Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P07140

- ACES_DROME

UniProt

P07140 - ACES_DROME

Protein

Acetylcholinesterase

Gene

Ace

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei276 – 2761Acyl-ester intermediate
    Active sitei405 – 4051Charge relay system
    Active sitei518 – 5181Charge relay system
    Sitei569 – 5691Not glycosylated

    GO - Molecular functioni

    1. acetylcholinesterase activity Source: FlyBase
    2. cholinesterase activity Source: FlyBase
    3. protein homodimerization activity Source: FlyBase

    GO - Biological processi

    1. acetylcholine catabolic process Source: FlyBase
    2. acetylcholine catabolic process in synaptic cleft Source: InterPro
    3. choline catabolic process Source: FlyBase
    4. phototaxis Source: FlyBase
    5. synaptic transmission Source: FlyBase
    6. synaptic transmission, cholinergic Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Neurotransmitter degradation

    Enzyme and pathway databases

    ReactomeiREACT_181231. Synthesis of PC.

    Protein family/group databases

    MEROPSiS09.979.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylcholinesterase (EC:3.1.1.7)
    Short name:
    AChE
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Ace
    ORF Names:CG17907
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0000024. Ace.

    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. cytoplasm Source: FlyBase
    4. plasma membrane Source: FlyBase
    5. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi126 – 1261N → D: Decrease in apparent molecular weight of 16 kDa subunit. 1 Publication
    Mutagenesisi174 – 1741N → S: Decrease in apparent molecular weight of 55 kDa subunit. Decrease in apparent molecular weight of 55 kDa subunit equivalent to the sum of decreases observed with S-174; D-133 and D-331; when associated with D-331 and D-531. 1 Publication
    Mutagenesisi328 – 3281C → V: No effect on apparent molecular weight. 1 Publication
    Mutagenesisi331 – 3311N → D: Decrease in apparent molecular weight of the 55 kDa subunit. Decrease in apparent molecular weight of 55 kDa subunit equivalent to the sum of individual decreases observed with S-174; D-331 and D-531; when associated with S-174 and D-531. 1 Publication
    Mutagenesisi531 – 5311N → D: Decrease in apparent molecular weight of the 55 kDa subunit. Decrease in apparent molecular weight of 55 kDa subunit equivalent to the sum of individual decreases observed with S-174; D-331 and D-531; when associated with S-174 and D-331. 1 Publication
    Mutagenesisi569 – 5691N → D: No change in apparent molecular weight of the 55 kDa subunit. 1 Publication
    Mutagenesisi615 – 6151C → R: Formation of 75 kDa monomer. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 619Acetylcholinesterase 55 kDa subunitPRO_0000008605
    Signal peptidei1 – 3838Add
    BLAST
    Chaini39 – 619581AcetylcholinesterasePRO_0000008603Add
    BLAST
    Chaini39 – ?Acetylcholinesterase 16 kDa subunitPRO_0000008604
    Propeptidei620 – 64930Removed in mature formSequence AnalysisPRO_0000008606Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi104 ↔ 131
    Glycosylationi126 – 1261N-linked (GlcNAc...)1 Publication
    Glycosylationi174 – 1741N-linked (GlcNAc...)1 Publication
    Disulfide bondi330 ↔ 345
    Glycosylationi331 – 3311N-linked (GlcNAc...)1 Publication
    Disulfide bondi480 ↔ 598
    Glycosylationi531 – 5311N-linked (GlcNAc...)1 Publication
    Disulfide bondi615 – 615Interchain
    Lipidationi619 – 6191GPI-anchor amidated serineSequence Analysis

    Post-translational modificationi

    Proteolytic cleavage into the 16 kDa subunit and the 55 kDa subunits originates from the hydrophilic peptide, aa 148-180, and is associated with excretion out of the cell.1 Publication
    Neither N-glycosylation nor dimerization is required for enzyme activity or substrate specificity, but protects the protein against proteolytic digestion.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiP07140.
    PRIDEiP07140.

    Expressioni

    Gene expression databases

    BgeeiP07140.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. The active unit is formed by non-covalent association of the 55 kDa and 16 kDa subunits.2 Publications

    Protein-protein interaction databases

    BioGridi66709. 1 interaction.
    MINTiMINT-878831.

