Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P51582

- P2RY4_HUMAN

UniProt

P51582 - P2RY4_HUMAN

Protein

P2Y purinoceptor 4

Gene

P2RY4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. ATP binding Source: Ensembl
    2. G-protein coupled purinergic nucleotide receptor activity Source: InterPro
    3. uridine nucleotide receptor activity Source: ProtInc
    4. UTP-activated nucleotide receptor activity Source: Ensembl

    GO - Biological processi

    1. phospholipase C-activating G-protein coupled receptor signaling pathway Source: ProtInc
    2. positive regulation of cytosolic calcium ion concentration Source: ProtInc
    3. transepithelial chloride transport Source: Ensembl

    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: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8542. P2RY4.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. basolateral plasma membrane Source: Ensembl
    3. integral component of plasma membrane Source: ProtInc
    4. plasma membrane Source: Reactome

    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. 1 PublicationAdd
    BLAST
    Mutagenesisi333 – 35927SSLAL…SSCST → AALALVALPEDAACRWAAAP QDAACAA: Greatly reduces agonist-induced desensitization and loss of cell surface receptors. 1 PublicationAdd
    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.

    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

    ArrayExpressiP51582.
    BgeeiP51582.
    CleanExiHS_P2RY4.
    GenevestigatoriP51582.

    Organism-specific databases

    HPAiCAB022644.

    Interactioni

    Protein-protein interaction databases

    BioGridi111069. 1 interaction.
    IntActiP51582. 1 interaction.
    STRINGi9606.ENSP00000363643.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B6Qmodel-A1-365[»]
    ProteinModelPortaliP51582.
    SMRiP51582. Positions 36-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3434ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini62 – 7211CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini96 – 11217ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini132 – 15423CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini175 – 19622ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini223 – 24624CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini270 – 28718ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini310 – 36556CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei35 – 6127Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei73 – 9523Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei113 – 13119Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei155 – 17420Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei197 – 22226Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei247 – 26923Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei288 – 30922Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG270952.
    HOGENOMiHOG000231307.
    HOVERGENiHBG101120.
    InParanoidiP51582.
    KOiK04271.
    OMAiHANNVCE.
    OrthoDBiEOG7QNVM4.
    PhylomeDBiP51582.
    TreeFamiTF350009.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    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

    MASTESSLLR SLGLSPGPGS SEVELDCWFD EDFKFILLPV SYAVVFVLGL    50
    GLNAPTLWLF IFRLRPWDAT ATYMFHLALS DTLYVLSLPT LIYYYAAHNH 100
    WPFGTEICKF VRFLFYWNLY CSVLFLTCIS VHRYLGICHP LRALRWGRPR 150
    LAGLLCLAVW LVVAGCLVPN LFFVTTSNKG TTVLCHDTTR PEEFDHYVHF 200
    SSAVMGLLFG VPCLVTLVCY GLMARRLYQP LPGSAQSSSR LRSLRTIAVV 250
    LTVFAVCFVP FHITRTIYYL ARLLEADCRV LNIVNVVYKV TRPLASANSC 300
    LDPVLYLLTG DKYRRQLRQL CGGGKPQPRT AASSLALVSL PEDSSCRWAA 350
    TPQDSSCSTP RADRL 365
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi1709524.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14398.1.
    PIRi S68679.
    RefSeqi NP_002556.1. NM_002565.3.
    UniGenei Hs.673854.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B6Q model - A 1-365 [» ]
    ProteinModelPortali P51582.
    SMRi P51582. Positions 36-323.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111069. 1 interaction.
    IntActi P51582. 1 interaction.
    STRINGi 9606.ENSP00000363643.

    Chemistry

    BindingDBi P51582.
    ChEMBLi CHEMBL2123.
    GuidetoPHARMACOLOGYi 325.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P51582.

    Polymorphism databases

    DMDMi 1709524.

    Proteomic databases

    PaxDbi P51582.
    PRIDEi P51582.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374519 ; ENSP00000363643 ; ENSG00000186912 .
    GeneIDi 5030.
    KEGGi hsa:5030.
    UCSCi uc004dxz.1. human.

    Organism-specific databases

    CTDi 5030.
    GeneCardsi GC0XM069478.
    HGNCi HGNC:8542. P2RY4.
    HPAi CAB022644.
    MIMi 300038. gene.
    neXtProti NX_P51582.
    PharmGKBi PA32871.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270952.
    HOGENOMi HOG000231307.
    HOVERGENi HBG101120.
    InParanoidi P51582.
    KOi K04271.
    OMAi HANNVCE.
    OrthoDBi EOG7QNVM4.
    PhylomeDBi P51582.
    TreeFami TF350009.

    Enzyme and pathway databases

    Reactomei REACT_18289. P2Y receptors.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    GeneWikii P2RY4.
    GenomeRNAii 5030.
    NextBioi 19374.
    PROi P51582.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51582.
    Bgeei P51582.
    CleanExi HS_P2RY4.
    Genevestigatori P51582.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR000018. P2Y4_rcpt.
    [Graphical view ]
    PANTHERi PTHR24231:SF21. PTHR24231:SF21. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PR01066. P2Y4PRNOCPTR.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 124 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