ACES_TETCF
ID ACES_TETCF Reviewed; 586 AA.
AC P04058;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Acetylcholinesterase;
DE Short=AChE;
DE EC=3.1.1.7;
DE Flags: Precursor;
GN Name=ache;
OS Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX NCBI_TaxID=7787;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-586.
RX PubMed=3753747; DOI=10.1038/319407a0;
RA Schumacher M., Camp S., Maulet Y., Newton M., McPhee-Quigley K.,
RA Taylor S.S., Friedmann T., Taylor P.;
RT "Primary structure of Torpedo californica acetylcholinesterase deduced from
RT its cDNA sequence.";
RL Nature 319:407-409(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RX PubMed=3198606; DOI=10.1016/s0021-9258(18)37378-2;
RA Schumacher M.;
RT "Multiple messenger RNA species give rise to the structural diversity in
RT acetylcholinesterase.";
RL J. Biol. Chem. 263:18979-18987(1988).
RN [3]
RP PROTEIN SEQUENCE OF 22-45 AND 214-237.
RX PubMed=3900071; DOI=10.1016/s0021-9258(17)39005-1;
RA MacPhee-Quigley K., Taylor P., Taylor S.;
RT "Primary structures of the catalytic subunits from two molecular forms of
RT acetylcholinesterase. A comparison of NH2-terminal and active center
RT sequences.";
RL J. Biol. Chem. 260:12185-12189(1985).
RN [4]
RP PROTEIN SEQUENCE OF 100-108.
RX PubMed=2068091; DOI=10.1073/pnas.88.14.6117;
RA Kreienkamp H.J., Weise C., Raba R., Aaviksaar A., Hucho F.;
RT "Anionic subsites of the catalytic center of acetylcholinesterase from
RT Torpedo and from cobra venom.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6117-6121(1991).
RN [5]
RP PROTEIN SEQUENCE OF 552-558.
RX PubMed=3335534; DOI=10.1016/s0021-9258(19)57277-5;
RA Gibney G., Macphee-Quigley K., Thompson B., Vedvick T., Low M.G.,
RA Taylor S.S., Taylor P.;
RT "Divergence in primary structure between the molecular forms of
RT acetylcholinesterase.";
RL J. Biol. Chem. 263:1140-1145(1988).
RN [6]
RP ALTERNATIVE SPLICING.
RX PubMed=2306366; DOI=10.1016/0896-6273(90)90103-m;
RA Maulet Y., Camp S., Gibney G., Rachinsky T.L., Ekstroem T.J., Taylor P.;
RT "Single gene encodes glycophospholipid-anchored and asymmetric
RT acetylcholinesterase forms: alternative coding exons contain inverted
RT repeat sequences.";
RL Neuron 4:289-301(1990).
RN [7]
RP DISULFIDE BONDS.
RX PubMed=3759980; DOI=10.1016/s0021-9258(18)67056-5;
RA McPhee-Quigley K., Vedvick T.S., Taylor P., Taylor S.S.;
RT "Profile of the disulfide bonds in acetylcholinesterase.";
RL J. Biol. Chem. 261:13565-13570(1986).
RN [8]
RP STRUCTURE OF THE GPI-ANCHOR.
RX PubMed=8257440; DOI=10.1042/bj2960473;
RA Mehlert A., Varon L., Silman I., Homans S.W., Ferguson M.A.;
RT "Structure of the glycosyl-phosphatidylinositol membrane anchor of
RT acetylcholinesterase from the electric organ of the electric-fish, Torpedo
RT californica.";
RL Biochem. J. 296:473-479(1993).
RN [9]
RP GPI-ANCHOR AT SER-564.
RX PubMed=8597567; DOI=10.1016/0167-4838(95)00205-7;
RA Bucht G., Hjalmarsson K.;
RT "Residues in Torpedo californica acetylcholinesterase necessary for
RT processing to a glycosyl phosphatidylinositol-anchored form.";
RL Biochim. Biophys. Acta 1292:223-232(1996).
RN [10]
RP MUTAGENESIS.
