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P21836 (ACES_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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

Isoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers By similarity. Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers. Ref.4

Subcellular location

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

Isoform H: Cell membrane; Lipid-anchorGPI-anchor; Extracellular side.

Tissue specificity

Predominates in most expressing tissues except erythrocytes where a glycophospholipid-attached form of ACHE predominates.

Miscellaneous

Synapses usually contain asymmetric molecules of cholinesterase, with a collagen-like part disulfide-bonded to the catalytic part. A different, globular type of cholinesterase occurs on the outer surfaces of cell membranes, including those of erythrocytes.

This is the catalytic subunit of an asymmetric or soluble form of ACHE.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
Synapse
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetylcholine catabolic process

Inferred from direct assay PubMed 16434405PubMed 7512968. Source: MGI

choline metabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

neurotransmitter receptor biosynthetic process

Inferred from mutant phenotype PubMed 14645660. Source: MGI

osteoblast development

Inferred from electronic annotation. Source: Ensembl

protein tetramerization

Inferred from direct assay PubMed 8626792. Source: MGI

receptor internalization

Inferred from mutant phenotype PubMed 14645660. Source: MGI

regulation of axonogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of dendrite morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of receptor recycling

Inferred from mutant phenotype PubMed 14645660. Source: MGI

retina development in camera-type eye

Inferred from mutant phenotype PubMed 15579149. Source: MGI

synapse assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

synaptic transmission, cholinergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

anchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

axon

Inferred from Biological aspect of Ancestor. Source: RefGenome

basal lamina

Inferred from direct assay PubMed 7885444. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 16434405. Source: MGI

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

endoplasmic reticulum lumen

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular space

Inferred from direct assay PubMed 16434405PubMed 8626792. Source: MGI

neuromuscular junction

Inferred from direct assay PubMed 7885444. Source: MGI

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 8626792. Source: MGI

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

presynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse

Inferred from direct assay PubMed 10995443PubMed 12533614. Source: MGI

   Molecular_functionacetylcholinesterase activity

Inferred from direct assay PubMed 16434405PubMed 7512968. Source: MGI

carboxylic ester hydrolase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

cholinesterase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

laminin binding

Inferred from physical interaction PubMed 15474030. Source: MGI

protein self-association

Inferred from physical interaction PubMed 8626792. Source: MGI

serine hydrolase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]
Isoform T (identifier: P21836-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform H (identifier: P21836-2)

The sequence of this isoform is not available.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 614583Acetylcholinesterase
PRO_0000008588

Sites

Active site2341Acyl-ester intermediate
Active site3651Charge relay system
Active site4781Charge relay system

Amino acid modifications

Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...)
Glycosylation4951N-linked (GlcNAc...)
Disulfide bond100 ↔ 127
Disulfide bond288 ↔ 303
Disulfide bond440 ↔ 560
Disulfide bond611Interchain By similarity

Secondary structure

........................................................................................................... 614
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform T [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 66E2512463C21172

FASTA61468,169
        10         20         30         40         50         60 
MRPPWYPLHT PSLAFPLLFL LLSLLGGGAR AEGREDPQLL VRVRGGQLRG IRLKAPGGPV 

        70         80         90        100        110        120 
SAFLGIPFAE PPVGSRRFMP PEPKRPWSGV LDATTFQNVC YQYVDTLYPG FEGTEMWNPN 

       130        140        150        160        170        180 
RELSEDCLYL NVWTPYPRPA SPTPVLIWIY GGGFYSGAAS LDVYDGRFLA QVEGAVLVSM 

       190        200        210        220        230        240 
NYRVGTFGFL ALPGSREAPG NVGLLDQRLA LQWVQENIAA FGGDPMSVTL FGESAGAASV 

       250        260        270        280        290        300 
GMHILSLPSR SLFHRAVLQS GTPNGPWATV SAGEARRRAT LLARLVGCPP GGAGGNDTEL 

       310        320        330        340        350        360 
IACLRTRPAQ DLVDHEWHVL PQESIFRFSF VPVVDGDFLS DTPEALINTG DFQDLQVLVG 

       370        380        390        400        410        420 
VVKDEGSYFL VYGVPGFSKD NESLISRAQF LAGVRIGVPQ ASDLAAEAVV LHYTDWLHPE 

       430        440        450        460        470        480 
DPTHLRDAMS AVVGDHNVVC PVAQLAGRLA AQGARVYAYI FEHRASTLTW PLWMGVPHGY 

       490        500        510        520        530        540 
EIEFIFGLPL DPSLNYTTEE RIFAQRLMKY WTNFARTGDP NDPRDSKSPQ WPPYTTAAQQ 

       550        560        570        580        590        600 
YVSLNLKPLE VRRGLRAQTC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN 

       610 
QFDHYSKQER CSDL 

« Hide

Isoform H (Sequence not available).

