Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P07140

- ACES_DROME

UniProt

P07140 - ACES_DROME

(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)

Protein

Acetylcholinesterase

Gene

Ace

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

ReactomeiREACT_181231. Synthesis of PC.

Protein family/group databases

MEROPSiS09.980.

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-KW
Complete GO annotation...

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.
ExpressionAtlasiP07140. differential.

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

        10         20         30         40         50
MAISCRQSRV LPMSLPLPLT IPLPLVLVLS LHLSGVCGVI DRLVVQTSSG
60 70 80 90 100
PVRGRSVTVQ GREVHVYTGI PYAKPPVEDL RFRKPVPAEP WHGVLDATGL
110 120 130 140 150
SATCVQERYE YFPGFSGEEI WNPNTNVSED CLYINVWAPA KARLRHGRGA
160 170 180 190 200
NGGEHPNGKQ ADTDHLIHNG NPQNTTNGLP ILIWIYGGGF MTGSATLDIY
210 220 230 240 250
NADIMAAVGN VIVASFQYRV GAFGFLHLAP EMPSEFAEEA PGNVGLWDQA
260 270 280 290 300
LAIRWLKDNA HAFGGNPEWM TLFGESAGSS SVNAQLMSPV TRGLVKRGMM
310 320 330 340 350
QSGTMNAPWS HMTSEKAVEI GKALINDCNC NASMLKTNPA HVMSCMRSVD
360 370 380 390 400
AKTISVQQWN SYSGILSFPS APTIDGAFLP ADPMTLMKTA DLKDYDILMG
410 420 430 440 450
NVRDEGTYFL LYDFIDYFDK DDATALPRDK YLEIMNNIFG KATQAEREAI
460 470 480 490 500
IFQYTSWEGN PGYQNQQQIG RAVGDHFFTC PTNEYAQALA ERGASVHYYY
510 520 530 540 550
FTHRTSTSLW GEWMGVLHGD EIEYFFGQPL NNSLQYRPVE RELGKRMLSA
560 570 580 590 600
VIEFAKTGNP AQDGEEWPNF SKEDPVYYIF STDDKIEKLA RGPLAARCSF
610 620 630 640
WNDYLPKVRS WAGTCDGDSG SASISPRLQL LGIAALIYIC AALRTKRVF
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

ChEMBLi CHEMBL2242744.

Protein family/group databases

MEROPSi S09.980.

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.
ExpressionAtlasi P07140. differential.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 152 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