ID   RGS8_HUMAN              Reviewed;         180 AA.
AC   P57771; B4DGL9; Q3SYD2;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 1.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Regulator of G-protein signaling 8;
DE            Short=RGS8;
GN   Name=RGS8;
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 2).
RX   PubMed=11318611; DOI=10.1006/geno.2001.6500;
RA   Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
RA   Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
RA   Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
RA   Carpten J.D.;
RT   "Cloning and characterization of 13 novel transcripts and the human RGS8
RT   gene from the 1q25 region encompassing the hereditary prostate cancer
RT   (HPC1) locus.";
RL   Genomics 73:211-222(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 42-173 IN COMPLEX WITH GNAI3,
RP   FUNCTION, AND INTERACTION WITH GNAI3.
RX   PubMed=18434541; DOI=10.1073/pnas.0801508105;
RA   Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J.,
RA   Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A.,
RA   Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.;
RT   "Structural diversity in the RGS domain and its interaction with
RT   heterotrimeric G protein alpha-subunits.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008).
CC   -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades,
CC       including signaling via muscarinic acetylcholine receptor CHRM2 and
CC       dopamine receptor DRD2 (By similarity). Inhibits signal transduction by
CC       increasing the GTPase activity of G protein alpha subunits, thereby
CC       driving them into their inactive GDP-bound form (PubMed:18434541).
CC       Modulates the activity of potassium channels that are activated in
CC       response to DRD2 and CHRM2 signaling (By similarity).
CC       {ECO:0000250|UniProtKB:P49804, ECO:0000269|PubMed:18434541}.
CC   -!- SUBUNIT: Interacts with GNAO1 (By similarity). Interacts with GNAI3.
CC       {ECO:0000250|UniProtKB:P49804, ECO:0000269|PubMed:18434541}.
CC   -!- INTERACTION:
CC       P57771; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10216117, EBI-618309;
CC       P57771-2; Q15834: CCDC85B; NbExp=3; IntAct=EBI-12058229, EBI-739674;
CC       P57771-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12058229, EBI-618309;
CC       P57771-2; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-12058229, EBI-10961706;
CC       P57771-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-12058229, EBI-10171697;
CC       P57771-2; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12058229, EBI-742388;
CC       P57771-2; Q8TAS1-2: UHMK1; NbExp=3; IntAct=EBI-12058229, EBI-12157345;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P49804};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P49804}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:P49804}. Membrane
CC       {ECO:0000250|UniProtKB:P49804}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P49804}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P49804}. Perikaryon
CC       {ECO:0000250|UniProtKB:P49804}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:P49804}. Nucleus {ECO:0000250|UniProtKB:P49804}.
CC       Note=Detected in Purkinje cell soma and dendrites. Associated with
CC       Purkinje cell membranes. Not detected in Purkinje cell nuclei. Detected
CC       in the nucleus after heterologous expression. Recruited to the cell
CC       membrane in the presence of GNAO1. {ECO:0000250|UniProtKB:P49804}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P57771-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P57771-2; Sequence=VSP_036421;
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DR   EMBL; AF297015; AAG45337.1; -; mRNA.
DR   EMBL; AF300649; AAG18443.1; -; mRNA.
DR   EMBL; AK296514; BAG59146.1; -; mRNA.
DR   EMBL; AK294660; BAG57830.1; -; mRNA.
DR   EMBL; AL353778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW91130.1; -; Genomic_DNA.
DR   EMBL; BC069677; AAH69677.1; -; mRNA.
DR   EMBL; BC069718; AAH69718.1; -; mRNA.
DR   EMBL; BC103865; AAI03866.1; -; mRNA.
DR   EMBL; BC103866; AAI03867.1; -; mRNA.
DR   EMBL; BC103867; AAI03868.1; -; mRNA.
DR   CCDS; CCDS1349.1; -. [P57771-2]
DR   CCDS; CCDS41443.1; -. [P57771-1]
DR   RefSeq; NP_001095920.1; NM_001102450.2. [P57771-1]
DR   RefSeq; NP_203131.1; NM_033345.3. [P57771-2]
DR   RefSeq; XP_005245612.1; XM_005245555.3.
DR   RefSeq; XP_011508391.1; XM_011510089.2. [P57771-2]
DR   RefSeq; XP_011508392.1; XM_011510090.2.
DR   RefSeq; XP_016858120.1; XM_017002631.1. [P57771-2]
DR   RefSeq; XP_016858121.1; XM_017002632.1.
DR   RefSeq; XP_016858122.1; XM_017002633.1.
DR   RefSeq; XP_016858123.1; XM_017002634.1.
DR   RefSeq; XP_016858124.1; XM_017002635.1.
DR   RefSeq; XP_016858125.1; XM_017002636.1.
DR   RefSeq; XP_016858126.1; XM_017002637.1.
DR   PDB; 2IHD; X-ray; 1.70 A; A=42-173.
DR   PDB; 2ODE; X-ray; 1.90 A; B/D=42-180.
DR   PDB; 5DO9; X-ray; 2.60 A; B/D/F=42-173.
DR   PDBsum; 2IHD; -.
DR   PDBsum; 2ODE; -.
DR   PDBsum; 5DO9; -.
DR   AlphaFoldDB; P57771; -.
DR   SMR; P57771; -.
DR   BioGRID; 124512; 12.
DR   DIP; DIP-59093N; -.
DR   IntAct; P57771; 10.
DR   STRING; 9606.ENSP00000258302; -.
DR   BindingDB; P57771; -.
DR   ChEMBL; CHEMBL2034803; -.
DR   GuidetoPHARMACOLOGY; 2813; -.
