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P51576 (P2RX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P2X purinoceptor 1

Short name=P2X1
Alternative name(s):
ATP receptor
Purinergic receptor
Gene names
Name:P2rx1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

Subunit structure

Homo- or heteropolymers By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the P2X receptor family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399P2X purinoceptor 1
PRO_0000161546

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

Sequences

Sequence LengthMass (Da)Tools
P51576 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8CBF6B97F569472E

FASTA39944,851
        10         20         30         40         50         60 
MARRLQDELS AFFFEYDTPR MVLVRNKKVG VIFRLIQLVV LVYVIGWVFV YEKGYQTSSG 

        70         80         90        100        110        120 
LISSVSVKLK GLAVTQLQGL GPQVWDVADY VFPAHGDSSF VVMTNFIMTP QQAQGHCAEN 

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

       190        200        210        220        230        240 
EAENFTLFIK NSISFPRFKV NRRNLVEEVN GTYMKKCLYH KILHPLCPVF SLGYVVRESG 

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

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

       370        380        390 
HYYKQKKFKY AEDMGPGEGE RDPAATSSTL GLQENMRTS 

« Hide

References

« Hide 'large scale' references
[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: 8834001] [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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Urinary bladder.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84896 mRNA. Translation: CAA59322.1.
AF250123, AF250121, AF250122 Genomic DNA. Translation: AAF68968.1.
AK035304 mRNA. Translation: BAC29024.1.
AL670399 Genomic DNA. Translation: CAI24783.1.
IPIIPI00123864.
RefSeqNP_032797.3. NM_008771.3.
UniGeneMm.25722.

3D structure databases

ProteinModelPortalP51576.
SMRP51576. Positions 30-354.
ModBaseSearch...

Protein-protein interaction databases

STRINGP51576.

PTM databases

PhosphoSiteP51576.

Proteomic databases

PRIDEP51576.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021141; ENSMUSP00000021141; ENSMUSG00000020787.
GeneID18436.
KEGGmmu:18436.

Organism-specific databases

CTD5023.
MGIMGI:1098235. P2rx1.

Phylogenomic databases

eggNOGmaNOG05754.
HOGENOMHBG713324.
HOVERGENHBG053086.
InParanoidP51576.
OMAFNFRFAR.
OrthoDBEOG42FSHT.
PhylomeDBP51576.

Gene expression databases

ArrayExpressP51576.
BgeeP51576.
GenevestigatorP51576.
GermOnlineENSMUSG00000020787. Mus musculus.

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

NextBio294106.
SOURCESearch...

Entry information

Entry nameP2RX1_MOUSE
AccessionPrimary (citable) accession number: P51576
Secondary accession number(s): Q5SRU4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 14, 2011
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families