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 24-JAN-2024, entry version 200. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7QYN; X-ray; 2.50 A; A/B=32-574. DR PDB; 7R02; X-ray; 2.30 A; A/B=32-574. DR PDB; 7R0A; X-ray; 2.80 A; A/B=32-574. DR PDB; 7R2F; X-ray; 2.30 A; A/B=32-574. DR PDB; 7R3C; X-ray; 2.40 A; A/B=32-574. DR PDB; 7R4E; X-ray; 3.00 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 PDBsum; 7QYN; -. DR PDBsum; 7R02; -. DR PDBsum; 7R0A; -. DR PDBsum; 7R2F; -. DR PDBsum; 7R3C; -. DR PDBsum; 7R4E; -. DR AlphaFoldDB; P21836; -. DR SMR; P21836; -. DR BioGRID; 197921; 3. DR IntAct; P21836; 2. 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 GlyCosmos; P21836; 3 sites, 2 glycans. DR GlyGen; P21836; 4 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P21836; -. DR PhosphoSitePlus; P21836; -. DR SwissPalm; P21836; -. DR PaxDb; 10090-ENSMUSP00000024099; -. DR ProteomicsDB; 285642; -. [P21836-1] DR Antibodypedia; 16701; 823 antibodies from 43 providers. DR DNASU; 11423; -. DR Ensembl; ENSMUST00000024099.11; ENSMUSP00000024099.5; ENSMUSG00000023328.15. [P21836-1] DR Ensembl; ENSMUST00000085934.4; ENSMUSP00000083097.4; ENSMUSG00000023328.15. [P21836-1] DR GeneID; 11423; -. DR KEGG; mmu:11423; -. DR UCSC; uc009abt.1; mouse. [P21836-1] DR AGR; MGI:87876; -. 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; 4386at2759; -. DR PhylomeDB; P21836; -. DR TreeFam; TF315470; -. DR BRENDA; 3.1.1.7; 3474. DR SABIO-RK; P21836; -. DR BioGRID-ORCS; 11423; 3 hits in 81 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 106 other cell types or tissues. DR ExpressionAtlas; P21836; baseline and differential. 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: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: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:0098552; C:side of membrane; IEA:UniProtKB-KW. 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: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: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: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 CDD; cd00312; Esterase_lipase; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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 PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1. DR PANTHER; PTHR43918:SF11; ACETYLCHOLINESTERASE; 1. DR Pfam; PF08674; AChE_tetra; 1. DR Pfam; PF00135; COesterase; 1. DR PRINTS; PR00878; CHOLNESTRASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. DR Genevisible; P21836; MM. 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 STRAND 107..110 FT /evidence="ECO:0007829|PDB:7R4E" 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 //