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Q867X3 (ACES_CULPP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 51. 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:ACE-1
OrganismCulex pipiens pipiens (Northern house mosquito)
Taxonomic identifier38569 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeCulicinaeCuliciniCulexCulex

Protein attributes

Sequence length132 AA.
Sequence statusFragment.
Protein existenceInferred from homology

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

A number of strains are susceptible to insecticides while others are resistant. Insensitivity to insecticides results from a loss of sensitivity of acetylcholinesterase to organophosphates and carbamates and is due to a variant at position 97. 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
   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

Chain‹1 – ›132›132Acetylcholinesterase
PRO_0000070280

Amino acid modifications

Glycosylation371N-linked (GlcNAc...) Potential
Disulfide bond45 ↔ 72 By similarity UniProtKB P22303

Natural variations

Natural variant971G → S in strain: Barriol, Espro, Padova and Praias. Ref.1

Experimental info

Non-terminal residue11
Non-terminal residue1321

Sequences

Sequence LengthMass (Da)Tools
Q867X3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 2F40C4B3FC2468E8

FASTA13214,543
        10         20         30         40         50         60 
SGKKVDAWMG IPYAQPPLGP LRFRHPRPAE RWTGVLNATK PPNSCVQIVD TVFGDFPGAT 

        70         80         90        100        110        120 
MWNPNTPLSE DCLYINVVVP RPRPKNAAVM LWIFGGGFYS GTATLDVYDH RTLASEENVI 

       130 
VVSLQYRVAS LG 

« 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 [GENOMIC DNA].
Strain: Barriol, Bleuet, BrugesA, BrugesB, Espro, Heteren, Killcare, Padova and Praias.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ512688 Genomic DNA. Translation: CAD54760.1.
AJ512690 Genomic DNA. Translation: CAD54762.1.
AJ512695 Genomic DNA. Translation: CAD54767.1.
AJ512696 Genomic DNA. Translation: CAD54768.1.
AJ512699 Genomic DNA. Translation: CAD54771.1.
AJ512701 Genomic DNA. Translation: CAD54773.1.
AJ512702 Genomic DNA. Translation: CAD54774.1.
AJ512708 Genomic DNA. Translation: CAD54780.1.
AJ512709 Genomic DNA. Translation: CAD54781.1.

3D structure databases

ProteinModelPortalQ867X3.
SMRQ867X3. Positions 2-132.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACES_CULPP
AccessionPrimary (citable) accession number: Q867X3
Secondary accession number(s): Q867X5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families