The transient receptor potential cation channel subfamily V member 1 (TRPV1), also known as the capsaicin receptor and the vanilloid receptor 1, is a protein that, in humans, is encoded by the TRPV1gene. It was the first isolated member of the transient receptor potential vanilloid receptor proteins that in turn are a sub-family of the transient receptor potential protein group.[5][6] This protein is a member of the TRPV group of transient receptor potential family of ion channels.[7]Fatty acidmetabolites with affinity for this receptor are produced by cyanobacteria, which diverged from eukaryotes at least 2000 million years ago (MYA).[8]
The function of TRPV1 is detection and regulation of body temperature. In addition, TRPV1 provides a sensation of scalding heat and pain (nociception). In primary afferent sensory neurons, it cooperates with TRPA1[9][10] (a chemical irritant receptor) to mediate the detection of noxious environmental stimuli.[11]
^Xue Q, Yu Y, Trilk SL, Jong BE, Schumacher MA (August 2001). "The genomic organization of the gene encoding the vanilloid receptor: evidence for multiple splice variants". Genomics. 76 (1–3): 14–20. doi:10.1006/geno.2001.6582. PMID11549313.
^Clapham DE, Julius D, Montell C, Schultz G (December 2005). "International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels". Pharmacological Reviews. 57 (4): 427–450. doi:10.1124/pr.57.4.6. PMID16382100. S2CID17936350.