Reviewed,
UniProtKB/Swiss-Prot P07692 (ACES_TORMA)
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January 19, 2010.
Version 88.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Acetylcholinesterase Short name=AChE EC=3.1.1.7 | ||
| Gene names |
| ||
| Organism | Torpedo marmorata (Marbled electric ray) | ||
| Taxonomic identifier | 7788 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Pristiorajea › Batoidea › Torpediniformes › Torpedinoidei › Torpedinidae › Torpedo |
Protein attributes
| Sequence length | 590 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. May be involved in cell-cell interactions. |
| Catalytic activity | Acetylcholine + H2O = choline + acetate. |
| Subunit structure | Isoform H form is an homodimer; the asymmetric form is a disulfide-bonded oligomer composed of a collagenic subunit (Q) and a variable number of T catalytic subunits. Ref.4 Ref.5 |
| Subcellular location | Isoform H: Cell membrane; Lipid-anchor › GPI-anchor. Cell junction › synapse. Isoform T: Cell membrane; Peripheral membrane protein. Cell junction › synapse. Note: Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane. |
| Tissue specificity | Found in the synapses and to a lower extent in extrajunctional areas of muscle and nerve, and on erythrocyte membranes. |
| Post-translational modification | An interchain disulfide bond is present in what becomes position 596 of the T By similarity). |
| Sequence similarities | Belongs to the type-B carboxylesterase/lipase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Neurotransmitter degradation |
| Cellular component | Cell junction Cell membrane Membrane 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) | |
| Biological process | acetylcholine catabolic process in synaptic cleft Inferred from electronic annotation. Source: InterPro |
| Cellular component | anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell junctionInferred from electronic annotation. Source: UniProtKB-KW 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... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform H (identifier: P07692-1) Also known as: Globular; 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. | ||||||
| Note: GPI-anchored form. | ||||||
| Isoform T (identifier: P07692-2) The sequence of this isoform differs from the canonical sequence as follows: 560-590: ACDGELSSSGTSSSKGIIFYVLFSILYLIFY → ETIDEAERQWKTEFHRWSSYMMHWKNQFDQYSRHENCAEL | ||||||
| Note: Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane. | ||||||
| Isoform 3 (identifier: P07692-3) The sequence of this isoform differs from the canonical sequence as follows: 560-590: ACDGELSSSGTSSSKGIIFYVLFSILYLIFY → GNVFAFHMQK...RCWESWGRIL |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | Ref.2 | ||||||||
| Chain | 25 – 567 | 543 | Acetylcholinesterase | PRO_0000008597 | |||||||
| Propeptide | 568 – 590 | 23 | Removed in mature form | PRO_0000008598 | |||||||
Sites | |||||||||||
| Active site | 224 | 1 | Acyl-ester intermediate By similarity | ||||||||
| Active site | 351 | 1 | Charge relay system By similarity | ||||||||
| Active site | 464 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Lipidation | 567 | 1 | GPI-anchor amidated serine | ||||||||
| Glycosylation | 83 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 440 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 481 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 557 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 91 ↔ 118 | By similarity | |||||||||
| Disulfide bond | 278 ↔ 289 | By similarity | |||||||||
| Disulfide bond | 426 ↔ 545 | By similarity | |||||||||
| Disulfide bond | 561 | Interchain | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 560 – 590 | 31 | ACDGE…YLIFY → GNVFAFHMQKVRTPAKTYHF GVIVAHLLLLSLPTASDVPR LASSKWWAHSDPLCSRRCWE SWGRIL in isoform 3. | VSP_001462 | |||||||
| Alternative sequence | 560 – 590 | 31 | ACDGE…YLIFY → ETIDEAERQWKTEFHRWSSY MMHWKNQFDQYSRHENCAEL in isoform T. | VSP_001461 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 41 | 1 | R → G AA sequence Ref.2 | ||||||||
Sequences
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References
| [1] | "cDNA sequences of Torpedo marmorata acetylcholinesterase: primary structure of the precursor of a catalytic subunit; existence of multiple 5'-untranslated regions." Sikorav J.-L., Krejci E., Massoulie J. EMBO J. 6:1865-1873(1987) [PubMed: 2820709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Electric organ. |
| [2] | "Identical N-terminal peptide sequences of asymmetric forms and of low-salt-soluble and detergent-soluble amphiphilic dimers of Torpedo acetylcholinesterase. Comparison with bovine acetylcholinesterase." Bon S., Chang J.Y., Strosberg A.D. FEBS Lett. 209:206-212(1986) [PubMed: 3792544] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-47. |
| [3] | "Complex alternative splicing of acetylcholinesterase transcripts in Torpedo electric organ; primary structure of the precursor of the glycolipid-anchored dimeric form." Sikorav J.-L., Duval N., Anselmet A., Bon S., Krejci E., Legay C., Osterlund M., Reimund B., Massoulie J. EMBO J. 7:2983-2993(1988) [PubMed: 3181125] [Abstract] Cited for: ALTERNATIVE SPLICING. Tissue: Electric organ. |
| [4] | "Molecular architecture of acetylcholinesterase collagen-tailed forms; construction of a glycolipid-tailed tetramer." Duval N., Krejci E., Grassi J., Coussen F., Massoulie J., Bon S. EMBO J. 11:3255-3261(1992) [PubMed: 1380451] [Abstract] Cited for: SUBUNITS INTERACTION. Tissue: Electric organ. |
| [5] | "H and T subunits of acetylcholinesterase from Torpedo, expressed in COS cells, generate all types of globular forms." Duval N., Massoulie J., Bon S. J. Cell Biol. 118:641-653(1992) [PubMed: 1639848] [Abstract] Cited for: SUBUNITS INTERACTION, SEQUENCE REVISION TO 421. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X05497 mRNA. Translation: CAA29047.1. X13172 mRNA. Translation: CAA31570.1. X13174 mRNA. Translation: CAA31572.1. X13173 mRNA. Translation: CAA31571.1. |
| PIR | A38868. S01293. |
3D structure databases | |
| SMR | P07692. Positions 28-560. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S09.979. |
Phylogenomic databases | |
| HOVERGEN | P07692. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.7. 39087. |
Family and domain databases | |
| InterPro | IPR000908. Acylcholinesterase_fish/snake. IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. IPR019819. Carboxylesterase_B_CS. IPR000997. Cholinesterase. [Graphical view] |
| PANTHER | PTHR11559. CarbesteraseB. 1 hit. |
| Pfam | PF00135. COesterase. 1 hit. [Graphical view] |
| PRINTS | PR00879. ACHEFISH. PR00878. CHOLNESTRASE. |
| PROSITE | PS00122. CARBOXYLESTERASE_B_1. 1 hit. PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACES_TORMA | ||||||||
| Accession | Primary (citable) accession number: P07692 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
