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Protein

P2X purinoceptor 1

Gene

P2rx1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

  • ATP binding Source: Ensembl
  • cation channel activity Source: MGI
  • drug binding Source: Ensembl
  • extracellular ATP-gated cation channel activity Source: GO_Central
  • purinergic nucleotide receptor activity Source: MGI
  • zinc ion binding Source: Ensembl

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • ceramide biosynthetic process Source: MGI
  • insemination Source: MGI
  • ion transport Source: MGI
  • neuronal action potential Source: Ensembl
  • platelet activation Source: MGI
  • positive regulation of ion transport Source: MGI
  • protein heterooligomerization Source: Ensembl
  • protein homooligomerization Source: Ensembl
  • purinergic nucleotide receptor signaling pathway Source: MGI
  • regulation of blood pressure Source: Ensembl
  • regulation of calcium ion transport Source: MGI
  • regulation of smooth muscle contraction Source: MGI
  • regulation of vascular smooth muscle contraction Source: MGI
  • regulation of vasoconstriction Source: MGI
  • response to ATP Source: MGI
  • response to organic substance Source: MGI
  • serotonin secretion by platelet Source: MGI
  • synaptic transmission, glutamatergic Source: Ensembl
  • vasoconstriction Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Apoptosis, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-139853. Elevation of cytosolic Ca2+ levels.
R-MMU-418346. Platelet homeostasis.

Names & Taxonomyi

Protein namesi
Recommended name:
P2X purinoceptor 1
Short name:
P2X1
Alternative name(s):
ATP receptor
Purinergic receptor
Gene namesi
Name:P2rx1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1098235. P2rx1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2828CytoplasmicSequence analysisAdd
BLAST
Transmembranei29 – 5022Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini51 – 338288ExtracellularSequence analysisAdd
BLAST
Transmembranei339 – 35820Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini359 – 39941CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5496.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399P2X purinoceptor 1PRO_0000161546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi117 ↔ 165By similarity
Disulfide bondi126 ↔ 149By similarity
Disulfide bondi132 ↔ 159By similarity
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence analysis
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi217 ↔ 227By similarity
Disulfide bondi261 ↔ 270By similarity
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence analysis
Modified residuei387 – 3871PhosphoserineBy similarity
Modified residuei388 – 3881PhosphoserineBy similarity
Modified residuei389 – 3891PhosphothreonineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP51576.
PaxDbiP51576.
PRIDEiP51576.

PTM databases

PhosphoSiteiP51576.

Expressioni

Gene expression databases

BgeeiP51576.
ExpressionAtlasiP51576. baseline and differential.
GenevisibleiP51576. MM.

Interactioni

Subunit structurei

Homo- or heteropolymers.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021141.

Chemistry

BindingDBiP51576.

Structurei

3D structure databases

ProteinModelPortaliP51576.
SMRiP51576. Positions 34-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni331 – 3388Pore-forming motifSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi351 – 3544Poly-Leu

Sequence similaritiesi

Belongs to the P2X receptor family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFJF. Eukaryota.
ENOG410XR0C. LUCA.
GeneTreeiENSGT00390000016028.
HOGENOMiHOG000232042.
HOVERGENiHBG053086.
InParanoidiP51576.
KOiK05215.
OMAiFKYAEDM.
OrthoDBiEOG78PV92.
PhylomeDBiP51576.
TreeFamiTF328633.

