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Q03311 (CHLE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cholinesterase
EC=3.1.1.8
Alternative name(s):
Acylcholine acylhydrolase
Butyrylcholine esterase
Choline esterase II
Pseudocholinesterase
Gene names
Name:Bche
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. Ref.5 Ref.6

Catalytic activity

An acylcholine + H2O = choline + a carboxylate.

Subunit structure

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

Subcellular location

Secreted By similarity.

Tissue specificity

Present in most cells except erythrocytes.

Disruption phenotype

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. Ref.7 Ref.8

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929
Chain30 – 603574Cholinesterase
PRO_0000008614

Regions

Region145 – 1462Substrate binding By similarity

Sites

Active site2271Acyl-ester intermediate By similarity
Active site3541Charge relay system By similarity
Active site4671Charge relay system By similarity

Amino acid modifications

Modified residue2271Phosphoserine By similarity
Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation4841N-linked (GlcNAc...) Potential
Glycosylation5101N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Disulfide bond94 ↔ 121 By similarity
Disulfide bond281 ↔ 292 By similarity
Disulfide bond429 ↔ 548 By similarity
Disulfide bond600Interchain By similarity

Experimental info

Sequence conflict1291P → R in AAA37328. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q03311 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 2CB79C46797B3713

FASTA60368,462
        10         20         30         40         50         60 
MQTQHTKVTQ THFLLWILLL CMPFGKSHTE EDFIITTKTG RVRGLSMPVL GGTVTAFLGI 

        70         80         90        100        110        120 
PYAQPPLGSL RFKKPQPLNK WPDIHNATQY ANSCYQNIDQ AFPGFQGSEM WNPNTNLSED 

       130        140        150        160        170        180 
CLYLNVWIPV PKPKNATVMV WIYGGGFQTG TSSLPVYDGK FLARVERVIV VSMNYRVGAL 

       190        200        210        220        230        240 
GFLAFPGNPD APGNMGLFDQ QLALQWVQRN IAAFGGNPKS ITIFGESAGA ASVSLHLLCP 

       250        260        270        280        290        300 
QSYPLFTRAI LESGSSNAPW AVKHPEEARN RTLTLAKFTG CSKENEMEMI KCLRSKDPQE 

       310        320        330        340        350        360 
ILRNERFVLP SDSILSINFG PTVDGDFLTD MPHTLLQLGK VKKAQILVGV NKDEGTAFLV 

       370        380        390        400        410        420 
YGAPGFSKDN DSLITRKEFQ EGLNMYFPGV SRLGKEAVLF YYVDWLGEQS PEVYRDALDD 

       430        440        450        460        470        480 
VIGDYNIICP ALEFTKKFAE LENNAFFYFF EHRSSKLPWP EWMGVMHGYE IEFVFGLPLG 

       490        500        510        520        530        540 
RRVNYTRAEE IFSRSIMKTW ANFAKYGHPN GTQGNSTMWP VFTSTEQKYL TLNTEKSKIY 

       550        560        570        580        590        600 
SKLRAPQCQF WRLFFPKVLE MTGDIDETEQ EWKAGFHRWS NYMMDWQNQF NDYTSKKESC 


TAL

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M99492 mRNA. Translation: AAA37328.1.
AK050337 mRNA. Translation: BAC34196.1.
CH466547 Genomic DNA. Translation: EDL15482.1.
IPIIPI00131168.
PIRS70849.
RefSeqNP_033868.3. NM_009738.3.
UniGeneMm.250719.

3D structure databases

ProteinModelPortalQ03311.
SMRQ03311. Positions 34-558, 565-593.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000029367.

Protein family/group databases

MEROPSS09.980.

PTM databases

PhosphoSiteQ03311.

Proteomic databases

PaxDbQ03311.
PRIDEQ03311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029367; ENSMUSP00000029367; ENSMUSG00000027792.
GeneID12038.
KEGGmmu:12038.

Organism-specific databases

CTD590.
MGIMGI:894278. Bche.

Phylogenomic databases

eggNOGCOG2272.
GeneTreeENSGT00700000104419.
HOGENOMHOG000091866.
HOVERGENHBG008839.
InParanoidQ543J3.
KOK01050.
OMALNVWVPD.
OrthoDBEOG46WZ86.

Enzyme and pathway databases

SABIO-RKQ03311.

Gene expression databases

BgeeQ03311.
CleanExMM_BCHE.
GenevestigatorQ03311.
GermOnlineENSMUSG00000027792. Mus musculus.

Family and domain databases

InterProIPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
ProDomPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ03311.
ChEMBLCHEMBL2528.
NextBio280293.
SOURCESearch...

Entry information

Entry nameCHLE_MOUSE
AccessionPrimary (citable) accession number: Q03311
Secondary accession number(s): Q543J3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 27, 2011
Last modified: April 3, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents