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Q03311

- CHLE_MOUSE

UniProt

Q03311 - CHLE_MOUSE

Protein

Cholinesterase

Gene

Bche

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    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

    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

    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.
    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 109 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