CHLE_MOUSE
ID CHLE_MOUSE Reviewed; 603 AA.
AC Q03311; Q543J3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cholinesterase;
DE EC=3.1.1.8;
DE AltName: Full=Acylcholine acylhydrolase;
DE AltName: Full=Butyrylcholine esterase;
DE AltName: Full=Choline esterase II;
DE AltName: Full=Pseudocholinesterase;
DE Flags: Precursor;
GN Name=Bche;
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 [MRNA].
RX PubMed=2400605; DOI=10.1016/0896-6273(90)90168-f;
RA Rachinsky T.L., Camp S., Li Y., Ekstroem T.J., Newton M., Taylor P.;
RT "Molecular cloning of mouse acetylcholinesterase: tissue distribution of
RT alternatively spliced mRNA species.";
RL Neuron 5:317-327(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 97-237.
RC TISSUE=Liver;
RX PubMed=2016308; DOI=10.1016/s0021-9258(20)89597-0;
RA Arpagaus M., Chatonnet A., Masson P., Newton M., Vaughan T.A.,
RA Bartels C.F., Nogueira C.P., la Du B.N., Lockridge O.;
RT "Use of the polymerase chain reaction for homology probing of
RT butyrylcholinesterase from several vertebrates.";
RL J. Biol. Chem. 266:6966-6974(1991).
RN [5]
RP FUNCTION.
RX PubMed=17212694; DOI=10.1111/j.1471-4159.2006.04347.x;
RA Hartmann J., Kiewert C., Duysen E.G., Lockridge O., Greig N.H., Klein J.;
RT "Excessive hippocampal acetylcholine levels in acetylcholinesterase-
RT deficient mice are moderated by butyrylcholinesterase activity.";
RL J. Neurochem. 100:1421-1429(2007).
RN [6]
RP FUNCTION.
RX PubMed=17467011; DOI=10.1016/j.lfs.2007.03.011;
RA Girard E., Bernard V., Minic J., Chatonnet A., Krejci E., Molgo J.;
RT "Butyrylcholinesterase and the control of synaptic responses in
RT acetylcholinesterase knockout mice.";
RL Life Sci. 80:2380-2385(2007).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=17194517; DOI=10.1016/j.tox.2006.11.069;
RA Duysen E.G., Li B., Darvesh S., Lockridge O.;
RT "Sensitivity of butyrylcholinesterase knockout mice to (--)-huperzine A and
RT donepezil suggests humans with butyrylcholinesterase deficiency may not
RT tolerate these Alzheimer's disease drugs and indicates
RT butyrylcholinesterase function in neurotransmission.";
RL Toxicology 233:60-69(2007).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=18056867; DOI=10.1124/jpet.107.133330;
RA Li B., Duysen E.G., Carlson M., Lockridge O.;
RT "The butyrylcholinesterase knockout mouse as a model for human
RT butyrylcholinesterase deficiency.";
RL J. Pharmacol. Exp. Ther. 324:1146-1154(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, and Lung;
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: Esterase with broad substrate specificity. Contributes to the
CC inactivation of the neurotransmitter acetylcholine. Can degrade
CC neurotoxic organophosphate esters. {ECO:0000269|PubMed:17212694,
CC ECO:0000269|PubMed:17467011}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acylcholine + H2O = a carboxylate + choline + H(+);
CC Xref=Rhea:RHEA:21964, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:35287; EC=3.1.1.8;
CC -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Present in most cells except erythrocytes.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the presence of
CC other cholinesterases. Hypersensitive to acetylcholinesterase
CC inhibitors, such as huperzine and donepezil. Treatment with the
CC acetylcholinesterase inhibitor donepezil causes convulsions and death
CC within 3 hours of dosing. {ECO:0000269|PubMed:17194517,
CC ECO:0000269|PubMed:18056867}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; M99492; AAA37328.1; -; mRNA.
DR EMBL; AK050337; BAC34196.1; -; mRNA.
DR EMBL; CH466547; EDL15482.1; -; Genomic_DNA.
DR CCDS; CCDS17411.1; -.
DR PIR; S70849; S70849.
DR RefSeq; NP_033868.3; NM_009738.3.
DR AlphaFoldDB; Q03311; -.
DR SMR; Q03311; -.
DR BioGRID; 198313; 1.
DR STRING; 10090.ENSMUSP00000029367; -.
DR BindingDB; Q03311; -.
DR ChEMBL; CHEMBL2528; -.
DR DrugCentral; Q03311; -.
DR ESTHER; mouse-BCHE; BCHE.
DR MEROPS; S09.980; -.
