Human Gene ACHE (ENST00000428317.7) Description and Page Index
Description: Homo sapiens acetylcholinesterase (Cartwright blood group) (ACHE), transcript variant 5, mRNA. (from RefSeq NM_001302622) RefSeq Summary (NM_001302622): Acetylcholinesterase hydrolyzes the neurotransmitter, acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. It is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. Acetylcholinesterase exists in multiple molecular forms which possess similar catalytic properties, but differ in their oligomeric assembly and mode of cell attachment to the cell surface. It is encoded by the single ACHE gene, and the structural diversity in the gene products arises from alternative mRNA splicing, and post-translational associations of catalytic and structural subunits. The major form of acetylcholinesterase found in brain, muscle and other tissues is the hydrophilic species, which forms disulfide-linked oligomers with collagenous, or lipid-containing structural subunits. The other, alternatively spliced form, expressed primarily in the erythroid tissues, differs at the C-terminal end, and contains a cleavable hydrophobic peptide with a GPI-anchor site. It associates with the membranes through the phosphoinositide (PI) moieties added post-translationally. AChE activity may constitute a sensitive biomarker of RBC ageing in vivo, and thus, may be of aid in understanding the effects of transfusion[provided by RefSeq, Sep 2019]. Gencode Transcript: ENST00000428317.7 Gencode Gene: ENSG00000087085.15 Transcript (Including UTRs) Position: hg38 chr7:100,889,994-100,896,129 Size: 6,136 Total Exon Count: 5 Strand: - Coding Region Position: hg38 chr7:100,890,214-100,894,232 Size: 4,019 Coding Exon Count: 4
ID:ACES_HUMAN DESCRIPTION: RecName: Full=Acetylcholinesterase; Short=AChE; EC=18.104.22.168; Flags: Precursor; FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis. CATALYTIC ACTIVITY: Acetylcholine + H(2)O = choline + acetate. SUBUNIT: 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. Isoform R may be monomeric. INTERACTION: Q9Y215:COLQ; NbExp=2; IntAct=EBI-1637793, EBI-1637847; P06733:ENO1; NbExp=2; IntAct=EBI-1637793, EBI-353877; P63244:GNB2L1; NbExp=2; IntAct=EBI-1637793, EBI-296739; SUBCELLULAR LOCATION: Cell junction, synapse. Secreted (By similarity). Cell membrane; Peripheral membrane protein (By similarity). SUBCELLULAR LOCATION: Isoform T: Nucleus. Note=Only observed in apoptotic nuclei. SUBCELLULAR LOCATION: Isoform H: Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side (By similarity). TISSUE SPECIFICITY: Isoform H is highly expressed in erythrocytes. POLYMORPHISM: ACHE is responsible for the Yt blood group system [MIM:112100]. The molecular basis of the Yt(a)=Yt1/Yt(b)=Yt2 blood group antigens is a single variation in position 353; His-353 corresponds to Yt(a) and the rare variant with Asn-353 to Yt(b). SIMILARITY: Belongs to the type-B carboxylesterase/lipase family. WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation database; URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=yt"; WEB RESOURCE: Name=Wikipedia; Note=Acetylcholinesterase entry; URL="http://en.wikipedia.org/wiki/Acetylcholinesterase"; WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/ache/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P22303
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.