ACE1_CAEBR
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 03-AUG-2022, entry version 130.
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}.
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; 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.CBG16374; -.
DR ESTHER; caebr-ACHE1; AChE.
DR MEROPS; S09.979; -.
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; CPGQETA; -.
DR OrthoDB; 754103at2759; -.
DR Proteomes; UP000008549; Chromosome X.
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; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase 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 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 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
