ACES_ANOGA
ID ACES_ANOGA Reviewed; 737 AA.
AC Q869C3; Q7PUR2; Q7RTM0; Q86GC7; Q8ISM4; Q8ISM7;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Acetylcholinesterase;
DE Short=AChE;
DE EC=3.1.1.7;
DE Flags: Precursor;
GN Name=Ace; Synonyms=ACE1, ACHE1; ORFNames=AGAP001356;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000312|EMBL:CAD56156.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Kisumu, Kisumu2, and YAO {ECO:0000312|EMBL:CAD56156.1};
RX PubMed=12736674; DOI=10.1038/423136b;
RA Weill M., Lutfalla G., Mogensen K., Chandre F., Berthomieu A., Berticat C.,
RA Pasteur N., Philips A., Fort P., Raymond M.;
RT "Insecticide resistance in mosquito vectors.";
RL Nature 423:136-137(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [3]
RP PARTIAL GENE STRUCTURE.
RX PubMed=12396499; DOI=10.1098/rspb.2002.2122;
RA Weill M., Fort P., Berthomi eu A., Dubois M.P., Pasteur N., Raymond M.;
RT "A novel acetylcholinesterase gene in mosquitoes codes for the insecticide
RT target and is non-homologous to the ace gene in Drosophila.";
RL Proc. R. Soc. B 269:2007-2016(2002).
CC -!- FUNCTION: Rapidly hydrolyzes choline released into the synapse.
CC {ECO:0000305}.
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:0000250|UniProtKB:P22303};
CC -!- SUBCELLULAR LOCATION: Synapse.
CC -!- POLYMORPHISM: Strains Kisumu and Kisumu2 are susceptible to
CC insecticides while strain YAO is resistant. Insensitivity to
CC insecticides results from a loss of sensitivity of acetylcholinesterase
CC to organophosphates and carbamates and is due to a variant at position
CC 280.
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; AJ488492; CAD32684.2; -; Genomic_DNA.
DR EMBL; AJ515149; CAD56156.1; -; Genomic_DNA.
DR EMBL; AJ515148; CAD56156.1; JOINED; Genomic_DNA.
DR EMBL; AJ515150; CAD56157.2; -; Genomic_DNA.
DR EMBL; AJ488492; CAD56157.2; JOINED; Genomic_DNA.
DR EMBL; AAAB01008987; EAA01151.3; -; Genomic_DNA.
DR EMBL; BN000066; CAD29865.2; -; Genomic_DNA.
DR RefSeq; XP_321792.2; XM_321792.4.
DR PDB; 5X61; X-ray; 3.40 A; A/B=162-714.
DR PDB; 5YDH; X-ray; 3.21 A; A/B=162-737.
DR PDB; 5YDI; X-ray; 3.45 A; A/B/C=162-714.
DR PDB; 5YDJ; X-ray; 3.04 A; A/B=1-737.
DR PDB; 6ARX; X-ray; 2.30 A; A/B=162-702.
DR PDB; 6ARY; X-ray; 2.26 A; A/B=162-702.
DR PDBsum; 5X61; -.
DR PDBsum; 5YDH; -.
DR PDBsum; 5YDI; -.
DR PDBsum; 5YDJ; -.
DR PDBsum; 6ARX; -.
DR PDBsum; 6ARY; -.
DR AlphaFoldDB; Q869C3; -.
DR SMR; Q869C3; -.
DR STRING; 7165.AGAP001356-PA; -.
DR BindingDB; Q869C3; -.
DR ChEMBL; CHEMBL2046266; -.
DR ESTHER; anoga-ACHE1; AChE.
DR PaxDb; Q869C3; -.
DR GeneID; 1281827; -.
DR KEGG; aga:AgaP_AGAP001356; -.
DR CTD; 1281827; -.
DR VEuPathDB; VectorBase:AGAP001356; -.
