ACES_HUMAN
ID ACES_HUMAN Reviewed; 614 AA.
AC P22303; A4D2E2; B7ZKZ0; D6W5X7; Q16169; Q29S23; Q2M324; Q504V3; Q53F46;
AC Q86TM9; Q86YX9; Q9BXP7;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Acetylcholinesterase {ECO:0000305};
DE Short=AChE;
DE EC=3.1.1.7 {ECO:0000269|PubMed:1517212};
DE Flags: Precursor;
GN Name=ACHE {ECO:0000312|HGNC:HGNC:108};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., 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 in
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., 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., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM H), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-546 (ISOFORMS H/R/T), AND GPI-ANCHOR AT GLY-588
RP (ISOFORM H).
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 project:
RT 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., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [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 erythrocyte
RT acetylcholinesterase.";
RL FEBS Lett. 247:279-282(1989).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-611.
RX PubMed=1748670; DOI=10.1016/s0021-9258(18)54380-5;
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 activity,
RT assembly, and secretion of recombinant human acetylcholinesterase.
RT Expression of acetylcholinesterase Cys-580-->Ala mutant.";
RL J. Biol. Chem. 266:23977-23984(1991).
RN [13]
RP FUNCTION, MUTAGENESIS OF ASP-206; SER-234; GLU-365; ASP-435 AND HIS-478,
RP AND CATALYTIC ACTIVITY.
RX PubMed=1517212; DOI=10.1016/s0021-9258(19)37091-7;
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 SK-N-SH
RT 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 models.";
RL J. Mol. Graph. Model. 15:318-327(1997).
RN [16] {ECO:0007744|PDB:1B41, ECO:0007744|PDB:1F8U}
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 32-614 IN COMPLEX WITH
RP FASCICULIN-2, GLYCOSYLATION AT ASN-381, AND DISULFIDE BOND.
RX PubMed=11053835; DOI=10.1107/s0907444900010659;
RA Kryger G., Harel M., Giles K., Toker L., Velan B., Lazar A., Kronman C.,
RA Barak D., Ariel N., Shafferman A., Silman I., Sussman J.L.;
RT "Structures of recombinant native and E202Q mutant human
RT acetylcholinesterase complexed with the snake-venom toxin fasciculin-II.";
RL Acta Crystallogr. D 56:1385-1394(2000).
RN [17] {ECO:0007744|PDB:1VZJ}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 575-614 IN COMPLEX WITH COLQ.
RX PubMed=15526038; DOI=10.1038/sj.emboj.7600425;
RA Dvir H., Harel M., Bon S., Liu W.-Q., Vidal M., Garbay C., Sussman J.L.,
RA Massoulie J., Silman I.;
RT "The synaptic acetylcholinesterase tetramer assembles around a polyproline
RT II helix.";
RL EMBO J. 23:4394-4405(2004).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF COMPLEX WITH FASCICULIN-2,
RP DISULFIDE BOND, AND GLYCOSYLATION AT ASN-381.
RX PubMed=20408548; DOI=10.1021/jm901853b;
RA Carletti E., Colletier J.P., Dupeux F., Trovaslet M., Masson P., Nachon F.;
RT "Structural evidence that human acetylcholinesterase inhibited by tabun
RT ages through O-dealkylation.";
RL J. Med. Chem. 53:4002-4008(2010).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 35-573 IN COMPLEX WITH
RP FASCICULIN-2; HUPERZINE A; GALANTAMINE AND DONEPEZIL, GLYCOSYLATION AT
RP ASN-296; ASN-381 AND ASN-495, AND DISULFIDE BOND.
RX PubMed=23035744; DOI=10.1021/jm300871x;
RA Cheung J., Rudolph M.J., Burshteyn F., Cassidy M.S., Gary E.N., Love J.,
RA Franklin M.C., Height J.J.;
RT "Structures of human acetylcholinesterase in complex with pharmacologically
RT important ligands.";
RL J. Med. Chem. 55:10282-10286(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 36-598 IN COMPLEX WITH
RP FASCICULIN-2 AND HUPRINE W, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-381.
