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The vanilloid receptor VR1 is an ion channel predominantly expressed by primary sensory neurons involved in nociception. Here we describe its biochemical properties and assess the subcellular localization, the glycosylation state and the quaternary structure of VR1 expressed in HEK293 cells and in the DRG‐derived cell line F‐11 (N18TG2 mouse neuroblastoma × rat dorsal root ganglia, hybridoma). VR1 was found to be glycosylated in both cell types. Of the five potential N‐glycosylation sites, the predicted transient receptor potential channel‐like transmembrane folding proposes N604 is localized extracellularly. We used site‐directed mutagenesis to mutate the Asn at position 604 to Thr. This mutated VR1 was not glycosylated, confirming the extracellular location of N604 and its role as the exclusive site of glycosylation of the VR1 protein. VR1 occured in high molecular mass complexes as assessed by blue …