GPA1_ARATH
ID GPA1_ARATH Reviewed; 383 AA.
AC P18064;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit {ECO:0000303|PubMed:2111018};
DE Short=GP-alpha-1 {ECO:0000303|PubMed:2111018};
GN Name=GPA1 {ECO:0000303|PubMed:2111018};
GN OrderedLocusNames=At2g26300 {ECO:0000312|Araport:AT2G26300};
GN ORFNames=T1D16.6 {ECO:0000312|EMBL:AAC14520.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2111018; DOI=10.1073/pnas.87.10.3821;
RA Ma H., Yanofsky M.F., Meyerowitz E.M.;
RT "Molecular cloning and characterization of GPA1, a G protein alpha subunit
RT gene from Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3821-3825(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=12912986; DOI=10.1074/jbc.m307321200;
RA Boisson B., Giglione C., Meinnel T.;
RT "Unexpected protein families including cell defense components feature in
RT the N-myristoylome of a higher eukaryote.";
RL J. Biol. Chem. 278:43418-43429(2003).
RN [6]
RP INTERACTION WITH PRN1.
RX PubMed=12837948; DOI=10.1105/tpc.011890;
RA Lapik Y.R., Kaufman L.S.;
RT "The Arabidopsis cupin domain protein AtPirin1 interacts with the G protein
RT alpha-subunit GPA1 and regulates seed germination and early seedling
RT development.";
RL Plant Cell 15:1578-1590(2003).
RN [7]
RP INTERACTION WITH RGS1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14500984; DOI=10.1126/science.1087790;
RA Chen J.G., Willard F.S., Huang J., Liang J., Chasse S.A., Jones A.M.,
RA Siderovski D.P.;
RT "A seven-transmembrane RGS protein that modulates plant cell
RT proliferation.";
RL Science 301:1728-1731(2003).
RN [8]
RP INTERACTION WITH PLDALPHA1.
RX PubMed=14594812; DOI=10.1074/jbc.m309529200;
RA Zhao J., Wang X.;
RT "Arabidopsis phospholipase Dalpha1 interacts with the heterotrimeric G-
RT protein alpha-subunit through a motif analogous to the DRY motif in G-
RT protein-coupled receptors.";
RL J. Biol. Chem. 279:1794-1800(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH GCR1.
RX PubMed=15155892; DOI=10.1105/tpc.020321;
RA Pandey S., Assmann S.M.;
RT "The Arabidopsis putative G protein-coupled receptor GCR1 interacts with
RT the G protein alpha subunit GPA1 and regulates abscisic acid signaling.";
RL Plant Cell 16:1616-1632(2004).
RN [10]
RP SUBUNIT, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-5, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17158913; DOI=10.1242/jcs.03284;
RA Adjobo-Hermans M.J.W., Goedhart J., Gadella T.W.J. Jr.;
RT "Plant G protein heterotrimers require dual lipidation motifs of Galpha and
RT Ggamma and do not dissociate upon activation.";
RL J. Cell Sci. 119:5087-5097(2006).
RN [11]
RP INTERACTION WITH THF1.
RX PubMed=16582010; DOI=10.1105/tpc.105.037259;
RA Huang J., Taylor J.P., Chen J.-G., Uhrig J.F., Schnell D.J., Nakagawa T.,
RA Korth K.L., Jones A.M.;
RT "The plastid protein THYLAKOID FORMATION1 and the plasma membrane G-protein
RT GPA1 interact in a novel sugar-signaling mechanism in Arabidopsis.";
RL Plant Cell 18:1226-1238(2006).
RN [12]
RP RETRACTED PAPER.
RC STRAIN=cv. Columbia;
RX PubMed=16581874; DOI=10.1104/pp.106.079038;
RA Pandey S., Chen J.-G., Jones A.M., Assmann S.M.;
RT "G-protein complex mutants are hypersensitive to abscisic acid regulation
RT of germination and postgermination development.";
RL Plant Physiol. 141:243-256(2006).
RN [13]
RP RETRACTION NOTICE OF PUBMED:16581874.
RX PubMed=31685692; DOI=10.1104/pp.19.01182;
RA Pandey S., Chen J.-G., Jones A.M., Assmann S.M.;
RL Plant Physiol. 181:1393-1393(2019).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ADT3.
