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Q9UBL9 (P2RX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. 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 2

Short name=P2X2
Alternative name(s):
ATP receptor
Purinergic receptor
Gene names
Name:P2RX2
Synonyms:P2X2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ion channel gated by extracellular ATP involved in a variety of cellular responses, such as excitatory postsynaptic responses in sensory neurons, neuromuscular junctions (NMJ) formation, hearing, perception of taste and peristalsis. In the inner ear, regulates sound transduction and auditory neurotransmission, outer hair cell electromotility, inner ear gap junctions, and K+ recycling. Mediates synaptic transmission between neurons and from neurons to smooth muscle. Ref.6

Subunit structure

Homotrimer and heterotrimer; functional P2XRs are organized as homomeric and heteromeric trimers.

Subcellular location

Cell membrane; Multi-pass membrane protein. Note: Localizes to the apical membranes of hair cells in the organ of Corti. Ref.6

Involvement in disease

Deafness, autosomal dominant, 41 (DFNA41) [MIM:608224]: A form of non-syndromic deafness characterized by onset of progressive sensorineural hearing loss usually in the second decade. The hearing loss is severe and ultimately affects all frequencies. Exposure to noise exacerbates the hearing loss, particularly at high frequencies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.7

Sequence similarities

Belongs to the P2X receptor family.

Ontologies

Keywords
   Biological processHearing
Ion transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseDeafness
Disease mutation
Non-syndromic deafness
   DomainTransmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to pain

Inferred from electronic annotation. Source: Ensembl

cation transport

Non-traceable author statement. Source: GOC

detection of hypoxic conditions in blood by carotid body chemoreceptor signaling

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement PubMed 9119082. Source: GOC

neuromuscular junction development

Inferred from electronic annotation. Source: Ensembl

neuromuscular synaptic transmission

Inferred from electronic annotation. Source: Ensembl

neuronal action potential

Inferred from electronic annotation. Source: Ensembl

peristalsis

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion transport into cytosol

Non-traceable author statement PubMed 17895406. Source: BHF-UCL

positive regulation of calcium-mediated signaling

Non-traceable author statement PubMed 17895406. Source: BHF-UCL

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 17895406. Source: GOC

response to ATP

Inferred from electronic annotation. Source: Ensembl

response to carbohydrate

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

sensory perception of taste

Inferred from electronic annotation. Source: Ensembl

skeletal muscle fiber development

Inferred from electronic annotation. Source: Ensembl

urinary bladder smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from electronic annotation. Source: Ensembl

integral component of nuclear inner membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

presynaptic membrane

Inferred from electronic annotation. Source: Ensembl

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Non-traceable author statement PubMed 17895406. Source: BHF-UCL

cadmium ion binding

Inferred from electronic annotation. Source: Ensembl

cobalt ion binding

Inferred from electronic annotation. Source: Ensembl

copper ion binding

Inferred from electronic annotation. Source: Ensembl

drug binding

Inferred from electronic annotation. Source: Ensembl

extracellular ATP-gated cation channel activity

Non-traceable author statement. Source: BHF-UCL

identical protein binding

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

ligand-gated ion channel activity

Traceable author statement PubMed 9119082. Source: ProtInc

mercury ion binding

Inferred from electronic annotation. Source: Ensembl

nickel cation binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol binding

Inferred from electronic annotation. Source: Ensembl

purinergic nucleotide receptor activity

Non-traceable author statement PubMed 17895406. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9UBL9-1)

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 B (identifier: Q9UBL9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     381-447: Missing.
Isoform C (identifier: Q9UBL9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     104-127: Missing.
Isoform D (identifier: Q9UBL9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     354-354: V → VVRNPLWGPSGCGGSTRPLHTGLCWPQ
Isoform H (identifier: Q9UBL9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     36-127: Missing.
Isoform I (identifier: Q9UBL9-6)

The sequence of this isoform differs from the canonical sequence as follows:
     38-152: NRRLGVLYRA...VAGELDMLGN → IHRAEKLPGE...GRGGVREAPR
Isoform K (identifier: Q9UBL9-7)

The sequence of this isoform differs from the canonical sequence as follows:
     104-127: Missing.
     154-258: LRTGRCVPYY...GESFTELAHK → ALQDLRGVRL...ELHRARTQGR
     381-447: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471P2X purinoceptor 2
PRO_0000161549

Regions

Topological domain1 – 4242Cytoplasmic Potential
Transmembrane43 – 6321Helical; Name=1; Potential
Topological domain64 – 337274Extracellular Potential
Transmembrane338 – 35821Helical; Name=2; Potential
Topological domain359 – 471113Cytoplasmic Potential
Region320 – 33314Pore-forming motif Potential

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential
Disulfide bond21 ↔ 439 By similarity
Disulfide bond125 ↔ 176 By similarity
Disulfide bond136 ↔ 159 By similarity
Disulfide bond142 ↔ 170 By similarity
Disulfide bond226 ↔ 236 By similarity
Disulfide bond270 ↔ 279 By similarity

