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P07692 (ACES_TORMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 106. 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·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
OrganismTorpedo marmorata (Marbled electric ray)
Taxonomic identifier7788 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTorpedo

Protein attributes

Sequence length590 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 + H2O = choline + acetate.

Subunit structure

Isoform H form is a homodimer; the asymmetric form is a disulfide-bonded oligomer composed of a collagenic subunit (Q) and a variable number of T catalytic subunits. Ref.4 Ref.5

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 596 of the T isoform (Bysimilarity).

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processacetylcholine catabolic process in synaptic cleft

Inferred from electronic annotation. Source: InterPro

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholinesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform H (identifier: P07692-1)

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.
Note: GPI-anchored form.
Isoform T (identifier: P07692-2)

The sequence of this isoform differs from the canonical sequence as follows:
     560-590: ACDGELSSSGTSSSKGIIFYVLFSILYLIFY → ETIDEAERQWKTEFHRWSSYMMHWKNQFDQYSRHENCAEL
Isoform 3 (identifier: P07692-3)

The sequence of this isoform differs from the canonical sequence as follows:
     560-590: ACDGELSSSGTSSSKGIIFYVLFSILYLIFY → GNVFAFHMQK...RCWESWGRIL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.2
Chain25 – 567543Acetylcholinesterase
PRO_0000008597
Propeptide568 – 59023Removed in mature form
PRO_0000008598

Sites

Active site2241Acyl-ester intermediate By similarity
Active site3511Charge relay system By similarity
Active site4641Charge relay system By similarity

Amino acid modifications

Lipidation5671GPI-anchor amidated serine By similarity
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Glycosylation4811N-linked (GlcNAc...) Potential
Glycosylation5571N-linked (GlcNAc...) Potential
Disulfide bond91 ↔ 118 By similarity
Disulfide bond278 ↔ 289 By similarity
Disulfide bond426 ↔ 545 By similarity
Disulfide bond561Interchain

Natural variations

Alternative sequence560 – 59031ACDGE…YLIFY → GNVFAFHMQKVRTPAKTYHF GVIVAHLLLLSLPTASDVPR LASSKWWAHSDPLCSRRCWE SWGRIL in isoform 3.
VSP_001462
Alternative sequence560 – 59031ACDGE…YLIFY → ETIDEAERQWKTEFHRWSSY MMHWKNQFDQYSRHENCAEL in isoform T.
VSP_001461

Experimental info

Sequence conflict411R → G AA sequence Ref.2

Sequences

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

Last modified June 1, 1994. Version 2.
Checksum: 73FAC284C9784F25

FASTA59066,744
        10         20         30         40         50         60 
MREMNLLVTS SLGVLLHLVV LCQADDDSEL LVNTKSGKVM RTRIPVLSSH ISAFLGIPFA 

        70         80         90        100        110        120 
EPPVGNMRFR RPEPKKPWSG VWNASTYPNN CQQYVDEQFP GFPGSEMWNP NREMSEDCLY 

       130        140        150        160        170        180 
LNIWVPSPRP KSATVMLWIY GGGFYSGSST LDVYNGKYLA YTEEVVLVSL SYRVGAFGFL 

       190        200        210        220        230        240 
ALHGSQEAPG NMGLLDQRMA LQWVHDNIQF FGGDPKTVTL FGESAGRASV GMHILSPGSR 

       250        260        270        280        290        300 
DLFRRAILQS GSPNCPWASV SVAEGRRRAV ELRRNLNCNL NSDEDLIQCL REKKPQELID 

       310        320        330        340        350        360 
VEWNVLPFDS IFRFSFVPVI DGEFFPTSLE SMLNAGNFKK TQILLGVNKD EGSFFLLYGA 

       370        380        390        400        410        420 
PGFSKDSESK ISREDFMSGV KLSVPHANDL GLDAVTLQYT DWMDDNNGIK NRDGLDDIVG 

       430        440        450        460        470        480 
DHNVICPLMH FVNKYTKFGN GTYLYFFNHR ASNLVWPEWM GVIHGYEIEF VFGLPLVKEL 

       490        500        510        520        530        540 
NYTAEEEALS RRIMHYWATF AKTGNPNEPH SQESKWPLFT TKEQKFIDLN TEPIKVHQRL 

       550        560        570        580        590 
RVQMCVFWNQ FLPKLLNATA CDGELSSSGT SSSKGIIFYV LFSILYLIFY 

« Hide

Isoform T [UniParc].

Checksum: 20C387082E8FAF9B
Show »

FASTA59968,511
Isoform 3 [UniParc].

Checksum: 6A277207F667035E
Show »

FASTA62570,909

References

[1]"cDNA sequences of Torpedo marmorata acetylcholinesterase: primary structure of the precursor of a catalytic subunit; existence of multiple 5'-untranslated regions."
Sikorav J.-L., Krejci E., Massoulie J.
EMBO J. 6:1865-1873(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Electric organ.
[2]"Identical N-terminal peptide sequences of asymmetric forms and of low-salt-soluble and detergent-soluble amphiphilic dimers of Torpedo acetylcholinesterase. Comparison with bovine acetylcholinesterase."
Bon S., Chang J.Y., Strosberg A.D.
FEBS Lett. 209:206-212(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-47.
[3]"Complex alternative splicing of acetylcholinesterase transcripts in Torpedo electric organ; primary structure of the precursor of the glycolipid-anchored dimeric form."
Sikorav J.-L., Duval N., Anselmet A., Bon S., Krejci E., Legay C., Osterlund M., Reimund B., Massoulie J.
EMBO J. 7:2983-2993(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
Tissue: Electric organ.
[4]"Molecular architecture of acetylcholinesterase collagen-tailed forms; construction of a glycolipid-tailed tetramer."
Duval N., Krejci E., Grassi J., Coussen F., Massoulie J., Bon S.
EMBO J. 11:3255-3261(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNITS INTERACTION.
Tissue: Electric organ.
[5]"H and T subunits of acetylcholinesterase from Torpedo, expressed in COS cells, generate all types of globular forms."
Duval N., Massoulie J., Bon S.
J. Cell Biol. 118:641-653(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNITS INTERACTION, SEQUENCE REVISION TO 421.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05497 mRNA. Translation: CAA29047.1.
X13172 mRNA. Translation: CAA31570.1.
X13174 mRNA. Translation: CAA31572.1.
X13173 mRNA. Translation: CAA31571.1.
PIRA38868.
S01293.

3D structure databases

ProteinModelPortalP07692.
SMRP07692. Positions 28-560.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP07692.

Protein family/group databases

MEROPSS09.979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008839.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000908. Acylcholinesterase_fish/snake.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00879. ACHEFISH.
PR00878. CHOLNESTRASE.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACES_TORMA
AccessionPrimary (citable) accession number: P07692
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 1, 1994
Last modified: June 11, 2014
This is version 106 of the entry and version 2 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