ID RGS3_HUMAN Reviewed; 1198 AA. AC P49796; A6NHA0; A8K0V1; B3KUB2; Q5VXB8; Q5VXC1; Q5VZ05; Q5VZ06; Q6ZRM5; AC Q8IUQ1; Q8NC47; Q8NFN4; Q8NFN5; Q8NFN6; Q8TD59; Q8TD68; Q8WV02; Q8WXA0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 27-MAR-2024, entry version 226. DE RecName: Full=Regulator of G-protein signaling 3; DE Short=RGP3; DE Short=RGS3; GN Name=RGS3; 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 [MRNA] (ISOFORM 1), AND FUNCTION. RX PubMed=8602223; DOI=10.1038/379742a0; RA Druey K.M., Blumer K.J., Kang V.H., Kehrl J.H.; RT "Inhibition of G-protein-mediated MAP kinase activation by a new mammalian RT gene family."; RL Nature 379:742-746(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 8), AND NUCLEOTIDE SEQUENCE RP [MRNA] OF 105-1198 (ISOFORM 1). RX PubMed=12036301; DOI=10.1006/geno.2002.6773; RA Kehrl J.H., Srikumar D., Harrison K., Wilson G.L., Shi C.S.; RT "Additional 5' exons in the RGS3 locus generate multiple mRNA transcripts, RT one of which accounts for the origin of human PDZ-RGS3."; RL Genomics 79:860-868(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 5 AND 9). RC TISSUE=Amygdala, and Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 4). RA Chatterjee T.K., Fisher R.A.; RT "Human PDZ-RGS3."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND PARTIAL NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). RC TISSUE=Brain, and Kidney; 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 [9] RP FUNCTION, INTERACTION WITH GNA11 AND GNA13, AND SUBCELLULAR LOCATION. RX PubMed=9858594; DOI=10.1128/mcb.19.1.714; RA Dulin N.O., Sorokin A., Reed E., Elliott S., Kehrl J.H., Dunn M.J.; RT "RGS3 inhibits G protein-mediated signaling via translocation to the RT membrane and binding to Galpha11."; RL Mol. Cell. Biol. 19:714-723(1999). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10749886; DOI=10.1074/jbc.m910079199; RA Dulin N.O., Pratt P., Tiruppathi C., Niu J., Voyno-Yasenetskaya T., RA Dunn M.J.; RT "Regulator of G protein signaling RGS3T is localized to the nucleus and RT induces apoptosis."; RL J. Biol. Chem. 275:21317-21323(2000). RN [11] RP FUNCTION, INTERACTION WITH HETERODIMERIC GNB1-GNG2, AND SUBCELLULAR RP LOCATION. RX PubMed=11294858; DOI=10.1074/jbc.m100089200; RA Shi C.-S., Lee S.B., Sinnarajah S., Dessauer C.W., Rhee S.G., Kehrl J.H.; RT "Regulator of G-protein signaling 3 (RGS3) inhibits G-beta1/gamma2-induced RT inositol phosphate production, mitogen-activated protein kinase activation, RT and Akt activation."; RL J. Biol. Chem. 276:24293-24300(2001). RN [12] RP ISGYLATION. RX PubMed=16884686; DOI=10.1016/j.bbrc.2006.07.076; RA Takeuchi T., Inoue S., Yokosawa H.; RT "Identification and Herc5-mediated ISGylation of novel target proteins."; RL Biochem. Biophys. Res. Commun. 348:473-477(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Prostate cancer; RX PubMed=17487921; DOI=10.1002/elps.200600782; RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; RT "Toward a global characterization of the phosphoproteome in prostate cancer RT cells: identification of phosphoproteins in the LNCaP cell line."; RL Electrophoresis 28:2027-2034(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-943, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-448, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: Down-regulates signaling from heterotrimeric G-proteins by CC increasing the GTPase activity of the alpha subunits, thereby driving CC them into their inactive GDP-bound form. Down-regulates G-protein- CC mediated release of inositol phosphates and activation of MAP kinases. CC {ECO:0000269|PubMed:10749886, ECO:0000269|PubMed:11294858, CC ECO:0000269|PubMed:8602223, ECO:0000269|PubMed:9858594}. CC -!