RX PubMed=2217185; DOI=10.1073/pnas.87.19.7546;
RA Gibney G., Camp S., Dionne M., McPhee-Quigley K., Taylor P.;
RT "Mutagenesis of essential functional residues in acetylcholinesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7546-7550(1990).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-558, ACTIVE SITE, GLYCOSYLATION
RP AT ASN-437, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=1678899; DOI=10.1126/science.1678899;
RA Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L.,
RA Silman I.;
RT "Atomic structure of acetylcholinesterase from Torpedo californica: a
RT prototypic acetylcholine-binding protein.";
RL Science 253:872-879(1991).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-556 IN COMPLEX WITH SUBSTRATE
RP ANALOGS.
RX PubMed=8415649; DOI=10.1073/pnas.90.19.9031;
RA Harel M., Schalk I., Ehret-Sabatier L., Bouet F., Goeldner M., Hirth C.,
RA Axelsen P.H., Silman I., Sussman J.L.;
RT "Quaternary ligand binding to aromatic residues in the active-site gorge of
RT acetylcholinesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9031-9035(1993).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-558 IN COMPLEX WITH
RP FASCICULIN-2, AND DISULFIDE BOND.
RX PubMed=8747462; DOI=10.1016/s0969-2126(01)00273-8;
RA Harel M., Kleywegt G.J., Ravelli R.B., Silman I., Sussman J.L.;
RT "Crystal structure of an acetylcholinesterase-fasciculin complex:
RT interaction of a three-fingered toxin from snake venom with its target.";
RL Structure 3:1355-1366(1995).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-558 IN COMPLEX WITH THE
RP INHIBITOR HUPERZINE A.
RX PubMed=8989325; DOI=10.1038/nsb0197-57;
RA Raves M.L., Harel M., Pang Y.P., Silman I., Kozikowski A.P., Sussman J.L.;
RT "Structure of acetylcholinesterase complexed with the nootropic alkaloid,
RT (-)-huperzine A.";
RL Nat. Struct. Biol. 4:57-63(1997).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-558.
RX PubMed=10231521; DOI=10.1021/bi982723p;
RA Bartolucci C., Perola E., Cellai L., Brufani M., Lamba D.;
RT "'Back door' opening implied by the crystal structure of a carbamoylated
RT acetylcholinesterase.";
RL Biochemistry 38:5714-5719(1999).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-558.
RX PubMed=10353814; DOI=10.1021/bi982678l;
RA Millard C.B., Kryger G., Ordentlich A., Greenblatt H.M., Harel M.,
RA Raves M.L., Segall Y., Barak D., Shafferman A., Silman I., Sussman J.L.;
RT "Crystal structures of aged phosphonylated acetylcholinesterase: nerve
RT agent reaction products at the atomic level.";
RL Biochemistry 38:7032-7039(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-564 IN COMPLEX WITH
RP GALANTHAMINE.
RX PubMed=10606746; DOI=10.1016/s0014-5793(99)01637-3;
RA Greenblatt H.M., Kryger G., Lewis T., Silman I., Sussman J.L.;
RT "Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3-A
RT resolution.";
RL FEBS Lett. 463:321-326(1999).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE
RP SYNTHETIC INHIBITOR ARICEPT, AND GLYCOSYLATION AT ASN-80; ASN-437; ASN-478
RP AND ASN-554.
RX PubMed=10368299; DOI=10.1016/s0969-2126(99)80040-9;
RA Kryger G., Silman I., Sussman J.L.;
RT "Structure of acetylcholinesterase complexed with E2020 (Aricept(R)):
RT implications for the design of new anti-Alzheimer drugs.";
RL Structure 7:297-307(1999).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE
RP SYNTHETIC INHIBITOR HUPRINE.
RX PubMed=11863435; DOI=10.1021/bi011652i;
RA Dvir H., Wong D.M., Harel M., Barril X., Orozco M., Luque F.J.,
RA Munoz-Torrero D., Camps P., Rosenberry T.L., Silman I., Sussman J.L.;
RT "3D structure of Torpedo californica acetylcholinesterase complexed with
RT huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates.";
RL Biochemistry 41:2970-2981(2002).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-556 IN COMPLEX WITH THE
RP SYNTHETIC INHIBITOR RIVASTIGMINE.
