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Protein

Cholinesterase

Gene

Bche

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.2 Publications

Catalytic activityi

An acylcholine + H2O = choline + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei227 – 2271Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei354 – 3541Charge relay systemBy similarity
Active sitei467 – 4671Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

ReactomeiREACT_330516. Synthesis, secretion, and deacylation of Ghrelin.
SABIO-RKQ03311.

Protein family/group databases

MEROPSiS09.980.

Names & Taxonomyi

Protein namesi
Recommended name:
Cholinesterase (EC:3.1.1.8)
Alternative name(s):
Acylcholine acylhydrolase
Butyrylcholine esterase
Choline esterase II
Pseudocholinesterase
Gene namesi
Name:Bche
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:894278. Bche.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: MGI
  • endoplasmic reticulum Source: MGI
  • endoplasmic reticulum lumen Source: Ensembl
  • extracellular space Source: GO_Central
  • membrane Source: Ensembl
  • nuclear envelope lumen Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

No visible phenotype; due to the presence of other cholinesterases. Hypersensitive to acetylcholinesterase inhibitors, such as huperzine and donepezil. Treatment with the acetylcholinesterase inhibitor donepezil causes convulsions and death within 3 hours of dosing.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Add
BLAST
Chaini30 – 603574CholinesterasePRO_0000008614Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi94 ↔ 121By similarity
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
Modified residuei227 – 2271PhosphoserineBy similarity
Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi281 ↔ 292By similarity
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi429 ↔ 548By similarity
Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi600 – 600InterchainBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ03311.
PaxDbiQ03311.
PRIDEiQ03311.

PTM databases

PhosphoSiteiQ03311.

Expressioni

Tissue specificityi

Present in most cells except erythrocytes.

Gene expression databases

BgeeiQ03311.
CleanExiMM_BCHE.
GenevestigatoriQ03311.

Interactioni

Subunit structurei

Homotetramer; disulfide-linked. Dimer of dimers (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029367.

Structurei

3D structure databases

ProteinModelPortaliQ03311.
SMRiQ03311. Positions 34-558, 565-593.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni145 – 1462Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ03311.
KOiK01050.
OMAiYIFGEPL.
OrthoDBiEOG789C9R.
TreeFamiTF315470.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
ProDomiPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03311-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTQHTKVTQ THFLLWILLL CMPFGKSHTE EDFIITTKTG RVRGLSMPVL
60 70 80 90 100
GGTVTAFLGI PYAQPPLGSL RFKKPQPLNK WPDIHNATQY ANSCYQNIDQ
110 120 130 140 150
AFPGFQGSEM WNPNTNLSED CLYLNVWIPV PKPKNATVMV WIYGGGFQTG
160 170 180 190 200
TSSLPVYDGK FLARVERVIV VSMNYRVGAL GFLAFPGNPD APGNMGLFDQ
210 220 230 240 250
QLALQWVQRN IAAFGGNPKS ITIFGESAGA ASVSLHLLCP QSYPLFTRAI
260 270 280 290 300
LESGSSNAPW AVKHPEEARN RTLTLAKFTG CSKENEMEMI KCLRSKDPQE
310 320 330 340 350
ILRNERFVLP SDSILSINFG PTVDGDFLTD MPHTLLQLGK VKKAQILVGV
360 370 380 390 400
NKDEGTAFLV YGAPGFSKDN DSLITRKEFQ EGLNMYFPGV SRLGKEAVLF
410 420 430 440 450
YYVDWLGEQS PEVYRDALDD VIGDYNIICP ALEFTKKFAE LENNAFFYFF
460 470 480 490 500
EHRSSKLPWP EWMGVMHGYE IEFVFGLPLG RRVNYTRAEE IFSRSIMKTW
510 520 530 540 550
ANFAKYGHPN GTQGNSTMWP VFTSTEQKYL TLNTEKSKIY SKLRAPQCQF
560 570 580 590 600
WRLFFPKVLE MTGDIDETEQ EWKAGFHRWS NYMMDWQNQF NDYTSKKESC

TAL
Length:603
Mass (Da):68,462
Last modified:July 27, 2011 - v2
Checksum:i2CB79C46797B3713
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291P → R in AAA37328 (PubMed:2400605).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99492 mRNA. Translation: AAA37328.1.
AK050337 mRNA. Translation: BAC34196.1.
CH466547 Genomic DNA. Translation: EDL15482.1.
CCDSiCCDS17411.1.
PIRiS70849.
RefSeqiNP_033868.3. NM_009738.3.
UniGeneiMm.250719.

