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Q03311

- CHLE_MOUSE

UniProt

Q03311 - CHLE_MOUSE

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Protein

Cholinesterase

Gene
Bche
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 intermediate By similarity
Active sitei354 – 3541Charge relay system By similarity
Active sitei467 – 4671Charge relay system By similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: UniProtKB
  2. carboxylic ester hydrolase activity Source: RefGenome
  3. choline binding Source: Ensembl
  4. cholinesterase activity Source: UniProtKB

GO - Biological processi

  1. choline metabolic process Source: RefGenome
  2. learning Source: Ensembl
  3. negative regulation of cell proliferation Source: Ensembl
  4. negative regulation of synaptic transmission Source: Ensembl
  5. neuroblast differentiation Source: Ensembl
  6. response to alkaloid Source: Ensembl
  7. response to drug Source: Ensembl
  8. response to folic acid Source: Ensembl
  9. response to glucocorticoid Source: Ensembl
  10. synaptic transmission, cholinergic Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

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: Chromosome 3

Organism-specific databases

MGIiMGI:894278. Bche.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. endoplasmic reticulum lumen Source: RefGenome
  3. extracellular space Source: RefGenome
  4. membrane Source: Ensembl
  5. 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...) Reviewed prediction
Disulfide bondi94 ↔ 121 By similarity
Glycosylationi135 – 1351N-linked (GlcNAc...) Reviewed prediction
Modified residuei227 – 2271Phosphoserine By similarity
Glycosylationi270 – 2701N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi281 ↔ 292 By similarity
Glycosylationi370 – 3701N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi429 ↔ 548 By similarity
Glycosylationi484 – 4841N-linked (GlcNAc...) Reviewed prediction
Glycosylationi510 – 5101N-linked (GlcNAc...) Reviewed prediction
Glycosylationi515 – 5151N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi600 – 600Interchain By 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.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029367.

Structurei

3D structure databases

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

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00740000115241.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ543J3.
KOiK01050.
OMAiIMKTWAN.
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

MQTQHTKVTQ THFLLWILLL CMPFGKSHTE EDFIITTKTG RVRGLSMPVL    50
GGTVTAFLGI PYAQPPLGSL RFKKPQPLNK WPDIHNATQY ANSCYQNIDQ 100
AFPGFQGSEM WNPNTNLSED CLYLNVWIPV PKPKNATVMV WIYGGGFQTG 150
TSSLPVYDGK FLARVERVIV VSMNYRVGAL GFLAFPGNPD APGNMGLFDQ 200
QLALQWVQRN IAAFGGNPKS ITIFGESAGA ASVSLHLLCP QSYPLFTRAI 250
LESGSSNAPW AVKHPEEARN RTLTLAKFTG CSKENEMEMI KCLRSKDPQE 300
ILRNERFVLP SDSILSINFG PTVDGDFLTD MPHTLLQLGK VKKAQILVGV 350
NKDEGTAFLV YGAPGFSKDN DSLITRKEFQ EGLNMYFPGV SRLGKEAVLF 400
YYVDWLGEQS PEVYRDALDD VIGDYNIICP ALEFTKKFAE LENNAFFYFF 450
EHRSSKLPWP EWMGVMHGYE IEFVFGLPLG RRVNYTRAEE IFSRSIMKTW 500
ANFAKYGHPN GTQGNSTMWP VFTSTEQKYL TLNTEKSKIY SKLRAPQCQF 550
WRLFFPKVLE MTGDIDETEQ EWKAGFHRWS NYMMDWQNQF NDYTSKKESC 600
TAL 603
Length:603
Mass (Da):68,462
Last modified:July 27, 2011 - v2
Checksum:i2CB79C46797B3713
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291P → R in AAA37328. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M99492 mRNA. Translation: AAA37328.1 .
AK050337 mRNA. Translation: BAC34196.1 .
CH466547 Genomic DNA. Translation: EDL15482.1 .
CCDSi CCDS17411.1.
PIRi S70849.
RefSeqi NP_033868.3. NM_009738.3.
UniGenei Mm.250719.

3D structure databases

ProteinModelPortali Q03311.
SMRi Q03311. Positions 34-558, 565-593.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000029367.

Chemistry

BindingDBi Q03311.
ChEMBLi CHEMBL2528.

Protein family/group databases

MEROPSi S09.980.

PTM databases

PhosphoSitei Q03311.

Proteomic databases

MaxQBi Q03311.
PaxDbi Q03311.
PRIDEi Q03311.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029367 ; ENSMUSP00000029367 ; ENSMUSG00000027792 .
GeneIDi 12038.
KEGGi mmu:12038.
UCSCi uc008pmv.1. mouse.

Organism-specific databases

CTDi 590.
MGIi MGI:894278. Bche.

Phylogenomic databases

eggNOGi COG2272.
GeneTreei ENSGT00740000115241.
HOGENOMi HOG000091866.
HOVERGENi HBG008839.
InParanoidi Q543J3.
KOi K01050.
OMAi IMKTWAN.
OrthoDBi EOG789C9R.
TreeFami TF315470.

Enzyme and pathway databases

SABIO-RK Q03311.

Miscellaneous databases

NextBioi 280293.
PROi Q03311.
SOURCEi Search...

Gene expression databases

Bgeei Q03311.
CleanExi MM_BCHE.
Genevestigatori Q03311.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view ]
Pfami PF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view ]
PRINTSi PR00878. CHOLNESTRASE.
ProDomi PD415333. AChE_tetra. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 108 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