P81908 (CHLE_HORSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cholinesterase
EC=3.1.1.8

Alternative name(s):
Acylcholine acylhydrolase
Butyrylcholine esterase
Choline esterase II
EQ-BCHE
Pseudocholinesterase

Gene names

Name:

BCHE

Organism

Equus caballus (Horse) [Reference proteome]

Taxonomic identifier

9796 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus › Equus

Protein attributes

Sequence length	574 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters By similarity.
Catalytic activity	An acylcholine + H2O = choline + a carboxylate.
Subunit structure	Homotetramer; disulfide-linked. Dimer of dimers By similarity.
Subcellular location	Secreted Ref.1.
Tissue specificity	Detected in blood plasma (at protein level). Present in most cells except erythrocytes. Ref.1
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	acetylcholinesterase activity Inferred from sequence or structural similarity. Source: UniProtKB carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 574	574	Cholinesterase		PRO_0000070285
Regions
	Region	116 – 117	2	Substrate binding By similarity
Sites
	Active site	198	1	Acyl-ester intermediate By similarity
	Active site	325	1	Charge relay system By similarity
	Active site	438	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	198	1	Phosphoserine By similarity
	Glycosylation	57	1	N-linked (GlcNAc...)
	Glycosylation	106	1	N-linked (GlcNAc...)
	Glycosylation	241	1	N-linked (GlcNAc...)
	Glycosylation	256	1	N-linked (GlcNAc...)
	Glycosylation	341	1	N-linked (GlcNAc...)
	Glycosylation	455	1	N-linked (GlcNAc...)
	Glycosylation	481	1	N-linked (GlcNAc...)
	Glycosylation	486	1	N-linked (GlcNAc...)
	Disulfide bond	65 ↔ 92		By similarity
	Disulfide bond	252 ↔ 263		By similarity
	Disulfide bond	400 ↔ 519		By similarity
	Disulfide bond	571		Interchain By similarity

Sequences

	Sequence		Length	Mass (Da)
	P81908 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 07755EE9FB9CB33E	FASTA	574	65,642
	10 20 30 40 50 60 EEDIIITTKN GKVRGMNLPV LGGTVTAFLG IPYAQPPLGR LRFKKPQSLT KWSNIWNATK 70 80 90 100 110 120 YANSCYQNTD QSFPGFLGSE MWNPNTELSE DCLYLNVWIP APKPKNATVM IWIYGGGFQT 130 140 150 160 170 180 GTSSLPVYDG KFLARVERVI VVSMNYRVGA LGFLALSENP EAPGNMGLFD QQLALQWVQK 190 200 210 220 230 240 NIAAFGGNPR SVTLFGESAG AASVSLHLLS PRSQPLFTRA ILQSGSSNAP WAVTSLYEAR 250 260 270 280 290 300 NRTLTLAKRM GCSRDNETEM IKCLRDKDPQ EILLNEVFVV PYDTLLSVNF GPTVDGDFLT 310 320 330 340 350 360 DMPDTLLQLG QFKRTQILVG VNKDEGTAFL VYGAPGFSKD NNSIITRKEF QEGLKIFFPR 370 380 390 400 410 420 VSEFGRESIL FHYMDWLDDQ RAENYREALD DVVGDYNIIC PALEFTRKFS ELGNDAFFYY 430 440 450 460 470 480 FEHRSTKLPW PEWMGVMHGY EIEFVFGLPL ERRVNYTRAE EILSRSIMKR WANFAKYGNP 490 500 510 520 530 540 NGTQNNSTRW PVFKSTEQKY LTLNTESPKV YTKLRAQQCR FWTLFFPKVL ELTGNIDEAE 550 560 570 REWKAGFHRW NNYMMDWKNQ FNDYTSKKES CSDF

References

[1]

"Amino acid sequence of horse serum butyrycholinesterase." Moorad D.R., Luo C., Garcia G.E., Doctor B.P. (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) Cited for: PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Plasma.

Cross-references

Sequence databases
UniGene	Eca.13015.
3D structure databases
ProteinModelPortal	P81908.
SMR	P81908. Positions 4-534, 536-567.
ModBase	Search...
Protein-protein interaction databases
STRING	9796.ENSECAP00000000166.
Protein family/group databases
MEROPS	S09.980.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG2272.
HOVERGEN	HBG008839.
InParanoid	P81908.
OrthoDB	EOG46WZ86.
Family and domain databases
InterPro	IPR014788. AChE_tetra. IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. IPR019819. Carboxylesterase_B_CS. IPR000997. Cholinesterase. [Graphical view]
Pfam	PF08674. AChE_tetra. 1 hit. PF00135. COesterase. 1 hit. [Graphical view]
PRINTS	PR00878. CHOLNESTRASE.
ProDom	PD415333. AChE_tetra. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00122. CARBOXYLESTERASE_B_1. 1 hit. PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P81908.
ChEMBL	CHEMBL5763.

Entry information

Entry name

CHLE_HORSE

Accession

Primary (citable) accession number: P81908

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program