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P32750

- CHLE_CANFA

UniProt

P32750 - CHLE_CANFA

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Protein

Cholinesterase

Gene

BCHE

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters (By similarity).By similarity

Catalytic activityi

An acylcholine + H2O = choline + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei131 – 1311Acyl-ester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. acetylcholinesterase activity Source: UniProtKB
  2. cholinesterase activity Source: UniProtKB

GO - Biological processi

  1. choline metabolic process Source: RefGenome
  2. synaptic transmission, cholinergic Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

MEROPSiS09.980.

Names & Taxonomyi

Protein namesi
Recommended name:
Cholinesterase (EC:3.1.1.8)
Alternative name(s):
Acylcholine acylhydrolase
Butyrylcholine esterase
Choline esterase II
Pseudocholinesterase
Gene namesi
Name:BCHE
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: RefGenome
  2. extracellular space Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›141›141CholinesterasePRO_0000070284Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
Modified residuei131 – 1311PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Expressioni

Tissue specificityi

Present in most cells except erythrocytes.

Interactioni

Subunit structurei

Homotetramer; disulfide-linked. Dimer of dimers (By similarity).By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000021376.

Structurei

3D structure databases

ProteinModelPortaliP32750.
SMRiP32750. Positions 1-141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 502Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2272.
HOGENOMiHOG000091866.
HOVERGENiHBG106132.
InParanoidiP32750.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P32750-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
NTDQSFPGFP GSEMWNPNTD LSEDCLYLNV WIPTPKPKNA TVMIWIYGGG
60 70 80 90 100
FQTGTSSLPV YDGKFLARVE RVIVVSVNYR VGALGFLALP GNPEAPGNLG
110 120 130 140
LFDQQLALQW VQKNIAAFGG NPKSVTLFGE SAGAGSVGLH L
Length:141
Mass (Da):15,086
Last modified:October 1, 1993 - v1
Checksum:i8F81584590111FCB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei141 – 1411

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62411 Genomic DNA. Translation: AAA51451.1.
PIRiE39768.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62411 Genomic DNA. Translation: AAA51451.1 .
PIRi E39768.

3D structure databases

ProteinModelPortali P32750.
SMRi P32750. Positions 1-141.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000021376.

Protein family/group databases

MEROPSi S09.980.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG2272.
HOGENOMi HOG000091866.
HOVERGENi HBG106132.
InParanoidi P32750.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
[Graphical view ]
PRINTSi PR00878. CHOLNESTRASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Use of the polymerase chain reaction for homology probing of butyrylcholinesterase from several vertebrates."
    Arpagaus M., Chatonnet A., Masson P., Newton M., Vaughan T.A., Bartels C.F., Nogueira C.P., la Du B.N., Lockridge O.
    J. Biol. Chem. 266:6966-6974(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.

Entry informationi

Entry nameiCHLE_CANFA
AccessioniPrimary (citable) accession number: P32750
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 1, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3