Family and domain databases

Gene3Di2.60.490.10. 1 hit.
InterProiIPR003044. P2X1_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERiPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF9. PTHR10125:SF9. 1 hit.
PfamiPF00864. P2X_receptor. 1 hit.
[Graphical view]
PIRSFiPIRSF005713. P2X_purinoceptor. 1 hit.
PRINTSiPR01308. P2X1RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsiTIGR00863. P2X. 1 hit.
PROSITEiPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51576-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARRLQDELS AFFFEYDTPR MVLVRNKKVG VIFRLIQLVV LVYVIGWVFV
60 70 80 90 100
YEKGYQTSSG LISSVSVKLK GLAVTQLQGL GPQVWDVADY VFPAHGDSSF
110 120 130 140 150
VVMTNFIMTP QQAQGHCAEN PEGGICQDDS GCTPGKAERK AQGIRTGNCV
160 170 180 190 200
PFNGTVKTCE IFGWCPVEVD DKIPSPALLH EAENFTLFIK NSISFPRFKV
210 220 230 240 250
NRRNLVEEVN GTYMKKCLYH KILHPLCPVF SLGYVVRESG QDFRSLAEKG
260 270 280 290 300
GVVGITIDWE CDLDWHVRHC KPIYQFHGLY GEKNLSPGFN FRFARHFVQN
310 320 330 340 350
GTNRRHLFKV FGIRFDILVD GKAGKFDIIP TMTTIGSGIG IFGVATVLCD
360 370 380 390
LLLLHILPKR HYYKQKKFKY AEDMGPGEGE RDPAATSSTL GLQENMRTS
Length:399
Mass (Da):44,851
Last modified:October 1, 1996 - v1
Checksum:i8CBF6B97F569472E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84896 mRNA. Translation: CAA59322.1.
AF250123, AF250121, AF250122 Genomic DNA. Translation: AAF68968.1.
AK035304 mRNA. Translation: BAC29024.1.
AL670399 Genomic DNA. Translation: CAI24783.1.
CCDSiCCDS24992.1.
RefSeqiNP_032797.3. NM_008771.3.
UniGeneiMm.25722.

Genome annotation databases

EnsembliENSMUST00000021141; ENSMUSP00000021141; ENSMUSG00000020787.
GeneIDi18436.
KEGGimmu:18436.
UCSCiuc007jzq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84896 mRNA. Translation: CAA59322.1.
AF250123, AF250121, AF250122 Genomic DNA. Translation: AAF68968.1.
AK035304 mRNA. Translation: BAC29024.1.
AL670399 Genomic DNA. Translation: CAI24783.1.
CCDSiCCDS24992.1.
RefSeqiNP_032797.3. NM_008771.3.
UniGeneiMm.25722.

3D structure databases

ProteinModelPortaliP51576.
SMRiP51576. Positions 34-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021141.

Chemistry

BindingDBiP51576.
ChEMBLiCHEMBL5496.

PTM databases

PhosphoSiteiP51576.

Proteomic databases

MaxQBiP51576.
PaxDbiP51576.
PRIDEiP51576.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021141; ENSMUSP00000021141; ENSMUSG00000020787.
GeneIDi18436.
KEGGimmu:18436.
UCSCiuc007jzq.2. mouse.

Organism-specific databases

CTDi5023.
MGIiMGI:1098235. P2rx1.

Phylogenomic databases

eggNOGiENOG410IFJF. Eukaryota.
ENOG410XR0C. LUCA.
GeneTreeiENSGT00390000016028.
HOGENOMiHOG000232042.
HOVERGENiHBG053086.
InParanoidiP51576.
KOiK05215.
OMAiFKYAEDM.
OrthoDBiEOG78PV92.
PhylomeDBiP51576.
TreeFamiTF328633.

Enzyme and pathway databases

ReactomeiR-MMU-139853. Elevation of cytosolic Ca2+ levels.
R-MMU-418346. Platelet homeostasis.

Miscellaneous databases

PROiP51576.
SOURCEiSearch...

Gene expression databases

BgeeiP51576.
ExpressionAtlasiP51576. baseline and differential.
GenevisibleiP51576. MM.

Family and domain databases

Gene3Di2.60.490.10. 1 hit.
InterProiIPR003044. P2X1_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERiPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF9. PTHR10125:SF9. 1 hit.
PfamiPF00864. P2X_receptor. 1 hit.
[Graphical view]
PIRSFiPIRSF005713. P2X_purinoceptor. 1 hit.
PRINTSiPR01308. P2X1RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsiTIGR00863. P2X. 1 hit.
PROSITEiPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and chromosomal localization of a human P2X receptor from the urinary bladder."
    Valera S., Talabot F., Evans R.J., Gos A., Antonarakis S.E., Morris M.A., Buell G.N.
    Recept. Channels 3:283-289(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: OF1.
    Tissue: Urinary bladder smooth muscle.
  2. "Mouse P2X1 purinergic receptor gene structure."
    Yu X.-M., Connolly A.J.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Urinary bladder.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiP2RX1_MOUSE
AccessioniPrimary (citable) accession number: P51576
Secondary accession number(s): Q5SRU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.