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Database: UniProt
Entry: P22303
LinkDB: P22303
Original site: P22303 
ID   ACES_HUMAN              Reviewed;         614 AA.
AC   P22303; A4D2E2; B7ZKZ0; D6W5X7; Q16169; Q29S23; Q2M324; Q504V3;
AC   Q53F46; Q86TM9; Q86YX9; Q9BXP7;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   26-NOV-2014, entry version 165.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor;
GN   Name=ACHE;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM T).
RX   PubMed=2263619; DOI=10.1073/pnas.87.24.9688;
RA   Soreq H., Ben-Aziz R., Prody C.A., Seidman S., Gnatt A., Neville L.,
RA   Lieman-Hurwitz J., Lev-Lehman E., Ginzberg D., Lipidot-Lifson Y.,
RA   Zakut H.;
RT   "Molecular cloning and construction of the coding region for human
RT   acetylcholinesterase reveals a G + C-rich attenuating structure.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9688-9692(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H; R AND T).
RX   PubMed=8299725; DOI=10.1006/excr.1994.1039;
RA   Karpel R., Ben Aziz-Aloya R., Sternfeld M., Ehrlich G., Ginzberg D.,
RA   Tarroni P., Clementi F., Zakut H., Soreq H.;
RT   "Expression of three alternative acetylcholinesterase messenger RNAs
RT   in human tumor cell lines of different tissue origins.";
RL   Exp. Cell Res. 210:268-277(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA   Yang L., Zhang X.J.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-34; ALA-135 AND
RP   ASN-353.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM H), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-546 (ISOFORMS H/R/T).
RC   TISSUE=Cerebellum, and Hippocampus;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 521-614.
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.,
RA   Miller W., 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   [11]
RP   PROTEIN SEQUENCE OF 256-273; 306-326; 396-422; 465-480 AND 528-551,
RP   FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Erythrocyte;
RX   PubMed=2714437; DOI=10.1016/0014-5793(89)81352-3;
RA   Chhajlani V., Derr D., Earles B., Schmell E., August T.;
RT   "Purification and partial amino acid sequence analysis of human
RT   erythrocyte acetylcholinesterase.";
RL   FEBS Lett. 247:279-282(1989).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-611.
RX   PubMed=1748670;
RA   Velan B., Grosfeld H., Kronman C., Leitner M., Gozes Y., Lazar A.,
RA   Flashner Y., Marcus D., Cohen S., Shafferman A.;
RT   "The effect of elimination of intersubunit disulfide bonds on the
RT   activity, assembly, and secretion of recombinant human
RT   acetylcholinesterase. Expression of acetylcholinesterase Cys-580-->Ala
RT   mutant.";
RL   J. Biol. Chem. 266:23977-23984(1991).
RN   [13]
RP   FUNCTION, AND MUTAGENESIS OF ASP-206; SER-234; GLU-365; ASP-435 AND
RP   HIS-478.
RX   PubMed=1517212;
RA   Shafferman A., Kronman C., Flashner Y., Leitner M., Grosfeld H.,
RA   Ordentlich A., Gozes Y., Cohen S., Ariel N., Barak D.;
RT   "Mutagenesis of human acetylcholinesterase. Identification of residues
RT   involved in catalytic activity and in polypeptide folding.";
RL   J. Biol. Chem. 267:17640-17648(1992).
RN   [14]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11985878; DOI=10.1016/S0168-0102(02)00005-6;
RA   Yang L., He H.Y., Zhang X.J.;
RT   "Increased expression of intranuclear AChE involved in apoptosis of
RT   SK-N-SH cells.";
RL   Neurosci. Res. 42:261-268(2002).
RN   [15]
RP   3D-STRUCTURE MODELING OF 35-574.
RX   PubMed=9640563; DOI=10.1016/S1093-3263(98)00005-9;
RA   Felder C.E., Botti S.A., Lifson S., Silman I., Sussman J.L.;
RT   "External and internal electrostatic potentials of cholinesterase
RT   models.";
RL   J. Mol. Graph. Model. 15:318-327(1997).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 32-614 IN COMPLEX WITH
RP   FASCICULIN-2, AND GLYCOSYLATION AT ASN-381 AND ASN-495.