RX PubMed=11888271; DOI=10.1021/bi020016x;
RA Bar-On P., Millard C.B., Harel M., Dvir H., Enz A., Sussman J.L.,
RA Silman I.;
RT "Kinetic and structural studies on the interaction of cholinesterases with
RT the anti-Alzheimer drug rivastigmine.";
RL Biochemistry 41:3555-3564(2002).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE
RP SYNTHETIC INHIBITOR CPT-11.
RX PubMed=15772291; DOI=10.1124/mol.104.009944;
RA Harel M., Hyatt J.L., Brumshtein B., Morton C.L., Yoon K.J., Wadkins R.M.,
RA Silman I., Sussman J.L., Potter P.M.;
RT "The crystal structure of the complex of the anticancer prodrug 7-ethyl-10-
RT [4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT-11) with
RT Torpedo californica acetylcholinesterase provides a molecular explanation
RT for its cholinergic action.";
RL Mol. Pharmacol. 67:1874-1881(2005).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-558 IN COMPLEXES WITH
RP SUBSTRATE AND SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-80 AND ASN-437,
RP ACTIVE SITE, AND ACTIVITY REGULATION.
RX PubMed=16763558; DOI=10.1038/sj.emboj.7601175;
RA Colletier J.-P., Fournier D., Greenblatt H.M., Stojan J., Sussman J.L.,
RA Zaccai G., Silman I., Weik M.;
RT "Structural insights into substrate traffic and inhibition in
RT acetylcholinesterase.";
RL EMBO J. 25:2746-2756(2006).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-558 IN COMPLEX WITH SOMAN,
RP ACTIVE SITE, AND DISULFIDE BONDS.
RX PubMed=19642642; DOI=10.1021/jm900433t;
RA Sanson B., Nachon F., Colletier J.P., Froment M.T., Toker L.,
RA Greenblatt H.M., Sussman J.L., Ashani Y., Masson P., Silman I., Weik M.;
RT "Crystallographic snapshots of nonaged and aged conjugates of soman with
RT acetylcholinesterase, and of a ternary complex of the aged conjugate with
RT pralidoxime.";
RL J. Med. Chem. 52:7593-7603(2009).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 23-556 IN COMPLEX WITH
RP GALANTHAMINE DERIVATIVES.
RX PubMed=20025280; DOI=10.1021/jm901296p;
RA Bartolucci C., Haller L.A., Jordis U., Fels G., Lamba D.;
RT "Probing Torpedo californica acetylcholinesterase catalytic gorge with two
RT novel bis-functional galanthamine derivatives.";
RL J. Med. Chem. 53:745-751(2010).
CC -!- FUNCTION: Terminates signal transduction at the neuromuscular junction
CC by rapid hydrolysis of the acetylcholine released into the synaptic
CC cleft. May be involved in cell-cell interactions.
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 -!- ACTIVITY REGULATION: Inhibited by substrate concentrations above 0.5
CC mM. {ECO:0000269|PubMed:16763558}.
CC -!- SUBUNIT: Isoform H form is a homodimer; the asymmetric form is a
CC disulfide-bonded oligomer composed of a collagenic subunit (Q) and a
CC variable number of T catalytic subunits. {ECO:0000269|PubMed:10368299,
CC ECO:0000269|PubMed:10606746, ECO:0000269|PubMed:11863435,
CC ECO:0000269|PubMed:11888271, ECO:0000269|PubMed:15772291,
CC ECO:0000269|PubMed:1678899, ECO:0000269|PubMed:19642642,
CC ECO:0000269|PubMed:20025280, ECO:0000269|PubMed:8415649,
CC ECO:0000269|PubMed:8747462, ECO:0000269|PubMed:8989325}.
CC -!- SUBCELLULAR LOCATION: [Isoform H]: Cell membrane; Lipid-anchor, GPI-
CC anchor. Synapse.
