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 01-MAY-2013, entry version 148.
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 -!- 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.
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. Secreted (By
CC similarity). Cell membrane; Peripheral membrane protein (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Isoform T: Nucleus. Note=Only observed in
CC apoptotic nuclei.
CC -!- SUBCELLULAR LOCATION: Isoform H: Cell membrane; Lipid-anchor, GPI-
CC anchor; Extracellular side (By similarity).
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;
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 -!- 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 -!- 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/";
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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 IPI; IPI00220026; -.
DR IPI; IPI00552259; -.
DR IPI; IPI00844209; -.
DR IPI; IPI00913969; -.
DR PIR; A39256; A39256.
DR RefSeq; NP_000656.1; NM_000665.3.
DR RefSeq; NP_056646.1; NM_015831.2.
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; 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 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; 4EY4; -.
DR PDBsum; 4EY5; -.
DR PDBsum; 4EY6; -.
DR PDBsum; 4EY7; -.
DR PDBsum; 4EY8; -.
DR ProteinModelPortal; P22303; -.
DR DIP; DIP-1119N; -.
DR IntAct; P22303; 6.
DR MINT; MINT-149019; -.
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.
DR Ensembl; ENST00000302913; ENSP00000303211; ENSG00000087085.
DR Ensembl; ENST00000411582; ENSP00000404865; ENSG00000087085.
DR Ensembl; ENST00000412389; ENSP00000394976; ENSG00000087085.
DR Ensembl; ENST00000419336; ENSP00000403474; ENSG00000087085.
DR Ensembl; ENST00000428317; ENSP00000414858; ENSG00000087085.
DR GeneID; 43; -.
DR KEGG; hsa:43; -.
DR UCSC; uc003uxd.3; human.
DR UCSC; uc003uxe.3; human.
DR UCSC; uc003uxh.3; human.
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 HOVERGEN; HBG008839; -.
DR KO; K01049; -.
DR OMA; QYVSLNL; -.
DR OrthoDB; EOG46WZ86; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_13685; Neuronal System.
DR SABIO-RK; P22303; -.
DR BindingDB; P22303; -.
DR ChEMBL; CHEMBL220; -.
DR DrugBank; DB01122; Ambenonium.
DR DrugBank; DB00572; Atropine.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB01245; Decamethonium.
DR DrugBank; DB00944; Demecarium bromide.
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; DB01400; Neostigmine.
DR DrugBank; DB00981; Physostigmine.
DR DrugBank; DB00545; Pyridostigmine.
DR DrugBank; DB00989; Rivastigmine.
DR DrugBank; DB00382; Tacrine.
DR DrugBank; DB01199; Tubocurarine.
DR EvolutionaryTrace; P22303; -.
DR GenomeRNAi; 43; -.
DR NextBio; 173; -.
DR ArrayExpress; P22303; -.
DR Bgee; P22303; -.
DR Genevestigator; P22303; -.
DR GermOnline; ENSG00000087085; Homo sapiens.
DR GO; GO:0031225; C:anchored to 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:0005615; C:extracellular space; IBA:RefGenome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HGNC.
DR GO; GO:0031594; C:neuromuscular junction; IBA:RefGenome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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:0004091; F:carboxylesterase activity; IBA:RefGenome.
DR GO; GO:0005518; F:collagen binding; 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: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:0007517; P:muscle organ development; TAS:UniProtKB.
DR GO; GO:0032223; P:negative regulation of synaptic transmission, cholinergic; IC:HGNC.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; TAS:Reactome.
DR GO; GO:0045212; P:neurotransmitter receptor biosynthetic process; IEA:Compara.
DR GO; GO:0002076; P:osteoblast development; IEP:HGNC.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
DR GO; GO:0050714; P:positive regulation of protein secretion; TAS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IEA:Compara.
DR GO; GO:0031623; P:receptor internalization; IEA:Compara.
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:Compara.
DR GO; GO:0009611; P:response to wounding; TAS:UniProtKB.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Compara.
DR GO; GO:0007416; P:synapse assembly; TAS:UniProtKB.
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 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 Potential.
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...) (Potential).
FT CARBOHYD 381 381 N-linked (GlcNAc...).
FT CARBOHYD 495 495 N-linked (GlcNAc...).
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 /FTId=VSP_035568.
FT VAR_SEQ 575 614 DTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL
FT -> ASEAPSTCPGFTHGEAAPRPGLPLPLLLLHQLLLLFLS
FT HLRRL (in isoform H).
FT /FTId=VSP_001457.
FT VAR_SEQ 575 603 DTLDEAERQWKAEFHRWSSYMVHWKNQFD -> GMQGPAGS
FT AGRRGVGARQCNPSLLPLASE (in isoform R).
FT /FTId=VSP_035569.
FT VAR_SEQ 604 614 Missing (in isoform R).
FT /FTId=VSP_035570.
FT VARIANT 34 34 R -> Q (in dbSNP:rs17881553).
FT /FTId=VAR_021325.
FT VARIANT 135 135 P -> A (in dbSNP:rs17885778).
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 /FTId=VAR_002359.
FT MUTAGEN 206 206 D->N: Misfolding, absence of secretion.
FT MUTAGEN 234 234 S->A: Loss of activity.
FT MUTAGEN 365 365 E->A: Loss of activity.
FT MUTAGEN 435 435 D->N: Misfolding, absence of secretion.
FT MUTAGEN 478 478 H->A: Loss of activity.
FT MUTAGEN 611 611 C->A: Impairment of interchain disulfide
FT bridge formation.
FT CONFLICT 279 279 A -> T (in Ref. 5; BAD97163).
FT CONFLICT 415 415 D -> G (in Ref. 5; BAD97163).
FT CONFLICT 486 486 F -> L (in Ref. 9; AAI43470).
FT HELIX 37 39
FT STRAND 40 43
FT STRAND 46 49
FT STRAND 51 53
FT STRAND 60 67
FT HELIX 74 76
FT STRAND 88 92
FT STRAND 99 101
FT HELIX 112 115
FT STRAND 123 125
FT STRAND 129 137
FT STRAND 143 149
FT TURN 153 155
FT HELIX 162 164
FT HELIX 167 173
FT STRAND 176 180
FT HELIX 185 189
FT STRAND 196 198
FT HELIX 202 217
FT HELIX 218 221
FT STRAND 223 233
FT HELIX 235 244
FT HELIX 247 250
FT STRAND 254 260
FT TURN 266 268
FT HELIX 272 285
FT HELIX 297 305
FT HELIX 309 315
FT HELIX 316 319
FT STRAND 320 323
FT STRAND 333 341
FT HELIX 343 348
FT STRAND 356 362
FT STRAND 364 366
FT HELIX 367 370
FT TURN 371 373
FT STRAND 379 381
FT HELIX 387 397
FT HELIX 403 413
FT HELIX 422 437
FT HELIX 439 451
FT STRAND 455 461
FT HELIX 472 474
FT TURN 478 481
FT HELIX 482 485
FT HELIX 488 490
FT HELIX 498 517
FT STRAND 526 528
FT TURN 536 538
FT STRAND 540 547
FT STRAND 550 553
FT HELIX 557 564
FT HELIX 566 572
FT HELIX 580 601
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
//
