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Reviewed, UniProtKB/Swiss-Prot Q867X2 (ACES_CULQU)

Last modified October 13, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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.
Sequence processingThe displayed sequence is not processed.
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

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
Q867X2-1 [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

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

HSSPHSSP built from PDB template 1EA5 based on UniProtKB P04058.
ModBaseSearch...

Protein family/group databases

MEROPSS09.979.

Genome annotation databases

UCSCW09B12.1.1. c. elegans.

Enzyme and pathway databases

BRENDA3.1.1.7. 118756.

Family and domain databases

InterProIPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PANTHERPTHR11559. CarbesteraseB. 1 hit.
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: October 13, 2009
This is version 37 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents