Transient receptor potential cation channel subfamily V member 5 (IPR008346)

Short name: TRPV5

Overlapping homologous superfamilies


Family relationships


TRP (transient receptor potential) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [PMID: 18535090].

TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies [PMID: 20025796]: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin), whose only member is the transmembrane protein 1, TRPP(polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogenous properties and complex regulation.

TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [PMID: 20861159].

The TRPV (vanilloid) subfamily can be divided into two distinct groups. The first, which comprises TRPV1, TRPV2, TRPV3, and TRPV4, has members which can be activated by temperature as well as chemical stimuli. They are involved in a range of functions including nociception, thermosensing and osmolarity sensing. The second group, which consists of TRPV5 and TRPV6, (also known as epithelial calcium channels 1 and 2) are involved in renal Ca2+ absorption/reabsorption [PMID: 19297520].

TRPV5 was first isolated from rat duodenum using an expression cloning system and, subsequently, from human small intestine [PMID: 10428857]. Its functional role is similar to TRPV6, being involved in response to a reduction in calcium. However, as its tissue distribution differs, the consequences of malfunction are likely to be different. TRPV5 appears to form the Icrac ion channel, which has a pivotal role in maintenance and regulation of calcium. This means that it is implicated in processes as diverse as exocytosis, enzyme regulation, apoptosis and cell proliferation. More specifically, the classic descriptions of Icrac in T-cells predict that antagonists to this channel should be useful in treating inflammatory diseases and in immunomodulation. It is also potentially involved in cell proliferation, and may be linked to human cancer [PMID: 11278579].

GO terms

Biological Process

GO:0006816 calcium ion transport

Molecular Function

GO:0005262 calcium channel activity

Cellular Component

GO:0016021 integral component of membrane

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.