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P49799

- RGS4_RAT

UniProt

P49799 - RGS4_RAT

Protein

Regulator of G-protein signaling 4

Gene

Rgs4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(z)-alpha is inhibited by phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)-alpha-1 is inhibited by palmitoylation of the G-protein.

    GO - Molecular functioni

    1. G-protein alpha-subunit binding Source: RGD
    2. GTPase activator activity Source: RGD

    GO - Biological processi

    1. negative regulation of G-protein coupled receptor protein signaling pathway Source: RGD
    2. positive regulation of GTPase activity Source: RGD
    3. termination of G-protein coupled receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Signal transduction inhibitor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of G-protein signaling 4
    Short name:
    RGP4
    Short name:
    RGS4
    Gene namesi
    Name:Rgs4
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 13

    Organism-specific databases

    RGDi3567. Rgs4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. cytosol Source: RGD
    3. membrane Source: RGD
    4. plasma membrane Source: RGD
    5. protein complex Source: RGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 205205Regulator of G-protein signaling 4PRO_0000204187Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21S-palmitoyl cysteineBy similarity
    Lipidationi12 – 121S-palmitoyl cysteineBy similarity
    Lipidationi95 – 951S-palmitoyl cysteineBy similarity

    Post-translational modificationi

    Either Cys-2 or Cys-12 or both are palmitoylated.By similarity
    Phosphorylated by cyclic GMP-dependent protein kinase.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP49799.
    PRIDEiP49799.

    PTM databases

    PhosphoSiteiP49799.

    Expressioni

    Gene expression databases

    GenevestigatoriP49799.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-6074N.
    IntActiP49799. 3 interactions.
    MINTiMINT-8049194.
    STRINGi10116.ENSRNOP00000003774.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi53 – 597
    Helixi63 – 686
    Helixi70 – 8213
    Helixi87 – 10014
    Turni104 – 1063
    Helixi107 – 11812
    Helixi131 – 14010
    Turni146 – 1494
    Helixi150 – 16213
    Helixi164 – 1685
    Helixi172 – 1754

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AGRX-ray2.80E/H1-205[»]
    1EZTNMR-A51-205[»]
    1EZYNMR-A51-205[»]
    DisProtiDP00063.
    ProteinModelPortaliP49799.
    SMRiP49799. Positions 51-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49799.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini62 – 178117RGSPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG318241.
    GeneTreeiENSGT00750000117382.
    HOGENOMiHOG000233512.
    HOVERGENiHBG013233.
    InParanoidiP49799.
    KOiK16449.
    OMAiDCPSLVP.
    OrthoDBiEOG7VHSZ5.
    PhylomeDBiP49799.
    TreeFamiTF315837.

    Family and domain databases

    Gene3Di1.10.196.10. 2 hits.
    InterProiIPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    [Graphical view]
    PfamiPF00615. RGS. 1 hit.
    [Graphical view]
    PRINTSiPR01301. RGSPROTEIN.
    SMARTiSM00315. RGS. 1 hit.
    [Graphical view]
    SUPFAMiSSF48097. SSF48097. 1 hit.
    PROSITEiPS50132. RGS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P49799-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCKGLAGLPA SCLRSAKDMK HRLGFLLQKS DSCEHSSSHS KKDKVVTCQR    50
    VSQEEVKKWA ESLENLINHE CGLAAFKAFL KSEYSEENID FWISCEEYKK 100
    IKSPSKLSPK AKKIYNEFIS VQATKEVNLD SCTREETSRN MLEPTITCFD 150
    EAQKKIFNLM EKDSYRRFLK SRFYLDLTNP SSCGAEKQKG AKSSADCTSL 200
    VPQCA 205
    Length:205
    Mass (Da):23,249
    Last modified:October 1, 1996 - v1
    Checksum:i9647C0EC909D0F6F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27767 mRNA. Translation: AAC52440.1.
    AF117211 mRNA. Translation: AAD12065.1.
    U32327 mRNA. Translation: AAC52367.1.
    RefSeqiNP_058910.1. NM_017214.1.
    UniGeneiRn.11065.

    Genome annotation databases

    EnsembliENSRNOT00000003774; ENSRNOP00000003774; ENSRNOG00000002773.
    GeneIDi29480.
    KEGGirno:29480.
    UCSCiRGD:3567. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27767 mRNA. Translation: AAC52440.1 .
    AF117211 mRNA. Translation: AAD12065.1 .
    U32327 mRNA. Translation: AAC52367.1 .
    RefSeqi NP_058910.1. NM_017214.1.
    UniGenei Rn.11065.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AGR X-ray 2.80 E/H 1-205 [» ]
    1EZT NMR - A 51-205 [» ]
    1EZY NMR - A 51-205 [» ]
    DisProti DP00063.
    ProteinModelPortali P49799.
    SMRi P49799. Positions 51-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6074N.
    IntActi P49799. 3 interactions.
    MINTi MINT-8049194.
    STRINGi 10116.ENSRNOP00000003774.

    PTM databases

    PhosphoSitei P49799.

    Proteomic databases

    PaxDbi P49799.
    PRIDEi P49799.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000003774 ; ENSRNOP00000003774 ; ENSRNOG00000002773 .
    GeneIDi 29480.
    KEGGi rno:29480.
    UCSCi RGD:3567. rat.

    Organism-specific databases

    CTDi 5999.
    RGDi 3567. Rgs4.

    Phylogenomic databases

    eggNOGi NOG318241.
    GeneTreei ENSGT00750000117382.
    HOGENOMi HOG000233512.
    HOVERGENi HBG013233.
    InParanoidi P49799.
    KOi K16449.
    OMAi DCPSLVP.
    OrthoDBi EOG7VHSZ5.
    PhylomeDBi P49799.
    TreeFami TF315837.

    Miscellaneous databases

    EvolutionaryTracei P49799.
    NextBioi 609328.
    PROi P49799.

    Gene expression databases

    Genevestigatori P49799.

    Family and domain databases

    Gene3Di 1.10.196.10. 2 hits.
    InterProi IPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    [Graphical view ]
    Pfami PF00615. RGS. 1 hit.
    [Graphical view ]
    PRINTSi PR01301. RGSPROTEIN.
    SMARTi SM00315. RGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48097. SSF48097. 1 hit.
    PROSITEi PS50132. RGS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family."
      Druey K.M., Blumer K.J., Kang V.H., Kehrl J.H.
      Nature 379:742-746(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The complete cDNA sequence analysis of the rat RGS4."
      Zhou M.-Y., Gomez-Sanchez C.E., Gomez-Sanchez E.P.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
    3. "EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins."
      Koelle M.R., Horvitz H.R.
      Cell 84:115-125(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 93-159.
      Tissue: Brain.
    4. "Natriuretic peptides inhibit G protein activation. Mediation through cross-talk between cyclic GMP-dependent protein kinase and regulators of G protein-signaling proteins."
      Pedram A., Razandi M., Kehrl J., Levin E.R.
      J. Biol. Chem. 275:7365-7372(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    5. "Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein alpha subunits."
      Tu Y., Wang J., Ross E.M.
      Science 278:1132-1135(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION.
    6. "Structure of RGS4 bound to AlF4-activated G(i alpha1): stabilization of the transition state for GTP hydrolysis."
      Tesmer J.J.G., Berman D.M., Gilman A.G., Sprang S.R.
      Cell 89:251-261(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH G(I)-ALPHA.

    Entry informationi

    Entry nameiRGS4_RAT
    AccessioniPrimary (citable) accession number: P49799
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3