RX PubMed=23679855; DOI=10.1042/bj20130013;
RA Nachon F., Carletti E., Ronco C., Trovaslet M., Nicolet Y., Jean L.,
RA Renard P.Y.;
RT "Crystal structures of human cholinesterases in complex with huprine W and
RT tacrine: elements of specificity for anti-Alzheimer's drugs targeting
RT acetyl- and butyryl-cholinesterase.";
RL Biochem. J. 453:393-399(2013).
RN [21]
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: Hydrolyzes rapidly the acetylcholine neurotransmitter
CC released into the synaptic cleft allowing to terminate the signal
CC transduction at the neuromuscular junction. 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:
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 Evidence={ECO:0000269|PubMed:1517212};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17562;
CC Evidence={ECO:0000305|PubMed:1517212};
CC -!- SUBUNIT: Interacts with PRIMA1. The interaction with PRIMA1 is required
CC to anchor it to the basal lamina of cells and organize into tetramers
CC (By similarity). Isoform H generates GPI-anchored dimers; disulfide
CC linked. Isoform T generates multiple structures, ranging from monomers
CC and dimers to collagen-tailed and hydrophobic-tailed forms, in which
CC catalytic tetramers are associated with anchoring proteins that attach
CC them to the basal lamina or to cell membranes. In the collagen-tailed
CC forms, isoform T subunits are associated with a specific collagen,
CC COLQ, which triggers the formation of isoform T tetramers, from
CC monomers and dimers. Isoform R may be monomeric. {ECO:0000250,
CC ECO:0000269|PubMed:11053835, ECO:0000269|PubMed:15526038}.
CC -!- INTERACTION:
CC P22303; Q9Y215: COLQ; NbExp=2; IntAct=EBI-1637793, EBI-1637847;
CC P22303; P06733: ENO1; NbExp=2; IntAct=EBI-1637793, EBI-353877;
CC P22303; P63244: RACK1; NbExp=2; IntAct=EBI-1637793, EBI-296739;
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:11985878,
CC ECO:0000269|PubMed:1748670}. Secreted {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral 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}; Lipid-
CC anchor, GPI-anchor {ECO:0000250}; Extracellular side {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 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 -!- 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 mutation
CC database;
CC URL="https://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="https://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 and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ACHEID44317ch7q22.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; 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_000665.4. [P22303-1]
DR RefSeq; NP_001269378.1; NM_001282449.1. [P22303-3]
DR RefSeq; NP_001289550.1; NM_001302621.1. [P22303-2]
DR RefSeq; NP_001289551.1; NM_001302622.1. [P22303-1]
DR RefSeq; NP_056646.1; NM_015831.2.
DR RefSeq; XP_006716058.1; XM_006715995.2.
DR RefSeq; XP_011514530.1; XM_011516228.2.
DR RefSeq; XP_011514531.1; XM_011516229.2.
DR PDB; 1B41; X-ray; 2.76 A; A=36-574.
DR PDB; 1F8U; X-ray; 2.90 A; A=32-614.
DR PDB; 1VZJ; X-ray; 2.35 A; A/B/C/D/E/F/G/H=575-614.
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 PDB; 4PQE; X-ray; 2.90 A; A=32-574.
DR PDB; 5FOQ; X-ray; 2.30 A; A/B=32-576.
DR PDB; 5FPQ; X-ray; 2.40 A; A/B=33-574.
DR PDB; 5HF5; X-ray; 2.15 A; A/B=33-574.
DR PDB; 5HF6; X-ray; 2.30 A; A/B=33-574.
DR PDB; 5HF8; X-ray; 2.80 A; A/B=33-574.
DR PDB; 5HF9; X-ray; 2.20 A; A/B=33-574.
