GenomeNet

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   19-MAR-2014, entry version 157.
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/";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ACHEID44317ch7q22.html";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   PIR; A39256; A39256.
DR   RefSeq; NP_000656.1; NM_000665.3.
DR   RefSeq; NP_001269378.1; NM_001282449.1.
DR   RefSeq; NP_056646.1; NM_015831.2.
DR   RefSeq; XP_005250414.1; XM_005250357.1.
DR   RefSeq; XP_005250415.1; XM_005250358.1.
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; 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   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   HOVERGEN; HBG008839; -.
DR   KO; K01049; -.
DR   OMA; RPPWCPL; -.
DR   OrthoDB; EOG789C9R; -.
DR   TreeFam; TF315470; -.
DR   Reactome; REACT_111217; Metabolism.
DR   Reactome; REACT_13685; Neuronal System.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   SABIO-RK; P22303; -.
DR   EvolutionaryTrace; P22303; -.
DR   GeneWiki; Acetylcholinesterase; -.
DR   GenomeRNAi; 43; -.
DR   NextBio; 173; -.
DR   PRO; PR:P22303; -.
DR   ArrayExpress; P22303; -.
DR   Bgee; P22303; -.
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: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: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: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:Ensembl.
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: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: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    306
FT   HELIX       309    315
FT   HELIX       316    319
FT   STRAND      320    322
FT   STRAND      333    341
FT   HELIX       343    349
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   STRAND      492    494
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       567    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
//
DBGET integrated database retrieval system