RX   PubMed=11053835; DOI=10.1107/S0907444900010659;
RA   Kryger G., Harel M., Giles K., Toker L., Velan B., Lazar A.,
RA   Kronman C., Barak D., Ariel N., Shafferman A., Silman I.,
RA   Sussman J.L.;
RT   "Structures of recombinant native and E202Q mutant human
RT   acetylcholinesterase complexed with the snake-venom toxin fasciculin-
RT   II.";
RL   Acta Crystallogr. D 56:1385-1394(2000).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 575-614 IN COMPLEX WITH
RP   COLQ.
RX   PubMed=15526038; DOI=10.1038/sj.emboj.7600425;
RA   Dvir H., Harel M., Bon S., Liu W.-Q., Vidal M., Garbay C.,
RA   Sussman J.L., Massoulie J., Silman I.;
RT   "The synaptic acetylcholinesterase tetramer assembles around a
RT   polyproline II helix.";
RL   EMBO J. 23:4394-4405(2004).
RN   [18]
RP   VARIANT BLOOD GROUP YT(B) ASN-353.
RX   PubMed=8488842;
RA   Bartels C.F., Zelinski T., Lockridge O.;
RT   "Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene
RT   accounts for YT blood group polymorphism.";
RL   Am. J. Hum. Genet. 52:928-936(1993).
CC   -!- FUNCTION: Terminates signal transduction at the neuromuscular
CC       junction by rapid hydrolysis of the acetylcholine released into
CC       the synaptic cleft. Role in neuronal apoptosis.
CC       {ECO:0000269|PubMed:11985878, ECO:0000269|PubMed:1517212,
CC       ECO:0000269|PubMed:1748670, ECO:0000269|PubMed:2714437}.
CC   -!- CATALYTIC ACTIVITY: Acetylcholine + H(2)O = choline + acetate.
CC   -!- SUBUNIT: Interacts with PRIMA1. The interaction with PRIMA1 is
CC       required to anchor it to the basal lamina of cells and organize
CC       into tetramers (By similarity). Isoform H generates GPI-anchored
CC       dimers; disulfide linked. Isoform T generates multiple structures,
CC       ranging from monomers and dimers to collagen-tailed and
CC       hydrophobic-tailed forms, in which catalytic tetramers are
CC       associated with anchoring proteins that attach them to the basal
CC       lamina or to cell membranes. In the collagen-tailed forms, isoform
CC       T subunits are associated with a specific collagen, COLQ, which
CC       triggers the formation of isoform T tetramers, from monomers and
CC       dimers. Isoform R may be monomeric. {ECO:0000250,
CC       ECO:0000269|PubMed:11053835, ECO:0000269|PubMed:15526038}.
CC   -!- INTERACTION:
CC       Q9Y215:COLQ; NbExp=2; IntAct=EBI-1637793, EBI-1637847;
CC       P06733:ENO1; NbExp=2; IntAct=EBI-1637793, EBI-353877;
CC       P63244:GNB2L1; NbExp=2; IntAct=EBI-1637793, EBI-296739;
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse
CC       {ECO:0000269|PubMed:11985878, ECO:0000269|PubMed:1748670}.
CC       Secreted {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Isoform T: Nucleus. Note=Only observed in
CC       apoptotic nuclei.
CC   -!- SUBCELLULAR LOCATION: Isoform H: Cell membrane {ECO:0000250};
CC       Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=T; Synonyms=ACHE-S, synaptic;
CC         IsoId=P22303-1; Sequence=Displayed;
CC       Name=H; Synonyms=ACHE-E, erythrocytic, E4-E5;
CC         IsoId=P22303-2; Sequence=VSP_001457;
CC         Note=GPI-anchor amidated glycine on Gly-588. Ref.9 (AAI43470)
CC         sequence is in conflict in position: 592:P->R. {ECO:0000305};
CC       Name=R; Synonyms=ACHE-R, readthrough;
CC         IsoId=P22303-4; Sequence=VSP_035569, VSP_035570;
CC       Name=4;
CC         IsoId=P22303-3; Sequence=VSP_035568;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Isoform H is highly expressed in erythrocytes.
CC       {ECO:0000269|PubMed:2714437}.
