Reviewed,
UniProtKB/Swiss-Prot Q867X3 (ACES_CULPP)
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 pipiens pipiens (Northern house mosquito) | ||
| Taxonomic identifier | 38569 [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. UniProtKB P22303 |
| 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_0000070280 | |||||||
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: Barriol, Espro, Padova and Praias. 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: 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 | |
| SMR | Q867X3. Positions 2-132. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.7. 293302. |
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_CULPP | ||||||||
| Accession | Primary (citable) accession number: Q867X3 Secondary accession number(s): Q867X5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with