- SUBUNIT: Binds EFNB1 and EFNB2 (By similarity). Binds the GNB1-GNG2 CC heterodimer. {ECO:0000250}. CC -!- INTERACTION: CC P49796; Q96AP0: ACD; NbExp=2; IntAct=EBI-2107809, EBI-717666; CC P49796; O15162: PLSCR1; NbExp=3; IntAct=EBI-2107809, EBI-740019; CC P49796-4; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12006708, EBI-3867333; CC P49796-8; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-10211517, EBI-739467; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9858594}. Nucleus CC {ECO:0000269|PubMed:10749886}. Cell membrane CC {ECO:0000269|PubMed:9858594}; Peripheral membrane protein CC {ECO:0000269|PubMed:9858594}. Note=Long isoforms are cytoplasmic and CC associated with the plasma membrane (PubMed:9858594). Short isoforms CC are nuclear (PubMed:10749886). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=3; CC IsoId=P49796-3; Sequence=Displayed; CC Name=1; CC IsoId=P49796-1; Sequence=VSP_013958; CC Name=2; Synonyms=RGS3T; CC IsoId=P49796-2; Sequence=VSP_005662; CC Name=4; Synonyms=1; CC IsoId=P49796-4; Sequence=VSP_013959, VSP_013963; CC Name=5; CC IsoId=P49796-5; Sequence=VSP_013961, VSP_013962, VSP_013964, CC VSP_013965; CC Name=6; Synonyms=C2PA-RGS3; CC IsoId=P49796-6; Sequence=VSP_013960; CC Name=7; CC IsoId=P49796-7; Sequence=VSP_047029; CC Name=8; Synonyms=RGS3S; CC IsoId=P49796-8; Sequence=VSP_047029, VSP_053533; CC Name=9; CC IsoId=P49796-9; Sequence=VSP_013959, VSP_013963, VSP_054690; CC -!- PTM: Phosphorylated by cyclic GMP-dependent protein kinase. CC {ECO:0000250}. CC -!- PTM: ISGylated. {ECO:0000305|PubMed:16884686}. CC -!- MISCELLANEOUS: [Isoform 2]: Nuclear. {ECO:0000269|PubMed:10749886}. 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; U27655; AAC50394.1; -; mRNA. DR EMBL; AF490838; AAM33253.1; -; mRNA. DR EMBL; AF490839; AAM33254.1; -; mRNA. DR EMBL; AF490840; AAM33255.1; -; mRNA. DR EMBL; AK074977; BAC11328.1; -; mRNA. DR EMBL; AK096840; BAG53374.1; -; mRNA. DR EMBL; AK128127; BAC87285.1; -; mRNA. DR EMBL; AK289666; BAF82355.1; -; mRNA. DR EMBL; AF493927; AAM12641.1; -; mRNA. DR EMBL; AF493941; AAM12655.1; -; mRNA. DR EMBL; AY585192; AAT79495.1; -; mRNA. DR EMBL; AF463495; AAL68829.1; -; Genomic_DNA. DR EMBL; AL137066; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL162727; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359455; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87388.1; -; Genomic_DNA. DR EMBL; CH471090; EAW87391.1; -; Genomic_DNA. DR EMBL; CH471090; EAW87393.1; -; Genomic_DNA. DR EMBL; BC019039; AAH19039.3; -; mRNA. DR EMBL; BC042555; AAH42555.1; -; mRNA. DR CCDS; CCDS35113.1; -. [P49796-5] DR CCDS; CCDS43869.1; -. [P49796-6] DR CCDS; CCDS65111.1; -. [P49796-9] DR CCDS; CCDS6797.1; -. [P49796-4] DR CCDS; CCDS6798.1; -. [P49796-1] DR PIR; S78089; S78089. DR RefSeq; NP_001263189.1; NM_001276260.1. [P49796-1] DR