O62763 (ACES_FELCA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 78.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Acetylcholinesterase Short name=AChE EC=3.1.1.7 | ||
| 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 | 611 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. |
| Catalytic activity | Acetylcholine + H2O = choline + acetate. |
| Subunit structure | Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers By similarity. Isoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers. |
| Subcellular location | Cell junction › synapse. Secreted. Cell membrane; Peripheral membrane protein By similarity. Isoform H: Cell membrane; Lipid-anchor › GPI-anchor; Extracellular side. |
| Sequence similarities | Belongs to the type-B carboxylesterase/lipase family. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform T (identifier: O62763-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform H (identifier: O62763-2) The sequence of this isoform differs from the canonical sequence as follows: 572-611: DTLDEAERQW...YSKQDRCSDL → ASKAPSTCSG...FLLLSRLLRL |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 31 | 31 | By similarity | ||||||||
| Chain | 32 – 611 | 580 | Acetylcholinesterase | PRO_0000008586 | |||||||
Sites | |||||||||||
| Active site | 231 | 1 | Acyl-ester intermediate By similarity | ||||||||
| Active site | 362 | 1 | Charge relay system By similarity | ||||||||
| Active site | 475 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 293 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 378 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 492 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 97 ↔ 124 | By similarity | |||||||||
| Disulfide bond | 285 ↔ 300 | By similarity | |||||||||
| Disulfide bond | 437 ↔ 557 | By similarity | |||||||||
| Disulfide bond | 608 | Interchain By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 572 – 611 | 40 | DTLDE…RCSDL → ASKAPSTCSGPAHGEAAPRP RPGLSLPLLLLLFLLLSRLL RL in isoform H. | VSP_001456 | |||||||
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 [GENOMIC DNA] (ISOFORMS H AND T). |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF053485 Genomic DNA. Translation: AAC08995.1. AF053485 Genomic DNA. Translation: AAC08996.1. |
| RefSeq | NP_001009203.1. NM_001009203.1. |
3D structure databases | |
| ProteinModelPortal | O62763. |
| SMR | O62763. Positions 33-605. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S09.979. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 493674. |
| KEGG | fca:493674. |
Organism-specific databases | |
| CTD | 43. |
Phylogenomic databases | |
| eggNOG | COG2272. |
| HOVERGEN | HBG008839. |
| KO | K01049. |
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 | ACES_FELCA | ||||||||
| Accession | Primary (citable) accession number: O62763 Secondary accession number(s): O62762 | ||||||||
| 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 |