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 25-JAN-2012, entry version 131. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=90212557; PubMed=2322535; DOI=10.1021/bi00453a015; RA Arpagaus M., Kott M., Vatsis K.P., Bartels C.F., la Du B.N., RA Lockridge O.; RT "Structure of the gene for human butyrylcholinesterase. Evidence for a RT single copy."; RL Biochemistry 29:124-131(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetus; RX MEDLINE=87231856; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=88016155; PubMed=3477799; DOI=10.1073/pnas.84.19.6682; RA McTiernan C., Adkins S., Chatonnet A., Vaughan T.A., Bartels C.F., RA Kott M., 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 [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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 29-602. RC TISSUE=Plasma; RX MEDLINE=87109144; PubMed=3542989; 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 PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS. RX MEDLINE=88007487; PubMed=3115973; 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 [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509 AND ASN-514, AND MASS RP SPECTROMETRY. 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 [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-85; ASN-369; RP ASN-483; ASN-509 AND ASN-514, AND MASS SPECTROMETRY. 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., RA Moore R.J., 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 [10] 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 RT functions as a bioscavenger of chemical warfare nerve agents."; RL Mol. Pharmacol. 76:612-617(2009). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134 AND ASN-284, AND MASS RP SPECTROMETRY. 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 RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [12] 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 [13] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH RP SUBSTRATE, SUBUNIT, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 RP AND ASN-513, 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 RT with substrate and products."; RL J. Biol. Chem. 278:41141-41147(2003). RN [14] 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 RT mechanisms of aging."; RL Biochemistry 44:1154-1162(2005). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION RP AT 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 [16] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 29-557 IN COMPLEX WITH RP MERCURY IONS AND BUTANOIC ACID, DISULFIDE BONDS, GLYCOSYLATION AT RP ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513, AND ENZYME 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 [17] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH RP TABUN, ENZYME REGULATION, MASS SPECTROMETRY, AND GLYCOSYLATION AT RP 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., RA Gillon E., Froment M.T., Lockridge O., Schopfer L.M., Masson P., RA Nachon F.; RT "Aging of cholinesterases phosphylated by tabun proceeds through O- RT dealkylation."; RL J. Am. Chem. Soc. 130:16011-16020(2008). RN [18] 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 RP ASN-513, AND ENZYME 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 [19] RP VARIANT BCHE DEFICIENCY GLY-98. RX MEDLINE=89128896; 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 RT dibucaine-resistant (atypical) variant form of human serum RT cholinesterase."; RL Proc. Natl. Acad. Sci. U.S.A. 86:953-957(1989). RN [20] RP VARIANT BCHE DEFICIENCY VAL-525. RX PubMed=1349196; RA Bartels C.F., James K., La Du B.N.; RT "DNA mutations associated with the human butyrylcholinesterase J- RT variant."; RL Am. J. Hum. Genet. 