Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9DDE3 (ACES_DANRE)

Last modified November 3, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Acetylcholinesterase
      Short name=AChE
    EC=3.1.1.7
Gene names
Name: ache
OrganismDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Hide | Top

Protein attributes

Sequence length634 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

Hide | Top

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 T tetramers from dimers.

Subcellular location

Cell junction › synapse. Secreted. Cell membrane; Peripheral membrane protein By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Hide | Top

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

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q9DDE3-1 [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

Hide | Top

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: 11016933] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

AJ251640 Genomic DNA. Translation: CAC19790.1.
IPIIPI00502706.
RefSeqNP_571921.1.
UniGeneDr.133438

3D structure databases

HSSPHSSP built from PDB template 1H23 based on UniProtKB P04058.
ModBaseSearch...

Protein family/group databases

MEROPSS09.979.

Genome annotation databases

EnsemblENSDART00000052989; ENSDARP00000052988; ENSDARG00000031796; Danio rerio. [Genome view]
GeneID114549.
KEGGdre:114549.

Organism-specific databases

CTD114549.
ZFINZDB-GENE-010906-1. ache.

Phylogenomic databases

HOGENOMQ9DDE3.
HOVERGENQ9DDE3.
OMAHYTDWLH.

Enzyme and pathway databases

BRENDA3.1.1.7. 96826.

Gene expression databases

ArrayExpressQ9DDE3.
BgeeQ9DDE3.

Family and domain databases

InterProIPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PANTHERPTHR11559. CarbesteraseB. 1 hit.
PfamPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

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: November 3, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectZebrafish annotation project

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents