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Cocaine esterase (EC 3.1.1.84) (Carboxylesterase 2) (CE-2) (hCE-2) (EC 3.1.1.1) (Methylumbelliferyl-acetate deacetylase 2) (EC 3.1.1.56)

 EST2_HUMAN              Reviewed;         559 AA.
O00748; A8K367; Q16859; Q5MAB8; Q7Z366; Q8IUP4; Q8TCP8;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
27-SEP-2017, entry version 147.
RecName: Full=Cocaine esterase;
EC=3.1.1.84;
AltName: Full=Carboxylesterase 2;
Short=CE-2;
Short=hCE-2;
EC=3.1.1.1;
AltName: Full=Methylumbelliferyl-acetate deacetylase 2;
EC=3.1.1.56;
Flags: Precursor;
Name=CES2; Synonyms=ICE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Small intestine;
PubMed=9144407; DOI=10.1006/bbrc.1997.6413;
Schwer H., Langmann T., Daig R., Becker A., Aslanidis C., Schmitz G.;
"Molecular cloning and characterization of a novel putative
carboxylesterase, present in human intestine and liver.";
Biochem. Biophys. Res. Commun. 233:117-120(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 27-34;
57-70; 227-235; 300-305; 346-351; 447-454; 458-466; 535-540 AND
546-551, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, GLYCOSYLATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Liver;
PubMed=9169443; DOI=10.1074/jbc.272.23.14769;
Pindel E.V., Kedishvili N.Y., Abraham T.L., Brzezinski M.R., Zhang J.,
Dean R.A., Bosron W.F.;
"Purification and cloning of a broad substrate specificity human liver
carboxylesterase that catalyzes the hydrolysis of cocaine and
heroin.";
J. Biol. Chem. 272:14769-14775(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Sone T., Ishida Y., Takabatake E., Wang C., Pohl L., Isobe M.;
"Molecular cloning and expression of a human liver cDNA encoding a
novel carboxylesterase.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Endometrial adenocarcinoma, and Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
VARIANT HIS-206.
PubMed=12721789; DOI=10.1007/s10038-003-0021-7;
Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C.,
Nakamura Y.;
"Catalog of 680 variations among eight cytochrome p450 (CYP) genes,
nine esterase genes, and two other genes in the Japanese population.";
J. Hum. Genet. 48:249-270(2003).
[13]
VARIANT TRP-34.
PubMed=15618752; DOI=10.2133/dmpk.18.327;
Kim S.-R., Nakamura T., Saito Y., Sai K., Nakajima T., Saito H.,
Shirao K., Minami H., Ohtsu A., Yoshida T., Saijo N., Ozawa S.,
Sawada J.;
"Twelve novel single nucleotide polymorphisms in the CES2 gene
encoding human carboxylesterase 2 (hCE-2).";
Drug Metab. Pharmacokinet. 18:327-332(2003).
-!- FUNCTION: Involved in the detoxification of xenobiotics and in the
activation of ester and amide prodrugs. Shows high catalytic
efficiency for hydrolysis of cocaine, 4-methylumbelliferyl
acetate, heroin and 6-monoacetylmorphine.
{ECO:0000269|PubMed:9169443}.
-!- CATALYTIC ACTIVITY: Cocaine + H(2)O = ecgonine methyl ester +
benzoate. {ECO:0000269|PubMed:9169443}.
-!- CATALYTIC ACTIVITY: A carboxylic ester + H(2)O = an alcohol + a
carboxylate. {ECO:0000255|PROSITE-ProRule:PRU10039,
ECO:0000269|PubMed:9169443}.
-!- CATALYTIC ACTIVITY: 4-methylumbelliferyl acetate + H(2)O = 4-
methylumbelliferone + acetate. {ECO:0000269|PubMed:9169443}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.39 mM for cocaine {ECO:0000269|PubMed:9169443};
KM=0.15 mM for 4-methylumbelliferyl acetate
{ECO:0000269|PubMed:9169443};
KM=6.8 mM for heroin {ECO:0000269|PubMed:9169443};
KM=0.13 mM for 6-monoacetylmorphine
{ECO:0000269|PubMed:9169443};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9169443}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O00748-1; Sequence=Displayed;
Name=2;
IsoId=O00748-2; Sequence=VSP_010161;
-!- TISSUE SPECIFICITY: Preferentially expressed in intestine with
moderate expression in liver. Within the intestine, highest
expression is found in small intestine with lower expression in
colon and rectum. {ECO:0000269|PubMed:9144407}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9169443}.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH32095.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAW29943.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAD28531.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAD98009.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ces2/";
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EMBL; Y09616; CAA70831.1; -; mRNA.
EMBL; D50579; BAA23606.1; -; mRNA.
EMBL; U60553; AAB03611.1; -; mRNA.
EMBL; AL713761; CAD28531.1; ALT_INIT; mRNA.