50:1104-1114(1992). RN [21] RP VARIANTS BCHE DEFICIENCY 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 [22] RP VARIANT BCHE DEFICIENCY ARG-393. RX PubMed=1611188; RA Hada T., Muratani K., Ohue T., Imanishi H., Moriwaki Y., Itoh M., RA Amuro Y., Higashino K.; RT "A variant serum cholinesterase and a confirmed point mutation at Gly- RT 365 to Arg found in a patient with liver cirrhosis."; RL Intern. Med. 31:357-362(1992). RN [23] RP VARIANTS BCHE DEFICIENCY GLY-98 AND MET-170. RX PubMed=1306123; RA Jensen F.S., Bartels C.F., La Du B.N.; RT "Structural basis of the butyrylcholinesterase H-variant segregating RT in two Danish families."; RL Pharmacogenetics 2:234-240(1992). RN [24] RP VARIANTS BCHE DEFICIENCY PRO-278; ARG-393; SER-446; CYS-543 AND RP 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., RA Izumi M., Etoh K.; RT "Genetic basis of the silent phenotype of serum butyrylcholinesterase RT in three compound heterozygotes."; RL Clin. Chim. Acta 235:41-57(1995). RN [25] RP VARIANT BCHE DEFICIENCY ILE-358. RX MEDLINE=96287386; 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 [26] RP VARIANTS BCHE DEFICIENCY CYS-61; SER-65; PHE-153; GLU-198; GLY-226; RP THR-229; ARG-499 AND LEU-546, AND CHARACTERIZATION OF VARIANTS BCHE RP DEFICIENCY SER-65; PHE-153; 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 RT butyrylcholinesterase (BCHE) gene."; RL Am. J. Hum. Genet. 58:52-64(1996). RN [27] RP VARIANT BCHE DEFICIENCY CYS-156. RX PubMed=9543549; DOI=10.1017/S0003480097006520; RA Hidaka K., Iuchi I., Tomita M., Watanabe Y., Minatogawa Y., RA Iwasaki K., Gotoh K., Shimizu C.; RT "Genetic analysis of a Japanese patient with butyrylcholinesterase RT deficiency."; RL Ann. Hum. Genet. 61:491-496(1997). RN [28] 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- RT resistant gene, by expression in human fetal kidney cells."; RL Biochem. Biophys. Res. Commun. 240:372-375(1997). RN [29] RP VARIANTS BCHE DEFICIENCY ILE-32 DEL; MET-52; SER-128; PRO-278; RP ARG-295; ILE-358; 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., RA Kanno T.; RT "Genetic mutations of butyrylcholine esterase identified from RT phenotypic abnormalities in Japan."; RL Clin. Chem. 43:924-929(1997). RN [30] RP VARIANTS BCHE DEFICIENCY GLY-98 AND ASP-143. RX PubMed=9110359; 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 [31] RP VARIANT BCHE DEFICIENCY 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 RT of human serum butyrylcholinesterase - a case of familial RT cholinesterasemia."; RL Clin. Chim. Acta 274:159-166(1998). RN [32] RP VARIANTS BCHE DEFICIENCY 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 RT family and the alterations of three-dimensional structure."; RL Clin. Chim. Acta 283:33-42(1999). RN [33] RP VARIANTS BCHE DEFICIENCY 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 RT butyrylcholinesterase."; RL Ann. Clin. Biochem. 39:154-156(2002). RN [34] RP VARIANTS BCHE DEFICIENCY ILE-56; TYR-124; CYS-414 AND LYS-488. RX PubMed=12881446; RA Yen T., Nightingale B.N., Burns J.C., Sullivan D.R., Stewart P.M.; RT "Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine RT apnea in an Australian population."; RL Clin. Chem. 49:1297-1308(2003). RN [35] RP VARIANTS BCHE DEFICIENCY 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., RA Chan Y.