ACE4_CAEBR
ID ACE4_CAEBR Reviewed; 604 AA.
AC Q9NDG8; A8WTF3; Q620F3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Acetylcholinesterase 4;
DE Short=AChE 4;
DE EC=3.1.1.7;
DE Flags: Precursor;
GN Name=ace-4; ORFNames=CBG02827;
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 [MRNA].
RC STRAIN=AF16;
RA Combes D., Grauso M., Fedon Y., Toutant J.-P., Arpagaus M.;
RT "A fourth acetylcholinesterase gene in Caenorhabditis briggsae.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}. Secreted {ECO:0000250}.
CC Cell membrane {ECO:0000250}; Peripheral membrane protein {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; AF159505; AAF80378.1; -; mRNA.
DR EMBL; HE601438; CAP23764.3; -; Genomic_DNA.
DR AlphaFoldDB; Q9NDG8; -.
DR SMR; Q9NDG8; -.
DR STRING; 6238.CBG02827; -.
DR ESTHER; caebr-ACHE4; AChE.
DR MEROPS; S09.980; -.
DR EnsemblMetazoa; CBG02827a.1; CBG02827a.1; WBGene00025805.
DR WormBase; CBG02827a; CBP37642; WBGene00025805; Cbr-ace-4.
DR eggNOG; KOG4389; Eukaryota.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; Q9NDG8; -.
DR OMA; ENTWAIN; -.
DR OrthoDB; 754103at2759; -.
DR Proteomes; UP000008549; Chromosome II.
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; IEA:UniProtKB-EC.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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..604
FT /note="Acetylcholinesterase 4"
FT /id="PRO_0000008611"
FT ACT_SITE 219
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 477
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..115
FT /evidence="ECO:0000250"
FT DISULFID 273..284
FT /evidence="ECO:0000250"
FT DISULFID 426..561
FT /evidence="ECO:0000250"
SQ SEQUENCE 604 AA; 69952 MW; 73D4B6A653B325C4 CRC64;
MKPKLVFLPF LIFITVFIEE SEAVHPVVLE TKLGDIRGNE FFFLSKKIRT FFGVPFAEPP
VEEFRFRKPR EKKQWKKLFD ATKPANACFQ TRDNYNTSFW GSEMWNANTQ ISEDCLYLNI
WAPADAYNLT VMVWFFGGGF YSGSPSLSIY DGRALAATQH VIVVNINYRL GPFGFLYLDH
PDAPGNMGLL DQQLALHWIR QNIVSFGGNP DKVSVFGQSA GAASIVAHLI APGSRGLFKN
AILQSGSLEN TWAINSPFRA KQKSEKLLEL VGCNKTTVEN SMSCLRLVSP EQLSLSTWNI
SLTYLEFPFV IVSRDKHFFG HLDARAALRE GDFNRDVNLM IGMNKDEGNY WNIYQLPQFF
DKAEPPELTR HQFDNLIDST FSIQPDIIRS AAKYIYSDPN CTDHGRKTRF YAGQMNQIVG
DYFFSCDSLW LADQFFLFLQ ICSTPNGSLK NPPKVFVYYF TQSSSANPWP KWTGAMHGYE
IEYVFGVPLS YSKIYKRREQ IFSRKIMQFW ASFAKNGTPR LRVLKNSEHW PEFNEHNNYR
WMQLRSGSNI RPIKRRKETE CQFWRRVKDT EYTAYLTQEY SSSCHINSYR ILLFIPFFFI
FSAF