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P07692

- ACES_TORMA

UniProt

P07692 - ACES_TORMA

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Protein
Acetylcholinesterase
Gene
ache
Organism
Torpedo marmorata (Marbled electric ray)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Acetylcholine + H2O = choline + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei224 – 2241Acyl-ester intermediate By similarity
Active sitei351 – 3511Charge relay system By similarity
Active sitei464 – 4641Charge relay system By similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. acetylcholine catabolic process in synaptic cleft Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Protein family/group databases

MEROPSiS09.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
Gene namesi
Name:ache
OrganismiTorpedo marmorata (Marbled electric ray)
Taxonomic identifieri7788 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTorpedo

Subcellular locationi

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.

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell junction Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-SubCell
  4. synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 Publication
Add
BLAST
Chaini25 – 567543Acetylcholinesterase
PRO_0000008597Add
BLAST
Propeptidei568 – 59023Removed in mature form
PRO_0000008598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi83 – 831N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi91 ↔ 118 By similarity
Disulfide bondi278 ↔ 289 By similarity
Disulfide bondi426 ↔ 545 By similarity
Glycosylationi440 – 4401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi481 – 4811N-linked (GlcNAc...) Reviewed prediction
Glycosylationi557 – 5571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi561 – 561Interchain
Lipidationi567 – 5671GPI-anchor amidated serine By similarity

Post-translational modificationi

An interchain disulfide bond is present in what becomes position 596 of the T isoform (By similarity).

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

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.2 Publications

Structurei

3D structure databases

ProteinModelPortaliP07692.
SMRiP07692. Positions 28-560.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG008839.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000908. Acylcholinesterase_fish/snake.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00879. ACHEFISH.
PR00878. CHOLNESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform H (identifier: P07692-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MREMNLLVTS SLGVLLHLVV LCQADDDSEL LVNTKSGKVM RTRIPVLSSH    50
ISAFLGIPFA EPPVGNMRFR RPEPKKPWSG VWNASTYPNN CQQYVDEQFP 100
GFPGSEMWNP NREMSEDCLY LNIWVPSPRP KSATVMLWIY GGGFYSGSST 150
LDVYNGKYLA YTEEVVLVSL SYRVGAFGFL ALHGSQEAPG NMGLLDQRMA 200
LQWVHDNIQF FGGDPKTVTL FGESAGRASV GMHILSPGSR DLFRRAILQS 250
GSPNCPWASV SVAEGRRRAV ELRRNLNCNL NSDEDLIQCL REKKPQELID 300
VEWNVLPFDS IFRFSFVPVI DGEFFPTSLE SMLNAGNFKK TQILLGVNKD 350
EGSFFLLYGA PGFSKDSESK ISREDFMSGV KLSVPHANDL GLDAVTLQYT 400
DWMDDNNGIK NRDGLDDIVG DHNVICPLMH FVNKYTKFGN GTYLYFFNHR 450
ASNLVWPEWM GVIHGYEIEF VFGLPLVKEL NYTAEEEALS RRIMHYWATF 500
AKTGNPNEPH SQESKWPLFT TKEQKFIDLN TEPIKVHQRL RVQMCVFWNQ 550
FLPKLLNATA CDGELSSSGT SSSKGIIFYV LFSILYLIFY 590

Note: GPI-anchored form.

Length:590
Mass (Da):66,744
Last modified:June 1, 1994 - v2
Checksum:i73FAC284C9784F25
GO
Isoform T (identifier: P07692-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:599
Mass (Da):68,511
Checksum:i20C387082E8FAF9B
GO
Isoform 3 (identifier: P07692-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:625
Mass (Da):70,909
Checksum:i6A277207F667035E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei560 – 59031ACDGE…YLIFY → GNVFAFHMQKVRTPAKTYHF GVIVAHLLLLSLPTASDVPR LASSKWWAHSDPLCSRRCWE SWGRIL in isoform 3.
VSP_001462Add
BLAST
Alternative sequencei560 – 59031ACDGE…YLIFY → ETIDEAERQWKTEFHRWSSY MMHWKNQFDQYSRHENCAEL in isoform T.
VSP_001461Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411R → G AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05497 mRNA. Translation: CAA29047.1.
X13172 mRNA. Translation: CAA31570.1.
X13174 mRNA. Translation: CAA31572.1.
X13173 mRNA. Translation: CAA31571.1.
PIRiA38868.
S01293.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05497 mRNA. Translation: CAA29047.1 .
X13172 mRNA. Translation: CAA31570.1 .
X13174 mRNA. Translation: CAA31572.1 .
X13173 mRNA. Translation: CAA31571.1 .
PIRi A38868.
S01293.

3D structure databases

ProteinModelPortali P07692.
SMRi P07692. Positions 28-560.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P07692.

Protein family/group databases

MEROPSi S09.979.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG008839.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000908. Acylcholinesterase_fish/snake.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
[Graphical view ]
PRINTSi PR00879. ACHEFISH.
PR00878. CHOLNESTRASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiACES_TORMA
AccessioniPrimary (citable) accession number: P07692
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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