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O42275

- ACES_ELEEL

UniProt

O42275 - ACES_ELEEL

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Protein

Acetylcholinesterase

Gene
ache
Organism
Electrophorus electricus (Electric eel) (Gymnotus electricus)
Status
Reviewed - 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 intermediate By similarity
Active sitei352 – 3521Charge relay system By similarity
Active sitei494 – 4941Charge relay system By 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

MEROPSiS09.979.

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 – 2323 Reviewed predictionAdd
BLAST
Chaini24 – 633610AcetylcholinesterasePRO_0000008594Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Structurei

3D structure databases

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

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

MKILDALLFP VIFIMFFIHL SIAQTDPELT IMTRLGQVQG TRLPVPDRSH    50
VIAFLGIPFA EPPLGKMRFK PPEPKKPWND VFDARDYPSA CYQYVDTSYP 100
GFSGTEMWNP NRMMSEDCLY LNVWVPATPR PHNLTVMVWI YGGGFYSGSS 150
SLDVYDGRYL AHSEKVVVVS MNYRVSAFGF LALNGSAEAP GNVGLLDQRL 200
ALQWVQDNIH FFGGNPKQVT IFGESAGAAS VGMHLLSPDS RPKFTRAILQ 250
SGVPNGPWRT VSFDEARRRA IKLGRLVGCP DGNDTDLIDC LRSKQPQDLI 300
DQEWLVLPFS GLFRFSFVPV IDGVVFPDTP EAMLNSGNFK DTQILLGVNQ 350
NEGSYFLIYG APGFSKDNES LITREDFLQG VKMSVPHANE IGLEAVILQY 400
TDWMDEDNPI KNREAMDDIV GDHNVVCPLQ HFAKMYAQYS ILQGQTGTAS 450
QGNLGWGNSG SASNSGNSQV SVYLYMFDHR ASNLVWPEWM GVIHGYEIEF 500
VFGLPLEKRL NYTLEEEKLS RRMMKYWANF ARTGNPNINV DGSIDSRRRW 550
PVFTSTEQKH VGLNTDSLKV HKGLKSQFCA LWNRFLPRLL NVTENIDDAE 600
RQWKAEFHRW SSYMMHWKNQ FDHYSKQERC TNL 633
Length:633
Mass (Da):71,815
Last modified:January 1, 1998 - v1
Checksum:iFC92FE7E4ADB84C3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF030422 Genomic DNA. Translation: AAB86606.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF030422 Genomic DNA. Translation: AAB86606.1 .

3D structure databases

ProteinModelPortali O42275.
SMRi O42275. Positions 28-591, 594-627.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi O42275.
ChEMBLi CHEMBL4078.

Protein family/group databases

MEROPSi S09.979.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG008839.

Enzyme and pathway databases

SABIO-RK O42275.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view ]
Pfami PF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 2 hits.
[Graphical view ]
PRINTSi PR00878. CHOLNESTRASE.
ProDomi PD415333. AChE_tetra. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF53474. SSF53474. 2 hits.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 72 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

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