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P51582 (P2RY4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
P2Y purinoceptor 4

Short name=P2Y4
Alternative name(s):
P2P
Uridine nucleotide receptor
Short name=UNR
Gene names
Name:P2RY4
Synonyms:NRU
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for UTP and UDP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. Not activated by ATP or ADP.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Pancreas.

Post-translational modification

Phosphorylation of Ser-333 and Ser-334 is a key step in agonist-dependent desensitization and loss of surface P2RY4. This phosphorylation does not involve PKC, nor other calcium activated kinases.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365P2Y purinoceptor 4
PRO_0000070020

Regions

Topological domain1 – 3434Extracellular Potential
Transmembrane35 – 6127Helical; Name=1; Potential
Topological domain62 – 7211Cytoplasmic Potential
Transmembrane73 – 9523Helical; Name=2; Potential
Topological domain96 – 11217Extracellular Potential
Transmembrane113 – 13119Helical; Name=3; Potential
Topological domain132 – 15423Cytoplasmic Potential
Transmembrane155 – 17420Helical; Name=4; Potential
Topological domain175 – 19622Extracellular Potential
Transmembrane197 – 22226Helical; Name=5; Potential
Topological domain223 – 24624Cytoplasmic Potential
Transmembrane247 – 26923Helical; Name=6; Potential
Topological domain270 – 28718Extracellular Potential
Transmembrane288 – 30922Helical; Name=7; Potential
Topological domain310 – 36556Cytoplasmic Potential

Amino acid modifications

Modified residue3331Phosphoserine Probable
Modified residue3341Phosphoserine Probable
Disulfide bond108 ↔ 185 By similarity

Natural variations

Natural variant1681V → M.
Corresponds to variant rs1152186 [ dbSNP | Ensembl ].
VAR_011854
Natural variant1781N → T. Ref.2 Ref.5
Corresponds to variant rs1152187 [ dbSNP | Ensembl ].
VAR_011855
Natural variant1911P → L.
Corresponds to variant rs1152188 [ dbSNP | Ensembl ].
VAR_011856
Natural variant2341S → A. Ref.2
Corresponds to variant rs3829709 [ dbSNP | Ensembl ].
VAR_049429

Experimental info

Mutagenesis2431S → A: No effect. Ref.6
Mutagenesis333 – 36533Missing: Abolishes agonist-induced phosphorylation. Prevents agonist-induced desensitization and loss of cell surface receptors. Ref.6
Mutagenesis333 – 35927SSLAL…SSCST → AALALVALPEDAACRWAAAP QDAACAA: Greatly reduces agonist-induced desensitization and loss of cell surface receptors. Ref.6
Mutagenesis3331S → A: Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-334 and A-339. Ref.6
Mutagenesis3341S → A: Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-333 and A-339. Ref.6
Mutagenesis3391S → A: Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-333 and A-334. Ref.6
Mutagenesis344 – 36522Missing: No effect on agonist-induced phosphorylation, no functional effect.
Mutagenesis356 – 36510Missing: No functional effect.
Sequence conflict861L → V in AAC50347. Ref.2
Sequence conflict1211C → S in AAH96068. Ref.5
Sequence conflict2471I → V in AAH96069. Ref.5
Sequence conflict3521P → T in AAH96069. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P51582 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 23E0AFED3B7BDEED

FASTA36540,963
        10         20         30         40         50         60 
MASTESSLLR SLGLSPGPGS SEVELDCWFD EDFKFILLPV SYAVVFVLGL GLNAPTLWLF 

        70         80         90        100        110        120 
IFRLRPWDAT ATYMFHLALS DTLYVLSLPT LIYYYAAHNH WPFGTEICKF VRFLFYWNLY 

       130        140        150        160        170        180 
CSVLFLTCIS VHRYLGICHP LRALRWGRPR LAGLLCLAVW LVVAGCLVPN LFFVTTSNKG 

       190        200        210        220        230        240 
TTVLCHDTTR PEEFDHYVHF SSAVMGLLFG VPCLVTLVCY GLMARRLYQP LPGSAQSSSR 

