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UniProtKB/Swiss-Prot entry P07140


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACES_DROME
Primary accession number P07140
Secondary accession number Q9VFY0
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on April 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 101)
Name and origin of the protein
Protein name Acetylcholinesterase [Precursor]
Synonyms AChE
EC 3.1.1.7
Contains Acetylcholinesterase 16 kDa subunit
Acetylcholinesterase 55 kDa subunit
Gene name
Name: Ace
ORFNames: CG17907
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3024971 [NCBI, ExPASy, EBI, Israel, Japan]
Hall L.M.C., Spierer P.;
"The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5' leader.";
EMBO J. 5:2949-2954(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Canton-S, MH19, and Oregon-R;
TISSUE=Embryo, and Pupae;
DOI=10.1016/0022-2836(89)90287-8; PubMed=2511327 [NCBI, ExPASy, EBI, Israel, Japan]
Fournier D., Karch F., Bride J.-M., Hall L.M.C., Berge J.-B., Spierer P.;
"Drosophila melanogaster acetylcholinesterase gene. Structure, evolution and mutations.";
J. Mol. Biol. 210:15-22(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
SUBUNIT.
DOI=10.1016/0014-5793(88)80507-6; PubMed=3139459 [NCBI, ExPASy, EBI, Israel, Japan]
Fournier D., Bride J.-M., Karsch F., Berge J.-B.;
"Acetylcholinesterase from Drosophila melanogaster. Identification of two subunits encoded by the same gene.";
FEBS Lett. 238:333-337(1988).
[6]
PROTEOLYTIC PROCESSING, GPI-ANCHOR, AND PROTEIN SEQUENCE OF 40-43.
DOI=10.1021/bi00417a038; PubMed=2975507 [NCBI, ExPASy, EBI, Israel, Japan]
Haas R., Marshall T.L., Rosenberry T.L.;
"Drosophila acetylcholinesterase: demonstration of a glycoinositol phospholipid anchor and an endogenous proteolytic cleavage.";
Biochemistry 27:6453-6457(1988).
[7]
GPI-ANCHOR.
DOI=10.1111/j.1471-4159.1988.tb10587.x; PubMed=2831298 [NCBI, ExPASy, EBI, Israel, Japan]
Fournier D., Berge J.-B., Cardoso de Almeida M.L., Bordier C.;
"Acetylcholinesterases from Musca domestica and Drosophila melanogaster brain are linked to membranes by a glycophospholipid anchor sensitive to an endogenous phospholipase.";
J. Neurochem. 50:1158-1163(1988).
[8]
GLYCOSYLATION AT ASN-126; ASN-174; ASN-331 AND ASN-531, ABSENCE OF GYCOSYLATION AT ASN-569, INTERCHAIN AT CYS-615, AND MUTAGENESIS OF ASN-126; ASN-174; CYS-328; ASN-331; ASN-531; ASN-569 AND CYS-615.
PubMed=1730712 [NCBI, ExPASy, EBI, Israel, Japan]
Mutero A., Fournier D.;
"Post-translational modifications of Drosophila acetylcholinesterase. In vitro mutagenesis and expression in Xenopus oocytes.";
J. Biol. Chem. 267:1695-1700(1992).
[9]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 41-623 IN COMPLEX WITH INHIBITOR.
PubMed=10892800 [NCBI, ExPASy, EBI, Israel, Japan]
Harel M., Kryger G., Rosenberry T.L., Mallender W.D., Lewis T., Fletcher R.J., Guss J.M., Silman I., Sussman J.L.;
"Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors.";
Protein Sci. 9:1063-1072(2000).
Comments
  • FUNCTION: Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine.
  • CATALYTIC ACTIVITY: Acetylcholine + H2O = choline + acetate.
  • SUBUNIT: Homodimer; disulfide-linked. The active unit is formed by non-covalent association of the 55 kDa and 16 kDa subunits.
  • SUBCELLULAR LOCATION: Cell junction, synapse. Cell membrane; Lipid-anchor, GPI-anchor. Note=Attached to the membrane of the neuronal cholinergic synapses by a GPI-anchor.
  • PTM: 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.
  • PTM: Neither N-glycosylation nor dimerization is required for enzyme activity or substrate specificity, but protects the protein against proteolytic digestion.
  • SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X05893; CAA29326.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAF54915.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A25363; A25363.
RefSeq NP_476953.1; -.
UniGene Dm.1179
3D structure databases
PDB
1DX4; X-ray; 2.70 A; A=39-621.[ExPASy / RCSB / EBI]
1QO9; X-ray; 2.70 A; A=39-621.[ExPASy / RCSB / EBI]
1QON; X-ray; 2.72 A; A=39-621.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DX4; -.
1QO9; -.
1QON; -.
DisProt DP00346; -.
ModBase P07140.
Protein-protein interaction databases
IntAct P07140; -.
Protein family/group databases
MEROPS S09.979; -.
Organism-specific databases
FlyBase FBgn0000024; Ace.
Gene expression databases
ArrayExpress P07140; -.
GermOnline CG17907; Drosophila melanogaster.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from FlyBase).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from FlyBase).
GO:0003990; Molecular function: acetylcholinesterase activity (inferred from direct assay from FlyBase).