Natural variations

Alternative sequence36 – 12792Missing in isoform H.
VSP_004495
Alternative sequence38 – 152115NRRLG…DMLGN → IHRAEKLPGERDGPRELHHH QGQGDHHVRAQSVGRGGVRE APR in isoform I.
VSP_004496
Alternative sequence104 – 12724Missing in isoform C and isoform K.
VSP_004497
Alternative sequence154 – 258105LRTGR…ELAHK → ALQDLRGVRLVPGGRWGLCQ PISGYDGPKFHHPHQEQHPL PQIPLLQGQHRRPHRRVPEA LHVPRGLRPLLPHLQAGLYR GEGWGELHRARTQGR in isoform K.
VSP_014135
Alternative sequence3541V → VVRNPLWGPSGCGGSTRPLH TGLCWPQ in isoform D.
VSP_004498
Alternative sequence381 – 44767Missing in isoform B and isoform K.
VSP_004499
Natural variant601V → L in DFNA41; found in heterozygous status in patients; abolished ATP-stimulated permeability. Ref.6
VAR_070687
Natural variant3531G → R in DFNA41. Ref.7
VAR_070688

Experimental info

Sequence conflict1 – 1414MAAAQ…AGATA → MV in AAD42947. Ref.3
Sequence conflict1 – 1414MAAAQ…AGATA → MV in AAD42948. Ref.3
Sequence conflict481V → A in AAQ54329. Ref.4

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 84CD61DA136EF420

FASTA47151,754
        10         20         30         40         50         60 
MAAAQPKYPA GATARRLARG CWSALWDYET PKVIVVRNRR LGVLYRAVQL LILLYFVWYV 

        70         80         90        100        110        120 
FIVQKSYQES ETGPESSIIT KVKGITTSEH KVWDVEEYVK PPEGGSVFSI ITRVEATHSQ 

       130        140        150        160        170        180 
TQGTCPESIR VHNATCLSDA DCVAGELDML GNGLRTGRCV PYYQGPSKTC EVFGWCPVED 

       190        200        210        220        230        240 
GASVSQFLGT MAPNFTILIK NSIHYPKFHF SKGNIADRTD GYLKRCTFHE ASDLYCPIFK 

       250        260        270        280        290        300 
LGFIVEKAGE SFTELAHKGG VIGVIINWDC DLDLPASECN PKYSFRRLDP KHVPASSGYN 

       310        320        330        340        350        360 
FRFAKYYKIN GTTTRTLIKA YGIRIDVIVH GQAGKFSLIP TIINLATALT SVGVGSFLCD 

       370        380        390        400        410        420 
WILLTFMNKN KVYSHKKFDK VCTPSHPSGS WPVTLARVLG QAPPEPGHRS EDQHPSPPSG 

       430        440        450        460        470 
QEGQQGAECG PAFPPLRPCP ISAPSEQMVD TPASEPAQAS TPTDPKGLAQ L 

« Hide

Isoform B [UniParc].

Checksum: 695AC6C1655DB952
Show »

FASTA40444,842
Isoform C [UniParc].

Checksum: BAF5513A27314D1D
Show »

FASTA44749,266
Isoform D [UniParc].

Checksum: FC4007F5BDD46E0E
Show »

FASTA49754,513
Isoform H [UniParc].

Checksum: 8D1AA9A069D7F008
Show »

FASTA37941,254
Isoform I [UniParc].

Checksum: 8B55562C9BAEAE5E
Show »

FASTA39943,726
Isoform K [UniParc].

Checksum: 36FC1F15D45624DC
Show »

FASTA37041,370

References

« Hide 'large scale' references
[1]"Molecular and functional characterization of human P2X(2) receptors."
Lynch K.J., Touma E., Niforatos W., Kage K.L., Burgard E.C., van Biesen T., Kowaluk E.A., Jarvis M.F.
Mol. Pharmacol. 56:1171-1181(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A; B; C AND D).
Tissue: Pituitary.
[2]"Cloning of the human P2X2 receptor cDNA and multiple splice variants."
McMahon R.A., Egan T.M., Hurley P.T., Nelson A., Rogers M., Martin F.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
Tissue: Placenta.
[3]"Cloning and molecular characterization of human P2X2 and its splice variants."
Chang T.K., Kosaka A.H., Oglesby I.B., Gever J.R., Lachnit W.G., Ford A.P.D.W., Chang D.J.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C; H AND I).
Tissue: Prostate.
[4]Lin L., Zheng G., Yu R., Li H., Shen C., Zhou G., Zhong G., Li M., Xiao W., Ke R., Yang S.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM K).
[5]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Mutation of the ATP-gated P2X(2) receptor leads to progressive hearing loss and increased susceptibility to noise."
Yan D., Zhu Y., Walsh T., Xie D., Yuan H., Sirmaci A., Fujikawa T., Wong A.C., Loh T.L., Du L., Grati M., Vlajkovic S.M., Blanton S., Ryan A.F., Chen Z.Y., Thorne P.R., Kachar B., Tekin M. expand/collapse author list , Zhao H.B., Housley G.D., King M.C., Liu X.Z.
Proc. Natl. Acad. Sci. U.S.A. 110:2228-2233(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DFNA41 LEU-60, CHARACTERIZATION OF VARIANT DFNA41 LEU-60, FUNCTION, SUBCELLULAR LOCATION.
[7]"A novel P2RX2 mutation in an Italian family affected by autosomal dominant nonsyndromic hearing loss."
Faletra F., Girotto G., D'Adamo A.P., Vozzi D., Morgan A., Gasparini P.
Gene 534:236-239(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DFNA41 ARG-353.
+Additional computationally mapped references.