CC   -!- POLYMORPHISM: ACHE is responsible for the Yt blood group system
CC       [MIM:112100]. The molecular basis of the Yt(a)=Yt1/Yt(b)=Yt2 blood
CC       group antigens is a single variation in position 353; His-353
CC       corresponds to Yt(a) and the rare variant with Asn-353 to Yt(b).
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
CC       mutation database;
CC       URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=yt";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Acetylcholinesterase entry;
CC       URL="http://en.wikipedia.org/wiki/Acetylcholinesterase";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/ache/";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ACHEID44317ch7q22.html";
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DR   EMBL; M55040; AAA68151.1; -; mRNA.
DR   EMBL; S71129; AAC60618.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF334270; AAO32948.1; -; mRNA.
DR   EMBL; AK291321; BAF84010.1; -; mRNA.
DR   EMBL; AK223443; BAD97163.1; -; mRNA.
DR   EMBL; AY750146; AAU43801.1; -; Genomic_DNA.
DR   EMBL; AC011895; AAP22364.1; -; Genomic_DNA.
DR   EMBL; AC011895; AAP22365.1; -; Genomic_DNA.
DR   EMBL; CH236956; EAL23812.1; -; Genomic_DNA.
DR   EMBL; CH236956; EAL23813.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76461.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76463.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76462.1; -; Genomic_DNA.
DR   EMBL; BC036813; AAH36813.1; -; mRNA.
DR   EMBL; BC105060; AAI05061.1; -; mRNA.
DR   EMBL; BC105062; AAI05063.1; -; mRNA.
DR   EMBL; BC143469; AAI43470.1; -; mRNA.
DR   EMBL; AF312032; AAK21003.1; -; Genomic_DNA.
DR   CCDS; CCDS5709.1; -. [P22303-1]
DR   CCDS; CCDS5710.1; -. [P22303-2]
DR   CCDS; CCDS64736.1; -. [P22303-3]
DR   PIR; A39256; A39256.
DR   RefSeq; NP_000656.1; NM_000665.3. [P22303-1]
DR   RefSeq; NP_001269378.1; NM_001282449.1. [P22303-3]
DR   RefSeq; NP_056646.1; NM_015831.2. [P22303-2]
DR   RefSeq; XP_005250414.1; XM_005250357.1. [P22303-2]
DR   RefSeq; XP_005250415.1; XM_005250358.1. [P22303-1]
DR   RefSeq; XP_006716058.1; XM_006715995.1. [P22303-2]
DR   UniGene; Hs.154495; -.
DR   PDB; 1B41; X-ray; 2.76 A; A=36-574.
DR   PDB; 1F8U; X-ray; 2.90 A; A=32-614.
DR   PDB; 1PUV; Model; -; A=37-574.
DR   PDB; 1PUW; Model; -; A=37-574.
DR   PDB; 1VZJ; X-ray; 2.35 A; A/B/C/D/E/F/G/H=575-614.
DR   PDB; 2CLJ; Model; -; A=32-574.
DR   PDB; 2X8B; X-ray; 2.95 A; A=32-614.
DR   PDB; 3LII; X-ray; 3.20 A; A/B=35-574.
DR   PDB; 4BDT; X-ray; 3.10 A; A=32-614.
DR   PDB; 4EY4; X-ray; 2.16 A; A/B=33-574.
DR   PDB; 4EY5; X-ray; 2.30 A; A/B=33-574.
DR   PDB; 4EY6; X-ray; 2.40 A; A/B=33-574.
DR   PDB; 4EY7; X-ray; 2.35 A; A/B=33-574.
DR   PDB; 4EY8; X-ray; 2.60 A; A=33-574.
DR   PDB; 4M0E; X-ray; 2.00 A; A/B=33-574.
DR   PDB; 4M0F; X-ray; 2.30 A; A/B=33-574.
DR   PDBsum; 1B41; -.
DR   PDBsum; 1F8U; -.
DR   PDBsum; 1PUV; -.
DR   PDBsum; 1PUW; -.
DR   PDBsum; 1VZJ; -.
DR   PDBsum; 2CLJ; -.
DR   PDBsum; 2X8B; -.
DR   PDBsum; 3LII; -.
DR   PDBsum; 4BDT; -.
