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O54803 (P2RX6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 6
Short name=P2X6
Alternative name(s):
ATP receptor
P2XM
Purinergic receptor
Purinergic receptor P2X-like 1
Gene names
Name:P2rx6
Synonyms:P2rxl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Receptor for ATP that acts as a ligand-gated ion channel By similarity.

Subunit structure

Unlike most P2XRs, P2RX6 does not seem to form homotrimers or heterotrimers By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Predominantly expressed in skeletal muscle. Also expressed in lung.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the P2X receptor family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379P2X purinoceptor 6
PRO_0000161558

Regions

Topological domain1 – 3131Cytoplasmic Potential
Transmembrane32 – 5221Helical; Name=1; Potential
Topological domain53 – 325273Extracellular Potential
Transmembrane326 – 34621Helical; Name=2; Potential
Topological domain347 – 37933Cytoplasmic Potential

Amino acid modifications

Modified residue561Phosphotyrosine By similarity
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Disulfide bond119 ↔ 169 By similarity
Disulfide bond130 ↔ 153 By similarity
Disulfide bond136 ↔ 163 By similarity
Disulfide bond220 ↔ 230 By similarity
Disulfide bond264 ↔ 273 By similarity

Experimental info

Sequence conflict2591S → T in BAA24693. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O54803 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 1C3CF265934134E5

FASTA37942,101
        10         20         30         40         50         60 
MASAAAAALV SWGFLDYKTE KYVLTRNCRV GVSQRLLQLA VVVYVIGWAL LAKKGYQERD 

        70         80         90        100        110        120 
LAPQTSVITK LKGVSVTQVK ELENRLWDVA DFVKPSQGEN VFFLVTNFLV TPAQVQGRCP 

       130        140        150        160        170        180 
EHPSVPLANC WADEDCPEGE TGTYSHGIKT GQCVVFNGTH RTCEIWSWCP VESGAVPRKP 

       190        200        210        220        230        240 
LLAQAKNFTL FIKNTVTFSK FNFSRSNALL TWDNTYFKHC LYDPLSSPYC PVFRIGDLVA 

       250        260        270        280        290        300 
MAGGDFEDLA LLGGAVGISI HWDCNLDTKG SDCCPQYSFQ LQQKGYNFRT ANHWWAASGV 

       310        320        330        340        350        360 
ETRSLLKLYG IRFDILVTGQ AGKFALIPTA ITVGTGAAWL GMVTFLCDLL LLYVDREAGF 

       370 
YWRTKYEEAR APKTTTNSS

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the murine P2XM receptor gene."
Nawa G., Urano T., Tokino T., Ochi T., Miyoshi Y.
J. Hum. Genet. 43:262-267(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB010883 mRNA. Translation: BAA24693.1.
AK138541 mRNA. Translation: BAE23697.1.
IPIIPI00974951.
RefSeqNP_001153033.1. NM_001159561.1.
NP_035158.2. NM_011028.2.
UniGeneMm.8032.

3D structure databases

ProteinModelPortalO54803.
SMRO54803. Positions 35-352.
ModBaseSearch...

PTM databases

PhosphoSiteO54803.

Proteomic databases

PRIDEO54803.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID18440.
KEGGmmu:18440.

Organism-specific databases

CTD9127.
MGIMGI:1337113. P2rx6.

Phylogenomic databases

eggNOGNOG47843.
HOGENOMHOG000232042.
HOVERGENHBG053086.
InParanoidQ3UUD0.
KOK05221.

Gene expression databases

ArrayExpressO54803.
BgeeO54803.
GenevestigatorO54803.
GermOnlineENSMUSG00000022758. Mus musculus.

Family and domain databases

Gene3D2.60.490.10. 1 hit.
InterProIPR003049. P2X6_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF10. PTHR10125:SF10. 1 hit.
PfamPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSPR01313. P2X6RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsTIGR00863. P2X. 1 hit.
PROSITEPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294124.
SOURCESearch...

Entry information

Entry nameP2RX6_MOUSE
AccessionPrimary (citable) accession number: O54803
Secondary accession number(s): Q3UUD0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 91 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents