R7BP_MOUSE
ID R7BP_MOUSE Reviewed; 257 AA.
AC Q8BQP9; Q0VF69; Q3UVC4; Q8CBD6; Q9CTP1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Regulator of G-protein signaling 7-binding protein;
DE AltName: Full=R7 family-binding protein;
GN Name=Rgs7bp; Synonyms=D13Bwg1146e, R7bp;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INTERACTION WITH RGS6; RGS7; RGS9 AND RGS11, PALMITOYLATION AT
RP CYS-252 AND CYS-253, AND MUTAGENESIS OF CYS-252 AND CYS-253.
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP TISSUE SPECIFICITY, AND INTERACTION WITH RGS6; RGS7; RGS9 AND RGS11.
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 FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, PALMITOYLATION
RP AT CYS-252 AND CYS-253, AND MUTAGENESIS OF ARG-243; ARG-246 AND
RP 252-CYS-CYS-253.
RX PubMed=16574655; DOI=10.1074/jbc.m600749200;
RA Song J.H., Waataja J.J., Martemyanov K.A.;
RT "Subcellular targeting of RGS9-2 is controlled by multiple molecular
RT determinants on its membrane anchor, R7BP.";
RL J. Biol. Chem. 281:15361-15369(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL DOMAIN, AND
RP MUTAGENESIS OF 242-ARG--ARG-247.
RX PubMed=16867977; DOI=10.1074/jbc.m604428200;
RA Drenan R.M., Doupnik C.A., Jayaraman M., Buchwalter A.L., Kaltenbronn K.M.,
RA Huettner J.E., Linder M.E., Blumer K.J.;
RT "R7BP augments the function of RGS7*Gbeta5 complexes by a plasma membrane-
RT targeting mechanism.";
RL J. Biol. Chem. 281:28222-28231(2006).
RN [7]
RP FUNCTION.
RX PubMed=17158100; DOI=10.1074/jbc.m610518200;
RA Anderson G.R., Semenov A., Song J.H., Martemyanov K.A.;
RT "The membrane anchor R7BP controls the proteolytic stability of the
RT striatal specific RGS protein, RGS9-2.";
RL J. Biol. Chem. 282:4772-4781(2007).
RN [8]
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).
RN [9]
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:0000269|PubMed:15897264, ECO:0000269|PubMed:16574655,
CC ECO:0000269|PubMed:16867977, ECO:0000269|PubMed:17158100}.
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:0000269|PubMed:15632198, ECO:0000269|PubMed:15897264}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15897264,
CC ECO:0000269|PubMed:16574655, ECO:0000269|PubMed:16867977,
CC ECO:0000269|PubMed:21343290}. Cytoplasm {ECO:0000269|PubMed:15897264,
CC ECO:0000269|PubMed:16574655}. Cell membrane
CC {ECO:0000269|PubMed:15897264, ECO:0000269|PubMed:16574655,
CC ECO:0000269|PubMed:16867977, ECO:0000269|PubMed:21343290}; Lipid-anchor
CC {ECO:0000269|PubMed:15897264, ECO:0000269|PubMed:16867977}.
CC Note=Shuttling between the plasma membrane, the cytoplasm and the
CC nucleus is regulated by palmitoylation (PubMed:15897264,
CC PubMed:21343290). {ECO:0000269|PubMed:15897264,
CC ECO:0000269|PubMed:21343290}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the central nervous
CC system including the retina but not in other non-neuronal tissues (at
CC protein level). {ECO:0000269|PubMed:15632198,
CC ECO:0000269|PubMed:15897264}.
CC -!- DOMAIN: The nuclear localization signal is both required for nuclear
CC localization and palmitoylation. {ECO:0000269|PubMed:16867977}.
CC -!- PTM: Palmitoylated (PubMed:15897264, PubMed:16574655, PubMed:21343290).
CC Undergoes rapid palmitoylation turnover (PubMed:21343290). De novo and
CC turnover palmitoylation are both mediated by ZDHHC2 (PubMed:21343290).
CC Palmitoylation regulates the cell membrane and nuclear shuttling and
CC the regulation of GPCR signaling (PubMed:15897264, PubMed:16574655,
CC PubMed:16867977, PubMed:21343290). Upon depalmitoylation, it is
CC targeted from the plasma membrane into the nucleus (PubMed:15897264,
CC PubMed:16574655). GPCR signaling inhibits depalmitoylation and promotes
CC localization to the plasma membrane (PubMed:21343290).
CC {ECO:0000269|PubMed:15897264, ECO:0000269|PubMed:16574655,
CC ECO:0000269|PubMed:16867977, ECO:0000269|PubMed:21343290}.
CC -!- SIMILARITY: Belongs to the RGS7BP/RGS9BP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29358.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ104214; AAZ09201.1; -; mRNA.
DR EMBL; AK020910; BAB32250.1; -; mRNA.
DR EMBL; AK036240; BAC29358.1; ALT_FRAME; mRNA.
