ACES_MOUSE
ID ACES_MOUSE Reviewed; 614 AA.
AC P21836;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Acetylcholinesterase;
DE Short=AChE;
DE EC=3.1.1.7;
DE Flags: Precursor;
GN Name=Ache;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2400605; DOI=10.1016/0896-6273(90)90168-f;
RA Rachinsky T.L., Camp S., Li Y., Ekstroem T.J., Newton M., Taylor P.;
RT "Molecular cloning of mouse acetylcholinesterase: tissue distribution of
RT alternatively spliced mRNA species.";
RL Neuron 5:317-327(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH PRIMA1.
RX PubMed=11804574; DOI=10.1016/s0896-6273(01)00584-0;
RA Perrier A.L., Massoulie J., Krejci E.;
RT "PRiMA: the membrane anchor of acetylcholinesterase in the brain.";
RL Neuron 33:275-285(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH FASCICULIN-2, AND
RP DISULFIDE BOND.
RX PubMed=8521480; DOI=10.1016/0092-8674(95)90128-0;
RA Bourne Y., Taylor P., Marchot P.;
RT "Acetylcholinesterase inhibition by fasciculin: crystal structure of the
RT complex.";
RL Cell 83:503-512(1995).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=9915834; DOI=10.1074/jbc.274.5.2963;
RA Bourne Y., Taylor P., Bougis P.E., Marchot P.;
RT "Crystal structure of mouse acetylcholinesterase. A peripheral site-
RT occluding loop in a tetrameric assembly.";
RL J. Biol. Chem. 274:2963-2970(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 34-573 IN COMPLEX WITH INHIBITOR.
RX PubMed=12505979; DOI=10.1093/emboj/cdg005;
RA Bourne Y., Taylor P., Radic Z., Marchot P.;
RT "Structural insights into ligand interactions at the acetylcholinesterase
RT peripheral anionic site.";
RL EMBO J. 22:1-12(2003).
CC -!- FUNCTION: Terminates signal transduction at the neuromuscular junction
CC by rapid hydrolysis of the acetylcholine released into the synaptic
CC cleft.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetylcholine + H2O = acetate + choline + H(+);
CC Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7;
CC -!- SUBUNIT: Isoform H generates GPI-anchored dimers; disulfide linked.
CC Isoform T generates multiple structures, ranging from monomers and
CC dimers to collagen-tailed and hydrophobic-tailed forms, in which
CC catalytic tetramers are associated with anchoring proteins that attach
CC them to the basal lamina or to cell membranes. In the collagen-tailed
CC forms, isoform T subunits are associated with a specific collagen,
CC COLQ, which triggers the formation of isoform T tetramers, from
CC monomers and dimers (By similarity). Interacts with PRIMA1. The
CC interaction with PRIMA1 is required to anchor it to the basal lamina of
CC cells and organize into tetramers. {ECO:0000250,
CC ECO:0000269|PubMed:11804574, ECO:0000269|PubMed:12505979}.
CC -!- SUBCELLULAR LOCATION: Synapse. Secreted. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform H]: Cell membrane; Lipid-anchor, GPI-
CC anchor; Extracellular side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=T;
CC IsoId=P21836-1; Sequence=Displayed;
CC Name=H;
CC IsoId=P21836-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Predominates in most expressing tissues except
CC erythrocytes where a glycophospholipid-attached form of ACHE
CC predominates.
CC -!- MISCELLANEOUS: Synapses usually contain asymmetric molecules of
CC cholinesterase, with a collagen-like part disulfide-bonded to the
CC catalytic part. A different, globular type of cholinesterase occurs on
CC the outer surfaces of cell membranes, including those of erythrocytes.
CC -!- MISCELLANEOUS: This is the catalytic subunit of an asymmetric or
CC soluble form of ACHE.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; X56518; CAA39867.1; -; mRNA.
DR EMBL; AF312033; AAK28816.1; -; Genomic_DNA.
DR EMBL; BC046327; AAH46327.1; -; mRNA.
DR CCDS; CCDS19763.1; -. [P21836-1]
DR PIR; JH0314; JH0314.
DR RefSeq; NP_001276939.1; NM_001290010.1. [P21836-1]
DR RefSeq; NP_033729.1; NM_009599.4. [P21836-1]
DR PDB; 1C2B; X-ray; 4.50 A; A=35-574.
