ACE1_CAEEL
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 03-AUG-2022, entry version 158.
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 iPTMnet; P38433; -.
DR EPD; P38433; -.
DR PaxDb; P38433; -.
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 CTD; 181706; -.
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; CPGQETA; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P38433; -.
DR PRO; PR:P38433; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000035; Expressed in larva and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
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 Gene3D; 3.40.50.1820; -; 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 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..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
