O62760 (CHLE_FELCA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 70.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cholinesterase EC=3.1.1.8 Alternative name(s): Acylcholine acylhydrolase Butyrylcholine esterase Choline esterase II Pseudocholinesterase | ||
| Gene names |
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| Organism | Felis catus (Cat) (Felis silvestris catus) [Complete proteome] | ||
| Taxonomic identifier | 9685 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis![]() |
Protein attributes
| Sequence length | 602 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters By similarity. |
| Catalytic activity | An acylcholine + H2O = choline + a carboxylate. |
| Subunit structure | Homotetramer; disulfide-linked. Dimer of dimers By similarity. |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the type-B carboxylesterase/lipase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase Serine esterase |
| PTM | Disulfide bond Glycoprotein Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Cellular_component | endoplasmic reticulum Inferred from electronic annotation. Source: Compara extracellular regionInferred from electronic annotation. Source: UniProtKB-SubCell membraneInferred from electronic annotation. Source: InterPro nuclear envelope lumenInferred from electronic annotation. Source: Compara |
| Molecular_function | acetylcholinesterase activity Inferred from sequence or structural similarity. Source: UniProtKB carboxylesterase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 28 | 28 | Potential | ||||||||
| Chain | 29 – 602 | 574 | Cholinesterase | PRO_0000008612 | |||||||
Regions | |||||||||||
| Region | 144 – 145 | 2 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 226 | 1 | Acyl-ester intermediate By similarity | ||||||||
| Active site | 353 | 1 | Charge relay system By similarity | ||||||||
| Active site | 466 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 226 | 1 | Phosphoserine By similarity | ||||||||
| Glycosylation | 85 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 134 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 269 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 284 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 369 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 483 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 509 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 513 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 514 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 93 ↔ 120 | By similarity | |||||||||
| Disulfide bond | 280 ↔ 291 | By similarity | |||||||||
| Disulfide bond | 428 ↔ 547 | By similarity | |||||||||
| Disulfide bond | 599 | Interchain By similarity | |||||||||
Sequences
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References
| [1] | "Determination of the DNA sequences of acetylcholinesterase and butyrylcholinesterase from cat and demonstration of the existence of both in cat plasma." Bartels C.F., Xie W., Miller-Lindholm A.K., Schopfer L.M., Lockridge O. Biochem. Pharmacol. 60:479-487(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pituitary. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF053483 mRNA. Translation: AAC06261.1. |
| RefSeq | NP_001009364.1. NM_001009364.1. |
3D structure databases | |
| ProteinModelPortal | O62760. |
| SMR | O62760. Positions 32-562, 564-593. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S09.980. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 493960. |
| KEGG | fca:493960. |
Organism-specific databases | |
| CTD | 590. |
Phylogenomic databases | |
| GeneTree | ENSGT00700000104419. |
| HOVERGEN | HBG008839. |
| KO | K01050. |
Family and domain databases | |
| InterPro | IPR014788. AChE_tetra. IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. IPR019819. Carboxylesterase_B_CS. IPR000997. Cholinesterase. [Graphical view] |
| Pfam | PF08674. AChE_tetra. 1 hit. PF00135. COesterase. 1 hit. [Graphical view] |
| PRINTS | PR00878. CHOLNESTRASE. |
| ProDom | PD415333. AChE_tetra. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00122. CARBOXYLESTERASE_B_1. 1 hit. PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CHLE_FELCA | ||||||||
| Accession | Primary (citable) accession number: O62760 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