DR   GlyGen; P57771; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P57771; -.
DR   PhosphoSitePlus; P57771; -.
DR   BioMuta; RGS8; -.
DR   DMDM; 13124465; -.
DR   MassIVE; P57771; -.
DR   PaxDb; 9606-ENSP00000258302; -.
DR   PeptideAtlas; P57771; -.
DR   ProteomicsDB; 57032; -. [P57771-1]
DR   ProteomicsDB; 57033; -. [P57771-2]
DR   Antibodypedia; 34440; 149 antibodies from 21 providers.
DR   DNASU; 85397; -.
DR   Ensembl; ENST00000258302.8; ENSP00000258302.4; ENSG00000135824.13. [P57771-2]
DR   Ensembl; ENST00000367556.5; ENSP00000356527.1; ENSG00000135824.13. [P57771-1]
DR   Ensembl; ENST00000367557.8; ENSP00000356528.4; ENSG00000135824.13. [P57771-1]
DR   Ensembl; ENST00000483095.6; ENSP00000426289.1; ENSG00000135824.13. [P57771-1]
DR   Ensembl; ENST00000515211.2; ENSP00000511884.1; ENSG00000135824.13. [P57771-1]
DR   GeneID; 85397; -.
DR   KEGG; hsa:85397; -.
DR   MANE-Select; ENST00000515211.2; ENSP00000511884.1; NM_001102450.3; NP_001095920.1.
DR   UCSC; uc001gpm.2; human. [P57771-1]
DR   AGR; HGNC:16810; -.
DR   CTD; 85397; -.
DR   DisGeNET; 85397; -.
DR   GeneCards; RGS8; -.
DR   HGNC; HGNC:16810; RGS8.
DR   HPA; ENSG00000135824; Group enriched (brain, retina).
DR   MIM; 607189; gene.
DR   neXtProt; NX_P57771; -.
DR   OpenTargets; ENSG00000135824; -.
DR   PharmGKB; PA34379; -.
DR   VEuPathDB; HostDB:ENSG00000135824; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000154304; -.
DR   HOGENOM; CLU_059863_3_1_1; -.
DR   InParanoid; P57771; -.
DR   OMA; MNKGMRT; -.
DR   OrthoDB; 22856at2759; -.
DR   PhylomeDB; P57771; -.
DR   TreeFam; TF315837; -.
DR   PathwayCommons; P57771; -.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; P57771; -.
DR   BioGRID-ORCS; 85397; 11 hits in 1138 CRISPR screens.
DR   ChiTaRS; RGS8; human.
DR   EvolutionaryTrace; P57771; -.
DR   GeneWiki; RGS8; -.
DR   GenomeRNAi; 85397; -.
DR   Pharos; P57771; Tchem.
DR   PRO; PR:P57771; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P57771; Protein.
DR   Bgee; ENSG00000135824; Expressed in lateral nuclear group of thalamus and 88 other cell types or tissues.
DR   ExpressionAtlas; P57771; baseline and differential.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR   GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:UniProtKB.
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:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR   GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; ISS:UniProtKB.
DR   CDD; cd08711; RGS_RGS8; 1.
DR   Gene3D; 1.10.196.10; -; 2.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR034949; RGS_RGS8.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR024066; RGS_subdom1/3.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   PANTHER; PTHR10845; REGULATOR OF G PROTEIN SIGNALING; 1.
DR   PANTHER; PTHR10845:SF147; REGULATOR OF G-PROTEIN SIGNALING 8; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50132; RGS; 1.
DR   Genevisible; P57771; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW   GTPase activation; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW   Signal transduction inhibitor.
FT   CHAIN           1..180
FT                   /note="Regulator of G-protein signaling 8"
FT                   /id="PRO_0000204199"
FT   DOMAIN          56..171
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49804"
FT   VAR_SEQ         1..9
FT                   /note="MAALLMPRR -> MWNTLTRSLSDHPVGKDPQAMRTGQRQ (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:11318611,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_036421"
FT   HELIX           47..52
FT                   /evidence="ECO:0007829|PDB:2IHD"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:2ODE"
FT   HELIX           57..61
FT                   /evidence="ECO:0007829|PDB:2IHD"
FT   HELIX           64..76
FT                   /evidence="ECO:0007829|PDB:2IHD"
FT   HELIX           81..92
FT                   /evidence="ECO:0007829|PDB:2IHD"
FT   HELIX           98..112
FT                   /evidence="ECO:0007829|PDB:2IHD"
FT   HELIX           125..134
FT                   /evidence="ECO:0007829|PDB:2IHD"
FT   TURN            140..143
FT                   /evidence="ECO:0007829|PDB:2IHD"
FT   HELIX           144..156
FT                   /evidence="ECO:0007829|PDB:2IHD"
FT   HELIX           158..163
FT                   /evidence="ECO:0007829|PDB:2IHD"
FT   HELIX           166..169
FT                   /evidence="ECO:0007829|PDB:2IHD"
FT   TURN            170..172
FT                   /evidence="ECO:0007829|PDB:5DO9"
SQ   SEQUENCE   180 AA;  20917 MW;  198965B4C27F64C9 CRC64;
     MAALLMPRRN KGMRTRLGCL SHKSDSCSDF TAILPDKPNR ALKRLSTEEA TRWADSFDVL
     LSHKYGVAAF RAFLKTEFSE ENLEFWLACE EFKKTRSTAK LVSKAHRIFE EFVDVQAPRE
     VNIDFQTREA TRKNLQEPSL TCFDQAQGKV HSLMEKDSYP RFLRSKMYLD LLSQSQRRLS
//