ID J3MDA9_ORYBR Unreviewed; 390 AA.
AC J3MDA9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Guanine nucleotide-binding protein alpha subunit {ECO:0000256|RuleBase:RU368109};
DE Short=GP-alpha {ECO:0000256|RuleBase:RU368109};
GN Name=102719211 {ECO:0000313|EnsemblPlants:OB06G20030.1};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB06G20030.1};
RN [1] {ECO:0000313|EnsemblPlants:OB06G20030.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB06G20030.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB06G20030.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (FEB-2015) to UniProtKB.
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. {ECO:0000256|RuleBase:RU368109}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC {ECO:0000256|RuleBase:RU368109}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU368109}.
CC -!- DOMAIN: The helical domain is required for self-activation.
CC {ECO:0000256|RuleBase:RU368109}.
CC -!- SIMILARITY: Belongs to the G-alpha family.
CC {ECO:0000256|ARBA:ARBA00005804, ECO:0000256|RuleBase:RU368109}.
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DR RefSeq; XP_006656002.1; XM_006655939.2.
DR AlphaFoldDB; J3MDA9; -.
DR STRING; 4533.J3MDA9; -.
DR EnsemblPlants; OB06G20030.1; OB06G20030.1; OB06G20030.
DR GeneID; 102719211; -.
DR Gramene; OB06G20030.1; OB06G20030.1; OB06G20030.
DR KEGG; obr:102719211; -.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_4_0_1; -.
DR OMA; QVIWADA; -.
DR OrthoDB; 2897309at2759; -.
DR Proteomes; UP000006038; Chromosome 6.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:UniProtKB-UniRule.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0010476; P:gibberellin mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0002758; P:innate immune response-activating signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0048639; P:positive regulation of developmental growth; IEA:EnsemblPlants.
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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU368109};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR602976-
KW 1}; Lipoprotein {ECO:0000256|RuleBase:RU368109};
KW Magnesium {ECO:0000256|PIRSR:PIRSR602976-2, ECO:0000256|RuleBase:RU368109};
KW Membrane {ECO:0000256|RuleBase:RU368109};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602976-2,
KW ECO:0000256|RuleBase:RU368109}; Myristate {ECO:0000256|RuleBase:RU368109};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU368109};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|RuleBase:RU368109};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU368109}.
FT BINDING 59..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 63
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
FT BINDING 173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 198..199
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
FT BINDING 232
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 298..301
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 366
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
SQ SEQUENCE 390 AA; 45348 MW; B003CC413D7CD8F9 CRC64;
MSVLTCVLDN MGSSCSRSHL LSEAETAENA KSADIDRRIL QETKAEQHIY KLLLLGAGES
GKSTIFKQIK LLFQTGFDEA ELRSYTSVIH ANVYQTIKVL YDGAKELYQV ESDSSKYVIC
PDNQEIGEKL SEIDGRSGYP LLSEELVHDV KKLWQDPAIQ ETYSRGSILQ LPDCAQYFME
NLDRLAEADY VPTKEDVLYA RVRTNGVVQI QFSPVGENKR GGEVYRLYDV GGQRNERRKW
IHLFEGVNAV IFCAAISEYD QMLFEDETKN RMMETKELFD WVLKQRCFEK TSFMLFLNKF
DIFERKIQKV PLSVCEWFKD YQPIAPGKQE VEHAYEFVKK KFEELYFQSS KPDRVDRVFK
IYRTTALDQK LVKKTFKLID ESMRRSREGT
//
