ID   RGS7_RAT                Reviewed;         477 AA.
AC   P49803; Q9R0R0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Regulator of G-protein signaling 7;
DE            Short=RGS7;
GN   Name=Rgs7;
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], FUNCTION, INTERACTION WITH GNAO1; GNAI3 AND
RP   GNAZ, AND TISSUE SPECIFICITY.
RX   PubMed=10092682; DOI=10.1074/jbc.274.14.9899;
RA   Saitoh O., Kubo Y., Odagiri M., Ichikawa M., Yamagata K., Sekine T.;
RT   "RGS7 and RGS8 differentially accelerate G protein-mediated modulation of
RT   K+ currents.";
RL   J. Biol. Chem. 274:9899-9904(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 364-429.
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   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=9315921; DOI=10.1523/jneurosci.17-20-08024.1997;
RA   Gold S.J., Ni Y.G., Dohlman H.G., Nestler E.J.;
RT   "Regulators of G-protein signaling (RGS) proteins: region-specific
RT   expression of nine subtypes in rat brain.";
RL   J. Neurosci. 17:8024-8037(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: GTPase activator component of the RGS7-GNB5 complex that
CC       regulates G protein-coupled receptor signaling cascades. The RGS7-GNB5
CC       complex acts as an inhibitor signal transduction by promoting the
CC       GTPase activity of G protein alpha subunits, such as GNAO1, thereby
CC       driving them into their inactive GDP-bound form. May play a role in
CC       synaptic vesicle exocytosis (By similarity). Glycine-dependent
CC       regulation of the RGS7-GNB5 complex by GPR158 affects mood and
CC       cognition via its ability to regulate neuronal excitability in L2/L3
CC       pyramidal neurons of the prefrontal cortex (By similarity). Modulates
CC       the activity of potassium channels that are activated by GNAO1 in
CC       response to muscarinic acetylcholine receptor M2/CHRM2 signaling
CC       (PubMed:10092682). {ECO:0000250|UniProtKB:O54829,
CC       ECO:0000250|UniProtKB:P49802, ECO:0000269|PubMed:10092682}.
CC   -!- SUBUNIT: Interacts with GNB5, forming the RGS7-GNB5 complex. Interacts
CC       with GPR158; promotes the GTPase activator activity of the RGS7-GNB5
CC       complex in absence of glycine, in contrast GTPase activator activity of
CC       the RGS7-GNB5 complex is inhibited in presence of glycine (By
CC       similarity). Interacts with GPR179 (By similarity). Interacts with
CC       PKD1; this prevents rapid proteasomal degradation. Interacts with
CC       RGS7BP, leading to regulate the subcellular location of the heterodimer
CC       formed with GNB5. Interacts (phosphorylated form) with 14-3-3 protein
CC       YWHAQ. Interacts with SNAPIN. Interacts with GNAI1 (By similarity).
CC       Interacts with GNAO1, GNAI3 and GNAZ (PubMed:10092682).
CC       {ECO:0000250|UniProtKB:O54829, ECO:0000250|UniProtKB:P49802,
CC       ECO:0000269|PubMed:10092682}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P49802}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P49802}. Cell membrane
CC       {ECO:0000250|UniProtKB:P49802}. Membrane
CC       {ECO:0000250|UniProtKB:P49802}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P49802}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P49802}. Note=Interaction with PKD1 promotes
CC       location at the cell membrane. Interaction with RGS7BP promotes
CC       location at the cell membrane. {ECO:0000250|UniProtKB:P49802}.
CC   -!- TISSUE SPECIFICITY: Brain-specific. Predominantly cerebellar granule
CC       cells. {ECO:0000269|PubMed:10092682, ECO:0000269|PubMed:9315921}.
CC   -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:O46470}.
CC   -!- PTM: Ubiquitinated, leading to rapid proteasomal degradation.
CC       {ECO:0000250|UniProtKB:P49802}.
CC   -!- PTM: Phosphorylation and subsequent interaction with 14-3-3 proteins
CC       inhibits GAP activity. {ECO:0000250|UniProtKB:P49802}.
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DR   EMBL; AB024398; BAA75635.1; -; mRNA.
DR   EMBL; U32328; AAC52368.1; -; mRNA.
DR   RefSeq; NP_062216.1; NM_019343.1.
DR   AlphaFoldDB; P49803; -.
DR   SMR; P49803; -.