       250        260        270        280        290        300 
LRSLRTIAVV LTVFAVCFVP FHITRTIYYL ARLLEADCRV LNIVNVVYKV TRPLASANSC 

       310        320        330        340        350        360 
LDPVLYLLTG DKYRRQLRQL CGGGKPQPRT AASSLALVSL PEDSSCRWAA TPQDSSCSTP 


RADRL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and functional expression of a human uridine nucleotide receptor."
Communi D., Pirotton S., Parmentier M., Boeynaems J.-M.
J. Biol. Chem. 270:30849-30852(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning, expression, and chromosomal localization of the human uridine nucleotide receptor gene."
Nguyen T., Erb L., Weisman G.A., Marchese A., Heng H.H.Q., Garrad R.C., George S.R., Turner J.T., O'Dowd B.F.
J. Biol. Chem. 270:30845-30848(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-178 AND ALA-234.
[3]"Molecular cloning and characterization of a novel orphan receptor (P2P) expressed in human pancreas that shows high structural homology to the P2U purinoceptor."
Stam N.J., Klomp J., van der Heuvel M., Olijve W.
FEBS Lett. 384:260-264(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Pancreas.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANT THR-178.
[6]"Differential regulation of the uridine nucleotide-activated P2Y4 and P2Y6 receptors. Ser-333 and Ser-334 in the carboxyl terminus are involved in agonist-dependent phosphorylation desensitization and internalization of the P2Y4 receptor."
Brinson A.E., Harden T.K.
J. Biol. Chem. 276:11939-11948(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-333 AND SER-334, MUTAGENESIS OF SER-243; SER-333; SER-334 AND SER-339.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91852 Genomic DNA. Translation: CAA62963.1.
U40223 Genomic DNA. Translation: AAC50347.1.
X96597 Genomic DNA. Translation: CAA65415.1.
AL357752 Genomic DNA. Translation: CAI41492.1.
BC095503 mRNA. Translation: AAH95503.1.
BC096067 mRNA. Translation: AAH96067.1.
BC096068 mRNA. Translation: AAH96068.1.
BC096069 mRNA. Translation: AAH96069.1.
BC096070 mRNA. Translation: AAH96070.1.
CCDSCCDS14398.1.
PIRS68679.
RefSeqNP_002556.1. NM_002565.3.
UniGeneHs.673854.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B6Qmodel-A1-365[»]
ProteinModelPortalP51582.
SMRP51582. Positions 36-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111069. 1 interaction.
IntActP51582. 1 interaction.
STRING9606.ENSP00000363643.

Chemistry

BindingDBP51582.
ChEMBLCHEMBL2123.
GuidetoPHARMACOLOGY325.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP51582.

Polymorphism databases

DMDM1709524.

Proteomic databases

PaxDbP51582.
PRIDEP51582.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374519; ENSP00000363643; ENSG00000186912.
GeneID5030.
KEGGhsa:5030.
UCSCuc004dxz.1. human.

Organism-specific databases

CTD5030.
GeneCardsGC0XM069478.
HGNCHGNC:8542. P2RY4.
HPACAB022644.
MIM300038. gene.
neXtProtNX_P51582.
PharmGKBPA32871.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270952.
HOGENOMHOG000231307.
HOVERGENHBG101120.
InParanoidP51582.
KOK04271.
OMAHANNVCE.
OrthoDBEOG7QNVM4.
PhylomeDBP51582.
TreeFamTF350009.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP51582.
BgeeP51582.
CleanExHS_P2RY4.
GenevestigatorP51582.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000018. P2Y4_rcpt.
[Graphical view]
PANTHERPTHR24231:SF21. PTHR24231:SF21. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR01066. P2Y4PRNOCPTR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiP2RY4.
GenomeRNAi5030.
NextBio19374.
PROP51582.
SOURCESearch...

Entry information

Entry nameP2RY4_HUMAN
AccessionPrimary (citable) accession number: P51582
Secondary accession number(s): Q4VBB7 expand/collapse secondary AC list , Q4VBB8, Q502W2, Q5JT22
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 122 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 X

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

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries