GAI_ARATH
ID GAI_ARATH Reviewed; 533 AA.
AC Q9LQT8; O23643; O23724;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=DELLA protein GAI {ECO:0000303|PubMed:9389651};
DE AltName: Full=GRAS family protein 3;
DE Short=AtGRAS-3;
DE AltName: Full=Gibberellic acid-insensitive mutant protein {ECO:0000303|PubMed:9389651};
DE AltName: Full=Restoration of growth on ammonia protein 2 {ECO:0000303|PubMed:9237632};
GN Name=GAI {ECO:0000303|PubMed:9389651};
GN Synonyms=RGA2 {ECO:0000303|PubMed:9237632};
GN OrderedLocusNames=At1g14920 {ECO:0000312|Araport:AT1G14920};
GN ORFNames=F10B6.34 {ECO:0000312|EMBL:AAF79228.1};
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9237632; DOI=10.1016/s0014-5793(97)00590-5;
RA Truong H.-N., Caboche M., Daniel-Vedele F.;
RT "Sequence and characterization of two Arabidopsis thaliana cDNAs isolated
RT by functional complementation of a yeast gln3 gdh1 mutant.";
RL FEBS Lett. 410:213-218(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF
RP 28-ASP--ALA-44.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9389651; DOI=10.1101/gad.11.23.3194;
RA Peng J., Carol P., Richards D.E., King K.E., Cowling R.J., Murphy G.P.,
RA Harberd N.P.;
RT "The Arabidopsis GAI gene defines a signaling pathway that negatively
RT regulates gibberellin responses.";
RL Genes Dev. 11:3194-3205(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=9490740; DOI=10.2307/3870695;
RA Silverstone A.L., Ciampaglio C.N., Sun T.-P.;
RT "The Arabidopsis RGA gene encodes a transcriptional regulator repressing
RT the gibberellin signal transduction pathway.";
RL Plant Cell 10:155-169(1998).
RN [7]
RP FUNCTION.
RX PubMed=11606551; DOI=10.1093/genetics/159.2.767;
RA King K.E., Moritz T., Harberd N.P.;
RT "Gibberellins are not required for normal stem growth in Arabidopsis
RT thaliana in the absence of GAI and RGA.";
RL Genetics 159:767-776(2001).
RN [8]
RP FUNCTION.
RX PubMed=11606552; DOI=10.1093/genetics/159.2.777;
RA Dill A., Sun T.-P.;
RT "Synergistic derepression of gibberellin signaling by removing RGA and GAI
RT function in Arabidopsis thaliana.";
RL Genetics 159:777-785(2001).
RN [9]
RP FUNCTION.
RX PubMed=11487693; DOI=10.2307/3871319;
RA Fu X., Sudhakar D., Peng J., Richards D.E., Christou P., Harberd N.P.;
RT "Expression of Arabidopsis GAI in transgenic rice represses multiple
RT gibberellin responses.";
RL Plant Cell 13:1791-1802(2001).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=11877383; DOI=10.1101/gad.969002;
RA Lee S., Cheng H., King K.E., Wang W., He Y., Hussain A., Lo J.,
RA Harberd N.P., Peng J.;
RT "Gibberellin regulates Arabidopsis seed germination via RGL2, a GAI/RGA-
RT like gene whose expression is up-regulated following imbibition.";
RL Genes Dev. 16:646-658(2002).
RN [11]
RP SUBCELLULAR LOCATION, LACK OF DEGRADATION, AND MUTAGENESIS OF
RP 135-LYS--LYS-138 AND 219-ARG--ARG-223.
RX PubMed=12492836; DOI=10.1046/j.1365-313x.2002.01478.x;
RA Fleck B., Harberd N.P.;
RT "Evidence that the Arabidopsis nuclear gibberellin signalling protein GAI
RT is not destabilised by gibberellin.";
RL Plant J. 32:935-947(2002).
RN [12]
RP FUNCTION.
RX PubMed=14973286; DOI=10.1242/dev.00992;
RA Cheng H., Qin L., Lee S., Fu X., Richards D.E., Cao D., Luo D.,
RA Harberd N.P., Peng J.;
RT "Gibberellin regulates Arabidopsis floral development via suppression of
RT DELLA protein function.";
RL Development 131:1055-1064(2004).
RN [13]
RP INTERACTION WITH GID2.
RX PubMed=15155881; DOI=10.1105/tpc.020958;
RA Dill A., Thomas S.G., Hu J., Steber C.M., Sun T.-P.;
RT "The Arabidopsis F-box protein SLEEPY1 targets gibberellin signaling
RT repressors for gibberellin-induced degradation.";
RL Plant Cell 16:1392-1405(2004).
RN [14]
RP INTERACTION WITH GID2.
RX PubMed=15161962; DOI=10.1105/tpc.021386;
RA Fu X., Richards D.E., Fleck B., Xie D., Burton N., Harberd N.P.;
RT "The Arabidopsis mutant sleepy1gar2-1 protein promotes plant growth by
RT increasing the affinity of the SCFSLY1 E3 ubiquitin ligase for DELLA
RT protein substrates.";
RL Plant Cell 16:1406-1418(2004).
RN [15]
RP INTERACTION WITH GID2.
RX PubMed=15173565; DOI=10.1104/pp.104.039578;
RA Tyler L., Thomas S.G., Hu J., Dill A., Alonso J.M., Ecker J.R., Sun T.-P.;
RT "Della proteins and gibberellin-regulated seed germination and floral
RT development in Arabidopsis.";
RL Plant Physiol. 135:1008-1019(2004).