CC -!- SUBCELLULAR LOCATION: [Isoform T]: Cell membrane; Peripheral membrane
CC protein. Synapse. Note=Attached to the membrane through disulfide
CC linkage with the collagenic subunit, itself bound to the membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=H; Synonyms=Globular;
CC IsoId=P04058-1; Sequence=Displayed;
CC Name=T;
CC IsoId=P04058-2; Sequence=VSP_001460;
CC -!- TISSUE SPECIFICITY: Found in the synapses and to a lower extent in
CC extrajunctional areas of muscle and nerve, and on erythrocyte
CC membranes.
CC -!- PTM: An interchain disulfide bond is present in what becomes position
CC 593 of the T isoform.
CC -!- MISCELLANEOUS: [Isoform H]: GPI-anchored form.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; X03439; CAA27169.1; -; mRNA.
DR EMBL; X56516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X56517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A00773; ACRYE.
DR PDB; 1ACJ; X-ray; 2.80 A; A=22-556.
DR PDB; 1ACL; X-ray; 2.80 A; A=22-556.
DR PDB; 1AMN; X-ray; 2.80 A; A=22-558.
DR PDB; 1AX9; X-ray; 2.80 A; A=22-558.
DR PDB; 1CFJ; X-ray; 2.60 A; A=22-558.
DR PDB; 1DX6; X-ray; 2.30 A; A=22-564.
DR PDB; 1E3Q; X-ray; 2.85 A; A=22-564.
DR PDB; 1E66; X-ray; 2.10 A; A=22-564.
DR PDB; 1EA5; X-ray; 1.80 A; A=22-558.
DR PDB; 1EEA; X-ray; 4.50 A; A=22-555.
DR PDB; 1EVE; X-ray; 2.50 A; A=22-564.
DR PDB; 1FSS; X-ray; 3.00 A; A=22-558.
DR PDB; 1GPK; X-ray; 2.10 A; A=22-558.
DR PDB; 1GPN; X-ray; 2.35 A; A=22-558.
DR PDB; 1GQR; X-ray; 2.20 A; A=25-556.
DR PDB; 1GQS; X-ray; 3.00 A; A=25-556.
DR PDB; 1H22; X-ray; 2.15 A; A=22-564.
DR PDB; 1H23; X-ray; 2.15 A; A=22-564.
DR PDB; 1HBJ; X-ray; 2.50 A; A=22-564.
DR PDB; 1JJB; X-ray; 2.30 A; A=25-556.
DR PDB; 1OCE; X-ray; 2.70 A; A=22-558.
DR PDB; 1ODC; X-ray; 2.20 A; A=22-564.
DR PDB; 1QID; X-ray; 2.05 A; A=22-558.
DR PDB; 1QIE; X-ray; 2.10 A; A=22-558.
DR PDB; 1QIF; X-ray; 2.10 A; A=22-558.
DR PDB; 1QIG; X-ray; 2.30 A; A=22-558.
DR PDB; 1QIH; X-ray; 2.50 A; A=22-558.
DR PDB; 1QII; X-ray; 2.65 A; A=22-558.
DR PDB; 1QIJ; X-ray; 2.80 A; A=22-558.
DR PDB; 1QIK; X-ray; 2.90 A; A=22-558.
DR PDB; 1QIM; X-ray; 3.00 A; A=22-558.
DR PDB; 1QTI; X-ray; 2.50 A; A=22-558.
DR PDB; 1SOM; X-ray; 2.20 A; A=22-564.
DR PDB; 1U65; X-ray; 2.61 A; A=22-564.
DR PDB; 1UT6; X-ray; 2.40 A; A=22-556.
DR PDB; 1VOT; X-ray; 2.50 A; A=22-558.
DR PDB; 1VXO; X-ray; 2.40 A; A=22-558.
DR PDB; 1VXR; X-ray; 2.20 A; A=22-558.
DR PDB; 1W4L; X-ray; 2.16 A; A=22-564.
DR PDB; 1W6R; X-ray; 2.05 A; A=22-564.
DR PDB; 1W75; X-ray; 2.40 A; A/B=22-564.
DR PDB; 1W76; X-ray; 2.30 A; A/B=22-564.
