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Protein

Acetylcholinesterase

Gene

ache

Organism
Electrophorus electricus (Electric eel) (Gymnotus electricus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.

Catalytic activityi

Acetylcholine + H2O = choline + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei225 – 2251Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei352 – 3521Charge relay systemBy similarity
Active sitei494 – 4941Charge relay systemBy similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. neurotransmitter catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

SABIO-RKO42275.

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
OrganismiElectrophorus electricus (Electric eel) (Gymnotus electricus)
Taxonomic identifieri8005 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiGymnotiformesGymnotoideiGymnotidaeElectrophorus

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB-SubCell
  4. synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 633610AcetylcholinesterasePRO_0000008594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 118By similarity
Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi279 ↔ 290By similarity
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi427 ↔ 579By similarity
Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi591 – 5911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi630 – 630InterchainBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Structurei

3D structure databases

ProteinModelPortaliO42275.
SMRiO42275. Positions 28-591, 594-627.
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.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 2 hits.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
ProDomiPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O42275-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKILDALLFP VIFIMFFIHL SIAQTDPELT IMTRLGQVQG TRLPVPDRSH
60 70 80 90 100
VIAFLGIPFA EPPLGKMRFK PPEPKKPWND VFDARDYPSA CYQYVDTSYP
110 120 130 140 150
GFSGTEMWNP NRMMSEDCLY LNVWVPATPR PHNLTVMVWI YGGGFYSGSS
160 170 180 190 200
SLDVYDGRYL AHSEKVVVVS MNYRVSAFGF LALNGSAEAP GNVGLLDQRL
210 220 230 240 250
ALQWVQDNIH FFGGNPKQVT IFGESAGAAS VGMHLLSPDS RPKFTRAILQ
260 270 280 290 300
SGVPNGPWRT VSFDEARRRA IKLGRLVGCP DGNDTDLIDC LRSKQPQDLI
310 320 330 340 350
DQEWLVLPFS GLFRFSFVPV IDGVVFPDTP EAMLNSGNFK DTQILLGVNQ
360 370 380 390 400
NEGSYFLIYG APGFSKDNES LITREDFLQG VKMSVPHANE IGLEAVILQY
410 420 430 440 450
TDWMDEDNPI KNREAMDDIV GDHNVVCPLQ HFAKMYAQYS ILQGQTGTAS
460 470 480 490 500
QGNLGWGNSG SASNSGNSQV SVYLYMFDHR ASNLVWPEWM GVIHGYEIEF
510 520 530 540 550
VFGLPLEKRL NYTLEEEKLS RRMMKYWANF ARTGNPNINV DGSIDSRRRW
560 570 580 590 600
PVFTSTEQKH VGLNTDSLKV HKGLKSQFCA LWNRFLPRLL NVTENIDDAE
610 620 630
RQWKAEFHRW SSYMMHWKNQ FDHYSKQERC TNL
Length:633
Mass (Da):71,815
Last modified:January 1, 1998 - v1
Checksum:iFC92FE7E4ADB84C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030422 Genomic DNA. Translation: AAB86606.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030422 Genomic DNA. Translation: AAB86606.1.

3D structure databases

ProteinModelPortaliO42275.
SMRiO42275. Positions 28-591, 594-627.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiO42275.
ChEMBLiCHEMBL4078.

Protein family/group databases

MEROPSiS09.980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008839.

Enzyme and pathway databases

SABIO-RKO42275.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 2 hits.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
ProDomiPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression of acetylcholinesterase from Electrophorus. Splicing pattern of the 3' exons in vivo and in transfected mammalian cells."
    Simon S., Massoulie J.
    J. Biol. Chem. 272:33045-33055(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiACES_ELEEL
AccessioniPrimary (citable) accession number: O42275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.