Family

P2X5 purinoceptor (IPR003048)

Short name: P2X5_purnocptor

Family relationships

Description

P2X purinoceptors are cell membrane ion channels, gated by adenosine 5'-triphosphate (ATP) and other nucleotides; they have been found to be widely expressed on mammalian cells, and, by means of their functional properties, can be differentiated into three sub-groups. The first group is almost equally well activated by ATP and its analogue alpha,betamethylene-ATP, whereas, the second group is not activated by the latter compound. A third type of receptor (also called P2Z) is distinguished by the fact that repeated or prolonged agonist application leads to the opening of much larger pores, allowing large molecules to traverse the cell membrane. This increased permeability rapidly leads to cell death, and lysis.

Molecular cloning studies have identified seven P2X receptor subtypes, designated P2X1-P2X7. These receptors are proteins that share 35-48% amino acid identity, and possess two putative transmembrane (TM) domains, separated by a long (~270 residues) intervening sequence, which is thought to form an extracellular loop. Around 1/4 of the residues within the loop are invariant between the cloned subtypes, including 10 characteristic cysteines.

Studies of the functional properties of heterologously expressed P2X receptors, together with the examination of their distribution in native tissues, suggests they likely occur as both homo- and heteromultimers in vivo [PMID: 10414359, PMID: 12270951].

The P2X5 receptor (along with P2X2, P2X4 and P2X6) falls into a group of receptors that are sensitive to ATP, but not alphabetamethyleneATP. Splice variants of P2X5 have been detected [PMID: 10414359].

GO terms

Biological Process

GO:0006811 ion transport

Molecular Function

GO:0005524 ATP binding
GO:0005216 ion channel activity
GO:0001614 purinergic nucleotide receptor activity

Cellular Component

GO:0016020 membrane

Contributing signatures

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