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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 intermediatePROSITE-ProRule annotation
Active sitei351 – 3511Charge relay systemBy similarity
Active sitei464 – 4641Charge relay systemBy 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

MEROPSiS09.980.

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-KW
  4. synapse Source: UniProtKB-KW
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 PublicationAdd
BLAST
Chaini25 – 567543AcetylcholinesterasePRO_0000008597Add
BLAST
Propeptidei568 – 59023Removed in mature formPRO_0000008598Add
BLAST

Amino acid modifications

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

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

        10         20         30         40         50
MREMNLLVTS SLGVLLHLVV LCQADDDSEL LVNTKSGKVM RTRIPVLSSH
60 70 80 90 100
ISAFLGIPFA EPPVGNMRFR RPEPKKPWSG VWNASTYPNN CQQYVDEQFP
110 120 130 140 150
GFPGSEMWNP NREMSEDCLY LNIWVPSPRP KSATVMLWIY GGGFYSGSST
160 170 180 190 200
LDVYNGKYLA YTEEVVLVSL SYRVGAFGFL ALHGSQEAPG NMGLLDQRMA
210 220 230 240 250
LQWVHDNIQF FGGDPKTVTL FGESAGRASV GMHILSPGSR DLFRRAILQS
260 270 280 290 300
GSPNCPWASV SVAEGRRRAV ELRRNLNCNL NSDEDLIQCL REKKPQELID
310 320 330 340 350
VEWNVLPFDS IFRFSFVPVI DGEFFPTSLE SMLNAGNFKK TQILLGVNKD
360 370 380 390 400
EGSFFLLYGA PGFSKDSESK ISREDFMSGV KLSVPHANDL GLDAVTLQYT
410 420 430 440 450
DWMDDNNGIK NRDGLDDIVG DHNVICPLMH FVNKYTKFGN GTYLYFFNHR
460 470 480 490 500
ASNLVWPEWM GVIHGYEIEF VFGLPLVKEL NYTAEEEALS RRIMHYWATF
510 520 530 540 550
AKTGNPNEPH SQESKWPLFT TKEQKFIDLN TEPIKVHQRL RVQMCVFWNQ
560 570 580 590
FLPKLLNATA CDGELSSSGT SSSKGIIFYV LFSILYLIFY

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411R → G AA sequence (PubMed:3792544)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei560 – 59031ACDGE…YLIFY → GNVFAFHMQKVRTPAKTYHF GVIVAHLLLLSLPTASDVPR LASSKWWAHSDPLCSRRCWE SWGRIL in isoform 3. CuratedVSP_001462Add
BLAST
Alternative sequencei560 – 59031ACDGE…YLIFY → ETIDEAERQWKTEFHRWSSY MMHWKNQFDQYSRHENCAEL in isoform T. CuratedVSP_001461Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 S09.980.

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: October 29, 2014
This is version 108 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