DR PDB; 1C2O; X-ray; 4.20 A; A/B/C/D=36-574.
DR PDB; 1J06; X-ray; 2.35 A; A/B=32-574.
DR PDB; 1J07; X-ray; 2.35 A; A/B=32-574.
DR PDB; 1KU6; X-ray; 2.50 A; A=32-580.
DR PDB; 1MAA; X-ray; 2.90 A; A/B/C/D=32-578.
DR PDB; 1MAH; X-ray; 3.20 A; A=32-574.
DR PDB; 1N5M; X-ray; 2.20 A; A/B=32-572.
DR PDB; 1N5R; X-ray; 2.25 A; A/B=32-574.
DR PDB; 1Q83; X-ray; 2.65 A; A/B=1-580.
DR PDB; 1Q84; X-ray; 2.45 A; A/B=1-580.
DR PDB; 2C0P; X-ray; 2.50 A; A/B=32-574.
DR PDB; 2C0Q; X-ray; 2.50 A; A/B=32-574.
DR PDB; 2GYU; X-ray; 2.20 A; A/B=32-574.
DR PDB; 2GYV; X-ray; 2.50 A; A/B=32-574.
DR PDB; 2GYW; X-ray; 2.40 A; A/B=32-574.
DR PDB; 2H9Y; X-ray; 2.40 A; A/B=32-574.
DR PDB; 2HA0; X-ray; 2.20 A; A/B=32-574.
DR PDB; 2HA2; X-ray; 2.05 A; A/B=32-574.
DR PDB; 2HA3; X-ray; 2.25 A; A/B=32-574.
DR PDB; 2HA4; X-ray; 2.56 A; A/B=32-574.
DR PDB; 2HA5; X-ray; 2.15 A; A/B=32-574.
DR PDB; 2HA6; X-ray; 2.25 A; A/B=32-574.
DR PDB; 2HA7; X-ray; 2.66 A; A/B=32-574.
DR PDB; 2JEY; X-ray; 2.70 A; A/B=32-574.
DR PDB; 2JEZ; X-ray; 2.60 A; A/B=32-574.
DR PDB; 2JF0; X-ray; 2.50 A; A/B=32-574.
DR PDB; 2JGE; X-ray; 2.60 A; A/B=32-574.
DR PDB; 2JGF; X-ray; 2.50 A; A/B=32-574.
DR PDB; 2JGI; X-ray; 2.90 A; A/B=32-574.
DR PDB; 2JGJ; X-ray; 2.50 A; A/B=32-574.
DR PDB; 2JGK; X-ray; 2.90 A; A/B=32-574.
DR PDB; 2JGL; X-ray; 2.60 A; A/B=32-574.
DR PDB; 2JGM; X-ray; 2.90 A; A/B=32-574.
DR PDB; 2WHP; X-ray; 2.20 A; A/B=32-573.
DR PDB; 2WHQ; X-ray; 2.15 A; A/B=32-574.
DR PDB; 2WHR; X-ray; 2.54 A; A/B=32-574.
DR PDB; 2WLS; X-ray; 2.60 A; A/B=32-574.
DR PDB; 2WU3; X-ray; 2.70 A; A/B=32-574.
DR PDB; 2WU4; X-ray; 2.40 A; A/B=32-574.
DR PDB; 2XUD; X-ray; 2.65 A; A/B=32-574.
DR PDB; 2XUF; X-ray; 2.55 A; A/B=32-575.
DR PDB; 2XUG; X-ray; 2.60 A; A/B=32-575.
DR PDB; 2XUH; X-ray; 2.65 A; A/B=32-574.
DR PDB; 2XUI; X-ray; 2.60 A; A/B=32-574.
DR PDB; 2XUJ; X-ray; 2.65 A; A/B=32-574.
DR PDB; 2XUK; X-ray; 2.75 A; A/B=32-574.
DR PDB; 2XUO; X-ray; 2.80 A; A/B=32-574.
DR PDB; 2XUP; X-ray; 2.70 A; A/B=32-574.
DR PDB; 2XUQ; X-ray; 2.70 A; A/B=32-574.
DR PDB; 2Y2U; X-ray; 2.60 A; A/B=32-574.
DR PDB; 2Y2V; X-ray; 2.45 A; A/B=32-574.
DR PDB; 3DL4; X-ray; 2.50 A; A/B=32-574.
