RGS7_RAT
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 03-AUG-2022, entry version 159.
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: Regulates G protein-coupled receptor signaling cascades.
CC Inhibits signal transduction by increasing the GTPase activity of G
CC protein alpha subunits, thereby driving them into their inactive GDP-
CC bound form. The RGS7/GNB5 dimer enhances GNAO1 GTPase activity. May
CC play a role in synaptic vesicle exocytosis. Modulates the activity of
CC potassium channels that are activated by GNAO1 in response to
CC muscarinic acetylcholine receptor M2/CHRM2 signaling (PubMed:10092682).
CC {ECO:0000250|UniProtKB:P49802, ECO:0000269|PubMed:10092682}.
CC -!- SUBUNIT: Interacts with PKD1; this prevents rapid proteasomal
CC degradation. Interacts with GNB5. Interacts with RGS7BP, leading to
CC regulate the subcellular location of the heterodimer formed with GNB5.
CC Interacts (phosphorylated form) with 14-3-3 protein YWHAQ. Interacts
CC with SNAPIN. Interacts with GNAI1 (By similarity). Interacts with
CC GNAO1, GNAI3 and GNAZ (PubMed:10092682). {ECO:0000250|UniProtKB:O54829,
CC ECO:0000250|UniProtKB:P49802, 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; P49803; -.
DR PRIDE; P49803; -.
DR Ensembl; ENSRNOT00000116817; ENSRNOP00000082844; ENSRNOG00000021984.
DR GeneID; 54296; -.
DR KEGG; rno:54296; -.
DR UCSC; RGD:3570; rat.
DR CTD; 6000; -.
DR RGD; 3570; Rgs7.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000156661; -.
DR InParanoid; P49803; -.
DR OrthoDB; 415625at2759; -.
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; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0044292; C:dendrite terminus; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA: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; IDA: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; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
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:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
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:0009409; P:response to cold; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 4.10.260.10; -; 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; 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 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; SM00224; GGL; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF48670; SSF48670; 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
