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P36196 (ACES_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylcholinesterase

Short name=AChE
EC=3.1.1.7
Gene names
Name:ACHE
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length767 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.

Catalytic activity

Acetylcholine + H2O = choline + acetate.

Subunit structure

Oligomer composed of disulfide-linked homodimers.

Subcellular location

Cell junctionsynapse. Secreted. Cell membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
Synapse
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholine metabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

neurotransmitter catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of axonogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of dendrite morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

synaptic transmission, cholinergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentaxon

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from Biological aspect of Ancestor. Source: RefGenome

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

endoplasmic reticulum lumen

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuromuscular junction

Inferred from Biological aspect of Ancestor. Source: RefGenome

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

presynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionacetylcholinesterase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

cholinesterase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 767748Acetylcholinesterase
PRO_0000008591

Sites

Active site2271Acyl-ester intermediate By similarity
Active site5201Charge relay system By similarity
Active site6331Charge relay system By similarity

Amino acid modifications

Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential
Glycosylation6501N-linked (GlcNAc...) Potential
Glycosylation7251N-linked (GlcNAc...) Potential
Disulfide bond94 ↔ 121 By similarity
Disulfide bond281 ↔ 292 By similarity
Disulfide bond595 ↔ 713 By similarity
Disulfide bond764Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
P36196 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: B1B3DF29C31F6062

FASTA76783,020
        10         20         30         40         50         60 
MAPLFLLLLL LLSPSPTSAH RFAYSAPNRP EVRTTTGSVR GLLIPAGPSG STAAAFLGIP 

        70         80         90        100        110        120 
FAVPPLGPLR FRPPLPIPTP WTGIRDADSQ PFACYQMVDT TFPGFQGSEM WNPNREMSED 

       130        140        150        160        170        180 
CLYLNVWTQK GDPTEPPVLV WIYGGGFTGG SVSLDVYDGR YLAAAEEAVV VSMNYRVGSL 

       190        200        210        220        230        240 
GFLALAGHRD APGNVGLWDQ RLALQWVRDN AEAFGGDPDL ITLFGESAGA ASVGFHLLSP 

       250        260        270        280        290        300 
HSKGLFRRAV LQSGSPNGPW ATIGAAEGRR RAAALGRAVG CPYGNETEFL GCLRGKEAAD 

       310        320        330        340        350        360 
VLEGEGVVMP PQSVFRFAFV PVVDGDFVVD SPDVALWGDY GVKGGEGGHG VEGGDGGYGV 

       370        380        390        400        410        420 
KGGDGVKGGY GGGYGARGVR EGDGDGGYGV KEGLREGYGV KEGYGVEGDG ANAYGARVPP 

       430        440        450        460        470        480 
RPHRDETPPD AYGAKGSADA YGAKAAPRPH RDETSPDAYG AKMPPRPHRD EASPDTYGAK 

       490        500        510        520        530        540 
MPPRPHRDET SPDAYGAKMP PRPHRAGGEV EVLLGAVRVE GSYFLVYGVP GFGKDNESLI 

       550        560        570        580        590        600 
SREEFLGGVR MGVPQATELA AEAVVLHYTD WLDADNPVKN REALDDIVGD HNVVCPLMAF 

       610        620        630        640        650        660 
AQRWAQRGGK VYAYLFDHRS STLLWPSWMG VPHGYEIEFV FGLPLEPRNN YTREEVELSR 

       670        680        690        700        710        720 
RIMRYWGNFA RTGDPNGGVG GPRWPPYTPS GQRYAHLNAR PLSVGHGLRT QICAFWTRFL 

       730        740        750        760 
PKLLNATGPP EDAEREWRLE FHRWSSYMGR WRTQFEHYSR QQPCATL 

« Hide

References

[1]"Cloning and analysis of chicken acetylcholinesterase transcripts from muscle and brain."
Randall W.R., Rimer M., Gough N.R.
Biochim. Biophys. Acta 1218:453-456(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03472 mRNA. Translation: AAA60456.1.
PIRS47639.
RefSeqNP_990749.1. NM_205418.1.
UniGeneGga.52373.
Gga.793.

3D structure databases

ProteinModelPortalP36196.
SMRP36196. Positions 32-333, 510-727, 731-761.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS09.979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396388.
KEGGgga:396388.

Organism-specific databases

CTD43.

Phylogenomic databases

HOVERGENHBG008839.
KOK01049.
PhylomeDBP36196.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 2 hits.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
ProDomPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF53474. SSF53474. 2 hits.
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816430.
PROP36196.

Entry information

Entry nameACES_CHICK
AccessionPrimary (citable) accession number: P36196
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 11, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families