DR PDB; 3DL7; X-ray; 2.50 A; A/B=32-574.
DR PDB; 3ZLT; X-ray; 2.60 A; A/B=32-574.
DR PDB; 3ZLU; X-ray; 2.60 A; A/B=32-574.
DR PDB; 3ZLV; X-ray; 2.50 A; A/B=32-574.
DR PDB; 4A16; X-ray; 2.65 A; A/B/C/D=35-574.
DR PDB; 4A23; X-ray; 2.40 A; A/B=32-574.
DR PDB; 4ARA; X-ray; 2.50 A; A/B=32-574.
DR PDB; 4ARB; X-ray; 2.25 A; A/B=32-574.
DR PDB; 4B7Z; X-ray; 2.30 A; A/B=32-574.
DR PDB; 4B80; X-ray; 2.50 A; A/B=32-574.
DR PDB; 4B81; X-ray; 2.80 A; A/B=32-574.
DR PDB; 4B82; X-ray; 2.10 A; A/B=32-574.
DR PDB; 4B83; X-ray; 2.40 A; A/B=32-574.
DR PDB; 4B84; X-ray; 2.60 A; A/B=32-574.
DR PDB; 4B85; X-ray; 2.10 A; A/B=32-574.
DR PDB; 4BC0; X-ray; 3.35 A; A/B/C/D=32-574.
DR PDB; 4BC1; X-ray; 2.95 A; A/B/C/D=32-574.
DR PDB; 4BTL; X-ray; 2.50 A; A/B=32-574.
DR PDB; 5DTI; X-ray; 2.00 A; A/B=32-573.
DR PDB; 5DTJ; X-ray; 2.71 A; A/B=32-573.
DR PDB; 5EHN; X-ray; 2.60 A; A/B=32-574.
DR PDB; 5EHQ; X-ray; 2.50 A; A/B=32-574.
DR PDB; 5EHZ; X-ray; 2.50 A; A/B=32-574.
DR PDB; 5EIA; X-ray; 2.70 A; A/B=32-574.
DR PDB; 5EIE; X-ray; 2.10 A; A/B=32-574.
DR PDB; 5EIH; X-ray; 2.70 A; A/B=32-574.
DR PDB; 5FKJ; X-ray; 3.13 A; A/B/C/D=32-574.
DR PDB; 5FPP; X-ray; 2.40 A; A/B=32-574.
DR PDB; 5FUM; X-ray; 2.50 A; A/B=32-574.
DR PDB; 5HCU; X-ray; 2.42 A; A/B=32-571.
DR PDB; 5OV9; X-ray; 2.40 A; A/B=32-574.
DR PDB; 6FSD; X-ray; 2.70 A; A/B=32-574.
DR PDB; 6FSE; X-ray; 2.70 A; A/B=32-574.
DR PDB; 6TD2; X-ray; 2.80 A; A/B=32-574.
DR PDB; 7QAK; X-ray; 2.60 A; A/B=32-574.
DR PDB; 7QB4; X-ray; 2.50 A; A/B=32-574.
DR PDBsum; 1C2B; -.
DR PDBsum; 1C2O; -.
DR PDBsum; 1J06; -.
DR PDBsum; 1J07; -.
DR PDBsum; 1KU6; -.
DR PDBsum; 1MAA; -.
DR PDBsum; 1MAH; -.
DR PDBsum; 1N5M; -.
DR PDBsum; 1N5R; -.
DR PDBsum; 1Q83; -.
DR PDBsum; 1Q84; -.
DR PDBsum; 2C0P; -.
DR PDBsum; 2C0Q; -.
DR PDBsum; 2GYU; -.
DR PDBsum; 2GYV; -.
DR PDBsum; 2GYW; -.
DR PDBsum; 2H9Y; -.
DR PDBsum; 2HA0; -.
DR PDBsum; 2HA2; -.
DR PDBsum; 2HA3; -.
DR PDBsum; 2HA4; -.
DR PDBsum; 2HA5; -.
DR PDBsum; 2HA6; -.
DR PDBsum; 2HA7; -.
DR PDBsum; 2JEY; -.
DR PDBsum; 2JEZ; -.
DR PDBsum; 2JF0; -.
DR PDBsum; 2JGE; -.
DR PDBsum; 2JGF; -.
