RGS1_ARATH
ID RGS1_ARATH Reviewed; 459 AA.
AC Q8H1F2; Q8RWS5; Q9LU81; Q9LU82;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Regulator of G-protein signaling 1;
DE Short=AtRGS1;
GN Name=RGS1; OrderedLocusNames=At3g26090; ORFNames=MPE11.27, MPE11.28;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION, FUNCTION, INTERACTION WITH GPA1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14500984; DOI=10.1126/science.1087790;
RA Chen J.G., Willard F.S., Huang J., Liang J., Chasse S.A., Jones A.M.,
RA Siderovski D.P.;
RT "A seven-transmembrane RGS protein that modulates plant cell
RT proliferation.";
RL Science 301:1728-1731(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15313575; DOI=10.1016/s0076-6879(04)89020-7;
RA Chen J.G., Jones A.M.;
RT "AtRGS1 function in Arabidopsis thaliana.";
RL Methods Enzymol. 389:338-350(2004).
RN [6]
RP FUNCTION.
RX PubMed=16714312; DOI=10.1093/jxb/erj167;
RA Chen Y., Ji F., Xie H., Liang J.;
RT "Overexpression of the regulator of G-protein signalling protein enhances
RT ABA-mediated inhibition of root elongation and drought tolerance in
RT Arabidopsis.";
RL J. Exp. Bot. 57:2101-2110(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16361523; DOI=10.1104/pp.105.069872;
RA Chen Y., Ji F., Xie H., Liang J., Zhang J.;
RT "The regulator of G-protein signaling proteins involved in sugar and
RT abscisic acid signaling in Arabidopsis seed germination.";
RL Plant Physiol. 140:302-310(2006).
RN [8]
RP FUNCTION, MUTAGENESIS OF GLU-320, INTERACTION WITH GPA1, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17951432; DOI=10.1073/pnas.0704751104;
RA Johnston C.A., Taylor J.P., Gao Y., Kimple A.J., Grigston J.C., Chen J.G.,
RA Siderovski D.P., Jones A.M., Willard F.S.;
RT "GTPase acceleration as the rate-limiting step in Arabidopsis G protein-
RT coupled sugar signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:17317-17322(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH GPA1.
RX PubMed=18817773; DOI=10.1016/j.febslet.2008.08.038;
RA Grigston J.C., Osuna D., Scheible W.R., Liu C., Stitt M., Jones A.M.;
RT "D-Glucose sensing by a plasma membrane regulator of G signaling protein,
RT AtRGS1.";
RL FEBS Lett. 582:3577-3584(2008).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18541915; DOI=10.1073/pnas.0800980105;
RA Fan L.M., Zhang W., Chen J.G., Taylor J.P., Jones A.M., Assmann S.M.;
RT "Abscisic acid regulation of guard-cell K+ and anion channels in Gbeta- and
RT RGS-deficient Arabidopsis lines.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8476-8481(2008).
RN [11]
RP INTERACTION WITH NDL1; NDL2 AND NDL3.
RX PubMed=19948787; DOI=10.1105/tpc.109.065557;
RA Mudgil Y., Uhrig J.F., Zhou J., Temple B., Jiang K., Jones A.M.;
RT "Arabidopsis N-MYC DOWNREGULATED-LIKE1, a positive regulator of auxin
RT transport in a G protein-mediated pathway.";
RL Plant Cell 21:3591-3609(2009).
RN [12]
RP FUNCTION.
RX PubMed=21325279; DOI=10.1074/jbc.m110.190355;
RA Jones J.C., Temple B.R., Jones A.M., Dohlman H.G.;
RT "Functional reconstitution of an atypical G protein heterotrimer and
RT regulator of G protein signaling protein (RGS1) from Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 286:13143-13150(2011).
RN [13]
RP INTERACTION WITH GPA1; WNK1; WNK8; WNK10 AND SYP23.
RX PubMed=21952135; DOI=10.1038/msb.2011.66;
RA Klopffleisch K., Phan N., Augustin K., Bayne R.S., Booker K.S.,
RA Botella J.R., Carpita N.C., Carr T., Chen J.G., Cooke T.R., Frick-Cheng A.,
RA Friedman E.J., Fulk B., Hahn M.G., Jiang K., Jorda L., Kruppe L., Liu C.,
RA Lorek J., McCann M.C., Molina A., Moriyama E.N., Mukhtar M.S., Mudgil Y.,
RA Pattathil S., Schwarz J., Seta S., Tan M., Temp U., Trusov Y., Urano D.,
RA Welter B., Yang J., Panstruga R., Uhrig J.F., Jones A.M.;
RT "Arabidopsis G-protein interactome reveals connections to cell wall
RT carbohydrates and morphogenesis.";
RL Mol. Syst. Biol. 7:532-532(2011).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-428, AND MUTAGENESIS
RP OF SER-428; SER-435 AND SER-436.
RX PubMed=22940907; DOI=10.1038/ncb2568;
RA Urano D., Phan N., Jones J.C., Yang J., Huang J., Grigston J., Taylor J.P.,
RA Jones A.M.;
RT "Endocytosis of the seven-transmembrane RGS1 protein activates G-protein-
RT coupled signalling in Arabidopsis.";
RL Nat. Cell Biol. 14:1079-1088(2012).
RN [15]
RP INDUCTION BY OZONE.
RX PubMed=21988569; DOI=10.1111/j.1365-3040.2011.02443.x;
RA Booker F., Burkey K., Morgan P., Fiscus E., Jones A.;
RT "Minimal influence of G-protein null mutations on ozone-induced changes in
RT gene expression, foliar injury, gas exchange and peroxidase activity in
RT Arabidopsis thaliana L.";
RL Plant Cell Environ. 35:668-681(2012).
RN [16]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RHIP1.
RX PubMed=26528314; DOI=10.3389/fpls.2015.00851;
RA Huang J.-P., Tunc-Ozdemir M., Chang Y., Jones A.M.;
RT "Cooperative control between AtRGS1 and AtHXK1 in a WD40-repeat protein
RT pathway in Arabidopsis thaliana.";
RL Front. Plant Sci. 6:851-851(2015).
CC -!- FUNCTION: Glucose-regulated GTPase-accelerating protein (GAP) for the
CC GTP-bound self-activating heterotrimeric G alpha protein GPA1.
CC Cooperates with G beta-gamma dimers to maintain an unactivated but
CC fully functional pool of GPA1. Phosphorylation-dependent endocytosis of
CC RGS1 physically uncouples the two proteins, resulting in signal
CC activation. Free AGB1 is essential, but not sufficient, for RGS1
CC endocytosis. Modulates cell proliferation, abscisic acid (ABA) and
CC drought stress signal transduction by acting in a hexokinase-
CC independent glucose-signaling pathway (PubMed:26528314). Involved in
CC the shapes of leaves, the development of floral buds, the elongation of
CC stems, siliques, and hypocotyls, the time of flowering and the
CC regulation of guard-cell K(+) and anion channels. Important for the
CC kinetics of voltage activation of inward K(+) current but not for the
CC current amplitude. {ECO:0000269|PubMed:14500984,
CC ECO:0000269|PubMed:15313575, ECO:0000269|PubMed:16361523,
CC ECO:0000269|PubMed:16714312, ECO:0000269|PubMed:17951432,
CC ECO:0000269|PubMed:18541915, ECO:0000269|PubMed:18817773,
CC ECO:0000269|PubMed:21325279, ECO:0000269|PubMed:22940907,
CC ECO:0000269|PubMed:26528314}.
CC -!- SUBUNIT: Interacts (via C-ter) with GPA1 (PubMed:14500984,
CC PubMed:17951432, PubMed:18817773, PubMed:21952135). Interacts with
CC WNK1, WNK8, WNK10, SYP23. The association with WNK8 at the plasma
CC membrane is triggered by induction of glucose and continues with
CC trafficking into endocytic compartments (PubMed:21952135). Interacts
CC with NDL1, NDL2 and NDL3 (PubMed:19948787). Interacts with RHIP1
CC (PubMed:26528314). {ECO:0000269|PubMed:14500984,
CC ECO:0000269|PubMed:17951432, ECO:0000269|PubMed:18817773,
CC ECO:0000269|PubMed:19948787, ECO:0000269|PubMed:21952135,
CC ECO:0000269|PubMed:26528314}.
CC -!- INTERACTION:
CC Q8H1F2; P18064: GPA1; NbExp=7; IntAct=EBI-1627025, EBI-443890;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endosome membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=accumulates at the nascent cell
CC plate during cytokinesis. {ECO:0000269|PubMed:14500984,
CC ECO:0000269|PubMed:17951432, ECO:0000269|PubMed:22940907}.
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls, cotyledons, guard cells
CC and root and shoot apical meristems. {ECO:0000269|PubMed:14500984,
CC ECO:0000269|PubMed:17951432, ECO:0000269|PubMed:18541915}.
CC -!- INDUCTION: Up-regulated by ozone. {ECO:0000269|PubMed:21988569}.
CC -!- DOMAIN: The C-terminal domain (249-459) is able to bind to and to
CC accelerate the GTPase activity of GPA1.
CC -!- PTM: Phosphorylated by WNK8 and WNK10, and in vitro by WNK1. Also
CC phosphorylated at Ser-435 or Ser-436. {ECO:0000269|PubMed:22940907}.