Genome annotation databases

EnsembliENSMUST00000029367; ENSMUSP00000029367; ENSMUSG00000027792.
GeneIDi12038.
KEGGimmu:12038.
UCSCiuc008pmv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99492 mRNA. Translation: AAA37328.1.
AK050337 mRNA. Translation: BAC34196.1.
CH466547 Genomic DNA. Translation: EDL15482.1.
CCDSiCCDS17411.1.
PIRiS70849.
RefSeqiNP_033868.3. NM_009738.3.
UniGeneiMm.250719.

3D structure databases

ProteinModelPortaliQ03311.
SMRiQ03311. Positions 34-558, 565-593.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029367.

Chemistry

BindingDBiQ03311.
ChEMBLiCHEMBL2528.

Protein family/group databases

MEROPSiS09.980.

PTM databases

PhosphoSiteiQ03311.

Proteomic databases

MaxQBiQ03311.
PaxDbiQ03311.
PRIDEiQ03311.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029367; ENSMUSP00000029367; ENSMUSG00000027792.
GeneIDi12038.
KEGGimmu:12038.
UCSCiuc008pmv.1. mouse.

Organism-specific databases

CTDi590.
MGIiMGI:894278. Bche.

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ03311.
KOiK01050.
OMAiYIFGEPL.
OrthoDBiEOG789C9R.
TreeFamiTF315470.

Enzyme and pathway databases

ReactomeiREACT_330516. Synthesis, secretion, and deacylation of Ghrelin.
SABIO-RKQ03311.

Miscellaneous databases

NextBioi280293.
PROiQ03311.
SOURCEiSearch...

Gene expression databases

BgeeiQ03311.
CleanExiMM_BCHE.
GenevestigatoriQ03311.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
ProDomiPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of mouse acetylcholinesterase: tissue distribution of alternatively spliced mRNA species."
    Rachinsky T.L., Camp S., Li Y., Ekstroem T.J., Newton M., Taylor P.
    Neuron 5:317-327(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Use of the polymerase chain reaction for homology probing of butyrylcholinesterase from several vertebrates."
    Arpagaus M., Chatonnet A., Masson P., Newton M., Vaughan T.A., Bartels C.F., Nogueira C.P., la Du B.N., Lockridge O.
    J. Biol. Chem. 266:6966-6974(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 97-237.
    Tissue: Liver.
  5. "Excessive hippocampal acetylcholine levels in acetylcholinesterase-deficient mice are moderated by butyrylcholinesterase activity."
    Hartmann J., Kiewert C., Duysen E.G., Lockridge O., Greig N.H., Klein J.
    J. Neurochem. 100:1421-1429(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Butyrylcholinesterase and the control of synaptic responses in acetylcholinesterase knockout mice."
    Girard E., Bernard V., Minic J., Chatonnet A., Krejci E., Molgo J.
    Life Sci. 80:2380-2385(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Sensitivity of butyrylcholinesterase knockout mice to (--)-huperzine A and donepezil suggests humans with butyrylcholinesterase deficiency may not tolerate these Alzheimer's disease drugs and indicates butyrylcholinesterase function in neurotransmission."
    Duysen E.G., Li B., Darvesh S., Lockridge O.
    Toxicology 233:60-69(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. "The butyrylcholinesterase knockout mouse as a model for human butyrylcholinesterase deficiency."
    Li B., Duysen E.G., Carlson M., Lockridge O.
    J. Pharmacol. Exp. Ther. 324:1146-1154(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCHLE_MOUSE
AccessioniPrimary (citable) accession number: Q03311
Secondary accession number(s): Q543J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.