ID   ACES_TRILK              Reviewed;         559 AA.
AC   W4VSJ0;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Acetylcholinesterase-1;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor;
OS   Trittame loki (Brush-footed trapdoor spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Barychelidae; Trittame.
OX   NCBI_TaxID=1295018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=24351713; DOI=10.3390/toxins5122488;
RA   Undheim E.A., Sunagar K., Herzig V., Kely L., Low D.H., Jackson T.N.,
RA   Jones A., Kurniawan N., King G.F., Ali S.A., Antunes A., Ruder T.,
RA   Fry B.G.;
RT   "A proteomics and transcriptomics investigation of the venom from the
RT   barychelid spider Trittame loki (brush-foot trapdoor).";
RL   Toxins 5:2488-2503(2013).
CC   -!- FUNCTION: Terminates signal transduction at the neuromuscular junction
CC       by rapid hydrolysis of the acetylcholine released into the synaptic
CC       cleft. {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: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; GAQE01000001; JAB84553.1; -; Transcribed_RNA.
DR   AlphaFoldDB; W4VSJ0; -.
DR   SMR; W4VSJ0; -.
DR   ESTHER; trilk-aces; Cholinesterase-like.
DR   ArachnoServer; AS002074; Acetylcholinesterase-1-Trittame loki.
DR   GO; GO:0005576; C:extracellular region; 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; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000997; Cholinesterase.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR00878; CHOLNESTRASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Neurotransmitter degradation;
KW   Phosphoprotein; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..559
FT                   /note="Acetylcholinesterase-1"
FT                   /id="PRO_0000429205"
FT   ACT_SITE        223
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        354
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        471
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        92..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        276..293
FT                   /evidence="ECO:0000250"
FT   DISULFID        432..550
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   559 AA;  62782 MW;  ABC3F6A31A8F42BD CRC64;
     MMLPRCFVTV LLMSSVLYIG GETSSEVLGP VVSTEAGSFQ GMELTTHGER VIYAFLGIPY
     AKPPTGLLRF KKPQPADFIQ GTYKATEKPP SCFQLDSDLQ LPWADPDSPM KEDCLFLNLW
     TPASLSTEEE ELKSVMVWIH GGGYTSGSSA LDVYDGQTLS SSGDVVVVTM NYRLDAFGFL
     NSLTEDAPGN MALYDQLLAL QWVHTNIKYF GGDPNKVTLF GESVGAFATS FLALSPLTKG
     LFQKIMLESG SAYNKLTVNS IDQAKNNNQL ATLVGCANET FTLISNPEEV VACMREVAPA
     KFTQTYYKEL GSEREKINFI FWPHFGDDIL PTRTAELIKE KNLTALFAGV NSVEGSALSV
     FFFPEVYQMF VESNLTLTKA YATILMNEFF KVFNFQDSAK AIEFYLGDVE DDDEEGIRSA
     LFGVVGDYII TCPTIYLADK YSERGANVQF YRFDRRPSTS QWPPEWMGAA HNDEIQFVFG
     MPVRYPEKYT EEERTLSEYM TRTWTNFVKS EDLKLKNGSQ WPSYSLSEPQ FATLQTNEQI
     IGSGQRKAEC DFWRPYFDI