RGS3_RAT
ID RGS3_RAT Reviewed; 967 AA.
AC P49797; Q5RKK6; Q920Q9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Regulator of G-protein signaling 3;
DE Short=RGS3;
DE AltName: Full=SRB-RGS;
GN Name=Rgs3;
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 [MRNA] (ISOFORM 1), INTERACTION WITH ESR1, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=11595167; DOI=10.1016/s0378-1119(01)00589-3;
RA Ikeda M., Hirokawa M., Satani N., Kinoshita T., Watanabe Y., Inoue H.,
RA Tone S., Ishikawa T., Minatogawa Y.;
RT "Molecular cloning and characterization of a steroid receptor-binding
RT regulator of G-protein signaling protein cDNA.";
RL Gene 273:207-214(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 873-939 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8548815; DOI=10.1016/s0092-8674(00)80998-8;
RA Koelle M.R., Horvitz H.R.;
RT "EGL-10 regulates G protein signaling in the C. elegans nervous system and
RT shares a conserved domain with many mammalian proteins.";
RL Cell 84:115-125(1996).
RN [4]
RP PHOSPHORYLATION.
RX PubMed=10702309; DOI=10.1074/jbc.275.10.7365;
RA Pedram A., Razandi M., Kehrl J., Levin E.R.;
RT "Natriuretic peptides inhibit G protein activation. Mediation through
RT cross-talk between cyclic GMP-dependent protein kinase and regulators of G
RT protein-signaling proteins.";
RL J. Biol. Chem. 275:7365-7372(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713 AND SER-716, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SUBUNIT: Binds EFNB1 and EFNB2. Binds the GNB1-GNG2 heterodimer (By
CC similarity). Binds ESR1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49796}.
CC Membrane {ECO:0000250|UniProtKB:P49796}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49796}. Nucleus {ECO:0000250|UniProtKB:P49796}.
CC Note=Long isoforms are cytoplasmic and associated with the plasma
CC membrane. Short isoforms are nuclear. {ECO:0000250|UniProtKB:P49796}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49797-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49797-2; Sequence=VSP_013971, VSP_013972;
CC -!- TISSUE SPECIFICITY: Detected in kidney, uterus, ovary, heart, brain,
CC spleen, lung and testis. {ECO:0000269|PubMed:11595167,
CC ECO:0000269|PubMed:8548815}.
CC -!- PTM: Phosphorylated by cyclic GMP-dependent protein kinase.
CC {ECO:0000269|PubMed:10702309}.
CC -!- PTM: ISGylated. {ECO:0000250}.
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DR EMBL; AB055153; BAB63460.1; -; mRNA.
DR EMBL; BC085710; AAH85710.1; -; mRNA.
DR EMBL; U32434; AAC52371.1; -; mRNA.
DR RefSeq; NP_062213.1; NM_019340.1. [P49797-1]
DR RefSeq; XP_006238327.1; XM_006238265.3. [P49797-2]
DR AlphaFoldDB; P49797; -.
DR SMR; P49797; -.
DR BioGRID; 248513; 2.
DR STRING; 10116.ENSRNOP00000055954; -.
DR iPTMnet; P49797; -.
DR PhosphoSitePlus; P49797; -.
DR PaxDb; P49797; -.
DR PRIDE; P49797; -.
DR GeneID; 54293; -.
DR KEGG; rno:54293; -.
DR UCSC; RGD:3566; rat. [P49797-1]
DR CTD; 5998; -.
DR RGD; 3566; Rgs3.
DR VEuPathDB; HostDB:ENSRNOG00000024501; -.
DR eggNOG; KOG3589; Eukaryota.
DR HOGENOM; CLU_038537_0_0_1; -.
DR InParanoid; P49797; -.
DR PhylomeDB; P49797; -.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P49797; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000024501; Expressed in lung and 20 other tissues.
DR ExpressionAtlas; P49797; baseline and differential.
DR Genevisible; P49797; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR CDD; cd08713; RGS_RGS3; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
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 Pfam; PF00595; PDZ; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Membrane; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Signal transduction inhibitor;
KW Ubl conjugation.
FT CHAIN 1..967
FT /note="Regulator of G-protein signaling 3"
FT /id="PRO_0000204184"
FT DOMAIN 18..95
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 842..967
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..676
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P49796"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC04"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC04"
FT VAR_SEQ 399..433
FT /note="MFETEADEKEMPLVEGKGPGAEERTPSKDPSPSQE -> KLHPYGSLQQEMG
FT PVTSINATQDRSFTSSGQTLIG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013971"
FT VAR_SEQ 434..967
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013972"
SQ SEQUENCE 967 AA; 106380 MW; 5C558885DBA63A5B CRC64;
MNRFNGLCKV CSERRYRQIT IRRGKDGFGF TICCDSPVRV QAVDSGGPAE RAGLQQLDTV
LQLNERPVEH WKCVELAHEI RSCPSEIILL VWRVVPQIKP GPDGGVLRRA SCKSTHDLLS
PPNKREKNCT HGAPTRPEQR HSCHLVCDSS DGLLLGGWER YTEVGKRSGQ HTLPALSRAT
TPTDPNYIIL APLNPGSQLL RPVYQEDAIP EEPGTTTKGK SYTGLGKKSR LMKTVQTMKG
HSNYQDCSAL RPHIPHSSYG TYVTLAPKVL VFPVFVQPLD LCNPARTLLL SEELLLYEGR
NKTSQVTLFA YSDLLLFTKE EEPGRCDVLR NPLYLQSVKL QEGSSEDLKF CVLYLAEKAE
CLFTLEAHSQ EQKKRVCWCL SENIAKQQQL AATPTERKMF ETEADEKEMP LVEGKGPGAE
ERTPSKDPSP SQELPPGQEL PPSKDPSPSQ ELPPGQELPP SKDPSPSQEL PPGQELPSSK
NPSPSQELPA GQDLPPRKES FSGQEAAPGP ESPSSEDIAT CQNPPQSPET STSKDSPPGQ
GSSPTTEVPS CQGLPAGQES TSQDPLLSQE PPAIPESSAS DQNVLPSQES PPSQGSLSEK
ALAEQTISPG ELPAATAGEP SASRPNFVIP EVRLDSAYSQ QDGAHGGSSG EDEDAEEGEE
GEEGEEDEED DTNDDNYGDR NEAKRSSLIE TGQGAEGGLS LRVQNSLRRR THSEGSLLQE
ARGPCFASDT TLHCSDGEGT TSTWAIPSPR TLKKELGRNG GSMHHLSLFF TGHRKMSGTD
LADDVEASRK RKSKNIAKDM KNKLAIFRRR NESPGAQPAG KADKTTKSFK PTSEEALKWS
ESLEKLLLHK YGLEVFQAFL RTEFSEENLE FWLACEDFKK VKSQSKMAAK AKKIFAEFIA
IQACKEVNLD SYTREHTKEN LQSITRGCFD LAQKRIFGLM EKDSYPRFLR SDLYLDLINQ
KKMSPPL