-W., 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 RT butyrylcholinesterase activity."; RL Clin. Chim. Acta 351:155-159(2005). RN [36] RP VARIANT BCHE DEFICIENCY PRO-335, AND CHARACTERIZATION OF VARIANT BCHE RP DEFICIENCY 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 RT in the Vysya community of India."; RL Pharmacogenet. Genomics 16:461-468(2006). RN [37] RP VARIANT BCHE DEFICIENCY 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 RT duration of action of mivacurium or succinylcholine during RT anaesthesia."; RL Pharmacogenet. Genomics 17:995-999(2007). CC -!- FUNCTION: Esterase with broad substrate specificity. Contributes CC to the inactivation of the neurotransmitter acetylcholine. Can CC degrade neurotoxic organophosphate esters. CC -!- CATALYTIC ACTIVITY: An acylcholine + H(2)O = choline + a CC carboxylate. CC -!- ENZYME REGULATION: Inhibited by mercury. Inhibited by Tabun. Tabun CC forms a covalent adduct with Ser-226 that becomes irreversible CC upon aging. CC -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level). CC Present in most cells except erythrocytes. CC -!- DISEASE: Defects in BCHE are the cause of butyrylcholinesterase CC deficiency (BChE deficiency) [MIM:177400]. BChE deficiency is a CC metabolic disorder characterized by prolonged apnoea after the use CC of certain anesthetic drugs, including the muscle relaxants CC succinylcholine or mivacurium and other ester local anesthetics. CC The duration of the prolonged apnoea varies significantly CC depending on the extent of the enzyme deficiency. BChE deficiency CC is a multifactorial disorder. The hereditary condition is CC transmitted as an autosomal recessive trait. CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; 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 IPI; IPI00025864; -. DR PIR; A33769; ACHU. DR RefSeq; NP_000046.1; NM_000055.2. DR UniGene; Hs.420483; -. DR PDB; 1EHO; Model; -; A=30-560. DR PDB; 1EHQ; Model; -; A=30-560. DR PDB; 1KCJ; Model; -; A=30-560. 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 PDBsum; 1EHO; -. DR PDBsum; 1EHQ; -. DR PDBsum; 1KCJ; -. 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 ProteinModelPortal; P06276; -. DR SMR; P06276; 32-562, 564-592. DR DIP; DIP-46476N; -. DR STRING; P06276; -. DR MEROPS; S09.980; -. DR DMDM; 116353; -. DR PRIDE; P06276; -. DR Ensembl; ENST00000264381; ENSP00000264381; ENSG00000114200. DR GeneID; 590; -. DR KEGG; hsa:590; -. DR UCSC; uc003fem.2; human. DR CTD; 590; -. DR GeneCards; GC03M165490; -. DR H-InvDB; HIX0003828; -. DR HGNC; HGNC:983; BCHE. DR HPA; HPA001560; -. DR MIM; 177400; gene+phenotype. DR neXtProt; NX_P06276; -. DR Orphanet; 132; Butyrylcholinesterase deficiency. DR Orphanet; 240861; Cisatracurium toxicity. DR Orphanet; 240891; Mivacurium toxicity. DR Orphanet; 240895; Pancuronium toxicity. DR Orphanet; 240907; Rocuronium toxicity. DR Orphanet; 240911; Satracurium toxicity. DR Orphanet; 241023; Susceptibility to prolonged paralysis due to cisatracurium treatment. DR Orphanet; 240917; Vecuronium toxicity. DR PharmGKB; PA25294; -. DR eggNOG; prNOG18197; -. DR HOGENOM; HBG716688; -. DR HOVERGEN; HBG008839; -. DR InParanoid; P06276; -. DR OMA; SILFHYM; -. DR OrthoDB; EOG46WZ86; -. DR PhylomeDB; P06276; -. DR Reactome; REACT_15380; Diabetes pathways. DR DrugBank; DB01122; Ambenonium. DR DrugBank; DB00572; Atropine. DR DrugBank; DB01408; Bambuterol. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB00122; Choline. DR DrugBank; DB00568; Cinnarizine. DR DrugBank; DB00944; Demecarium bromide. DR DrugBank; DB00527; Dibucaine. DR DrugBank; DB00843; Donepezil. DR DrugBank; DB01057; Echothiophate Iodide. DR DrugBank; DB01010; Edrophonium. DR DrugBank; DB00392; Ethopropazine. DR DrugBank; DB00292; Etomidate. DR DrugBank; DB00674; Galantamine. DR DrugBank; DB00941; Hexafluronium bromide. DR DrugBank; DB00677; Isoflurophate. DR DrugBank; DB00358; Mefloquine. DR DrugBank; DB01226; Mivacurium. DR DrugBank; DB01400; Neostigmine. DR DrugBank; DB01337; Pancuronium. DR DrugBank; DB00733; Pralidoxime. DR DrugBank; DB01035; Procainamide. DR DrugBank; DB00545; Pyridostigmine. DR DrugBank; DB00989; Rivastigmine. DR DrugBank; DB00202; Succinylcholine. DR DrugBank; DB00871; Terbutaline. DR DrugBank; DB01116; Trimethaphan. DR NextBio; 2405; -. DR ArrayExpress; P06276; -. DR Bgee; P06276; -. DR CleanEx; HS_BCHE; -. DR Genevestigator; P06276; -. DR GermOnline; ENSG00000114200; Homo sapiens. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:RefGenome. DR GO; GO:0005615; C:extracellular space; IBA:RefGenome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0003990; F:acetylcholinesterase activity; ISS:UniProtKB. DR GO; GO:0001540; F:beta-amyloid binding; NAS:UniProtKB. DR GO; GO:0004091; F:carboxylesterase activity; IBA:RefGenome. DR GO; GO:0019899; F:enzyme binding; NAS:UniProtKB. DR GO; GO:0019695; P:choline metabolic process; IBA:RefGenome. DR GO; GO:0050783; P:cocaine metabolic process; TAS:UniProtKB. DR GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:RefGenome. 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 KO; K01050; -. DR Pfam; PF08674; AChE_tetra; 1. DR Pfam; PF00135; COesterase; 1. DR PRINTS; PR00878; CHOLNESTRASE. DR ProDom; PD415333; AChE_tetra; 1. DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Disease mutation; Disulfide bond; Glycoprotein; Hydrolase; KW Polymorphism; Reference proteome; Secreted; Serine esterase; Signal. FT SIGNAL 1 28 FT CHAIN 29 602 Cholinesterase. FT /FTId=PRO_0000008613. FT REGION 144 145 Substrate binding. FT ACT_SITE 226 226 Acyl-ester intermediate. FT ACT_SITE 353 353 Charge relay system. FT ACT_SITE 466 466 Charge relay system. FT CARBOHYD 45 45 N-linked (GlcNAc...). FT CARBOHYD 85 85 N-linked (GlcNAc...). FT CARBOHYD 134 134 N-linked (GlcNAc...). FT CARBOHYD 269 269 N-linked (GlcNAc...). FT CARBOHYD 284 284 N-linked (GlcNAc...). FT CARBOHYD 369 369 N-linked (GlcNAc...). FT CARBOHYD 483 483 N-linked (GlcNAc...). FT CARBOHYD 509 509 N-linked (GlcNAc...). FT CARBOHYD 513 513 N-linked (GlcNAc...). FT CARBOHYD 514 514 N-linked (GlcNAc...). FT DISULFID 93 120 FT DISULFID 280 291 FT DISULFID 428 547 FT DISULFID 599 599 Interchain. FT VARIANT 32 32 Missing (in BChE deficiency). FT /FTId=VAR_040011. FT VARIANT 52 52 T -> M (in BChE deficiency; FT dbSNP:rs56309853). FT /FTId=VAR_040012. FT VARIANT 56 56 F -> I (in BChE deficiency). FT /FTId=VAR_040013. FT VARIANT 61 61 Y -> C (in BChE deficiency; enzymatically FT inactive in the plasma). FT /FTId=VAR_040014. FT VARIANT 65 65 P -> S (in BChE deficiency; seems to FT cause reduced expression of the protein). FT /FTId=VAR_040015. FT VARIANT 98 98 D -> G (in BChE deficiency; BChE atypical FT form; dibucaine-resistant; FT dbSNP:rs1799807). FT /FTId=VAR_002360. FT