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Q867X2

- ACES_CULQU

UniProt

Q867X2 - ACES_CULQU

Protein

Acetylcholinesterase

Gene

ACE-1

Organism
Culex quinquefasciatus (Southern house mosquito) (Culex pungens)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
  1. Functioni

    Rapidly hydrolyzes choline released into the synapse.Curated

    Catalytic activityi

    Acetylcholine + H2O = choline + acetate.1 Publication

    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

    Protein family/group databases

    MEROPSiS09.979.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylcholinesterase (EC:3.1.1.7)
    Short name:
    AChE
    Gene namesi
    Name:ACE-1
    OrganismiCulex quinquefasciatus (Southern house mosquito) (Culex pungens)Imported
    Taxonomic identifieri7176 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeCulicinaeCuliciniCulexCulex

    Subcellular locationi

    Cell junctionsynapse By similarity. Secreted By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity

    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
    Chaini‹1 – ›132›132AcetylcholinesterasePRO_0000070281Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi45 ↔ 72By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ867X2.
    SMRiQ867X2. Positions 2-132.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    IPR019819. Carboxylesterase_B_CS.
    IPR000997. Cholinesterase.
    [Graphical view]
    PfamiPF00135. COesterase. 1 hit.
    [Graphical view]
    PRINTSiPR00878. CHOLNESTRASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Q867X2-1 [UniParc]FASTAAdd to Basket

    « Hide

    SGKKVDAWMG IPYAQPPLGP LRFRHPRPAE RWTGVLNATK PPNSCVQIVD    50
    TVFGDFPGAT MWNPNTPLSE DCLYINVVVP RPRPKNAAVM LWIFGGGFYS 100
    GTATLDVYDH RTLASEENVI VVSLQYRVAS LG 132
    Length:132
    Mass (Da):14,543
    Last modified:June 1, 2003 - v1
    Checksum:i2F40C4B3FC2468E8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11Imported
    Non-terminal residuei132 – 1321Imported

    Polymorphismi

    A number of strains are susceptible to insecticides while others are resistant. Insensitivity to insecticides results from a loss of sensitivity of acetylcholinesterase to organophosphates and carbamates and is due to a variant at position 97.1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti97 – 971G → S in strain: BO, DJI, Harare, Martinique, Recife, Supercar, TemR and Trans; confers resistance to insecticides. 1 Publication
    Natural varianti114 – 1141A → T in strain: TemR and Trans. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ512689 Genomic DNA. Translation: CAD54761.1.
    AJ512691 Genomic DNA. Translation: CAD54763.1.
    AJ512692 Genomic DNA. Translation: CAD54764.1.
    AJ512693 Genomic DNA. Translation: CAD54765.1.
    AJ512694 Genomic DNA. Translation: CAD54766.1.
    AJ512697 Genomic DNA. Translation: CAD54769.1.
    AJ512698 Genomic DNA. Translation: CAD54770.1.
    AJ512700 Genomic DNA. Translation: CAD54772.1.
    AJ512703 Genomic DNA. Translation: CAD54775.1.
    AJ512704 Genomic DNA. Translation: CAD54776.1.
    AJ512705 Genomic DNA. Translation: CAD54777.1.
    AJ512706 Genomic DNA. Translation: CAD54778.1.
    AJ512707 Genomic DNA. Translation: CAD54779.1.
    AJ512710 Genomic DNA. Translation: CAD54782.1.
    AJ512711 Genomic DNA. Translation: CAD54783.1.
    AJ512712 Genomic DNA. Translation: CAD54784.1.
    AJ512713 Genomic DNA. Translation: CAD54785.1.
    AJ512714 Genomic DNA. Translation: CAD54786.1.
    AJ512715 Genomic DNA. Translation: CAD54787.1.
    AJ512717 Genomic DNA. Translation: CAD54789.1.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ512689 Genomic DNA. Translation: CAD54761.1 .
    AJ512691 Genomic DNA. Translation: CAD54763.1 .
    AJ512692 Genomic DNA. Translation: CAD54764.1 .
    AJ512693 Genomic DNA. Translation: CAD54765.1 .
    AJ512694 Genomic DNA. Translation: CAD54766.1 .
    AJ512697 Genomic DNA. Translation: CAD54769.1 .
    AJ512698 Genomic DNA. Translation: CAD54770.1 .
    AJ512700 Genomic DNA. Translation: CAD54772.1 .
    AJ512703 Genomic DNA. Translation: CAD54775.1 .
    AJ512704 Genomic DNA. Translation: CAD54776.1 .
    AJ512705 Genomic DNA. Translation: CAD54777.1 .
    AJ512706 Genomic DNA. Translation: CAD54778.1 .
    AJ512707 Genomic DNA. Translation: CAD54779.1 .
    AJ512710 Genomic DNA. Translation: CAD54782.1 .
    AJ512711 Genomic DNA. Translation: CAD54783.1 .
    AJ512712 Genomic DNA. Translation: CAD54784.1 .
    AJ512713 Genomic DNA. Translation: CAD54785.1 .
    AJ512714 Genomic DNA. Translation: CAD54786.1 .
    AJ512715 Genomic DNA. Translation: CAD54787.1 .
    AJ512717 Genomic DNA. Translation: CAD54789.1 .

    3D structure databases

    ProteinModelPortali Q867X2.
    SMRi Q867X2. Positions 2-132.
    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.
    IPR002018. CarbesteraseB.
    IPR019819. Carboxylesterase_B_CS.
    IPR000997. Cholinesterase.
    [Graphical view ]
    Pfami PF00135. COesterase. 1 hit.
    [Graphical view ]
    PRINTSi PR00878. CHOLNESTRASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BEDImported, BOImported, BouakeImported, BrazzaImported, BresilImported, BSQImported, DJIImported, HarareImported, LingImported, MaduraiImported, MaoImported, MartiniqueImported, MooreaImported, ProRImported, RecifeImported, SlabImported, SupercarImported, TemRImported, ThaiImported and TransImported.

    Entry informationi

    Entry nameiACES_CULQU
    AccessioniPrimary (citable) accession number: Q867X2
    Secondary accession number(s): Q867X1, Q867X4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 22, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 55 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