CHLE_HUMAN
ID CHLE_HUMAN Reviewed; 602 AA.
AC P06276; A8K7P8;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Cholinesterase;
DE EC=3.1.1.8;
DE AltName: Full=Acylcholine acylhydrolase;
DE AltName: Full=Butyrylcholine esterase;
DE AltName: Full=Choline esterase II;
DE AltName: Full=Pseudocholinesterase;
DE Flags: Precursor;
GN Name=BCHE; Synonyms=CHE1;
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].
RC TISSUE=Fetus;
RX PubMed=3035536; DOI=10.1073/pnas.84.11.3555;
RA Prody C.A., Zevin-Sonkin D., Gnatt A., Goldberg O., Soreq H.;
RT "Isolation and characterization of full-length cDNA clones coding for
RT cholinesterase from fetal human tissues.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3555-3559(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3477799; DOI=10.1073/pnas.84.19.6682;
RA McTiernan C., Adkins S., Chatonnet A., Vaughan T.A., Bartels C.F., Kott M.,
RA Rosenberry T.L., la Du B.N., Lockridge O.;
RT "Brain cDNA clone for human cholinesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6682-6686(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2322535; DOI=10.1021/bi00453a015;
RA Arpagaus M., Kott M., Vatsis K.P., Bartels C.F., la Du B.N., Lockridge O.;
RT "Structure of the gene for human butyrylcholinesterase. Evidence for a
RT single copy.";
RL Biochemistry 29:124-131(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-567.
RC TISSUE=Stomach;
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].
RC TISSUE=Skin;
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 [6]
RP PROTEIN SEQUENCE OF 29-602, AND SIGNAL SEQUENCE CLEAVAGE SITE.
RC TISSUE=Plasma;
RX PubMed=3542989; DOI=10.1016/s0021-9258(19)75818-9;
RA Lockridge O., Bartels C.F., Vaughan T.A., Wong C.K., Norton S.E.,
RA Johnson L.L.;
RT "Complete amino acid sequence of human serum cholinesterase.";
RL J. Biol. Chem. 262:549-557(1987).
RN [7]
RP PROTEIN SEQUENCE OF 29-37; 43-68; 71-163; 167-290; 294-522; 528-543 AND
RP 549-602, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION, AND
RP HOMOTETRAMERIZATION.
RC TISSUE=Plasma;
RX PubMed=20946535; DOI=10.1111/j.1423-0410.2010.01415.x;
RA Weber A., Butterweck H., Mais-Paul U., Teschner W., Lei L., Muchitsch E.M.,
RA Kolarich D., Altmann F., Ehrlich H.J., Schwarz H.P.;
RT "Biochemical, molecular and preclinical characterization of a double-virus-
RT reduced human butyrylcholinesterase preparation designed for clinical
RT use.";
RL Vox Sang. 100:285-297(2011).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX PubMed=3115973; DOI=10.1016/s0021-9258(18)45149-6;
RA Lockridge O., Adkins S., la Du B.N.;
RT "Location of disulfide bonds within the sequence of human serum
RT cholinesterase.";
RL J. Biol. Chem. 262:12945-12952(1987).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509 AND ASN-514.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-85; ASN-369; ASN-483;
RP ASN-509 AND ASN-514.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP GLYCOSYLATION AT ASN-45; ASN-85; ASN-134; ASN-269; ASN-284; ASN-369 AND
RP ASN-483, AND CHARACTERIZATION OF GLYCOSYLATION.
RX PubMed=18203274; DOI=10.1002/pmic.200700720;
RA Kolarich D., Weber A., Pabst M., Stadlmann J., Teschner W., Ehrlich H.,
RA Schwarz H.P., Altmann F.;
RT "Glycoproteomic characterization of butyrylcholinesterase from human
RT plasma.";
RL Proteomics 8:254-263(2008).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SUBUNIT.
RX PubMed=19542320; DOI=10.1124/mol.109.055665;
RA Chilukuri N., Duysen E.G., Parikh K., diTargiani R., Doctor B.P.,
RA Lockridge O., Saxena A.;
RT "Adenovirus-transduced human butyrylcholinesterase in mouse blood functions
RT as a bioscavenger of chemical warfare nerve agents.";
RL Mol. Pharmacol. 76:612-617(2009).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134 AND ASN-284.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [14]
RP GLYCOSYLATION AT ASN-284.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19452557; DOI=10.1002/prot.22442;
RA Amitay M., Shurki A.;
RT "The structure of G117H mutant of butyrylcholinesterase: nerve agents
RT scavenger.";
RL Proteins 77:370-377(2009).
RN [16]
RP PHOSPHORYLATION AT SER-226.
RX PubMed=22444575; DOI=10.1016/j.aca.2012.02.023;
RA Aryal U.K., Lin C.T., Kim J.S., Heibeck T.H., Wang J., Qian W.J., Lin Y.;
RT "Identification of phosphorylated butyrylcholinesterase in human plasma
RT using immunoaffinity purification and mass spectrometry.";
RL Anal. Chim. Acta 723:68-75(2012).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT BCHED ASP-232.
RX PubMed=25054547; DOI=10.1371/journal.pone.0101552;
RA Delacour H., Lushchekina S., Mabboux I., Bousquet A., Ceppa F.,
RA Schopfer L.M., Lockridge O., Masson P.;
RT "Characterization of a novel BCHE 'silent' allele: point mutation
RT (p.Val204Asp) causes loss of activity and prolonged apnea with
RT suxamethonium.";
RL PLoS ONE 9:E101552-E101552(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH SUBSTRATE,
RP SUBUNIT, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513,
RP DISULFIDE BONDS, AND ACTIVE SITE.
RX PubMed=12869558; DOI=10.1074/jbc.m210241200;
RA Nicolet Y., Lockridge O., Masson P., Fontecilla-Camps J.C., Nachon F.;
RT "Crystal structure of human butyrylcholinesterase and of its complexes with
RT substrate and products.";
RL J. Biol. Chem. 278:41141-41147(2003).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH
RP ECHOTHIOPHATE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-85; ASN-134;
RP ASN-269; ASN-369 AND ASN-513.
RX PubMed=15667209; DOI=10.1021/bi048238d;
RA Nachon F., Asojo O.A., Borgstahl G.E.O., Masson P., Lockridge O.;
RT "Role of water in aging of human butyrylcholinesterase inhibited by
RT echothiophate: the crystal structure suggests two alternative mechanisms of
RT aging.";
RL Biochemistry 44:1154-1162(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT
RP ASN-85; ASN-134; ASN-369 AND ASN-513, AND SUBUNIT.
RX PubMed=17768338; DOI=10.1107/s1744309107037335;
RA Ngamelue M.N., Homma K., Lockridge O., Asojo O.A.;
RT "Crystallization and X-ray structure of full-length recombinant human
RT butyrylcholinesterase.";
RL Acta Crystallogr. F 63:723-727(2007).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 29-557 IN COMPLEX WITH MERCURY
RP IONS AND BUTANOIC ACID, DISULFIDE BONDS, GLYCOSYLATION AT ASN-85; ASN-134;
RP ASN-269; ASN-369 AND ASN-513, AND ACTIVITY REGULATION.
