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P47824 (P2RX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
P2X purinoceptor 1

Short name=P2X1
Alternative name(s):
ATP receptor
Purinergic receptor
RP-2 protein
Gene names
Name:P2rx1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death.

Subunit structure

Homo- or heteropolymers.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

High levels in vas deferens and urinary bladder. Lower extent in spinal cord, coeliac ganglion, lung and spleen (probably in the smooth muscle part of both organs).

Developmental stage

Expressed during apoptosis in thymocytes.

Induction

By irradiation and dexamethasone (in thymocytes).

Sequence similarities

Belongs to the P2X receptor family.

Ontologies

Keywords
   Biological processApoptosis
Ion transport
Transport
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionIonic channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein heterooligomerization

Inferred from direct assay. Source: RGD

protein homooligomerization

Inferred from direct assay. Source: RGD

regulation of action potential in neuron

Inferred from direct assay. Source: RGD

regulation of blood pressure

Inferred from mutant phenotype. Source: RGD

synaptic transmission, glutamatergic

Inferred from mutant phenotype. Source: RGD

vasoconstriction

Inferred from mutant phenotype. Source: RGD

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane raft

Inferred from direct assay. Source: RGD

plasma membrane

Inferred from direct assay. Source: RGD

protein complex

Inferred from direct assay. Source: RGD

synaptosome

Inferred from direct assay. Source: RGD

   Molecular functionATP binding

Inferred from direct assay. Source: RGD

drug binding

Inferred from direct assay. Source: RGD

extracellular ATP-gated cation channel activity

Inferred from direct assay. Source: RGD

protein binding

Inferred from physical interaction. Source: RGD

purinergic nucleotide receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

zinc ion binding

Inferred from direct assay. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399P2X purinoceptor 1
PRO_0000161547

Regions

Topological domain1 – 2828Cytoplasmic Potential
Transmembrane29 – 5022Helical; Name=1; Potential
Topological domain51 – 338288Extracellular Potential
Transmembrane339 – 35820Helical; Name=2; Potential
Topological domain359 – 39941Cytoplasmic Potential
Region331 – 3388Pore-forming motif Potential
Compositional bias351 – 3544Poly-Leu

Amino acid modifications

Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Disulfide bond117 ↔ 165 By similarity
Disulfide bond126 ↔ 149 By similarity
Disulfide bond132 ↔ 159 By similarity
Disulfide bond217 ↔ 227 By similarity
Disulfide bond261 ↔ 270 By similarity

Experimental info

Sequence conflict189 – 20113IKNSI…RFKVN → PQLAHGCYPCPPH Ref.3

Sequences

Sequence LengthMass (Da)Tools
P47824 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 04B79E171D78AEC2

FASTA39944,957
        10         20         30         40         50         60 
MARRLQDELS AFFFEYDTPR MVLVRNKKVG VIFRLIQLVV LVYVIGWVFV YEKGYQTSSD 

        70         80         90        100        110        120 
LISSVSVKLK GLAVTQLQGL GPQVWDVADY VFPAHGDSSF VVMTNFIVTP QQTQGHCAEN 

       130        140        150        160        170        180 
PEGGICQDDS GCTPGKAERK AQGIRTGNCV PFNGTVKTCE IFGWCPVEVD DKIPSPALLR 

       190        200        210        220        230        240 
EAENFTLFIK NSISFPRFKV NRRNLVEEVN GTYMKKCLYH KIQHPLCPVF NLGYVVRESG 

       250        260        270        280        290        300 
QDFRSLAEKG GVVGITIDWK CDLDWHVRHC KPIYQFHGLY GEKNLSPGFN FRFARHFVQN 

       310        320        330        340        350        360 
GTNRRHLFKV FGIHFDILVD GKAGKFDIIP TMTTIGSGIG IFGVATVLCD LLLLHILPKR 

       370        380        390 
HYYKQKKFKY AEDMGPGEGE HDPVATSSTL GLQENMRTS 

« Hide

References

« Hide 'large scale' references
[1]"A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP."
Valera S., Hussy N., Evans R.J., Adami N., North R.A., Surprenant A., Buell G.N.
Nature 371:516-519(1994) [PubMed: 7523951] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Vas deferens.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[3]"Identification of mRNAs associated with programmed cell death in immature thymocytes."
Owens G.P., Hahn W.E., Cohen J.J.
Mol. Cell. Biol. 11:4177-4188(1991) [PubMed: 2072913] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-399.
Strain: Sprague-Dawley.
Tissue: Thymus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80477 mRNA. Translation: CAA56647.1.
BC061742 mRNA. Translation: AAH61742.1.
M80602 mRNA. Translation: AAA42065.1.
IPIIPI00190984.
PIRS50860.
RefSeqNP_037129.1. NM_012997.2.
UniGeneRn.91176.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP47824.

Protein family/group databases

TCDB1.A.7.1.1. ATP-gated P2X receptor cation channel (P2X Receptor) family.

PTM databases

PhosphoSiteP47824.

Proteomic databases

PRIDEP47824.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25505.
KEGGrno:25505.
UCSCNM_012997. rat.

Organism-specific databases

CTD5023.
RGD3240. P2rx1.

Phylogenomic databases

eggNOGmaNOG05754.
GeneTreeENSGT00390000016028.
HOVERGENHBG053086.
InParanoidP47824.
OrthoDBEOG42FSHT.

Gene expression databases

ArrayExpressP47824.
GenevestigatorP47824.
GermOnlineENSRNOG00000017606. Rattus norvegicus.

Family and domain databases

InterProIPR003044. P2X1_purnocptor.
IPR001429. P2X_purnocptor.
[Graphical view]
KOK05215.
PANTHERPTHR10125. ATP_P2X_rcpt. 1 hit.
PTHR10125:SF9. PTHR10125:SF9. 1 hit.
PfamPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSPR01308. P2X1RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsTIGR00863. P2X. 1 hit.
PROSITEPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio606921.

Entry information

Entry nameP2RX1_RAT
AccessionPrimary (citable) accession number: P47824
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 14, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families