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O42275

- ACES_ELEEL

UniProt

O42275 - ACES_ELEEL

Protein

Acetylcholinesterase

Gene

ache

Organism
Electrophorus electricus (Electric eel) (Gymnotus electricus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.

    Catalytic activityi

    Acetylcholine + H2O = choline + acetate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei225 – 2251Acyl-ester intermediatePROSITE-ProRule annotation
    Active sitei352 – 3521Charge relay systemBy similarity
    Active sitei494 – 4941Charge relay systemBy similarity

    GO - Molecular functioni

    1. acetylcholinesterase activity Source: UniProtKB-EC

    GO - Biological processi

    1. neurotransmitter catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Neurotransmitter degradation

    Enzyme and pathway databases

    SABIO-RKO42275.

    Protein family/group databases

    MEROPSiS09.979.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylcholinesterase (EC:3.1.1.7)
    Short name:
    AChE
    Gene namesi
    Name:ache
    OrganismiElectrophorus electricus (Electric eel) (Gymnotus electricus)
    Taxonomic identifieri8005 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiGymnotiformesGymnotoideiGymnotidaeElectrophorus

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. extracellular region Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell
    4. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Secreted, Synapse

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 633610AcetylcholinesterasePRO_0000008594Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi91 ↔ 118By similarity
    Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi279 ↔ 290By similarity
    Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi427 ↔ 579By similarity
    Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi591 – 5911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi630 – 630InterchainBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Structurei

    3D structure databases

    ProteinModelPortaliO42275.
    SMRiO42275. Positions 28-591, 594-627.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    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. 2 hits.
    [Graphical view]
    PRINTSiPR00878. CHOLNESTRASE.
    ProDomiPD415333. AChE_tetra. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF53474. SSF53474. 2 hits.
    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.

    O42275-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKILDALLFP VIFIMFFIHL SIAQTDPELT IMTRLGQVQG TRLPVPDRSH    50
    VIAFLGIPFA EPPLGKMRFK PPEPKKPWND VFDARDYPSA CYQYVDTSYP 100
    GFSGTEMWNP NRMMSEDCLY LNVWVPATPR PHNLTVMVWI YGGGFYSGSS 150
    SLDVYDGRYL AHSEKVVVVS MNYRVSAFGF LALNGSAEAP GNVGLLDQRL 200
    ALQWVQDNIH FFGGNPKQVT IFGESAGAAS VGMHLLSPDS RPKFTRAILQ 250
    SGVPNGPWRT VSFDEARRRA IKLGRLVGCP DGNDTDLIDC LRSKQPQDLI 300
    DQEWLVLPFS GLFRFSFVPV IDGVVFPDTP EAMLNSGNFK DTQILLGVNQ 350
    NEGSYFLIYG APGFSKDNES LITREDFLQG VKMSVPHANE IGLEAVILQY 400
    TDWMDEDNPI KNREAMDDIV GDHNVVCPLQ HFAKMYAQYS ILQGQTGTAS 450
    QGNLGWGNSG SASNSGNSQV SVYLYMFDHR ASNLVWPEWM GVIHGYEIEF 500
    VFGLPLEKRL NYTLEEEKLS RRMMKYWANF ARTGNPNINV DGSIDSRRRW 550
    PVFTSTEQKH VGLNTDSLKV HKGLKSQFCA LWNRFLPRLL NVTENIDDAE 600
    RQWKAEFHRW SSYMMHWKNQ FDHYSKQERC TNL 633
    Length:633
    Mass (Da):71,815
    Last modified:January 1, 1998 - v1
    Checksum:iFC92FE7E4ADB84C3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF030422 Genomic DNA. Translation: AAB86606.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF030422 Genomic DNA. Translation: AAB86606.1 .

    3D structure databases

    ProteinModelPortali O42275.
    SMRi O42275. Positions 28-591, 594-627.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi O42275.
    ChEMBLi CHEMBL4078.

    Protein family/group databases

    MEROPSi S09.979.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG008839.

    Enzyme and pathway databases

    SABIO-RK O42275.

    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. 2 hits.
    [Graphical view ]
    PRINTSi PR00878. CHOLNESTRASE.
    ProDomi PD415333. AChE_tetra. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF53474. SSF53474. 2 hits.
    PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
    PS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of acetylcholinesterase from Electrophorus. Splicing pattern of the 3' exons in vivo and in transfected mammalian cells."
      Simon S., Massoulie J.
      J. Biol. Chem. 272:33045-33055(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiACES_ELEEL
    AccessioniPrimary (citable) accession number: O42275
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3