RX PubMed=17355286; DOI=10.1111/j.1742-4658.2007.05732.x;
RA Frasco M.F., Colletier J.-P., Weik M., Carvalho F., Guilhermino L.,
RA Stojan J., Fournier D.;
RT "Mechanisms of cholinesterase inhibition by inorganic mercury.";
RL FEBS J. 274:1849-1861(2007).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH TABUN,
RP ACTIVITY REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND GLYCOSYLATION
RP AT ASN-85; ASN-134; ASN-284; ASN-369 AND ASN-513.
RX PubMed=18975951; DOI=10.1021/ja804941z;
RA Carletti E., Li H., Li B., Ekstroem F., Nicolet Y., Loiodice M., Gillon E.,
RA Froment M.T., Lockridge O., Schopfer L.M., Masson P., Nachon F.;
RT "Aging of cholinesterases phosphylated by tabun proceeds through O-
RT dealkylation.";
RL J. Am. Chem. Soc. 130:16011-16020(2008).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH TABUN
RP ANALOGS, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-284; ASN-369 AND ASN-513,
RP AND ACTIVITY REGULATION.
RX PubMed=19368529; DOI=10.1042/bj20090091;
RA Carletti E., Aurbek N., Gillon E., Loiodice M., Nicolet Y.,
RA Fontecilla-Camps J.C., Masson P., Thiermann H., Nachon F., Worek F.;
RT "Structure-activity analysis of aging and reactivation of human
RT butyrylcholinesterase inhibited by analogues of tabun.";
RL Biochem. J. 421:97-106(2009).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH TACRINE,
RP DISULFIDE BOND, AND GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-284;
RP ASN-369 AND ASN-513.
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 [26]
RP VARIANT BCHED GLY-98.
RX PubMed=2915989; DOI=10.1073/pnas.86.3.953;
RA McGuire M.C., Nogueira C.P., Bartels C.F., Lightstone H., Hajra A.,
RA van der Spek A.F.L., Lockridge O., la Du B.N.;
RT "Identification of the structural mutation responsible for the dibucaine-
RT resistant (atypical) variant form of human serum cholinesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:953-957(1989).
RN [27]
RP VARIANT BCHED VAL-525.
RX PubMed=1349196;
RA Bartels C.F., James K., La Du B.N.;
RT "DNA mutations associated with the human butyrylcholinesterase J-variant.";
RL Am. J. Hum. Genet. 50:1104-1114(1992).
RN [28]
RP VARIANTS BCHED MET-271 AND VAL-418.
RX PubMed=1415224;
RA Nogueira C.P., Bartels C.F., McGuire M.C., Adkins S., Lubrano T.,
RA Rubinstein H.M., Lightstone H., Van Der Spek A.F.L., Lockridge O.,
RA La Du B.N.;
RT "Identification of two different point mutations associated with the
RT fluoride-resistant phenotype for human butyrylcholinesterase.";
RL Am. J. Hum. Genet. 51:821-828(1992).
RN [29]
RP VARIANT BCHED ARG-393.
RX PubMed=1611188; DOI=10.2169/internalmedicine.31.357;
RA Hada T., Muratani K., Ohue T., Imanishi H., Moriwaki Y., Itoh M., Amuro Y.,
RA Higashino K.;
RT "A variant serum cholinesterase and a confirmed point mutation at Gly-365
RT to Arg found in a patient with liver cirrhosis.";
RL Intern. Med. 31:357-362(1992).
RN [30]
RP VARIANTS BCHED GLY-98 AND MET-170.
RX PubMed=1306123; DOI=10.1097/00008571-199210000-00006;
RA Jensen F.S., Bartels C.F., La Du B.N.;
RT "Structural basis of the butyrylcholinesterase H-variant segregating in two
RT Danish families.";
RL Pharmacogenetics 2:234-240(1992).
RN [31]
RP VARIANTS BCHED PRO-278; ARG-393; SER-446; CYS-543 AND THR-567.
RX PubMed=7634491; DOI=10.1016/0009-8981(95)06014-1;
RA Maekawa M., Sudo K., Kanno T., Kotani K., Dey D.C., Ishikawa J., Izumi M.,
RA Etoh K.;
RT "Genetic basis of the silent phenotype of serum butyrylcholinesterase in
RT three compound heterozygotes.";
RL Clin. Chim. Acta 235:41-57(1995).
RN [32]
RP VARIANT BCHED ILE-358.
RX PubMed=8680411; DOI=10.1002/humu.1380060411;
RA Iida S., Kinoshita M., Fujii H., Moriyama Y., Nakamura Y., Yura N.,
RA Moriwaki K.;
RT "Mutations of human butyrylcholinesterase gene in a family with
RT hypocholinesterasemia.";
RL Hum. Mutat. 6:349-351(1995).
RN [33]
RP VARIANTS BCHED CYS-61; SER-65; PHE-153; GLU-198; GLY-226; THR-229; ARG-499
RP AND LEU-546, AND CHARACTERIZATION OF VARIANTS BCHED SER-65; PHE-153;
RP GLU-198; ARG-499 AND LEU-546.
RX PubMed=8554068;
RA Primo-Parmo S.L., Bartels C.F., Wiersema B., van der Spek A.F.L.,
RA Innis J.W., La Du B.N.;
RT "Characterization of 12 silent alleles of the human butyrylcholinesterase
RT (BCHE) gene.";
RL Am. J. Hum. Genet. 58:52-64(1996).
RN [34]
RP VARIANT BCHED CYS-156.
RX PubMed=9543549; DOI=10.1046/j.1469-1809.1997.6160491.x;
RA Hidaka K., Iuchi I., Tomita M., Watanabe Y., Minatogawa Y., Iwasaki K.,
RA Gotoh K., Shimizu C.;
RT "Genetic analysis of a Japanese patient with butyrylcholinesterase
RT deficiency.";
RL Ann. Hum. Genet. 61:491-496(1997).
RN [35]
RP VARIANT BUTYRYLCHOLINESTERASE DEFICIENCY ILE-358.
RX PubMed=9388484; DOI=10.1006/bbrc.1997.7658;
RA Sudo K., Maekawa M., Akizuki S., Magara T., Ogasawara H., Tanaka T.;
RT "Human butyrylcholinesterase L330I mutation belongs to a fluoride-resistant
RT gene, by expression in human fetal kidney cells.";
RL Biochem. Biophys. Res. Commun. 240:372-375(1997).
RN [36]
RP VARIANTS BCHED ILE-32 DEL; MET-52; SER-128; PRO-278; ARG-295; ILE-358;
RP ARG-393; SER-446; CYS-543 AND THR-567.
RX PubMed=9191541;
RA Maekawa M., Sudo K., Dey D.C., Ishikawa J., Izumi M., Kotani K., Kanno T.;
RT "Genetic mutations of butyrylcholine esterase identified from phenotypic
RT abnormalities in Japan.";
RL Clin. Chem. 43:924-929(1997).
RN [37]
RP VARIANTS BCHED GLY-98 AND ASP-143.