Web resources

Wikipedia

P2X receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF190822 mRNA. Translation: AAF19170.1.
AF190823 mRNA. Translation: AAF19171.1.
AF190824 mRNA. Translation: AAF19172.1.
AF190825 mRNA. Translation: AAF19173.1.
AF190826 Genomic DNA. Translation: AAF19174.1.
AF109387 mRNA. Translation: AAD42947.1.
AF109388 mRNA. Translation: AAD42948.1.
AF260426 mRNA. Translation: AAF74201.1.
AF260427 mRNA. Translation: AAF74202.1.
AF260428 mRNA. Translation: AAF74203.1.
AF260429 mRNA. Translation: AAF74204.1.
AY346374 mRNA. Translation: AAQ54329.1.
AC131212 Genomic DNA. No translation available.
RefSeqNP_001269093.1. NM_001282164.1.
NP_001269094.1. NM_001282165.1.
NP_036358.2. NM_012226.4.
NP_057402.1. NM_016318.3.
NP_733782.1. NM_170682.3.
NP_733783.1. NM_170683.3.
NP_777361.1. NM_174872.2.
NP_777362.1. NM_174873.2.
UniGeneHs.258580.

3D structure databases

ProteinModelPortalQ9UBL9.
SMRQ9UBL9. Positions 42-364.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ9UBL9.
ChEMBLCHEMBL2531.

PTM databases

PhosphoSiteQ9UBL9.

Polymorphism databases

DMDM12643353.

Proteomic databases

PaxDbQ9UBL9.
PRIDEQ9UBL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343948; ENSP00000343339; ENSG00000187848. [Q9UBL9-4]
ENST00000348800; ENSP00000345095; ENSG00000187848. [Q9UBL9-2]
ENST00000350048; ENSP00000343904; ENSG00000187848. [Q9UBL9-3]
ENST00000351222; ENSP00000344502; ENSG00000187848. [Q9UBL9-5]
ENST00000352418; ENSP00000341419; ENSG00000187848. [Q9UBL9-6]
ENST00000389110; ENSP00000373762; ENSG00000187848. [Q9UBL9-1]
ENST00000449132; ENSP00000405531; ENSG00000187848. [Q9UBL9-7]
GeneID22953.
KEGGhsa:22953.
UCSCuc001uki.1. human. [Q9UBL9-2]
uc001ukj.1. human. [Q9UBL9-1]
uc001ukk.1. human. [Q9UBL9-4]
uc001ukl.1. human. [Q9UBL9-3]
uc001ukm.1. human. [Q9UBL9-6]
uc001ukn.1. human. [Q9UBL9-5]
uc001uko.1. human. [Q9UBL9-7]

Organism-specific databases

CTD22953.
GeneCardsGC12P133195.
HGNCHGNC:15459. P2RX2.
HPAHPA014025.
MIM600844. gene.
608224. phenotype.
neXtProtNX_Q9UBL9.
Orphanet90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
PharmGKBPA32862.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68669.
HOVERGENHBG053086.
KOK05216.
OMALYFVWYV.
PhylomeDBQ9UBL9.
TreeFamTF328633.

Gene expression databases

BgeeQ9UBL9.
GenevestigatorQ9UBL9.

Family and domain databases

Gene3D2.60.490.10. 1 hit.
InterProIPR003045. P2X2_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF4. PTHR10125:SF4. 1 hit.
PfamPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSPR01309. P2X2RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsTIGR00863. P2X. 1 hit.
PROSITEPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiP2RX2.
GenomeRNAi22953.
NextBio43725.
PROQ9UBL9.
SOURCESearch...

Entry information

Entry nameP2RX2_HUMAN
AccessionPrimary (citable) accession number: Q9UBL9
Secondary accession number(s): A6NGB4 expand/collapse secondary AC list , A6NH93, A6NHC2, A6NHU3, A6NIG9, Q6V9R6, Q9NR37, Q9NR38, Q9UHD5, Q9UHD6, Q9UHD7, Q9Y637, Q9Y638
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 117 of the entry and version 1 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 12

Human chromosome 12: entries, gene names and cross-references to MIM