GBB_ARATH
ID GBB_ARATH Reviewed; 377 AA.
AC P49177;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Guanine nucleotide-binding protein subunit beta;
DE AltName: Full=AGB1;
DE AltName: Full=transducin;
GN Name=GB1; OrderedLocusNames=At4g34460; ORFNames=T4L20.40;
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].
RC STRAIN=cv. Columbia;
RX PubMed=7937804; DOI=10.1073/pnas.91.20.9554;
RA Weiss C.A., Garnaat C.W., Mukai K., Hu Y., Ma H.;
RT "Isolation of cDNAs encoding guanine nucleotide-binding protein beta-
RT subunit homologues from maize (ZGB1) and Arabidopsis (AGB1).";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9554-9558(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 INTERACTION WITH GG1.
RC STRAIN=cv. Columbia;
RX PubMed=11121078; DOI=10.1073/pnas.97.26.14784;
RA Mason M.G., Botella J.R.;
RT "Completing the heterotrimer: isolation and characterization of an
RT Arabidopsis thaliana G protein gamma-subunit cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14784-14788(2000).
RN [5]
RP INTERACTION WITH GG2.
RC STRAIN=cv. Columbia;
RX PubMed=11513956; DOI=10.1016/s0167-4781(01)00262-7;
RA Mason M.G., Botella J.R.;
RT "Isolation of a novel G-protein gamma-subunit from Arabidopsis thaliana and
RT its interaction with Gbeta.";
RL Biochim. Biophys. Acta 1520:147-153(2001).
RN [6]
RP SUBUNIT, AND SUBCELLULAR 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 [7]
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 [8]
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, TISSUE SPECIFICITY, AND INDUCTION
RP BY ALTERNARIA BRASSICICOLA AND FUSARIUM OXYSPORUM.
RC STRAIN=cv. Columbia;
RX PubMed=17468261; DOI=10.1105/tpc.107.050096;
RA Trusov Y., Rookes J.E., Tilbrook K., Chakravorty D., Mason M.G.,
RA Anderson D., Chen J.-G., Jones A.M., Botella J.R.;
RT "Heterotrimeric G protein gamma subunits provide functional selectivity in
RT Gbetagamma dimer signaling in Arabidopsis.";
RL Plant Cell 19:1235-1250(2007).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17492287; DOI=10.1007/s00299-007-0356-1;
RA Anderson D.J., Botella J.R.;
RT "Expression analysis and subcellular localization of the Arabidopsis
RT thaliana G-protein beta-subunit AGB1.";
RL Plant Cell Rep. 26:1469-1480(2007).
RN [11]
RP DWD MOTIF.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18397373; DOI=10.1111/j.1365-313x.2008.03506.x;
RA Pandey S., Monshausen G.B., Ding L., Assmann S.M.;
RT "Regulation of root-wave response by extra large and conventional G
RT proteins in Arabidopsis thaliana.";
RL Plant J. 55:311-322(2008).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=18441222; DOI=10.1104/pp.108.117655;
RA Trusov Y., Zhang W., Assmann S.M., Botella J.R.;
RT "Ggamma1 + Ggamma2 not equal to Gbeta: heterotrimeric G protein Ggamma-
RT deficient mutants do not recapitulate all phenotypes of Gbeta-deficient
RT mutants.";
RL Plant Physiol. 147:636-649(2008).
RN [14]
RP INTERACTION WITH XLG2.
RX PubMed=19825634; DOI=10.1093/mp/ssp001;
RA Zhu H., Li G.J., Ding L., Cui X., Berg H., Assmann S.M., Xia Y.;
RT "Arabidopsis extra large G-protein 2 (XLG2) interacts with the Gbeta
RT subunit of heterotrimeric G protein and functions in disease resistance.";
RL Mol. Plant 2:513-525(2009).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH NDL1; NDL2 AND NDL3.
RC STRAIN=cv. Columbia;
RX PubMed=19948787; DOI=10.1105/tpc.109.065557;
RA Mudgil Y., Uhrig J.F., Zhou J., Temple B., Jiang K., Jones A.M.;
RT "Arabidopsis N-MYC DOWNREGULATED-LIKE1, a positive regulator of auxin
RT transport in a G protein-mediated pathway.";
RL Plant Cell 21:3591-3609(2009).
RN [16]
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 [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21980142; DOI=10.1093/mp/ssr082;
RA Delgado-Cerezo M., Sanchez-Rodriguez C., Escudero V., Miedes E.,
RA Fernandez P.V., Jorda L., Hernandez-Blanco C., Sanchez-Vallet A.,
RA Bednarek P., Schulze-Lefert P., Somerville S., Estevez J.M., Persson S.,
RA Molina A.;
RT "Arabidopsis heterotrimeric G-protein regulates cell wall defense and
RT resistance to necrotrophic fungi.";
RL Mol. Plant 5:98-114(2012).