    Structurei

    Secondary structure

    1
    649
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 475
    Beta strandi50 – 534
    Beta strandi55 – 595
    Beta strandi62 – 7110
    Helixi78 – 803
    Helixi116 – 1194
    Beta strandi133 – 1397
    Beta strandi177 – 1859
    Turni189 – 1913
    Helixi198 – 2003
    Helixi203 – 2097
    Beta strandi212 – 2165
    Helixi222 – 2254
    Helixi229 – 2313
    Helixi234 – 2363
    Turni237 – 2393
    Beta strandi240 – 2423
    Helixi244 – 25815
    Helixi261 – 2633
    Beta strandi265 – 27511
    Helixi277 – 28711
    Turni289 – 2935
    Beta strandi297 – 3026
    Helixi308 – 3103
    Helixi314 – 32714
    Helixi332 – 3354
    Helixi339 – 3468
    Helixi351 – 3577
    Helixi358 – 3614
    Beta strandi376 – 3794
    Turni383 – 3864
    Helixi387 – 3893
    Helixi392 – 3943
    Beta strandi396 – 4027
    Beta strandi404 – 4063
    Helixi407 – 4137
    Turni414 – 4174
    Beta strandi420 – 4223
    Helixi428 – 43811
    Turni439 – 4413
    Helixi444 – 45310
    Beta strandi458 – 4603
    Helixi464 – 47714
    Helixi479 – 49113
    Beta strandi495 – 5017
    Helixi512 – 5143
    Helixi520 – 5256
    Helixi528 – 5303
    Helixi538 – 55720
    Beta strandi572 – 5754
    Beta strandi578 – 5803
    Beta strandi584 – 5863
    Beta strandi588 – 5914
    Helixi592 – 60211
    Helixi605 – 6095

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DX4X-ray2.70A39-623[»]
    1QO9X-ray2.70A39-623[»]
    1QONX-ray2.72A39-623[»]
    DisProtiDP00346.
    ProteinModelPortaliP07140.
    SMRiP07140. Positions 41-612.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07140.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2272.
    InParanoidiP07140.
    KOiK01049.
    OrthoDBiEOG789C9R.
    PhylomeDBiP07140.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    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.

    P07140-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAISCRQSRV LPMSLPLPLT IPLPLVLVLS LHLSGVCGVI DRLVVQTSSG    50
    PVRGRSVTVQ GREVHVYTGI PYAKPPVEDL RFRKPVPAEP WHGVLDATGL 100
    SATCVQERYE YFPGFSGEEI WNPNTNVSED CLYINVWAPA KARLRHGRGA 150
    NGGEHPNGKQ ADTDHLIHNG NPQNTTNGLP ILIWIYGGGF MTGSATLDIY 200
    NADIMAAVGN VIVASFQYRV GAFGFLHLAP EMPSEFAEEA PGNVGLWDQA 250
    LAIRWLKDNA HAFGGNPEWM TLFGESAGSS SVNAQLMSPV TRGLVKRGMM 300
    QSGTMNAPWS HMTSEKAVEI GKALINDCNC NASMLKTNPA HVMSCMRSVD 350
    AKTISVQQWN SYSGILSFPS APTIDGAFLP ADPMTLMKTA DLKDYDILMG 400
    NVRDEGTYFL LYDFIDYFDK DDATALPRDK YLEIMNNIFG KATQAEREAI 450
    IFQYTSWEGN PGYQNQQQIG RAVGDHFFTC PTNEYAQALA ERGASVHYYY 500
    FTHRTSTSLW GEWMGVLHGD EIEYFFGQPL NNSLQYRPVE RELGKRMLSA 550
    VIEFAKTGNP AQDGEEWPNF SKEDPVYYIF STDDKIEKLA RGPLAARCSF 600
    WNDYLPKVRS WAGTCDGDSG SASISPRLQL LGIAALIYIC AALRTKRVF 649
    Length:649
    Mass (Da):71,785
    Last modified:April 1, 1988 - v1
    Checksum:i5863C73FF99028C0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991G → R in AAF54915. (PubMed:10731132)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05893 mRNA. Translation: CAA29326.1.
    AE014297 Genomic DNA. Translation: AAF54915.1.
    PIRiA25363.
    RefSeqiNP_001163600.1. NM_001170129.2.
    NP_476953.1. NM_057605.5.
    UniGeneiDm.1179.