RX PubMed=9110359; DOI=10.1097/00008571-199702000-00004;
RA Primo-Parmo S.L., Lightstone H., La Du B.N.;
RT "Characterization of an unstable variant (BChE115D) of human
RT butyrylcholinesterase.";
RL Pharmacogenetics 7:27-34(1997).
RN [38]
RP VARIANT BCHED VAL-227.
RX PubMed=9694584; DOI=10.1016/s0009-8981(98)00058-8;
RA Sakamoto N., Hidaka K., Fujisawa T., Maeda M., Iuchi I.;
RT "Identification of a point mutation associated with a silent phenotype of
RT human serum butyrylcholinesterase - a case of familial cholinesterasemia.";
RL Clin. Chim. Acta 274:159-166(1998).
RN [39]
RP VARIANTS BCHED ILE-358; ARG-393 AND CYS-543.
RX PubMed=10404729; DOI=10.1016/s0009-8981(99)00030-3;
RA Asanuma K., Yagihashi A., Uehara N., Kida T., Watanabe N.;
RT "Three point mutations of human butyrylcholinesterase in a Japanese family
RT and the alterations of three-dimensional structure.";
RL Clin. Chim. Acta 283:33-42(1999).
RN [40]
RP VARIANTS BCHED GLY-98; HIS-98; MET-271 AND THR-567.
RX PubMed=11928765; DOI=10.1258/0004563021901775;
RA Boeck A.T., Fry D.L., Sastre A., Lockridge O.;
RT "Naturally occurring mutation, Asp70His, in human butyrylcholinesterase.";
RL Ann. Clin. Biochem. 39:154-156(2002).
RN [41]
RP VARIANTS BCHED ILE-56; TYR-124; CYS-414 AND LYS-488.
RX PubMed=12881446; DOI=10.1373/49.8.1297;
RA Yen T., Nightingale B.N., Burns J.C., Sullivan D.R., Stewart P.M.;
RT "Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine apnea in
RT an Australian population.";
RL Clin. Chem. 49:1297-1308(2003).
RN [42]
RP VARIANTS BCHED CYS-414 AND LEU-502.
RX PubMed=15563885; DOI=10.1016/j.cccn.2004.09.004;
RA On-Kei Chan A., Lam C.-W., Tong S.-F., Man Tung C., Yung K., Chan Y.-W.,
RA Au K.-M., Yuen Y.-P., Hung C.-T., Ng K.-P., Shek C.-C.;
RT "Novel mutations in the BCHE gene in patients with no butyrylcholinesterase
RT activity.";
RL Clin. Chim. Acta 351:155-159(2005).
RN [43]
RP VARIANT MET-127, AND VARIANTS BCHED GLY-98; ARG-103 AND ASP-118.
RX PubMed=15781196; DOI=10.1016/j.ymgme.2004.12.005;
RA Souza R.L., Mikami L.R., Maegawa R.O., Chautard-Freire-Maia E.A.;
RT "Four new mutations in the BCHE gene of human butyrylcholinesterase in a
RT Brazilian blood donor sample.";
RL Mol. Genet. Metab. 84:349-353(2005).
RN [44]
RP VARIANT BCHED PRO-335, AND CHARACTERIZATION OF VARIANT BCHED PRO-335.
RX PubMed=16788378; DOI=10.1097/01.fpc.0000197464.37211.77;
RA Manoharan I., Wieseler S., Layer P.G., Lockridge O., Boopathy R.;
RT "Naturally occurring mutation Leu307Pro of human butyrylcholinesterase in
RT the Vysya community of India.";
RL Pharmacogenet. Genomics 16:461-468(2006).
RN [45]
RP CHARACTERIZATION OF VARIANT MET-127, AND CHARACTERIZATION OF VARIANTS BCHED
RP ARG-103 AND ASP-118.
RX PubMed=17700357; DOI=10.1097/01.fpc.0000236333.49422.86;
RA Mikami L.R., Wieseler S., Souza R.L., Schopfer L.M., Lockridge O.,
RA Chautard-Freire-Maia E.A.;
RT "Expression of three naturally occurring genetic variants (G75R, E90D,
RT I99M) of the BCHE gene of human butyrylcholinesterase.";
RL Pharmacogenet. Genomics 17:681-685(2007).
RN [46]
RP VARIANT BCHED ASP-356.
RX PubMed=18075469; DOI=10.1097/fpc.0b013e3282f06646;
RA Gaetke M.R., Bundgaard J.R., Viby-Mogensen J.;
RT "Two novel mutations in the BCHE gene in patients with prolonged duration
RT of action of mivacurium or succinylcholine during anaesthesia.";
RL Pharmacogenet. Genomics 17:995-999(2007).
RN [47]
RP VARIANT BCHED CYS-361, VARIANTS ARG-40; MET-322 AND TRP-498,
RP CHARACTERIZATION OF VARIANT BCHED CYS-361, AND CHARACTERIZATION OF VARIANTS
RP ARG-40; MET-322 AND TRP-498.
RX PubMed=18300943; DOI=10.1097/fpc.0b013e3282f5107e;
RA Mikami L.R., Wieseler S., Souza R.L., Schopfer L.M., Nachon F.,
RA Lockridge O., Chautard-Freire-Maia E.A.;
RT "Five new naturally occurring mutations of the BCHE gene and frequencies of
RT 12 butyrylcholinesterase alleles in a Brazilian population.";
RL Pharmacogenet. Genomics 18:213-218(2008).
RN [48]
RP VARIANTS BCHED VAL-62 AND GLY-98, AND CHARACTERIZATION OF VARIANTS BCHED
RP VAL-62 AND GLY-98.
RX PubMed=25264279; DOI=10.1016/j.bcp.2014.09.014;
RA Delacour H., Lushchekina S., Mabboux I., Ceppa F., Masson P.,
RA Schopfer L.M., Lockridge O.;
RT "Characterization of a novel butyrylcholinesterase point mutation
RT (p.Ala34Val), 'silent' with mivacurium.";
RL Biochem. Pharmacol. 92:476-483(2014).
CC -!- FUNCTION: Esterase with broad substrate specificity. Contributes to the
CC inactivation of the neurotransmitter acetylcholine. Can degrade
CC neurotoxic organophosphate esters. {ECO:0000269|PubMed:19452557,
CC ECO:0000269|PubMed:19542320}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acylcholine + H2O = a carboxylate + choline + H(+);
CC Xref=Rhea:RHEA:21964, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:35287; EC=3.1.1.8;
CC Evidence={ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19452557};
CC -!- ACTIVITY REGULATION: Inhibited by mercury. Inhibited by Tabun. Tabun
CC forms a covalent adduct with Ser-226 that becomes irreversible upon
CC aging. {ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:18975951,
CC ECO:0000269|PubMed:19368529}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.0 uM for butyrylthiocholine (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:25054547};
CC -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers.
CC {ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209,
CC ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338,
CC ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19368529,
CC ECO:0000269|PubMed:19542320, ECO:0000269|PubMed:3115973}.
