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Q869C3

- ACES_ANOGA

UniProt

Q869C3 - ACES_ANOGA

Protein

Acetylcholinesterase

Gene

Ace

Organism
Anopheles gambiae (African malaria mosquito)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 3 (04 Apr 2006)
      Previous versions | rss
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    Functioni

    Rapidly hydrolyzes choline released into the synapse.Curated

    Catalytic activityi

    Acetylcholine + H2O = choline + acetate.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei360 – 3601Acyl-ester intermediatePROSITE-ProRule annotation
    Active sitei486 – 4861Charge relay systemBy similarity
    Active sitei600 – 6001Charge relay systemBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. choline metabolic process Source: RefGenome
    2. neurotransmitter catabolic process Source: UniProtKB-KW
    3. synaptic transmission, cholinergic Source: RefGenome

    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
    Synonyms:ACE1, ACHE1
    ORF Names:AGAP001356
    OrganismiAnopheles gambiae (African malaria mosquito)Imported
    Taxonomic identifieri7165 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
    ProteomesiUP000007062: Chromosome 2R

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Synapse

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838Sequence AnalysisAdd
    BLAST
    Chaini39 – 737699AcetylcholinesterasePRO_0000008599Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi228 ↔ 255By similarity
    Disulfide bondi414 ↔ 427By similarity
    Disulfide bondi562 ↔ 683By similarity
    Glycosylationi670 – 6701N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AZGmodel-A115-737[»]
    ProteinModelPortaliQ869C3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2272.
    HOGENOMiHOG000091866.
    InParanoidiQ869C3.
    KOiK01049.
    OMAiNRDMSED.
    OrthoDBiEOG7353WH.
    PhylomeDBiQ869C3.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    IPR000997. Cholinesterase.
    [Graphical view]
    PfamiPF00135. COesterase. 1 hit.
    [Graphical view]
    PRINTSiPR00878. 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.

    Q869C3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEIRGLLMGR LRLGRRMVPL GLLGVTALLL ILPPFALVQG RHHELNNGAA    50
    IGSHQLSAAA GVGLASQSAQ SGSLASGVMS SVPAAGASSS SSSSLLSSSA 100
    EDDVARITLS KDADAFFTPY IGHGESVRII DAELGTLEHV HSGATPRRRG 150
    LTRRESNSDA NDNDPLVVNT DKGRIRGITV DAPSGKKVDV WLGIPYAQPP 200
    VGPLRFRHPR PAEKWTGVLN TTTPPNSCVQ IVDTVFGDFP GATMWNPNTP 250
    LSEDCLYINV VAPRPRPKNA AVMLWIFGGG FYSGTATLDV YDHRALASEE 300
    NVIVVSLQYR VASLGFLFLG TPEAPGNAGL FDQNLALRWV RDNIHRFGGD 350
    PSRVTLFGES AGAVSVSLHL LSALSRDLFQ RAILQSGSPT APWALVSREE 400
    ATLRALRLAE AVGCPHEPSK LSDAVECLRG KDPHVLVNNE WGTLGICEFP 450
    FVPVVDGAFL DETPQRSLAS GRFKKTEILT GSNTEEGYYF IIYYLTELLR 500
    KEEGVTVTRE EFLQAVRELN PYVNGAARQA IVFEYTDWTE PDNPNSNRDA 550
    LDKMVGDYHF TCNVNEFAQR YAEEGNNVYM YLYTHRSKGN PWPRWTGVMH 600
    GDEINYVFGE PLNPTLGYTE DEKDFSRKIM RYWSNFAKTG NPNPNTASSE 650
    FPEWPKHTAH GRHYLELGLN TSFVGRGPRL RQCAFWKKYL PQLVAATSNL 700
    PGPAPPSEPC ESSAFFYRPD LIVLLVSLLT ATVRFIQ 737
    Length:737
    Mass (Da):80,902
    Last modified:April 4, 2006 - v3
    Checksum:iFDE9CCAE34DF2421
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351F → S in CAD56157. (PubMed:12736674)Curated
    Sequence conflicti65 – 651A → S in CAD56157. (PubMed:12736674)Curated

    Polymorphismi

    Strains Kisumu and Kisumu2 are susceptible to insecticides while strain YAO is resistant. Insensitivity to insecticides results from a loss of sensitivity of acetylcholinesterase to organophosphates and carbamates and is due to a variant at position 280.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti127 – 1271V → A in strain: Kisumu2 and YAO.
    Natural varianti280 – 2801G → S in strain: YAO; confers resistance to insecticides. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ488492 Genomic DNA. Translation: CAD32684.2.
    AJ515149, AJ515148 Genomic DNA. Translation: CAD56156.1.
    AJ515150, AJ488492 Genomic DNA. Translation: CAD56157.2.
    AAAB01008987 Genomic DNA. Translation: EAA01151.3.
    BN000066 Genomic DNA. Translation: CAD29865.2.
    RefSeqiXP_321792.2. XM_321792.4.

    Genome annotation databases

    EnsemblMetazoaiAGAP001356-RA; AGAP001356-PA; AGAP001356.
    GeneIDi1281827.
    KEGGiaga:AgaP_AGAP001356.
    VectorBaseiAGAP001357. Anopheles gambiae.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ488492 Genomic DNA. Translation: CAD32684.2 .
    AJ515149 , AJ515148 Genomic DNA. Translation: CAD56156.1 .
    AJ515150 , AJ488492 Genomic DNA. Translation: CAD56157.2 .
    AAAB01008987 Genomic DNA. Translation: EAA01151.3 .
    BN000066 Genomic DNA. Translation: CAD29865.2 .
    RefSeqi XP_321792.2. XM_321792.4.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AZG model - A 115-737 [» ]
    ProteinModelPortali Q869C3.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL2046266.

    Protein family/group databases

    MEROPSi S09.979.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai AGAP001356-RA ; AGAP001356-PA ; AGAP001356 .
    GeneIDi 1281827.
    KEGGi aga:AgaP_AGAP001356.
    VectorBasei AGAP001357. Anopheles gambiae.

    Organism-specific databases

    CTDi 1281827.

    Phylogenomic databases

    eggNOGi COG2272.
    HOGENOMi HOG000091866.
    InParanoidi Q869C3.
    KOi K01049.
    OMAi NRDMSED.
    OrthoDBi EOG7353WH.
    PhylomeDBi Q869C3.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    IPR000997. Cholinesterase.
    [Graphical view ]
    Pfami PF00135. COesterase. 1 hit.
    [Graphical view ]
    PRINTSi 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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Kisumu, Kisumu2 and YAOImported.
    2. "The genome sequence of the malaria mosquito Anopheles gambiae."
      Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F.
      , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.
      Science 298:129-149(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PEST.
    3. "A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non-homologous to the ace gene in Drosophila."
      Weill M., Fort P., Berthomi eu A., Dubois M.P., Pasteur N., Raymond M.
      Proc. R. Soc. B 269:2007-2016(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL GENE STRUCTURE.

    Entry informationi

    Entry nameiACES_ANOGA
    AccessioniPrimary (citable) accession number: Q869C3
    Secondary accession number(s): Q7PUR2
    , Q7RTM0, Q86GC7, Q8ISM4, Q8ISM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 22, 2003
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 94 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3