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Q867X2 (ACES_CULQU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 47. 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 quinquefasciatus (Southern house mosquito) (Culex pungens)
Taxonomic identifier7176 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeCulicinaeCuliciniCulexCulex

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. Ref.1

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: EC

carboxylesterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›132›132Acetylcholinesterase
PRO_0000070281

Amino acid modifications

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

Natural variations

Natural variant971G → S in strain: BO, DJI, Harare, Martinique, Recife, Supercar, TemR and Trans; confers resistance to insecticides. Ref.1
Natural variant1141A → T in strain: TemR and Trans. Ref.1

Experimental info

Non-terminal residue11
Non-terminal residue1321

Sequences

Sequence LengthMass (Da)Tools
Q867X2 [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: 12736674] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BED, BO, Bouake, Brazza, Bresil, BSQ, DJI, Harare, Ling, Madurai, Mao, Martinique, Moorea, ProR, Recife, Slab, Supercar, TemR, Thai and Trans.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ512689 Genomic DNA. Translation: CAD54761.1.
AJ512691 Genomic DNA. Translation: CAD54763.1.
AJ512692 Genomic DNA. Translation: CAD54764.1.
AJ512693 Genomic DNA. Translation: CAD54765.1.
AJ512694 Genomic DNA. Translation: CAD54766.1.
AJ512697 Genomic DNA. Translation: CAD54769.1.
AJ512698 Genomic DNA. Translation: CAD54770.1.
AJ512700 Genomic DNA. Translation: CAD54772.1.
AJ512703 Genomic DNA. Translation: CAD54775.1.
AJ512704 Genomic DNA. Translation: CAD54776.1.
AJ512705 Genomic DNA. Translation: CAD54777.1.
AJ512706 Genomic DNA. Translation: CAD54778.1.
AJ512707 Genomic DNA. Translation: CAD54779.1.
AJ512710 Genomic DNA. Translation: CAD54782.1.
AJ512711 Genomic DNA. Translation: CAD54783.1.
AJ512712 Genomic DNA. Translation: CAD54784.1.
AJ512713 Genomic DNA. Translation: CAD54785.1.
AJ512714 Genomic DNA. Translation: CAD54786.1.
AJ512715 Genomic DNA. Translation: CAD54787.1.
AJ512717 Genomic DNA. Translation: CAD54789.1.

3D structure databases

ProteinModelPortalQ867X2.
SMRQ867X2. Positions 2-132.
ModBaseSearch...

Protein family/group databases

MEROPSS09.979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

GeneTreeEMGT00050000001175.

Family and domain databases

InterProIPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
PROSITEPS00122. CARBOXYLESTERASE_B_1. Partial match.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACES_CULQU
AccessionPrimary (citable) accession number: Q867X2
Secondary accession number(s): Q867X1, Q867X4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 47 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