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Q9DDE3

- ACES_DANRE

UniProt

Q9DDE3 - ACES_DANRE

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Protein
Acetylcholinesterase
Gene
ache
Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 5 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 sitei495 – 4951Charge relay system By similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: ZFIN
  2. cholinesterase activity Source: RefGenome

GO - Biological processi

  1. acetylcholine catabolic process Source: ZFIN
  2. cellular response to methanol Source: ZFIN
  3. choline metabolic process Source: RefGenome
  4. myofibril assembly Source: ZFIN
  5. neuromuscular junction development Source: ZFIN
  6. neuron development Source: ZFIN
  7. regulation of synapse structure and activity Source: ZFIN
  8. response to amphetamine Source: ZFIN
  9. response to ethanol Source: ZFIN
  10. synaptic transmission, cholinergic Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

ReactomeiREACT_174660. Synthesis of PC.

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
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Chromosome 7

Organism-specific databases

ZFINiZDB-GENE-010906-1. ache.

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. endoplasmic reticulum lumen Source: RefGenome
  3. extracellular space Source: RefGenome
  4. plasma membrane Source: UniProtKB-SubCell
  5. 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 prediction
Add
BLAST
Chaini24 – 634611Acetylcholinesterase
PRO_0000008593Add
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 ↔ 580 By similarity
Glycosylationi512 – 5121N-linked (GlcNAc...) Reviewed prediction
Glycosylationi592 – 5921N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi631 – 631Interchain By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Gene expression databases

BgeeiQ9DDE3.

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliQ9DDE3.
SMRiQ9DDE3. Positions 28-592, 595-628.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00740000115241.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ9DDE3.
KOiK01049.
OMAiWEAFADI.
OrthoDBiEOG789C9R.
PhylomeDBiQ9DDE3.
TreeFamiTF315470.

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.

Q9DDE3-1 [UniParc]FASTAAdd to Basket

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MKTSDILLLP TVLLTFLFHN CFAQAEPDLV VATRLGRVQG TRLPVPDRSH    50
VIAFLGIPYA EPPIGKRRFK RAEPKKPWNN VFEAKEFSNA CYQFVDTSYP 100
GFPGIEMWNP NRVMSEDCLY LNVWVPPTPR PQNLTVMVWI YGGGFYSGSS 150
SLDVYDGRYL AYTEKVVVVS MNYRVGAFGF LALNGSSDAP GNVGLYDQRL 200
ALQWVQENIH FFGGNPKQVT IFGESAGAAS VGMHVLSPDS RPLFTRAILQ 250
SGVPNTPWAT VTFDEARRRT TKLGKLVGCT WGNDTELIDC LRNKHPQELI 300
DQEWQVLPWS SLFRFSFVPV VDGVFFPDTP DAMISSGNFK YTQILLGVNQ 350
DEGSYFLLYG APGFSKDNES LISREDFLES VKMGVPHAND IGLEAVILQY 400
TDWMDENNGQ KNRDAMDDIV GDQNVICPLQ HFAKSYAQYA ALHAQSSAAA 450
PGTLGWGNSG PTGYNSGNSH GAVYLYLFDH RASNLAWPEW MGVIHGYEIE 500
FVFGLPLEKR LNYTAEEEKL SRRIMRYWAN FARTGNPNVN TDGTMDSRRR 550
WPQFSANEQK HVGLNTEPMK VHKGLRTQFC ALWNRFLPRL LNITDNIDDV 600
ERQWKVEFHR WSSYMMHWKS QFDHYSKQER CTDL 634
Length:634
Mass (Da):71,998
Last modified:March 1, 2001 - v1
Checksum:i47F348EA8A7C1E52
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ251640 Genomic DNA. Translation: CAC19790.1.
RefSeqiNP_571921.1. NM_131846.1.
UniGeneiDr.133438.

Genome annotation databases

EnsembliENSDART00000052989; ENSDARP00000052988; ENSDARG00000031796.
GeneIDi114549.
KEGGidre:114549.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ251640 Genomic DNA. Translation: CAC19790.1 .
RefSeqi NP_571921.1. NM_131846.1.
UniGenei Dr.133438.

3D structure databases

ProteinModelPortali Q9DDE3.
SMRi Q9DDE3. Positions 28-592, 595-628.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.979.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSDART00000052989 ; ENSDARP00000052988 ; ENSDARG00000031796 .
GeneIDi 114549.
KEGGi dre:114549.

Organism-specific databases

CTDi 43.
ZFINi ZDB-GENE-010906-1. ache.

Phylogenomic databases

eggNOGi COG2272.
GeneTreei ENSGT00740000115241.
HOGENOMi HOG000091866.
HOVERGENi HBG008839.
InParanoidi Q9DDE3.
KOi K01049.
OMAi WEAFADI.
OrthoDBi EOG789C9R.
PhylomeDBi Q9DDE3.
TreeFami TF315470.

Enzyme and pathway databases

Reactomei REACT_174660. Synthesis of PC.

Miscellaneous databases

NextBioi 20796951.
PROi Q9DDE3.

Gene expression databases

Bgeei Q9DDE3.

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. "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].

Entry informationi

Entry nameiACES_DANRE
AccessioniPrimary (citable) accession number: Q9DDE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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