DR PDB; 1ZGB; X-ray; 2.30 A; A=22-564.
DR PDB; 1ZGC; X-ray; 2.10 A; A/B=22-564.
DR PDB; 2ACE; X-ray; 2.50 A; A=22-558.
DR PDB; 2ACK; X-ray; 2.40 A; A=22-558.
DR PDB; 2BAG; X-ray; 2.40 A; A=22-564.
DR PDB; 2C4H; X-ray; 2.15 A; A=22-558.
DR PDB; 2C58; X-ray; 2.30 A; A=22-558.
DR PDB; 2C5F; X-ray; 2.60 A; A=22-558.
DR PDB; 2C5G; X-ray; 1.95 A; A=22-558.
DR PDB; 2CEK; X-ray; 2.20 A; A=22-556.
DR PDB; 2CKM; X-ray; 2.15 A; A=22-564.
DR PDB; 2CMF; X-ray; 2.50 A; A=22-564.
DR PDB; 2DFP; X-ray; 2.30 A; A=23-556.
DR PDB; 2J3D; X-ray; 2.60 A; A=22-564.
DR PDB; 2J3Q; X-ray; 2.80 A; A=22-564.
DR PDB; 2J4F; X-ray; 2.80 A; A=22-564.
DR PDB; 2V96; X-ray; 2.40 A; A/B=22-558.
DR PDB; 2V97; X-ray; 2.40 A; A/B=22-558.
DR PDB; 2V98; X-ray; 3.00 A; A/B=22-558.
DR PDB; 2VA9; X-ray; 2.40 A; A/B=22-558.
DR PDB; 2VJA; X-ray; 2.30 A; A/B=22-558.
DR PDB; 2VJB; X-ray; 2.39 A; A/B=22-558.
DR PDB; 2VJC; X-ray; 2.20 A; A/B=22-558.
DR PDB; 2VJD; X-ray; 2.30 A; A/B=22-558.
DR PDB; 2VQ6; X-ray; 2.71 A; A=22-564.
DR PDB; 2VT6; X-ray; 2.40 A; A/B=22-558.
DR PDB; 2VT7; X-ray; 2.20 A; A/B=22-558.
DR PDB; 2W6C; X-ray; 2.69 A; X=1-586.
DR PDB; 2WFZ; X-ray; 1.95 A; A=22-558.
DR PDB; 2WG0; X-ray; 2.20 A; A=22-558.
DR PDB; 2WG1; X-ray; 2.20 A; A=22-558.
DR PDB; 2WG2; X-ray; 1.95 A; A=22-558.
DR PDB; 2XI4; X-ray; 2.30 A; A/B=22-558.
DR PDB; 3GEL; X-ray; 2.39 A; A=25-556.
DR PDB; 3I6M; X-ray; 2.26 A; A=23-556.
DR PDB; 3I6Z; X-ray; 2.19 A; A=23-556.
DR PDB; 3M3D; X-ray; 2.34 A; A=22-564.
DR PDB; 3ZV7; X-ray; 2.26 A; A=22-564.
DR PDB; 4TVK; X-ray; 2.30 A; A=23-556.
DR PDB; 4W63; X-ray; 2.80 A; A=23-556.
DR PDB; 4X3C; X-ray; 2.60 A; A=23-556.
DR PDB; 5BWB; X-ray; 2.57 A; A=22-558.
DR PDB; 5BWC; X-ray; 2.45 A; A=22-558.
DR PDB; 5DLP; X-ray; 2.70 A; A=22-564.
DR PDB; 5E2I; X-ray; 2.65 A; A=25-556.
DR PDB; 5E4J; X-ray; 2.54 A; A=25-556.
DR PDB; 5E4T; X-ray; 2.43 A; A=22-564.
DR PDB; 5EHX; X-ray; 2.10 A; A=25-556.
DR PDB; 5EI5; X-ray; 2.10 A; A=23-556.
DR PDB; 5IH7; X-ray; 2.40 A; A=23-556.
DR PDB; 5NAP; X-ray; 2.17 A; A=22-564.
DR PDB; 5NAU; X-ray; 2.25 A; A=22-564.
