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Q867X3 (ACES_CULPP) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 45. 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 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. 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: 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_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: 12736674] [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...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_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: October 19, 2011
This is version 45 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