CC -!- INTERACTION:
CC P06276; P54252: ATXN3; NbExp=3; IntAct=EBI-7936069, EBI-946046;
CC P06276; P46379-2: BAG6; NbExp=3; IntAct=EBI-7936069, EBI-10988864;
CC P06276; P06276: BCHE; NbExp=8; IntAct=EBI-7936069, EBI-7936069;
CC P06276; P55212: CASP6; NbExp=3; IntAct=EBI-7936069, EBI-718729;
CC P06276; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-7936069, EBI-12593112;
CC P06276; O14901: KLF11; NbExp=3; IntAct=EBI-7936069, EBI-948266;
CC P06276; P13473-2: LAMP2; NbExp=3; IntAct=EBI-7936069, EBI-21591415;
CC P06276; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-7936069, EBI-5280197;
CC P06276; P62826: RAN; NbExp=3; IntAct=EBI-7936069, EBI-286642;
CC P06276; P67812: SEC11A; NbExp=3; IntAct=EBI-7936069, EBI-1042500;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19368529,
CC ECO:0000269|PubMed:19542320}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
CC Present in most cells except erythrocytes.
CC {ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19542320}.
CC -!- PTM: N-glycosylated. No other PTM detected (PubMed:20946535). The major
CC N-glycan structures are of the complex diantennary type with 1 and 2 N-
CC acetylneuraminic acid molecules (Neu5Ac) making up approximately 33%
CC and 47% of the total N-glycans, respectively. Only low amounts of
CC fucosylated diantennary N-glycans are detected (approximately 2%).
CC Triantennary N-glycans with or without fucose amount to approximately
CC 13%, whereas 5% of the total N-glycans are of the oligomannosidic or
CC hybrid type. {ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:14760718,
CC ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338,
CC ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951,
CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:20946535}.
CC -!- DISEASE: Butyrylcholinesterase deficiency (BCHED) [MIM:617936]: An
CC autosomal recessive metabolic condition characterized by increased
CC sensitivity to certain anesthetic drugs, including the muscle relaxants
CC succinylcholine or mivacurium. BCHED results in slower hydrolysis of
CC these drugs and, consequently, a prolonged neuromuscular block, leading
CC to apnea. The duration of the prolonged apnea varies significantly
CC depending on the extent of the enzyme deficiency.
CC {ECO:0000269|PubMed:10404729, ECO:0000269|PubMed:11928765,
CC ECO:0000269|PubMed:12881446, ECO:0000269|PubMed:1306123,
CC ECO:0000269|PubMed:1349196, ECO:0000269|PubMed:1415224,
CC ECO:0000269|PubMed:15563885, ECO:0000269|PubMed:15781196,
CC ECO:0000269|PubMed:1611188, ECO:0000269|PubMed:16788378,
CC ECO:0000269|PubMed:17700357, ECO:0000269|PubMed:18075469,
CC ECO:0000269|PubMed:18300943, ECO:0000269|PubMed:25054547,
CC ECO:0000269|PubMed:25264279, ECO:0000269|PubMed:2915989,
CC ECO:0000269|PubMed:7634491, ECO:0000269|PubMed:8554068,
CC ECO:0000269|PubMed:8680411, ECO:0000269|PubMed:9110359,
CC ECO:0000269|PubMed:9191541, ECO:0000269|PubMed:9388484,
CC ECO:0000269|PubMed:9543549, ECO:0000269|PubMed:9694584}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; M32391; AAA99296.1; -; Genomic_DNA.
DR EMBL; M32389; AAA99296.1; JOINED; Genomic_DNA.
DR EMBL; M32390; AAA99296.1; JOINED; Genomic_DNA.
DR EMBL; M16541; AAA98113.1; -; mRNA.
DR EMBL; M16474; AAA52015.1; -; mRNA.
DR EMBL; AK292063; BAF84752.1; -; mRNA.
DR EMBL; BC018141; AAH18141.1; -; mRNA.
DR CCDS; CCDS3198.1; -.
DR PIR; A33769; ACHU.
DR RefSeq; NP_000046.1; NM_000055.3.
DR PDB; 1P0I; X-ray; 2.00 A; A=29-557.
DR PDB; 1P0M; X-ray; 2.38 A; A=29-557.
DR PDB; 1P0P; X-ray; 2.30 A; A=29-557.
DR PDB; 1P0Q; X-ray; 2.43 A; A=29-557.
DR PDB; 1XLU; X-ray; 2.20 A; A=29-557.
DR PDB; 1XLV; X-ray; 2.25 A; A=29-557.
DR PDB; 1XLW; X-ray; 2.10 A; A=29-557.
DR PDB; 2J4C; X-ray; 2.75 A; A=29-557.
DR PDB; 2PM8; X-ray; 2.80 A; A/B=29-602.
DR PDB; 2WID; X-ray; 2.30 A; A=29-557.
DR PDB; 2WIF; X-ray; 2.25 A; A=29-557.
DR PDB; 2WIG; X-ray; 2.15 A; A=29-557.
DR PDB; 2WIJ; X-ray; 2.10 A; A=29-557.
DR PDB; 2WIK; X-ray; 2.10 A; A=29-557.
DR PDB; 2WIL; X-ray; 3.10 A; A/B=29-557.
DR PDB; 2WSL; X-ray; 2.00 A; A=29-557.
DR PDB; 2XMB; X-ray; 2.10 A; A=29-557.
DR PDB; 2XMC; X-ray; 2.40 A; A=29-557.
DR PDB; 2XMD; X-ray; 2.30 A; A=29-557.
DR PDB; 2XMG; X-ray; 2.70 A; A=29-557.
DR PDB; 2XQF; X-ray; 2.10 A; A=31-557.
DR PDB; 2XQG; X-ray; 2.30 A; A=31-557.
DR PDB; 2XQI; X-ray; 2.60 A; A=31-557.
DR PDB; 2XQJ; X-ray; 2.40 A; A=31-557.
DR PDB; 2XQK; X-ray; 2.40 A; A=31-557.
DR PDB; 2Y1K; X-ray; 2.50 A; A=29-557.
DR PDB; 3DJY; X-ray; 2.10 A; A=29-557.
DR PDB; 3DKK; X-ray; 2.31 A; A=29-557.
DR PDB; 3O9M; X-ray; 2.98 A; A/B=29-602.
DR PDB; 4AQD; X-ray; 2.50 A; A/B=29-557.
DR PDB; 4AXB; X-ray; 2.40 A; A=31-557.
DR PDB; 4B0O; X-ray; 2.35 A; A=29-557.
DR PDB; 4B0P; X-ray; 2.50 A; A=29-557.
DR PDB; 4BBZ; X-ray; 2.70 A; A=29-557.
DR PDB; 4BDS; X-ray; 2.10 A; A=29-557.
DR PDB; 4TPK; X-ray; 2.70 A; A/B=1-602.
DR PDB; 4XII; X-ray; 2.70 A; A/B=29-572.
DR PDB; 5DYT; X-ray; 2.55 A; A/B=28-557.
DR PDB; 5DYW; X-ray; 2.50 A; A/B=28-557.
DR PDB; 5DYY; X-ray; 2.65 A; A/B=28-557.
DR PDB; 5K5E; X-ray; 2.80 A; A/B=29-557.
DR PDB; 5LKR; X-ray; 2.52 A; A/B=29-602.
DR PDB; 5NN0; X-ray; 2.10 A; A=29-557.
DR PDB; 6EMI; X-ray; 2.48 A; A/B=29-557.
DR PDB; 6EP4; X-ray; 2.30 A; A=29-557.
DR PDB; 6EQP; X-ray; 2.35 A; A=29-557.
DR PDB; 6EQQ; X-ray; 2.40 A; A=29-557.
DR PDB; 6ESJ; X-ray; 2.98 A; A/B=29-557.
DR PDB; 6ESY; X-ray; 2.80 A; A/B=29-557.
DR PDB; 6EUL; X-ray; 2.60 A; A=31-558.
DR PDB; 6EYF; X-ray; 2.60 A; A=31-557.
DR PDB; 6EZ2; X-ray; 2.70 A; A/B=31-557.
DR PDB; 6F7Q; X-ray; 2.60 A; A/B=29-557.
DR PDB; 6I0B; X-ray; 2.38 A; A=29-557.
DR PDB; 6I0C; X-ray; 2.67 A; A=29-557.
DR PDB; 6I2T; EM; 5.70 A; A/B/C/D=29-602.
DR PDB; 6QAA; X-ray; 1.90 A; A=1-557.
DR PDB; 6QAB; X-ray; 2.49 A; A=1-557.
DR PDB; 6QAC; X-ray; 2.77 A; A=1-557.
DR PDB; 6QAD; X-ray; 2.50 A; A=1-557.
DR PDB; 6QAE; X-ray; 2.49 A; A=1-557.
DR PDB; 6R6V; X-ray; 2.50 A; A=32-557.
DR PDB; 6R6W; X-ray; 2.47 A; A=32-557.
DR PDB; 6RUA; X-ray; 2.75 A; A/B=29-602.
DR PDB; 6SAM; X-ray; 2.50 A; A=29-557.
DR PDB; 6T9P; X-ray; 2.70 A; A=29-557.
DR PDB; 6T9S; X-ray; 2.70 A; A=29-557.
DR PDB; 6XTA; X-ray; 2.50 A; A=29-557.
DR PDB; 6ZWI; X-ray; 1.85 A; A=29-557.
DR PDB; 7AIY; X-ray; 2.94 A; A/B=1-602.
DR PDB; 7AMZ; X-ray; 2.25 A; A=29-557.
DR PDB; 7AWG; X-ray; 2.00 A; A=29-557.
DR PDB; 7AWH; X-ray; 2.30 A; A=29-557.
DR PDB; 7AWI; X-ray; 2.30 A; A=29-557.
DR PDB; 7BGC; X-ray; 2.40 A; A=29-557.
DR PDB; 7BO3; X-ray; 2.20 A; A=29-557.
DR PDB; 7BO4; X-ray; 2.40 A; A=29-557.
DR PDBsum; 1P0I; -.
DR PDBsum; 1P0M; -.
DR PDBsum; 1P0P; -.
DR PDBsum; 1P0Q; -.
DR PDBsum; 1XLU; -.
DR PDBsum; 1XLV; -.
DR PDBsum; 1XLW; -.
DR PDBsum; 2J4C; -.
DR PDBsum; 2PM8; -.
DR PDBsum; 2WID; -.
DR PDBsum; 2WIF; -.
DR PDBsum; 2WIG; -.
DR PDBsum; 2WIJ; -.
DR PDBsum; 2WIK; -.
DR PDBsum; 2WIL; -.
DR PDBsum; 2WSL; -.
DR PDBsum; 2XMB; -.
DR PDBsum; 2XMC; -.
DR PDBsum; 2XMD; -.
DR PDBsum; 2XMG; -.
DR PDBsum; 2XQF; -.
DR PDBsum; 2XQG; -.
DR PDBsum; 2XQI; -.
DR PDBsum; 2XQJ; -.
DR PDBsum; 2XQK; -.
DR PDBsum; 2Y1K; -.
DR PDBsum; 3DJY; -.
DR PDBsum; 3DKK; -.
DR PDBsum; 3O9M; -.
DR PDBsum; 4AQD; -.
DR PDBsum; 4AXB; -.
DR PDBsum; 4B0O; -.
DR PDBsum; 4B0P; -.
DR PDBsum; 4BBZ; -.
DR PDBsum; 4BDS; -.
DR PDBsum; 4TPK; -.
DR PDBsum; 4XII; -.
DR PDBsum; 5DYT; -.
DR PDBsum; 5DYW; -.
DR PDBsum; 5DYY; -.
DR PDBsum; 5K5E; -.
DR PDBsum; 5LKR; -.
DR PDBsum; 5NN0; -.
DR PDBsum; 6EMI; -.
DR PDBsum; 6EP4; -.
DR PDBsum; 6EQP; -.
DR PDBsum; 6EQQ; -.
DR PDBsum; 6ESJ; -.
DR PDBsum; 6ESY; -.
DR PDBsum; 6EUL; -.
DR PDBsum; 6EYF; -.
DR PDBsum; 6EZ2; -.
DR PDBsum; 6F7Q; -.
DR PDBsum; 6I0B; -.
DR PDBsum; 6I0C; -.
DR PDBsum; 6I2T; -.
DR PDBsum; 6QAA; -.
DR PDBsum; 6QAB; -.
DR PDBsum; 6QAC; -.
DR PDBsum; 6QAD; -.
DR PDBsum; 6QAE; -.
DR PDBsum; 6R6V; -.
DR PDBsum; 6R6W; -.
DR PDBsum; 6RUA; -.
DR PDBsum; 6SAM; -.
DR PDBsum; 6T9P; -.
DR PDBsum; 6T9S; -.
DR PDBsum; 6XTA; -.
DR PDBsum; 6ZWI; -.
DR PDBsum; 7AIY; -.
DR PDBsum; 7AMZ; -.
DR PDBsum; 7AWG; -.
DR PDBsum; 7AWH; -.
DR PDBsum; 7AWI; -.
DR PDBsum; 7BGC; -.
DR PDBsum; 7BO3; -.
DR PDBsum; 7BO4; -.
DR AlphaFoldDB; P06276; -.
DR SMR; P06276; -.
DR BioGRID; 107064; 62.
DR DIP; DIP-46476N; -.
DR IntAct; P06276; 39.
DR MINT; P06276; -.
DR STRING; 9606.ENSP00000264381; -.
DR BindingDB; P06276; -.
DR ChEMBL; CHEMBL1914; -.
DR DrugBank; DB08200; (1R)-menthyl hexyl phosphonate group.
DR DrugBank; DB08201; (1S)-menthyl hexyl phosphonate group.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB07940; 9-(3-IODOBENZYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE.
DR DrugBank; DB03672; 9-N-Phenylmethylamino-Tacrine.
DR DrugBank; DB08897; Aclidinium.
DR DrugBank; DB01122; Ambenonium.
DR DrugBank; DB06692; Aprotinin.
DR DrugBank; DB01408; Bambuterol.
DR DrugBank; DB00868; Benzonatate.
DR DrugBank; DB06756; Betaine.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB03568; Butyric Acid.
DR DrugBank; DB04250; Butyrylthiocholine.
DR DrugBank; DB06774; Capsaicin.
DR DrugBank; DB01161; Chloroprocaine.
