ID   RGS1_RAT                Reviewed;         209 AA.
AC   P97844; A0A0H2UHC4; Q4KM99;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 3.
DT   02-SEP-2026, entry version 148.
DE   RecName: Full=Regulator of G protein signaling 1;
DE            Short=RGS1;
GN   Name=Rgs1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thymus;
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 92-171.
RA   Greenwood M.T., Guo Y., Hussain S.N.A.;
RT   "The rat RGS1 gene is expressed in multiple tissues.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades,
CC       including signaling downstream of the N-formylpeptide chemoattractant
CC       receptors and leukotriene receptors. Inhibits B cell chemotaxis toward
CC       CXCL12 (By similarity). Inhibits signal transduction by increasing the
CC       GTPase activity of G protein alpha subunits, thereby driving them into
CC       their inactive GDP-bound form (By similarity).
CC       {ECO:0000250|UniProtKB:Q08116, ECO:0000250|UniProtKB:Q9JL25}.
CC   -!- SUBUNIT: Interacts with GNAI1 and GNAQ. {ECO:0000250|UniProtKB:Q08116}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q08116};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q08116}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:Q08116}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q08116}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P97844-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97844-2; Sequence=VSP_058127;
CC   -!- TISSUE SPECIFICITY: Expressed in multiple tissues. {ECO:0000305|Ref.4}.
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DR   EMBL; AABR07021216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473958; EDM09598.1; -; Genomic_DNA.
DR   EMBL; BC098681; AAH98681.1; -; mRNA.
DR   EMBL; U77698; AAB48300.1; -; mRNA.
DR   RefSeq; NP_001388206.1; NM_001401277.1. [P97844-1]
DR   RefSeq; NP_062209.1; NM_019336.3. [P97844-2]
DR   AlphaFoldDB; P97844; -.
DR   SMR; P97844; -.
DR   FunCoup; P97844; 184.
DR   STRING; 10116.ENSRNOP00000005251; -.
DR   PhosphoSitePlus; P97844; -.
DR   PaxDb; 10116-ENSRNOP00000005251; -.
DR   Ensembl; ENSRNOT00000005251.9; ENSRNOP00000005251.6; ENSRNOG00000003895.9. [P97844-2]
DR   GeneID; 54289; -.
DR   KEGG; rno:54289; -.
DR   UCSC; RGD:3561; rat. [P97844-1]
DR   AGR; RGD:3561; -.
DR   CTD; 5996; -.
DR   RGD; 3561; Rgs1.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000157316; -.
DR   HOGENOM; CLU_059863_3_3_1; -.
DR   InParanoid; P97844; -.
DR   OMA; CMVPHIE; -.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   PRO; PR:P97844; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003895; Expressed in colon and 16 other cell types or tissues.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:RGD.
DR   GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0061737; P:leukotriene signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR   FunFam; 1.10.167.10:FF:000001; Putative regulator of g-protein signaling 12; 1.
DR   FunFam; 1.10.196.10:FF:000009; Regulator of G-protein signaling 1; 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; 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:SF34; REGULATOR OF G-PROTEIN SIGNALING 1; 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.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Cytoplasm; GTPase activation;
KW   Membrane; Reference proteome; Signal transduction inhibitor.
FT   CHAIN           1..209
FT                   /note="Regulator of G protein signaling 1"
FT                   /id="PRO_0000204177"
FT   DOMAIN          85..200
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          18..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..47
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_058127"
SQ   SEQUENCE   209 AA;  24096 MW;  939CCD55ADB06432 CRC64;
     MRAAAISMPR LNKMPGMFFS ASPKDSKEPS HSLLDDNKQK KRPKTFGMDM KAYLRSMIPH
     LESGMKSSKS KDILSAEEVM QWSQSLEKLL ANQMGQNVFG KFLKSEFSEE NIEFWLACED
     YKKTETDLLH NKAEHIYKAF VHSDAVKQIN IDFHTRESTA KKIKTPTPTC FDEAQKVIYA
     LMEKDSYPRF LKSNIYLNLL NDLQANTLK
//