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Reviewed, UniProtKB/Swiss-Prot Q869C3 (ACES_ANOGA)

Last modified November 3, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Acetylcholinesterase
      Short name=AChE
    EC=3.1.1.7
Gene names
Name: Ace
Synonyms: ACE1, ACHE1
ORF Names: AGAP001356
OrganismAnopheles gambiae (African malaria mosquito) [Complete proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

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Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Rapidly hydrolyzes choline released into the synapse.

Catalytic activity

Acetylcholine + H2O = choline + acetate. UniProtKB P22303

Subcellular location

Cell junction › synapse.

Polymorphism

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. Ref.1

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

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Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Synapse
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processneurotransmitter catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetylcholinesterase activity

Inferred from electronic annotation. Source: EC

cholinesterase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 Potential
Chain39 – 737699Acetylcholinesterase
PRO_0000008599

Sites

Active site3601Acyl-ester intermediate By similarity UniProtKB P22303
Active site4861Charge relay system By similarity UniProtKB P22303
Active site6001Charge relay system By similarity UniProtKB P22303

Amino acid modifications

Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation6701N-linked (GlcNAc...) Potential
Disulfide bond228 ↔ 255 By similarity UniProtKB P22303
Disulfide bond414 ↔ 427 By similarity UniProtKB P22303
Disulfide bond562 ↔ 683 By similarity UniProtKB P22303

Natural variations

Natural variant1271V → A in strain: Kisumu2 and YAO. Ref.1
Natural variant2801G → S in strain: YAO; confers resistance to insecticides. Ref.1

Experimental info

Sequence conflict351F → S in CAD56157. Ref.1
Sequence conflict651A → S in CAD56157. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q869C3-1 [UniParc].

Last modified April 4, 2006. Version 3.
Checksum: FDE9CCAE34DF2421

FASTA73780,902
        10         20         30         40         50         60 
MEIRGLLMGR LRLGRRMVPL GLLGVTALLL ILPPFALVQG RHHELNNGAA IGSHQLSAAA 

        70         80         90        100        110        120 
GVGLASQSAQ SGSLASGVMS SVPAAGASSS SSSSLLSSSA EDDVARITLS KDADAFFTPY 

       130        140        150        160        170        180 
IGHGESVRII DAELGTLEHV HSGATPRRRG LTRRESNSDA NDNDPLVVNT DKGRIRGITV 

       190        200        210        220        230        240 
DAPSGKKVDV WLGIPYAQPP VGPLRFRHPR PAEKWTGVLN TTTPPNSCVQ IVDTVFGDFP 

       250        260        270        280        290        300 
GATMWNPNTP LSEDCLYINV VAPRPRPKNA AVMLWIFGGG FYSGTATLDV YDHRALASEE 

       310        320        330        340        350        360 
NVIVVSLQYR VASLGFLFLG TPEAPGNAGL FDQNLALRWV RDNIHRFGGD PSRVTLFGES 

       370        380        390        400        410        420 
AGAVSVSLHL LSALSRDLFQ RAILQSGSPT APWALVSREE ATLRALRLAE AVGCPHEPSK 

       430        440        450        460        470        480 
LSDAVECLRG KDPHVLVNNE WGTLGICEFP FVPVVDGAFL DETPQRSLAS GRFKKTEILT 

       490        500        510        520        530        540 
GSNTEEGYYF IIYYLTELLR KEEGVTVTRE EFLQAVRELN PYVNGAARQA IVFEYTDWTE 

       550        560        570        580        590        600 
PDNPNSNRDA LDKMVGDYHF TCNVNEFAQR YAEEGNNVYM YLYTHRSKGN PWPRWTGVMH 

       610        620        630        640        650        660 
GDEINYVFGE PLNPTLGYTE DEKDFSRKIM RYWSNFAKTG NPNPNTASSE FPEWPKHTAH 

       670        680        690        700        710        720 
GRHYLELGLN TSFVGRGPRL RQCAFWKKYL PQLVAATSNL PGPAPPSEPC ESSAFFYRPD 

       730 
LIVLLVSLLT ATVRFIQ

« Hide

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References

« Hide 'large scale' references
[1]"Insecticide resistance in mosquito vectors."
Weill M., Lutfalla G., Mogensen K., Chandre F., Berthomieu A., Berticat C., Pasteur N., Philips A., Fort P., Raymond M.
Nature 423:136-137(2003) [PubMed: 12736674] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Kisumu, Kisumu2 and YAO.
[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. expand/collapse author list , 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(2002) [PubMed: 12364791] [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(2002) [PubMed: 12396499] [Abstract]
Cited for: PARTIAL GENE STRUCTURE.

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Cross-references

Sequence databases

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.
RefSeqXP_321792.2.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2AZGmodel-A115-737[»]
ModBaseSearch...

Protein family/group databases

MEROPSS09.979.

Genome annotation databases

EnsemblAGAP001356-RA; AGAP001356-PA; AGAP001356; Anopheles gambiae. [Genome view]
GeneID1281827.
KEGGaga:AgaP_AGAP001356.
VectorBaseAGAP001357. Anopheles gambiae.

Organism-specific databases

CTD1281827.

Phylogenomic databases

HOGENOMQ869C3.
OMAGICEFPF.

Enzyme and pathway databases

BRENDA3.1.1.7. 165157.

Family and domain databases

InterProIPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PANTHERPTHR11559. CarbesteraseB. 1 hit.
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameACES_ANOGA
AccessionPrimary (citable) accession number: Q869C3
Secondary accession number(s): Q7PUR2 expand/collapse secondary AC list , Q7RTM0, Q86GC7, Q8ISM4, Q8ISM7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: April 4, 2006
Last modified: November 3, 2009
This is version 57 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents