ID   ACE1_CAEBR              Reviewed;         620 AA.
AC   Q27459; A8XNK7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Acetylcholinesterase 1;
DE            Short=AChE 1;
DE            EC=3.1.1.7;
DE   Flags: Precursor;
GN   Name=ace-1; ORFNames=CBG16374;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8912924; DOI=10.3109/10425179609008446;
RA   Grauso M., Culetto E., Berge J.-B., Toutant J.-P., Arpagaus M.;
RT   "Sequence comparison of ACE-1, the gene encoding acetylcholinesterase of
RT   class A, in the two nematodes Caenorhabditis elegans and Caenorhabditis
RT   briggsae.";
RL   DNA Seq. 6:217-227(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Rapidly hydrolyzes choline released into the synapse.
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   -!- 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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; U41846; AAB41269.1; -; Genomic_DNA.
DR   EMBL; HE600961; CAP34096.3; -; Genomic_DNA.
DR   RefSeq; XP_002643631.1; XM_002643585.1.
DR   AlphaFoldDB; Q27459; -.
DR   SMR; Q27459; -.
DR   STRING; 6238.Q27459; -.
DR   ESTHER; caebr-ACHE1; ACHE.
DR   MEROPS; S09.979; -.
DR   GlyCosmos; Q27459; 4 sites, No reported glycans.
DR   EnsemblMetazoa; CBG16374.1; CBG16374.1; WBGene00036330.
DR   GeneID; 8585625; -.
DR   KEGG; cbr:CBG_16374; -.
DR   CTD; 8585625; -.
DR   WormBase; CBG16374; CBP03902; WBGene00036330; Cbr-ace-1.
DR   eggNOG; KOG4389; Eukaryota.
DR   HOGENOM; CLU_006586_13_0_1; -.
DR   InParanoid; Q27459; -.
DR   OMA; YNASFAN; -.
DR   OrthoDB; 4386at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
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; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR   GO; GO:0006581; P:acetylcholine catabolic process; IBA:GO_Central.
DR   GO; GO:0019695; P:choline metabolic process; IBA:GO_Central.
DR   GO; GO:0040012; P:regulation of locomotion; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
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_0000008609"
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:0000255"
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:0000255"
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;  71501 MW;  69D73CD3996E11FC CRC64;
     MRYSLLFFIF LPCVITAVDL IHLHDGSPLF GEEVLSQTGK PLTRFLGIPF AEPPIGNLRF
     RKPKPKQPWR IPFNATTPPN SCIQSEDTYF GDFYGSTMWN PNTKLSEDCL YLNVYVPGKV
     DPNKKLAVMI WVYGGGFWSG TSTLDVYDGR ILTVEENVIL VAMNYRVSIF GFLYMNRSEA
     PGNMGMWDQL LAMKWVHKNI DLFGGDTSRI TLFGESAGAA SVSIHMLSQK SAPYFHRAII
     QSGSATSPWA IEPRDVALAR AVILYNAMKC GNMSLISPDY DRILDCFQRA DADALRENEW
     APVREFGDFP WVPVVDGDFL LENAQTSLKQ GNFKKTQLLA GSNRDESIYF LTYQLPDIFP
     VADFFSKSEF IKDRQTWIKG VKDLLPRQIL KCQLTLAAVL HEYEPQDLPI SAQNWLNAMD
     KMLGDYHFTC SVNEMALAHT KHGGDTFYYY FTHRATQQTW PEWMGVLHGY EINFIFGEPF
     NQKRFNYTDE ERELSNRFMR YWANFAKTGD PNKNEDGSFT QDIWPKYNSV SMEYMNMTVE
     SSYPGQNRIG HGPRRKECAF WKAYLPNLMA AVADVGDPYL VWKQQMDKWQ NEYITDWQYH
     FEQYKRYQTY RQSDSETCGG
//