DR PDB; 5NUU; X-ray; 2.50 A; A=22-564.
DR PDB; 6EUC; X-ray; 2.22 A; A=25-556.
DR PDB; 6EUE; X-ray; 2.00 A; A=24-556.
DR PDB; 6EWK; X-ray; 2.22 A; A=25-556.
DR PDB; 6EZG; X-ray; 2.20 A; A/B=22-558.
DR PDB; 6EZH; X-ray; 2.60 A; A/B=22-558.
DR PDB; 6FLD; X-ray; 2.40 A; A=25-556.
DR PDB; 6FQN; X-ray; 2.30 A; A=25-556.
DR PDB; 6G17; X-ray; 2.20 A; A=22-558.
DR PDB; 6G1U; X-ray; 1.79 A; A/B=22-586.
DR PDB; 6G1V; X-ray; 1.82 A; A/B=22-586.
DR PDB; 6G1W; X-ray; 1.90 A; A/B=22-586.
DR PDB; 6G4M; X-ray; 2.63 A; A/B=22-558.
DR PDB; 6G4N; X-ray; 2.90 A; A/B=22-558.
DR PDB; 6G4O; X-ray; 2.78 A; A/B=22-558.
DR PDB; 6G4P; X-ray; 2.83 A; A/B=22-558.
DR PDB; 6H12; X-ray; 2.20 A; A/B=22-586.
DR PDB; 6H13; X-ray; 2.80 A; A/B=22-586.
DR PDB; 6H14; X-ray; 1.86 A; A/B=22-586.
DR PDB; 6TT0; X-ray; 2.80 A; A=25-556.
DR PDB; 7AIS; X-ray; 1.75 A; A/B=1-586.
DR PDB; 7AIT; X-ray; 2.10 A; A/B=1-586.
DR PDB; 7AIU; X-ray; 2.00 A; A/B=1-586.
DR PDB; 7AIV; X-ray; 2.55 A; A/B=1-586.
DR PDB; 7AIW; X-ray; 1.90 A; A/B=1-586.
DR PDB; 7AIX; X-ray; 1.86 A; A=1-586.
DR PDB; 7B2W; X-ray; 2.65 A; A=22-558.
DR PDB; 7B38; X-ray; 1.85 A; A=25-556.
DR PDB; 7B8E; X-ray; 2.23 A; A=22-558.
DR PDBsum; 1ACJ; -.
DR PDBsum; 1ACL; -.
DR PDBsum; 1AMN; -.
DR PDBsum; 1AX9; -.
DR PDBsum; 1CFJ; -.
DR PDBsum; 1DX6; -.
DR PDBsum; 1E3Q; -.
DR PDBsum; 1E66; -.
DR PDBsum; 1EA5; -.
DR PDBsum; 1EEA; -.
DR PDBsum; 1EVE; -.
DR PDBsum; 1FSS; -.
DR PDBsum; 1GPK; -.
DR PDBsum; 1GPN; -.
DR PDBsum; 1GQR; -.
DR PDBsum; 1GQS; -.
DR PDBsum; 1H22; -.
DR PDBsum; 1H23; -.
DR PDBsum; 1HBJ; -.
DR PDBsum; 1JJB; -.
DR PDBsum; 1OCE; -.
DR PDBsum; 1ODC; -.
DR PDBsum; 1QID; -.
DR PDBsum; 1QIE; -.
DR PDBsum; 1QIF; -.
DR PDBsum; 1QIG; -.
DR PDBsum; 1QIH; -.
DR PDBsum; 1QII; -.
DR PDBsum; 1QIJ; -.
DR PDBsum; 1QIK; -.
DR PDBsum; 1QIM; -.
DR PDBsum; 1QTI; -.
DR PDBsum; 1SOM; -.
DR PDBsum; 1U65; -.
DR PDBsum; 1UT6; -.
DR PDBsum; 1VOT; -.
DR PDBsum; 1VXO; -.
DR PDBsum; 1VXR; -.
DR PDBsum; 1W4L; -.
DR PDBsum; 1W6R; -.
DR PDBsum; 1W75; -.
