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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 intermediatePROSITE-ProRule annotation
Active sitei352 – 3521Charge relay systemBy similarity
Active sitei495 – 4951Charge relay systemBy 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.
REACT_234881. Neurotransmitter Clearance In The Synaptic Cleft.

Protein family/group databases

MEROPSiS09.980.

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-KW
  5. synapse Source: UniProtKB-KW
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 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 634611AcetylcholinesterasePRO_0000008593Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 118By similarity
Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi279 ↔ 290By similarity
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi427 ↔ 580By similarity
Glycosylationi512 – 5121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi592 – 5921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi631 – 631InterchainBy 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00760000118946.
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

« Hide

        10         20         30         40         50
MKTSDILLLP TVLLTFLFHN CFAQAEPDLV VATRLGRVQG TRLPVPDRSH
60 70 80 90 100
VIAFLGIPYA EPPIGKRRFK RAEPKKPWNN VFEAKEFSNA CYQFVDTSYP
110 120 130 140 150
GFPGIEMWNP NRVMSEDCLY LNVWVPPTPR PQNLTVMVWI YGGGFYSGSS
160 170 180 190 200
SLDVYDGRYL AYTEKVVVVS MNYRVGAFGF LALNGSSDAP GNVGLYDQRL
210 220 230 240 250
ALQWVQENIH FFGGNPKQVT IFGESAGAAS VGMHVLSPDS RPLFTRAILQ
260 270 280 290 300
SGVPNTPWAT VTFDEARRRT TKLGKLVGCT WGNDTELIDC LRNKHPQELI
310 320 330 340 350
DQEWQVLPWS SLFRFSFVPV VDGVFFPDTP DAMISSGNFK YTQILLGVNQ
360 370 380 390 400
DEGSYFLLYG APGFSKDNES LISREDFLES VKMGVPHAND IGLEAVILQY
410 420 430 440 450
TDWMDENNGQ KNRDAMDDIV GDQNVICPLQ HFAKSYAQYA ALHAQSSAAA
460 470 480 490 500
PGTLGWGNSG PTGYNSGNSH GAVYLYLFDH RASNLAWPEW MGVIHGYEIE
510 520 530 540 550
FVFGLPLEKR LNYTAEEEKL SRRIMRYWAN FARTGNPNVN TDGTMDSRRR
560 570 580 590 600
WPQFSANEQK HVGLNTEPMK VHKGLRTQFC ALWNRFLPRL LNITDNIDDV
610 620 630
ERQWKVEFHR WSSYMMHWKS QFDHYSKQER CTDL
Length:634
Mass (Da):71,998
Last modified:March 1, 2001 - v1
Checksum:i47F348EA8A7C1E52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 S09.980.

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 ENSGT00760000118946.
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.
REACT_234881. Neurotransmitter Clearance In The Synaptic Cleft.

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: November 26, 2014
This is version 96 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