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1.A.7.1.2
ATP-gated cation channel (purinoceptor or ATP-neuroreceptor).  His33 and Ser345 are proximal to each other across an intra-subunit interface, and the relative movement between the two TMSs is likely important for transmitting the action of ATP binding to the opening of the channel (Liang et al. 2013).  Two processes contribute to receptor desensitization, one, bath calcium-independent and the other, bath calcium-dependent, the latter being more important (Coddou et al. 2015).  ATP dissociation causes reduction in outer pore expansion compared to the ATP-bound state. Moreover, the inner and outer ends of adjacent pore-lining helices come closer during opening, likely through a hinge-bending motion (Habermacher et al. 2016).

Accession Number:P49653
Protein Name:P2X2 aka P2RX2
Length:472
Molecular Weight:52617.00
Species:Rattus norvegicus (Rat) [10116]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate cations

Cross database links:

Genevestigator: P49653
DIP: DIP-48329N
RefSeq: NP_446108.2   
Entrez Gene ID: 114115   
Pfam: PF00864   
KEGG: rno:114115   

Gene Ontology

GO:0043197 C:dendritic spine
GO:0016021 C:integral to membrane
GO:0005624 C:membrane fraction
GO:0043025 C:neuronal cell body
GO:0005886 C:plasma membrane
GO:0014069 C:postsynaptic density
GO:0042734 C:presynaptic membrane
GO:0043195 C:terminal button
GO:0005524 F:ATP binding
GO:0046870 F:cadmium ion binding
GO:0050897 F:cobalt ion binding
GO:0005507 F:copper ion binding
GO:0008144 F:drug binding
GO:0004931 F:extracellular ATP-gated cation channel acti...
GO:0042802 F:identical protein binding
GO:0045340 F:mercury ion binding
GO:0016151 F:nickel ion binding
GO:0035091 F:phosphoinositide binding
GO:0004872 F:receptor activity
GO:0008270 F:zinc ion binding
GO:0006811 P:ion transport
GO:0051291 P:protein heterooligomerization
GO:0051260 P:protein homooligomerization
GO:0019228 P:regulation of action potential in neuron

References (4)

[1] “New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor.”  Brake A.J.et.al.   7523952
[2] “Desensitization of the P2X(2) receptor controlled by alternative splicing.”  Braendle U.et.al.   9119082
[3] “Identification of a short form of the P2xR1-purinoceptor subunit produced by alternative splicing in the pituitary and cochlea.”  Housley G.D.et.al.   7542879
[4] “Intracellular disulfide bond that affects ATP responsiveness of P2X(2) receptor/channel.”  Nakazawa K.et.al.   12921863

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MVRRLARGCW SAFWDYETPK VIVVRNRRLG FVHRMVQLLI LLYFVWYVFI VQKSYQDSET 
61:	GPESSIITKV KGITMSEDKV WDVEEYVKPP EGGSVVSIIT RIEVTPSQTL GTCPESMRVH 
121:	SSTCHSDDDC IAGQLDMQGN GIRTGHCVPY YHGDSKTCEV SAWCPVEDGT SDNHFLGKMA 
181:	PNFTILIKNS IHYPKFKFSK GNIASQKSDY LKHCTFDQDS DPYCPIFRLG FIVEKAGENF 
241:	TELAHKGGVI GVIINWNCDL DLSESECNPK YSFRRLDPKY DPASSGYNFR FAKYYKINGT 
301:	TTTRTLIKAY GIRIDVIVHG QAGKFSLIPT IINLATALTS IGVGSFLCDW ILLTFMNKNK 
361:	LYSHKKFDKV RTPKHPSSRW PVTLALVLGQ IPPPPSHYSQ DQPPSPPSGE GPTLGEGAEL 
421:	PLAVQSPRPC SISALTEQVV DTLGQHMGQR PPVPEPSQQD STSTDPKGLA QL