DR PDBsum; 1W76; -.
DR PDBsum; 1ZGB; -.
DR PDBsum; 1ZGC; -.
DR PDBsum; 2ACE; -.
DR PDBsum; 2ACK; -.
DR PDBsum; 2BAG; -.
DR PDBsum; 2C4H; -.
DR PDBsum; 2C58; -.
DR PDBsum; 2C5F; -.
DR PDBsum; 2C5G; -.
DR PDBsum; 2CEK; -.
DR PDBsum; 2CKM; -.
DR PDBsum; 2CMF; -.
DR PDBsum; 2DFP; -.
DR PDBsum; 2J3D; -.
DR PDBsum; 2J3Q; -.
DR PDBsum; 2J4F; -.
DR PDBsum; 2V96; -.
DR PDBsum; 2V97; -.
DR PDBsum; 2V98; -.
DR PDBsum; 2VA9; -.
DR PDBsum; 2VJA; -.
DR PDBsum; 2VJB; -.
DR PDBsum; 2VJC; -.
DR PDBsum; 2VJD; -.
DR PDBsum; 2VQ6; -.
DR PDBsum; 2VT6; -.
DR PDBsum; 2VT7; -.
DR PDBsum; 2W6C; -.
DR PDBsum; 2WFZ; -.
DR PDBsum; 2WG0; -.
DR PDBsum; 2WG1; -.
DR PDBsum; 2WG2; -.
DR PDBsum; 2XI4; -.
DR PDBsum; 3GEL; -.
DR PDBsum; 3I6M; -.
DR PDBsum; 3I6Z; -.
DR PDBsum; 3M3D; -.
DR PDBsum; 3ZV7; -.
DR PDBsum; 4TVK; -.
DR PDBsum; 4W63; -.
DR PDBsum; 4X3C; -.
DR PDBsum; 5BWB; -.
DR PDBsum; 5BWC; -.
DR PDBsum; 5DLP; -.
DR PDBsum; 5E2I; -.
DR PDBsum; 5E4J; -.
DR PDBsum; 5E4T; -.
DR PDBsum; 5EHX; -.
DR PDBsum; 5EI5; -.
DR PDBsum; 5IH7; -.
DR PDBsum; 5NAP; -.
DR PDBsum; 5NAU; -.
DR PDBsum; 5NUU; -.
DR PDBsum; 6EUC; -.
DR PDBsum; 6EUE; -.
DR PDBsum; 6EWK; -.
DR PDBsum; 6EZG; -.
DR PDBsum; 6EZH; -.
DR PDBsum; 6FLD; -.
DR PDBsum; 6FQN; -.
DR PDBsum; 6G17; -.
DR PDBsum; 6G1U; -.
DR PDBsum; 6G1V; -.
DR PDBsum; 6G1W; -.
DR PDBsum; 6G4M; -.
DR PDBsum; 6G4N; -.
DR PDBsum; 6G4O; -.
DR PDBsum; 6G4P; -.
DR PDBsum; 6H12; -.
DR PDBsum; 6H13; -.
DR PDBsum; 6H14; -.
DR PDBsum; 6TT0; -.
DR PDBsum; 7AIS; -.
DR PDBsum; 7AIT; -.
DR PDBsum; 7AIU; -.
DR PDBsum; 7AIV; -.
DR PDBsum; 7AIW; -.
DR PDBsum; 7AIX; -.
DR PDBsum; 7B2W; -.
DR PDBsum; 7B38; -.
DR PDBsum; 7B8E; -.
DR AlphaFoldDB; P04058; -.
DR SMR; P04058; -.
DR MINT; P04058; -.
DR BindingDB; P04058; -.
DR ChEMBL; CHEMBL4780; -.
DR DrugCentral; P04058; -.
DR ESTHER; torca-ACHE; AChE.
DR MEROPS; S09.980; -.
DR iPTMnet; P04058; -.
DR BioCyc; MetaCyc:MON-16823; -.
DR BRENDA; 3.1.1.7; 6395.
DR EvolutionaryTrace; P04058; -.
DR PRO; PR:P04058; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0043083; C:synaptic cleft; IEA:GOC.
