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P49799

- RGS4_RAT

UniProt

P49799 - RGS4_RAT

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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

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
Complete GO annotation...

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
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.

Miscellaneous databases

EvolutionaryTraceiP49799.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 178117RGS
Add
BLAST

Sequence similaritiesi

Contains 1 RGS domain.

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...

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: April 16, 2014
This is version 108 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

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