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Protein

Acetylcholinesterase

Gene

Ace

Organism
Anopheles gambiae (African malaria mosquito)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Rapidly hydrolyzes choline released into the synapse.Curated

Catalytic activityi

Acetylcholine + H2O = choline + acetate.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei360 – 3601Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei486 – 4861Charge relay systemBy similarity
Active sitei600 – 6001Charge relay systemBy similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: UniProtKB-EC
  2. carboxylic ester hydrolase activity Source: GO_Central

GO - Biological processi

  1. neurotransmitter catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Protein family/group databases

MEROPSiS09.980.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
Gene namesi
Name:Ace
Synonyms:ACE1, ACHE1
ORF Names:AGAP001356
OrganismiAnopheles gambiae (African malaria mosquito)Imported
Taxonomic identifieri7165 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
ProteomesiUP000007062 Componenti: Chromosome 2R

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. extracellular space Source: GO_Central
  3. synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3838Sequence AnalysisAdd
BLAST
Chaini39 – 737699AcetylcholinesterasePRO_0000008599Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi228 ↔ 255By similarity
Disulfide bondi414 ↔ 427By similarity
Disulfide bondi562 ↔ 683By similarity
Glycosylationi670 – 6701N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AZGmodel-A115-737[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
HOGENOMiHOG000091866.
InParanoidiQ869C3.
KOiK01049.
OMAiGPTRETQ.
OrthoDBiEOG7353WH.
PhylomeDBiQ869C3.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q869C3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIRGLLMGR LRLGRRMVPL GLLGVTALLL ILPPFALVQG RHHELNNGAA
60 70 80 90 100
IGSHQLSAAA GVGLASQSAQ SGSLASGVMS SVPAAGASSS SSSSLLSSSA
110 120 130 140 150
EDDVARITLS KDADAFFTPY IGHGESVRII DAELGTLEHV HSGATPRRRG
160 170 180 190 200
LTRRESNSDA NDNDPLVVNT DKGRIRGITV DAPSGKKVDV WLGIPYAQPP
210 220 230 240 250
VGPLRFRHPR PAEKWTGVLN TTTPPNSCVQ IVDTVFGDFP GATMWNPNTP
260 270 280 290 300
LSEDCLYINV VAPRPRPKNA AVMLWIFGGG FYSGTATLDV YDHRALASEE
310 320 330 340 350
NVIVVSLQYR VASLGFLFLG TPEAPGNAGL FDQNLALRWV RDNIHRFGGD
360 370 380 390 400
PSRVTLFGES AGAVSVSLHL LSALSRDLFQ RAILQSGSPT APWALVSREE
410 420 430 440 450
ATLRALRLAE AVGCPHEPSK LSDAVECLRG KDPHVLVNNE WGTLGICEFP
460 470 480 490 500
FVPVVDGAFL DETPQRSLAS GRFKKTEILT GSNTEEGYYF IIYYLTELLR
510 520 530 540 550
KEEGVTVTRE EFLQAVRELN PYVNGAARQA IVFEYTDWTE PDNPNSNRDA
560 570 580 590 600
LDKMVGDYHF TCNVNEFAQR YAEEGNNVYM YLYTHRSKGN PWPRWTGVMH
610 620 630 640 650
GDEINYVFGE PLNPTLGYTE DEKDFSRKIM RYWSNFAKTG NPNPNTASSE
660 670 680 690 700
FPEWPKHTAH GRHYLELGLN TSFVGRGPRL RQCAFWKKYL PQLVAATSNL
710 720 730
PGPAPPSEPC ESSAFFYRPD LIVLLVSLLT ATVRFIQ
Length:737
Mass (Da):80,902
Last modified:April 3, 2006 - v3
Checksum:iFDE9CCAE34DF2421
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351F → S in CAD56157 (PubMed:12736674).Curated
Sequence conflicti65 – 651A → S in CAD56157 (PubMed:12736674).Curated

Polymorphismi

Strains Kisumu and Kisumu2 are susceptible to insecticides while strain YAO is resistant. Insensitivity to insecticides results from a loss of sensitivity of acetylcholinesterase to organophosphates and carbamates and is due to a variant at position 280.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti127 – 1271V → A in strain: Kisumu2 and YAO.
Natural varianti280 – 2801G → S in strain: YAO; confers resistance to insecticides. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ488492 Genomic DNA. Translation: CAD32684.2.
AJ515149, AJ515148 Genomic DNA. Translation: CAD56156.1.
AJ515150, AJ488492 Genomic DNA. Translation: CAD56157.2.
AAAB01008987 Genomic DNA. Translation: EAA01151.3.
BN000066 Genomic DNA. Translation: CAD29865.2.
RefSeqiXP_321792.2. XM_321792.4.

Genome annotation databases

EnsemblMetazoaiAGAP001356-RA; AGAP001356-PA; AGAP001356.
GeneIDi1281827.
KEGGiaga:AgaP_AGAP001356.
VectorBaseiAGAP001357. Anopheles gambiae.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ488492 Genomic DNA. Translation: CAD32684.2.
AJ515149, AJ515148 Genomic DNA. Translation: CAD56156.1.
AJ515150, AJ488492 Genomic DNA. Translation: CAD56157.2.
AAAB01008987 Genomic DNA. Translation: EAA01151.3.
BN000066 Genomic DNA. Translation: CAD29865.2.
RefSeqiXP_321792.2. XM_321792.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AZGmodel-A115-737[»]
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL2046266.

Protein family/group databases

MEROPSiS09.980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiAGAP001356-RA; AGAP001356-PA; AGAP001356.
GeneIDi1281827.
KEGGiaga:AgaP_AGAP001356.
VectorBaseiAGAP001357. Anopheles gambiae.

Organism-specific databases

CTDi1281827.

Phylogenomic databases

eggNOGiCOG2272.
HOGENOMiHOG000091866.
InParanoidiQ869C3.
KOiK01049.
OMAiGPTRETQ.
OrthoDBiEOG7353WH.
PhylomeDBiQ869C3.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Kisumu, Kisumu2 and YAOImported.
  2. "The genome sequence of the malaria mosquito Anopheles gambiae."
    Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F.
    , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.
    Science 298:129-149(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PEST.
  3. "A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non-homologous to the ace gene in Drosophila."
    Weill M., Fort P., Berthomi eu A., Dubois M.P., Pasteur N., Raymond M.
    Proc. R. Soc. B 269:2007-2016(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL GENE STRUCTURE.

Entry informationi

Entry nameiACES_ANOGA
AccessioniPrimary (citable) accession number: Q869C3
Secondary accession number(s): Q7PUR2
, Q7RTM0, Q86GC7, Q8ISM4, Q8ISM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2003
Last sequence update: April 3, 2006
Last modified: March 31, 2015
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.