DR GO; GO:0003990; F:acetylcholinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000908; Acylcholinesterase_fish/snake.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000997; Cholinesterase.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR00879; ACHEFISH.
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;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation;
KW Serine esterase; Signal; Synapse.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:3900071"
FT CHAIN 22..564
FT /note="Acetylcholinesterase"
FT /id="PRO_0000008595"
FT PROPEP 565..586
FT /note="Removed in mature form"
FT /id="PRO_0000008596"
FT ACT_SITE 221
FT /note="Acyl-ester intermediate"
FT ACT_SITE 348
FT /note="Charge relay system"
FT ACT_SITE 461
FT /note="Charge relay system"
FT LIPID 564
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000269|PubMed:8597567"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10368299,
FT ECO:0000269|PubMed:16763558"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10368299,
FT ECO:0000269|PubMed:16763558, ECO:0000269|PubMed:1678899"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10368299"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10368299"
FT DISULFID 88..115
FT DISULFID 275..286
FT DISULFID 423..542
FT DISULFID 558
FT /note="Interchain"
FT VAR_SEQ 557..586
FT /note="ACDGELSSSGTSSSKGIIFYVLFSILYLIF -> ETIDEAERQWKTEFHRWS
FT SYMMHWKNQFDHYSRHESCAEL (in isoform T)"
FT /evidence="ECO:0000305"
FT /id="VSP_001460"
FT MUTAGEN 220
FT /note="E->H: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2217185"
FT MUTAGEN 220
FT /note="E->Q,D: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:2217185"
FT MUTAGEN 221
FT /note="S->C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2217185"
FT MUTAGEN 221
FT /note="S->V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2217185"
FT MUTAGEN 446
FT /note="H->Q: Almost no loss of activity."
FT /evidence="ECO:0000269|PubMed:2217185"
FT MUTAGEN 461
FT /note="H->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2217185"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6FLD"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1OCE"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3ZV7"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:7AIS"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 189..204
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 210..220
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:7AIS"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:7AIS"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1QID"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4W63"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 326..332
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2WFZ"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:6H12"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:2WG1"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:5NAU"
FT HELIX 405..420
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 422..435
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 439..444
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:7AIS"
FT TURN 461..464
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 481..500
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:2CKM"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:7AIW"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 522..529
FT /evidence="ECO:0007829|PDB:7AIS"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 539..546
FT /evidence="ECO:0007829|PDB:7AIS"
FT HELIX 548..555
FT /evidence="ECO:0007829|PDB:7AIS"
SQ SEQUENCE 586 AA; 65906 MW; 731D5F0F3ABA62A8 CRC64;
MNLLVTSSLG VLLHLVVLCQ ADDHSELLVN TKSGKVMGTR VPVLSSHISA FLGIPFAEPP
VGNMRFRRPE PKKPWSGVWN ASTYPNNCQQ YVDEQFPGFS GSEMWNPNRE MSEDCLYLNI
WVPSPRPKST TVMVWIYGGG FYSGSSTLDV YNGKYLAYTE EVVLVSLSYR VGAFGFLALH
GSQEAPGNVG LLDQRMALQW VHDNIQFFGG DPKTVTIFGE SAGGASVGMH ILSPGSRDLF
RRAILQSGSP NCPWASVSVA EGRRRAVELG RNLNCNLNSD EELIHCLREK KPQELIDVEW
NVLPFDSIFR FSFVPVIDGE FFPTSLESML NSGNFKKTQI LLGVNKDEGS FFLLYGAPGF
SKDSESKISR EDFMSGVKLS VPHANDLGLD AVTLQYTDWM DDNNGIKNRD GLDDIVGDHN
VICPLMHFVN KYTKFGNGTY LYFFNHRASN LVWPEWMGVI HGYEIEFVFG LPLVKELNYT
AEEEALSRRI MHYWATFAKT GNPNEPHSQE SKWPLFTTKE QKFIDLNTEP MKVHQRLRVQ
MCVFWNQFLP KLLNATACDG ELSSSGTSSS KGIIFYVLFS ILYLIF