CC -!- DISRUPTION PHENOTYPE: Increased cell elongation and longer hypocotyls
CC when grown in the dark. Longer primary roots when grown in light due to
CC increased cell production in root meristem. Loss of stratification
CC requirement for seed germination. Decreased sensitivity to glucose and
CC abscisic acid (ABA) in seed germination process (PubMed:26528314). No
CC effect on ABA inhibition of stomatal opening.
CC {ECO:0000269|PubMed:14500984, ECO:0000269|PubMed:15313575,
CC ECO:0000269|PubMed:16361523, ECO:0000269|PubMed:18541915,
CC ECO:0000269|PubMed:26528314}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01073.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB01074.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB023041; BAB01073.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB023041; BAB01074.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77116.1; -; Genomic_DNA.
DR EMBL; AY091142; AAM14091.1; -; mRNA.
DR EMBL; AY150429; AAN12971.1; -; mRNA.
DR RefSeq; NP_189238.2; NM_113514.4.
DR AlphaFoldDB; Q8H1F2; -.
DR SMR; Q8H1F2; -.
DR BioGRID; 7538; 151.
DR IntAct; Q8H1F2; 8.
DR MINT; Q8H1F2; -.
DR STRING; 3702.AT3G26090.1; -.
DR iPTMnet; Q8H1F2; -.
DR PaxDb; Q8H1F2; -.
DR PRIDE; Q8H1F2; -.
DR ProteomicsDB; 236855; -.
DR EnsemblPlants; AT3G26090.1; AT3G26090.1; AT3G26090.
DR GeneID; 822207; -.
DR Gramene; AT3G26090.1; AT3G26090.1; AT3G26090.
DR KEGG; ath:AT3G26090; -.
DR Araport; AT3G26090; -.
DR TAIR; locus:2092180; AT3G26090.
DR eggNOG; ENOG502QVMV; Eukaryota.
DR HOGENOM; CLU_589758_0_0_1; -.
DR InParanoid; Q8H1F2; -.
DR OMA; VMSVNFL; -.
DR OrthoDB; 536748at2759; -.
DR PhylomeDB; Q8H1F2; -.
DR PRO; PR:Q8H1F2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H1F2; baseline and differential.
DR Genevisible; Q8H1F2; AT.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IMP:TAIR.
DR GO; GO:0005096; F:GTPase activator activity; IDA:TAIR.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IDA:TAIR.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:TAIR.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009749; P:response to glucose; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endosome; Membrane; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor; Transmembrane; Transmembrane helix.
FT CHAIN 1..459
FT /note="Regulator of G-protein signaling 1"
FT /id="PRO_0000421264"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 295..413
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 429..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22940907"
FT MUTAGEN 320
FT /note="E->K: Loss of GTPase-accelerating activity, loss of
FT interaction with GPA1 and loss of endocytosis."
FT /evidence="ECO:0000269|PubMed:17951432"
FT MUTAGEN 428
FT /note="S->A: Loss of endocytosis; when associated with A-
FT 435 and A-436."
FT /evidence="ECO:0000269|PubMed:22940907"
FT MUTAGEN 435
FT /note="S->A: Loss of endocytosis; when associated with A-
FT 428 and A-436."
FT /evidence="ECO:0000269|PubMed:22940907"
FT MUTAGEN 436
FT /note="S->A: Loss of endocytosis; when associated with A-
FT 428 and A-435."
FT /evidence="ECO:0000269|PubMed:22940907"
FT CONFLICT 426
FT /note="G -> R (in Ref. 3; AAM14091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 52947 MW; 43AA65CD0417488E CRC64;
MASGCALHGG CPSDYVAVAI SVICFFVLLS RSVLPCLIHK APRTNSSSFW IPVIQVISSF
NLLFSIMMSV NLLRFRTKHW WRYCYLWAVW IEGPLGFGLL MSCRITQAFQ LYFIFVKKRL
PPVKSYIFLP LVLLPWIFGA AIIHATKPLN DKCHMGLQWT FPVAGLHALY VLALIAFTRA
VRHVEFRFDE LRDLWKGILV SATSIVIWVT AFVLNEIHEE ISWLQVASRF VLLVTGGILV
VVFFSISSNQ PLLSQISLKK RQNFEFQRMG QALGIPDSGL LFRKEEFRPV DPNEPLDKLL
LNKRFRHSFM EFADSCYAGE TLHFFEEVYE HGKIPEDDSI RRIYMARHIM EKFIVAGAEM
ELNLSHKTRQ EILTTQDLTH TDLFKNALNE VMQLIKMNLV RDYWSSIYFI KFKEEESCHE
AMHKEGYSFS SPRLSSVQGS DDPFYQEHMS KSSRCSSPG
