The　transient　receptor　potential　cation　channel,　subfamily　A,　member　1　(TRPA1)　is　conserved　between　many　arthropods,　and　in　some　has　been　shown　to　function　as　a　chemosensor　for　noxious　compounds.　Activation　of　arthropod　TRPA1　channels　by　temperature　fluctuations　has　been　tested　in　only　a　few　insect　species,　and　all　of　them　were　shown　to　be　activated　by　heat.　The　recent　identification　of　chemosensitive　TRPA1　channels　from　two　honey　bee　ectoparasitic　mite　species　(VdTRPA1　and　TmTRPA1)　have　provided　an　opportunity　to　study　the　temperature-dependent　activation　and　the　temperature-associated　physiological　functions　of　TRPA1　channels　in　non-insect　arthropods.　We　found　that　both　mite　TRPA1　channels　are　heat　sensitive　and　capable　of　rescuing　the　temperature-related　behavioral　defects　of　a　＜i＞Drosophila　melanogaster　trpA1＜/i＞　mutant.　These　results　suggest　that　heat-sensitivity　of　TRPA1　could　be　conserved　between　many　arthropods　despite　its　amino　acid　sequence　diversity.　Nevertheless,　the　ankyrin　repeats　(ARs)　6　and　7　are　well-conserved　between　six　heat-sensitive　arthropod　TRPA1　channels　and　have　critical　roles　for　the　heat　activation　of　VdTRPA1.