ID GPA1_ORYSJ Reviewed; 380 AA. AC Q0DJ33; P49083; Q2HNY6; Q43604; Q5KQF9; Q5W732; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 2. DT 27-MAR-2024, entry version 127. DE RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit; DE Short=GP-alpha-1; DE AltName: Full=Protein Daikoku dwarf {ECO:0000303|PubMed:10377457}; DE AltName: Full=Protein Dwarf1; GN Name=GPA1 {ECO:0000305}; GN Synonyms=D1 {ECO:0000303|PubMed:10377457}, GA1, RGA1 GN {ECO:0000303|PubMed:7767602}; GN OrderedLocusNames=Os05g0333200 {ECO:0000312|EMBL:BAF17140.1}, GN LOC_Os05g26890 {ECO:0000305}; ORFNames=OJ1005_D04.15, OSJNBa0049D13.1; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Nipponbare; TISSUE=Leaf; RX PubMed=7767602; DOI=10.1093/oxfordjournals.pcp.a078767; RA Ishikawa A., Tsubouchi H., Iwasaki Y., Asahi T.; RT "Molecular cloning and characterization of a cDNA for the alpha subunit of RT a G protein from rice."; RL Plant Cell Physiol. 36:353-359(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y; RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J., RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F., RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.; RT "A fine physical map of the rice chromosome 5."; RL Mol. Genet. Genomics 274:337-345(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [5] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [6] RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=10377457; DOI=10.1073/pnas.96.13.7575; RA Fujisawa Y., Kato T., Ohki S., Ishikawa A., Kitano H., Sasaki T., Asahi T., RA Iwasaki Y.; RT "Suppression of the heterotrimeric G protein causes abnormal morphology, RT including dwarfism, in rice."; RL Proc. Natl. Acad. Sci. U.S.A. 96:7575-7580(1999). RN [7] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=10468600; DOI=10.1073/pnas.96.18.10284; RA Ashikari M., Wu J., Yano M., Sasaki T., Yoshimura A.; RT "Rice gibberellin-insensitive dwarf mutant gene Dwarf 1 encodes the alpha- RT subunit of GTP-binding protein."; RL Proc. Natl. Acad. Sci. U.S.A. 96:10284-10289(1999). RN [8] RP FUNCTION. RX PubMed=11027362; DOI=10.1073/pnas.97.21.11638; RA Ueguchi-Tanaka M., Fujisawa Y., Kobayashi M., Ashikari M., Iwasaki Y., RA Kitano H., Matsuoka M.; RT "Rice dwarf mutant d1, which is defective in the alpha subunit of the RT heterotrimeric G protein, affects gibberellin signal transduction."; RL Proc. Natl. Acad. Sci. U.S.A. 97:11638-11643(2000). RN [9] RP FUNCTION, AND INDUCTION. RX PubMed=12237405; DOI=10.1073/pnas.192244099; RA Suharsono U., Fujisawa Y., Kawasaki T., Iwasaki Y., Satoh H., Shimamoto K.; RT "The heterotrimeric G protein alpha subunit acts upstream of the small RT GTPase Rac in disease resistance of rice."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13307-13312(2002). RN [10] RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLN-223. RX PubMed=15078334; DOI=10.1111/j.1365-313x.2004.02046.x; RA Kato C., Mizutani T., Tamaki H., Kumagai H., Kamiya T., Hirobe A., RA Fujisawa Y., Kato H., Iwasaki Y.; RT "Characterization of heterotrimeric G protein complexes in rice plasma RT membrane."; RL Plant J. 38:320-331(2004). RN [11] RP FUNCTION, AND INDUCTION. RX PubMed=17117160; DOI=10.1038/sj.cr.7310111; RA Wang L., Xu Y.Y., Ma Q.B., Li D., Xu Z.H., Chong K.; RT "Heterotrimeric G protein alpha subunit is involved in rice brassinosteroid RT response."; RL Cell Res. 16:916-922(2006). RN [12] RP FUNCTION. RX PubMed=19036785; DOI=10.1093/pcp/pcn182; RA Oki K., Inaba N., Kitagawa K., Fujioka S., Kitano H., Fujisawa Y., Kato H., RA Iwasaki Y.; RT "Function of the alpha subunit of rice heterotrimeric G protein in RT brassinosteroid signaling."; RL Plant Cell Physiol. 