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P49799 (RGS4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Regulator of G-protein signaling 4

Short name=RGP4
Short name=RGS4
Gene names
Name:Rgs4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Post-translational modification

Either Cys-2 or Cys-12 or both are palmitoylated By similarity.

Phosphorylated by cyclic GMP-dependent protein kinase. Ref.4

Sequence similarities

Contains 1 RGS domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205Regulator of G-protein signaling 4
PRO_0000204187

Regions

Domain62 – 178117RGS

Amino acid modifications

Lipidation21S-palmitoyl cysteine By similarity
Lipidation121S-palmitoyl cysteine By similarity
Lipidation951S-palmitoyl cysteine By similarity

Secondary structure

..................... 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49799 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 9647C0EC909D0F6F

FASTA20523,249
        10         20         30         40         50         60 
MCKGLAGLPA SCLRSAKDMK HRLGFLLQKS DSCEHSSSHS KKDKVVTCQR VSQEEVKKWA 

        70         80         90        100        110        120 
ESLENLINHE CGLAAFKAFL KSEYSEENID FWISCEEYKK IKSPSKLSPK AKKIYNEFIS 

       130        140        150        160        170        180 
VQATKEVNLD SCTREETSRN MLEPTITCFD EAQKKIFNLM EKDSYRRFLK SRFYLDLTNP 

       190        200 
SSCGAEKQKG AKSSADCTSL VPQCA 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27767 mRNA. Translation: AAC52440.1.
AF117211 mRNA. Translation: AAD12065.1.
U32327 mRNA. Translation: AAC52367.1.
RefSeqNP_058910.1. NM_017214.1.
UniGeneRn.11065.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AGRX-ray2.80E/H1-205[»]
1EZTNMR-A51-205[»]
1EZYNMR-A51-205[»]
DisProtDP00063.
ProteinModelPortalP49799.
SMRP49799. Positions 51-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6074N.
IntActP49799. 3 interactions.
MINTMINT-8049194.
STRING10116.ENSRNOP00000003774.

PTM databases

PhosphoSiteP49799.

Proteomic databases

PaxDbP49799.
PRIDEP49799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000003774; ENSRNOP00000003774; ENSRNOG00000002773.
GeneID29480.
KEGGrno:29480.
UCSCRGD:3567. rat.

Organism-specific databases

CTD5999.
RGD3567. Rgs4.

Phylogenomic databases

eggNOGNOG318241.
GeneTreeENSGT00750000117382.
HOGENOMHOG000233512.
HOVERGENHBG013233.
InParanoidP49799.
KOK16449.
OMADCPSLVP.
OrthoDBEOG7VHSZ5.
PhylomeDBP49799.
TreeFamTF315837.

Gene expression databases

GenevestigatorP49799.

Family and domain databases

Gene3D1.10.196.10. 2 hits.
InterProIPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view]
PfamPF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR01301. RGSPROTEIN.
SMARTSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
PROSITEPS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP49799.
NextBio609328.
PROP49799.

Entry information

Entry nameRGS4_RAT
AccessionPrimary (citable) accession number: P49799
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references