description
Transient receptor potential (TRP) channel proteins were first discovered in Drosophila melanogaster and have many homologues in other species including humans. TRPs form cationic channels that can detect sensory stimuli such as temperature, pH or oxidative stress and transduce that into either electrical (change in membrane potential) or chemical signals (change in intracellular Ca2+ concentration). In humans, there are 28 TRP genes arranged into 6 subfamilies; TRPA, TRPC, TRPM, TRPML, TRPP, and TRPV (Wu et al. 2010). Each TRP channel subunit consists of six putative transmembrane-spanning segments (S1-S6) with a pore-forming loop between S5 and S6. These subunits assemble into tetramers to form functional channels. All functionally characterized TRP channels are permeable to Ca2+ except TRMP4 and 5 which are only permeable to monovalent cations such as Na+ (Latorre et al. 2009). Most TRPs can cause channelopathies which are risk factors for many disease states (Nilius & Owsianik 2010)

external resources
NCBI:1269954
REACTOME:R-HSA-3295583
PUBMED:20716668
PUBMED:20347603
PUBMED:20025796
PUBMED:20127491

genes
TRPM1 , TRPC1 , TRPC3 , TRPC4 , TRPC5 , TRPC6 , TRPM2 , TRPV1 , TRPA1 , TRPC4AP , TRPM5 , TRPV2 , TRPM4 , TRPM7 , MCOLN3 , TRPV6 , TRPV5 , TRPC7 , MCOLN1 , TRPV4 , TRPM8 , TRPM3 , TRPM6 , TRPV3 , MCOLN2 ,