DR GlyGen; Q03311; 7 sites.
DR iPTMnet; Q03311; -.
DR PhosphoSitePlus; Q03311; -.
DR CPTAC; non-CPTAC-3902; -.
DR jPOST; Q03311; -.
DR MaxQB; Q03311; -.
DR PaxDb; Q03311; -.
DR PeptideAtlas; Q03311; -.
DR PRIDE; Q03311; -.
DR ProteomicsDB; 283908; -.
DR Antibodypedia; 879; 445 antibodies from 40 providers.
DR DNASU; 12038; -.
DR Ensembl; ENSMUST00000029367; ENSMUSP00000029367; ENSMUSG00000027792.
DR GeneID; 12038; -.
DR KEGG; mmu:12038; -.
DR UCSC; uc008pmv.1; mouse.
DR CTD; 590; -.
DR MGI; MGI:894278; Bche.
DR VEuPathDB; HostDB:ENSMUSG00000027792; -.
DR eggNOG; KOG4389; Eukaryota.
DR GeneTree; ENSGT00940000157023; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; Q03311; -.
DR OMA; EMRYICP; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q03311; -.
DR TreeFam; TF315470; -.
DR Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR SABIO-RK; Q03311; -.
DR BioGRID-ORCS; 12038; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q03311; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q03311; protein.
DR Bgee; ENSMUSG00000027792; Expressed in duodenum and 162 other tissues.
DR ExpressionAtlas; Q03311; baseline and differential.
DR Genevisible; Q03311; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005641; C:nuclear envelope lumen; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003990; F:acetylcholinesterase activity; IDA:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0033265; F:choline binding; ISO:MGI.
DR GO; GO:0004104; F:cholinesterase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006581; P:acetylcholine catabolic process; IBA:GO_Central.
DR GO; GO:0019695; P:choline metabolic process; ISO:MGI.
DR GO; GO:0007612; P:learning; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:MGI.
DR GO; GO:0014016; P:neuroblast differentiation; ISO:MGI.
DR GO; GO:0043279; P:response to alkaloid; ISO:MGI.
DR GO; GO:0051593; P:response to folic acid; ISO:MGI.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
DR GO; GO:0007584; P:response to nutrient; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR014788; AChE_tetra.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000997; Cholinesterase.
DR Pfam; PF08674; AChE_tetra; 1.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR00878; CHOLNESTRASE.
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; Glycoprotein; Hydrolase; Phosphoprotein;
KW Reference proteome; Secreted; Serine esterase; Signal.
FT SIGNAL 1..29
FT CHAIN 30..603
FT /note="Cholinesterase"
FT /id="PRO_0000008614"
FT ACT_SITE 227
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"
FT ACT_SITE 467
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 145..146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06276"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..121
FT /evidence="ECO:0000250"
FT DISULFID 281..292
FT /evidence="ECO:0000250"
FT DISULFID 429..548
FT /evidence="ECO:0000250"
FT DISULFID 600
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 129
FT /note="P -> R (in Ref. 1; AAA37328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 68462 MW; 2CB79C46797B3713 CRC64;
MQTQHTKVTQ THFLLWILLL CMPFGKSHTE EDFIITTKTG RVRGLSMPVL GGTVTAFLGI
PYAQPPLGSL RFKKPQPLNK WPDIHNATQY ANSCYQNIDQ AFPGFQGSEM WNPNTNLSED
CLYLNVWIPV PKPKNATVMV WIYGGGFQTG TSSLPVYDGK FLARVERVIV VSMNYRVGAL
GFLAFPGNPD APGNMGLFDQ QLALQWVQRN IAAFGGNPKS ITIFGESAGA ASVSLHLLCP
QSYPLFTRAI LESGSSNAPW AVKHPEEARN RTLTLAKFTG CSKENEMEMI KCLRSKDPQE
ILRNERFVLP SDSILSINFG PTVDGDFLTD MPHTLLQLGK VKKAQILVGV NKDEGTAFLV
YGAPGFSKDN DSLITRKEFQ EGLNMYFPGV SRLGKEAVLF YYVDWLGEQS PEVYRDALDD
VIGDYNIICP ALEFTKKFAE LENNAFFYFF EHRSSKLPWP EWMGVMHGYE IEFVFGLPLG
RRVNYTRAEE IFSRSIMKTW ANFAKYGHPN GTQGNSTMWP VFTSTEQKYL TLNTEKSKIY
SKLRAPQCQF WRLFFPKVLE MTGDIDETEQ EWKAGFHRWS NYMMDWQNQF NDYTSKKESC
TAL