DR   PDBsum; 4EY4; -.
DR   PDBsum; 4EY5; -.
DR   PDBsum; 4EY6; -.
DR   PDBsum; 4EY7; -.
DR   PDBsum; 4EY8; -.
DR   PDBsum; 4M0E; -.
DR   PDBsum; 4M0F; -.
DR   ProteinModelPortal; P22303; -.
DR   SMR; P22303; 35-573, 575-608.
DR   BioGrid; 106561; 2.
DR   DIP; DIP-1119N; -.
DR   IntAct; P22303; 8.
DR   MINT; MINT-149019; -.
DR   BindingDB; P22303; -.
DR   ChEMBL; CHEMBL2095233; -.
DR   DrugBank; DB01122; Ambenonium.
DR   DrugBank; DB00122; Choline.
DR   DrugBank; DB01245; Decamethonium.
DR   DrugBank; DB00944; Demecarium.
DR   DrugBank; DB00449; Dipivefrin.
DR   DrugBank; DB00843; Donepezil.
DR   DrugBank; DB01010; Edrophonium.
DR   DrugBank; DB01364; Ephedrine.
DR   DrugBank; DB00674; Galantamine.
DR   DrugBank; DB00483; Gallamine Triethiodide.
DR   DrugBank; DB00677; Isoflurophate.
DR   DrugBank; DB00358; Mefloquine.
DR   DrugBank; DB00805; Minaprine.
DR   DrugBank; DB01400; Neostigmine.
DR   DrugBank; DB00981; Physostigmine.
DR   DrugBank; DB00733; Pralidoxime.
DR   DrugBank; DB00545; Pyridostigmine.
DR   DrugBank; DB00989; Rivastigmine.
DR   DrugBank; DB01199; Tubocurarine.
DR   GuidetoPHARMACOLOGY; 2465; -.
DR   MEROPS; S09.979; -.
DR   PhosphoSite; P22303; -.
DR   DMDM; 113037; -.
DR   SWISS-2DPAGE; P22303; -.
DR   PaxDb; P22303; -.
DR   PRIDE; P22303; -.
DR   Ensembl; ENST00000241069; ENSP00000241069; ENSG00000087085. [P22303-1]
DR   Ensembl; ENST00000302913; ENSP00000303211; ENSG00000087085. [P22303-2]
DR   Ensembl; ENST00000411582; ENSP00000404865; ENSG00000087085. [P22303-2]
DR   Ensembl; ENST00000412389; ENSP00000394976; ENSG00000087085. [P22303-1]
DR   Ensembl; ENST00000419336; ENSP00000403474; ENSG00000087085. [P22303-3]
DR   Ensembl; ENST00000428317; ENSP00000414858; ENSG00000087085. [P22303-1]
DR   GeneID; 43; -.
DR   KEGG; hsa:43; -.
DR   UCSC; uc003uxd.3; human. [P22303-1]
DR   UCSC; uc003uxe.3; human. [P22303-2]
DR   UCSC; uc003uxh.3; human. [P22303-3]
DR   CTD; 43; -.
DR   GeneCards; GC07M100487; -.
DR   HGNC; HGNC:108; ACHE.
DR   HPA; HPA019704; -.
DR   MIM; 100740; gene+phenotype.
DR   MIM; 112100; phenotype.
DR   neXtProt; NX_P22303; -.
DR   PharmGKB; PA20; -.
DR   eggNOG; COG2272; -.
DR   GeneTree; ENSGT00760000118946; -.
DR   HOVERGEN; HBG008839; -.
DR   InParanoid; P22303; -.
DR   KO; K01049; -.
DR   OMA; RPPWCPL; -.
DR   OrthoDB; EOG789C9R; -.
DR   PhylomeDB; P22303; -.
DR   TreeFam; TF315470; -.
DR   Reactome; REACT_121238; Synthesis of PC.
DR   Reactome; REACT_13583; Neurotransmitter Clearance In The Synaptic Cleft.
DR   Reactome; REACT_19189; Synthesis, secretion, and deacylation of Ghrelin.
DR   SABIO-RK; P22303; -.
DR   ChiTaRS; ACHE; human.
DR   EvolutionaryTrace; P22303; -.