DR   BioGRID; 248516; 1.
DR   CORUM; P49803; -.
DR   STRING; 10116.ENSRNOP00000063631; -.
DR   CarbonylDB; P49803; -.
DR   iPTMnet; P49803; -.
DR   PhosphoSitePlus; P49803; -.
DR   jPOST; P49803; -.
DR   PaxDb; 10116-ENSRNOP00000063631; -.
DR   Ensembl; ENSRNOT00000116817.1; ENSRNOP00000082844.1; ENSRNOG00000021984.7.
DR   Ensembl; ENSRNOT00055039554; ENSRNOP00055032125; ENSRNOG00055022991.
DR   Ensembl; ENSRNOT00060047353; ENSRNOP00060039417; ENSRNOG00060027170.
DR   Ensembl; ENSRNOT00065037779; ENSRNOP00065030551; ENSRNOG00065022162.
DR   GeneID; 54296; -.
DR   KEGG; rno:54296; -.
DR   UCSC; RGD:3570; rat.
DR   AGR; RGD:3570; -.
DR   CTD; 6000; -.
DR   RGD; 3570; Rgs7.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000156661; -.
DR   InParanoid; P49803; -.
DR   OMA; CACRMVP; -.
DR   OrthoDB; 22856at2759; -.
DR   PhylomeDB; P49803; -.
DR   TreeFam; TF351956; -.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:P49803; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0044292; C:dendrite terminus; ISO:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR   GO; GO:0098793; C:presynapse; ISO: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:0031681; F:G-protein beta-subunit binding; IPI:RGD.
DR   GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:RGD.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IDA:RGD.
DR   GO; GO:0060078; P:regulation of postsynaptic membrane potential; ISO:RGD.
DR   GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   CDD; cd04450; DEP_RGS7-like; 1.
DR   CDD; cd00068; GGL; 1.
DR   CDD; cd08738; RGS_RGS7; 1.
DR   Gene3D; 1.10.1240.60; -; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR015898; G-protein_gamma-like_dom.
DR   InterPro; IPR036284; GGL_sf.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR047016; RGS6/7/9/11.
DR   InterPro; IPR047017; RGS6/7/9/11_DHEX_sf.
DR   InterPro; IPR040759; RGS_DHEX.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45746; LP21163P; 1.
DR   PANTHER; PTHR45746:SF7; REGULATOR OF G-PROTEIN SIGNALING 7; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   Pfam; PF00615; RGS; 1.
DR   Pfam; PF18148; RGS_DHEX; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM01224; G_gamma; 1.
DR   SMART; SM00224; GGL; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; GTPase activation; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Reference proteome;
KW   Signal transduction inhibitor; Ubl conjugation.
FT   CHAIN           1..477
FT                   /note="Regulator of G-protein signaling 7"
FT                   /id="PRO_0000204198"
FT   DOMAIN          37..112
FT                   /note="DEP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT   DOMAIN          255..316
FT                   /note="G protein gamma"
FT   DOMAIN          333..448
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          236..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O54829"
FT   MOD_RES         243
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O54829"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49802"
SQ   SEQUENCE   477 AA;  55691 MW;  4BA05410865DDC4A CRC64;
     MAQGNNYGQT SNGVAEESPN MLVYRKMEDV IARMQDEKNG IPIRTVKSFL SKIPSVFSGS
     DIVQWLIKNL TIEDPVEALH LGTLMAAHGY FFPISDHVLT LKDDGTFYRF QTPYFWPSNC
     WEPENTDYAV YLCKRTMQNK ARLELADYEA ESLARLQRAF ARKWEFIFMQ AEAQAKVDKK
     RDKIERKILD SQERAFWDVH RPVPGCVNTT EVDIKKSSRM RNPHKTRKSV YGLQNDIRSH
     SPTHTPTPET KPPTEDELHR QIKYWQIQLD RHRLKMSKVA DSLLSYTEQY VEYDPFLVPP
     DPSNPWLSDD TTFWELEASK EPSQQRVKRW GFGMDEALKD PVGREQFLKF LESEFSSENL
     RFWLAVEDLK KRPIREVPSR VQEIWQEFLA PGAPSAINLD SKSYDKTTQN VKEPGRYTFE
     DAQEHIYKLM KSDSYPRFIR SSAYQELLQA KRKGRNIPIF PCHKNCTPTL RASTNLL
//