DR eggNOG; KOG4389; Eukaryota.
DR InParanoid; Q869C3; -.
DR OMA; CDHLVAP; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q869C3; -.
DR PRO; PR:Q869C3; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR ExpressionAtlas; Q869C3; differential.
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:0006581; P:acetylcholine catabolic process; IBA:GO_Central.
DR GO; GO:0019695; P:choline metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase;
KW Neurotransmitter degradation; Reference proteome; Serine esterase; Signal;
KW Synapse.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..737
FT /note="Acetylcholinesterase"
FT /id="PRO_0000008599"
FT REGION 141..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 360
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 486
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 600
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 228..255
FT /evidence="ECO:0000250"
FT DISULFID 414..427
FT /evidence="ECO:0000250"
FT DISULFID 562..683
FT /evidence="ECO:0000250"
FT VARIANT 127
FT /note="V -> A (in strain: Kisumu2 and YAO)"
FT VARIANT 280
FT /note="G -> S (in strain: YAO; confers resistance to
FT insecticides)"
FT /evidence="ECO:0000269|PubMed:12736674"
FT CONFLICT 35
FT /note="F -> S (in Ref. 1; CAD56157)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="A -> S (in Ref. 1; CAD56157)"
FT /evidence="ECO:0000305"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5YDH"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5YDH"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:6ARY"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:5YDJ"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 328..343
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 349..359
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:6ARY"
FT TURN 373..377
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:6ARY"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:5YDJ"
FT HELIX 398..411
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 433..438
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:5YDH"
FT HELIX 488..494
FT /evidence="ECO:0007829|PDB:6ARY"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 509..519
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 525..534
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 544..559
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 561..573
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 578..583
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:6ARY"
FT TURN 600..603
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 604..607
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:5X61"
FT HELIX 620..639
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:6ARY"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:6ARY"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 680..687
FT /evidence="ECO:0007829|PDB:6ARY"
FT HELIX 689..696
FT /evidence="ECO:0007829|PDB:6ARY"
SQ SEQUENCE 737 AA; 80902 MW; FDE9CCAE34DF2421 CRC64;
MEIRGLLMGR LRLGRRMVPL GLLGVTALLL ILPPFALVQG RHHELNNGAA IGSHQLSAAA
GVGLASQSAQ SGSLASGVMS SVPAAGASSS SSSSLLSSSA EDDVARITLS KDADAFFTPY
IGHGESVRII DAELGTLEHV HSGATPRRRG LTRRESNSDA NDNDPLVVNT DKGRIRGITV
DAPSGKKVDV WLGIPYAQPP VGPLRFRHPR PAEKWTGVLN TTTPPNSCVQ IVDTVFGDFP
GATMWNPNTP LSEDCLYINV VAPRPRPKNA AVMLWIFGGG FYSGTATLDV YDHRALASEE
NVIVVSLQYR VASLGFLFLG TPEAPGNAGL FDQNLALRWV RDNIHRFGGD PSRVTLFGES
AGAVSVSLHL LSALSRDLFQ RAILQSGSPT APWALVSREE ATLRALRLAE AVGCPHEPSK
LSDAVECLRG KDPHVLVNNE WGTLGICEFP FVPVVDGAFL DETPQRSLAS GRFKKTEILT
GSNTEEGYYF IIYYLTELLR KEEGVTVTRE EFLQAVRELN PYVNGAARQA IVFEYTDWTE
PDNPNSNRDA LDKMVGDYHF TCNVNEFAQR YAEEGNNVYM YLYTHRSKGN PWPRWTGVMH
GDEINYVFGE PLNPTLGYTE DEKDFSRKIM RYWSNFAKTG NPNPNTASSE FPEWPKHTAH
GRHYLELGLN TSFVGRGPRL RQCAFWKKYL PQLVAATSNL PGPAPPSEPC ESSAFFYRPD
LIVLLVSLLT ATVRFIQ
