RGS1_HUMAN
ID RGS1_HUMAN Reviewed; 209 AA.
AC Q08116; B2RDM9; B4DZY0; Q07918; Q9H1W2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Regulator of G-protein signaling 1;
DE Short=RGS1;
DE AltName: Full=B-cell activation protein BL34 {ECO:0000303|PubMed:8473738};
DE AltName: Full=Early response protein 1R20;
GN Name=RGS1; Synonyms=1R20, BL34, IER1;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Skeletal muscle, and Thymus;
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=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-209 (ISOFORM 1).
RC TISSUE=Skin;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 6-209 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=B-cell;
RX PubMed=8473738;
RA Hong J.X., Wilson G.L., Fox C.H., Kehrl J.H.;
RT "Isolation and characterization of a novel B cell activation gene.";
RL J. Immunol. 150:3895-3904(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-209 (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=8241276; DOI=10.1016/0167-4781(93)90163-8;
RA Newton J.S., Deed R.W., Mitchell E.L.D., Murphy J.J., Norton J.D.;
RT "A B cell specific immediate early human gene is located on chromosome band
RT 1q31 and encodes an alpha helical basic phosphoprotein.";
RL Biochim. Biophys. Acta 1216:314-316(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-209 (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 (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-209 (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10480894; DOI=10.1074/jbc.274.38.26860;
RA Denecke B., Meyerdierks A., Boettger E.C.;
RT "RGS1 is expressed in monocytes and acts as a GTPase-activating protein for
RT G-protein-coupled chemoattractant receptors.";
RL J. Biol. Chem. 274:26860-26868(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 63-205 IN COMPLEX WITH GNAI1,
RP INTERACTION WITH GNAI1 AND GNAQ, AND FUNCTION.
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 downstream of the N-formylpeptide chemoattractant
CC receptors and leukotriene receptors (PubMed:10480894). Inhibits B cell
CC chemotaxis toward CXCL12 (By similarity). Inhibits signal transduction
CC by increasing the GTPase activity of G protein alpha subunits thereby
CC driving them into their inactive GDP-bound form (PubMed:10480894,
CC PubMed:18434541). {ECO:0000250|UniProtKB:Q9JL25,
CC ECO:0000269|PubMed:10480894, ECO:0000269|PubMed:18434541}.
CC -!- SUBUNIT: Interacts with GNAI1 and GNAQ. {ECO:0000269|PubMed:18434541}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10480894};
CC Peripheral membrane protein {ECO:0000269|PubMed:10480894}; Cytoplasmic
CC side {ECO:0000269|PubMed:10480894}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:10480894}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q08116-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08116-2; Sequence=VSP_036422;
CC -!- TISSUE SPECIFICITY: Detected in peripheral blood monocytes
CC (PubMed:10480894). Expression is relatively low in B-cells and chronic
CC lymphocytic leukemia B-cells; however, in other types of malignant B-
CC cell such as non-Hodgkin lymphoma and hairy cell leukemia, expression
CC is constitutively high (PubMed:8473738). {ECO:0000269|PubMed:10480894,
CC ECO:0000269|PubMed:8473738}.
CC -!- INDUCTION: In response to several B-cell activation signals.
CC {ECO:0000269|PubMed:8473738}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB26289.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH15510.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG37976.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG64242.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA51826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK303138; BAG64242.1; ALT_INIT; mRNA.
DR EMBL; AK315607; BAG37976.1; ALT_INIT; mRNA.
DR EMBL; AL136987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015510; AAH15510.1; ALT_INIT; mRNA.
DR EMBL; S59049; AAB26289.1; ALT_INIT; mRNA.
DR EMBL; X73427; CAA51826.1; ALT_INIT; mRNA.
DR EMBL; AF493925; AAM12639.1; -; mRNA.
DR EMBL; BT006668; AAP35314.1; -; mRNA.
DR CCDS; CCDS1375.2; -. [Q08116-1]
DR PIR; S43436; S43436.
DR RefSeq; NP_002913.3; NM_002922.3. [Q08116-1]
DR PDB; 2BV1; X-ray; 2.00 A; A/B=63-205.
DR PDB; 2GTP; X-ray; 2.55 A; C/D=63-205.
DR PDBsum; 2BV1; -.
DR PDBsum; 2GTP; -.
DR AlphaFoldDB; Q08116; -.
DR SMR; Q08116; -.
