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P07140 (ACES_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylcholinesterase

Short name=AChE
EC=3.1.1.7
Gene names
Name:Ace
ORF Names:CG17907
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length649 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Acetylcholine + H2O = choline + acetate.

Subunit structure

Homodimer; disulfide-linked. The active unit is formed by non-covalent association of the 55 kDa and 16 kDa subunits. Ref.5

Subcellular location

Cell junctionsynapse. Cell membrane; Lipid-anchorGPI-anchor. Note: Attached to the membrane of the neuronal cholinergic synapses by a GPI-anchor. Ref.6 Ref.7

Post-translational modification

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.

Neither N-glycosylation nor dimerization is required for enzyme activity or substrate specificity, but protects the protein against proteolytic digestion.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Synapse
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacetylcholine catabolic process

Inferred from direct assay PubMed 8028587. Source: FlyBase

acetylcholine catabolic process in synaptic cleft

Inferred from electronic annotation. Source: InterPro

choline catabolic process

Inferred from direct assay PubMed 1611033. Source: FlyBase

phototaxis

Inferred from mutant phenotype PubMed 6790339. Source: FlyBase

synaptic transmission

Inferred from mutant phenotype PubMed 14507965. Source: FlyBase

synaptic transmission, cholinergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay PubMed 3141264. Source: FlyBase

plasma membrane

Inferred from direct assay PubMed 20462449PubMed 3141264. Source: FlyBase

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholinesterase activity

Inferred from direct assay PubMed 8028587. Source: FlyBase

cholinesterase activity

Inferred from direct assay PubMed 1611033. Source: FlyBase

protein homodimerization activity

Inferred from mutant phenotype PubMed 8028587. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838
Chain39 – 619581Acetylcholinesterase
PRO_0000008603
Chain39 – ?Acetylcholinesterase 16 kDa subunitPRO_0000008604
Chain? – 619Acetylcholinesterase 55 kDa subunitPRO_0000008605
Propeptide620 – 64930Removed in mature form Potential
PRO_0000008606

Sites

Active site2761Acyl-ester intermediate
Active site4051Charge relay system
Active site5181Charge relay system
Site5691Not glycosylated

Amino acid modifications

Lipidation6191GPI-anchor amidated serine Potential
Glycosylation1261N-linked (GlcNAc...) Ref.8
Glycosylation1741N-linked (GlcNAc...) Ref.8
Glycosylation3311N-linked (GlcNAc...) Ref.8
Glycosylation5311N-linked (GlcNAc...) Ref.8
Disulfide bond104 ↔ 131
Disulfide bond330 ↔ 345
Disulfide bond480 ↔ 598
Disulfide bond615Interchain

Experimental info

Mutagenesis1261N → D: Decrease in apparent molecular weight of 16 kDa subunit. Ref.8
Mutagenesis1741N → 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. Ref.8
Mutagenesis3281C → V: No effect on apparent molecular weight. Ref.8
Mutagenesis3311N → 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. Ref.8
Mutagenesis5311N → 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. Ref.8
Mutagenesis5691N → D: No change in apparent molecular weight of the 55 kDa subunit. Ref.8
Mutagenesis6151C → R: Formation of 75 kDa monomer. Ref.8
Sequence conflict991G → R in AAF54915. Ref.3

Secondary structure

....................................................................................................... 649
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07140 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 5863C73FF99028C0

FASTA64971,785
        10         20         30         40         50         60 
MAISCRQSRV LPMSLPLPLT IPLPLVLVLS LHLSGVCGVI DRLVVQTSSG PVRGRSVTVQ 

        70         80         90        100        110        120 
GREVHVYTGI PYAKPPVEDL RFRKPVPAEP WHGVLDATGL SATCVQERYE YFPGFSGEEI 

       130        140        150        160        170        180 
WNPNTNVSED CLYINVWAPA KARLRHGRGA NGGEHPNGKQ ADTDHLIHNG NPQNTTNGLP 

       190        200        210        220        230        240 
ILIWIYGGGF MTGSATLDIY NADIMAAVGN VIVASFQYRV GAFGFLHLAP EMPSEFAEEA 

       250        260        270        280        290        300 
PGNVGLWDQA LAIRWLKDNA HAFGGNPEWM TLFGESAGSS SVNAQLMSPV TRGLVKRGMM 

       310        320        330        340        350        360 
QSGTMNAPWS HMTSEKAVEI GKALINDCNC NASMLKTNPA HVMSCMRSVD AKTISVQQWN 

       370        380        390        400        410        420 
SYSGILSFPS APTIDGAFLP ADPMTLMKTA DLKDYDILMG NVRDEGTYFL LYDFIDYFDK 

       430        440        450        460        470        480 
DDATALPRDK YLEIMNNIFG KATQAEREAI IFQYTSWEGN PGYQNQQQIG RAVGDHFFTC 

       490        500        510        520        530        540 
PTNEYAQALA ERGASVHYYY FTHRTSTSLW GEWMGVLHGD EIEYFFGQPL NNSLQYRPVE 

       550        560        570        580        590        600 
RELGKRMLSA VIEFAKTGNP AQDGEEWPNF SKEDPVYYIF STDDKIEKLA RGPLAARCSF 

       610        620        630        640 
WNDYLPKVRS WAGTCDGDSG SASISPRLQL LGIAALIYIC AALRTKRVF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05893 mRNA. Translation: CAA29326.1.
AE014297 Genomic DNA. Translation: AAF54915.1.
PIRA25363.
RefSeqNP_001163600.1. NM_001170129.2.
NP_476953.1. NM_057605.5.
UniGeneDm.1179.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DX4X-ray2.70A39-623[»]
1QO9X-ray2.70A39-623[»]
1QONX-ray2.72A39-623[»]
DisProtDP00346.
ProteinModelPortalP07140.
SMRP07140. Positions 41-612.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66709. 1 interaction.
MINTMINT-878831.

Chemistry

DrugBankDB00772. Malathion.

Protein family/group databases

MEROPSS09.979.

Proteomic databases

PaxDbP07140.
PRIDEP07140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID41625.
KEGGdme:Dmel_CG17907.

Organism-specific databases

CTD1636.
FlyBaseFBgn0000024. Ace.

Phylogenomic databases

eggNOGCOG2272.
InParanoidP07140.
KOK01049.
OrthoDBEOG789C9R.
PhylomeDBP07140.

Gene expression databases

BgeeP07140.

Family and domain databases

InterProIPR001445. Acylcholinesterase_insect.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00880. ACHEINSECT.
PR00878. CHOLNESTRASE.
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07140.
GenomeRNAi41625.
NextBio824699.

Entry information

Entry nameACES_DROME
AccessionPrimary (citable) accession number: P07140
Secondary accession number(s): Q9VFY0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase