R7BP_HUMAN
ID R7BP_HUMAN Reviewed; 257 AA.
AC Q6MZT1; B7Z3X1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
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=R7BP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-255.
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-255.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-257, AND VARIANT VAL-255.
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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:0000250|UniProtKB:Q8BQP9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BQP9}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8BQP9}; 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:0000250|UniProtKB:Q8BQP9}.
CC -!- DOMAIN: The nuclear localization signal is both required for nuclear
CC localization and palmitoylation. {ECO:0000250|UniProtKB:Q8BQP9}.
CC -!- PTM: Palmitoylated. Undergoes rapid palmitoylation turnover. De novo
CC and turnover palmitoylation are both mediated by ZDHHC2. Palmitoylation
CC regulates the cell membrane and nuclear shuttling and the regulation of
CC GPCR signaling. Upon depalmitoylation, it is targeted from the plasma
CC membrane into the nucleus. GPCR signaling inhibits depalmitoylation and
CC promotes localization to the plasma membrane.
CC {ECO:0000250|UniProtKB:Q8BQP9}.
CC -!- SIMILARITY: Belongs to the RGS7BP/RGS9BP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK296443; BAH12357.1; -; mRNA.
DR EMBL; AC091862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC035143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471137; EAW51372.1; -; Genomic_DNA.
DR EMBL; BC140707; AAI40708.1; -; mRNA.
DR EMBL; BX640900; CAE45947.1; -; mRNA.
DR CCDS; CCDS34170.1; -.
DR RefSeq; NP_001025046.1; NM_001029875.2.
DR RefSeq; NP_001258819.1; NM_001271890.1.
DR RefSeq; NP_001258820.1; NM_001271891.1.
DR AlphaFoldDB; Q6MZT1; -.
DR SMR; Q6MZT1; -.
DR BioGRID; 134967; 3.
DR IntAct; Q6MZT1; 1.
DR STRING; 9606.ENSP00000334851; -.
DR PhosphoSitePlus; Q6MZT1; -.
DR BioMuta; RGS7BP; -.
DR DMDM; 296452985; -.
DR MassIVE; Q6MZT1; -.
DR PaxDb; Q6MZT1; -.
DR PeptideAtlas; Q6MZT1; -.
DR PRIDE; Q6MZT1; -.
DR ProteomicsDB; 66586; -.
DR TopDownProteomics; Q6MZT1; -.
DR Antibodypedia; 63779; 11 antibodies from 8 providers.
DR DNASU; 401190; -.
DR Ensembl; ENST00000334025.3; ENSP00000334851.2; ENSG00000186479.5.
DR GeneID; 401190; -.
DR KEGG; hsa:401190; -.
DR MANE-Select; ENST00000334025.3; ENSP00000334851.2; NM_001029875.3; NP_001025046.1.
DR UCSC; uc003jtj.5; human.
DR CTD; 401190; -.
DR DisGeNET; 401190; -.
DR GeneCards; RGS7BP; -.
DR HGNC; HGNC:23271; RGS7BP.
DR HPA; ENSG00000186479; Tissue enhanced (brain).
DR MIM; 610890; gene.
DR neXtProt; NX_Q6MZT1; -.
DR OpenTargets; ENSG00000186479; -.
DR PharmGKB; PA162401279; -.
DR VEuPathDB; HostDB:ENSG00000186479; -.
DR eggNOG; ENOG502QPUF; Eukaryota.
DR GeneTree; ENSGT00940000153725; -.
DR HOGENOM; CLU_112711_0_0_1; -.
DR InParanoid; Q6MZT1; -.
DR OMA; MRDMKNL; -.
DR OrthoDB; 1068921at2759; -.
DR PhylomeDB; Q6MZT1; -.
DR TreeFam; TF330985; -.
DR PathwayCommons; Q6MZT1; -.
DR SignaLink; Q6MZT1; -.
DR BioGRID-ORCS; 401190; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; RGS7BP; human.
DR GenomeRNAi; 401190; -.
DR Pharos; Q6MZT1; Tbio.
DR PRO; PR:Q6MZT1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q6MZT1; protein.
DR Bgee; ENSG00000186479; Expressed in lateral nuclear group of thalamus and 122 other tissues.
DR Genevisible; Q6MZT1; HS.
DR GO; GO:0099031; C:anchored component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
DR GO; GO:0044327; C:dendritic spine head; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IEA:Ensembl.
DR InterPro; IPR026512; RGS7BP/RGS9BP.
DR PANTHER; PTHR21029; PTHR21029; 1.
PE 2: Evidence at transcript 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_0000287595"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..196
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 176..196
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"
FT VARIANT 255
FT /note="I -> V (in dbSNP:rs889248)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_032334"
SQ SEQUENCE 257 AA; 28962 MW; 889F690C6DCC40F5 CRC64;
MSSAPNGRKK RPSRSTRSSI FQISKPPLQS GDWERRGSGS ESAHKTQRAL DDCKMLVQEF
NTQVALYREL VISIGDVSVS CPSLRAEMHK TRTKGCEMAR QAHQKLAAIS GPEDGEIHPE
ICRLYIQLQC CLEMYTTEML KSICLLGSLQ FHRKGKEPGG GTKSLDCKIE ESAETPALED
SSSSPVDSQQ HSWQVSTDIE NTERDMREMK NLLSKLRETM PLPLKNQDDS SLLNLTPYPL
VRRRKRRFFG LCCLISS