Gene_Locus Report

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Gene_locus Report for: anoga-ACHE1

Anopheles gambiae; A. funestus; A. minimus; A. moucheti; A. nili; A. pseudopunctipennis; A. sacharovi; A. stephensi; A. sundaicus; A. albimanus; Anopheles sinensis; A. vagus; A. melas; A. arabiensis; A. christyi; A. coluzzii; A. epiroticus; A. funestus; A. merus; A. quadriannulatus; A. stephensi A. atroparvu; A. farauti A. maculatus; A. pseudopunctipennis; A. vestitipennis; A. culicifacies; A. minimus; A. dirus acetylchlolinesterase 1

Comment
Partial sequence from this gene found in many other anopheles mosquitos: As the sequences are very close and in order to keep track of comparison of mutations, only one entry in ESTHER groups the sequences of these different strains. The important mutation G119S_anoga-ACHE1 responsible for insecticide resistance was found in most of these species. Aedes albopictus (Forest day mosquito) Q868Q2 AJ438598, Anopheles arabiensis (Mosquito) Q868P7 AJ438603, Anopheles darlingi Q868Q1 AJ438599, Anopheles funestus Q0N3S4_ANOFN Q868P6 AJ438604, Anopheles minimus Q868P9 AJ438601, Anopheles moucheti Q868P8 AJ438602, Anopheles nili Q868P1 AJ438609, Anopheles pseudopunctipennis AJ438605 Q868P5, Anopheles sacharovi Q868P4 AJ438606, Anopheles stephensi (Indo-Pakistan malaria mosquito) Q868P3 AJ438607, Anopheles sundaicus Q868Q0 AJ438600. Weill et al 2004 Q70LH8 Q70LH7 Anopheles albimanus (New world malaria mosquito); Anopheles sinensis; Anopheles vagus; Anopheles melas; nopheles arabiensis; Anopheles christyi; Anopheles coluzzii; Anopheles epiroticus; Anopheles funestus; Anopheles merus; Anopheles quadriannulatus; Anopheles stephensi; Anopheles atroparvu; Anopheles farauti; Anopheles maculatus; Anopheles pseudopunctipennis; Anopheles vestitipennis; Anopheles culicifacies; Anopheles minimus Anopheles dirus


Relationship
Family|ACHE
Block| C
Position in NCBI Life Tree|Anopheles gambiae
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Protostomia: N E > Ecdysozoa: N E > Panarthropoda: N E > Arthropoda: N E > Mandibulata: N E > Pancrustacea: N E > Hexapoda: N E > Insecta: N E > Dicondylia: N E > Pterygota: N E > Neoptera: N E > Holometabola: N E > Diptera: N E > Nematocera: N E > Culicomorpha: N E > Culicoidea: N E > Culicidae: N E > Anophelinae: N E > Anopheles [genus]: N E > Cellia: N E > Pyretophorus: N E > gambiae species complex: N E > Anopheles gambiae: N E
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data


Molecular evidence
Database
1 mutation: anoga-ACHE1
6 structures (e.g. : 5X61, 5YDH, 5YDI... more)
No kinetic