DR EMBL; AK046733; BAC32849.1; -; mRNA.
DR EMBL; AK137417; BAE23346.1; -; mRNA.
DR EMBL; BC118957; AAI18958.1; -; mRNA.
DR CCDS; CCDS36774.1; -.
DR RefSeq; NP_084155.2; NM_029879.2.
DR AlphaFoldDB; Q8BQP9; -.
DR SMR; Q8BQP9; -.
DR BioGRID; 206866; 6.
DR STRING; 10090.ENSMUSP00000066614; -.
DR iPTMnet; Q8BQP9; -.
DR PhosphoSitePlus; Q8BQP9; -.
DR SwissPalm; Q8BQP9; -.
DR MaxQB; Q8BQP9; -.
DR PaxDb; Q8BQP9; -.
DR PeptideAtlas; Q8BQP9; -.
DR PRIDE; Q8BQP9; -.
DR ProteomicsDB; 255062; -.
DR Antibodypedia; 63779; 11 antibodies from 8 providers.
DR DNASU; 52882; -.
DR Ensembl; ENSMUST00000063551; ENSMUSP00000066614; ENSMUSG00000021719.
DR GeneID; 52882; -.
DR KEGG; mmu:52882; -.
DR UCSC; uc007rtp.1; mouse.
DR CTD; 401190; -.
DR MGI; MGI:106334; Rgs7bp.
DR VEuPathDB; HostDB:ENSMUSG00000021719; -.
DR eggNOG; ENOG502QPUF; Eukaryota.
DR GeneTree; ENSGT00940000153725; -.
DR HOGENOM; CLU_112711_0_0_1; -.
DR InParanoid; Q8BQP9; -.
DR OMA; MRDMKNL; -.
DR OrthoDB; 1068921at2759; -.
DR PhylomeDB; Q8BQP9; -.
DR TreeFam; TF330985; -.
DR BioGRID-ORCS; 52882; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Rgs7bp; mouse.
DR PRO; PR:Q8BQP9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BQP9; protein.
DR Bgee; ENSMUSG00000021719; Expressed in caudate-putamen and 166 other tissues.
DR Genevisible; Q8BQP9; MM.
DR GO; GO:0099031; C:anchored component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0044327; C:dendritic spine head; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IDA:SynGO.
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_0000287596"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..247
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:16574655,
FT ECO:0000269|PubMed:16867977"
FT LIPID 252
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:15897264,
FT ECO:0000305|PubMed:16574655"
FT LIPID 253
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:15897264,
FT ECO:0000305|PubMed:16574655"
FT MUTAGEN 242..247
FT /note="Missing: Abolishes nuclear localization and
FT palmitoylation."
FT /evidence="ECO:0000269|PubMed:16867977"
FT MUTAGEN 243
FT /note="R->E: Abolishes nuclear localization; when
FT associated with E-246."
FT /evidence="ECO:0000269|PubMed:16574655"
FT MUTAGEN 246
FT /note="R->E: Abolishes nuclear localization; when
FT associated with E-243."
FT /evidence="ECO:0000269|PubMed:16574655"
FT MUTAGEN 252..253
FT /note="CC->AA: Abolishes palmitoylation."
FT /evidence="ECO:0000269|PubMed:16574655"
FT MUTAGEN 252
FT /note="C->S: Strongly reduces palmitoylation and its
FT ability to regulate GPCR signaling. Abolishes
FT palmitoylation and its ability to regulate GPCR signaling;
FT when associated with S-253."
FT /evidence="ECO:0000269|PubMed:15897264"
FT MUTAGEN 253
FT /note="C->S: Strongly reduces palmitoylation and its
FT ability to regulate GPCR signaling. Abolishes
FT palmitoylation and its ability to regulate GPCR signaling;
FT when associated with S-252."
FT /evidence="ECO:0000269|PubMed:15897264"
FT CONFLICT 15
FT /note="S -> A (in Ref. 2; BAB32250)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="Q -> R (in Ref. 2; BAB32250)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="S -> F (in Ref. 2; BAB32250)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="E -> Q (in Ref. 2; BAE23346)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="L -> V (in Ref. 2; BAB32250)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="S -> G (in Ref. 3; AAI18958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 29023 MW; 1825969A5E64D544 CRC64;
MSSAPNGRKK RPSRSTRSSI FQISKPPLQS GDWERRGSGS ESAHKTQRAL DDCKMLVQEF
NTQVALYREL VISIGDVSVS CPSLRAEMHK TRTKGCEMAR QAHQKLAAIS GPEDGEIHPE
ICRLYIQLQC CLEMYTTEML KSICLLGSLQ FHRKGKEASG GAKNLDSKIE ENAETPALED
SLSSPLESQQ QCWQVATDIE NTERDMREMK NLLSKLRETM PLPLKNQDDS SLLNLTPYPM
VRRRKRRFFG LCCLVSS