DR DrugBank; DB00856; Chlorphenesin.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR DrugBank; DB00527; Cinchocaine.
DR DrugBank; DB00515; Cisplatin.
DR DrugBank; DB04920; Clevidipine.
DR DrugBank; DB00907; Cocaine.
DR DrugBank; DB00979; Cyclopentolate.
DR DrugBank; DB01245; Decamethonium.
DR DrugBank; DB00944; Demecarium.
DR DrugBank; DB11397; Dichlorvos.
DR DrugBank; DB02811; Diethyl phosphonate.
DR DrugBank; DB00711; Diethylcarbamazine.
DR DrugBank; DB00449; Dipivefrin.
DR DrugBank; DB07681; DODECANESULFONATE ION.
DR DrugBank; DB00843; Donepezil.
DR DrugBank; DB01135; Doxacurium.
DR DrugBank; DB01057; Echothiophate.
DR DrugBank; DB01010; Edrophonium.
DR DrugBank; DB01364; Ephedrine.
DR DrugBank; DB03822; Ethyl dihydrogen phosphate.
DR DrugBank; DB08658; Ethyl hydrogen diethylamidophosphate.
DR DrugBank; DB00674; Galantamine.
DR DrugBank; DB00941; Hexafluronium.
DR DrugBank; DB00762; Irinotecan.
DR DrugBank; DB00677; Isoflurophate.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB00772; Malathion.
DR DrugBank; DB00888; Mechlorethamine.
DR DrugBank; DB00358; Mefloquine.
DR DrugBank; DB02845; Methylphosphinic Acid.
DR DrugBank; DB08893; Mirabegron.
DR DrugBank; DB01226; Mivacurium.
DR DrugBank; DB09205; Moxisylyte.
DR DrugBank; DB01400; Neostigmine.
DR DrugBank; DB00585; Nizatidine.
DR DrugBank; DB00892; Oxybuprocaine.
DR DrugBank; DB01337; Pancuronium.
DR DrugBank; DB00082; Pegvisomant.
DR DrugBank; DB00183; Pentagastrin.
DR DrugBank; DB00790; Perindopril.
DR DrugBank; DB04892; Phenserine.
DR DrugBank; DB03976; Phosphorylisopropane.
DR DrugBank; DB01338; Pipecuronium.
DR DrugBank; DB00733; Pralidoxime.
DR DrugBank; DB01035; Procainamide.
DR DrugBank; DB00721; Procaine.
DR DrugBank; DB00392; Profenamine.
DR DrugBank; DB09288; Propacetamol.
DR DrugBank; DB00545; Pyridostigmine.
DR DrugBank; DB00178; Ramipril.
DR DrugBank; DB05386; Regramostim.
DR DrugBank; DB00989; Rivastigmine.
DR DrugBank; DB05875; Sar9, Met (O2)11-Substance P.
DR DrugBank; DB00202; Succinylcholine.
DR DrugBank; DB00391; Sulpiride.
DR DrugBank; DB00382; Tacrine.
DR DrugBank; DB00871; Terbutaline.
DR DrugBank; DB04572; Thiotepa.
DR DrugBank; DB14031; Tretamine.
DR DrugBank; DB00620; Triamcinolone.
DR DrugBank; DB00508; Triflupromazine.
DR DrugBank; DB01116; Trimethaphan.
DR DrugBank; DB01199; Tubocurarine.
DR DrugCentral; P06276; -.
DR GuidetoPHARMACOLOGY; 2471; -.
DR ESTHER; human-BCHE; BCHE.
DR MEROPS; S09.980; -.
DR GlyConnect; 1109; 12 N-Linked glycans (4 sites).
DR GlyGen; P06276; 13 sites, 12 N-linked glycans (4 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P06276; -.
DR PhosphoSitePlus; P06276; -.
DR BioMuta; BCHE; -.
DR DMDM; 116353; -.
DR CPTAC; non-CPTAC-2645; -.
DR EPD; P06276; -.
DR jPOST; P06276; -.
DR MassIVE; P06276; -.
DR MaxQB; P06276; -.
DR PaxDb; P06276; -.
DR PeptideAtlas; P06276; -.
DR PRIDE; P06276; -.
DR ProteomicsDB; 51880; -.
DR ABCD; P06276; 4 sequenced antibodies.
DR Antibodypedia; 879; 445 antibodies from 40 providers.
DR DNASU; 590; -.
DR Ensembl; ENST00000264381.8; ENSP00000264381.3; ENSG00000114200.10.
DR GeneID; 590; -.
DR KEGG; hsa:590; -.
DR MANE-Select; ENST00000264381.8; ENSP00000264381.3; NM_000055.4; NP_000046.1.
DR UCSC; uc003fem.5; human.
DR CTD; 590; -.
DR DisGeNET; 590; -.
DR GeneCards; BCHE; -.
DR HGNC; HGNC:983; BCHE.
DR HPA; ENSG00000114200; Tissue enriched (liver).
DR MalaCards; BCHE; -.
DR MIM; 177400; gene.
DR MIM; 617936; phenotype.
DR neXtProt; NX_P06276; -.
DR OpenTargets; ENSG00000114200; -.
DR Orphanet; 132; Butyrylcholinesterase deficiency.
DR Orphanet; 413693; Prediction of curariform drugs toxicity.
DR PharmGKB; PA25294; -.
DR VEuPathDB; HostDB:ENSG00000114200; -.
DR eggNOG; KOG4389; Eukaryota.
DR GeneTree; ENSGT00940000157023; -.
DR InParanoid; P06276; -.
DR OMA; EMRYICP; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P06276; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.8; 2681.
DR PathwayCommons; P06276; -.
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 Reactome; R-HSA-9749641; Aspirin ADME.
DR SABIO-RK; P06276; -.
DR SignaLink; P06276; -.
DR SIGNOR; P06276; -.
DR BioGRID-ORCS; 590; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; BCHE; human.
DR EvolutionaryTrace; P06276; -.
DR GeneWiki; Butyrylcholinesterase; -.
DR GenomeRNAi; 590; -.
DR Pharos; P06276; Tclin.
DR PRO; PR:P06276; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P06276; protein.
DR Bgee; ENSG00000114200; Expressed in parietal pleura and 160 other tissues.
DR ExpressionAtlas; P06276; baseline and differential.
DR Genevisible; P06276; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003990; F:acetylcholinesterase activity; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; NAS:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0003824; F:catalytic activity; NAS:UniProtKB.
DR GO; GO:0033265; F:choline binding; IEA:Ensembl.
DR GO; GO:0004104; F:cholinesterase activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006581; P:acetylcholine catabolic process; IBA:GO_Central.
DR GO; GO:0019695; P:choline metabolic process; IBA:GO_Central.
DR GO; GO:0050783; P:cocaine metabolic process; TAS:UniProtKB.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl.
DR GO; GO:0014016; P:neuroblast differentiation; IEA:Ensembl.
DR GO; GO:0016486; P:peptide hormone processing; TAS:Reactome.
DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
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; Direct protein sequencing; Disease variant; Disulfide bond;
KW Glycoprotein; Hydrolase; Phosphoprotein; Reference proteome; Secreted;
KW Serine esterase; Sialic acid; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:20946535,
FT ECO:0000269|PubMed:3542989"
FT CHAIN 29..602
FT /note="Cholinesterase"
FT /id="PRO_0000008613"
FT ACT_SITE 226
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039,
FT ECO:0000269|PubMed:12869558"
FT ACT_SITE 353
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:12869558"
FT ACT_SITE 466
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:12869558"
FT BINDING 110
FT /ligand="tacrine"
FT /ligand_id="ChEBI:CHEBI:187896"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0007744|PDB:4BDS"
FT BINDING 144..145
FT /ligand="substrate"
FT BINDING 466
FT /ligand="tacrine"
FT /ligand_id="ChEBI:CHEBI:187896"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0007744|PDB:4BDS"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22444575"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:18203274"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:12869558,
FT ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338,
FT ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951,
FT ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:12869558,
FT ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:17355286,
FT ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18203274,
FT ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:12869558,
FT ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:17355286,
FT ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:19368529,
FT ECO:0000269|PubMed:23679855"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:18203274,
FT ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19368529,
FT ECO:0000269|PubMed:23679855"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:12869558,
FT ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338,
FT ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951,
FT ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:18203274"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3542989"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12869558,
FT ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:17355286,
FT ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18975951,
FT ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3542989"
FT DISULFID 93..120
FT DISULFID 280..291
FT DISULFID 428..547
FT DISULFID 599
FT /note="Interchain"
FT VARIANT 32
FT /note="Missing (in BCHED)"
FT /evidence="ECO:0000269|PubMed:9191541"
FT /id="VAR_040011"
FT VARIANT 40
FT /note="K -> R (does not affect enzymatic activity;
FT dbSNP:rs116047990)"
FT /evidence="ECO:0000269|PubMed:18300943"
FT /id="VAR_072094"
FT VARIANT 52
FT /note="T -> M (in BCHED; dbSNP:rs56309853)"
FT /evidence="ECO:0000269|PubMed:9191541"
FT /id="VAR_040012"
FT VARIANT 56
FT /note="F -> I (in BCHED; dbSNP:rs531738678)"
FT /evidence="ECO:0000269|PubMed:12881446"
FT /id="VAR_040013"
FT VARIANT 61
FT /note="Y -> C (in BCHED; enzymatically inactive in the
FT plasma; dbSNP:rs116097205)"
FT /evidence="ECO:0000269|PubMed:8554068"
FT /id="VAR_040014"
FT VARIANT 62
FT /note="A -> V (in BCHED; reduced enzyme activity with
FT butyrylthiocholine as substrate; inactive with
FT butyrylthiocholine as substrate in the presence of G-98; 2-
FT fold lower affinity for butyrylthiocholine; 10-fold lower
FT affinity for butyrylthiocholine in the presence of G-98;
FT dbSNP:rs1553778274)"
FT /evidence="ECO:0000269|PubMed:25264279"
FT /id="VAR_072730"
FT VARIANT 65
FT /note="P -> S (in BCHED; seems to cause reduced expression
FT of the protein; dbSNP:rs148170012)"
FT /evidence="ECO:0000269|PubMed:8554068"
FT /id="VAR_040015"
FT VARIANT 98
FT /note="D -> G (in BCHED; atypical form; reduced enzyme
FT activity with butyrylthiocholine as substrate; inactive
FT with butyrylthiocholine as substrate in the presence of V-
FT 62; 2-fold lower affinity for butyrylthiocholine; 10-fold
FT lower affinity for butyrylthiocholine in the presence of V-
FT 62 or at homozygosity; dbSNP:rs1799807)"
FT /evidence="ECO:0000269|PubMed:11928765,
FT ECO:0000269|PubMed:1306123, ECO:0000269|PubMed:15781196,
FT ECO:0000269|PubMed:25264279, ECO:0000269|PubMed:2915989,
FT ECO:0000269|PubMed:9110359"
FT /id="VAR_002360"
FT VARIANT 98
FT /note="D -> H (in BCHED)"
FT /evidence="ECO:0000269|PubMed:11928765"
FT /id="VAR_040016"
FT VARIANT 103
FT /note="G -> R (in BCHED; reduced enzyme activity;
FT dbSNP:rs979653503)"
FT /evidence="ECO:0000269|PubMed:15781196,
FT ECO:0000269|PubMed:17700357"
FT /id="VAR_072095"
FT VARIANT 118
FT /note="E -> D (in BCHED; the mutant undergoes rapid
FT degradation)"
FT /evidence="ECO:0000269|PubMed:15781196,
FT ECO:0000269|PubMed:17700357"
FT /id="VAR_072096"
FT VARIANT 124
FT /note="N -> Y (in BCHED; dbSNP:rs1339128583)"
FT /evidence="ECO:0000269|PubMed:12881446"
FT /id="VAR_040017"
FT VARIANT 127
FT /note="I -> M (does not affect enzyme activity;
FT dbSNP:rs755600722)"
FT /evidence="ECO:0000269|PubMed:15781196,
FT ECO:0000269|PubMed:17700357"
FT /id="VAR_072097"
FT VARIANT 128
FT /note="P -> S (in BCHED; dbSNP:rs3732880)"
FT /evidence="ECO:0000269|PubMed:9191541"
FT /id="VAR_040018"
FT VARIANT 143
FT /note="G -> D (in BCHED; dbSNP:rs201820739)"
FT /evidence="ECO:0000269|PubMed:9110359"
FT /id="VAR_040019"
FT VARIANT 153
FT /note="L -> F (in BCHED; seems to cause reduced expression
FT of the protein; dbSNP:rs747598704)"
FT /evidence="ECO:0000269|PubMed:8554068"
FT /id="VAR_040020"
FT VARIANT 156
FT /note="Y -> C (in BCHED; dbSNP:rs121918558)"
FT /evidence="ECO:0000269|PubMed:9543549"
FT /id="VAR_040021"
FT VARIANT 170
FT /note="V -> M (in BCHED; allele H variant;
FT dbSNP:rs527843566)"
FT /evidence="ECO:0000269|PubMed:1306123"
FT /id="VAR_040022"
FT VARIANT 198
FT /note="D -> E (in BCHED; seems to cause reduced expression
