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Q86GC8 (ACES_CULPI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:ACHE1
OrganismCulex pipiens (House mosquito)
Taxonomic identifier7175 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeCulicinaeCuliciniCulexCulex

Protein attributes

Sequence length702 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Rapidly hydrolyzes choline released into the synapse.

Catalytic activity

Acetylcholine + H2O = choline + acetate. UniProtKB P22303

Subcellular location

Cell junctionsynapse By similarity. Secreted By similarity. Cell membrane; Peripheral membrane protein By similarity.

Polymorphism

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. Ref.1

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
Synapse
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological_processneurotransmitter catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholinesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636 Potential
Chain37 – 702666Acetylcholinesterase
PRO_0000008602

Sites

Active site3271Acyl-ester intermediate By similarity UniProtKB P22303
Active site4531Charge relay system By similarity UniProtKB P22303
Active site5671Charge relay system By similarity UniProtKB P22303

Amino acid modifications

Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation6371N-linked (GlcNAc...) Potential
Disulfide bond195 ↔ 222 By similarity UniProtKB P22303
Disulfide bond381 ↔ 394 By similarity UniProtKB P22303
Disulfide bond529 ↔ 650 By similarity UniProtKB P22303

Natural variations

Natural variant2471G → S in strain: SR; confers resistance to insecticides. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q86GC8 [UniParc].

Last modified August 22, 2003. Version 2.
Checksum: 4B11ABF5EA824A07

FASTA70278,179
        10         20         30         40         50         60 
MEIRGLITRL LGPCHLRHLI LCSLGLYSIL VQSVHCRHHD IGSSVAHQLG SKYSQSSSLS 

        70         80         90        100        110        120 
SSSQSSSSLA EEATLNKDSD AFFTPYIGHG DSVRIVDAEL GTLEREHIHS TTTRRRGLTR 

       130        140        150        160        170        180 
RESSSDATDS DPLVITTDKG KIRGTTLEAP SGKKVDAWMG IPYAQPPLGP LRFRHPRPAE 

       190        200        210        220        230        240 
RWTGVLNATK PPNSCVQIVD TVFGDFPGAT MWNPNTPLSE DCLYINVVVP RPRPKNAAVM 

       250        260        270        280        290        300 
LWIFGGGFYS GTATLDVYDH RTLASEENVI VVSLQYRVAS LGFLFLGTPE APGNAGLFDQ 

       310        320        330        340        350        360 
NLALRWVRDN IHRFGGDPSR VTLFGESAGA VSVSLHLLSA LSRDLFQRAI LQSGSPTAPW 

       370        380        390        400        410        420 
ALVSREEATL RALRLAEAVN CPHDATKLSD AVECLRTKDP NELVDNEWGT LGICEFPFVP 

       430        440        450        460        470        480 
VVDGAFLDET PQRSLASGRF KKTDILTGSN TEEGYYFIIY YLTELLRKEE GVTVTREEFL 

       490        500        510        520        530        540 
QAVRELNPYV NGAARQAIVF EYTDWIEPDN PNSNRDALDK MVGDYHFTCN VNEFAQRYAE 

       550        560        570        580        590        600 
EGNNVFMYLY THRSKGNPWP RWTGVMHGDE INYVFGEPLN SALGYQDDEK DFSRKIMRYW 

       610        620        630        640        650        660 
SNFAKTGNPN PSTPSVDLPE WPKHTAHGRH YLELGLNTTF VGRGPRLRQC AFWKKYLPQL 

       670        680        690        700 
VAATSNLQVT PAPSVPCESS STSYRSTLLL IVTLLLVTRF KI 

« Hide

References

[1]"Insecticide resistance in mosquito vectors."
Weill M., Lutfalla G., Mogensen K., Chandre F., Berthomieu A., Berticat C., Pasteur N., Philips A., Fort P., Raymond M.
Nature 423:136-137(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SLAB and SR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ515147 mRNA. Translation: CAD56155.1.
AJ489456 mRNA. Translation: CAD33707.2.

3D structure databases

ProteinModelPortalQ86GC8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7176.CPIJ006034-PA.

Protein family/group databases

MEROPSS09.979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACES_CULPI
AccessionPrimary (citable) accession number: Q86GC8
Secondary accession number(s): Q86GD0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: June 11, 2014
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families