Wang,J., Han,Z. and Wang,Y. Cloning and sequencing of an acetylcholinesterase gene from the diamondback moth, Plutella xylostella L. two sequences differing by C-term length Ni X.-Y., Tomita T., Kasai S., Kono Y. AY061975 and AY032625
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Protostomia: NE > Ecdysozoa: NE > Panarthropoda: NE > Arthropoda: NE > Mandibulata: NE > Pancrustacea: NE > Hexapoda: NE > Insecta: NE > Dicondylia: NE > Pterygota: NE > Neoptera: NE > Holometabola: NE > Amphiesmenoptera: NE > Lepidoptera: NE > Glossata: NE > Neolepidoptera: NE > Heteroneura: NE > Ditrysia: NE > Yponomeutoidea: NE > Plutellidae: NE > Plutella: NE > Plutella xylostella: NE
LegendThis 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 MIYNSKIVFTKLLLCICVCGARGRSWANHHDTTTSTTPAPTTTTPAPKNF HNDPLIVETKSGLVKGYAKTVMGREVHIFTGIPFAKPPLGPLRFRKPVPI EPWHGVLEATAMPNSCYQERYEYFPGFEGEEMWNPNTNISEDCLYLNIWV PQHLRVRHHQDKPLTERPKVPILVWIYGGGYMSGTATLDLYKADIMASSS DVIVASMQYRVGAFGFLYLNKYFSPGSEEAAGNMGLWDQQLAIRWIKDNA RAFGGDPELITLFGESAGGGSVSLHMLSPEMKGLFKRGILQSGTLNAPWS WMTGERAQDIGKVLVDDCNCNSSLLAVDPSLVMDCMRGVDAKTISVQQWN SYTGILGFPSAPTVDGVFLPKDPDTMMKEGSFHNTEVLLGSNQDEGTYFL LYDFLDYFEKDGPSFLQREKFLEIVDTIFKEFSKIKREAIVFQYTDWEEI TDGYLNQKMIADIVGDYFFVCPTNYFAEVLADSGVDVYYYYFTHRTSTSL WGEWMGVMHGDEMEYVFGHPLNMSLQYHTRERDLAAHIMQSFTRFALTGK PHKPEEKWPVYSRASPHYYTYSADAASGPAPPRGPRASACAFWNHFLNKL NELEHVPCDGAVTGPYSSMAGKSLPIVLLTALATTAAL
References
Title: Mutations of acetylcholinesterase1 contribute to prothiofos-resistance in Plutella xylostella (L.) Lee DW, Choi JY, Kim WT, Je YH, Song JT, Chung BK, Boo KS, Koh YH Ref: Biochemical & Biophysical Research Communications, 353:591, 2007 : PubMed
Insensitive acetylcholinesterase (AChE) is involved in the resistance of organophosphorous and carbamate insecticides. We cloned a novel full-length AChE cDNA encoding ace1 gene from adult heads of the diamondback moth (DBM, Plutella xylostella). The ace1 gene encoding 679 amino acids has conserved motifs including catalytic triad, choline-binding site and acyl pocket. Northern blot analysis revealed that the ace1 gene was expressed much higher than the ace2 in all examined body parts. The biochemical properties of expressed AChEs showed substrate specificity for acetylthiocholine iodide and inhibitor specificity for BW284C51 and eserine. Three mutations of AChE1 (D229G, A298S, and G324A) were identified in the prothiofos-resistant strain, two of which (A298S and G324A) were expected to be involved in the prothiofos-resistance through three-dimensional modeling. In vitro functional expression of AChEs in Sf9 cells revealed that only resistant AChE1 is less inhibited with paraoxon, suggesting that resistant AChE1 is responsible for prothiofos-resistance.
Title: cDNA and deduced proteine sequence of acetylcholinesterase from the diamond back moth Plutella xylostella (L.) (Lepidoptera: Plutellidae) Ni XY, Tomita T, Kasai S, Kono Y Ref: Appl Entomol Zool, 38:49, 2003 : PubMed
