ID K7M5X9_SOYBN Unreviewed; 384 AA.
AC K7M5X9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Guanine nucleotide-binding protein alpha subunit {ECO:0000256|RuleBase:RU368109};
DE Short=GP-alpha {ECO:0000256|RuleBase:RU368109};
GN Name=100781223 {ECO:0000313|EnsemblPlants:KRH15592};
GN ORFNames=GLYMA_14G098000 {ECO:0000313|EMBL:KRH15593.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH15593.1};
RN [1] {ECO:0000313|EMBL:KRH15593.1, ECO:0000313|EnsemblPlants:KRH15592}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH15592};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH15593.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH15592}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH15592};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH15593.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH15593.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. {ECO:0000256|ARBA:ARBA00003069,
CC 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|ARBA:ARBA00011356, 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}.
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; CM000847; KRH15592.1; -; Genomic_DNA.
DR EMBL; CM000847; KRH15593.1; -; Genomic_DNA.
DR AlphaFoldDB; K7M5X9; -.
DR EnsemblPlants; KRH15592; KRH15592; GLYMA_14G098000.
DR EnsemblPlants; KRH15593; KRH15593; GLYMA_14G098000.
DR Gramene; KRH15592; KRH15592; GLYMA_14G098000.
DR Gramene; KRH15593; KRH15593; GLYMA_14G098000.
DR HOGENOM; CLU_014184_4_0_1; -.
DR Proteomes; UP000008827; Chromosome 14.
DR ExpressionAtlas; K7M5X9; baseline and differential.
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 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};
KW Myristate {ECO:0000256|ARBA:ARBA00022707, 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:UP000008827};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU368109}.
FT BINDING 49..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
FT BINDING 163
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 188..189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
FT BINDING 222
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 288..291
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
SQ SEQUENCE 384 AA; 44809 MW; 980CDF18D359CFCE CRC64;
MGLLCSRNRR YNDADAEESA QTAEIERRIE LETKAEKHIQ KLLLLGAGES GKSTIFKQIK
LLFQTGFDEA ELKSYLPVIH ANVYQTIKLL HDGSKEFAQN DVDSSKYVIS NENKEIGEKL
SEIGGRLDYP YLTKELAQEI ENLWKDPAIQ ETYARGSELQ IPDCTDYFME NLQRLSDTNY
VPTKEDVLYA RVRTSGVVEI QFSPVGESKK SGEVYRLFDV GGQRNERRKW IHLFEGVSAV
IFCAAISEYD QTLFEDENRN RMTETKELFE WILKQPCFEK TSFMLFLNKF DIFEKKILKV
PLNVCEWFKD YQPVSTGKQE IEHAYEFVKK KFEESYFQST APDRVDRVFK IYRTTALDQK
VVKKTFKLVD ETLRRRNLFE AGLL
//
