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Q9DDE3 (ACES_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. 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
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length634 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.

Subunit structure

Dimers and collagen-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform Ttetramers from dimers.

Subcellular location

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

Miscellaneous

No other isoforms exist. This protein corresponds to the T isoform inother species.

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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetylcholine catabolic process

Inferred from direct assay Ref.1. Source: ZFIN

cellular response to methanol

Inferred from direct assay PubMed 16806813. Source: ZFIN

choline metabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

myofibril assembly

Inferred from mutant phenotype PubMed 11753420. Source: ZFIN

neuromuscular junction development

Inferred from mutant phenotype PubMed 11753420. Source: ZFIN

neuron development

Inferred from mutant phenotype PubMed 11753420. Source: ZFIN

regulation of synapse structure and activity

Inferred from mutant phenotype PubMed 15136152. Source: ZFIN

response to amphetamine

Inferred from mutant phenotype PubMed 16470869. Source: ZFIN

response to ethanol

Inferred from direct assay PubMed 17888594. Source: ZFIN

synaptic transmission, cholinergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum lumen

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholinesterase activity

Inferred from direct assay Ref.1. Source: ZFIN

cholinesterase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 634611Acetylcholinesterase
PRO_0000008593

Sites

Active site2251Acyl-ester intermediate By similarity
Active site3521Charge relay system By similarity
Active site4951Charge relay system By similarity

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation5121N-linked (GlcNAc...) Potential
Glycosylation5921N-linked (GlcNAc...) Potential
Disulfide bond91 ↔ 118 By similarity
Disulfide bond279 ↔ 290 By similarity
Disulfide bond427 ↔ 580 By similarity
Disulfide bond631Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DDE3 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 47F348EA8A7C1E52

FASTA63471,998
        10         20         30         40         50         60 
MKTSDILLLP TVLLTFLFHN CFAQAEPDLV VATRLGRVQG TRLPVPDRSH VIAFLGIPYA 

        70         80         90        100        110        120 
EPPIGKRRFK RAEPKKPWNN VFEAKEFSNA CYQFVDTSYP GFPGIEMWNP NRVMSEDCLY 

       130        140        150        160        170        180 
LNVWVPPTPR PQNLTVMVWI YGGGFYSGSS SLDVYDGRYL AYTEKVVVVS MNYRVGAFGF 

       190        200        210        220        230        240 
LALNGSSDAP GNVGLYDQRL ALQWVQENIH FFGGNPKQVT IFGESAGAAS VGMHVLSPDS 

       250        260        270        280        290        300 
RPLFTRAILQ SGVPNTPWAT VTFDEARRRT TKLGKLVGCT WGNDTELIDC LRNKHPQELI 

       310        320        330        340        350        360 
DQEWQVLPWS SLFRFSFVPV VDGVFFPDTP DAMISSGNFK YTQILLGVNQ DEGSYFLLYG 

       370        380        390        400        410        420 
APGFSKDNES LISREDFLES VKMGVPHAND IGLEAVILQY TDWMDENNGQ KNRDAMDDIV 

       430        440        450        460        470        480 
GDQNVICPLQ HFAKSYAQYA ALHAQSSAAA PGTLGWGNSG PTGYNSGNSH GAVYLYLFDH 

       490        500        510        520        530        540 
RASNLAWPEW MGVIHGYEIE FVFGLPLEKR LNYTAEEEKL SRRIMRYWAN FARTGNPNVN 

       550        560        570        580        590        600 
TDGTMDSRRR WPQFSANEQK HVGLNTEPMK VHKGLRTQFC ALWNRFLPRL LNITDNIDDV 

       610        620        630 
ERQWKVEFHR WSSYMMHWKS QFDHYSKQER CTDL 

« Hide

References

[1]"Zebrafish acetylcholinesterase is encoded by a single gene localized on linkage group 7. gene structure and polymorphism; molecular forms and expression pattern during development."
Bertrand C., Chatonnet A., Takke C., Yan Y., Postlethwait J., Toutant J.-P., Cousin X.
J. Biol. Chem. 276:464-474(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ251640 Genomic DNA. Translation: CAC19790.1.
RefSeqNP_571921.1. NM_131846.1.
UniGeneDr.133438.

3D structure databases

ProteinModelPortalQ9DDE3.
SMRQ9DDE3. Positions 28-592, 595-628.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS09.979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000052989; ENSDARP00000052988; ENSDARG00000031796.
GeneID114549.
KEGGdre:114549.

Organism-specific databases

CTD43.
ZFINZDB-GENE-010906-1. ache.

Phylogenomic databases

eggNOGCOG2272.
GeneTreeENSGT00740000115241.
HOGENOMHOG000091866.
HOVERGENHBG008839.
InParanoidQ9DDE3.
KOK01049.
OMAWEAFADI.
OrthoDBEOG789C9R.
PhylomeDBQ9DDE3.
TreeFamTF315470.

Gene expression databases

BgeeQ9DDE3.

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...

Other

NextBio20796951.
PROQ9DDE3.

Entry information

Entry nameACES_DANRE
AccessionPrimary (citable) accession number: Q9DDE3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 92 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