GPA1_ORYSI
ID GPA1_ORYSI Reviewed; 380 AA.
AC A2Y3B5; 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 92.
DE RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
DE Short=GP-alpha-1;
DE AltName: Full=Protein Dwarf1;
GN Name=GPA1; Synonyms=D1, GA1, RGA1; ORFNames=OsI_018808;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. IR36; TISSUE=Coleoptile;
RX PubMed=7766894; DOI=10.1007/bf00020885;
RA Seo H.S., Kim H.Y., Lee S.Y., Bahk J.D., Cho M.J.;
RT "Molecular cloning and characterization of RGA1 encoding a G protein alpha
RT subunit from rice (Oryza sativa L. IR-36).";
RL Plant Mol. Biol. 27:1119-1131(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-325.
RX AGRICOLA=IND43738818;
RA Guo Y.L., Ge S.;
RT "Molecular phylogeny of Oryzeae (Poaceae) based on DNA sequences from
RT chloroplast, mitochondrial, and nuclear genomes.";
RL Am. J. Bot. 92:1548-1558(2005).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. May function in a signal transduction pathway required for
CC normal growth and development of internodes, leaves, panicles and
CC seeds. Involved in gibberellin signal transduction. Involved in R gene-
CC mediated disease resistance. Functions upstream of the small GTPase
CC RAC1 in the early steps of signaling. Involved in brassinosteroid
CC response. May not be a signaling molecule in BRI1-mediated perception
CC or transduction. {ECO:0000250|UniProtKB:Q0DJ33}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site. Interacts
CC with COLD1. {ECO:0000250|UniProtKB:Q0DJ33}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q0DJ33}.
CC -!- DOMAIN: The helical domain (69-189) is required for self-activation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA98738.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L28001; AAC41657.1; -; mRNA.
DR EMBL; L35844; AAA98738.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY792541; AAX54917.1; -; Genomic_DNA.
DR PIR; S56670; S56670.
DR PIR; T03980; T03980.
DR AlphaFoldDB; A2Y3B5; -.
DR SMR; A2Y3B5; -.
DR STRING; 39946.A2Y3B5; -.
DR PRIDE; A2Y3B5; -.
DR HOGENOM; CLU_014184_4_0_1; -.
DR Proteomes; UP000007015; Chromosome 5.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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_0000295659"
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 CONFLICT 48
FT /note="G -> A (in Ref. 1; AAA98738)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="A -> V (in Ref. 1; AAA98738)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="D -> V (in Ref. 1; AAA98738/AAC41657)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="F -> C (in Ref. 1; AAA98738/AAC41657)"
FT /evidence="ECO:0000305"
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
