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Cholinesterase (EC 3.1.1.8) (Acylcholine acylhydrolase) (Butyrylcholine esterase) (Choline esterase II) (EQ-BCHE) (Pseudocholinesterase)

 CHLE_HORSE              Reviewed;         574 AA.
P81908;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
10-MAY-2017, entry version 83.
RecName: Full=Cholinesterase;
EC=3.1.1.8;
AltName: Full=Acylcholine acylhydrolase;
AltName: Full=Butyrylcholine esterase;
AltName: Full=Choline esterase II;
AltName: Full=EQ-BCHE;
AltName: Full=Pseudocholinesterase;
Name=BCHE;
Equus caballus (Horse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9796;
[1]
PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Plasma;
Moorad D.R., Luo C., Garcia G.E., Doctor B.P.;
"Amino acid sequence of horse serum butyrycholinesterase.";
(In) Doctor B.P., Taylor P., Quinn D.M., Rotundo R.L., Gentry M.K.
(eds.);
Structure and function of cholinesterases and related proteins,
pp.145-146, Plenum Press, New York and London (1998).
-!- FUNCTION: Esterase with broad substrate specificity. Contributes
to the inactivation of the neurotransmitter acetylcholine. Can
degrade neurotoxic organophosphate esters (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: An acylcholine + H(2)O = choline + a
carboxylate.
-!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
Present in most cells except erythrocytes. {ECO:0000269|Ref.1}.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
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UniGene; Eca.13015; -.
ProteinModelPortal; P81908; -.
SMR; P81908; -.
STRING; 9796.ENSECAP00000000166; -.
BindingDB; P81908; -.
ChEMBL; CHEMBL5763; -.
ESTHER; horse-BCHE; BCHE.
MEROPS; S09.980; -.
PaxDb; P81908; -.
PRIDE; P81908; -.
eggNOG; KOG4389; Eukaryota.
eggNOG; COG2272; LUCA.
HOVERGEN; HBG008839; -.
InParanoid; P81908; -.
Proteomes; UP000002281; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0003990; F:acetylcholinesterase activity; ISS:UniProtKB.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
GO; GO:0004104; F:cholinesterase activity; ISS:UniProtKB.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR014788; AChE_tetra.
InterPro; IPR002018; CarbesteraseB.
InterPro; IPR019826; Carboxylesterase_B_AS.
InterPro; IPR019819; Carboxylesterase_B_CS.
InterPro; IPR000997; Cholinesterase.
Pfam; PF08674; AChE_tetra; 1.
Pfam; PF00135; COesterase; 1.
PRINTS; PR00878; CHOLNESTRASE.
ProDom; PD415333; AChE_tetra; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Phosphoprotein; Reference proteome; Secreted;
Serine esterase.
CHAIN 1 574 Cholinesterase.
/FTId=PRO_0000070285.
REGION 116 117 Substrate binding. {ECO:0000250}.
ACT_SITE 198 198 Acyl-ester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10039}.
ACT_SITE 325 325 Charge relay system. {ECO:0000250}.
ACT_SITE 438 438 Charge relay system. {ECO:0000250}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000250|UniProtKB:P06276}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
CARBOHYD 455 455 N-linked (GlcNAc...) asparagine.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
CARBOHYD 486 486 N-linked (GlcNAc...) asparagine.
DISULFID 65 92 {ECO:0000250}.
DISULFID 252 263 {ECO:0000250}.
DISULFID 400 519 {ECO:0000250}.
DISULFID 571 571 Interchain. {ECO:0000250}.
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


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