RN [18]
RP INTERACTION WITH WNK8.
RX PubMed=22940907; DOI=10.1038/ncb2568;
RA Urano D., Phan N., Jones J.C., Yang J., Huang J., Grigston J., Taylor J.P.,
RA Jones A.M.;
RT "Endocytosis of the seven-transmembrane RGS1 protein activates G-protein-
RT coupled signalling in Arabidopsis.";
RL Nat. Cell Biol. 14:1079-1088(2012).
RN [19]
RP INTERACTION WITH RACK1A; RACK1B AND 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 [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ZAR1.
RX PubMed=27014878; DOI=10.1371/journal.pgen.1005933;
RA Yu T.Y., Shi D.Q., Jia P.F., Tang J., Li H.J., Liu J., Yang W.C.;
RT "The Arabidopsis receptor kinase ZAR1 is required for zygote asymmetric
RT division and its daughter cell fate.";
RL PLoS Genet. 12:E1005933-E1005933(2016).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction. The heterotrimeric G-protein controls defense responses to
CC necrotrophic and vascular fungi probably by modulating cell wall-
CC related genes expression (e.g. lower xylose content in cell walls);
CC involved in resistance to fungal pathogens such as Alternaria
CC brassicicola and Fusarium oxysporum. Modulates root architecture (e.g.
CC lateral root formation). Acts with XGL3 in the positive regulation of
CC root waving and root skewing. Involved in the asymmetric division of
CC zygote and specification of apical and basal cell lineages
CC (PubMed:27014878). {ECO:0000269|PubMed:17468261,
CC ECO:0000269|PubMed:18397373, ECO:0000269|PubMed:18441222,
CC ECO:0000269|PubMed:19948787, ECO:0000269|PubMed:20862254,
CC ECO:0000269|PubMed:21980142, ECO:0000269|PubMed:27014878}.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC Interacts with the gamma subunits GG1 and GG2. The dimers GB1-GG1 and
CC GB1-GG2 interact with NDL1, NDL2 and NDL3. Interacts with WNK8.
CC Interacts with XLG2 (PubMed:11121078, PubMed:11513956, PubMed:17158913,
CC PubMed:17468261, PubMed:19825634, PubMed:19948787, PubMed:22940907).
CC Interacts with RACK1A, RACK1B and RACK1C (PubMed:25731164). Interacts
CC with ZAR1 (via GBeta-binding domain) (PubMed:27014878).
CC {ECO:0000269|PubMed:11121078, ECO:0000269|PubMed:11513956,
CC ECO:0000269|PubMed:17158913, ECO:0000269|PubMed:17468261,
CC ECO:0000269|PubMed:19825634, ECO:0000269|PubMed:19948787,
CC ECO:0000269|PubMed:22940907, ECO:0000269|PubMed:25731164,
CC ECO:0000269|PubMed:27014878}.
CC -!- INTERACTION:
CC P49177; Q9FDX9: GG1; NbExp=8; IntAct=EBI-1632851, EBI-1750878;
CC P49177; Q93V47: GG2; NbExp=2; IntAct=EBI-1632851, EBI-1751115;
CC P49177; P18064: GPA1; NbExp=4; IntAct=EBI-1632851, EBI-443890;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17158913,
CC ECO:0000269|PubMed:17492287, ECO:0000269|PubMed:27014878}. Cytoplasm
CC {ECO:0000269|PubMed:17158913}. Nucleus {ECO:0000269|PubMed:17492287,
CC ECO:0000269|PubMed:27014878}. Note=Localized to the cell membrane when
CC attached to gamma subunits as GG1 and GG2 or to both the plasma
CC membrane and the nucleus when interacting with ZAR1.
CC {ECO:0000269|PubMed:17158913, ECO:0000269|PubMed:27014878}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P49177-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings (especially at the
CC hypocotyl/root junction), roots, leaves (restricted to veins and guard
CC cells), and flowers (PubMed:17468261, PubMed:18441222). Also present in
CC hydathods (PubMed:17468261). Expressed in guard cells, mesophyll tissue
CC of cotyledons, trichomes and whole siliques, but not in seeds
CC (PubMed:17492287). {ECO:0000269|PubMed:17468261,
CC ECO:0000269|PubMed:17492287, ECO:0000269|PubMed:18441222}.
CC -!- DEVELOPMENTAL STAGE: In flowers, mostly expressed in stigma and pollen,
CC and moderately present in sepals and stamen filaments. In siliques,
CC observed at both ends, gradually disappearing toward the center.
