ID   CHLE_BOVIN              Reviewed;         602 AA.
AC   P32749; Q08DR6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   24-JAN-2024, entry version 149.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-236.
RC   TISSUE=Lung;
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}.
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DR   EMBL; BC123600; AAI23601.1; -; mRNA.
DR   EMBL; M62410; AAA51412.1; -; Genomic_DNA.
DR   PIR; F39768; F39768.
DR   RefSeq; NP_001070374.1; NM_001076906.1.
DR   AlphaFoldDB; P32749; -.
DR   SMR; P32749; -.
DR   STRING; 9913.ENSBTAP00000014794; -.
DR   ESTHER; bovin-BCHE; BCHE.
DR   MEROPS; S09.980; -.
DR   GlyCosmos; P32749; 9 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000014794; -.
DR   Ensembl; ENSBTAT00000068356.1; ENSBTAP00000068076.1; ENSBTAG00000011139.6.
DR   GeneID; 534616; -.
DR   KEGG; bta:534616; -.
DR   CTD; 590; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011139; -.
DR   VGNC; VGNC:26443; BCHE.
DR   eggNOG; KOG4389; Eukaryota.
DR   GeneTree; ENSGT00940000157023; -.
DR   HOGENOM; CLU_006586_13_0_1; -.
DR   InParanoid; P32749; -.
DR   OMA; YICPGID; -.
DR   TreeFam; TF315470; -.
DR   BRENDA; 3.1.1.8; 908.
DR   Reactome; R-BTA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR   Reactome; R-BTA-9749641; Aspirin ADME.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000011139; Expressed in duodenum and 97 other cell types or tissues.
DR   ExpressionAtlas; P32749; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
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:0004104; F:cholinesterase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0006581; P:acetylcholine catabolic process; IBA:GO_Central.
DR   GO; GO:0019695; P:choline metabolic process; IBA:GO_Central.
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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Phosphoprotein;
KW   Reference proteome; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..602
FT                   /note="Cholinesterase"
FT                   /id="PRO_0000070283"
FT   ACT_SITE        226
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        353
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        466
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         144..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06276"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        513
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   602 AA;  68867 MW;  CDFB404E64C46935 CRC64;
     MQSRSTVIYI RFVLWFLLLW VLFEKSHTEE DIIITTKNGK VRGMHLPVLG GTVTAFLGIP
     YAQPPLGRLR FKKPQSLTKW PDIWNATKYA NSCYQNTDQS FPGFLGSEMW NPNTDLSEDC
     LYLNVWIPTP KPKNATVMIW IYGGSFQTGT SSLHVYDGKF LARVERVIVV SMNYRVGALG
     FLALPGNPEA PGNVGLFDQQ LALQWVQKNI AAFGGNPKSV TLFGESAGAA SVSLHLLSPE
     SHPLFTRAIL QSGSSNAPWA VTSRYEARNR TLTLAKFIGC SRENDTEIIK CLRNKDPQEI
     LRHEVFVVPY GTLLSVNFGP TVDGDFLTDM PDTLLQLGQF KKTQILVGVN KDEGTAFLVY
     GAPGFSKDNN SIITRKEFQE GLKIFFPGVS EFGKESILFH YMDWLDDQRA EKYREALDDV
     VGDYNIICPA LEFTKKFSDM GNNAFFYYFE HRSSKLPWPE WMGVMHGYEI EFVFGLPLER
     RVNYTKAEEI FSRSIMKRWA NFAKYGNPNG TQNNSTRWPV FKSNEQKYFT LNTESPKVNT
     KLRAQQCRFW TLFFPKVLEI TGNIDEVERE WKAGFHRWNN YMMDWKNQFN DYTSKKESCA
     GL
//