Acetylcholinesterase precursor - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot P21836 (ACES_MOUSE)

Last modified November 25, 2008. Version 82. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
    Acetylcholinesterase
      Short name=AChE
    EC=3.1.1.7

Gene names

Name:

Ache

Organism

Mus musculus (Mouse)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	614 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 + H(2)O = 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.
Subcellular location	Cell junction › synapse. Secreted. Cell membrane; Peripheral membrane proteinBy similarity. Isoform H: Cell membrane; Lipid-anchor › GPI-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 process	Neurotransmitter degradation
Cellular component	Cell junction Cell membrane Membrane Secreted Synapse
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	acetylcholine catabolic process Inferred from direct assay. Source: MGI neurotransmitter receptor biosynthetic process Inferred from mutant phenotype. Source: MGI protein tetramerization Inferred from direct assay. Source: MGI receptor internalization Inferred from mutant phenotype. Source: MGI regulation of receptor recycling Inferred from mutant phenotype. Source: MGI retina development in camera-type eye Inferred from mutant phenotype. Source: MGI
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from direct assay. Source: MGI extracellular space Inferred from direct assay. Source: MGI synapse Inferred from direct assay. Source: MGI
Molecular function	acetylcholinesterase activity Inferred from direct assay. Source: MGI cholinesterase activity Inferred from electronic annotation. Source: InterPro laminin binding Inferred from physical interaction. Source: MGI protein self-association Inferred from physical interaction. Source: MGI
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.
Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

31

Chain

583

Acetylcholinesterase

PRO_0000008588

Sites

Active site

1

Acyl-ester intermediate

Active site

1

Charge relay system

Active site

1

Charge relay system

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...)

Glycosylation

1

N-linked (GlcNAc...)

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Interchain By similarity

Secondary structure

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614

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform T [UniParc].

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

614

68,169

        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

Isoform H (Sequence not available).

–

–

References

	« Hide 'large scale' referencesShow '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: 2400605] [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: 11239002] [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: 15489334] [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: 11804574] [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: 8521480] [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: 9915834] [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: 12505979] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 34-573 IN COMPLEX WITH INHIBITOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

X56518 mRNA. Translation: CAA39867.1.
AF312033 Genomic DNA. Translation: AAK28816.1.
BC046327 mRNA. Translation: AAH46327.1.

PIR

RefSeq

UniGene

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C2B	X-ray	4.50	A