R7BP_RAT
ID R7BP_RAT Reviewed; 257 AA.
AC Q5FVH8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Regulator of G-protein signaling 7-binding protein;
DE AltName: Full=R7 family-binding protein;
GN Name=Rgs7bp; Synonyms=R7bp;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [2]
RP SUBCELLULAR LOCATION, AND PALMITOYLATION.
RX PubMed=21343290; DOI=10.1074/jbc.m110.193763;
RA Jia L., Linder M.E., Blumer K.J.;
RT "Gi/o signaling and the palmitoyltransferase DHHC2 regulate palmitate
RT cycling and shuttling of RGS7 family-binding protein.";
RL J. Biol. Chem. 286:13695-13703(2011).
CC -!- FUNCTION: Regulator of G protein-coupled receptor (GPCR) signaling.
CC Regulatory subunit of the R7-Gbeta5 complexes that acts by controlling
CC the subcellular location of the R7-Gbeta5 complexes. When
CC palmitoylated, it targets the R7-Gbeta5 complexes to the plasma
CC membrane, leading to inhibit G protein alpha subunits. When it is
CC unpalmitoylated, the R7-Gbeta5 complexes undergo a nuclear/cytoplasmic
CC shuttling. May also act by controlling the proteolytic stability of R7
CC proteins, probably by protecting them from degradation.
CC {ECO:0000250|UniProtKB:Q8BQP9}.
CC -!- SUBUNIT: Interacts with 'R7' family proteins RGS6, RGS7, RGS9 and
CC RGS11. Component of some R7-Gbeta5 complex composed of some R7 protein
CC (RGS6, RGS7, RGS9 or RGS11), Gbeta5 (GNB5) and RGS7BP.
CC {ECO:0000250|UniProtKB:Q8BQP9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21343290}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BQP9}. Cell membrane
CC {ECO:0000269|PubMed:21343290}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q8BQP9}. Note=Shuttling between the plasma
CC membrane, the cytoplasm and the nucleus is regulated by palmitoylation.
CC {ECO:0000269|PubMed:21343290}.
CC -!- DOMAIN: The nuclear localization signal is both required for nuclear
CC localization and palmitoylation. {ECO:0000250|UniProtKB:Q8BQP9}.
CC -!- PTM: Palmitoylated (PubMed:21343290). Undergoes rapid palmitoylation
CC turnover (PubMed:21343290). De novo and turnover palmitoylation are
CC both mediated by ZDHHC2 (PubMed:21343290). Palmitoylation regulates the
CC cell membrane and nuclear shuttling and the regulation of GPCR
CC signaling (By similarity). Upon depalmitoylation, it is targeted from
CC the plasma membrane into the nucleus (By similarity). GPCR signaling
CC inhibits depalmitoylation and promotes localization to the plasma
CC membrane (PubMed:21343290). {ECO:0000250|UniProtKB:Q8BQP9,
CC ECO:0000269|PubMed:21343290}.
CC -!- SIMILARITY: Belongs to the RGS7BP/RGS9BP family. {ECO:0000305}.
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DR EMBL; BC089977; AAH89977.1; -; mRNA.
DR RefSeq; NP_001012347.1; NM_001012347.1.
DR AlphaFoldDB; Q5FVH8; -.
DR SMR; Q5FVH8; -.
DR STRING; 10116.ENSRNOP00000018058; -.
DR SwissPalm; Q5FVH8; -.
DR PaxDb; Q5FVH8; -.
DR PRIDE; Q5FVH8; -.
DR Ensembl; ENSRNOT00000018058; ENSRNOP00000018058; ENSRNOG00000013389.
DR GeneID; 294715; -.
DR KEGG; rno:294715; -.
DR UCSC; RGD:1309360; rat.
DR CTD; 401190; -.
DR RGD; 1309360; Rgs7bp.
DR eggNOG; ENOG502QPUF; Eukaryota.
DR GeneTree; ENSGT00940000153725; -.
DR HOGENOM; CLU_112711_0_0_1; -.
DR InParanoid; Q5FVH8; -.
DR OrthoDB; 1068921at2759; -.
DR PhylomeDB; Q5FVH8; -.
DR TreeFam; TF330985; -.
DR PRO; PR:Q5FVH8; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Genevisible; Q5FVH8; RN.
DR GO; GO:0099031; C:anchored component of postsynaptic density membrane; ISO:RGD.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0044327; C:dendritic spine head; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; ISO:RGD.
DR InterPro; IPR026512; RGS7BP/RGS9BP.
DR PANTHER; PTHR21029; PTHR21029; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Lipoprotein; Membrane; Nucleus; Palmitate;
KW Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..257
FT /note="Regulator of G-protein signaling 7-binding protein"
FT /id="PRO_0000287597"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..247
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 177..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 252
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 253
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 257 AA; 28966 MW; 43312921B56319E9 CRC64;
MSSAPNGRKK RPSRSTRSSI FQISKPPLQS GDWERRGSGS ESAHKTQRAL DDCKMLVQEF
NTQVALYREL VISIGDVSVS CPSLRAEMHK TRTKGCEMAR QAHQKLAAIS GPEDGEIHPE
ICRLYIQLQC CLEMYTTEML KSICLLGSLQ FHRKGKEASG GAKSLDSKIE ENAETPALED
SLSSPLDSQQ QSWQVATDIE NTERDMREMK NLLSKLRETM PLPLKNQDDS SLLNLTPYPM
VRRRKRRFFG LCCLVSS
