CHLE_HORSE
ID CHLE_HORSE Reviewed; 574 AA.
AC P81908;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=EQ-BCHE;
DE AltName: Full=Pseudocholinesterase;
GN Name=BCHE;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Plasma;
RA Moorad D.R., Luo C., Garcia G.E., Doctor B.P.;
RT "Amino acid sequence of horse serum butyrycholinesterase.";
RL (In) Doctor B.P., Taylor P., Quinn D.M., Rotundo R.L., Gentry M.K. (eds.);
RL Structure and function of cholinesterases and related proteins, pp.145-146,
RL Plenum Press, New York and London (1998).
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:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
CC Present in most cells except erythrocytes. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P81908; -.
DR SMR; P81908; -.
DR STRING; 9796.ENSECAP00000000166; -.
DR BindingDB; P81908; -.
DR ChEMBL; CHEMBL5763; -.
DR DrugCentral; P81908; -.
DR ESTHER; horse-BCHE; BCHE.
DR MEROPS; S09.980; -.
DR PaxDb; P81908; -.
DR InParanoid; P81908; -.
DR BRENDA; 3.1.1.8; 2120.
DR Proteomes; UP000002281; 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; IPR014788; AChE_tetra.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000997; Cholinesterase.
DR Pfam; PF08674; AChE_tetra; 1.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Phosphoprotein; Reference proteome; Secreted; Serine esterase.
FT CHAIN 1..574
FT /note="Cholinesterase"
FT /id="PRO_0000070285"
FT ACT_SITE 198
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 438
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06276"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 65..92
FT /evidence="ECO:0000250"
FT DISULFID 252..263
FT /evidence="ECO:0000250"
FT DISULFID 400..519
FT /evidence="ECO:0000250"
FT DISULFID 571
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 574 AA; 65642 MW; 07755EE9FB9CB33E CRC64;
EEDIIITTKN GKVRGMNLPV LGGTVTAFLG IPYAQPPLGR LRFKKPQSLT KWSNIWNATK
YANSCYQNTD QSFPGFLGSE MWNPNTELSE DCLYLNVWIP APKPKNATVM IWIYGGGFQT
GTSSLPVYDG KFLARVERVI VVSMNYRVGA LGFLALSENP EAPGNMGLFD QQLALQWVQK
NIAAFGGNPR SVTLFGESAG AASVSLHLLS PRSQPLFTRA ILQSGSSNAP WAVTSLYEAR
NRTLTLAKRM GCSRDNETEM IKCLRDKDPQ EILLNEVFVV PYDTLLSVNF GPTVDGDFLT
DMPDTLLQLG QFKRTQILVG VNKDEGTAFL VYGAPGFSKD NNSIITRKEF QEGLKIFFPR
VSEFGRESIL FHYMDWLDDQ RAENYREALD DVVGDYNIIC PALEFTRKFS ELGNDAFFYY
FEHRSTKLPW PEWMGVMHGY EIEFVFGLPL ERRVNYTRAE EILSRSIMKR WANFAKYGNP
NGTQNNSTRW PVFKSTEQKY LTLNTESPKV YTKLRAQQCR FWTLFFPKVL ELTGNIDEAE
REWKAGFHRW NNYMMDWKNQ FNDYTSKKES CSDF