50:161-172(2009). RN [13] RP FUNCTION, AND INTERACTION WITH TUD1. RX PubMed=23526892; DOI=10.1371/journal.pgen.1003391; RA Hu X., Qian Q., Xu T., Zhang Y., Dong G., Gao T., Xie Q., Xue Y.; RT "The U-box E3 ubiquitin ligase TUD1 functions with a heterotrimeric G alpha RT subunit to regulate Brassinosteroid-mediated growth in rice."; RL PLoS Genet. 9:E1003391-E1003391(2013). RN [14] RP INTERACTION WITH COLD1. RC STRAIN=cv. Dongjin, and cv. Nipponbare; RX PubMed=25728666; DOI=10.1016/j.cell.2015.01.046; RA Ma Y., Dai X., Xu Y., Luo W., Zheng X., Zeng D., Pan Y., Lin X., Liu H., RA Zhang D., Xiao J., Guo X., Xu S., Niu Y., Jin J., Zhang H., Xu X., Li L., RA Wang W., Qian Q., Ge S., Chong K.; RT "COLD1 confers chilling tolerance in rice."; RL Cell 160:1209-1221(2015). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved CC as modulators or transducers in various transmembrane signaling systems CC (Probable). May function in a signal transduction pathway required for CC normal growth and development of internodes, leaves, panicles and seeds CC (PubMed:10377457). Involved in gibberellin signal transduction CC (PubMed:10468600, PubMed:11027362). Involved in R gene-mediated disease CC resistance. Functions upstream of the small GTPase RAC1 in the early CC steps of signaling (PubMed:12237405). Involved in brassinosteroid (BR) CC response. May not be a signaling molecule in BRI1-mediated perception CC or transduction (PubMed:17117160, PubMed:19036785). Acts together with CC the E3 ubiquitin ligase TUD1 to mediate a BR signaling pathway that CC affects plant growth and development (PubMed:23526892). CC {ECO:0000269|PubMed:10377457, ECO:0000269|PubMed:10468600, CC ECO:0000269|PubMed:11027362, ECO:0000269|PubMed:12237405, CC ECO:0000269|PubMed:17117160, ECO:0000269|PubMed:19036785, CC ECO:0000269|PubMed:23526892, ECO:0000305}. CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The CC alpha chain contains the guanine nucleotide binding site CC (PubMed:15078334). Interacts with COLD1 (PubMed:25728666). Interacts CC with TUD1 (PubMed:23526892). {ECO:0000269|PubMed:15078334, CC ECO:0000269|PubMed:23526892, ECO:0000269|PubMed:25728666}. CC -!- INTERACTION: CC Q0DJ33; Q40687: RGB1; NbExp=2; IntAct=EBI-1100098, EBI-1100119; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15078334}. CC -!- TISSUE SPECIFICITY: Highly expressed in young internodes. Expressed in CC the base of the stamen, pistil, lemma, and palea before flowering and CC in the pericarp of the ovary after fertilization. CC {ECO:0000269|PubMed:10377457}. CC -!- INDUCTION: By infection with an avirulent race of rice blast fungus CC (M.grisea) and sphingolipid elicitors (PubMed:12237405). Down-regulated CC by a virulent race of rice blast fungus (M.grisea) (PubMed:12237405). CC Down-regulated by 24-epi-brassinolide (PubMed:17117160). CC {ECO:0000269|PubMed:12237405, ECO:0000269|PubMed:17117160}. CC -!- DOMAIN: The helical domain (69-189) is required for self-activation. CC {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Dwarf plants and small seeds (PubMed:10377457, CC PubMed:10468600). Short internodes, leaves and panicles CC (PubMed:10377457). {ECO:0000269|PubMed:10377457, CC ECO:0000269|PubMed:10468600}. CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAF17140.