Reviewed,
UniProtKB/Swiss-Prot Q867X2 (ACES_CULQU)
Last modified
January 19, 2010.
Version 39.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acetylcholinesterase Short name=AChE EC=3.1.1.7 | ||
| Gene names |
| ||
| Organism | Culex quinquefasciatus (Southern house mosquito) (Culex pungens) | ||
| Taxonomic identifier | 7176 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Culicinae › Culicini › Culex › Culex |
Protein attributes
| Sequence length | 132 AA. |
| Sequence status | Fragment. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Rapidly hydrolyzes choline released into the synapse. |
| Catalytic activity | Acetylcholine + H2O = choline + acetate. Ref.1 |
| Subcellular location | Cell junction › synapse 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 process | Neurotransmitter degradation |
| Cellular component | Cell junction Cell membrane Membrane Secreted Synapse |
| Coding sequence diversity | Polymorphism |
| Molecular function | Hydrolase Serine esterase |
| PTM | Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | neurotransmitter catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cell junction Inferred from electronic annotation. Source: UniProtKB-KW extracellular regionInferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membraneInferred from electronic annotation. Source: UniProtKB-SubCell synapseInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acetylcholinesterase activity Inferred from electronic annotation. Source: EC cholinesterase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›132 | ›132 | Acetylcholinesterase | PRO_0000070281 | |||||||
Amino acid modifications | |||||||||||
| Glycosylation | 37 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 45 ↔ 72 | By similarity UniProtKB P22303 | |||||||||
Natural variations | |||||||||||
| Natural variant | 97 | 1 | G → S in strain: BO, DJI, Harare, Martinique, Recife, Supercar, TemR and Trans; confers resistance to insecticides. Ref.1 | ||||||||
| Natural variant | 114 | 1 | A → T in strain: TemR and Trans. Ref.1 | ||||||||
Experimental info | |||||||||||
| Non-terminal residue | 1 | 1 | |||||||||
| Non-terminal residue | 132 | 1 | |||||||||
Sequences
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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 | |
| SMR | Q867X2. Positions 2-132. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S09.979. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.7. 118756. |
Family and domain databases | |
| InterPro | IPR002018. CarbesteraseB. IPR019819. Carboxylesterase_B_CS. IPR000997. Cholinesterase. [Graphical view] |
| PANTHER | PTHR11559. CarbesteraseB. 1 hit. |
| Pfam | PF00135. COesterase. 1 hit. [Graphical view] |
| PRINTS | PR00878. CHOLNESTRASE. |
| PROSITE | PS00122. CARBOXYLESTERASE_B_1. Partial match. PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACES_CULQU | ||||||||
| Accession | Primary (citable) accession number: Q867X2 Secondary accession number(s): Q867X1, Q867X4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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