DR   GeneWiki; Acetylcholinesterase; -.
DR   GenomeRNAi; 43; -.
DR   NextBio; 173; -.
DR   PRO; PR:P22303; -.
DR   Bgee; P22303; -.
DR   ExpressionAtlas; P22303; baseline and differential.
DR   Genevestigator; P22303; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; IBA:RefGenome.
DR   GO; GO:0005605; C:basal lamina; NAS:HGNC.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0009986; C:cell surface; IBA:RefGenome.
DR   GO; GO:0030425; C:dendrite; IBA:RefGenome.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:RefGenome.
DR   GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:RefGenome.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HGNC.
DR   GO; GO:0016020; C:membrane; IDA:HGNC.
DR   GO; GO:0031594; C:neuromuscular junction; IBA:RefGenome.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045211; C:postsynaptic membrane; IBA:RefGenome.
DR   GO; GO:0042734; C:presynaptic membrane; IBA:RefGenome.
DR   GO; GO:0045202; C:synapse; IDA:HGNC.
DR   GO; GO:0042166; F:acetylcholine binding; NAS:UniProtKB.
DR   GO; GO:0003990; F:acetylcholinesterase activity; IMP:UniProtKB.
DR   GO; GO:0001540; F:beta-amyloid binding; TAS:UniProtKB.
DR   GO; GO:0004104; F:cholinesterase activity; IDA:HGNC.
DR   GO; GO:0005518; F:collagen binding; IDA:HGNC.
DR   GO; GO:0016787; F:hydrolase activity; IDA:HGNC.
DR   GO; GO:0043236; F:laminin binding; IDA:BHF-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; NAS:UniProtKB.
DR   GO; GO:0017171; F:serine hydrolase activity; IDA:HGNC.
DR   GO; GO:0006581; P:acetylcholine catabolic process; IDA:HGNC.
DR   GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; NAS:UniProtKB.
DR   GO; GO:0042982; P:amyloid precursor protein metabolic process; TAS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; TAS:UniProtKB.
DR   GO; GO:0019695; P:choline metabolic process; IBA:RefGenome.
DR   GO; GO:0006260; P:DNA replication; TAS:UniProtKB.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
DR   GO; GO:0007517; P:muscle organ development; TAS:UniProtKB.
DR   GO; GO:0032223; P:negative regulation of synaptic transmission, cholinergic; IC:HGNC.
DR   GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; TAS:Reactome.
DR   GO; GO:0045212; P:neurotransmitter receptor biosynthetic process; IEA:Ensembl.
DR   GO; GO:0002076; P:osteoblast development; IEP:HGNC.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
DR   GO; GO:0006644; P:phospholipid metabolic process; TAS:Reactome.
DR   GO; GO:0050714; P:positive regulation of protein secretion; TAS:UniProtKB.
DR   GO; GO:0051262; P:protein tetramerization; IEA:Ensembl.
DR   GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR   GO; GO:0050770; P:regulation of axonogenesis; IBA:RefGenome.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:RefGenome.
DR   GO; GO:0001919; P:regulation of receptor recycling; IEA:Ensembl.
DR   GO; GO:0009611; P:response to wounding; TAS:UniProtKB.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0007416; P:synapse assembly; TAS:UniProtKB.
DR   GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:RefGenome.
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   ProDom; PD415333; AChE_tetra; 1.
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; Blood group antigen;
KW   Cell junction; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation;
KW   Nucleus; Polymorphism; Reference proteome; Secreted; Serine esterase;
KW   Signal; Synapse.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32    614       Acetylcholinesterase.
FT                                /FTId=PRO_0000008587.
FT   ACT_SITE    234    234       Acyl-ester intermediate.
FT   ACT_SITE    365    365       Charge relay system.
FT   ACT_SITE    478    478       Charge relay system.
FT   CARBOHYD    296    296       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    381    381       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:11053835}.
FT   CARBOHYD    495    495       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:11053835}.
FT   DISULFID    100    127
FT   DISULFID    288    303
FT   DISULFID    440    560
FT   DISULFID    611    611       Interchain.
FT   VAR_SEQ     357    444       Missing (in isoform 4).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_035568.
