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P56161

- ACES_ANOST

UniProt

P56161 - ACES_ANOST

Protein

Acetylcholinesterase

Gene
N/A
Organism
Anopheles stephensi (Indo-Pakistan malaria mosquito)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine.

    Catalytic activityi

    Acetylcholine + H2O = choline + acetate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei261 – 2611Acyl-ester intermediatePROSITE-ProRule annotation
    Active sitei390 – 3901Charge relay systemBy similarity
    Active sitei504 – 5041Charge relay systemBy similarity

    GO - Molecular functioni

    1. acetylcholinesterase activity Source: UniProtKB-EC

    GO - Biological processi

    1. acetylcholine catabolic process in synaptic cleft Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Neurotransmitter degradation

    Protein family/group databases

    MEROPSiS09.979.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylcholinesterase (EC:3.1.1.7)
    Short name:
    AChE
    OrganismiAnopheles stephensi (Indo-Pakistan malaria mosquito)
    Taxonomic identifieri30069 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

    Subcellular locationi

    Cell junctionsynapse. Cell membrane; Lipid-anchorGPI-anchor
    Note: Attached to the membrane of the neuronal cholinergic synapses by a GPI-anchor.

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. cell junction Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell
    4. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Synapse

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 647618AcetylcholinesterasePRO_0000008600Add
    BLAST
    Propeptidei648 – 66417Removed in mature formSequence AnalysisPRO_0000008601Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi95 ↔ 122By similarity
    Glycosylationi117 – 1171N-linked (GlcNAc...)By similarity
    Disulfide bondi315 ↔ 330By similarity
    Glycosylationi316 – 3161N-linked (GlcNAc...)By similarity
    Disulfide bondi466 ↔ 588By similarity
    Glycosylationi517 – 5171N-linked (GlcNAc...)By similarity
    Lipidationi647 – 6471GPI-anchor amidated asparagineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP56161.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR001445. Acylcholinesterase_insect.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    IPR000997. Cholinesterase.
    [Graphical view]
    PfamiPF00135. COesterase. 1 hit.
    [Graphical view]
    PRINTSiPR00880. ACHEINSECT.
    PR00878. CHOLNESTRASE.
    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.

    P56161-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFVNQRTRRP YMSVFVLVLG AAVICPAYGI IDRLVVQTSS GPIRGRSTMV    50
    QGREVHVFNG VPFAKPPVDS LRFKKPVPAE PWHGVLDATR LPPSCIQERY 100
    EYFPGFAGEE MWNPNTNVSE DCLYLNIWVP TKTRLRHGRG LNFGSNDYFQ 150
    DDDDFQRQHQ SKGGLAMLVW IYGGGFMSGT STLDIYNAEI LAAVGNVIVA 200
    SMQYRVGAFG FLYLAPYING YEEDAPGNMG MWDQALAIRW LKENAKAFGG 250
    DPDLITLFGE SAGGSSVSLH LLSPVTRGLS KRGILQSGTL NAPWSHMTAE 300
    KALQIAEGLI DDCNCNLTML KESPSTVMQC MRNVDAKTIS VQQWNSYSGI 350
    LGFPSAPTID GVFMTADPMT MLREANLEGI DILVGSNRDE GTYFLLYDFI 400
    DYFEKDAATS LPRDKFLEIM NTIFNKASEP EREAIIFQYT GWESGNDGYQ 450
    NQHQVGRAVG DHFFICPTNE FALGLTERGA SVHYYYFTHR TSTSLWGEWM 500
    GVLHGDEVEY IFGQPMNASL QYRQRERDLS RRMVLSVSEF ARTGNPALEG 550
    EHWPLYTREN PIFFIFNAEG EDDLRGEKYG RGPMATSCAF WNDFLPRLRA 600
    WSVPSKSPCN LLEQMSIASV SSTMPIVVMV VLVLIPLCAW WWAIKKNKTP 650
    PHPQVILETR AFMH 664
    Length:664
    Mass (Da):74,629
    Last modified:November 1, 1997 - v1
    Checksum:i0BFBF9414F8020C7
    GO

    Cross-referencesi

    3D structure databases

    ProteinModelPortali P56161.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S09.979.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR001445. Acylcholinesterase_insect.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    IPR000997. Cholinesterase.
    [Graphical view ]
    Pfami PF00135. COesterase. 1 hit.
    [Graphical view ]
    PRINTSi PR00880. ACHEINSECT.
    PR00878. CHOLNESTRASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
    PS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The acetylcholinesterase gene of Anopheles stephensi."
      Hall L.M.C., Malcolm C.A.
      Cell. Mol. Neurobiol. 11:131-141(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiACES_ANOST
    AccessioniPrimary (citable) accession number: P56161
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3