DR PDB; 5HFA; X-ray; 2.20 A; A/B=33-574.
DR PDB; 5HQ3; X-ray; 2.60 A; A=32-578, B=32-579.
DR PDB; 6CQT; X-ray; 2.27 A; A/B=33-574.
DR PDB; 6CQU; X-ray; 2.31 A; A/B=33-574.
DR PDB; 6CQV; X-ray; 2.60 A; A/B=33-574.
DR PDB; 6CQW; X-ray; 2.28 A; A/B=33-574.
DR PDB; 6CQX; X-ray; 2.40 A; A/B=33-574.
DR PDB; 6CQY; X-ray; 2.45 A; A/B=33-574.
DR PDB; 6CQZ; X-ray; 2.22 A; A/B=33-574.
DR PDB; 6F25; X-ray; 3.05 A; A/B=36-574.
DR PDB; 6NEA; X-ray; 2.42 A; A/B=33-574.
DR PDB; 6NTG; X-ray; 2.65 A; A/B=33-574.
DR PDB; 6NTH; X-ray; 2.42 A; A/B=33-574.
DR PDB; 6NTK; X-ray; 2.41 A; A/B=33-574.
DR PDB; 6NTL; X-ray; 2.25 A; A/B=33-574.
DR PDB; 6NTM; X-ray; 2.55 A; A/B=33-574.
DR PDB; 6NTN; X-ray; 2.70 A; A/B=33-574.
DR PDB; 6NTO; X-ray; 2.05 A; A/B=33-574.
DR PDB; 6O4W; X-ray; 2.35 A; A/B=32-578.
DR PDB; 6O4X; X-ray; 2.30 A; A/B=32-578.
DR PDB; 6O50; X-ray; 2.35 A; A/B=32-578.
DR PDB; 6O52; X-ray; 3.20 A; A/B=32-578.
DR PDB; 6O5R; X-ray; 2.80 A; A/B=32-578.
DR PDB; 6O5S; X-ray; 2.80 A; A/B=32-578.
DR PDB; 6O5V; X-ray; 2.15 A; A/B=32-578.
DR PDB; 6O66; X-ray; 2.45 A; A/B=32-578.
DR PDB; 6O69; X-ray; 2.08 A; A=33-574.
DR PDB; 6U34; X-ray; 2.40 A; A/B=35-578.
DR PDB; 6U37; X-ray; 2.25 A; A/B=32-578.
DR PDB; 6U3P; X-ray; 3.00 A; A/B=32-578.
DR PDB; 6WUV; X-ray; 2.63 A; A/B=33-574.
DR PDB; 6WUY; X-ray; 2.46 A; A/B=33-574.
DR PDB; 6WUZ; X-ray; 2.25 A; A/B=33-574.
DR PDB; 6WV1; X-ray; 2.37 A; A/B=33-574.
DR PDB; 6WVC; X-ray; 2.60 A; A/B=33-574.
DR PDB; 6WVO; X-ray; 2.19 A; A/B=33-574.
DR PDB; 6WVP; X-ray; 2.31 A; A/B=33-574.
DR PDB; 6WVQ; X-ray; 2.29 A; A/B=33-574.
DR PDB; 6ZWE; X-ray; 3.00 A; A/B=33-574.
DR PDB; 7D9O; X-ray; 2.45 A; A/B=32-574.
DR PDB; 7D9P; X-ray; 2.85 A; A/B=32-574.
DR PDB; 7D9Q; X-ray; 2.66 A; A/B=32-574.
DR PDB; 7E3D; X-ray; 2.50 A; A/B=35-574.
DR PDB; 7E3H; X-ray; 2.45 A; A/B=35-574.
DR PDB; 7E3I; X-ray; 2.85 A; A/B=35-574.
DR PDB; 7RB5; X-ray; 2.80 A; A=32-578.
