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Protein

P2Y purinoceptor 4

Gene

P2RY4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_18289. P2Y receptors.
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
P2Y purinoceptor 4
Short name:
P2Y4
Alternative name(s):
P2P
Uridine nucleotide receptor
Short name:
UNR
Gene namesi
Name:P2RY4
Synonyms:NRU
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:8542. P2RY4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3434ExtracellularSequence AnalysisAdd
BLAST
Transmembranei35 – 6127Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini62 – 7211CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei73 – 9523Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini96 – 11217ExtracellularSequence AnalysisAdd
BLAST
Transmembranei113 – 13119Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini132 – 15423CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei155 – 17420Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini175 – 19622ExtracellularSequence AnalysisAdd
BLAST
Transmembranei197 – 22226Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini223 – 24624CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei247 – 26923Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini270 – 28718ExtracellularSequence AnalysisAdd
BLAST
Transmembranei288 – 30922Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini310 – 36556CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: Ensembl
  • cytosol Source: GOC
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi243 – 2431S → A: No effect. 1 Publication
Mutagenesisi333 – 36533Missing : Abolishes agonist-induced phosphorylation. Prevents agonist-induced desensitization and loss of cell surface receptors. Add
BLAST
Mutagenesisi333 – 35927SSLAL…SSCST → AALALVALPEDAACRWAAAP QDAACAA: Greatly reduces agonist-induced desensitization and loss of cell surface receptors. Add
BLAST
Mutagenesisi333 – 3331S → A: Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-334 and A-339. 1 Publication
Mutagenesisi334 – 3341S → A: Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-333 and A-339. 1 Publication
Mutagenesisi339 – 3391S → A: Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-333 and A-334. 1 Publication
Mutagenesisi344 – 36522Missing : No effect on agonist-induced phosphorylation, no functional effect. Add
BLAST
Mutagenesisi356 – 36510Missing : No functional effect.

Organism-specific databases

PharmGKBiPA32871.

Polymorphism and mutation databases

BioMutaiP2RY4.
DMDMi1709524.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 365365P2Y purinoceptor 4PRO_0000070020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi108 ↔ 185PROSITE-ProRule annotation
Modified residuei333 – 3331Phosphoserine1 Publication
Modified residuei334 – 3341Phosphoserine1 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP51582.
PRIDEiP51582.

PTM databases

PhosphoSiteiP51582.

Expressioni

Tissue specificityi

Pancreas.

Gene expression databases

BgeeiP51582.
CleanExiHS_P2RY4.
GenevisibleiP51582. HS.

Organism-specific databases

HPAiCAB022644.