FT of the protein; dbSNP:rs781368801)"
FT /evidence="ECO:0000269|PubMed:8554068"
FT /id="VAR_040023"
FT VARIANT 226
FT /note="S -> G (in BCHED; enzymatically inactive in the
FT plasma; dbSNP:rs370077923)"
FT /evidence="ECO:0000269|PubMed:8554068"
FT /id="VAR_040024"
FT VARIANT 227
FT /note="A -> V (in BCHED)"
FT /evidence="ECO:0000269|PubMed:9694584"
FT /id="VAR_040025"
FT VARIANT 229
FT /note="A -> T (in BCHED; enzymatically inactive in the
FT plasma)"
FT /evidence="ECO:0000269|PubMed:8554068"
FT /id="VAR_040026"
FT VARIANT 232
FT /note="V -> D (in BCHED)"
FT /evidence="ECO:0000269|PubMed:25054547"
FT /id="VAR_072098"
FT VARIANT 271
FT /note="T -> M (in BCHED; allele fluoride-1;
FT dbSNP:rs28933389)"
FT /evidence="ECO:0000269|PubMed:11928765,
FT ECO:0000269|PubMed:1415224"
FT /id="VAR_040027"
FT VARIANT 278
FT /note="T -> P (in BCHED; dbSNP:rs892642457)"
FT /evidence="ECO:0000269|PubMed:7634491,
FT ECO:0000269|PubMed:9191541"
FT /id="VAR_040028"
FT VARIANT 283
FT /note="E -> D (in dbSNP:rs16849700)"
FT /id="VAR_040029"
FT VARIANT 295
FT /note="K -> R (in BCHED; dbSNP:rs115624085)"
FT /evidence="ECO:0000269|PubMed:9191541"
FT /id="VAR_040030"
FT VARIANT 322
FT /note="V -> M (does not affect enzymatic activity;
FT dbSNP:rs754644618)"
FT /evidence="ECO:0000269|PubMed:18300943"
FT /id="VAR_072099"
FT VARIANT 335
FT /note="L -> P (in BCHED; expressed at very low level;
FT dbSNP:rs104893684)"
FT /evidence="ECO:0000269|PubMed:16788378"
FT /id="VAR_040031"
FT VARIANT 356
FT /note="A -> D (in BCHED; dbSNP:rs770337031)"
FT /evidence="ECO:0000269|PubMed:18075469"
FT /id="VAR_040032"
FT VARIANT 358
FT /note="L -> I (in BCHED; BChE variant form; fluoride-
FT resistant; dbSNP:rs121918557)"
FT /evidence="ECO:0000269|PubMed:10404729,
FT ECO:0000269|PubMed:8680411, ECO:0000269|PubMed:9191541,
FT ECO:0000269|PubMed:9388484"
FT /id="VAR_002362"
FT VARIANT 361
FT /note="G -> C (in BCHED; results in 20% of activity
FT compared to wild-type)"
FT /evidence="ECO:0000269|PubMed:18300943"
FT /id="VAR_072100"
FT VARIANT 393
FT /note="G -> R (in BCHED; dbSNP:rs115129687)"
FT /evidence="ECO:0000269|PubMed:10404729,
FT ECO:0000269|PubMed:1611188, ECO:0000269|PubMed:7634491,
FT ECO:0000269|PubMed:9191541"
FT /id="VAR_040033"
FT VARIANT 414
FT /note="R -> C (in BCHED; dbSNP:rs745364489)"
FT /evidence="ECO:0000269|PubMed:12881446,
FT ECO:0000269|PubMed:15563885"
FT /id="VAR_040034"
FT VARIANT 418
FT /note="G -> V (in BCHED; allele fluoride-2;
FT dbSNP:rs28933390)"
FT /evidence="ECO:0000269|PubMed:1415224"
FT /id="VAR_040035"
FT VARIANT 446
FT /note="F -> S (in BCHED)"
FT /evidence="ECO:0000269|PubMed:7634491,
FT ECO:0000269|PubMed:9191541"
FT /id="VAR_040036"
FT VARIANT 488
FT /note="E -> K (in BCHED; dbSNP:rs200998515)"
FT /evidence="ECO:0000269|PubMed:12881446"
FT /id="VAR_040037"
FT VARIANT 498
FT /note="R -> W (does not affect enzymatic activity;
FT dbSNP:rs115017300)"
FT /evidence="ECO:0000269|PubMed:18300943"
FT /id="VAR_072101"
FT VARIANT 499
FT /note="W -> R (in BCHED; seems to cause reduced expression
FT of the protein)"
FT /evidence="ECO:0000269|PubMed:8554068"
FT /id="VAR_040038"
FT VARIANT 502
FT /note="F -> L (in BCHED; dbSNP:rs769316835)"
FT /evidence="ECO:0000269|PubMed:15563885"
FT /id="VAR_040039"
FT VARIANT 525
FT /note="E -> V (in BCHED; allele J variant;
FT dbSNP:rs121918556)"
FT /evidence="ECO:0000269|PubMed:1349196"
FT /id="VAR_040040"
FT VARIANT 543
FT /note="R -> C (in BCHED; dbSNP:rs199660374)"
FT /evidence="ECO:0000269|PubMed:10404729,
FT ECO:0000269|PubMed:7634491, ECO:0000269|PubMed:9191541"
FT /id="VAR_040041"
FT VARIANT 546
FT /note="Q -> L (in BCHED; seems to cause reduced expression
FT of the protein)"
FT /evidence="ECO:0000269|PubMed:8554068"
FT /id="VAR_040042"
FT VARIANT 567
FT /note="A -> T (in BCHED; allele K variant; with reduced
FT enzyme activity; dbSNP:rs1803274)"
FT /evidence="ECO:0000269|PubMed:11928765,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:7634491,
FT ECO:0000269|PubMed:9191541"
FT /id="VAR_002364"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2XMB"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:6ZWI"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 194..209
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:6ZWI"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:4BDS"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:1P0P"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:6ZWI"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:6EQP"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:2WSL"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:6ZWI"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:2WIK"
FT HELIX 412..425
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 427..438
FT /evidence="ECO:0007829|PDB:6ZWI"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:6ZWI"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 486..505
FT /evidence="ECO:0007829|PDB:6ZWI"
FT TURN 511..514
FT /evidence="ECO:0007829|PDB:6ZWI"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 527..531
FT /evidence="ECO:0007829|PDB:6ZWI"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 544..551
FT /evidence="ECO:0007829|PDB:6ZWI"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:6ZWI"
SQ SEQUENCE 602 AA; 68418 MW; C9836409D9057F27 CRC64;
MHSKVTIICI RFLFWFLLLC MLIGKSHTED DIIIATKNGK VRGMNLTVFG GTVTAFLGIP
YAQPPLGRLR FKKPQSLTKW SDIWNATKYA NSCCQNIDQS FPGFHGSEMW NPNTDLSEDC
LYLNVWIPAP KPKNATVLIW IYGGGFQTGT SSLHVYDGKF LARVERVIVV SMNYRVGALG
FLALPGNPEA PGNMGLFDQQ LALQWVQKNI AAFGGNPKSV TLFGESAGAA SVSLHLLSPG
SHSLFTRAIL QSGSFNAPWA VTSLYEARNR TLNLAKLTGC SRENETEIIK CLRNKDPQEI
LLNEAFVVPY GTPLSVNFGP TVDGDFLTDM PDILLELGQF KKTQILVGVN KDEGTAFLVY
GAPGFSKDNN SIITRKEFQE GLKIFFPGVS EFGKESILFH YTDWVDDQRP ENYREALGDV
VGDYNFICPA LEFTKKFSEW GNNAFFYYFE HRSSKLPWPE WMGVMHGYEI EFVFGLPLER
RDNYTKAEEI LSRSIVKRWA NFAKYGNPNE TQNNSTSWPV FKSTEQKYLT LNTESTRIMT
KLRAQQCRFW TSFFPKVLEM TGNIDEAEWE WKAGFHRWNN YMMDWKNQFN DYTSKKESCV
GL
