RGS4_RAT
ID RGS4_RAT Reviewed; 205 AA.
AC P49799;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Regulator of G-protein signaling 4;
DE Short=RGP4;
DE Short=RGS4;
GN Name=Rgs4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8602223; DOI=10.1038/379742a0;
RA Druey K.M., Blumer K.J., Kang V.H., Kehrl J.H.;
RT "Inhibition of G-protein-mediated MAP kinase activation by a new mammalian
RT gene family.";
RL Nature 379:742-746(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Zhou M.-Y., Gomez-Sanchez C.E., Gomez-Sanchez E.P.;
RT "The complete cDNA sequence analysis of the rat RGS4.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 93-159.
RC TISSUE=Brain;
RX PubMed=8548815; DOI=10.1016/s0092-8674(00)80998-8;
RA Koelle M.R., Horvitz H.R.;
RT "EGL-10 regulates G protein signaling in the C. elegans nervous system and
RT shares a conserved domain with many mammalian proteins.";
RL Cell 84:115-125(1996).
RN [4]
RP PHOSPHORYLATION.
RX PubMed=10702309; DOI=10.1074/jbc.275.10.7365;
RA Pedram A., Razandi M., Kehrl J., Levin E.R.;
RT "Natriuretic peptides inhibit G protein activation. Mediation through
RT cross-talk between cyclic GMP-dependent protein kinase and regulators of G
RT protein-signaling proteins.";
RL J. Biol. Chem. 275:7365-7372(2000).
RN [5]
RP INHIBITION.
RX PubMed=9353196; DOI=10.1126/science.278.5340.1132;
RA Tu Y., Wang J., Ross E.M.;
RT "Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G
RT protein alpha subunits.";
RL Science 278:1132-1135(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH G(I)-ALPHA.
RX PubMed=9108480; DOI=10.1016/s0092-8674(00)80204-4;
RA Tesmer J.J.G., Berman D.M., Gilman A.G., Sprang S.R.;
RT "Structure of RGS4 bound to AlF4-activated G(i alpha1): stabilization of
RT the transition state for GTP hydrolysis.";
RL Cell 89:251-261(1997).
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.
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:0000269|PubMed:10702309}.
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DR EMBL; U27767; AAC52440.1; -; mRNA.
DR EMBL; AF117211; AAD12065.1; -; mRNA.
DR EMBL; U32327; AAC52367.1; -; mRNA.
DR RefSeq; NP_058910.1; NM_017214.1.
DR PDB; 1AGR; X-ray; 2.80 A; E/H=1-205.
DR PDB; 1EZT; NMR; -; A=51-205.
DR PDB; 1EZY; NMR; -; A=51-205.
DR PDBsum; 1AGR; -.
DR PDBsum; 1EZT; -.
DR PDBsum; 1EZY; -.
DR AlphaFoldDB; P49799; -.
DR BMRB; P49799; -.
DR SMR; P49799; -.
DR CORUM; P49799; -.
DR DIP; DIP-6074N; -.
DR IntAct; P49799; 3.
DR MINT; P49799; -.
DR STRING; 10116.ENSRNOP00000003774; -.
DR GuidetoPHARMACOLOGY; 2811; -.
DR PhosphoSitePlus; P49799; -.
DR SwissPalm; P49799; -.
DR PaxDb; P49799; -.
DR Ensembl; ENSRNOT00000003774; ENSRNOP00000003774; ENSRNOG00000002773.
DR GeneID; 29480; -.
DR KEGG; rno:29480; -.
DR UCSC; RGD:3567; rat.
DR CTD; 5999; -.
DR RGD; 3567; Rgs4.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000159036; -.
DR HOGENOM; CLU_059863_3_0_1; -.
DR InParanoid; P49799; -.
DR OMA; LINHECG; -.
DR OrthoDB; 1435659at2759; -.
DR PhylomeDB; P49799; -.
DR TreeFam; TF315837; -.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR EvolutionaryTrace; P49799; -.
DR PRO; PR:P49799; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002773; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; P49799; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:1990791; P:dorsal root ganglion development; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IDA:RGD.
DR GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; IDA:RGD.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:1900924; P:negative regulation of glycine import across plasma membrane; IMP:RGD.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:RGD.
DR GO; GO:0010460; P:positive regulation of heart rate; IMP:RGD.
DR GO; GO:0110053; P:regulation of actin filament organization; IDA:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:RGD.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR CDD; cd08714; RGS_RGS4; 1.
DR DisProt; DP00063; -.
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 1: Evidence at protein level;
KW 3D-structure; Lipoprotein; Palmitate; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..205
FT /note="Regulator of G-protein signaling 4"
FT /id="PRO_0000204187"
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 HELIX 53..59
FT /evidence="ECO:0007829|PDB:1AGR"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:1AGR"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:1AGR"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:1AGR"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1AGR"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:1AGR"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:1AGR"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:1AGR"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:1AGR"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:1AGR"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1AGR"
SQ SEQUENCE 205 AA; 23249 MW; 9647C0EC909D0F6F CRC64;
MCKGLAGLPA SCLRSAKDMK HRLGFLLQKS DSCEHSSSHS KKDKVVTCQR VSQEEVKKWA
ESLENLINHE CGLAAFKAFL KSEYSEENID FWISCEEYKK IKSPSKLSPK AKKIYNEFIS
VQATKEVNLD SCTREETSRN MLEPTITCFD EAQKKIFNLM EKDSYRRFLK SRFYLDLTNP
SSCGAEKQKG AKSSADCTSL VPQCA
