO:0000269|PubMed:9169443};
CC Note=kcat is 43 min(-1), 49 min(-1), 150 min(-1) with 2-
CC arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and
CC prostaglandin E2 1-glyceryl ester as substrates, respectively.
CC {ECO:0000269|PubMed:21049984};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9169443}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:22446793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1;
CC IsoId=O00748-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00748-2; Sequence=VSP_010161;
CC Name=3;
CC IsoId=O00748-4; Sequence=VSP_059804;
CC Name=4;
CC IsoId=O00748-5; Sequence=VSP_059804, VSP_010161;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in intestine with moderate
CC expression in liver. Within the intestine, highest expression is found
CC in small intestine with lower expression in colon and rectum.
CC {ECO:0000269|PubMed:9144407}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:9169443}.
CC -!- MISCELLANEOUS: [Isoform 3]: Probably produced by alternative initiation
CC of isoform 1. Does not contain a signal peptide. The biological
CC function of the extra amino acids in the N-terminus remains to be
CC determined. {ECO:0000303|PubMed:28677105}.
CC -!- MISCELLANEOUS: [Isoform 4]: Probably produced by alternative initiation
CC of isoform 2. Does not contain a signal peptide. The biological
CC function of the extra amino acids in the N-terminus remains to be
CC determined. {ECO:0000303|PubMed:28677105}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ces2/";
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DR EMBL; Y09616; CAA70831.1; -; mRNA.
DR EMBL; D50579; BAA23606.1; -; mRNA.
DR EMBL; U60553; AAB03611.1; -; mRNA.
DR EMBL; AL713761; CAD28531.1; -; mRNA.
DR EMBL; AK290482; BAF83171.1; -; mRNA.
DR EMBL; BX538086; CAD98009.1; -; mRNA.
DR EMBL; AY851164; AAW29943.1; -; Genomic_DNA.
DR EMBL; AC009084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW83058.1; -; Genomic_DNA.
DR EMBL; CH471092; EAW83059.1; -; Genomic_DNA.
DR EMBL; BC032095; AAH32095.1; -; mRNA.
DR CCDS; CCDS10825.1; -. [O00748-1]
DR CCDS; CCDS45507.1; -. [O00748-2]
DR PIR; JC5408; JC5408.
DR RefSeq; NP_003860.2; NM_003869.5. [O00748-1]
DR RefSeq; NP_932327.1; NM_198061.2. [O00748-2]
DR AlphaFoldDB; O00748; -.
DR SMR; O00748; -.
DR BioGRID; 114351; 35.
DR IntAct; O00748; 3.
DR STRING; 9606.ENSP00000317842; -.
DR BindingDB; O00748; -.
DR ChEMBL; CHEMBL3180; -.
DR DrugBank; DB06695; Dabigatran etexilate.
DR DrugBank; DB14845; Filgotinib.
DR DrugBank; DB00762; Irinotecan.
DR DrugBank; DB06209; Prasugrel.
DR DrugBank; DB16349; Vicagrel.
DR DrugCentral; O00748; -.
DR SwissLipids; SLP:000001424; -.
DR ESTHER; human-CES2; Carb_B_Chordata.
DR MEROPS; S09.984; -.
DR GlyGen; O00748; 2 sites.
DR iPTMnet; O00748; -.
DR PhosphoSitePlus; O00748; -.
DR BioMuta; CES2; -.
DR EPD; O00748; -.
DR jPOST; O00748; -.
DR MassIVE; O00748; -.
DR MaxQB; O00748; -.
DR PaxDb; O00748; -.
DR PeptideAtlas; O00748; -.
DR PRIDE; O00748; -.
DR ProteomicsDB; 48014; -. [O00748-1]
DR ProteomicsDB; 48015; -. [O00748-2]
DR Antibodypedia; 15599; 370 antibodies from 34 providers.
DR DNASU; 8824; -.
DR Ensembl; ENST00000317091.10; ENSP00000317842.5; ENSG00000172831.14. [O00748-1]
DR Ensembl; ENST00000417689.6; ENSP00000394452.2; ENSG00000172831.14. [O00748-2]
DR GeneID; 8824; -.
DR KEGG; hsa:8824; -.
DR MANE-Select; ENST00000317091.10; ENSP00000317842.5; NM_001365405.1; NP_001352334.1.
