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 24-JAN-2024, entry version 107. 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.Q9NDG8; -. DR ESTHER; caebr-ACHE4; ACHE. DR MEROPS; S09.980; -. DR GlyCosmos; Q9NDG8; 6 sites, No reported glycans. 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; 4386at2759; -. DR Proteomes; UP000008549; Chromosome II. 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 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:SF2; CARBOXYLIC ESTER HYDROLASE; 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 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 //