ACES_DANRE
ID ACES_DANRE Reviewed; 634 AA.
AC Q9DDE3;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Acetylcholinesterase;
DE Short=AChE {ECO:0000303|PubMed:11016933};
DE EC=3.1.1.7 {ECO:0000269|PubMed:11016933};
DE Flags: Precursor;
GN Name=ache;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE,
RP SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11016933; DOI=10.1074/jbc.m006308200;
RA Bertrand C., Chatonnet A., Takke C., Yan Y., Postlethwait J.,
RA Toutant J.-P., Cousin X.;
RT "Zebrafish acetylcholinesterase is encoded by a single gene localized on
RT linkage group 7. gene structure and polymorphism; molecular forms and
RT expression pattern during development.";
RL J. Biol. Chem. 276:464-474(2001).
CC -!- FUNCTION: Terminates signal transduction at the neuromuscular junction
CC by rapid hydrolysis of the acetylcholine released into the synaptic
CC cleft.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetylcholine + H2O = acetate + choline + H(+);
CC Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7;
CC Evidence={ECO:0000269|PubMed:11016933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17562;
CC Evidence={ECO:0000305|PubMed:11016933};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=230 uM for acetylcholine {ECO:0000269|PubMed:11016933};
CC -!- SUBUNIT: Dimers and collagen-tailed forms, in which catalytic tetramers
CC are associated with anchoring proteins that attach them to the basal
CC lamina or to cell membranes. In the collagen-tailed forms, subunits are
CC associated with a specific collagen, COLQ, which triggers the formation
CC of isoform T tetramers from dimers. {ECO:0000269|PubMed:11016933}.
CC -!- SUBCELLULAR LOCATION: Synapse. Secreted. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: First detected in the trunk, in discrete regions
CC of paraxial mesodermal segmental plate at 12 h of devel-opment (6-
CC somite stage). In older embryos a weak diffused staining is found, even
CC in unsegmented presomitic mesoderm. Expression, probably located in
CC myoblasts, proceeds in a rostro-caudal sequence according to the state
CC of differentiation of the somites. Initial narrow staining
CC progressively enlarged in the differentiating somite. At all stages,
CC the ventral part of anterior somites showed more intense staining than
CC the dorsal part. In the posterior brain expression and activity appear
CC after 14 h. At 24h, detected in all primary neurons in the brain.
CC Expression in cranial ganglia can be detected in whole embryo until
CC about 36h. Expressed also in a sensory system in anterior and
CC posteriorlateral line ganglia as seen in the embryo at 24h. In addition
CC the heart shows strong expression from its early morphogenesis.
CC {ECO:0000269|PubMed:11016933}.
CC -!- MISCELLANEOUS: No other isoforms exist. This protein corresponds to the
CC T isoform in other species.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ251640; CAC19790.1; -; Genomic_DNA.
DR RefSeq; NP_571921.1; NM_131846.2.
DR AlphaFoldDB; Q9DDE3; -.
DR SMR; Q9DDE3; -.
DR STRING; 7955.ENSDARP00000052988; -.
DR ChEMBL; CHEMBL3308995; -.
DR ESTHER; danre-ACHE; AChE.
DR MEROPS; S09.980; -.
DR PaxDb; Q9DDE3; -.
DR Ensembl; ENSDART00000052989; ENSDARP00000052988; ENSDARG00000031796.
DR GeneID; 114549; -.
DR KEGG; dre:114549; -.
DR CTD; 43; -.
DR ZFIN; ZDB-GENE-010906-1; ache.
DR eggNOG; KOG4389; Eukaryota.
DR GeneTree; ENSGT00940000157637; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; Q9DDE3; -.
DR OMA; CDHLVAP; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q9DDE3; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.7; 928.
DR PRO; PR:Q9DDE3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000031796; Expressed in muscle tissue and 25 other tissues.
DR ExpressionAtlas; Q9DDE3; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0003990; F:acetylcholinesterase activity; IDA:ZFIN.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0006581; P:acetylcholine catabolic process; IDA:ZFIN.
DR GO; GO:0071405; P:cellular response to methanol; IDA:ZFIN.
DR GO; GO:0019695; P:choline metabolic process; IBA:GO_Central.
DR GO; GO:0030239; P:myofibril assembly; IMP:ZFIN.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:ZFIN.
DR GO; GO:0048666; P:neuron development; IMP:ZFIN.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IMP:ZFIN.
DR GO; GO:0001975; P:response to amphetamine; IMP:ZFIN.
DR GO; GO:0045471; P:response to ethanol; IDA:ZFIN.
DR GO; GO:0009749; P:response to glucose; IDA:ZFIN.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR014788; AChE_tetra.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000997; Cholinesterase.
DR Pfam; PF08674; AChE_tetra; 1.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR00878; CHOLNESTRASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Neurotransmitter degradation; Reference proteome; Secreted;
KW Serine esterase; Signal; Synapse.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..634
FT /note="Acetylcholinesterase"
FT /id="PRO_0000008593"
FT ACT_SITE 225
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 352
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 495
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..118
FT /evidence="ECO:0000250"
FT DISULFID 279..290
FT /evidence="ECO:0000250"
FT DISULFID 427..580
FT /evidence="ECO:0000250"
FT DISULFID 631
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 634 AA; 71998 MW; 47F348EA8A7C1E52 CRC64;
MKTSDILLLP TVLLTFLFHN CFAQAEPDLV VATRLGRVQG TRLPVPDRSH VIAFLGIPYA
EPPIGKRRFK RAEPKKPWNN VFEAKEFSNA CYQFVDTSYP GFPGIEMWNP NRVMSEDCLY
LNVWVPPTPR PQNLTVMVWI YGGGFYSGSS SLDVYDGRYL AYTEKVVVVS MNYRVGAFGF
LALNGSSDAP GNVGLYDQRL ALQWVQENIH FFGGNPKQVT IFGESAGAAS VGMHVLSPDS
RPLFTRAILQ SGVPNTPWAT VTFDEARRRT TKLGKLVGCT WGNDTELIDC LRNKHPQELI
DQEWQVLPWS SLFRFSFVPV VDGVFFPDTP DAMISSGNFK YTQILLGVNQ DEGSYFLLYG
APGFSKDNES LISREDFLES VKMGVPHAND IGLEAVILQY TDWMDENNGQ KNRDAMDDIV
GDQNVICPLQ HFAKSYAQYA ALHAQSSAAA PGTLGWGNSG PTGYNSGNSH GAVYLYLFDH
RASNLAWPEW MGVIHGYEIE FVFGLPLEKR LNYTAEEEKL SRRIMRYWAN FARTGNPNVN
TDGTMDSRRR WPQFSANEQK HVGLNTEPMK VHKGLRTQFC ALWNRFLPRL LNITDNIDDV
ERQWKVEFHR WSSYMMHWKS QFDHYSKQER CTDL