Interactioni

Protein-protein interaction databases

IntActiP51582. 1 interaction.
STRINGi9606.ENSP00000363643.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B6Qmodel-A1-365[»]
ProteinModelPortaliP51582.
SMRiP51582. Positions 36-321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG270952.
GeneTreeiENSGT00760000118784.
HOGENOMiHOG000231307.
HOVERGENiHBG101120.
InParanoidiP51582.
KOiK04271.
OMAiYMFHLAL.
OrthoDBiEOG7QNVM4.
PhylomeDBiP51582.
TreeFamiTF350009.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000018. P2Y4_rcpt.
[Graphical view]
PANTHERiPTHR24231:SF21. PTHR24231:SF21. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01066. P2Y4PRNOCPTR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51582-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTESSLLR SLGLSPGPGS SEVELDCWFD EDFKFILLPV SYAVVFVLGL
60 70 80 90 100
GLNAPTLWLF IFRLRPWDAT ATYMFHLALS DTLYVLSLPT LIYYYAAHNH
110 120 130 140 150
WPFGTEICKF VRFLFYWNLY CSVLFLTCIS VHRYLGICHP LRALRWGRPR
160 170 180 190 200
LAGLLCLAVW LVVAGCLVPN LFFVTTSNKG TTVLCHDTTR PEEFDHYVHF
210 220 230 240 250
SSAVMGLLFG VPCLVTLVCY GLMARRLYQP LPGSAQSSSR LRSLRTIAVV
260 270 280 290 300
LTVFAVCFVP FHITRTIYYL ARLLEADCRV LNIVNVVYKV TRPLASANSC
310 320 330 340 350
LDPVLYLLTG DKYRRQLRQL CGGGKPQPRT AASSLALVSL PEDSSCRWAA
360
TPQDSSCSTP RADRL
Length:365
Mass (Da):40,963
Last modified:October 1, 1996 - v1
Checksum:i23E0AFED3B7BDEED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861L → V in AAC50347 (PubMed:8537335).Curated
Sequence conflicti121 – 1211C → S in AAH96068 (PubMed:15489334).Curated
Sequence conflicti247 – 2471I → V in AAH96069 (PubMed:15489334).Curated
Sequence conflicti352 – 3521P → T in AAH96069 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti168 – 1681V → M.
Corresponds to variant rs1152186 [ dbSNP | Ensembl ].
VAR_011854
Natural varianti178 – 1781N → T.2 Publications
Corresponds to variant rs1152187 [ dbSNP | Ensembl ].
VAR_011855
Natural varianti191 – 1911P → L.
Corresponds to variant rs1152188 [ dbSNP | Ensembl ].
VAR_011856
Natural varianti234 – 2341S → A.1 Publication
Corresponds to variant rs3829709 [ dbSNP | Ensembl ].
VAR_049429

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14398.1.
PIRiS68679.
RefSeqiNP_002556.1. NM_002565.3.
UniGeneiHs.673854.

Genome annotation databases

EnsembliENST00000374519; ENSP00000363643; ENSG00000186912.
GeneIDi5030.
KEGGihsa:5030.
UCSCiuc004dxz.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14398.1.
PIRiS68679.
RefSeqiNP_002556.1. NM_002565.3.
UniGeneiHs.673854.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B6Qmodel-A1-365[»]
ProteinModelPortaliP51582.
SMRiP51582. Positions 36-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP51582. 1 interaction.
STRINGi9606.ENSP00000363643.

Chemistry

BindingDBiP51582.
ChEMBLiCHEMBL2123.
GuidetoPHARMACOLOGYi325.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP51582.

Polymorphism and mutation databases

BioMutaiP2RY4.
DMDMi1709524.

Proteomic databases

PaxDbiP51582.
PRIDEiP51582.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374519; ENSP00000363643; ENSG00000186912.
GeneIDi5030.
KEGGihsa:5030.
UCSCiuc004dxz.1. human.

Organism-specific databases

CTDi5030.
GeneCardsiGC0XM069478.
HGNCiHGNC:8542. P2RY4.
HPAiCAB022644.
MIMi300038. gene.
neXtProtiNX_P51582.
PharmGKBiPA32871.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG270952.
GeneTreeiENSGT00760000118784.
HOGENOMiHOG000231307.
HOVERGENiHBG101120.
InParanoidiP51582.
KOiK04271.
OMAiYMFHLAL.
OrthoDBiEOG7QNVM4.
PhylomeDBiP51582.
TreeFamiTF350009.

Enzyme and pathway databases

ReactomeiREACT_18289. P2Y receptors.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

GeneWikiiP2RY4.
GenomeRNAii5030.
NextBioi19374.
PROiP51582.
SOURCEiSearch...

Gene expression databases

BgeeiP51582.
CleanExiHS_P2RY4.
GenevisibleiP51582. HS.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000018. P2Y4_rcpt.
[Graphical view]
PANTHERiPTHR24231:SF21. PTHR24231:SF21. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01066. P2Y4PRNOCPTR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiP2RY4_HUMAN
AccessioniPrimary (citable) accession number: P51582
Secondary accession number(s): Q4VBB7
, Q4VBB8, Q502W2, Q5JT22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.