{PDOC00932}
{PS01212; P2X_RECEPTOR}
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* ATP P2X receptors signature *
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P2X purinoreceptors  [1,2]  are  cation-selective  ion  channels  that open on
binding to  extracellular  ATP; they play a role in fast synaptic transmission
between neurones,  and  from  autonomic  nerves to smooth muscles. When ATP is
released as  a  neurotransmitter from central and peripheral nerves it acts at
P2X receptors to produce postsynaptic depolarization and excitation.

P2X receptors  are  from  397 to 595 amino acids long. They consist of a short
intracellular N-terminus  region  followed  by a transmembrane domain, a large
extracellular loop   that   contains   10   conserved   cysteines,   a  second
transmembrane segment and a C-terminal intracellular tail.

Currently, seven forms (P2X1 to P2X7) of P2X receptors are known.

As a  signature pattern, we selected a conserved region located in the central
part of  the  extracellular  domain  and  which  contains two of the conserved
cysteines.

-Consensus pattern: G-G-x-[LIVM]-G-[LIVM]-x-[IV]-x-W-x-C-[DN]-L-D-x(5)-C-x-P-
                    x-Y-x-F
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 1997 / First entry.

[ 1] Surprenant A., Buell G.N., North R.A.
     "P2X receptors bring new structure to ligand-gated ion channels."
     Trends Neurosci. 18:224-229(1995).
     PubMed=7541920
[ 2] Kennedy C., Leff P.
     "How should P2X purinoceptors be classified pharmacologically?"
     Trends Pharmacol. Sci. 16:168-174(1995).
     PubMed=7624972

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