RefSeq; NP_001263190.1; NM_001276261.1. [P49796-9] DR RefSeq; NP_001263191.1; NM_001276262.1. DR RefSeq; NP_001269851.1; NM_001282922.1. [P49796-1] DR RefSeq; NP_001269852.1; NM_001282923.1. DR RefSeq; NP_060260.3; NM_017790.4. [P49796-5] DR RefSeq; NP_570613.2; NM_130795.3. [P49796-4] DR RefSeq; NP_602299.1; NM_134427.2. DR RefSeq; NP_652759.3; NM_144488.5. [P49796-6] DR RefSeq; NP_652760.2; NM_144489.3. DR RefSeq; XP_006717282.1; XM_006717219.2. DR RefSeq; XP_006717289.1; XM_006717226.2. DR RefSeq; XP_006717293.1; XM_006717230.3. DR RefSeq; XP_011517198.1; XM_011518896.1. DR RefSeq; XP_011517199.1; XM_011518897.2. DR RefSeq; XP_011517200.1; XM_011518898.1. DR RefSeq; XP_011517202.1; XM_011518900.1. DR RefSeq; XP_011517203.1; XM_011518901.1. DR RefSeq; XP_016870494.1; XM_017015005.1. DR RefSeq; XP_016870495.1; XM_017015006.1. DR PDB; 2F5Y; X-ray; 2.39 A; A/B=300-384. DR PDB; 2OJ4; X-ray; 2.30 A; A=1064-1190. DR PDB; 3FBK; X-ray; 2.00 A; A/B=134-276. DR PDBsum; 2F5Y; -. DR PDBsum; 2OJ4; -. DR PDBsum; 3FBK; -. DR AlphaFoldDB; P49796; -. DR BMRB; P49796; -. DR SMR; P49796; -. DR BioGRID; 111930; 64. DR IntAct; P49796; 56. DR MINT; P49796; -. DR STRING; 9606.ENSP00000363255; -. DR GlyGen; P49796; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P49796; -. DR PhosphoSitePlus; P49796; -. DR SwissPalm; P49796; -. DR BioMuta; RGS3; -. DR DMDM; 67477383; -. DR EPD; P49796; -. DR jPOST; P49796; -. DR MassIVE; P49796; -. DR MaxQB; P49796; -. DR PaxDb; 9606-ENSP00000363255; -. DR PeptideAtlas; P49796; -. DR ProteomicsDB; 3705; -. DR ProteomicsDB; 56123; -. [P49796-3] DR ProteomicsDB; 56124; -. [P49796-1] DR ProteomicsDB; 56125; -. [P49796-2] DR ProteomicsDB; 56126; -. [P49796-4] DR ProteomicsDB; 56127; -. [P49796-5] DR ProteomicsDB; 56128; -. [P49796-6] DR ProteomicsDB; 65662; -. DR Antibodypedia; 15339; 195 antibodies from 30 providers. DR DNASU; 5998; -. DR Ensembl; ENST00000317613.10; ENSP00000312844.6; ENSG00000138835.24. [P49796-5] DR Ensembl; ENST00000343817.9; ENSP00000340284.5; ENSG00000138835.24. [P49796-4] DR Ensembl; ENST00000350696.9; ENSP00000259406.7; ENSG00000138835.24. [P49796-3] DR Ensembl; ENST00000374134.7; ENSP00000363249.3; ENSG00000138835.24. [P49796-1] DR Ensembl; ENST00000374140.6; ENSP00000363255.2; ENSG00000138835.24. [P49796-3] DR Ensembl; ENST00000394646.7; ENSP00000378141.3; ENSG00000138835.24. [P49796-9] DR Ensembl; ENST00000462143.5; ENSP00000420356.1; ENSG00000138835.24. [P49796-1] DR GeneID; 5998; -. DR KEGG; hsa:5998; -. DR UCSC; uc004bhq.5; human. [P49796-3] DR AGR; HGNC:9999; -. DR CTD; 5998; -. DR DisGeNET; 5998; -. DR GeneCards; RGS3; -. DR HGNC; HGNC:9999; RGS3. DR HPA; ENSG00000138835; Tissue enhanced (choroid). DR MIM; 602189; gene. DR neXtProt; NX_P49796; -. DR OpenTargets; ENSG00000138835; -. DR PharmGKB; PA34374; -. DR VEuPathDB; HostDB:ENSG00000138835; -. DR eggNOG; KOG3589; Eukaryota. DR GeneTree; ENSGT00940000154416; -. DR HOGENOM; CLU_005574_0_0_1; -. DR InParanoid; P49796; -. DR OMA; CVDLAHE; -. DR OrthoDB; 22856at2759; -. DR PhylomeDB; P49796; -. DR TreeFam; TF351952; -. DR PathwayCommons; P49796; -. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR SignaLink; P49796; -. DR BioGRID-ORCS; 5998; 17 hits in 1146 CRISPR screens. DR ChiTaRS; RGS3; human. DR EvolutionaryTrace; P49796; -. DR GeneWiki; RGS3; -. DR GenomeRNAi; 5998; -. DR Pharos; P49796; Tbio. DR PRO; PR:P49796; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P49796; Protein. DR Bgee; ENSG00000138835; Expressed in apex of heart and 194 other cell types or tissues. DR ExpressionAtlas; P49796; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc. DR GO; GO:0003924; F:GTPase activity; TAS:Reactome. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome. DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW. DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc. DR CDD; cd08685; C2_RGS-like; 1. DR CDD; cd00992; PDZ_signaling; 1. DR CDD; cd08713; RGS_RGS3; 1. DR Gene3D; 1.10.196.10; -; 2. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR016137; RGS. DR InterPro; IPR034951; RGS_RGS3. DR InterPro; IPR036305; RGS_sf. DR InterPro; IPR024066; RGS_subdom1/3. DR InterPro; IPR044926; RGS_subdomain_2. DR PANTHER; PTHR46848; REGULATOR OF G-PROTEIN SIGNALING 3; 1. DR PANTHER; PTHR46848:SF1; REGULATOR OF G-PROTEIN SIGNALING 3; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00615; RGS; 1. DR PRINTS; PR01301; RGSPROTEIN. DR SMART; SM00239; C2; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00315; RGS; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50132; RGS; 1. DR Genevisible; P49796; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Membrane; KW Methylation; Nucleus; Phosphoprotein; Reference proteome; KW Signal transduction inhibitor; Ubl conjugation. FT CHAIN 1..1198 FT /note="Regulator of G-protein signaling 3" FT /id="PRO_0000204182" FT DOMAIN 137..256 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 299..376 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 1073..1198 FT /note="RGS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171" FT REGION 669..933 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1007..1026 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1032..1056 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 680..697 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 710..724 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 725..750 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 753..777 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 876..906 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1008..1026 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 448 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 674 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 943 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 946 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9DC04" FT MOD_RES 978 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9DC04" FT MOD_RES 1007 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9DC04" FT VAR_SEQ 1..1027 FT /note="MPVIPALWEVEMGRSQGQEIETILANRSHSDSTPLPNFLSGSHRPECCTCRL FT LTASGAQDSLPFGRRLYSGPWRSCEEVCHVSVLSVLSTSCGLSLSLPIFPGWMEWLSPD FT IALPRRDEWTQTSPARKRITHAKVQGAGQLRLSIDAQDRVLLLHIIEGKGLISKQPGTC FT DPYVKISLIPEDSRLRHQKTQTVPDCRDPAFHEHFFFPVQEEDDQKRLLVTVWNRASQS FT RQSGLIGCMSFGVKSLLTPDKEISGWYYLLGEHLGRTKHLKVARRRLRPLRDPLLRMPG FT GGDTENGKKLKITIPRGKDGFGFTICCDSPVRVQAVDSGGPAERAGLQQLDTVLQLNER FT PVEHWKCVELAHEIRSCPSEIILLVWRMVPQVKPGPDGGVLRRASCKSTHDLQSPPNKR FT EKNCTHGVQARPEQRHSCHLVCDSSDGLLLGGWERYTEVAKRGGQHTLPALSRATAPTD FT PNYIILAPLNPGSQLLRPVYQEDTIPEESGSPSKGKSYTGLGKKSRLMKTVQTMKGHGN