EMBL; AK290482; BAF83171.1; -; mRNA.
EMBL; BX538086; CAD98009.1; ALT_INIT; mRNA.
EMBL; AY851164; AAW29943.1; ALT_INIT; Genomic_DNA.
EMBL; AC009084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032095; AAH32095.1; ALT_INIT; mRNA.
PIR; JC5408; JC5408.
RefSeq; NP_003860.2; NM_003869.5.
RefSeq; NP_932327.1; NM_198061.2.
UniGene; Hs.282975; -.
ProteinModelPortal; O00748; -.
SMR; O00748; -.
BioGrid; 114351; 1.
IntAct; O00748; 1.
STRING; 9606.ENSP00000317842; -.
BindingDB; O00748; -.
ChEMBL; CHEMBL3180; -.
DrugBank; DB06695; Dabigatran etexilate.
DrugBank; DB00762; Irinotecan.
DrugBank; DB00688; Mycophenolate mofetil.
DrugBank; DB06209; Prasugrel.
SwissLipids; SLP:000001424; -.
ESTHER; human-CES2; Carb_B_Chordata.
MEROPS; S09.984; -.
iPTMnet; O00748; -.
PhosphoSitePlus; O00748; -.
BioMuta; CES2; -.
EPD; O00748; -.
MaxQB; O00748; -.
PaxDb; O00748; -.
PeptideAtlas; O00748; -.
PRIDE; O00748; -.
DNASU; 8824; -.
Ensembl; ENST00000417689; ENSP00000394452; ENSG00000172831.
GeneID; 8824; -.
KEGG; hsa:8824; -.
UCSC; uc002eqq.4; human. [O00748-1]
CTD; 8824; -.
DisGeNET; 8824; -.
EuPathDB; HostDB:ENSG00000172831.11; -.
GeneCards; CES2; -.
HGNC; HGNC:1864; CES2.
HPA; HPA018897; -.
MIM; 605278; gene.
neXtProt; NX_O00748; -.
PharmGKB; PA377; -.
eggNOG; KOG1516; Eukaryota.
eggNOG; COG2272; LUCA.
HOGENOM; HOG000091866; -.
HOVERGEN; HBG008839; -.
InParanoid; O00748; -.
KO; K03927; -.
PhylomeDB; O00748; -.
TreeFam; TF315470; -.
BRENDA; 3.1.1.1; 2681.
BRENDA; 3.1.1.84; 2681.
Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
SABIO-RK; O00748; -.
ChiTaRS; CES2; human.
GeneWiki; Carboxylesterase_2; -.
GenomeRNAi; 8824; -.
PRO; PR:O00748; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000172831; -.
CleanEx; HS_CES2; -.
ExpressionAtlas; O00748; baseline and differential.
Genevisible; O00748; HS.
GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:BHF-UCL.
GO; GO:0047374; F:methylumbelliferyl-acetate deacetylase activity; IEA:UniProtKB-EC.
GO; GO:0009056; P:catabolic process; TAS:ProtInc.
GO; GO:0006693; P:prostaglandin metabolic process; IDA:BHF-UCL.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002018; CarbesteraseB.
InterPro; IPR019826; Carboxylesterase_B_AS.
InterPro; IPR019819; Carboxylesterase_B_CS.
Pfam; PF00135; COesterase; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
Polymorphism; Pyrrolidone carboxylic acid; Reference proteome;
Serine esterase; Signal.
SIGNAL 1 26 {ECO:0000269|PubMed:9169443}.
CHAIN 27 559 Cocaine esterase.
/FTId=PRO_0000008572.
MOTIF 556 559 Prevents secretion from ER.
{ECO:0000255}.
ACT_SITE 228 228 Acyl-ester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10039}.
ACT_SITE 345 345 Charge relay system. {ECO:0000250}.
ACT_SITE 457 457 Charge relay system. {ECO:0000250}.
MOD_RES 27 27 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P14943}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 95 123 {ECO:0000250}.
DISULFID 280 291 {ECO:0000250}.
VAR_SEQ 458 474 GDELPFVFRSFFGGNYI -> V (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_010161.
VARIANT 34 34 R -> W. {ECO:0000269|PubMed:15618752}.
/FTId=VAR_018396.
VARIANT 206 206 R -> H. {ECO:0000269|PubMed:12721789}.
/FTId=VAR_018397.
CONFLICT 2 10 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 180 180 G -> S (in Ref. 4; BAF83171).
{ECO:0000305}.
CONFLICT 239 239 V -> M (in Ref. 4; BAF83171).
{ECO:0000305}.
CONFLICT 385 385 F -> S (in Ref. 5; CAD98009).
{ECO:0000305}.
CONFLICT 519 519 Q -> R (in Ref. 5; CAD98009).
{ECO:0000305}.
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


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