DR PDBsum; 2JGI; -.
DR PDBsum; 2JGJ; -.
DR PDBsum; 2JGK; -.
DR PDBsum; 2JGL; -.
DR PDBsum; 2JGM; -.
DR PDBsum; 2WHP; -.
DR PDBsum; 2WHQ; -.
DR PDBsum; 2WHR; -.
DR PDBsum; 2WLS; -.
DR PDBsum; 2WU3; -.
DR PDBsum; 2WU4; -.
DR PDBsum; 2XUD; -.
DR PDBsum; 2XUF; -.
DR PDBsum; 2XUG; -.
DR PDBsum; 2XUH; -.
DR PDBsum; 2XUI; -.
DR PDBsum; 2XUJ; -.
DR PDBsum; 2XUK; -.
DR PDBsum; 2XUO; -.
DR PDBsum; 2XUP; -.
DR PDBsum; 2XUQ; -.
DR PDBsum; 2Y2U; -.
DR PDBsum; 2Y2V; -.
DR PDBsum; 3DL4; -.
DR PDBsum; 3DL7; -.
DR PDBsum; 3ZLT; -.
DR PDBsum; 3ZLU; -.
DR PDBsum; 3ZLV; -.
DR PDBsum; 4A16; -.
DR PDBsum; 4A23; -.
DR PDBsum; 4ARA; -.
DR PDBsum; 4ARB; -.
DR PDBsum; 4B7Z; -.
DR PDBsum; 4B80; -.
DR PDBsum; 4B81; -.
DR PDBsum; 4B82; -.
DR PDBsum; 4B83; -.
DR PDBsum; 4B84; -.
DR PDBsum; 4B85; -.
DR PDBsum; 4BC0; -.
DR PDBsum; 4BC1; -.
DR PDBsum; 4BTL; -.
DR PDBsum; 5DTI; -.
DR PDBsum; 5DTJ; -.
DR PDBsum; 5EHN; -.
DR PDBsum; 5EHQ; -.
DR PDBsum; 5EHZ; -.
DR PDBsum; 5EIA; -.
DR PDBsum; 5EIE; -.
DR PDBsum; 5EIH; -.
DR PDBsum; 5FKJ; -.
DR PDBsum; 5FPP; -.
DR PDBsum; 5FUM; -.
DR PDBsum; 5HCU; -.
DR PDBsum; 5OV9; -.
DR PDBsum; 6FSD; -.
DR PDBsum; 6FSE; -.
DR PDBsum; 6TD2; -.
DR PDBsum; 7QAK; -.
DR PDBsum; 7QB4; -.
DR AlphaFoldDB; P21836; -.
DR SMR; P21836; -.
DR BioGRID; 197921; 3.
DR IntAct; P21836; 1.
DR MINT; P21836; -.
DR STRING; 10090.ENSMUSP00000024099; -.
DR BindingDB; P21836; -.
DR ChEMBL; CHEMBL3198; -.
DR DrugCentral; P21836; -.
DR ESTHER; mouse-ACHE; AChE.
DR MEROPS; S09.979; -.
DR GlyConnect; 2100; 2 N-Linked glycans (1 site).
DR GlyGen; P21836; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P21836; -.
DR PhosphoSitePlus; P21836; -.
DR SwissPalm; P21836; -.
DR PaxDb; P21836; -.
DR PRIDE; P21836; -.
DR ProteomicsDB; 285642; -. [P21836-1]
DR Antibodypedia; 16701; 766 antibodies from 43 providers.
DR DNASU; 11423; -.
DR Ensembl; ENSMUST00000024099; ENSMUSP00000024099; ENSMUSG00000023328. [P21836-1]
DR Ensembl; ENSMUST00000085934; ENSMUSP00000083097; ENSMUSG00000023328. [P21836-1]
DR GeneID; 11423; -.
DR KEGG; mmu:11423; -.
DR UCSC; uc009abt.1; mouse. [P21836-1]
DR CTD; 43; -.
DR MGI; MGI:87876; Ache.
DR VEuPathDB; HostDB:ENSMUSG00000023328; -.
DR eggNOG; KOG4389; Eukaryota.
DR GeneTree; ENSGT00940000157637; -.
DR InParanoid; P21836; -.
DR OMA; CDHLVAP; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P21836; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.7; 3474.
DR SABIO-RK; P21836; -.
