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Database: UniProt
Entry: A0A1Y9H1Y9_9DIPT
LinkDB: A0A1Y9H1Y9_9DIPT
Original site: A0A1Y9H1Y9_9DIPT 
ID   A0A1Y9H1Y9_9DIPT        Unreviewed;       733 AA.
AC   A0A1Y9H1Y9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Acetylcholinesterase {ECO:0000256|ARBA:ARBA00020419};
DE            EC=3.1.1.7 {ECO:0000256|ARBA:ARBA00013276};
OS   Anopheles dirus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR015679-PA, ECO:0000313|Proteomes:UP000075884};
RN   [1] {ECO:0000313|Proteomes:UP000075884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles dirus WRAIR2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ADIR015679-PA}
RP   IDENTIFICATION.
RC   STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR015679-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- FUNCTION: Rapidly hydrolyzes choline released into the synapse.
CC       {ECO:0000256|ARBA:ARBA00037263}.
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:0000256|ARBA:ARBA00000347};
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000256|ARBA:ARBA00034103}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000256|ARBA:ARBA00005964}.
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DR   AlphaFoldDB; A0A1Y9H1Y9; -.
DR   STRING; 7168.A0A1Y9H1Y9; -.
DR   ESTHER; anoga-ACHE1; ACHE.
DR   EnsemblMetazoa; ADIR015679-RA; ADIR015679-PA; ADIR015679.
DR   VEuPathDB; VectorBase:ADIR015679; -.
DR   OrthoDB; 4386at2759; -.
DR   Proteomes; UP000075884; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0003990; F:acetylcholinesterase activity; IEA:UniProtKB-EC.
DR   CDD; cd00312; Esterase_lipase; 1.
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:SF12; ACETYLCHOLINESTERASE 1; 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   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Neurotransmitter degradation {ECO:0000256|ARBA:ARBA00022867};
KW   Serine esterase {ECO:0000256|ARBA:ARBA00022487};
KW   Signal {ECO:0000256|SAM:SignalP}; Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           41..733
FT                   /note="Acetylcholinesterase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011005351"
FT   TRANSMEM        711..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          162..682
FT                   /note="Carboxylesterase type B"
FT                   /evidence="ECO:0000259|Pfam:PF00135"
FT   REGION          120..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        356
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600997-1"
FT   ACT_SITE        482
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600997-1"
FT   ACT_SITE        596
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600997-1"
SQ   SEQUENCE   733 AA;  80057 MW;  C7CE10639205F0E3 CRC64;
     MEIRGLLMAR LRLGRRQVPL QVLCASALLL LLPPSALVHG RHHELNNGAA IGAHQLSAAG
     GAASLTSQPS GSAGSLAAGA AAAAVAAGAG SSASSSLSSS SAEDDVARIT LSKDAGHGES
     VRIIDPELGT LEREHVHSGA TPRRRGLTRR ESNADANDND PLVVNTDKGR IRGITVEAPS
     GKKVDVWLGI PYAQPPVGPL RFRHPRPAEK WTGVLNATTP PNSCVQIVDT VFGDFPGATM
     WNPNTPLSED CLYINVVAPR PRPKNAAVML WIFGGGFYSG TATLDVYDHR ALASEENVIV
     VSLQYRVASL GFLFLGTPEA PGNAGLFDQN LALRWVRDNI HRFGGDPSRV TLFGESAGAV
     SVSLHLLSAL SRDLFQRAIL QSGSPTAPWA LVSREEATLR ALRLAEAVGC PHEPSKLSES
     VECLRGKDPH VLVNNEWGTL GICEFPFVPV VDGAFLDETP QRSLASGRFK KTEILTGSNT
     EEGYYFIIYY LTELLRKEEG VTVSREEFLQ AVRELNPYVN GAARQAIVFE YTDWTEPDNP
     NSNRDALDKM VGDYHFTCNV NEFAQRYAEE GNNVYMYLYT HRSKGNPWPR WTGVMHGDEI
     NYVFGEPLNP TLGYTEDEKD FSRKVMRYWS NFAKTGNPNP STASSEFPEW PKHTAHGRHY
     LELGLNTSFV GRGPRLRQCA FWKKYLPQLV AATSNLQVAA PPSAPCESSA FFYRPNLIVL
     LVALLSVAIR FIQ
//
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