No Substrate
4 inhibitors (e.g. : 6FSD-10, 6FSE-15, Difluoromethyl-ketone-BT7... more)
>3 Genbank links 95 more: AJ488492, AJZ73939, AJ512511
>3 UniProt links 16 more: Q0N3S4, Q869C3, V9QMZ0
2 Ncbi-nid : 19612317, 24938963
2 Ncbi-pid : 21288858, 24938964
>3 Structure links 3 more: 6ARY, 6ARX, 5YDI
>3 UniProt links 49 more: Q869C3, Q868P1, Q868P5
>3 Interpro links 49 more: Q869C3, Q868P1, Q868P5
>3 Prodom links 49 more: Q869C3, Q868P1, Q868P5
>3 Pfam links 49 more: Q869C3, Q868P1, Q868P5
>3 PIRSF links 49 more: Q869C3, Q868P1, Q868P5
>3 SUPERFAM links 49 more: Q869C3, Q868P1, Q868P5
Sequence
Graphical view for this peptide sequence: anoga-ACHE1
Colored MSA for ACHE (raw)
MEIRGLLMGRLRLGRRMVPLGLLGVTALLLILPPSALVQGRHHELNNGAA
IGSHQLSAAAGVGLSSQSAQSGSLASGVMSSVPAAGASSSSSSSLLSSSA
EDDVARITLSKDADAFFTPYIGHGESVRIIDAELGTLEHVHSGATPRRRG
LTRRESNSDANDNDPLVVNTDKGRIRGITVDAPSGKKVDVWLGIPYAQPP
VGPLRFRHPRPAEKWTGVLNTTTPPNSCVQIVDTVFGDFPGATMWNPNTP
LSEDCLYINVVAPRPRPKNAAVMLWIFGGGFYSGTATLDVYDHRALASEE
NVIVVSLQYRVASLGFLFLGTPEAPGNAGLFDQNLALRWVRDNIHRFGGD
PSRVTLFGESAGAVSVSLHLLSALSRDLFQRAILQSGSPTAPWALVSREE
ATLRALRLAEAVGCPHEPSKLSDAVECLRGKDPHVLVNNEWGTLGICEFP
FVPVVDGAFLDETPQRSLASGRFKKTEILTGSNTEEGYYFIIYYLTELLR
KEEGVTVTREEFLQAVRELNPYVNGAARQAIVFEYTDWTEPDNPNSNRDA
LDKMVGDYHFTCNVNEFAQRYAEEGNNVYMYLYTHRSKGNPWPRWTGVMH
GDEINYVFGEPLNPTLGYTEDEKDFSRKIMRYWSNFAKTGNPNPNTASSE
FPEWPKHTAHGRHYLELGLNTSFVGRGPRLRQCAFWKKYLPQLVAATSNL
PGPAPPSEPCESSAFFYRPDLIVLLVSLLTATVRFIQ
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MEIRGLLMGRLRLGRRMVPLGLLGVTALLLILPPSALVQGRHHELNNGAA
IGSHQLSAAAGVGLSSQSAQSGSLASGVMSSVPAAGASSSSSSSLLSSSA
EDDVARITLSKDADAFFTPYIGHGESVRIIDAELGTLEHVHSGATPRRRG
LTRRESNSDANDNDPLVVNTDKGRIRGITVDAPSGKKVDVWLGIPYAQPP
VGPLRFRHPRPAEKWTGVLNTTTPPNSCVQIVDTVFGDFPGATMWNPNTP
LSEDCLYINVVAPRPRPKNAAVMLWIFGGGFYSGTATLDVYDHRALASEE
NVIVVSLQYRVASLGFLFLGTPEAPGNAGLFDQNLALRWVRDNIHRFGGD
PSRVTLFGESAGAVSVSLHLLSALSRDLFQRAILQSGSPTAPWALVSREE
ATLRALRLAEAVGCPHEPSKLSDAVECLRGKDPHVLVNNEWGTLGICEFP
FVPVVDGAFLDETPQRSLASGRFKKTEILTGSNTEEGYYFIIYYLTELLR
KEEGVTVTREEFLQAVRELNPYVNGAARQAIVFEYTDWTEPDNPNSNRDA
LDKMVGDYHFTCNVNEFAQRYAEEGNNVYMYLYTHRSKGNPWPRWTGVMH
GDEINYVFGEPLNPTLGYTEDEKDFSRKIMRYWSNFAKTGNPNPNTASSE
FPEWPKHTAHGRHYLELGLNTSFVGRGPRLRQCAFWKKYLPQLVAATSNL
PGPAPPSEPCESSAFFYRPDLIVLLVSLLTATVRFIQ


References
26 more
    Title: Distribution of acetylcholinesterase (Ace-1(R)) target-site G119S mutation and resistance to carbamates and organophosphates in Anopheles gambiae sensu lato populations from Cameroon
    Binyang AJ, Elanga-Ndille E, Tene-Fossog B, Ndo C, Nouage L, Assatse T, Fotso-Toguem Y, Tabue R, Zeukeng F and Wondji CS <3 more author(s)>
    Ref: Parasit Vectors, 15:53, 2022 : PubMed

            

    Title: Structure of the G119S Mutant Acetylcholinesterase of the Malaria Vector Anopheles gambiae Reveals Basis of Insecticide Resistance
    Cheung J, Mahmood A, Kalathur R, Liu L, Carlier PR
    Ref: Structure, 26:130, 2018 : PubMed

            

    Title: Crystal structure of acetylcholinesterase catalytic subunits of the malaria vector Anopheles gambiae
    Han Q, Wong DM, Robinson H, Ding H, Lam PC, Totrov MM, Carlier PR, Li J
    Ref: Insect Sci, 25:721, 2018 : PubMed

            


Other Papers


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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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