DR BioGRID; 111928; 8.
DR DIP; DIP-59091N; -.
DR IntAct; Q08116; 7.
DR STRING; 9606.ENSP00000356429; -.
DR iPTMnet; Q08116; -.
DR PhosphoSitePlus; Q08116; -.
DR BioMuta; RGS1; -.
DR DMDM; 229470360; -.
DR EPD; Q08116; -.
DR jPOST; Q08116; -.
DR MassIVE; Q08116; -.
DR PaxDb; Q08116; -.
DR PeptideAtlas; Q08116; -.
DR PRIDE; Q08116; -.
DR ProteomicsDB; 58570; -. [Q08116-1]
DR ProteomicsDB; 58571; -. [Q08116-2]
DR Antibodypedia; 34458; 357 antibodies from 32 providers.
DR DNASU; 5996; -.
DR Ensembl; ENST00000367459.8; ENSP00000356429.3; ENSG00000090104.12. [Q08116-1]
DR Ensembl; ENST00000469578.2; ENSP00000464323.1; ENSG00000090104.12. [Q08116-2]
DR GeneID; 5996; -.
DR KEGG; hsa:5996; -.
DR MANE-Select; ENST00000367459.8; ENSP00000356429.3; NM_002922.4; NP_002913.3.
DR UCSC; uc001gsi.2; human. [Q08116-1]
DR CTD; 5996; -.
DR DisGeNET; 5996; -.
DR GeneCards; RGS1; -.
DR HGNC; HGNC:9991; RGS1.
DR HPA; ENSG00000090104; Low tissue specificity.
DR MIM; 600323; gene.
DR neXtProt; NX_Q08116; -.
DR OpenTargets; ENSG00000090104; -.
DR PharmGKB; PA34361; -.
DR VEuPathDB; HostDB:ENSG00000090104; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000157316; -.
DR HOGENOM; CLU_059863_3_3_1; -.
DR InParanoid; Q08116; -.
DR OMA; NGKEDCK; -.
DR PhylomeDB; Q08116; -.
DR TreeFam; TF315837; -.
DR PathwayCommons; Q08116; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; Q08116; -.
DR BioGRID-ORCS; 5996; 7 hits in 1059 CRISPR screens.
DR ChiTaRS; RGS1; human.
DR EvolutionaryTrace; Q08116; -.
DR GeneWiki; RGS1; -.
DR GenomeRNAi; 5996; -.
DR Pharos; Q08116; Tbio.
DR PRO; PR:Q08116; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q08116; protein.
DR Bgee; ENSG00000090104; Expressed in C1 segment of cervical spinal cord and 171 other tissues.
DR Genevisible; Q08116; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005516; F:calmodulin binding; TAS:ProtInc.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0061737; P:leukotriene signaling pathway; IDA:UniProtKB.
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:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 2.
DR IDEAL; IID00609; -.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR030409; RGS1.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR10845:SF34; PTHR10845:SF34; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW GTPase activation; Membrane; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..209
FT /note="Regulator of G-protein signaling 1"
FT /id="PRO_0000204175"
FT DOMAIN 85..200
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT VAR_SEQ 149..209
FT /note="INIDFRTRESTAKKIKAPTPTCFDEAQKVIYTLMEKDSYPRFLKSDIYLNLL
FT NDLQANSLK -> VSIKLIIISFSIKDPICRNNI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036422"
FT CONFLICT 177
FT /note="V -> A (in Ref. 1; BAG37976)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="D -> H (in Ref. 5; CAA51826)"
FT /evidence="ECO:0000305"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2BV1"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:2BV1"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2BV1"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:2BV1"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:2BV1"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:2BV1"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2BV1"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:2BV1"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:2BV1"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:2BV1"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:2BV1"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:2BV1"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:2BV1"
SQ SEQUENCE 209 AA; 23858 MW; D8D7D8E80819496A CRC64;
MRAAAISTPK LDKMPGMFFS ANPKELKGTT HSLLDDKMQK RRPKTFGMDM KAYLRSMIPH
LESGMKSSKS KDVLSAAEVM QWSQSLEKLL ANQTGQNVFG SFLKSEFSEE NIEFWLACED
YKKTESDLLP CKAEEIYKAF VHSDAAKQIN IDFRTRESTA KKIKAPTPTC FDEAQKVIYT
LMEKDSYPRF LKSDIYLNLL NDLQANSLK