DR PDB; 7RB6; X-ray; 2.40 A; A/B=32-578.
DR PDB; 7RB7; X-ray; 2.60 A; A/B=32-578.
DR PDBsum; 1B41; -.
DR PDBsum; 1F8U; -.
DR PDBsum; 1VZJ; -.
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 PDBsum; 4PQE; -.
DR PDBsum; 5FOQ; -.
DR PDBsum; 5FPQ; -.
DR PDBsum; 5HF5; -.
DR PDBsum; 5HF6; -.
DR PDBsum; 5HF8; -.
DR PDBsum; 5HF9; -.
DR PDBsum; 5HFA; -.
DR PDBsum; 5HQ3; -.
DR PDBsum; 6CQT; -.
DR PDBsum; 6CQU; -.
DR PDBsum; 6CQV; -.
DR PDBsum; 6CQW; -.
DR PDBsum; 6CQX; -.
DR PDBsum; 6CQY; -.
DR PDBsum; 6CQZ; -.
DR PDBsum; 6F25; -.
DR PDBsum; 6NEA; -.
DR PDBsum; 6NTG; -.
DR PDBsum; 6NTH; -.
DR PDBsum; 6NTK; -.
DR PDBsum; 6NTL; -.
DR PDBsum; 6NTM; -.
DR PDBsum; 6NTN; -.
DR PDBsum; 6NTO; -.
DR PDBsum; 6O4W; -.
DR PDBsum; 6O4X; -.
DR PDBsum; 6O50; -.
DR PDBsum; 6O52; -.
DR PDBsum; 6O5R; -.
DR PDBsum; 6O5S; -.
DR PDBsum; 6O5V; -.
DR PDBsum; 6O66; -.
DR PDBsum; 6O69; -.
DR PDBsum; 6U34; -.
DR PDBsum; 6U37; -.
DR PDBsum; 6U3P; -.
DR PDBsum; 6WUV; -.
DR PDBsum; 6WUY; -.
DR PDBsum; 6WUZ; -.
DR PDBsum; 6WV1; -.
DR PDBsum; 6WVC; -.
DR PDBsum; 6WVO; -.
DR PDBsum; 6WVP; -.
DR PDBsum; 6WVQ; -.
DR PDBsum; 6ZWE; -.
DR PDBsum; 7D9O; -.
DR PDBsum; 7D9P; -.
DR PDBsum; 7D9Q; -.
DR PDBsum; 7E3D; -.
DR PDBsum; 7E3H; -.
DR PDBsum; 7E3I; -.
DR PDBsum; 7RB5; -.
DR PDBsum; 7RB6; -.
DR PDBsum; 7RB7; -.
DR AlphaFoldDB; P22303; -.
DR SASBDB; P22303; -.
DR SMR; P22303; -.
DR BioGRID; 106561; 4.
DR DIP; DIP-1119N; -.
DR ELM; P22303; -.
DR IntAct; P22303; 8.
DR MINT; P22303; -.
DR STRING; 9606.ENSP00000303211; -.
DR BindingDB; P22303; -.
DR ChEMBL; CHEMBL220; -.
DR DrugBank; DB07846; (3,4,8b-Trimethyl-3-oxido-2,3a-dihydro-1H-pyrrolo[2,3-b]indol-3-ium-7-yl) N-(2-ethylphenyl)carbamate.
DR DrugBank; DB02673; (4aS,6R,8aS)-11-[8-(1,3-Dioxo-1,3-dihydro-2H-isoindol-2-yl)octyl]-6-hydroxy-3-methoxy-5,6,9,10-tetrahydro-4aH-[1]benzofuro[3a,3,2-ef][2]benzazepin-11-ium.
DR DrugBank; DB04617; (9S)-9-[(8-AMMONIOOCTYL)AMINO]-1,2,3,4,9,10-HEXAHYDROACRIDINIUM.
DR DrugBank; DB04614; (R)-tacrine(10)-hupyridone.
