RGS4_MOUSE
ID RGS4_MOUSE Reviewed; 205 AA.
AC O08899; Q99L30;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Regulator of G-protein signaling 4;
DE Short=RGS4;
GN Name=Rgs4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Substantia nigra;
RX PubMed=9425263; DOI=10.1006/bbrc.1997.7802;
RA Nomoto S., Adachi K., Yang L.X., Hirata Y., Muraguchi S., Kiuchi K.;
RT "Distribution of RGS4 mRNA in mouse brain shown by in situ hybridization.";
RL Biochem. Biophys. Res. Commun. 241:281-287(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC activity of G protein alpha subunits thereby driving them into their
CC inactive GDP-bound form. Activity on G(z)-alpha is inhibited by
CC phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)-
CC alpha-1 is inhibited by palmitoylation of the G-protein (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, moderately low
CC levels in heart, and very low levels in lung, liver, and skeletal
CC muscle.
CC -!- PTM: Either Cys-2 or Cys-12 or both are palmitoylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated by cyclic GMP-dependent protein kinase.
CC {ECO:0000250}.
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DR EMBL; AB004315; BAA20400.1; -; mRNA.
DR EMBL; BC003882; AAH03882.1; -; mRNA.
DR CCDS; CCDS15465.1; -.
DR RefSeq; NP_033088.2; NM_009062.3.
DR AlphaFoldDB; O08899; -.
DR BMRB; O08899; -.
DR SMR; O08899; -.
DR BioGRID; 202884; 1.
DR ELM; O08899; -.
DR STRING; 10090.ENSMUSP00000027991; -.
DR iPTMnet; O08899; -.
DR PhosphoSitePlus; O08899; -.
DR PaxDb; O08899; -.
DR PRIDE; O08899; -.
DR ProteomicsDB; 255194; -.
DR DNASU; 19736; -.
DR GeneID; 19736; -.
DR KEGG; mmu:19736; -.
DR CTD; 5999; -.
DR MGI; MGI:108409; Rgs4.
DR eggNOG; KOG3589; Eukaryota.
DR InParanoid; O08899; -.
DR OrthoDB; 1435659at2759; -.
DR PhylomeDB; O08899; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 19736; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Rgs4; mouse.
DR PRO; PR:O08899; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O08899; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; ISO:MGI.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:1900924; P:negative regulation of glycine import across plasma membrane; ISO:MGI.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0010460; P:positive regulation of heart rate; ISO:MGI.
DR GO; GO:0110053; P:regulation of actin filament organization; ISO:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:MGI.
DR CDD; cd08714; RGS_RGS4; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034952; RGS4.
DR InterPro; IPR034953; RGS_RGS4.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR10845:SF184; PTHR10845:SF184; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50132; RGS; 1.
PE 2: Evidence at transcript level;
KW Lipoprotein; Palmitate; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..205
FT /note="Regulator of G-protein signaling 4"
FT /id="PRO_0000204186"
FT DOMAIN 62..178
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT LIPID 2
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 12
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 95
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 162
FT /note="R -> K (in Ref. 2; AAH03882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 205 AA; 23289 MW; 5D79581711A1F67C CRC64;
MCKGLAGLPA SCLRSAKDMK HRLGFLLQKS DSCEHSSSHS KKDKVVTCQR VSQEEVKKWA
ESLENLIHHE CGLAAFKAFL KSEYSEENID FWISCEEYKK IKSPSKLSPK AKKIYNEFIS
VQATKEVNLD SCTREETSRN MLQPTITCFD EAQKKIFNLM ERDSYRRFLK SRFYLDLTNP
SSCGAEKQKG AKSSADCTSL VSQCA