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P21927

- CHLE_RABIT

UniProt

P21927 - CHLE_RABIT

Protein

Cholinesterase

Gene

BCHE

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      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 By similarity.By similarity

    Catalytic activityi

    An acylcholine + H2O = choline + a carboxylate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei205 – 2051Acyl-ester intermediatePROSITE-ProRule annotation
    Active sitei332 – 3321Charge relay systemBy similarity
    Active sitei445 – 4451Charge relay systemBy similarity

    GO - Molecular functioni

    1. acetylcholinesterase activity Source: UniProtKB
    2. cholinesterase activity Source: UniProtKB

    GO - Biological processi

    1. metabolic process Source: GOC

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 88Sequence Analysis
    Chaini9 – 581573CholinesterasePRO_0000008616Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi72 ↔ 99By similarity
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
    Modified residuei205 – 2051PhosphoserineBy similarity
    Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi259 ↔ 270By similarity
    Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi348 – 3481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi407 ↔ 526By similarity
    Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi488 – 4881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi578 – 578InterchainBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Expressioni

    Tissue specificityi

    Present in most cells except erythrocytes.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000006971.

    Structurei

    3D structure databases

    ProteinModelPortaliP21927.
    SMRiP21927. Positions 11-541, 543-572.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni123 – 1242Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2272.
    HOGENOMiHOG000091866.
    HOVERGENiHBG008839.

    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.

    P21927-1 [UniParc]FASTAAdd to Basket

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    MVTRSSHTED VIITTKNGRI RGINLPVFGG TVTAFLGIPY AQPPLGRLRF    50
    KKPQSLTKWS DIWNATKYAN SCCQNIDQSF PGFHGSEMWN PNTDLSEDCL 100
    YLNVWIPTPK PKNATVMIWI YGGGFQTGTS SLQVYDGKFL TRVERVIVVS 150
    MNYRVGALGF LALPGNPEAP GNMGLFDQQL ALQWVQKNIA AFGGNPKSVT 200
    LFGESAGAAS VSLHLLSPRS HPLFTRAILQ SGSSNAPWEV MSLHEARNRT 250
    LTLAKFVGCS TENETEIIKC LRNKDAQEIL LNEVFVVPFD SLLSVNFGPT 300
    VDGDFLTDMP DTLLQLGQLK KTQILVGVNK DEGTAFLVYG APGFSKDNTS 350
    IITRKEFQEG LKIFFPGVSE FGKESILFHY TDWVDEQRPE NYREALDDVV 400
    GDYNFICPAL EFTKKFSEWG NNAFFYYFEH RSSKLPWPEW MGVMHGYEIE 450
    FVFGLPLERR VNYTKAEEIL SRSIMKRWAN FAKYGNPNGT QNNSTRWPVF 500
    KSTEQKYLTL NTESPRIYTK LRAQQCRFWT LFFPKVLEMT GNIDEAEQEW 550
    KAGFHRWNNY MMAWKNHFND YTSKKERCAG F 581
    Length:581
    Mass (Da):66,156
    Last modified:May 1, 1991 - v1
    Checksum:iFE8B199E7B32EB0A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52090, X52091, X52092 Genomic DNA. Translation: CAA36308.1.
    M62779 Genomic DNA. Translation: AAA31169.1.
    PIRiS10255. C39768.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52090 , X52091 , X52092 Genomic DNA. Translation: CAA36308.1 .
    M62779 Genomic DNA. Translation: AAA31169.1 .
    PIRi S10255. C39768.

    3D structure databases

    ProteinModelPortali P21927.
    SMRi P21927. Positions 11-541, 543-572.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000006971.

    Protein family/group databases

    MEROPSi S09.980.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG2272.
    HOGENOMi HOG000091866.
    HOVERGENi HBG008839.

    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. "Complete sequence of rabbit butyrylcholinesterase."
      Jbilo O., Roudani S., Chatonnet A.
      Nucleic Acids Res. 18:3990-3990(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: New Zealand.
    2. "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 [GENOMIC DNA] OF 75-215.
      Tissue: Liver.

    Entry informationi

    Entry nameiCHLE_RABIT
    AccessioniPrimary (citable) accession number: P21927
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3