GO:0004104; Molecular function: cholinesterase activity (inferred from direct assay from FlyBase).
GO:0042803; Molecular function: protein homodimerization activity (inferred from mutant phenotype from FlyBase).
GO:0006581; Biological process: acetylcholine catabolic process (inferred from direct assay from FlyBase).
GO:0042426; Biological process: choline catabolic process (inferred from direct assay from FlyBase).
GO:0042331; Biological process: phototaxis (inferred from mutant phenotype from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR001445; Acylcholinesterase_insect.
IPR002018; CarbesteraseB.
IPR000997; Cholinesterase.
Graphical view of domain structure.
PANTHER PTHR11559; CarbesteraseB; 1.
Pfam PF00135; COesterase; 1.
Pfam graphical view of domain structure.
PRINTS PR00880; ACHEINSECT.
PR00878; CHOLNESTRASE.
PROSITE PS00122; CARBOXYLESTERASE_B_1; 1.
PS00941; CARBOXYLESTERASE_B_2; 1.
BLOCKS P07140.
ProtoNet P07140.
Genome annotation databases
Ensembl CG17907; Drosophila melanogaster. [Contig view]
GeneID 41625; -.
KEGG dme:Dmel_CG17907; -.
Phylogenomic databases
HOGENOM P07140; -.
Other
DrugBank DB00772; Malathion.
LinkHub P07140; -.
NextBio 824699; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell junction; Cell membrane; Complete proteome; Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation; Serine esterase; Signal; Synapse.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    38  38      
CHAIN   39   619  581     Acetylcholinesterase. PRO_0000008603
CHAIN   39     ?        Acetylcholinesterase 16 kDa subunit. PRO_0000008604
CHAIN   ?   619        Acetylcholinesterase 55 kDa subunit. PRO_0000008605
PROPEP   620   649  30     Removed in mature form (Potential). PRO_0000008606
ACT_SITE   276   276        Acyl-ester intermediate. 
ACT_SITE   405   405        Charge relay system. 
ACT_SITE   518   518        Charge relay system. 
LIPID   619   619        GPI-anchor amidated serine (Potential). 
CARBOHYD   126   126        N-linked (GlcNAc...). 
CARBOHYD   174   174        N-linked (GlcNAc...). 
CARBOHYD   331   331        N-linked (GlcNAc...). 
CARBOHYD   531   531        N-linked (GlcNAc...). 
DISULFID   104   131         
DISULFID   330   345         
DISULFID   480   598         
DISULFID   615   615        Interchain. 
MUTAGEN   126   126        N->D: Decrease in apparent molecular weight of 16 kDa subunit. 
MUTAGEN   174   174        N->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. 
MUTAGEN   328   328        C->V: No effect on apparent molecular weight. 
MUTAGEN   331   331        N->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. 
MUTAGEN   531   531        N->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. 
MUTAGEN   569   569        N->D: No change in apparent molecular weight of the 55 kDa subunit. 
MUTAGEN   615   615        C->R: Formation of 75 kDa monomer. 
CONFLICT   99    99        G -> R (in Ref. 3; AAF54915). 
STRAND   43    47  5      
STRAND   50    53  4      
STRAND   55    59  5      
STRAND   62    71  10      
HELIX   78    80  3      
HELIX   116   119  4      
STRAND   133   139  7      
STRAND   177   185  9      
TURN   189   191  3      
HELIX   198   200  3      
HELIX   203   209  7      
STRAND   212   216  5      
HELIX   222   225  4      
HELIX   229   231  3      
HELIX   234   236  3      
HELIX   244   258  15      
HELIX   261   263  3      
STRAND   265   275  11      
HELIX   277   287  11      
TURN   289   293  5      
STRAND   297   302  6      
HELIX   308   310  3      
HELIX   314   327  14      
HELIX   332   335  4      
HELIX   339   346  8      
HELIX   351   357  7      
HELIX   358   361  4      
STRAND   376   379  4      
TURN   383   386  4      
HELIX   387   389  3      
HELIX   392   394  3      
STRAND   396   402  7      
STRAND   404   406  3      
HELIX   407   413  7      
TURN   414   417  4      
STRAND   420   422  3      
HELIX   428   438  11      
TURN   439   441  3      
HELIX   444   453  10      
HELIX   464   477  14      
HELIX   479   491  13      
STRAND   495   501  7      
HELIX   512   514  3      
HELIX   520   525  6      
HELIX   528   530  3      
HELIX   538   557  20      
STRAND   572   575  4      
STRAND   578   580  3      
STRAND   584   586  3      
HELIX   592   602  11      
HELIX   605   609  5      
Sequence information
Length: 649 AA [This is the length of the unprocessed precursor] Molecular weight: 71785 Da [This is the MW of the unprocessed precursor] CRC64: 5863C73FF99028C0 [This is a checksum on the sequence]
        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 

P07140 in FASTA format

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