DR DrugBank; DB04615; (S)-tacrine(10)-hupyridone.
DR DrugBank; DB07756; 1-[3-({[(4-AMINO-5-FLUORO-2-METHYLQUINOLIN-3-YL)METHYL]THIO}METHYL)PHENYL]-2,2,2-TRIFLUOROETHANE-1,1-DIOL.
DR DrugBank; DB07701; 1-BENZYL-4-[(5,6-DIMETHOXY-1-INDANON-2-YL)METHYL]PIPERIDINE.
DR DrugBank; DB02404; 1-Deoxy-1-Thio-Heptaethylene Glycol.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB08615; 2-[4-(DIMETHYLAMINO)PHENYL]-6-HYDROXY-3-METHYL-1,3-BENZOTHIAZOL-3-IUM.
DR DrugBank; DB02343; 3,6,9,12,15-Pentaoxaheptadecane.
DR DrugBank; DB02226; 3,8-Diamino-6-Phenyl-5-[6-[1-[2-[(1,2,3,4-Tetrahydro-9-Acridinyl)Amino]Ethyl]-1h-1,2,3-Triazol-4-Yl]Hexyl]-Phenanthridinium.
DR DrugBank; DB03005; 3,8-Diamino-6-Phenyl-5-[6-[1-[2-[(1,2,3,4-Tetrahydro-9-Acridinyl)Amino]Ethyl]-1h-1,2,3-Triazol-5-Yl]Hexyl]-Phenanthridinium.
DR DrugBank; DB04114; 3-Chloro-9-Ethyl-6,7,8,9,10,11-Hexahydro-7,11-Methanocycloocta[B]Quinolin-12-Amine.
DR DrugBank; DB03128; Acetylcholine.
DR DrugBank; DB01122; Ambenonium.
DR DrugBank; DB03283; beta-L-fucose.
DR DrugBank; DB00411; Carbamoylcholine.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR DrugBank; DB01245; Decamethonium.
DR DrugBank; DB00944; Demecarium.
DR DrugBank; DB08357; Diethylene glycol diethyl ether.
DR DrugBank; DB08996; Dimetacrine.
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; DB06525; Ganstigmine.
DR DrugBank; DB04864; Huperzine A.
DR DrugBank; DB03348; Huperzine B.
DR DrugBank; DB07555; Hydroxy(oxo)(2-{(1S)-2,2,2-trifluoro-1-[2-(trimethylarsonio)ethoxy]ethyl}phenyl)ammonium.
DR DrugBank; DB00677; Isoflurophate.
DR DrugBank; DB04924; Itopride.
DR DrugBank; DB03359; M-(N,N,N-Trimethylammonio)-2,2,2-Trifluoro-1,1-Dihydroxyethylbenzene.
DR DrugBank; DB00358; Mefloquine.
DR DrugBank; DB00940; Methantheline.
DR DrugBank; DB02825; Methylphosphinate.
DR DrugBank; DB02845; Methylphosphinic Acid.
DR DrugBank; DB08167; Methylthioninium.
DR DrugBank; DB04021; MF268.
DR DrugBank; DB00805; Minaprine.
DR DrugBank; DB01805; Monoisopropylphosphorylserine.
DR DrugBank; DB03740; N-acetyl-alpha-D-glucosamine.
DR DrugBank; DB04556; NAP-226-90.
DR DrugBank; DB01400; Neostigmine.
DR DrugBank; DB04892; Phenserine.
DR DrugBank; DB00981; Physostigmine.
DR DrugBank; DB00733; Pralidoxime.
DR DrugBank; DB02166; Propidium.
DR DrugBank; DB00545; Pyridostigmine.
DR DrugBank; DB00863; Ranitidine.
DR DrugBank; DB00989; Rivastigmine.
DR DrugBank; DB00382; Tacrine.
DR DrugBank; DB04616; TACRINE(8)-4-AMINOQUINOLINE.