FT   VAR_SEQ     575    614       DTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL
FT                                -> ASEAPSTCPGFTHGEAAPRPGLPLPLLLLHQLLLLFLS
FT                                HLRRL (in isoform H).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:8299725}.
FT                                /FTId=VSP_001457.
FT   VAR_SEQ     575    603       DTLDEAERQWKAEFHRWSSYMVHWKNQFD -> GMQGPAGS
FT                                AGRRGVGARQCNPSLLPLASE (in isoform R).
FT                                {ECO:0000303|PubMed:8299725}.
FT                                /FTId=VSP_035569.
FT   VAR_SEQ     604    614       Missing (in isoform R).
FT                                {ECO:0000303|PubMed:8299725}.
FT                                /FTId=VSP_035570.
FT   VARIANT      34     34       R -> Q (in dbSNP:rs17881553).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_021325.
FT   VARIANT     135    135       P -> A (in dbSNP:rs17885778).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_021326.
FT   VARIANT     333    333       V -> E (in dbSNP:rs8286).
FT                                /FTId=VAR_011934.
FT   VARIANT     353    353       H -> N (in Yt(b) antigen;
FT                                dbSNP:rs1799805).
FT                                {ECO:0000269|PubMed:8488842,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_002359.
FT   MUTAGEN     206    206       D->N: Misfolding, absence of secretion.
FT                                {ECO:0000269|PubMed:1517212}.
FT   MUTAGEN     234    234       S->A: Loss of activity.
FT                                {ECO:0000269|PubMed:1517212}.
FT   MUTAGEN     365    365       E->A: Loss of activity.
FT                                {ECO:0000269|PubMed:1517212}.
FT   MUTAGEN     435    435       D->N: Misfolding, absence of secretion.
FT                                {ECO:0000269|PubMed:1517212}.
FT   MUTAGEN     478    478       H->A: Loss of activity.
FT                                {ECO:0000269|PubMed:1517212}.
FT   MUTAGEN     611    611       C->A: Impairment of interchain disulfide
FT                                bridge formation.
FT                                {ECO:0000269|PubMed:1748670}.
FT   CONFLICT    279    279       A -> T (in Ref. 5; BAD97163).
FT                                {ECO:0000305}.
FT   CONFLICT    415    415       D -> G (in Ref. 5; BAD97163).
FT                                {ECO:0000305}.
FT   CONFLICT    486    486       F -> L (in Ref. 9; AAI43470).
FT                                {ECO:0000305}.
FT   HELIX        37     39       {ECO:0000244|PDB:4M0E}.
FT   STRAND       40     43       {ECO:0000244|PDB:4M0E}.
FT   STRAND       46     49       {ECO:0000244|PDB:4M0E}.
FT   STRAND       51     53       {ECO:0000244|PDB:4M0E}.
FT   STRAND       60     67       {ECO:0000244|PDB:4M0E}.
FT   HELIX        74     76       {ECO:0000244|PDB:4M0E}.
FT   STRAND       88     92       {ECO:0000244|PDB:4M0E}.
FT   STRAND       99    101       {ECO:0000244|PDB:4M0E}.
FT   HELIX       112    115       {ECO:0000244|PDB:4M0E}.
FT   STRAND      123    125       {ECO:0000244|PDB:4M0E}.
FT   STRAND      129    137       {ECO:0000244|PDB:4M0E}.
FT   STRAND      143    149       {ECO:0000244|PDB:4M0E}.
FT   TURN        153    155       {ECO:0000244|PDB:4M0E}.
FT   HELIX       162    164       {ECO:0000244|PDB:4M0E}.
FT   HELIX       167    173       {ECO:0000244|PDB:4M0E}.
FT   STRAND      176    180       {ECO:0000244|PDB:4M0E}.
FT   HELIX       185    189       {ECO:0000244|PDB:4M0E}.
FT   STRAND      196    198       {ECO:0000244|PDB:4EY4}.
FT   HELIX       202    217       {ECO:0000244|PDB:4M0E}.
FT   HELIX       218    221       {ECO:0000244|PDB:4M0E}.
FT   STRAND      223    233       {ECO:0000244|PDB:4M0E}.
FT   HELIX       235    244       {ECO:0000244|PDB:4M0E}.