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; D38232; BAA07405.1; -; mRNA. DR EMBL; AC117264; AAV43839.1; -; Genomic_DNA. DR EMBL; AC144739; AAW57778.2; -; Genomic_DNA. DR EMBL; AP008211; BAF17140.1; ALT_INIT; Genomic_DNA. DR EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_015639183.1; XM_015783697.1. DR AlphaFoldDB; Q0DJ33; -. DR SMR; Q0DJ33; -. DR BioGRID; 807485; 235. DR IntAct; Q0DJ33; 1. DR STRING; 39947.Q0DJ33; -. DR PaxDb; 39947-Q0DJ33; -. DR EnsemblPlants; Os05t0333200-01; Os05t0333200-01; Os05g0333200. DR GeneID; 4338448; -. DR Gramene; Os05t0333200-01; Os05t0333200-01; Os05g0333200. DR KEGG; osa:4338448; -. DR eggNOG; KOG0082; Eukaryota. DR HOGENOM; CLU_014184_4_0_1; -. DR InParanoid; Q0DJ33; -. DR OrthoDB; 2897309at2759; -. DR Proteomes; UP000000763; Chromosome 5. DR Proteomes; UP000059680; Chromosome 5. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central. DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW. DR GO; GO:0010476; P:gibberellin mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0002758; P:innate immune response-activating signaling pathway; IMP:UniProtKB. DR GO; GO:0048639; P:positive regulation of developmental growth; IMP:UniProtKB. DR CDD; cd00066; G-alpha; 1. DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR001019; Gprotein_alpha_su. DR InterPro; IPR011025; GproteinA_insert. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR002976; Plant_Gprotein_alpha. DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1. DR PANTHER; PTHR10218:SF302; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-8 SUBUNIT-RELATED; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR01242; GPROTEINAPLT. DR SMART; SM00275; G_alpha; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1. DR PROSITE; PS51882; G_ALPHA; 1. DR Genevisible; Q0DJ33; OS. PE 1: Evidence at protein level; KW Cell membrane; GTP-binding; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Myristate; Nucleotide-binding; Palmitate; Plant defense; KW Reference proteome; Transducer. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..380 FT /note="Guanine nucleotide-binding protein alpha-1 subunit" FT /id="PRO_0000203622" FT DOMAIN 38..380 FT /note="G-alpha" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 41..54 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 186..194 FT /note="G2 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 215..224 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 284..291 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 354..359 FT /note="G5 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT COMPBIAS 1..18 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 46..53 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 53 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 188..194 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 219..223 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 288..291 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 356 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000250|UniProtKB:P18064" FT LIPID 5 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P18064" FT MUTAGEN 223 FT /note="Q->L: Constitutively active." FT /evidence="ECO:0000269|PubMed:15078334" SQ SEQUENCE 380 AA; 44206 MW; 4EEFAEDAB4463612 CRC64; MGSSCSRSHS LSEAETTKNA KSADIDRRIL QETKAEQHIH KLLLLGAGES GKSTIFKQIK LLFQTGFDEA ELRSYTSVIH ANVYQTIKIL YEGAKELSQV ESDSSKYVIS PDNQEIGEKL SDIDGRLDYP LLNKELVLDV KRLWQDPAIQ ETYLRGSILQ LPDCAQYFME NLDRLAEAGY VPTKEDVLYA RVRTNGVVQI QFSPVGENKR GGEVYRLYDV GGQRNERRKW IHLFEGVNAV IFCAAISEYD QMLFEDETKN RMMETKELFD WVLKQRCFEK TSFILFLNKF DIFEKKIQKV PLSVCEWFKD YQPIAPGKQE VEHAYEFVKK KFEELYFQSS KPDRVDRVFK IYRTTALDQK LVKKTFKLID ESMRRSREGT //