ID   ACE1_CAEEL              Reviewed;         620 AA.
AC   P38433;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Acetylcholinesterase 1;
DE            Short=ACE-1 {ECO:0000303|PubMed:8144590};
DE            Short=AChE 1;
DE            EC=3.1.1.7 {ECO:0000305|PubMed:8144590};
DE   Flags: Precursor;
GN   Name=ace-1; ORFNames=W09B12.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=Bristol N2;
RX   PubMed=8144590; DOI=10.1016/s0021-9258(17)36976-4;
RA   Arpagaus M., Fedon Y., Cousin X., Chatonnet A., Berge J.-B., Fournier D.,
RA   Toutant J.-P.;
RT   "cDNA sequence, gene structure, and in vitro expression of ace-1, the gene
RT   encoding acetylcholinesterase of class A in the nematode Caenorhabditis
RT   elegans.";
RL   J. Biol. Chem. 269:9957-9965(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74 AND ASN-486, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- FUNCTION: Rapidly hydrolyzes acetylcholine and releases choline into
CC       the synapse (Probable). It can hydrolyze propionylcholine and
CC       butyrylthiocholine in vitro (Probable). {ECO:0000305|PubMed:8144590}.
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:0000305|PubMed:8144590};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17562;
CC         Evidence={ECO:0000305|PubMed:8144590};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=57 uM for acetylthiocholine {ECO:0000269|PubMed:8144590};
CC   -!- SUBUNIT: Oligomer composed of disulfide-linked homodimers.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}. Secreted {ECO:0000250}.
CC       Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Note=May be secreted or membrane associated via a non-catalytic
CC       subunit.
CC   -!- DEVELOPMENTAL STAGE: Detected at all stages. Found to be more abundant
CC       in larval stages than in embryos or adults.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; X75331; CAA53080.1; -; mRNA.
DR   EMBL; FO081067; CCD68912.1; -; Genomic_DNA.
DR   PIR; A54413; A54413.
DR   PIR; T29347; T29347.
DR   RefSeq; NP_510660.1; NM_078259.6.
DR   AlphaFoldDB; P38433; -.
DR   SMR; P38433; -.
DR   BioGRID; 46591; 1.
DR   STRING; 6239.W09B12.1.2; -.
DR   ChEMBL; CHEMBL3341583; -.
DR   ESTHER; caeel-ACHE1; ACHE.
DR   MEROPS; S09.979; -.
DR   GlyCosmos; P38433; 4 sites, No reported glycans.
DR   iPTMnet; P38433; -.
DR   EPD; P38433; -.
DR   PaxDb; 6239-W09B12-1-2; -.
DR   PeptideAtlas; P38433; -.
DR   EnsemblMetazoa; W09B12.1.1; W09B12.1.1; WBGene00000035.
DR   GeneID; 181706; -.
DR   KEGG; cel:CELE_W09B12.1; -.
DR   UCSC; W09B12.1.1; c. elegans.
DR   AGR; WB:WBGene00000035; -.
DR   WormBase; W09B12.1; CE07569; WBGene00000035; ace-1.
DR   eggNOG; KOG4389; Eukaryota.
DR   GeneTree; ENSGT00940000159300; -.
DR   HOGENOM; CLU_006586_13_0_1; -.
DR   InParanoid; P38433; -.
DR   OMA; YNASFAN; -.
DR   OrthoDB; 4386at2759; -.
DR   PhylomeDB; P38433; -.
DR   Reactome; R-CEL-112311; Neurotransmitter clearance.
DR   Reactome; R-CEL-1483191; Synthesis of PC.
DR   Reactome; R-CEL-9749641; Aspirin ADME.
DR   PRO; PR:P38433; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00000035; Expressed in larva and 3 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0043083; C:synaptic cleft; IEA:GOC.
DR   GO; GO:0003990; F:acetylcholinesterase activity; IDA:WormBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:WormBase.
DR   GO; GO:0006581; P:acetylcholine catabolic process; IDA:WormBase.
DR   GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; IC:WormBase.
DR   GO; GO:0019695; P:choline metabolic process; IBA:GO_Central.
DR   GO; GO:0040012; P:regulation of locomotion; IGI:WormBase.
DR   CDD; cd00312; Esterase_lipase; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000997; Cholinesterase.
DR   PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1.
DR   PANTHER; PTHR43918:SF12; ACETYLCHOLINESTERASE 1; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR00878; CHOLNESTRASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..620
FT                   /note="Acetylcholinesterase 1"
FT                   /id="PRO_0000008610"
FT   ACT_SITE        216
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        346
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        468
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        486
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        536
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..286
FT                   /evidence="ECO:0000250"
FT   DISULFID        430..558
FT                   /evidence="ECO:0000250"
FT   DISULFID        618
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   620 AA;  71433 MW;  61D78C4899F55C65 CRC64;
     MRNSLLFFIF LPSTILAVDL IHLHDGSPLF GEEVLSQTGK PLTRFQGIPF AEPPVGNLRF
     KKPKPKQPWR IPLNATTPPN SCIQSEDTYF GDFYGSTMWN ANTKLSEDCL YLNVYVPGKV
     DPNKKLAVMV WVYGGGFWSG TATLDVYDGR ILTVEENVIL VAMNYRVSIF GFLYMNRPEA
     PGNMGMWDQL LAMKWVHKNI DLFGGDLSRI TLFGESAGAA SVSIHMLSPK SAPYFHRAII
     QSGSATSPWA IEPRDVALAR AVILYNAMKC GNMSLINPDY DRILDCFQRA DADALRENEW
     APVREFGDFP WVPVVDGDFL LENAQTSLKQ GNFKKTQLLA GSNRDESIYF LTYQLPDIFP
     VADFFTKTDF IKDRQLWIKG VKDLLPRQIL KCQLTLAAVL HEYEPQDLPV TPRDWINAMD
     KMLGDYHFTC SVNEMALAHT KHGGDTYYYY FTHRASQQTW PEWMGVLHGY EINFIFGEPL
     NQKRFNYTDE ERELSNRFMR YWANFAKTGD PNKNEDGSFT QDVWPKYNSV SMEYMNMTVE
     SSYPSMKRIG HGPRRKECAF WKAYLPNLMA AVADVGDPYL VWKQQMDKWQ NEYITDWQYH
     FEQYKRYQTY RQSDSETCGG
//