FT   HELIX       247    250       {ECO:0000244|PDB:4M0E}.
FT   STRAND      254    260       {ECO:0000244|PDB:4M0E}.
FT   TURN        266    268       {ECO:0000244|PDB:4M0E}.
FT   HELIX       272    285       {ECO:0000244|PDB:4M0E}.
FT   HELIX       297    306       {ECO:0000244|PDB:4M0E}.
FT   HELIX       309    315       {ECO:0000244|PDB:4M0E}.
FT   HELIX       316    319       {ECO:0000244|PDB:4M0E}.
FT   STRAND      320    322       {ECO:0000244|PDB:4M0E}.
FT   STRAND      333    341       {ECO:0000244|PDB:4M0E}.
FT   HELIX       343    349       {ECO:0000244|PDB:4M0E}.
FT   STRAND      356    362       {ECO:0000244|PDB:4M0E}.
FT   STRAND      364    366       {ECO:0000244|PDB:4EY7}.
FT   HELIX       367    370       {ECO:0000244|PDB:4M0E}.
FT   TURN        371    373       {ECO:0000244|PDB:4M0E}.
FT   STRAND      379    381       {ECO:0000244|PDB:4EY8}.
FT   HELIX       387    397       {ECO:0000244|PDB:4M0E}.
FT   HELIX       403    413       {ECO:0000244|PDB:4M0E}.
FT   HELIX       422    437       {ECO:0000244|PDB:4M0E}.
FT   HELIX       439    451       {ECO:0000244|PDB:4M0E}.
FT   STRAND      455    461       {ECO:0000244|PDB:4M0E}.
FT   HELIX       472    474       {ECO:0000244|PDB:4M0E}.
FT   TURN        478    481       {ECO:0000244|PDB:4M0E}.
FT   HELIX       482    485       {ECO:0000244|PDB:4M0E}.
FT   HELIX       488    490       {ECO:0000244|PDB:4M0E}.
FT   STRAND      492    494       {ECO:0000244|PDB:4BDT}.
FT   HELIX       498    517       {ECO:0000244|PDB:4M0E}.
FT   STRAND      526    528       {ECO:0000244|PDB:2X8B}.
FT   TURN        536    538       {ECO:0000244|PDB:4M0E}.
FT   STRAND      540    547       {ECO:0000244|PDB:4M0E}.
FT   STRAND      550    553       {ECO:0000244|PDB:4M0E}.
FT   HELIX       557    564       {ECO:0000244|PDB:4M0E}.
FT   HELIX       567    572       {ECO:0000244|PDB:4M0E}.
FT   HELIX       580    601       {ECO:0000244|PDB:1VZJ}.
SQ   SEQUENCE   614 AA;  67796 MW;  B9AA84C77831C302 CRC64;
     MRPPQCLLHT PSLASPLLLL LLWLLGGGVG AEGREDAELL VTVRGGRLRG IRLKTPGGPV
     SAFLGIPFAE PPMGPRRFLP PEPKQPWSGV VDATTFQSVC YQYVDTLYPG FEGTEMWNPN
     RELSEDCLYL NVWTPYPRPT SPTPVLVWIY GGGFYSGASS LDVYDGRFLV QAERTVLVSM
     NYRVGAFGFL ALPGSREAPG NVGLLDQRLA LQWVQENVAA FGGDPTSVTL FGESAGAASV
     GMHLLSPPSR GLFHRAVLQS GAPNGPWATV GMGEARRRAT QLAHLVGCPP GGTGGNDTEL
     VACLRTRPAQ VLVNHEWHVL PQESVFRFSF VPVVDGDFLS DTPEALINAG DFHGLQVLVG
     VVKDEGSYFL VYGAPGFSKD NESLISRAEF LAGVRVGVPQ VSDLAAEAVV LHYTDWLHPE
     DPARLREALS DVVGDHNVVC PVAQLAGRLA AQGARVYAYV FEHRASTLSW PLWMGVPHGY
     EIEFIFGIPL DPSRNYTAEE KIFAQRLMRY WANFARTGDP NEPRDPKAPQ WPPYTAGAQQ
     YVSLDLRPLE VRRGLRAQAC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN
     QFDHYSKQDR CSDL
//
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