Structure of the gene for human butyrylcholinesterase. Evidence for a single copy.

P06276 A8K7P8 CHLE_HUMAN Cholinesterase 3.1.1.8 Acylcholine acylhydrolase Butyrylcholine esterase Choline esterase II Pseudocholinesterase BCHE CHE1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. NUCLEOTIDE SEQUENCE [MRNA] Fetus Brain cDNA clone for human cholinesterase. NUCLEOTIDE SEQUENCE [MRNA] Brain Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT THR-567 Stomach The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Skin Complete amino acid sequence of human serum cholinesterase. PROTEIN SEQUENCE OF 29-602 Plasma Location of disulfide bonds within the sequence of human serum cholinesterase. PARTIAL PROTEIN SEQUENCE DISULFIDE BONDS Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509 AND ASN-514 MASS SPECTROMETRY Plasma Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-85; ASN-369; ASN-483; ASN-509 AND ASN-514 MASS SPECTROMETRY Plasma Adenovirus-transduced human butyrylcholinesterase in mouse blood functions as a bioscavenger of chemical warfare nerve agents. FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY SUBUNIT Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134 AND ASN-284 MASS SPECTROMETRY Liver The structure of G117H mutant of butyrylcholinesterase: nerve agents scavenger. FUNCTION CATALYTIC ACTIVITY Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH SUBSTRATE SUBUNIT GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513 DISULFIDE BONDS ACTIVE SITE Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging. X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH ECHOTHIOPHATE DISULFIDE BONDS GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513 Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase. X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) DISULFIDE BONDS GLYCOSYLATION AT ASN-85; ASN-134; ASN-369 AND ASN-513 SUBUNIT Mechanisms of cholinesterase inhibition by inorganic mercury. X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 29-557 IN COMPLEX WITH MERCURY IONS AND BUTANOIC ACID DISULFIDE BONDS GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513 ENZYME REGULATION Aging of cholinesterases phosphylated by tabun proceeds through O-dealkylation. X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH TABUN ENZYME REGULATION MASS SPECTROMETRY GLYCOSYLATION AT ASN-85; ASN-134; ASN-284; ASN-369 AND ASN-513 Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun. X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH TABUN ANALOGS CATALYTIC ACTIVITY SUBCELLULAR LOCATION TISSUE SPECIFICITY GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-284; ASN-369 AND ASN-513 ENZYME REGULATION Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase. VARIANT BCHE DEFICIENCY GLY-98 DNA mutations associated with the human butyrylcholinesterase J-variant. VARIANT BCHE DEFICIENCY VAL-525 Identification of two different point mutations associated with the fluoride-resistant phenotype for human butyrylcholinesterase. VARIANTS BCHE DEFICIENCY MET-271 AND VAL-418 A variant serum cholinesterase and a confirmed point mutation at Gly-365 to Arg found in a patient with liver cirrhosis. VARIANT BCHE DEFICIENCY ARG-393 Structural basis of the butyrylcholinesterase H-variant segregating in two Danish families. VARIANTS BCHE DEFICIENCY GLY-98 AND MET-170 Genetic basis of the silent phenotype of serum butyrylcholinesterase in three compound heterozygotes. VARIANTS BCHE DEFICIENCY PRO-278; ARG-393; SER-446; CYS-543 AND THR-567 Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia. VARIANT BCHE DEFICIENCY ILE-358 Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene. VARIANTS BCHE DEFICIENCY CYS-61; SER-65; PHE-153; GLU-198; GLY-226; THR-229; ARG-499 AND LEU-546 CHARACTERIZATION OF VARIANTS BCHE DEFICIENCY SER-65; PHE-153; GLU-198; ARG-499 AND LEU-546 Genetic analysis of a Japanese patient with butyrylcholinesterase deficiency. VARIANT BCHE DEFICIENCY CYS-156 Human butyrylcholinesterase L330I mutation belongs to a fluoride-resistant gene, by expression in human fetal kidney cells. VARIANT BUTYRYLCHOLINESTERASE DEFICIENCY ILE-358 Genetic mutations of butyrylcholine esterase identified from phenotypic abnormalities in Japan. VARIANTS BCHE DEFICIENCY ILE-32 DEL; MET-52; SER-128; PRO-278; ARG-295; ILE-358; ARG-393; SER-446; CYS-543 AND THR-567 Characterization of an unstable variant (BChE115D) of human butyrylcholinesterase. VARIANTS BCHE DEFICIENCY GLY-98 AND ASP-143 Identification of a point mutation associated with a silent phenotype of human serum butyrylcholinesterase - a case of familial cholinesterasemia. VARIANT BCHE DEFICIENCY VAL-227 Three point mutations of human butyrylcholinesterase in a Japanese family and the alterations of three-dimensional structure. VARIANTS BCHE DEFICIENCY ILE-358; ARG-393 AND CYS-543 Naturally occurring mutation, Asp70His, in human butyrylcholinesterase. VARIANTS BCHE DEFICIENCY GLY-98; HIS-98; MET-271 AND THR-567 Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine apnea in an Australian population. VARIANTS BCHE DEFICIENCY ILE-56; TYR-124; CYS-414 AND LYS-488 Novel mutations in the BCHE gene in patients with no butyrylcholinesterase activity. VARIANTS BCHE DEFICIENCY CYS-414 AND LEU-502 Naturally occurring mutation Leu307Pro of human butyrylcholinesterase in the Vysya community of India. VARIANT BCHE DEFICIENCY PRO-335 CHARACTERIZATION OF VARIANT BCHE DEFICIENCY PRO-335 Two novel mutations in the BCHE gene in patients with prolonged duration of action of mivacurium or succinylcholine during anaesthesia. VARIANT BCHE DEFICIENCY ASP-356 Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. An acylcholine + H(2)O = choline + a carboxylate. Inhibited by mercury. Inhibited by Tabun. Tabun forms a covalent adduct with Ser-226 that becomes irreversible upon aging. Homotetramer; disulfide-linked. Dimer of dimers. Secreted Detected in blood plasma (at protein level). Present in most cells except erythrocytes. Defects in BCHE are the cause of butyrylcholinesterase deficiency (BChE deficiency) [MIM:177400]. BChE deficiency is a metabolic disorder characterized by prolonged apnoea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium and other ester local anesthetics. The duration of the prolonged apnoea varies significantly depending on the extent of the enzyme deficiency. BChE deficiency is a multifactorial disorder. The hereditary condition is transmitted as an autosomal recessive trait. Belongs to the type-B carboxylesterase/lipase family. 3D-structure Complete proteome Direct protein sequencing Disease mutation Disulfide bond Glycoprotein Hydrolase Polymorphism Reference proteome Secreted Serine esterase Signal T M F I Y C P S D G D H N Y P S G D L F Y C V M D E S G A V A T T M T P E D K R L P A D L I G R R C G V F S E K W R F L E V R C Q L A T MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV GL Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms Distributed under the Creative Commons Attribution-NoDerivs License