P23795 (ACES_BOVIN)
Reviewed,
UniProtKB/Swiss-Prot
Last modified
August 10, 2010.
Version 79.
History...
Names and origin
| Protein names | Recommended name: Acetylcholinesterase Short name=AChE EC=3.1.1.7 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 613 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
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
| Keywords | |
|---|---|
| Biological process | Neurotransmitter degradation |
| Cellular component | Cell junction Cell membrane Membrane Secreted Synapse |
| Coding sequence diversity | Alternative splicing |
| Domain | Signal |
| Molecular function | Hydrolase Serine esterase |
| PTM | Disulfide bond GPI-anchor Glycoprotein Lipoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cell junctionInferred from electronic annotation. Source: UniProtKB-KW synapseInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acetylcholinesterase activity Inferred from electronic annotation. Source: EC beta-amyloid bindingInferred from direct assay. Source: HGNC cholinesterase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform T (identifier: P23795-1) 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: P23795-2) The sequence of this isoform differs from the canonical sequence as follows: 574-613: DTLDEAERQW...YSKQDRCSDL → ASEAPCTCSG...LFLLSRLLRL |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 30 | 30 | Ref.3 | ||||||||
| Chain | 31 – 613 | 583 | Acetylcholinesterase | PRO_0000008585 | |||||||
Sites | |||||||||||
| Active site | 233 | 1 | Acyl-ester intermediate By similarity | ||||||||
| Active site | 364 | 1 | Charge relay system By similarity | ||||||||
| Active site | 477 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 91 | 1 | N-linked (GlcNAc...) Probable | ||||||||
| Glycosylation | 295 | 1 | N-linked (GlcNAc...) Probable | ||||||||
| Glycosylation | 380 | 1 | N-linked (GlcNAc...) Probable | ||||||||
| Glycosylation | 494 | 1 | N-linked (GlcNAc...) Probable | ||||||||
| Disulfide bond | 99 ↔ 126 | By similarity | |||||||||
| Disulfide bond | 287 ↔ 302 | By similarity | |||||||||
| Disulfide bond | 439 ↔ 559 | By similarity | |||||||||
| Disulfide bond | 610 | Interchain By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 574 – 613 | 40 | DTLDE…RCSDL → ASEAPCTCSGPAHGEAAPRP RPGLPLPLLLLLFLLSRLLR L in isoform H. | VSP_001455 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 24 | 1 | I → L in AAI23899. Ref.2 | ||||||||
| Sequence conflict | 46 | 1 | R → E AA sequence Ref.3 | ||||||||
| Sequence conflict | 169 | 1 | T → V AA sequence Ref.3 | ||||||||
| Sequence conflict | 212 | 1 | W → S AA sequence Ref.3 | ||||||||
| Sequence conflict | 323 | 1 | S → H AA sequence Ref.3 | ||||||||
| Sequence conflict | 352 | 1 | H → V AA sequence Ref.3 | ||||||||
| Sequence conflict | 424 | 1 | L → W AA sequence Ref.3 | ||||||||
| Sequence conflict | 524 | 1 | D → A AA sequence Ref.3 | ||||||||
| Sequence conflict | 549 – 554 | 6 | EVRRGL → GVPQAS AA sequence Ref.3 | ||||||||
| Sequence conflict | 571 | 1 | S → N AA sequence Ref.3 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Bovine acetylcholinesterase: cloning, expression and characterization." Mendelson I., Kronman C., Ariel N., Shafferman A., Velan B. Biochem. J. 334:251-259(1998) [PubMed: 9693127] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Tissue: Kidney. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T). Strain: Hereford. Tissue: Basal ganglia. |
| [3] | "Complete amino acid sequence of fetal bovine serum acetylcholinesterase and its comparison in various regions with other cholinesterases." Doctor B.P., Chapman T.C., Christner C.E., Deal C.D., de la Hoz D.M., Gentry M.K., Ogert R.A., Rush R.S., Smyth K.K., Wolfe A.D. FEBS Lett. 266:123-127(1990) [PubMed: 2365060] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-613 (ISOFORM H). Tissue: Fetal serum. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF061815, AF061813, AF061814 Genomic DNA. Translation: AAC64270.1. BC123898 mRNA. Translation: AAI23899.1. |
| IPI | IPI00687338. IPI00711550. |
| RefSeq | NP_001069688.1. |
| UniGene | Bt.1299. |
3D structure databases | |
| ProteinModelPortal | P23795. |
| SMR | P23795. Positions 35-573, 574-607. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P23795. |
Protein family/group databases | |
| MEROPS | S09.979. |
PTM databases | |
| GlycoSuiteDB | P23795. |
Genome annotation databases | |
| Ensembl | ENSBTAT00000001512; ENSBTAP00000001512; ENSBTAG00000001139; Bos taurus. [Genome view] |
| GeneID | 540446. |
| KEGG | bta:540446. |
Organism-specific databases | |
| CTD | 540446. |
Phylogenomic databases | |
| eggNOG | maNOG13227. |
| HOVERGEN | HBG008839. |
| InParanoid | P23795. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.7. 251. |
Family and domain databases | |
| InterPro | IPR014788. AChE_tetra. IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. IPR019819. Carboxylesterase_B_CS. IPR000997. Cholinesterase. [Graphical view] |
| PANTHER | PTHR11559. CarbesteraseB. 1 hit. |
| 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_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P23795 Secondary accession number(s): O97579, Q08D79 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with


