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O15547 (P2RX6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·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, P2X6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.7

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed predominantly in skeletal muscle.

Post-translational modification

N-glycosylated. Ref.7

Sequence similarities

Belongs to the P2X receptor family.

Caution

It is uncertain whether Met-1 or Met-11 is the initiator.

Sequence caution

The sequence AAF13303.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAF13303.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

The sequence AAH33488.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAI09210.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA22046.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA22047.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcation transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

muscle contraction

Traceable author statement Ref.1. Source: ProtInc

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from physical interaction PubMed 15313628. Source: BHF-UCL

purinergic nucleotide receptor signaling pathway

Non-traceable author statement PubMed 12088286. Source: GOC

signal transduction

Traceable author statement Ref.1. Source: ProtInc

transmembrane transport

Traceable author statement Ref.1. Source: GOC

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcell junction

Inferred from direct assay PubMed 12088286. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 12088286. Source: BHF-UCL

dendritic spine

Inferred from electronic annotation. Source: Ensembl

integral component of nuclear inner membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Non-traceable author statement PubMed 12088286. Source: BHF-UCL

channel activity

Traceable author statement Ref.1. Source: ProtInc

extracellular ATP-gated cation channel activity

Non-traceable author statement PubMed 12088286. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 15313628. Source: BHF-UCL

purinergic nucleotide receptor activity

Non-traceable author statement PubMed 12088286. Source: BHF-UCL

transmembrane signaling receptor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15547-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O15547-2)

The sequence of this isoform differs from the canonical sequence as follows:
     30-55: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441P2X purinoceptor 6
PRO_0000161557

Regions

Topological domain11 – 3929Cytoplasmic Potential
Transmembrane40 – 6021Helical; Name=1; Potential
Topological domain61 – 333273Extracellular Potential
Transmembrane334 – 35421Helical; Name=2; Potential
Topological domain355 – 44187Cytoplasmic Potential

Amino acid modifications

Modified residue641Phosphotyrosine Ref.6
Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...) Potential
Disulfide bond127 ↔ 177 By similarity
Disulfide bond138 ↔ 161 By similarity
Disulfide bond144 ↔ 171 By similarity
Disulfide bond228 ↔ 238 By similarity
Disulfide bond272 ↔ 281 By similarity

Natural variations

Alternative sequence30 – 5526Missing in isoform 2.
VSP_044799
Natural variant381V → G.
Corresponds to variant rs2006846 [ dbSNP | Ensembl ].
VAR_057664
Natural variant2421R → H. Ref.4
Corresponds to variant rs2277838 [ dbSNP | Ensembl ].
VAR_020338

Experimental info

Sequence conflict3931L → F in AAF13303. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: EFD45BDC81234A64

FASTA44148,829
        10         20         30         40         50         60 
MCPQLAGAGS MGSPGATTGW GLLDYKTEKY VMTRNWRVGA LQRLLQFGIV VYVVGWALLA 

        70         80         90        100        110        120 
KKGYQERDLE PQFSIITKLK GVSVTQIKEL GNRLWDVADF VKPPQGENVF FLVTNFLVTP 

       130        140        150        160        170        180 
AQVQGRCPEH PSVPLANCWV DEDCPEGEGG THSHGVKTGQ CVVFNGTHRT CEIWSWCPVE 

       190        200        210        220        230        240 
SGVVPSRPLL AQAQNFTLFI KNTVTFSKFN FSKSNALETW DPTYFKHCRY EPQFSPYCPV 

       250        260        270        280        290        300 
FRIGDLVAKA GGTFEDLALL GGSVGIRVHW DCDLDTGDSG CWPHYSFQLQ EKSYNFRTAT 

       310        320        330        340        350        360 
HWWEQPGVEA RTLLKLYGIR FDILVTGQAG KFGLIPTAVT LGTGAAWLGV VTFFCDLLLL 

       370        380        390        400        410        420 
YVDREAHFYW RTKYEEAKAP KATANSVWRE LALASQARLA ECLRRSSAPA PTATAAGSQT 

       430        440 
QTPGWPCPSS DTHLPTHSGS L 

« Hide

Isoform 2 [UniParc].

Checksum: 3E32A59741527671
Show »

FASTA41545,808

References

« Hide 'large scale' references
[1]"Cloning of P2XM, a novel human P2X receptor gene regulated by p53."
Urano T., Nishimori H., Han H., Furuhata T., Kimura Y., Nakamura Y., Tokino T.
Cancer Res. 57:3281-3287(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-441 (ISOFORM 1), VARIANT HIS-242.
Tissue: Brain.
[5]"Cloning and tissue distribution of a human cDNA encoding P2X6 purinoceptor."
Cheng X., Jin H., Huang C.-C.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-441 (ISOFORM 1).
Tissue: Skeletal muscle.
[6]"Identification of the phosphotyrosine proteome from thrombin activated platelets."
Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G., Fitzgerald D.J.
Proteomics 2:642-648(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-64.
[7]"Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize."
Barrera N.P., Ormond S.J., Henderson R.M., Murrell-Lagnado R.D., Edwardson J.M.
J. Biol. Chem. 280:10759-10765(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, GLYCOSYLATION.
+Additional computationally mapped references.

Web resources

Wikipedia

P2X receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002059 Genomic DNA. Translation: BAA22047.1. Different initiation.
AB002058 mRNA. Translation: BAA22046.1. Different initiation.
CR456535 mRNA. Translation: CAG30421.1.
AC002472 Genomic DNA. No translation available.
BC033488 mRNA. Translation: AAH33488.1. Different initiation.
BC109209 mRNA. Translation: AAI09210.1. Different initiation.
AF065385 mRNA. Translation: AAF13303.1. Sequence problems.
RefSeqNP_001153026.1. NM_001159554.1.
NP_005437.2. NM_005446.3.
UniGeneHs.113275.

3D structure databases

ProteinModelPortalO15547.
SMRO15547. Positions 41-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114575. 1 interaction.
IntActO15547. 1 interaction.
STRING9606.ENSP00000416193.

Chemistry

BindingDBO15547.
ChEMBLCHEMBL2670.

PTM databases

PhosphoSiteO15547.

Proteomic databases

PaxDbO15547.
PRIDEO15547.

Protocols and materials databases

DNASU9127.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336296; ENSP00000338797; ENSG00000099957.
ENST00000401443; ENSP00000385309; ENSG00000099957. [O15547-2]
ENST00000413302; ENSP00000416193; ENSG00000099957. [O15547-1]
GeneID9127.
KEGGhsa:9127.
UCSCuc010gsu.1. human. [O15547-1]

Organism-specific databases

CTD9127.
GeneCardsGC22P021364.
HGNCHGNC:8538. P2RX6.
HPAHPA028776.
HPA028777.
MIM608077. gene.
neXtProtNX_O15547.
PharmGKBPA162398523.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47843.
HOGENOMHOG000232042.
HOVERGENHBG053086.
InParanoidO15547.
KOK05221.
OMARCPEHPS.
OrthoDBEOG78PV92.
PhylomeDBO15547.
TreeFamTF328633.

Gene expression databases

ArrayExpressO15547.
BgeeO15547.
CleanExHS_P2RX6.
GenevestigatorO15547.

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

GeneWikiP2RX6.
GenomeRNAi9127.
NextBio34213.
PROO15547.
SOURCESearch...

Entry information

Entry nameP2RX6_HUMAN
AccessionPrimary (citable) accession number: O15547
Secondary accession number(s): F6V3D7 expand/collapse secondary AC list , Q32MB6, Q58F04, Q6IC33, Q9UL50
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM