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Protein

Acetylcholinesterase

Gene

Ace

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei276Acyl-ester intermediate1
Active sitei405Charge relay system1
Active sitei518Charge relay system1

GO - Molecular functioni

  • acetylcholinesterase activity Source: FlyBase
  • cholinesterase activity Source: FlyBase
  • protein homodimerization activity Source: CAFA
  • sulfate binding Source: CAFA

GO - Biological processi

  • acetylcholine catabolic process Source: FlyBase
  • acetylcholine catabolic process in synaptic cleft Source: InterPro
  • chemical synaptic transmission Source: FlyBase
  • choline catabolic process Source: FlyBase
  • phototaxis Source: FlyBase

Keywordsi

Molecular functionHydrolase, Serine esterase
Biological processNeurotransmitter degradation

Enzyme and pathway databases

BRENDAi3.1.1.7 1994
ReactomeiR-DME-112311 Neurotransmitter clearance
R-DME-1483191 Synthesis of PC

Protein family/group databases

ESTHERidrome-ACHE AChE
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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0000024 Ace

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi126N → D: Decrease in apparent molecular weight of 16 kDa subunit. 1 Publication1
Mutagenesisi174N → 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 Publication1
Mutagenesisi328C → V: No effect on apparent molecular weight. 1 Publication1
Mutagenesisi331N → 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 Publication1
Mutagenesisi531N → 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 Publication1
Mutagenesisi569N → D: No change in apparent molecular weight of the 55 kDa subunit. 1 Publication1
Mutagenesisi615C → R: Formation of 75 kDa monomer. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2242744

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000008605? – 619Acetylcholinesterase 55 kDa subunit
Signal peptidei1 – 38Add BLAST38
ChainiPRO_000000860339 – 619AcetylcholinesteraseAdd BLAST581
ChainiPRO_000000860439 – ?Acetylcholinesterase 16 kDa subunit
PropeptideiPRO_0000008606620 – 649Removed in mature formSequence analysisAdd BLAST30

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi104 ↔ 131
Glycosylationi126N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi174N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi330 ↔ 345
Glycosylationi331N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi480 ↔ 598
Glycosylationi531N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi615Interchain
Lipidationi619GPI-anchor amidated serineSequence analysis1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei569Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP07140
PRIDEiP07140

PTM databases

iPTMnetiP07140

Expressioni

Gene expression databases

BgeeiFBgn0000024
ExpressionAtlasiP07140 baseline and differential
GenevisibleiP07140 DM

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

GO - Molecular functioni

  • protein homodimerization activity Source: CAFA

Protein-protein interaction databases

BioGridi66709, 6 interactors
STRINGi7227.FBpp0289713

Structurei

Secondary structure

1649
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 47Combined sources5
Beta strandi50 – 53Combined sources4
Beta strandi55 – 59Combined sources5
Beta strandi62 – 71Combined sources10
Helixi78 – 80Combined sources3
Helixi116 – 119Combined sources4
Beta strandi133 – 139Combined sources7
Beta strandi177 – 185Combined sources9
Turni189 – 191Combined sources3
Helixi198 – 200Combined sources3
Helixi203 – 209Combined sources7
Beta strandi212 – 216Combined sources5
Helixi222 – 225Combined sources4
Helixi229 – 231Combined sources3
Helixi234 – 236Combined sources3
Turni237 – 239Combined sources3
Beta strandi240 – 242Combined sources3
Helixi244 – 258Combined sources15
Helixi261 – 263Combined sources3
Beta strandi265 – 275Combined sources11
Helixi277 – 287Combined sources11
Turni289 – 293Combined sources5
Beta strandi297 – 302Combined sources6
Helixi308 – 310Combined sources3
Helixi314 – 327Combined sources14
Helixi332 – 335Combined sources4
Helixi339 – 346Combined sources8
Helixi351 – 357Combined sources7
Helixi358 – 361Combined sources4
Beta strandi376 – 379Combined sources4
Turni383 – 386Combined sources4
Helixi387 – 389Combined sources3
Helixi392 – 394Combined sources3
Beta strandi396 – 402Combined sources7
Beta strandi404 – 406Combined sources3
Helixi407 – 413Combined sources7
Turni414 – 417Combined sources4
Beta strandi420 – 422Combined sources3
Helixi428 – 438Combined sources11
Turni439 – 441Combined sources3
Helixi444 – 453Combined sources10
Beta strandi458 – 460Combined sources3
Helixi464 – 477Combined sources14
Helixi479 – 491Combined sources13
Beta strandi495 – 501Combined sources7
Helixi512 – 514Combined sources3
Helixi520 – 525Combined sources6
Helixi528 – 530Combined sources3
Helixi538 – 557Combined sources20
Beta strandi572 – 575Combined sources4
Beta strandi578 – 580Combined sources3
Beta strandi584 – 586Combined sources3
Beta strandi588 – 591Combined sources4
Helixi592 – 602Combined sources11
Helixi605 – 609Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DX4X-ray2.70A39-623[»]
1QO9X-ray2.70A39-623[»]
1QONX-ray2.72A39-623[»]
DisProtiDP00346
ProteinModelPortaliP07140
SMRiP07140
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07140

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4389 Eukaryota
COG2272 LUCA
InParanoidiP07140
KOiK01049
OrthoDBiEOG091G0I4G
PhylomeDBiP07140

Family and domain databases

InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR001445 Acylcholinesterase_insect
IPR002018 CarbesteraseB
IPR019826 Carboxylesterase_B_AS
IPR019819 Carboxylesterase_B_CS
IPR000997 Cholinesterase
PfamiView protein in Pfam
PF00135 COesterase, 1 hit
PRINTSiPR00880 ACHEINSECT
PR00878 CHOLNESTRASE
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00122 CARBOXYLESTERASE_B_1, 1 hit
PS00941 CARBOXYLESTERASE_B_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti99G → R in AAF54915 (PubMed:10731132).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiACES_DROME
AccessioniPrimary (citable) accession number: P07140
Secondary accession number(s): Q9VFY0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 23, 2018
This is version 181 of the entry and version 1 of the sequence. See 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

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