RGS1_MOUSE
ID RGS1_MOUSE Reviewed; 209 AA.
AC Q9JL25; Q3TBD1; Q3TC18; Q3TD56; Q3U477;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Regulator of G-protein signaling 1;
DE Short=RGS1;
GN Name=Rgs1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-209 (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Lymph node;
RX PubMed=10779778; DOI=10.4049/jimmunol.164.9.4720;
RA Reif K., Cyster J.G.;
RT "RGS molecule expression in murine B lymphocytes and ability to down-
RT regulate chemotaxis to lymphoid chemokines.";
RL J. Immunol. 164:4720-4729(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-209 (ISOFORM 1).
RC STRAIN=C57BL/6J; 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).
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 (PubMed:10779778). Inhibits signal transduction by increasing
CC the GTPase activity of G protein alpha subunits thereby driving them
CC into their inactive GDP-bound form (By similarity).
CC {ECO:0000250|UniProtKB:Q08116, ECO:0000269|PubMed:10779778}.
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=Q9JL25-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JL25-2; Sequence=VSP_036732;
CC -!- TISSUE SPECIFICITY: Detected in spleen, lymph node and intestine.
CC {ECO:0000269|PubMed:10779778}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF34624.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH28634.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23749.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE32557.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE41748.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE42139.1; Type=Erroneous initiation; Evidence={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; AK138688; BAE23749.1; ALT_INIT; mRNA.
DR EMBL; AK154394; BAE32557.1; ALT_INIT; mRNA.
DR EMBL; AK170366; BAE41748.1; ALT_INIT; mRNA.
DR EMBL; AK170957; BAE42139.1; ALT_INIT; mRNA.
DR EMBL; AK171306; BAE42382.1; -; mRNA.
DR EMBL; AF215667; AAF34624.1; ALT_INIT; mRNA.
DR EMBL; BC028634; AAH28634.1; ALT_INIT; mRNA.
DR CCDS; CCDS15349.2; -. [Q9JL25-1]
DR RefSeq; NP_056626.2; NM_015811.2. [Q9JL25-1]
DR AlphaFoldDB; Q9JL25; -.
DR SMR; Q9JL25; -.
DR BioGRID; 206110; 1.
DR IntAct; Q9JL25; 3.
DR STRING; 10090.ENSMUSP00000140624; -.
DR MoonDB; Q9JL25; Predicted.
DR iPTMnet; Q9JL25; -.
DR PhosphoSitePlus; Q9JL25; -.
DR EPD; Q9JL25; -.
DR PaxDb; Q9JL25; -.
DR PRIDE; Q9JL25; -.
DR ProteomicsDB; 253263; -. [Q9JL25-1]
DR ProteomicsDB; 253264; -. [Q9JL25-2]
DR Antibodypedia; 34458; 357 antibodies from 32 providers.
DR DNASU; 50778; -.
DR Ensembl; ENSMUST00000189061; ENSMUSP00000140624; ENSMUSG00000026358. [Q9JL25-1]
DR GeneID; 50778; -.
DR KEGG; mmu:50778; -.
DR UCSC; uc007cxj.2; mouse. [Q9JL25-1]
DR CTD; 5996; -.
DR MGI; MGI:1354694; Rgs1.
DR VEuPathDB; HostDB:ENSMUSG00000026358; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000157316; -.
DR HOGENOM; CLU_059863_3_3_1; -.
DR InParanoid; Q9JL25; -.
DR OMA; NGKEDCK; -.
DR OrthoDB; 1240467at2759; -.
DR PhylomeDB; Q9JL25; -.
DR TreeFam; TF315837; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 50778; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Rgs1; mouse.
DR PRO; PR:Q9JL25; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9JL25; protein.
DR Bgee; ENSMUSG00000026358; Expressed in stroma of bone marrow and 46 other tissues.
DR ExpressionAtlas; Q9JL25; baseline and differential.
DR Genevisible; Q9JL25; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
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:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR030409; RGS1.
DR InterPro; IPR036305; RGS_sf.
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 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_0000204176"
FT DOMAIN 85..200
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 19..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..42
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 /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036732"
FT CONFLICT 12
FT /note="N -> D (in Ref. 1; BAE42139/BAE32557)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="I -> M (in Ref. 1; BAE42139/BAE32557/BAE42382)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="R -> K (in Ref. 1; BAE42139/BAE32557/BAE42382)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="Y -> C (in Ref. 1; BAE32557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 24107 MW; F483A1690A3E2EB0 CRC64;
MRAAAISMPR LNKMPGMFFS ASPKDSKEHS HSLLDDKKQK KRPKTFGMDV KTYLRSMIPH
LESGMKSAKS KDILSAEEVM QWSQSLEKLL ANQTGQNVFG RFLKSEFSEE NIEFWLACED
YKKTETDLLH NKAENIYKAF VHSDAVKQIN IDFHTRESTA KKIKTPTPTS FDEAQKVIYS
LMEKDSYPRF LKSNIYLNLL NDLQANTLK