CC {ECO:0000269|PubMed:18441222}.
CC -!- INDUCTION: Induced locally by Alternaria brassicicola but systemically
CC by Fusarium oxysporum. {ECO:0000269|PubMed:17468261}.
CC -!- DOMAIN: The DWD box is required for interaction with DDB1A.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Shorter hypocotyls and abnormal roots
CC architecture; more auxin-induced lateral roots. Enhanced susceptibility
CC to necrotrophic and vascular pathogenic fungi, such as Alternaria
CC brassicicola, Plectosphaerella cucumerina and Fusarium oxysporum
CC associated with a disturbed expression of genes involved in cell wall
CC metabolism. Longer and wider primary roots with faster growth. Severely
CC compromised root waving and abnormal root skewing response.
CC Hypersensitivity to ethylene (ACC). {ECO:0000269|PubMed:17468261,
CC ECO:0000269|PubMed:18397373, ECO:0000269|PubMed:18441222,
CC ECO:0000269|PubMed:19948787, ECO:0000269|PubMed:20862254,
CC ECO:0000269|PubMed:21980142}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {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; U12232; AAA50445.1; -; mRNA.
DR EMBL; AL023094; CAA18825.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80163.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86381.1; -; Genomic_DNA.
DR PIR; T05266; T05266.
DR RefSeq; NP_195172.1; NM_119611.5. [P49177-1]
DR AlphaFoldDB; P49177; -.
DR SMR; P49177; -.
DR BioGRID; 14879; 96.
DR DIP; DIP-40108N; -.
DR IntAct; P49177; 11.
DR STRING; 3702.AT4G34460.1; -.
DR TCDB; 8.A.92.1.2; the g-protein AlphaBetaGama complex (gpc) family.
DR PaxDb; P49177; -.
DR PRIDE; P49177; -.
DR EnsemblPlants; AT4G34460.1; AT4G34460.1; AT4G34460. [P49177-1]
DR GeneID; 829597; -.
DR Gramene; AT4G34460.1; AT4G34460.1; AT4G34460. [P49177-1]
DR KEGG; ath:AT4G34460; -.
DR Araport; AT4G34460; -.
DR TAIR; locus:2139489; AT4G34460.
DR eggNOG; KOG0286; Eukaryota.
DR InParanoid; P49177; -.
DR PhylomeDB; P49177; -.
DR PRO; PR:P49177; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P49177; baseline and differential.
DR Genevisible; P49177; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IPI:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:TAIR.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:TAIR.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:1905392; P:plant organ morphogenesis; IMP:TAIR.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:2000280; P:regulation of root development; IGI:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR GO; GO:0009991; P:response to extracellular stimulus; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IGI:TAIR.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR001632; Gprotein_B.
DR InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19850; PTHR19850; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00319; GPROTEINB.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Cell membrane;
KW Cytoplasm; Membrane; Nucleus; Plant defense; Reference proteome; Repeat;
KW Transducer; WD repeat.
FT CHAIN 1..377
FT /note="Guanine nucleotide-binding protein subunit beta"
FT /id="PRO_0000127722"
FT REPEAT 63..93
FT /note="WD 1"
FT REPEAT 105..135
FT /note="WD 2"
FT REPEAT 154..185
FT /note="WD 3"
FT REPEAT 202..233
FT /note="WD 4"
FT REPEAT 246..276
FT /note="WD 5"
FT REPEAT 292..323
FT /note="WD 6"
FT REPEAT 339..369
FT /note="WD 7"
FT MOTIF 220..235
FT /note="DWD box 1"
FT MOTIF 263..278
FT /note="DWD box 1"
SQ SEQUENCE 377 AA; 41006 MW; 06673A2F707A2F44 CRC64;
MSVSELKERH AVATETVNNL RDQLRQRRLQ LLDTDVARYS AAQGRTRVSF GATDLVCCRT
LQGHTGKVYS LDWTPERNRI VSASQDGRLI VWNALTSQKT HAIKLPCAWV MTCAFSPNGQ
SVACGGLDSV CSIFSLSSTA DKDGTVPVSR MLTGHRGYVS CCQYVPNEDA HLITSSGDQT
CILWDVTTGL KTSVFGGEFQ SGHTADVLSV SISGSNPNWF ISGSCDSTAR LWDTRAASRA
VRTFHGHEGD VNTVKFFPDG YRFGTGSDDG TCRLYDIRTG HQLQVYQPHG DGENGPVTSI
AFSVSGRLLF AGYASNNTCY VWDTLLGEVV LDLGLQQDSH RNRISCLGLS ADGSALCTGS
WDSNLKIWAF GGHRRVI