DR DrugBank; DB01199; Tubocurarine.
DR DrugBank; DB13503; Tyrothricin.
DR DrugBank; DB04859; Zanapezil.
DR DrugCentral; P22303; -.
DR GuidetoPHARMACOLOGY; 2465; -.
DR ESTHER; human-ACHE; AChE.
DR MEROPS; S09.979; -.
DR GlyGen; P22303; 3 sites.
DR iPTMnet; P22303; -.
DR PhosphoSitePlus; P22303; -.
DR BioMuta; ACHE; -.
DR DMDM; 113037; -.
DR SWISS-2DPAGE; P22303; -.
DR jPOST; P22303; -.
DR MassIVE; P22303; -.
DR PaxDb; P22303; -.
DR PeptideAtlas; P22303; -.
DR PRIDE; P22303; -.
DR ProteomicsDB; 53971; -. [P22303-1]
DR ProteomicsDB; 53972; -. [P22303-2]
DR ProteomicsDB; 53973; -. [P22303-3]
DR ProteomicsDB; 53974; -. [P22303-4]
DR Antibodypedia; 16701; 766 antibodies from 43 providers.
DR DNASU; 43; -.
DR Ensembl; ENST00000241069.11; ENSP00000241069.5; ENSG00000087085.16. [P22303-1]
DR Ensembl; ENST00000302913.8; ENSP00000303211.4; ENSG00000087085.16. [P22303-2]
DR Ensembl; ENST00000411582.4; ENSP00000404865.1; ENSG00000087085.16. [P22303-2]
DR Ensembl; ENST00000412389.5; ENSP00000394976.1; ENSG00000087085.16. [P22303-1]
DR Ensembl; ENST00000419336.6; ENSP00000403474.2; ENSG00000087085.16. [P22303-3]
DR Ensembl; ENST00000428317.7; ENSP00000414858.1; ENSG00000087085.16. [P22303-1]
DR GeneID; 43; -.
DR KEGG; hsa:43; -.
DR MANE-Select; ENST00000241069.11; ENSP00000241069.5; NM_000665.5; NP_000656.1.
DR UCSC; uc003uxd.4; human. [P22303-1]
DR CTD; 43; -.
DR DisGeNET; 43; -.
DR GeneCards; ACHE; -.
DR HGNC; HGNC:108; ACHE.
DR HPA; ENSG00000087085; Group enriched (brain, skeletal muscle, tongue).
DR MalaCards; ACHE; -.
DR MIM; 100740; gene+phenotype.
DR MIM; 112100; phenotype.
DR neXtProt; NX_P22303; -.
DR OpenTargets; ENSG00000087085; -.
DR PharmGKB; PA20; -.
DR VEuPathDB; HostDB:ENSG00000087085; -.
DR eggNOG; KOG4389; Eukaryota.
DR GeneTree; ENSGT00940000157637; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; P22303; -.
DR OMA; CDHLVAP; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P22303; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.7; 2681.
DR BRENDA; 3.5.1.13; 2681.
DR PathwayCommons; P22303; -.
DR Reactome; R-HSA-112311; Neurotransmitter clearance.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR SABIO-RK; P22303; -.
DR SignaLink; P22303; -.
DR SIGNOR; P22303; -.
DR BioGRID-ORCS; 43; 118 hits in 1086 CRISPR screens.
DR ChiTaRS; ACHE; human.
DR EvolutionaryTrace; P22303; -.
DR GeneWiki; Acetylcholinesterase; -.
DR GenomeRNAi; 43; -.
DR Pharos; P22303; Tclin.
DR PRO; PR:P22303; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P22303; protein.
DR Bgee; ENSG00000087085; Expressed in hindlimb stylopod muscle and 128 other tissues.
DR ExpressionAtlas; P22303; baseline and differential.
DR Genevisible; P22303; HS.