References

« Hide 'large scale' references
[1]"Molecular cloning of mouse acetylcholinesterase: tissue distribution of alternatively spliced mRNA species."
Rachinsky T.L., Camp S., Li Y., Ekstroem T.J., Newton M., Taylor P.
Neuron 5:317-327(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5."
Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F.
Nucleic Acids Res. 29:1352-1365(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Retina.
[4]"PRiMA: the membrane anchor of acetylcholinesterase in the brain."
Perrier A.L., Massoulie J., Krejci E.
Neuron 33:275-285(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRIMA1.
[5]"Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex."
Bourne Y., Taylor P., Marchot P.
Cell 83:503-512(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH FASCICULIN.
[6]"Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly."
Bourne Y., Taylor P., Bougis P.E., Marchot P.
J. Biol. Chem. 274:2963-2970(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[7]"Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site."
Bourne Y., Taylor P., Radic Z., Marchot P.
EMBO J. 22:1-12(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 34-573 IN COMPLEX WITH INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56518 mRNA. Translation: CAA39867.1.
AF312033 Genomic DNA. Translation: AAK28816.1.
BC046327 mRNA. Translation: AAH46327.1.
PIRJH0314.
RefSeqNP_033729.1. NM_009599.4.
UniGeneMm.255464.
Mm.489229.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C2BX-ray4.50A35-574[»]
1C2OX-ray4.20A/B/C/D36-574[»]
1J06X-ray2.35A/B32-574[»]
1J07X-ray2.35A/B32-574[»]
1KU6X-ray2.50A32-580[»]
1MAAX-ray2.90A/B/C/D32-578[»]
1MAHX-ray3.20A32-574[»]
1N5MX-ray2.20A/B32-572[»]
1N5RX-ray2.25A/B32-574[»]
1Q83X-ray2.65A/B1-580[»]
1Q84X-ray2.45A/B1-580[»]
2C0PX-ray2.50A/B32-574[»]
2C0QX-ray2.50A/B32-574[»]
2GYUX-ray2.20A/B32-574[»]
2GYVX-ray2.50A/B32-574[»]
2GYWX-ray2.40A/B32-574[»]
2H9YX-ray2.40A/B32-574[»]
2HA0X-ray2.20A/B32-574[»]
2HA2X-ray2.05A/B32-574[»]
2HA3X-ray2.25A/B32-574[»]
2HA4X-ray2.56A/B32-574[»]
2HA5X-ray2.15A/B32-574[»]
2HA6X-ray2.25A/B32-574[»]
2HA7X-ray2.66A/B32-574[»]
2JEYX-ray2.70A/B32-574[»]
2JEZX-ray2.60A/B32-574[»]
2JF0X-ray2.50A/B32-574[»]
2JGEX-ray2.60A/B32-574[»]
2JGFX-ray2.50A/B32-574[»]
2JGIX-ray2.90A/B32-574[»]
2JGJX-ray2.50A/B32-574[»]
2JGKX-ray2.90A/B32-574[»]
2JGLX-ray2.60A/B32-574[»]
2JGMX-ray2.90A/B32-574[»]
2WHPX-ray2.20A/B32-573[»]
2WHQX-ray2.15A/B32-574[»]
2WHRX-ray2.54A/B32-574[»]
2WLSX-ray2.60A/B32-574[»]
2WU3X-ray2.70A/B32-574[»]
2WU4X-ray2.40A/B32-574[»]
2XUDX-ray2.65A/B32-574[»]
2XUFX-ray2.55A/B32-574[»]
2XUGX-ray2.60A/B32-574[»]
2XUHX-ray2.65A/B32-574[»]
2XUIX-ray2.60A/B32-574[»]
2XUJX-ray2.65A/B32-574[»]
2XUKX-ray2.75A/B32-574[»]
2XUOX-ray2.80A/B32-574[»]
2XUPX-ray2.70A/B32-574[»]
2XUQX-ray2.70A/B32-574[»]
2Y2UX-ray2.60A/B32-574[»]
2Y2VX-ray2.45A/B32-574[»]
3DL4X-ray2.50A/B32-574[»]
3DL7X-ray2.50A/B32-574[»]
3ZLTX-ray2.60A/B32-574[»]
3ZLUX-ray2.60A/B32-574[»]
3ZLVX-ray2.50A/B32-574[»]
4A16X-ray2.65A/B/C/D35-574[»]
4A23X-ray2.40A/B32-574[»]
4ARAX-ray2.50A/B32-574[»]
4ARBX-ray2.25A/B32-574[»]
4B7ZX-ray2.30A/B32-576[»]
4B80X-ray2.50A/B32-576[»]
4B81X-ray2.80A/B32-574[»]
4B82X-ray2.10A/B32-574[»]
4B83X-ray2.40A/B32-574[»]
4B84X-ray2.60A/B32-574[»]
4B85X-ray2.10A/B32-574[»]
4BC0X-ray3.35A/B/C/D32-574[»]
4BC1X-ray2.95A/B/C/D32-574[»]
4BTLX-ray2.50A/B32-574[»]
ProteinModelPortalP21836.
SMRP21836. Positions 35-608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197921. 1 interaction.
IntActP21836. 2 interactions.
MINTMINT-1206315.

Chemistry

BindingDBP21836.
ChEMBLCHEMBL3198.

Protein family/group databases

MEROPSS09.979.

PTM databases

PhosphoSiteP21836.

Proteomic databases

PaxDbP21836.
PRIDEP21836.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024099; ENSMUSP00000024099; ENSMUSG00000023328. [P21836-1]
ENSMUST00000085934; ENSMUSP00000083097; ENSMUSG00000023328. [P21836-1]
GeneID11423.
KEGGmmu:11423.
UCSCuc009abt.1. mouse. [P21836-1]

Organism-specific databases

CTD43.
MGIMGI:87876. Ache.

Phylogenomic databases

eggNOGCOG2272.
HOGENOMHOG000091866.
HOVERGENHBG008839.
InParanoidP21836.
KOK01049.
OMARPPWCPL.
OrthoDBEOG789C9R.
PhylomeDBP21836.
TreeFamTF315470.

Enzyme and pathway databases

SABIO-RKP21836.

Gene expression databases

ArrayExpressP21836.
BgeeP21836.
CleanExMM_ACHE.
GenevestigatorP21836.

Family and domain databases

InterProIPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
ProDomPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21836.
NextBio278674.
PROP21836.
SOURCESearch...

Entry information

Entry nameACES_MOUSE
AccessionPrimary (citable) accession number: P21836
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 133 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot