RGS7_MOUSE
ID RGS7_MOUSE Reviewed; 469 AA.
AC O54829; E9QLB9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Regulator of G-protein signaling 7;
DE Short=RGS7;
GN Name=Rgs7;
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].
RX PubMed=9459445; DOI=10.1016/s0896-6273(00)80437-7;
RA He W., Cowan C.W., Wensel T.G.;
RT "RGS9, a GTPase accelerator for phototransduction.";
RL Neuron 20:95-102(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INTERACTION WITH 14-3-3 PROTEIN YWHAQ, AND TISSUE SPECIFICITY.
RX PubMed=10862767; DOI=10.1074/jbc.m002905200;
RA Benzing T., Yaffe M.B., Arnould T., Sellin L., Schermer B., Schilling B.,
RA Schreiber R., Kunzelmann K., Leparc G.G., Kim E., Walz G.;
RT "14-3-3 interacts with regulator of G protein signaling proteins and
RT modulates their activity.";
RL J. Biol. Chem. 275:28167-28172(2000).
RN [4]
RP INTERACTION WITH RGS7BP.
RX PubMed=15632198; DOI=10.1074/jbc.c400596200;
RA Martemyanov K.A., Yoo P.J., Skiba N.P., Arshavsky V.Y.;
RT "R7BP, a novel neuronal protein interacting with RGS proteins of the R7
RT family.";
RL J. Biol. Chem. 280:5133-5136(2005).
RN [5]
RP INTERACTION WITH RGS7BP.
RX PubMed=15897264; DOI=10.1083/jcb.200502007;
RA Drenan R.M., Doupnik C.A., Boyle M.P., Muglia L.J., Huettner J.E.,
RA Linder M.E., Blumer K.J.;
RT "Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a
RT novel membrane anchor for the RGS7 family.";
RL J. Cell Biol. 169:623-633(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND THR-243, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC {ECO:0000250|UniProtKB:P49802}.
CC -!- SUBUNIT: Interacts with PKD1; this prevents rapid proteasomal
CC degradation. Interacts with GNB5 (By similarity). Interacts with
CC RGS7BP, leading to regulate the subcellular location of the heterodimer
CC formed with GNB5 (PubMed:15632198, PubMed:15897264). Interacts
CC (phosphorylated form) with 14-3-3 protein YWHAQ (PubMed:10862767).
CC Interacts with SNAPIN. Interacts with GNAI1 (By similarity). Interacts
CC with GNAO1, GNAI3 and GNAZ (By similarity).
CC {ECO:0000250|UniProtKB:P49802, ECO:0000250|UniProtKB:P49803,
CC ECO:0000269|PubMed:10862767, ECO:0000269|PubMed:15632198,
CC ECO:0000269|PubMed:15897264}.
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: Detected in brain (at protein level).
CC {ECO:0000269|PubMed:10862767}.
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; AF011360; AAC99483.1; -; mRNA.
DR EMBL; AC102499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15546.1; -.
DR RefSeq; NP_036010.2; NM_011880.3.
DR AlphaFoldDB; O54829; -.
DR SMR; O54829; -.
DR BioGRID; 204852; 6.
DR STRING; 10090.ENSMUSP00000027812; -.
DR iPTMnet; O54829; -.
DR PhosphoSitePlus; O54829; -.
DR MaxQB; O54829; -.
DR PaxDb; O54829; -.
DR PeptideAtlas; O54829; -.
DR PRIDE; O54829; -.
DR ProteomicsDB; 254959; -.
DR Antibodypedia; 620; 238 antibodies from 28 providers.
DR DNASU; 24012; -.
DR Ensembl; ENSMUST00000027812; ENSMUSP00000027812; ENSMUSG00000026527.
DR Ensembl; ENSMUST00000192227; ENSMUSP00000142278; ENSMUSG00000026527.
DR GeneID; 24012; -.
DR KEGG; mmu:24012; -.
DR UCSC; uc007dtk.2; mouse.
DR CTD; 6000; -.
DR MGI; MGI:1346089; Rgs7.
DR VEuPathDB; HostDB:ENSMUSG00000026527; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000156661; -.
DR InParanoid; O54829; -.
DR OrthoDB; 415625at2759; -.
DR PhylomeDB; O54829; -.
DR TreeFam; TF351956; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR BioGRID-ORCS; 24012; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Rgs7; mouse.
DR PRO; PR:O54829; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O54829; protein.
DR Bgee; ENSMUSG00000026527; Expressed in facial nucleus and 145 other tissues.
DR ExpressionAtlas; O54829; baseline and differential.
DR Genevisible; O54829; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0044292; C:dendrite terminus; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
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:0031681; F:G-protein beta-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; IDA:MGI.
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:MGI.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IDA:SynGO.
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..469
FT /note="Regulator of G-protein signaling 7"
FT /id="PRO_0000204197"
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..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49803"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49802"
FT CONFLICT 461
FT /note="R -> S (in Ref. 1; AAC99483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 54792 MW; AE4B91280D87F211 CRC64;
MAQGNNYGQT SNGVADESPN MLVYRKMEDV IARMQDEKNG IPIRTVKSFL SKIPSVFSGS
DIVQWLIKNL TIEDPVEALH LGTLMAAHGY FFPISDHVLT LKDDGTFYRF QTPYFWPSNC
WEPENTDYAV YLCKRTMQNK ARLELADYEA ESLARLQRAF ARKWEFIFMQ AEAQAKVDKK
RDKIERKILD SQERAFWDVH RPVPGCVNTT EVDIKKSSRM RNPHKTRKSV YGLQNDIRSH
SPTHTPTPET KPPTEDELHQ QIKYWQIQLD RHRLKMSKVA DSLLSYTEQY VEYDPFLVPP
DPSNPWLSDD TTFWELEASK EPSQQRVKRW GFGMDEALKD PVGREQFLKF LESEFSSENL
RFWLAVEDLK RRPIREVPSR VQEIWQEFLA PGAPSAINLD SKSYDKTTQN VKEPGRYTFE
DAQEHIYKLM KSDSYPRFIR SSAYQELLQA KRKGKTLTSK RLTSLVQSY
