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Reviewed, UniProtKB/Swiss-Prot P04058 (ACES_TORCA)

Last modified November 25, 2008. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
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 namesRecommended name:
    Acetylcholinesterase
      Short name=AChE
    EC=3.1.1.7
Gene names
Name: ache
OrganismTorpedo californica (Pacific electric ray)
Taxonomic identifier7787 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiSqualeaHypnosqualeaPristiorajeaBatoideaTorpediniformesTorpedinoideiTorpedinidaeTorpedo

Protein attributes

Sequence length586 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. May be involved in cell-cell interactions.

Catalytic activity

Acetylcholine + H(2)O = choline + acetate.

Enzyme regulation

Inhibited by substrate concentrations above 0.5 mM.

Subunit structure

Isoform H form is an homodimer; the asymmetric form is a disulfide-bonded oligomer composed of a collagenic subunit (Q) and a variable number of T catalytic subunits.

Subcellular location

Isoform H: Cell membrane; Lipid-anchorGPI-anchor. Cell junctionsynapse.

Isoform T: Cell membrane; Peripheral membrane protein. Cell junctionsynapse. Note= Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.

Tissue specificity

Found in the synapses and to a lower extent in extrajunctional areas of muscle and nerve, and on erythrocyte membranes.

Post-translational modification

An interchain disulfide bond is present in what becomes position 593 of the T isoform.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Notes: Additional isoforms seem to exist.
Isoform H (identifier: P04058-1)

Also known as: Globular;

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.
Notes: GPI-anchored form.
Isoform T (identifier: P04058-2)

The sequence of this isoform differs from the canonical sequence as follows:
     557-586: ACDGELSSSGTSSSKGIIFYVLFSILYLIF → ETIDEAERQWKTEFHRWSSYMMHWKNQFDHYSRHESCAEL
Notes: Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 564543Acetylcholinesterase
PRO_0000008595
Propeptide565 – 58622Removed in mature form
PRO_0000008596

Sites

Active site2211Acyl-ester intermediate
Active site3481Charge relay system
Active site4611Charge relay system

Amino acid modifications

Lipidation5641GPI-anchor amidated serine
Glycosylation801N-linked (GlcNAc...)
Glycosylation4371N-linked (GlcNAc...)
Glycosylation4781N-linked (GlcNAc...)
Glycosylation5541N-linked (GlcNAc...)
Disulfide bond88 ↔ 115
Disulfide bond275 ↔ 286
Disulfide bond423 ↔ 542
Disulfide bond558Interchain

Natural variations

Alternative sequence557 – 58630ACDGE…LYLIF → ETIDEAERQWKTEFHRWSSY MMHWKNQFDHYSRHESCAEL in isoform T.
VSP_001460

Experimental info

Mutagenesis2201E → H: Loss of activity
Mutagenesis2201E → Q or D: Decrease in activity
Mutagenesis2211S → C: Loss of activity
Mutagenesis2211S → V: Loss of activity
Mutagenesis4461H → Q: Almost no loss of activity
Mutagenesis4611H → Q: Loss of activity

Secondary structure

........................................................................................... 586
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform H (Globular) [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 731D5F0F3ABA62A8

FASTA58665,906
        10         20         30         40         50         60 
MNLLVTSSLG VLLHLVVLCQ ADDHSELLVN TKSGKVMGTR VPVLSSHISA FLGIPFAEPP 

        70         80         90        100        110        120 
VGNMRFRRPE PKKPWSGVWN ASTYPNNCQQ YVDEQFPGFS GSEMWNPNRE MSEDCLYLNI 

       130        140        150        160        170        180 
WVPSPRPKST TVMVWIYGGG FYSGSSTLDV YNGKYLAYTE EVVLVSLSYR VGAFGFLALH 

       190        200        210        220        230        240 
GSQEAPGNVG LLDQRMALQW VHDNIQFFGG DPKTVTIFGE SAGGASVGMH ILSPGSRDLF 

       250        260        270        280        290        300 
RRAILQSGSP NCPWASVSVA EGRRRAVELG RNLNCNLNSD EELIHCLREK KPQELIDVEW 

       310        320        330        340        350        360 
NVLPFDSIFR FSFVPVIDGE FFPTSLESML NSGNFKKTQI LLGVNKDEGS FFLLYGAPGF 

       370        380        390        400        410        420 
SKDSESKISR EDFMSGVKLS VPHANDLGLD AVTLQYTDWM DDNNGIKNRD GLDDIVGDHN 

       430        440        450        460        470        480 
VICPLMHFVN KYTKFGNGTY LYFFNHRASN LVWPEWMGVI HGYEIEFVFG LPLVKELNYT 

       490        500        510        520        530        540 
AEEEALSRRI MHYWATFAKT GNPNEPHSQE SKWPLFTTKE QKFIDLNTEP MKVHQRLRVQ 

       550        560        570        580 
MCVFWNQFLP KLLNATACDG ELSSSGTSSS KGIIFYVLFS ILYLIF 

« Hide

Isoform T [UniParc].

Checksum: 36D5E9A30F9E6065
Show »

59667,818

References

[1]"Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence."
Schumacher M., Camp S., Maulet Y., Newton M., McPhee-Quigley K., Taylor S.S., Friedmann T., Taylor P.
Nature 319:407-409(1986) [PubMed: 3753747] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-586.
[2]"Multiple messenger RNA species give rise to the structural diversity in acetylcholinesterase."
Schumacher M.
J. Biol. Chem. 263:18979-18987(1988) [PubMed: 3198606] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
[3]"Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences."
MacPhee-Quigley K., Taylor P., Taylor S.
J. Biol. Chem. 260:12185-12189(1985) [PubMed: 3900071] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-45 AND 214-237.
[4]"Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom."
Kreienkamp H.J., Weise C., Raba R., Aaviksaar A., Hucho F.
Proc. Natl. Acad. Sci. U.S.A. 88:6117-6121(1991) [PubMed: 2068091] [Abstract]
Cited for: PROTEIN SEQUENCE OF 100-108.
[5]"Divergence in primary structure between the molecular forms of acetylcholinesterase."
Gibney G., Macphee-Quigley K., Thompson B., Vedvick T., Low M.G., Taylor S.S., Taylor P.
J. Biol. Chem. 263:1140-1145(1988) [PubMed: 3335534] [Abstract]
Cited for: PROTEIN SEQUENCE OF 552-558.
[6]"Single gene encodes glycophospholipid-anchored and asymmetric acetylcholinesterase forms: alternative coding exons contain inverted repeat sequences."
Maulet Y., Camp S., Gibney G., Rachinsky T.L., Ekstroem T.J., Taylor P.
Neuron 4:289-301(1990) [PubMed: 2306366] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[7]"Profile of the disulfide bon