RX PubMed=16415218; DOI=10.1104/pp.105.071282;
RA Warpeha K.M., Lateef S.S., Lapik Y., Anderson M., Lee B.-S., Kaufman L.S.;
RT "G-protein-coupled receptor 1, G-protein Galpha-subunit 1, and prephenate
RT dehydratase 1 are required for blue light-induced production of
RT phenylalanine in etiolated Arabidopsis.";
RL Plant Physiol. 140:844-855(2006).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=17322342; DOI=10.1104/pp.106.089904;
RA Warpeha K.M., Upadhyay S., Yeh J., Adamiak J., Hawkins S.I., Lapik Y.R.,
RA Anderson M.B., Kaufman L.S.;
RT "The GCR1, GPA1, PRN1, NF-Y signal chain mediates both blue light and
RT abscisic acid responses in Arabidopsis.";
RL Plant Physiol. 143:1590-1600(2007).
RN [16]
RP INTERACTION WITH RGS1.
RX PubMed=17951432; DOI=10.1073/pnas.0704751104;
RA Johnston C.A., Taylor J.P., Gao Y., Kimple A.J., Grigston J.C., Chen J.G.,
RA Siderovski D.P., Jones A.M., Willard F.S.;
RT "GTPase acceleration as the rate-limiting step in Arabidopsis G protein-
RT coupled sugar signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:17317-17322(2007).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=18499742; DOI=10.1093/pcp/pcn078;
RA Gao Y., Wang S., Asami T., Chen J.-G.;
RT "Loss-of-function mutations in the Arabidopsis heterotrimeric G-protein
RT alpha subunit enhance the developmental defects of brassinosteroid
RT signaling and biosynthesis mutants.";
RL Plant Cell Physiol. 49:1013-1024(2008).
RN [18]
RP INTERACTION WITH GTG1 AND GTG2.
RX PubMed=19135895; DOI=10.1016/j.cell.2008.12.026;
RA Pandey S., Nelson D.C., Assmann S.M.;
RT "Two novel GPCR-type G proteins are abscisic acid receptors in
RT Arabidopsis.";
RL Cell 136:136-148(2009).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20862254; DOI=10.1371/journal.pone.0012833;
RA Booker K.S., Schwarz J., Garrett M.B., Jones A.M.;
RT "Glucose attenuation of auxin-mediated bimodality in lateral root formation
RT is partly coupled by the heterotrimeric G protein complex.";
RL PLoS ONE 5:E12833-E12833(2010).
RN [20]
RP INTERACTION WITH PLDALPHA1.
RX PubMed=23913032; DOI=10.1007/978-1-62703-532-3_3;
RA Zhao J., Wang X.;
RT "Biochemical analysis of the interaction between phospholipase Dalpha1 and
RT GTP-binding protein alpha-subunit from Arabidopsis thaliana.";
RL Methods Mol. Biol. 1043:21-35(2013).
RN [21]
RP LACK OF INTERACTION WITH RACK1A; RACK1B OR RACK1C.
RX PubMed=25731164; DOI=10.1038/nature14243;
RA Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y., Djonovic S.,
RA Millet Y., Bush J., McConkey B.J., Sheen J., Ausubel F.M.;
RT "Pathogen-secreted proteases activate a novel plant immune pathway.";
RL Nature 521:213-216(2015).
RN [22]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CAND2/PMTR1.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=29702752; DOI=10.1111/jpi.12500;
RA Wei J., Li D.-X., Zhang J.-R., Shan C., Rengel Z., Song Z.-B., Chen Q.;
RT "Phytomelatonin receptor PMTR1-mediated signaling regulates stomatal
RT closure in Arabidopsis thaliana.";
RL J. Pineal Res. 65:E12500-E12500(2018).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 37-383 IN COMPLEX WITH GTP AND
RP MAGNESIUM ION, FUNCTION, AND SELF-ACTIVATION.
RX PubMed=21304159; DOI=10.1126/scisignal.2001446;
RA Jones J.C., Duffy J.W., Machius M., Temple B.R., Dohlman H.G., Jones A.M.;
RT "The crystal structure of a self-activating G protein alpha subunit reveals
RT its distinct mechanism of signal initiation.";
RL Sci. Signal. 4:RA8-RA8(2011).
CC -!- FUNCTION: Exhibits a fast rate of basal nucleotide exchange. Guanine
CC nucleotide-binding proteins (G proteins) are involved as modulators or
CC transducers in various transmembrane signaling systems. Together with
CC GCR1, may regulate the cell cycle via a signaling cascade that uses
CC phosphatidylinositol-specific phospholipase C (PI-PLC) as an effector
CC and inositol 1,4,5-trisphosphate (IP(3)) as a second messenger.
CC Promotes abscisic acid (ABA) responses in guard cells. Involved in the
CC blue light (BL) signaling. Together with GCR1 and ADT3, required for
CC BL-mediated synthesis of phenylpyruvate and subsequently of
CC phenylalanine (Phe), in etiolated seedlings. Modulates root
CC architecture (e.g. lateral root formation). Negatively regulated by
CC RGS1. In collaboration with CAND2/PMTR1, regulates the melatonin-
CC mediated stomatal closure involving H(2)O(2) and Ca(2+) signals
CC (PubMed:29702752). {ECO:0000269|PubMed:15155892,
CC ECO:0000269|PubMed:16415218, ECO:0000269|PubMed:17322342,
CC ECO:0000269|PubMed:20862254, ECO:0000269|PubMed:21304159,
CC ECO:0000269|PubMed:29702752}.
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 RGS1, THF1, the pirin protein PRN1, GTG1 and GTG2. Binds to GCR1.
CC May interact with ADT3 (PubMed:12837948, PubMed:14500984,
CC PubMed:15155892, PubMed:16415218, PubMed:16582010, PubMed:17158913,
CC PubMed:17951432, PubMed:19135895, PubMed:21304159). No interactions
CC with RACK1A, RACK1B or RACK1C (PubMed:25731164). Interacts with
CC PLDALPHA1 (PubMed:14594812, PubMed:23913032). Interacts with
CC CAND2/PMTR1 (PubMed:29702752). {ECO:0000269|PubMed:12837948,
CC ECO:0000269|PubMed:14500984, ECO:0000269|PubMed:14594812,
CC ECO:0000269|PubMed:15155892, ECO:0000269|PubMed:16415218,
CC ECO:0000269|PubMed:16582010, ECO:0000269|PubMed:17158913,
CC ECO:0000269|PubMed:17951432, ECO:0000269|PubMed:19135895,
CC ECO:0000269|PubMed:21304159, ECO:0000269|PubMed:23913032,
CC ECO:0000269|PubMed:25731164, ECO:0000269|PubMed:29702752}.
CC -!- INTERACTION:
CC P18064; P49177: GB1; NbExp=4; IntAct=EBI-443890, EBI-1632851;
CC P18064; O04714: GCR1; NbExp=6; IntAct=EBI-443890, EBI-443899;
CC P18064; F4IEM5: GCR2; NbExp=5; IntAct=EBI-443890, EBI-1804974;
CC P18064; Q9XIP7: GTG1; NbExp=2; IntAct=EBI-443890, EBI-2214605;
CC P18064; Q0WQG8: GTG2; NbExp=2; IntAct=EBI-443890, EBI-2214623;
CC P18064; Q38882: PLDALPHA1; NbExp=3; IntAct=EBI-443890, EBI-962294;
CC P18064; Q9LX49: PRN1; NbExp=3; IntAct=EBI-443890, EBI-1606661;
CC P18064; Q8H1F2: RGS1; NbExp=7; IntAct=EBI-443890, EBI-1627025;
CC P18064; Q9SKT0: THF1; NbExp=4; IntAct=EBI-443890, EBI-972220;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14500984,
CC ECO:0000269|PubMed:17158913}.
CC -!- TISSUE SPECIFICITY: More abundant in roots and/or leaves.
CC {ECO:0000269|PubMed:14500984}.
CC -!- DOMAIN: The helical domain (68-188) is required for self-activation.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to ABA and glucose (Glc) during
CC and after seed germination. Altered response to blue light (BL).
CC Abnormal roots architecture; more auxin-induced lateral roots. Reduced
CC H(2)O(2) concentration in melatonin-treated guard cells associated with
CC impaired abscisic acid- (ABA) and melatonin-induced stomatal aperture
CC (PubMed:29702752). {ECO:0000269|PubMed:16415218,
CC ECO:0000269|PubMed:17322342, ECO:0000269|PubMed:18499742,
CC ECO:0000269|PubMed:20862254, ECO:0000269|PubMed:29702752}.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
CC -!- CAUTION: An article reported a role as negative regulator of ABA during
CC seed germination; however, this paper was later retracted.
CC {ECO:0000305|PubMed:16581874, ECO:0000305|PubMed:31685692}.
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DR EMBL; M32887; AAA32805.1; -; mRNA.
DR EMBL; AC004484; AAC14520.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07820.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62935.1; -; Genomic_DNA.
DR EMBL; AY093966; AAM16227.1; -; mRNA.
DR EMBL; AF385704; AAK60296.1; -; mRNA.
DR PIR; A35864; RGMUOA.
DR RefSeq; NP_001325056.1; NM_001336055.1.
DR RefSeq; NP_180198.1; NM_128187.3.
DR PDB; 2XTZ; X-ray; 2.34 A; A/B/C=37-383.