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:0005604; C:basement membrane; NAS:HGNC-UCL.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IDA:HGNC-UCL.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HGNC-UCL.
DR GO; GO:0016020; C:membrane; IDA:HGNC-UCL.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IDA:HGNC-UCL.
DR GO; GO:0043083; C:synaptic cleft; IEA:GOC.
DR GO; GO:0042166; F:acetylcholine binding; IDA:HGNC-UCL.
DR GO; GO:0003990; F:acetylcholinesterase activity; IDA:HGNC-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; TAS:UniProtKB.
DR GO; GO:0004104; F:cholinesterase activity; IDA:HGNC-UCL.
DR GO; GO:0005518; F:collagen binding; IDA:HGNC-UCL.
DR GO; GO:0016787; F:hydrolase activity; IDA:HGNC-UCL.
DR GO; GO:0043236; F:laminin binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:HGNC-UCL.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0017171; F:serine hydrolase activity; IDA:HGNC-UCL.
DR GO; GO:0006581; P:acetylcholine catabolic process; IDA:HGNC-UCL.
DR GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; NAS:UniProtKB.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; TAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:HGNC-UCL.
DR GO; GO:0032223; P:negative regulation of synaptic transmission, cholinergic; IC:HGNC-UCL.
DR GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR GO; GO:0002076; P:osteoblast development; IEP:HGNC-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0050714; P:positive regulation of protein secretion; TAS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR GO; GO:0001919; P:regulation of receptor recycling; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; TAS:UniProtKB.
DR DisProt; DP01964; -.
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 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; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation; Nucleus;
KW Reference proteome; Secreted; Serine esterase; Signal; Synapse.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..614
FT /note="Acetylcholinesterase"
FT /id="PRO_0000008587"
FT ACT_SITE 234
FT /note="Acyl-ester intermediate"
FT ACT_SITE 365
FT /note="Charge relay system"
FT ACT_SITE 478
FT /note="Charge relay system"
FT BINDING 117
FT /ligand="galanthamine"
FT /ligand_id="ChEBI:CHEBI:178021"
FT /evidence="ECO:0007744|PDB:4EY6"
FT BINDING 117
FT /ligand="huperzine A"
FT /ligand_id="ChEBI:CHEBI:178022"
FT /evidence="ECO:0007744|PDB:4EY5"
FT BINDING 153
FT /ligand="huprine W"
FT /ligand_id="ChEBI:CHEBI:188158"
FT /evidence="ECO:0007744|PDB:4BDT"
FT BINDING 164
FT /ligand="huperzine A"
FT /ligand_id="ChEBI:CHEBI:178022"
FT /evidence="ECO:0007744|PDB:4EY5"
FT BINDING 233..234
FT /ligand="galanthamine"
FT /ligand_id="ChEBI:CHEBI:178021"
FT /evidence="ECO:0007744|PDB:4EY6"
FT BINDING 234
FT /ligand="huprine W"
FT /ligand_id="ChEBI:CHEBI:188158"
FT /evidence="ECO:0007744|PDB:4BDT"
FT BINDING 368
FT /ligand="galanthamine"
FT /ligand_id="ChEBI:CHEBI:178021"
FT /evidence="ECO:0007744|PDB:4EY6"
FT BINDING 368
FT /ligand="huperzine A"
FT /ligand_id="ChEBI:CHEBI:178022"
FT /evidence="ECO:0007744|PDB:4EY5"
FT BINDING 470
FT /ligand="huprine W"
FT /ligand_id="ChEBI:CHEBI:188158"
FT /evidence="ECO:0007744|PDB:4BDT"
FT BINDING 478
FT /ligand="huprine W"
FT /ligand_id="ChEBI:CHEBI:188158"
FT /evidence="ECO:0007744|PDB:4BDT"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23035744,
FT ECO:0007744|PDB:4EY4, ECO:0007744|PDB:4EY5,
FT ECO:0007744|PDB:4EY6, ECO:0007744|PDB:4EY7"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11053835,
FT ECO:0000269|PubMed:20408548, ECO:0000269|PubMed:23035744,
FT ECO:0000269|PubMed:23679855, ECO:0007744|PDB:1B41,
