[1]
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NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0896-6273(90)90168-F; PubMed=2400605 [NCBI, ExPASy, EBI, Israel, Japan]
Rachinsky T.L.,
Camp S.,
Li Y.,
Ekstroem T.J.,
Newton M.,
Taylor P.;
"Molecular cloning of mouse acetylcholinesterase: tissue distribution of alternatively spliced mRNA species.";
Neuron 5:317-327(1990).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
DOI=10.1093/nar/29.6.1352; PubMed=11239002 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson M.D.,
Riemer C.,
Martindale D.W.,
Schnupf P.,
Boright A.P.,
Cheung T.L.,
Hardy D.M.,
Schwartz S.,
Scherer S.W.,
Tsui L.-C.,
Miller W.,
Koop B.F.;
"Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5.";
Nucleic Acids Res. 29:1352-1365(2001).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Retina;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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INTERACTION WITH PRIMA1.
DOI=10.1016/S0896-6273(01)00584-0; PubMed=11804574 [NCBI, ExPASy, EBI, Israel, Japan]
Perrier A.L.,
Massoulie J.,
Krejci E.;
"PRiMA: the membrane anchor of acetylcholinesterase in the brain.";
Neuron 33:275-285(2002).
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[5]
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X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH FASCICULIN.
DOI=10.1016/0092-8674(95)90128-0; PubMed=8521480 [NCBI, ExPASy, EBI, Israel, Japan]
Bourne Y.,
Taylor P.,
Marchot P.;
"Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex.";
Cell 83:503-512(1995).
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[6]
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X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
DOI=10.1074/jbc.274.5.2963; PubMed=9915834 [NCBI, ExPASy, EBI, Israel, Japan]
Bourne Y.,
Taylor P.,
Bougis P.E.,
Marchot P.;
"Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly.";
J. Biol. Chem. 274:2963-2970(1999).
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[7]
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X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 34-573 IN COMPLEX WITH INHIBITOR.
DOI=10.1093/emboj/cdg005; PubMed=12505979 [NCBI, ExPASy, EBI, Israel, Japan]
Bourne Y.,
Taylor P.,
Radic Z.,
Marchot P.;
"Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site.";
EMBO J. 22:1-12(2003).
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- 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: 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 (By similarity). Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers.
- SUBCELLULAR LOCATION: Cell junction, synapse. Secreted. Cell membrane; Peripheral membrane protein (By similarity).
- SUBCELLULAR LOCATION: Isoform H: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
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| Name | H |
| Isoform ID | P21836-2 |
| Note: No experimental confirmation available. |
| The sequence of this isoform is not described. |
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- TISSUE SPECIFICITY: Predominates in most expressing tissues except erythrocytes where a glycophospholipid-attached form of ACHE predominates.
- MISCELLANEOUS: Synapses usually contain asymmetric molecules of cholinesterase, with a collagen-like part disulfide-bonded to the catalytic part. A different, globular type of cholinesterase occurs on the outer surfaces of cell membranes, including those of erythrocytes.
- MISCELLANEOUS: This is the catalytic subunit of an asymmetric or soluble form of ACHE.
- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
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