DR PDBsum; 2XTZ; -.
DR AlphaFoldDB; P18064; -.
DR SMR; P18064; -.
DR BioGRID; 2522; 56.
DR DIP; DIP-31793N; -.
DR IntAct; P18064; 19.
DR MINT; P18064; -.
DR STRING; 3702.AT2G26300.1; -.
DR TCDB; 8.A.92.1.2; the g-protein AlphaBetaGama complex (gpc) family.
DR iPTMnet; P18064; -.
DR SwissPalm; P18064; -.
DR PaxDb; P18064; -.
DR PRIDE; P18064; -.
DR ProteomicsDB; 248501; -.
DR EnsemblPlants; AT2G26300.1; AT2G26300.1; AT2G26300.
DR EnsemblPlants; AT2G26300.2; AT2G26300.2; AT2G26300.
DR GeneID; 817170; -.
DR Gramene; AT2G26300.1; AT2G26300.1; AT2G26300.
DR Gramene; AT2G26300.2; AT2G26300.2; AT2G26300.
DR KEGG; ath:AT2G26300; -.
DR Araport; AT2G26300; -.
DR TAIR; locus:2005529; AT2G26300.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_4_0_1; -.
DR InParanoid; P18064; -.
DR OMA; QVIWADA; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P18064; -.
DR BioCyc; ARA:AT2G26300-MON; -.
DR PRO; PR:P18064; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P18064; baseline and differential.
DR Genevisible; P18064; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0016247; F:channel regulator activity; IMP:TAIR.
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; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:TAIR.
DR GO; GO:0051020; F:GTPase binding; IPI:TAIR.
DR GO; GO:0005095; F:GTPase inhibitor activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009785; P:blue light signaling pathway; IMP:UniProtKB.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IMP:TAIR.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:TAIR.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009749; P:response to glucose; IGI:TAIR.
DR GO; GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IMP:TAIR.
DR GO; GO:0019236; P:response to pheromone; IMP:UniProtKB.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; IMP:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IMP:TAIR.
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 3D-structure; Abscisic acid signaling pathway; Cell membrane; GTP-binding;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..383
FT /note="Guanine nucleotide-binding protein alpha-1 subunit"
FT /id="PRO_0000203618"
FT DOMAIN 37..383
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..53
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 185..193
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 214..223
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 283..290
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 353..358
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 48..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21304159,
FT ECO:0007744|PDB:2XTZ"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21304159,
FT ECO:0007744|PDB:2XTZ"
FT BINDING 162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21304159,
FT ECO:0007744|PDB:2XTZ"
FT BINDING 187..188
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21304159,
FT ECO:0007744|PDB:2XTZ"
FT BINDING 193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21304159,
FT ECO:0007744|PDB:2XTZ"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21304159,
FT ECO:0007744|PDB:2XTZ"
FT BINDING 221
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21304159,
FT ECO:0007744|PDB:2XTZ"
FT BINDING 287..290
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21304159,
FT ECO:0007744|PDB:2XTZ"
FT BINDING 355
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21304159,
FT ECO:0007744|PDB:2XTZ"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12912986,
FT ECO:0000269|PubMed:17158913"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:17158913"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 75..99
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:2XTZ"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:2XTZ"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2XTZ"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2XTZ"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:2XTZ"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 316..337
FT /evidence="ECO:0007829|PDB:2XTZ"
FT TURN 341..345
FT /evidence="ECO:0007829|PDB:2XTZ"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:2XTZ"
FT HELIX 358..378
FT /evidence="ECO:0007829|PDB:2XTZ"
SQ SEQUENCE 383 AA; 44546 MW; 46BF8650E067F968 CRC64;
MGLLCSRSRH HTEDTDENTQ AAEIERRIEQ EAKAEKHIRK LLLLGAGESG KSTIFKQIKL
LFQTGFDEGE LKSYVPVIHA NVYQTIKLLH DGTKEFAQNE TDSAKYMLSS ESIAIGEKLS
EIGGRLDYPR LTKDIAEGIE TLWKDPAIQE TCARGNELQV PDCTKYLMEN LKRLSDINYI
PTKEDVLYAR VRTTGVVEIQ FSPVGENKKS GEVYRLFDVG GQRNERRKWI HLFEGVTAVI
FCAAISEYDQ TLFEDEQKNR MMETKELFDW VLKQPCFEKT SFMLFLNKFD IFEKKVLDVP
LNVCEWFRDY QPVSSGKQEI EHAYEFVKKK FEELYYQNTA PDRVDRVFKI YRTTALDQKL
VKKTFKLVDE TLRRRNLLEA GLL
