ID   CHLE_CANLF              Reviewed;         141 AA.
AC   P32750;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 111.
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: Fragment;
GN   Name=BCHE;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=2016308; DOI=10.1016/s0021-9258(20)89597-0;
RA   Arpagaus M., Chatonnet A., Masson P., Newton M., Vaughan T.A.,
RA   Bartels C.F., Nogueira C.P., la Du B.N., Lockridge O.;
RT   "Use of the polymerase chain reaction for homology probing of
RT   butyrylcholinesterase from several vertebrates.";
RL   J. Biol. Chem. 266:6966-6974(1991).
CC   -!- FUNCTION: Esterase with broad substrate specificity. Contributes to the
CC       inactivation of the neurotransmitter acetylcholine. Can degrade
CC       neurotoxic organophosphate esters (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Present in most cells except erythrocytes.
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; M62411; AAA51451.1; -; Genomic_DNA.
DR   PIR; E39768; E39768.
DR   AlphaFoldDB; P32750; -.
DR   SMR; P32750; -.
DR   STRING; 9615.ENSCAFP00000021376; -.
DR   BindingDB; P32750; -.
DR   ChEMBL; CHEMBL4630814; -.
DR   ESTHER; canfa-BCHE; BCHE.
DR   MEROPS; S09.980; -.
DR   PaxDb; P32750; -.
DR   eggNOG; KOG4389; Eukaryota.
DR   InParanoid; P32750; -.
DR   BRENDA; 3.1.1.8; 1153.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003990; F:acetylcholinesterase activity; ISS:UniProtKB.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0004104; F:cholinesterase activity; ISS:UniProtKB.
DR   GO; GO:0006581; P:acetylcholine catabolic process; IBA:GO_Central.
DR   GO; GO:0019695; P:choline metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000997; Cholinesterase.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Phosphoprotein;
KW   Reference proteome; Secreted; Serine esterase.
FT   CHAIN           <1..>141
FT                   /note="Cholinesterase"
FT                   /id="PRO_0000070284"
FT   ACT_SITE        131
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   BINDING         49..50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06276"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         141
SQ   SEQUENCE   141 AA;  15086 MW;  8F81584590111FCB CRC64;
     NTDQSFPGFP GSEMWNPNTD LSEDCLYLNV WIPTPKPKNA TVMIWIYGGG FQTGTSSLPV
     YDGKFLARVE RVIVVSVNYR VGALGFLALP GNPEAPGNLG LFDQQLALQW VQKNIAAFGG
     NPKSVTLFGE SAGAGSVGLH L