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UniProtKB/Swiss-Prot entry P07692


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACES_TORMA
Primary accession number P07692
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on June 1, 1994 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 80)
Name and origin of the protein
Protein name Acetylcholinesterase [Precursor]
Synonyms AChE
EC 3.1.1.7
Gene name
Name: ache
From
Torpedo marmorata (Marbled electric ray) [TaxID: 7788] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; Elasmobranchii; Squalea; Hypnosqualea; Pristiorajea; Batoidea; Torpediniformes; Torpedinoidei; Torpedinidae; Torpedo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Electric organ;
PubMed=2820709 [NCBI, ExPASy, EBI, Israel, Japan]
Sikorav J.-L., Krejci E., Massoulie J.;
"cDNA sequences of Torpedo marmorata acetylcholinesterase: primary structure of the precursor of a catalytic subunit; existence of multiple 5'-untranslated regions.";
EMBO J. 6:1865-1873(1987).
[2]
PROTEIN SEQUENCE OF 25-47.
DOI=10.1016/0014-5793(86)81112-7; PubMed=3792544 [NCBI, ExPASy, EBI, Israel, Japan]
Bon S., Chang J.Y., Strosberg A.D.;
"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.";
FEBS Lett. 209:206-212(1986).
[3]
ALTERNATIVE SPLICING.
TISSUE=Electric organ;
PubMed=3181125 [NCBI, ExPASy, EBI, Israel, Japan]
Sikorav J.-L., Duval N., Anselmet A., Bon S., Krejci E., Legay C., Osterlund M., Reimund B., Massoulie J.;
"Complex alternative splicing of acetylcholinesterase transcripts in Torpedo electric organ; primary structure of the precursor of the glycolipid-anchored dimeric form.";
EMBO J. 7:2983-2993(1988).
[4]
SUBUNITS INTERACTION.
TISSUE=Electric organ;
PubMed=1380451 [NCBI, ExPASy, EBI, Israel, Japan]
Duval N., Krejci E., Grassi J., Coussen F., Massoulie J., Bon S.;
"Molecular architecture of acetylcholinesterase collagen-tailed forms; construction of a glycolipid-tailed tetramer.";
EMBO J. 11:3255-3261(1992).
[5]
SUBUNITS INTERACTION, AND SEQUENCE REVISION TO 421.
DOI=10.1083/jcb.118.3.641; PubMed=1639848 [NCBI, ExPASy, EBI, Israel, Japan]
Duval N., Massoulie J., Bon S.;
"H and T subunits of acetylcholinesterase from Torpedo, expressed in COS cells, generate all types of globular forms.";
J. Cell Biol. 118:641-653(1992).
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: 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-anchor, GPI-anchor. Cell junction, synapse.
  • SUBCELLULAR LOCATION: Isoform T: Cell membrane; Peripheral membrane protein. Cell junction, synapse. Note=Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.
    NameH
    SynonymsGlobular
    Isoform IDP07692-1
    Note: GPI-anchored form.
    This is the isoform sequence displayed in this entry.
    NameT
    Isoform IDP07692-2
    Features which should be applied to build the isoform sequence: VSP_001461.
    Name3
    Isoform IDP07692-3
    Features which should be applied to build the isoform sequence: VSP_001462.
  • TISSUE SPECIFICITY: Found in the synapses and to a lower extent in extrajunctional areas of muscle and nerve, and on erythrocyte membranes.
  • PTM: An interchain disulfide bond is present in what becomes position 596 of the T isoform (By similarity).
  • SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X05497; CAA29047.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13172; CAA31570.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13174; CAA31572.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13173; CAA31571.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38868; A38868.
S01293; S01293.
3D structure databases
HSSP P04058; 1EA5. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
SMR P07692; 28-559.
ModBase P07692.
Protein family/group databases
MEROPS S09.979; -.
Ontologies
GO
GO:0031225; Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0030054; Cellular component: cell junction (inferred from electronic annotation from UniProtKB-KW).
GO:0045202; Cellular component: synapse (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000908; Acylcholinesterase_fish/snake.
IPR002018; CarbesteraseB.
IPR000997; Cholinesterase.
Graphical view of domain structure.
PANTHER PTHR11559; CarbesteraseB; 1.
Pfam PF00135; COesterase; 1.
Pfam graphical view of domain structure.
PRINTS PR00879; ACHEFISH.
PR00878; CHOLNESTRASE.
PROSITE PS00122; CARBOXYLESTERASE_B_1; 1.
PS00941; CARBOXYLESTERASE_B_2; 1.
BLOCKS P07692.
ProtoNet P07692.
Phylogenomic databases
HOVERGEN P07692; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cell junction; Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation; Serine esterase; Signal; Synapse.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    24  24      
CHAIN   25   567  543     Acetylcholinesterase. PRO_0000008597
PROPEP   568   590  23     Removed in mature form. PRO_0000008598
ACT_SITE   224   224        Acyl-ester intermediate (By similarity). 
ACT_SITE   351   351        Charge relay system (By similarity). 
ACT_SITE   464   464        Charge relay system (By similarity). 
LIPID   567   567        GPI-anchor amidated serine. 
CARBOHYD   83    83        N-linked (GlcNAc...) (Potential). 
CARBOHYD   440   440        N-linked (GlcNAc...) (Potential). 
CARBOHYD   481   481        N-linked (GlcNAc...) (Potential). 
CARBOHYD   557   557        N-linked (GlcNAc...) (Potential). 
DISULFID   91   118        By similarity. 
DISULFID   278   289        By similarity. 
DISULFID   426   545        By similarity. 
DISULFID   561   561        Interchain. 
VAR_SEQ   560   590        ACDGELSSSGTSSSKGIIFYVLFSILYLIFY -> GNVFAFHMQKVRTPAKTYHFGVIVAHLLLLSLPTASDVPR LASSKWWAHSDPLCSRRCWESWGRIL (in isoform 3). VSP_001462
VAR_SEQ   560   590        ACDGELSSSGTSSSKGIIFYVLFSILYLIFY -> ETIDEAERQWKTEFHRWSSYMMHWKNQFDQYSRHENCAEL (in isoform T). VSP_001461
CONFLICT   41    41        R -> G (in Ref. 2; AA sequence). 
Sequence information
Length: 590 AA [This is the length of the unprocessed precursor] Molecular weight: 66744 Da [This is the MW of the unprocessed precursor] CRC64: 73FAC284C9784F25 [This is a checksum on the sequence]
        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 

P07692 in FASTA format

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View entry in raw text format (no links)
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