GEPHE SUMMARY Print
Show more ... ular organisms; Eukaryota; Opisthokonta; Metazoa; Eumetazoa; Bilateria; Protostomia; Ecdysozoa; Panarthropoda; Arthropoda; Mandibulata; Pancrustacea; Hexapoda; Insecta; Dicondylia; Pterygota; Neoptera
NCBI Taxonomy ID
is Taxon A an Infraspecies?
dogbane pyralid moth
dogbane pyralid moth; dogbane pyralid
Show more ... da; Insecta; Dicondylia; Pterygota; Neoptera; Holometabola; Amphiesmenoptera; Lepidoptera; Glossata; Neolepidoptera; Heteroneura; Ditrysia; Obtectomera; Pyraloidea; Crambidae; Pyraustinae; Saucrobotys
NCBI Taxonomy ID
is Taxon B an Infraspecies?
Generic Gene Name
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
GO - Molecular Function
GO:0005524 : ATP binding ... show more
GO - Biological Process
GO - Cellular Component
GO:0016021 : integral component of membrane ... show more
SNP Coding Change
Molecular Details of the Mutation
|Taxon A||Taxon B||Position|
Ujvari B; Casewell NR; Sunagar K; Arbuckle K; Wüster W; Lo N; O'Meally D; Beckmann C; et al. ... show more
The question about whether evolution is unpredictable and stochastic or intermittently constrained along predictable pathways is the subject of a fundamental debate in biology, in which understanding convergent evolution plays a central role. At the molecular level, documented examples of convergence are rare and limited to occurring within specific taxonomic groups. Here we provide evidence of constrained convergent molecular evolution across the metazoan tree of life. We show that resistance to toxic cardiac glycosides produced by plants and bufonid toads is mediated by similar molecular changes to the sodium-potassium-pump (Na(+)/K(+)-ATPase) in insects, amphibians, reptiles, and mammals. In toad-feeding reptiles, resistance is conferred by two point mutations that have evolved convergently on four occasions, whereas evidence of a molecular reversal back to the susceptible state in varanid lizards migrating to toad-free areas suggests that toxin resistance is maladaptive in the absence of selection. Importantly, resistance in all taxa is mediated by replacements of 2 of the 12 amino acids comprising the Na(+)/K(+)-ATPase H1-H2 extracellular domain that constitutes a core part of the cardiac glycoside binding site. We provide mechanistic insight into the basis of resistance by showing that these alterations perturb the interaction between the cardiac glycoside bufalin and the Na(+)/K(+)-ATPase. Thus, similar selection pressures have resulted in convergent evolution of the same molecular solution across the breadth of the animal kingdom, demonstrating how a scarcity of possible solutions to a selective challenge can lead to highly predictable evolutionary responses.
44 (ABCA2, BTR1- Cadherin-like protein, Ha_BtR, ABCC2, cadherin, para (kdr), Chitin synthase 1 (CHS1), CYP6BG1, FMO2, MAP4K4, Acetylcholinesterase (Ace-1), resistance to dieldrin, Cpm1, esterase B1, Acetylcholinesterase (Ace-2), alcohol dehydrogenase (Adh), Aldehyde dehydrogenase (Aldh), CG11699, Cyp12d1, Cyp28d1, Cyp28d1-Cyp28d2, cyp6d2, cyp6g1, GSS (glutathione synthetase), GSTE1-E10 cluster, kin of irre (kire), PHGPx, RnrS, SOD1, Ugt86Dd, Acetylcholinesterase (Ace), CYP6D1, esterase isozyme E7 = E3, CYP6AB3, CYP6P9 cluster (CYP6P9a and CYP6P9b), CYP6P9; CYP6P4 cluster, CYP9M10, esterase B1 + esterase A, esterase B1 = esterase beta1, esterase isozyme E3, CHKov1, CYP6B1, CYP6B4, FMO1)
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