FT ECO:0007744|PDB:1F8U, ECO:0007744|PDB:2X8B,
FT ECO:0007744|PDB:4BDT, ECO:0007744|PDB:4EY4,
FT ECO:0007744|PDB:4EY5, ECO:0007744|PDB:4EY6,
FT ECO:0007744|PDB:4EY7, ECO:0007744|PDB:4EY8"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23035744,
FT ECO:0007744|PDB:4EY8"
FT DISULFID 100..127
FT DISULFID 288..303
FT DISULFID 440..560
FT DISULFID 611
FT /note="Interchain"
FT VAR_SEQ 357..444
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_035568"
FT VAR_SEQ 575..614
FT /note="DTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL -> ASEAPSTC
FT PGFTHGEAAPRPGLPLPLLLLHQLLLLFLSHLRRL (in isoform H)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8299725"
FT /id="VSP_001457"
FT VAR_SEQ 575..603
FT /note="DTLDEAERQWKAEFHRWSSYMVHWKNQFD -> GMQGPAGSAGRRGVGARQC
FT NPSLLPLASE (in isoform R)"
FT /evidence="ECO:0000303|PubMed:8299725"
FT /id="VSP_035569"
FT VAR_SEQ 604..614
FT /note="Missing (in isoform R)"
FT /evidence="ECO:0000303|PubMed:8299725"
FT /id="VSP_035570"
FT VARIANT 34
FT /note="R -> Q (in dbSNP:rs17881553)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_021325"
FT VARIANT 135
FT /note="P -> A (in dbSNP:rs17885778)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_021326"
FT VARIANT 333
FT /note="V -> E (in dbSNP:rs8286)"
FT /id="VAR_011934"
FT VARIANT 353
FT /note="H -> N (in Yt(b) antigen; dbSNP:rs1799805)"
FT /evidence="ECO:0000269|PubMed:8488842, ECO:0000269|Ref.6"
FT /id="VAR_002359"
FT MUTAGEN 206
FT /note="D->N: Misfolding, absence of secretion."
FT /evidence="ECO:0000269|PubMed:1517212"
FT MUTAGEN 234
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1517212"
FT MUTAGEN 365
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1517212"
FT MUTAGEN 435
FT /note="D->N: Misfolding, absence of secretion."
FT /evidence="ECO:0000269|PubMed:1517212"
FT MUTAGEN 478
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1517212"
FT MUTAGEN 611
FT /note="C->A: Impairment of interchain disulfide bridge
FT formation."
FT /evidence="ECO:0000269|PubMed:1748670"
FT CONFLICT 279
FT /note="A -> T (in Ref. 5; BAD97163)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="D -> G (in Ref. 5; BAD97163)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="F -> L (in Ref. 9; AAI43470)"
FT /evidence="ECO:0000305"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:4M0E"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4EY4"
FT HELIX 202..217
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:4M0E"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:4M0E"
FT TURN 286..290
FT /evidence="ECO:0007829|PDB:6O5R"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 309..315
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6O69"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:4M0E"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:6CQW"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:6ZWE"
FT HELIX 422..437
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 439..451
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:4M0E"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:4BDT"
FT HELIX 498..517
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:6WVQ"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 540..547
FT /evidence="ECO:0007829|PDB:4M0E"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 557..564
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 567..572
FT /evidence="ECO:0007829|PDB:4M0E"
FT HELIX 580..601
FT /evidence="ECO:0007829|PDB:1VZJ"
FT LIPID P22303-2:588
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT P22303-2:592
FT /note="P -> R (in Ref. 9; AAI43470)"
FT /evidence="ECO:0000305"
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
