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O42275 (ACES_ELEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylcholinesterase

Short name=AChE
EC=3.1.1.7
Gene names
Name:ache
OrganismElectrophorus electricus (Electric eel) (Gymnotus electricus)
Taxonomic identifier8005 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiGymnotiformesGymnotoideiGymnotidaeElectrophorus

Protein attributes

Sequence length633 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

Acetylcholine + H2O = choline + acetate.

Subcellular location

Cell junctionsynapse. Secreted. Cell membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
Synapse
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological_processneurotransmitter catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholinesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 633610Acetylcholinesterase
PRO_0000008594

Sites

Active site2251Acyl-ester intermediate By similarity
Active site3521Charge relay system By similarity
Active site4941Charge relay system By similarity

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation5111N-linked (GlcNAc...) Potential
Glycosylation5911N-linked (GlcNAc...) Potential
Disulfide bond91 ↔ 118 By similarity
Disulfide bond279 ↔ 290 By similarity
Disulfide bond427 ↔ 579 By similarity
Disulfide bond630Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
O42275 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: FC92FE7E4ADB84C3

FASTA63371,815
        10         20         30         40         50         60 
MKILDALLFP VIFIMFFIHL SIAQTDPELT IMTRLGQVQG TRLPVPDRSH VIAFLGIPFA 

        70         80         90        100        110        120 
EPPLGKMRFK PPEPKKPWND VFDARDYPSA CYQYVDTSYP GFSGTEMWNP NRMMSEDCLY 

       130        140        150        160        170        180 
LNVWVPATPR PHNLTVMVWI YGGGFYSGSS SLDVYDGRYL AHSEKVVVVS MNYRVSAFGF 

       190        200        210        220        230        240 
LALNGSAEAP GNVGLLDQRL ALQWVQDNIH FFGGNPKQVT IFGESAGAAS VGMHLLSPDS 

       250        260        270        280        290        300 
RPKFTRAILQ SGVPNGPWRT VSFDEARRRA IKLGRLVGCP DGNDTDLIDC LRSKQPQDLI 

       310        320        330        340        350        360 
DQEWLVLPFS GLFRFSFVPV IDGVVFPDTP EAMLNSGNFK DTQILLGVNQ NEGSYFLIYG 

       370        380        390        400        410        420 
APGFSKDNES LITREDFLQG VKMSVPHANE IGLEAVILQY TDWMDEDNPI KNREAMDDIV 

       430        440        450        460        470        480 
GDHNVVCPLQ HFAKMYAQYS ILQGQTGTAS QGNLGWGNSG SASNSGNSQV SVYLYMFDHR 

       490        500        510        520        530        540 
ASNLVWPEWM GVIHGYEIEF VFGLPLEKRL NYTLEEEKLS RRMMKYWANF ARTGNPNINV 

       550        560        570        580        590        600 
DGSIDSRRRW PVFTSTEQKH VGLNTDSLKV HKGLKSQFCA LWNRFLPRLL NVTENIDDAE 

       610        620        630 
RQWKAEFHRW SSYMMHWKNQ FDHYSKQERC TNL 

« Hide

References

[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF030422 Genomic DNA. Translation: AAB86606.1.

3D structure databases

ProteinModelPortalO42275.
SMRO42275. Positions 28-591, 594-627.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBO42275.
ChEMBLCHEMBL4078.

Protein family/group databases

MEROPSS09.979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008839.

Enzyme and pathway databases

SABIO-RKO42275.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 2 hits.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
ProDomPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF53474. SSF53474. 2 hits.
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACES_ELEEL
AccessionPrimary (citable) accession number: O42275
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families