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 27-MAR-2024, entry version 234. 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 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}. 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; 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; 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 PDB; 7Q1M; X-ray; 2.79 A; A=29-557. DR PDB; 7Q1N; X-ray; 2.35 A; A=29-557. DR PDB; 7Q1O; X-ray; 2.65 A; A=29-557. DR PDB; 7Q1P; X-ray; 2.35 A; A=29-557. DR PDB; 7QBQ; X-ray; 2.49 A; A=29-557. DR PDB; 7QBR; X-ray; 2.13 A; A=29-557. DR PDB; 7QHD; X-ray; 2.04 A; A=29-557. DR PDB; 7QHE; X-ray; 2.47 A; A=29-557. DR PDB; 7ZPB; X-ray; 2.31 A; A=29-557. DR PDB; 8AI7; X-ray; 2.13 A; F=29-557. DR PDB; 8AM1; X-ray; 2.53 A; A=29-557. DR PDB; 8AM2; X-ray; 2.50 A; A=29-557. DR PDB; 8CGO; X-ray; 2.65 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; 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 PDBsum; 7Q1M; -. DR PDBsum; 7Q1N; -. DR PDBsum; 7Q1O; -. DR PDBsum; 7Q1P; -. DR PDBsum; 7QBQ; -. DR PDBsum; 7QBR; -. DR PDBsum; 7QHD; -. DR PDBsum; 7QHE; -. DR PDBsum; 7ZPB; -. DR PDBsum; 8AI7; -. DR PDBsum; 8AM1; -. DR PDBsum; 8AM2; -. DR PDBsum; 8CGO; -. DR AlphaFoldDB; P06276; -. DR EMDB; EMD-0256; -. DR EMDB; EMD-4400; -. DR SMR; P06276; -. DR BioGRID; 107064; 65. 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; DB03128; Acetylcholine. 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; DB01064; Isoprenaline. 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 GlyCosmos; P06276; 10 sites, 12 glycans. DR GlyGen; P06276; 13 sites, 15 N-linked glycans (4 sites), 1 O-linked glycan (1 site). DR iPTMnet; P06276; -. DR PhosphoSitePlus; P06276; -. DR SwissPalm; 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; 9606-ENSP00000264381; -. DR PeptideAtlas; P06276; -. DR ProteomicsDB; 51880; -. DR ABCD; P06276; 4 sequenced antibodies. DR Antibodypedia; 879; 507 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 AGR; HGNC:983; -. 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; Hereditary butyrylcholinesterase deficiency. DR PharmGKB; PA25294; -. DR VEuPathDB; HostDB:ENSG00000114200; -. DR eggNOG; KOG4389; Eukaryota. DR GeneTree; ENSGT00940000157023; -. DR InParanoid; P06276; -. DR OMA; YICPGID; -. DR OrthoDB; 4386at2759; -. 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 1167 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 162 other cell types or tissues. DR ExpressionAtlas; P06276; baseline and differential. 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: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 CDD; cd00312; Esterase_lipase; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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 PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1. DR PANTHER; PTHR43918:SF5; CHOLINESTERASE; 1. DR Pfam; PF08674; AChE_tetra; 1. DR Pfam; PF00135; COesterase; 1. DR PRINTS; PR00878; CHOLNESTRASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. DR Genevisible; P06276; HS. 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; FT 2-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 FT V-62; 2-fold lower affinity for butyrylthiocholine; 10-fold FT lower affinity for butyrylthiocholine in the presence of FT V-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; FT fluoride-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 //