FT YQNCPVVRPHATHSSYGTYVTLAPKVLVFPVFVQPLDLCNPARTLLLSEELLLYEGRNK FT AAEVTLFAYSDLLLFTKEDEPGRCDVLRNPLYLQSVKLQEGSSEDLKFCVLYLAEKAEC FT LFTLEAHSQEQKKRVCWCLSENIAKQQQLAASPPDSKMFETEADEKREMALEEGKGPGA FT EDSPPSKEPSPGQELPPGQDLPPNKDSPSGQEPAPSQEPLSSKDSATSEGSPPGPDAPP FT SKDVPPCQEPPPAQDLSPCQDLPAGQEPLPHQDPLLTKDLPAIQESPTRDLPPCQDLPP FT SQVSLPAKALTEDTMSSGDLLAATGDPPAAPRPAFVIPEVRLDSTYSQKAGAEQGCSGD FT EEDAEEAEEVEEGEEGEEDEDEDTSDDNYGERSEAKRSSMIETGQGAEGGLSLRVQNSL FT RRRTHSEGSLLQEPRGPCFASDTTLHCSDGEGAASTWGMPSPSTLKKELGRNGGSMHHL FT SLFFTGHRKMSGADTVGDDDEASRKRKSKNL -> MVTRRPVTNSWDWLPAGAAPEAVP FT CRHMPLSRLPLRVGQKEFFFPLPLLVPPISWLLLSESQPRLVPGSPVIRPGFQRACVAA FT ACTVAARCPGRGVGDRSQSGASYRPICGPKVGGPTEMLRGMYLTRNGNLQRRHTMKE FT (in isoform 7 and isoform 8)" FT /evidence="ECO:0000303|PubMed:12036301" FT /id="VSP_047029" FT VAR_SEQ 1..992 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_005662" FT VAR_SEQ 1..679 FT /note="Missing (in isoform 1)" FT /evidence="ECO:0000303|PubMed:12036301, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:8602223, FT ECO:0000303|Ref.5" FT /id="VSP_013958" FT VAR_SEQ 1..281 FT /note="Missing (in isoform 4 and isoform 9)" FT /evidence="ECO:0000303|PubMed:12036301, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8602223, ECO:0000303|Ref.5" FT /id="VSP_013959" FT VAR_SEQ 1..112 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013961" FT VAR_SEQ 1..104 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:12036301" FT /id="VSP_013960" FT VAR_SEQ 113..138 FT /note="ALPRRDEWTQTSPARKRITHAKVQGA -> MERSLHRVSLGSRRAHPDLSFY FT LTTF (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013962" FT VAR_SEQ 282..299 FT /note="PLLRMPGGGDTENGKKLK -> MNRFNGLCKVCSERRYRQ (in isoform FT 4 and isoform 9)" FT /evidence="ECO:0000303|PubMed:12036301, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8602223, ECO:0000303|Ref.5" FT /id="VSP_013963" FT VAR_SEQ 679..1004 FT /note="Missing (in isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054690" FT VAR_SEQ 680..714 FT /note="MFETEADEKREMALEEGKGPGAEDSPPSKEPSPGQ -> KLHPFGSLQQEMG FT PVNSTNATQDRSFTSPGQTLIG (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013964" FT VAR_SEQ 715..1198 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013965" FT VAR_SEQ 1198 FT /note="L -> LDYKDDDDK (in isoform 8)" FT /evidence="ECO:0000303|PubMed:12036301" FT /id="VSP_053533" FT VARIANT 129 FT /note="R -> K (in dbSNP:rs16933949)" FT /id="VAR_051794" FT VARIANT 809 FT /note="R -> Q (in dbSNP:rs41305473)" FT /id="VAR_061769" FT CONFLICT 170 FT /note="C -> W (in Ref. 2; AAM33254)" FT /evidence="ECO:0000305" FT CONFLICT 206 FT /note="F -> S (in Ref. 3; BAC11328)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="T -> A (in Ref. 2; AAM33254)" FT /evidence="ECO:0000305" FT CONFLICT 462 FT /note="A -> V (in Ref. 4; AAL68829)" FT /evidence="ECO:0000305" FT CONFLICT 585 FT /note="A -> V (in Ref. 2; AAM33255)" FT /evidence="ECO:0000305" FT CONFLICT 632 FT /note="C -> R (in Ref. 3; BAC11328)" FT /evidence="ECO:0000305" FT CONFLICT 705 FT /note="Missing (in Ref. 2; AAM33254)" FT /evidence="ECO:0000305" FT CONFLICT 725 FT /note="N -> S (in Ref. 8; AAH42555)" FT /evidence="ECO:0000305" FT CONFLICT 873 FT /note="Q -> H (in Ref. 2; AAM33254)" FT /evidence="ECO:0000305" FT CONFLICT 883..884 FT /note="EE -> KQ (in Ref. 2; AAM33254)" FT /evidence="ECO:0000305" FT CONFLICT 984 FT /note="K -> R (in Ref. 5; AAM12641)" FT /evidence="ECO:0000305" FT CONFLICT 1127 FT /note="A -> V (in Ref. 2; AAM33253)" FT /evidence="ECO:0000305" FT STRAND 140..161 FT /evidence="ECO:0007829|PDB:3FBK" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:3FBK" FT STRAND 172..180 FT /evidence="ECO:0007829|PDB:3FBK" FT STRAND 200..208 FT /evidence="ECO:0007829|PDB:3FBK" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:3FBK" FT STRAND 216..224 FT /evidence="ECO:0007829|PDB:3FBK" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:3FBK" FT STRAND 233..241 FT /evidence="ECO:0007829|PDB:3FBK" FT HELIX 242..245 FT /evidence="ECO:0007829|PDB:3FBK" FT STRAND 252..257 FT /evidence="ECO:0007829|PDB:3FBK" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:3FBK" FT STRAND 299..303 FT /evidence="ECO:0007829|PDB:2F5Y" FT STRAND 310..314 FT /evidence="ECO:0007829|PDB:2F5Y" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:2F5Y" FT STRAND 320..324 FT /evidence="ECO:0007829|PDB:2F5Y" FT HELIX 329..333 FT /evidence="ECO:0007829|PDB:2F5Y" FT STRAND 340..344 FT /evidence="ECO:0007829|PDB:2F5Y" FT HELIX 354..362 FT /evidence="ECO:0007829|PDB:2F5Y" FT STRAND 365..374 FT /evidence="ECO:0007829|PDB:2F5Y" FT HELIX 1066..1070 FT /evidence="ECO:0007829|PDB:2OJ4" FT HELIX 1074..1078 FT /evidence="ECO:0007829|PDB:2OJ4" FT HELIX 1081..1093 FT /evidence="ECO:0007829|PDB:2OJ4" FT HELIX 1097..1109 FT /evidence="ECO:0007829|PDB:2OJ4" FT HELIX 1115..1129 FT /evidence="ECO:0007829|PDB:2OJ4" FT HELIX 1142..1150 FT /evidence="ECO:0007829|PDB:2OJ4" FT TURN 1157..1160 FT /evidence="ECO:0007829|PDB:2OJ4" FT HELIX 1161..1173 FT /evidence="ECO:0007829|PDB:2OJ4" FT HELIX 1175..1181 FT /evidence="ECO:0007829|PDB:2OJ4" FT HELIX 1183..1186 FT /evidence="ECO:0007829|PDB:2OJ4" FT TURN 1187..1189 FT /evidence="ECO:0007829|PDB:2OJ4" SQ SEQUENCE 1198 AA; 132336 MW; E615DA49022EFFE4 CRC64; MPVIPALWEV EMGRSQGQEI ETILANRSHS DSTPLPNFLS GSHRPECCTC RLLTASGAQD SLPFGRRLYS GPWRSCEEVC HVSVLSVLST SCGLSLSLPI FPGWMEWLSP DIALPRRDEW TQTSPARKRI THAKVQGAGQ LRLSIDAQDR VLLLHIIEGK GLISKQPGTC DPYVKISLIP EDSRLRHQKT QTVPDCRDPA FHEHFFFPVQ EEDDQKRLLV TVWNRASQSR QSGLIGCMSF GVKSLLTPDK EISGWYYLLG EHLGRTKHLK VARRRLRPLR DPLLRMPGGG DTENGKKLKI TIPRGKDGFG FTICCDSPVR VQAVDSGGPA ERAGLQQLDT VLQLNERPVE HWKCVELAHE IRSCPSEIIL LVWRMVPQVK PGPDGGVLRR ASCKSTHDLQ SPPNKREKNC THGVQARPEQ RHSCHLVCDS SDGLLLGGWE RYTEVAKRGG QHTLPALSRA TAPTDPNYII LAPLNPGSQL LRPVYQEDTI PEESGSPSKG KSYTGLGKKS RLMKTVQTMK GHGNYQNCPV VRPHATHSSY GTYVTLAPKV LVFPVFVQPL DLCNPARTLL LSEELLLYEG RNKAAEVTLF AYSDLLLFTK EDEPGRCDVL RNPLYLQSVK LQEGSSEDLK FCVLYLAEKA ECLFTLEAHS QEQKKRVCWC LSENIAKQQQ LAASPPDSKM FETEADEKRE MALEEGKGPG AEDSPPSKEP SPGQELPPGQ DLPPNKDSPS GQEPAPSQEP LSSKDSATSE GSPPGPDAPP SKDVPPCQEP PPAQDLSPCQ DLPAGQEPLP HQDPLLTKDL PAIQESPTRD LPPCQDLPPS QVSLPAKALT EDTMSSGDLL AATGDPPAAP RPAFVIPEVR LDSTYSQKAG AEQGCSGDEE DAEEAEEVEE GEEGEEDEDE DTSDDNYGER SEAKRSSMIE TGQGAEGGLS LRVQNSLRRR THSEGSLLQE PRGPCFASDT TLHCSDGEGA ASTWGMPSPS TLKKELGRNG GSMHHLSLFF TGHRKMSGAD TVGDDDEASR KRKSKNLAKD MKNKLGIFRR RNESPGAPPA GKADKMMKSF KPTSEEALKW GESLEKLLVH KYGLAVFQAF LRTEFSEENL EFWLACEDFK KVKSQSKMAS KAKKIFAEYI AIQACKEVNL DSYTREHTKD NLQSVTRGCF DLAQKRIFGL MEKDSYPRFL RSDLYLDLIN QKKMSPPL //