DR BioGRID-ORCS; 11423; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Ache; mouse.
DR EvolutionaryTrace; P21836; -.
DR PRO; PR:P21836; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P21836; protein.
DR Bgee; ENSMUSG00000023328; Expressed in medulla oblongata and 105 other tissues.
DR ExpressionAtlas; P21836; baseline and differential.
DR Genevisible; P21836; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; ISO:MGI.
DR GO; GO:0042166; F:acetylcholine binding; ISO:MGI.
DR GO; GO:0003990; F:acetylcholinesterase activity; IDA:MGI.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0033265; F:choline binding; ISO:MGI.
DR GO; GO:0004104; F:cholinesterase activity; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0016787; F:hydrolase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0043236; F:laminin binding; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; IPI:MGI.
DR GO; GO:0017171; F:serine hydrolase activity; ISO:MGI.
DR GO; GO:0006581; P:acetylcholine catabolic process; IDA:MGI.
DR GO; GO:0008291; P:acetylcholine metabolic process; ISO:MGI.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0019695; P:choline metabolic process; ISO:MGI.
DR GO; GO:0070997; P:neuron death; ISO:MGI.
DR GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; IMP:MGI.
DR GO; GO:0001919; P:regulation of receptor recycling; IMP:MGI.
DR GO; GO:0046677; P:response to antibiotic; ISO:MGI.
DR GO; GO:0032868; P:response to insulin; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0007416; P:synapse assembly; ISO:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR014788; AChE_tetra.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000997; Cholinesterase.
DR Pfam; PF08674; AChE_tetra; 1.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR00878; CHOLNESTRASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Neurotransmitter degradation; Reference proteome; Secreted;
KW Serine esterase; Signal; Synapse.
FT SIGNAL 1..31
FT CHAIN 32..614
FT /note="Acetylcholinesterase"
FT /id="PRO_0000008588"
FT ACT_SITE 234
FT /note="Acyl-ester intermediate"
FT ACT_SITE 365
FT /note="Charge relay system"
FT ACT_SITE 478
FT /note="Charge relay system"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 100..127
FT DISULFID 288..303
FT DISULFID 440..560
FT DISULFID 611
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:5DTI"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:5EHZ"
FT HELIX 202..217
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:5DTI"
FT TURN 286..290
FT /evidence="ECO:0007829|PDB:4A16"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:4A16"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 309..315
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:5DTI"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:5EIE"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:5DTI"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:1KU6"
FT HELIX 422..437
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 439..451
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:5DTI"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 498..517
FT /evidence="ECO:0007829|PDB:5DTI"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:4ARB"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:4B82"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 540..547
FT /evidence="ECO:0007829|PDB:5DTI"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 557..564
FT /evidence="ECO:0007829|PDB:5DTI"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:5DTI"
SQ SEQUENCE 614 AA; 68169 MW; 66E2512463C21172 CRC64;
MRPPWYPLHT PSLAFPLLFL LLSLLGGGAR AEGREDPQLL VRVRGGQLRG IRLKAPGGPV
SAFLGIPFAE PPVGSRRFMP PEPKRPWSGV LDATTFQNVC YQYVDTLYPG FEGTEMWNPN
RELSEDCLYL NVWTPYPRPA SPTPVLIWIY GGGFYSGAAS LDVYDGRFLA QVEGAVLVSM
NYRVGTFGFL ALPGSREAPG NVGLLDQRLA LQWVQENIAA FGGDPMSVTL FGESAGAASV
GMHILSLPSR SLFHRAVLQS GTPNGPWATV SAGEARRRAT LLARLVGCPP GGAGGNDTEL
IACLRTRPAQ DLVDHEWHVL PQESIFRFSF VPVVDGDFLS DTPEALINTG DFQDLQVLVG
VVKDEGSYFL VYGVPGFSKD NESLISRAQF LAGVRIGVPQ ASDLAAEAVV LHYTDWLHPE
DPTHLRDAMS AVVGDHNVVC PVAQLAGRLA AQGARVYAYI FEHRASTLTW PLWMGVPHGY
EIEFIFGLPL DPSLNYTTEE RIFAQRLMKY WTNFARTGDP NDPRDSKSPQ WPPYTTAAQQ
YVSLNLKPLE VRRGLRAQTC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN
QFDHYSKQER CSDL
