CHLE_SHEEP
ID CHLE_SHEEP Reviewed; 141 AA.
AC P32753;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
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; M62780; AAA31509.1; -; Genomic_DNA.
DR PIR; B39768; B39768.
DR AlphaFoldDB; P32753; -.
DR SMR; P32753; -.
DR STRING; 9940.ENSOARP00000001621; -.
DR ESTHER; sheep-BCHE; BCHE.
DR MEROPS; S09.980; -.
DR eggNOG; KOG4389; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003990; F:acetylcholinesterase activity; ISS:UniProtKB.
DR GO; GO:0004104; F:cholinesterase activity; ISS:UniProtKB.
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_0000070288"
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; 15234 MW; 5FDFAA11730564D3 CRC64;
NTDQSFPGFL GSEMWNPNTD LSEDCLYLNV WIPTPKPKNA TVMIWIYGGS FQTGTSSLHV
YDGKFLARVE RVIVVSMNYR VGALGFLALP GNPEAPGNVG LFDQQLALQW VQKNIAAFGG
NPKSVTLFGE SAGAASVSLH L