    Genome annotation databases

    GeneIDi41625.
    KEGGidme:Dmel_CG17907.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05893 mRNA. Translation: CAA29326.1 .
    AE014297 Genomic DNA. Translation: AAF54915.1 .
    PIRi A25363.
    RefSeqi NP_001163600.1. NM_001170129.2.
    NP_476953.1. NM_057605.5.
    UniGenei Dm.1179.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DX4 X-ray 2.70 A 39-623 [» ]
    1QO9 X-ray 2.70 A 39-623 [» ]
    1QON X-ray 2.72 A 39-623 [» ]
    DisProti DP00346.
    ProteinModelPortali P07140.
    SMRi P07140. Positions 41-612.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66709. 1 interaction.
    MINTi MINT-878831.

    Chemistry

    DrugBanki DB00772. Malathion.

    Protein family/group databases

    MEROPSi S09.979.

    Proteomic databases

    PaxDbi P07140.
    PRIDEi P07140.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 41625.
    KEGGi dme:Dmel_CG17907.

    Organism-specific databases

    CTDi 1636.
    FlyBasei FBgn0000024. Ace.

    Phylogenomic databases

    eggNOGi COG2272.
    InParanoidi P07140.
    KOi K01049.
    OrthoDBi EOG789C9R.
    PhylomeDBi P07140.

    Enzyme and pathway databases

    Reactomei REACT_181231. Synthesis of PC.

    Miscellaneous databases

    EvolutionaryTracei P07140.
    GenomeRNAii 41625.
    NextBioi 824699.

    Gene expression databases

    Bgeei P07140.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    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 Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5' leader."
      Hall L.M.C., Spierer P.
      EMBO J. 5:2949-2954(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Drosophila melanogaster acetylcholinesterase gene. Structure, evolution and mutations."
      Fournier D., Karch F., Bride J.-M., Hall L.M.C., Berge J.-B., Spierer P.
      J. Mol. Biol. 210:15-22(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Canton-S, MH19 and Oregon-R.
      Tissue: Embryo and Pupae.
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. "Acetylcholinesterase from Drosophila melanogaster. Identification of two subunits encoded by the same gene."
      Fournier D., Bride J.-M., Karsch F., Berge J.-B.
      FEBS Lett. 238:333-337(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    6. "Drosophila acetylcholinesterase: demonstration of a glycoinositol phospholipid anchor and an endogenous proteolytic cleavage."
      Haas R., Marshall T.L., Rosenberry T.L.
      Biochemistry 27:6453-6457(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, GPI-ANCHOR, PROTEIN SEQUENCE OF 40-43.
    7. "Acetylcholinesterases from Musca domestica and Drosophila melanogaster brain are linked to membranes by a glycophospholipid anchor sensitive to an endogenous phospholipase."
      Fournier D., Berge J.-B., Cardoso de Almeida M.L., Bordier C.
      J. Neurochem. 50:1158-1163(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR.
    8. "Post-translational modifications of Drosophila acetylcholinesterase. In vitro mutagenesis and expression in Xenopus oocytes."
      Mutero A., Fournier D.
      J. Biol. Chem. 267:1695-1700(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-126; ASN-174; ASN-331 AND ASN-531, ABSENCE OF GLYCOSYLATION AT ASN-569, INTERCHAIN AT CYS-615, MUTAGENESIS OF ASN-126; ASN-174; CYS-328; ASN-331; ASN-531; ASN-569 AND CYS-615.
    9. "Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors."
      Harel M., Kryger G., Rosenberry T.L., Mallender W.D., Lewis T., Fletcher R.J., Guss J.M., Silman I., Sussman J.L.
      Protein Sci. 9:1063-1072(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 41-623 IN COMPLEX WITH INHIBITOR.

    Entry informationi

    Entry nameiACES_DROME
    AccessioniPrimary (citable) accession number: P07140
    Secondary accession number(s): Q9VFY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3