DR UCSC; uc002eqq.4; human. [O00748-1]
DR UCSC; uc002eqr.4; human.
DR CTD; 8824; -.
DR DisGeNET; 8824; -.
DR GeneCards; CES2; -.
DR HGNC; HGNC:1864; CES2.
DR HPA; ENSG00000172831; Tissue enhanced (intestine, liver).
DR MIM; 605278; gene.
DR neXtProt; NX_O00748; -.
DR OpenTargets; ENSG00000172831; -.
DR PharmGKB; PA377; -.
DR VEuPathDB; HostDB:ENSG00000172831; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000153793; -.
DR HOGENOM; CLU_006586_13_2_1; -.
DR InParanoid; O00748; -.
DR OMA; NIANTVC; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; O00748; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.1; 2681.
DR BRENDA; 3.1.1.84; 2681.
DR PathwayCommons; O00748; -.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SABIO-RK; O00748; -.
DR SignaLink; O00748; -.
DR BioGRID-ORCS; 8824; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; CES2; human.
DR GeneWiki; Carboxylesterase_2; -.
DR GenomeRNAi; 8824; -.
DR Pharos; O00748; Tchem.
DR PRO; PR:O00748; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O00748; protein.
DR Bgee; ENSG00000172831; Expressed in jejunal mucosa and 203 other tissues.
DR ExpressionAtlas; O00748; baseline and differential.
DR Genevisible; O00748; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:BHF-UCL.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0047374; F:methylumbelliferyl-acetate deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009056; P:catabolic process; TAS:ProtInc.
DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:BHF-UCL.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
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 initiation; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Lipid metabolism; Pyrrolidone carboxylic acid; Reference proteome;
KW Serine esterase; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:9169443"
FT CHAIN 27..559
FT /note="Cocaine esterase"
FT /id="PRO_0000008572"
FT MOTIF 556..559
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
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 CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
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 VAR_SEQ 1
FT /note="M -> MTAQSRSPTTPTFPGPSQRTPLTPCPVQTPRLGKALIHCWTDPGQPL
FT GEQQRVRRQRTETSEPTM (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:28677105"
FT /id="VSP_059804"
FT VAR_SEQ 458..474
FT /note="GDELPFVFRSFFGGNYI -> V (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_010161"
FT VARIANT 34
FT /note="R -> W (in dbSNP:rs72547531)"
FT /evidence="ECO:0000269|PubMed:15618752"
FT /id="VAR_018396"
FT VARIANT 206
FT /note="R -> H (in dbSNP:rs8192924)"
FT /evidence="ECO:0000269|PubMed:12721789"
FT /id="VAR_018397"
FT CONFLICT 2..10
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="G -> S (in Ref. 4; BAF83171)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="V -> M (in Ref. 4; BAF83171)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="F -> S (in Ref. 5; CAD98009)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="Q -> R (in Ref. 5; CAD98009)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 61807 MW; E2EBCABA2995339A CRC64;
MRLHRLRARL SAVACGLLLL LVRGQGQDSA SPIRTTHTGQ VLGSLVHVKG ANAGVQTFLG
IPFAKPPLGP LRFAPPEPPE SWSGVRDGTT HPAMCLQDLT AVESEFLSQF NMTFPSDSMS
EDCLYLSIYT PAHSHEGSNL PVMVWIHGGA LVFGMASLYD GSMLAALENV VVVIIQYRLG
VLGFFSTGDK HATGNWGYLD QVAALRWVQQ NIAHFGGNPD RVTIFGESAG GTSVSSLVVS
PISQGLFHGA IMESGVALLP GLIASSADVI STVVANLSAC DQVDSEALVG CLRGKSKEEI
LAINKPFKMI PGVVDGVFLP RHPQELLASA DFQPVPSIVG VNNNEFGWLI PKVMRIYDTQ
KEMDREASQA ALQKMLTLLM LPPTFGDLLR EEYIGDNGDP QTLQAQFQEM MADSMFVIPA
LQVAHFQCSR APVYFYEFQH QPSWLKNIRP PHMKADHGDE LPFVFRSFFG GNYIKFTEEE
EQLSRKMMKY WANFARNGNP NGEGLPHWPL FDQEEQYLQL NLQPAVGRAL KAHRLQFWKK
ALPQKIQELE EPEERHTEL
