GPA1_ORYSJ
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 03-AUG-2022, entry version 121.
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,
GN RGA1 {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};
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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; 4530.OS05T0333200-00; -.
DR PaxDb; Q0DJ33; -.
DR PRIDE; 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; 754573at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q0DJ33; OS.
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 signal transduction; 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; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR10218; 1.
DR PANTHER; PTHR10218:SF333; PTHR10218:SF333; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR01242; GPROTEINAPLT.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
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
