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Protein

Acetylcholinesterase

Gene

ACHE1

Organism
Culex pipiens (House mosquito)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Rapidly hydrolyzes choline released into the synapse.Curated

Catalytic activityi

Acetylcholine + H2O = choline + acetate.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei327 – 3271Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei453 – 4531Charge relay systemBy similarity
Active sitei567 – 5671Charge relay systemBy similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. neurotransmitter catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Protein family/group databases

MEROPSiS09.980.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
Gene namesi
Name:ACHE1
OrganismiCulex pipiens (House mosquito)Imported
Taxonomic identifieri7175 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeCulicinaeCuliciniCulexCulex

Subcellular locationi

  1. Cell junctionsynapse By similarity
  2. Secreted By similarity
  3. Cell membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB-SubCell
  4. synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Sequence AnalysisAdd
BLAST
Chaini37 – 702666AcetylcholinesterasePRO_0000008602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi195 ↔ 222By similarity
Disulfide bondi381 ↔ 394By similarity
Disulfide bondi529 ↔ 650By similarity
Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi7176.CPIJ006034-PA.

Structurei

3D structure databases

ProteinModelPortaliQ86GC8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. 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.

Q86GC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIRGLITRL LGPCHLRHLI LCSLGLYSIL VQSVHCRHHD IGSSVAHQLG
60 70 80 90 100
SKYSQSSSLS SSSQSSSSLA EEATLNKDSD AFFTPYIGHG DSVRIVDAEL
110 120 130 140 150
GTLEREHIHS TTTRRRGLTR RESSSDATDS DPLVITTDKG KIRGTTLEAP
160 170 180 190 200
SGKKVDAWMG IPYAQPPLGP LRFRHPRPAE RWTGVLNATK PPNSCVQIVD
210 220 230 240 250
TVFGDFPGAT MWNPNTPLSE DCLYINVVVP RPRPKNAAVM LWIFGGGFYS
260 270 280 290 300
GTATLDVYDH RTLASEENVI VVSLQYRVAS LGFLFLGTPE APGNAGLFDQ
310 320 330 340 350
NLALRWVRDN IHRFGGDPSR VTLFGESAGA VSVSLHLLSA LSRDLFQRAI
360 370 380 390 400
LQSGSPTAPW ALVSREEATL RALRLAEAVN CPHDATKLSD AVECLRTKDP
410 420 430 440 450
NELVDNEWGT LGICEFPFVP VVDGAFLDET PQRSLASGRF KKTDILTGSN
460 470 480 490 500
TEEGYYFIIY YLTELLRKEE GVTVTREEFL QAVRELNPYV NGAARQAIVF
510 520 530 540 550
EYTDWIEPDN PNSNRDALDK MVGDYHFTCN VNEFAQRYAE EGNNVFMYLY
560 570 580 590 600
THRSKGNPWP RWTGVMHGDE INYVFGEPLN SALGYQDDEK DFSRKIMRYW
610 620 630 640 650
SNFAKTGNPN PSTPSVDLPE WPKHTAHGRH YLELGLNTTF VGRGPRLRQC
660 670 680 690 700
AFWKKYLPQL VAATSNLQVT PAPSVPCESS STSYRSTLLL IVTLLLVTRF

KI
Length:702
Mass (Da):78,179
Last modified:August 22, 2003 - v2
Checksum:i4B11ABF5EA824A07
GO

Polymorphismi

Strain SLAB is susceptible to insecticides while strain SR is resistant. Insensitivity to insecticides results from a loss of sensitivity of acetylcholinesterase to organophosphates and carbamates and is due to a variant at position 247.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti247 – 2471G → S in strain: SR; confers resistance to insecticides. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ515147 mRNA. Translation: CAD56155.1.
AJ489456 mRNA. Translation: CAD33707.2.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ515147 mRNA. Translation: CAD56155.1.
AJ489456 mRNA. Translation: CAD33707.2.

3D structure databases

ProteinModelPortaliQ86GC8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7176.CPIJ006034-PA.

Protein family/group databases

MEROPSiS09.980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: SLABImported and SRImported.

Entry informationi

Entry nameiACES_CULPI
AccessioniPrimary (citable) accession number: Q86GC8
Secondary accession number(s): Q86GD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: January 7, 2015
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.