VARIANT 98 98 D -> H (in BChE deficiency). FT /FTId=VAR_040016. FT VARIANT 124 124 N -> Y (in BChE deficiency). FT /FTId=VAR_040017. FT VARIANT 128 128 P -> S (in BChE deficiency; FT dbSNP:rs3732880). FT /FTId=VAR_040018. FT VARIANT 143 143 G -> D (in BChE deficiency). FT /FTId=VAR_040019. FT VARIANT 153 153 L -> F (in BChE deficiency; seems to FT cause reduced expression of the protein). FT /FTId=VAR_040020. FT VARIANT 156 156 Y -> C (in BChE deficiency). FT /FTId=VAR_040021. FT VARIANT 170 170 V -> M (in BChE deficiency; allele H FT variant). FT /FTId=VAR_040022. FT VARIANT 198 198 D -> E (in BChE deficiency; seems to FT cause reduced expression of the protein). FT /FTId=VAR_040023. FT VARIANT 226 226 S -> G (in BChE deficiency; enzymatically FT inactive in the plasma). FT /FTId=VAR_040024. FT VARIANT 227 227 A -> V (in BChE deficiency). FT /FTId=VAR_040025. FT VARIANT 229 229 A -> T (in BChE deficiency; enzymatically FT inactive in the plasma). FT /FTId=VAR_040026. FT VARIANT 271 271 T -> M (in BChE deficiency; allele FT fluoride-1; dbSNP:rs28933389). FT /FTId=VAR_040027. FT VARIANT 278 278 T -> P (in BChE deficiency). FT /FTId=VAR_040028. FT VARIANT 283 283 E -> D (in dbSNP:rs16849700). FT /FTId=VAR_040029. FT VARIANT 295 295 K -> R (in BChE deficiency). FT /FTId=VAR_040030. FT VARIANT 335 335 L -> P (in BChE deficiency; expressed at FT very low level). FT /FTId=VAR_040031. FT VARIANT 356 356 A -> D (in BChE deficiency). FT /FTId=VAR_040032. FT VARIANT 358 358 L -> I (in BChE deficiency; BChE variant FT form; fluoride-resistant; Japanese type). FT /FTId=VAR_002362. FT VARIANT 393 393 G -> R (in BChE deficiency). FT /FTId=VAR_040033. FT VARIANT 414 414 R -> C (in BChE deficiency). FT /FTId=VAR_040034. FT VARIANT 418 418 G -> V (in BChE deficiency; allele FT fluoride-2; dbSNP:rs28933390). FT /FTId=VAR_040035. FT VARIANT 446 446 F -> S (in BChE deficiency). FT /FTId=VAR_040036. FT VARIANT 488 488 E -> K (in BChE deficiency). FT /FTId=VAR_040037. FT VARIANT 499 499 W -> R (in BChE deficiency; seems to FT cause reduced expression of the protein). FT /FTId=VAR_040038. FT VARIANT 502 502 F -> L (in BChE deficiency). FT /FTId=VAR_040039. FT VARIANT 525 525 E -> V (in BChE deficiency; allele J FT variant). FT /FTId=VAR_040040. FT VARIANT 543 543 R -> C (in BChE deficiency). FT /FTId=VAR_040041. FT VARIANT 546 546 Q -> L (in BChE deficiency; seems to FT cause reduced expression of the protein). FT /FTId=VAR_040042. FT VARIANT 567 567 A -> T (in BChE deficiency; allele K FT variant; with reduced enzyme activity; FT dbSNP:rs1803274). FT /FTId=VAR_002364. FT STRAND 33 36 FT STRAND 39 42 FT STRAND 44 48 FT STRAND 51 60 FT HELIX 67 69 FT STRAND 82 85 FT HELIX 105 108 FT STRAND 122 130 FT STRAND 133 141 FT TURN 145 147 FT HELIX 154 156 FT HELIX 159 165 FT STRAND 168 172 FT HELIX 177 181 FT HELIX 194 209 FT HELIX 210 213 FT STRAND 215 225 FT HELIX 227 237 FT HELIX 239 244 FT STRAND 246 252 FT HELIX 264 277 FT HELIX 285 292 FT HELIX 297 304 FT HELIX 305 307 FT STRAND 308 310 FT STRAND 324 326 FT HELIX 331 336 FT STRAND 345 350 FT HELIX 355 358 FT TURN 359 361 FT HELIX 375 385 FT HELIX 391 401 FT HELIX 412 425 FT HELIX 427 438 FT TURN 439 441 FT STRAND 444 449 FT HELIX 460 462 FT TURN 466 469 FT HELIX 470 473 FT HELIX 476 478 FT HELIX 486 505 FT TURN 511 514 FT TURN 523 525 FT STRAND 527 531 FT STRAND 538 541 FT HELIX 544 551 FT TURN 552 555 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 //