RN [16]
RP FUNCTION.
RX PubMed=15128937; DOI=10.1073/pnas.0402377101;
RA Yu H., Ito T., Zhao Y., Peng J., Kumar P., Meyerowitz E.M.;
RT "Floral homeotic genes are targets of gibberellin signaling in flower
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7827-7832(2004).
RN [17]
RP FUNCTION.
RX PubMed=16034591; DOI=10.1007/s00425-005-0057-3;
RA Cao D., Hussain A., Cheng H., Peng J.;
RT "Loss of function of four DELLA genes leads to light- and gibberellin-
RT independent seed germination in Arabidopsis.";
RL Planta 223:105-113(2005).
RN [18]
RP INTERACTION WITH GID1A; GID1B AND GID1C.
RX PubMed=16709201; DOI=10.1111/j.1365-313x.2006.02748.x;
RA Nakajima M., Shimada A., Takashi Y., Kim Y.C., Park S.H.,
RA Ueguchi-Tanaka M., Suzuki H., Katoh E., Iuchi S., Kobayashi M., Maeda T.,
RA Matsuoka M., Yamaguchi I.;
RT "Identification and characterization of Arabidopsis gibberellin
RT receptors.";
RL Plant J. 46:880-889(2006).
RN [19]
RP FUNCTION.
RX PubMed=17933900; DOI=10.1105/tpc.107.054999;
RA Zentella R., Zhang Z.L., Park M., Thomas S.G., Endo A., Murase K.,
RA Fleet C.M., Jikumaru Y., Nambara E., Kamiya Y., Sun T.P.;
RT "Global analysis of della direct targets in early gibberellin signaling in
RT Arabidopsis.";
RL Plant Cell 19:3037-3057(2007).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PFD3 AND PFD5.
RX PubMed=23583555; DOI=10.1016/j.cub.2013.03.053;
RA Locascio A., Blazquez M.A., Alabadi D.;
RT "Dynamic regulation of cortical microtubule organization through prefoldin-
RT DELLA interaction.";
RL Curr. Biol. 23:804-809(2013).
RN [21]
RP INTERACTION WITH BOI; BRG1; BRG2 AND BRG3, AND DISRUPTION PHENOTYPE.
RX PubMed=23482857; DOI=10.1105/tpc.112.108951;
RA Park J., Nguyen K.T., Park E., Jeon J.S., Choi G.;
RT "DELLA proteins and their interacting RING Finger proteins repress
RT gibberellin responses by binding to the promoters of a subset of
RT gibberellin-responsive genes in Arabidopsis.";
RL Plant Cell 25:927-943(2013).
RN [22]
RP INTERACTION WITH NUP58.
RX PubMed=23840761; DOI=10.1371/journal.pone.0067661;
RA Ferrandez-Ayela A., Alonso-Peral M.M., Sanchez-Garcia A.B., Micol-Ponce R.,
RA Perez-Perez J.M., Micol J.L., Ponce M.R.;
RT "Arabidopsis TRANSCURVATA1 encodes NUP58, a component of the nucleopore
RT central channel.";
RL PLoS ONE 8:E67661-E67661(2013).
RN [23]
RP FUNCTION, INDUCTION BY IMBIBITION, AND INTERACTION WITH PDF2 AND ATML1.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=24989044; DOI=10.1105/tpc.114.127647;
RA Rombola-Caldentey B., Rueda-Romero P., Iglesias-Fernandez R., Carbonero P.,
RA Onate-Sanchez L.;
RT "Arabidopsis DELLA and two HD-ZIP transcription factors regulate GA
RT signaling in the epidermis through the L1 box cis-element.";
RL Plant Cell 26:2905-2919(2014).
RN [24]
RP FUNCTION, INTERACTION WITH GAF1/IDD2 AND ENY/IDD1, SUBCELLULAR LOCATION,
RP AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=25035403; DOI=10.1105/tpc.114.125690;
RA Fukazawa J., Teramura H., Murakoshi S., Nasuno K., Nishida N., Ito T.,
RA Yoshida M., Kamiya Y., Yamaguchi S., Takahashi Y.;
RT "DELLAs function as coactivators of GAI-ASSOCIATED FACTOR1 in regulation of
RT gibberellin homeostasis and signaling in Arabidopsis.";
RL Plant Cell 26:2920-2938(2014).
RN [25]
RP INTERACTION WITH TOPP4.
RX PubMed=25010794; DOI=10.1371/journal.pgen.1004464;
RA Qin Q., Wang W., Guo X., Yue J., Huang Y., Xu X., Li J., Hou S.;
RT "Arabidopsis DELLA protein degradation is controlled by a type-one protein
RT phosphatase, TOPP4.";
RL PLoS Genet. 10:E1004464-E1004464(2014).
RN [26]
RP INTERACTION WITH TCP14 AND TCP15.
RX PubMed=25655823; DOI=10.1016/j.molp.2014.11.018;
RA Resentini F., Felipo-Benavent A., Colombo L., Blazquez M.A., Alabadi D.,
RA Masiero S.;
RT "TCP14 and TCP15 mediate the promotion of seed germination by gibberellins
RT in Arabidopsis thaliana.";
RL Mol. Plant 8:482-485(2015).
RN [27]
RP INTERACTION WITH FLZ5.
RX DOI=10.1016/j.cpb.2015.10.004;
RA Nietzsche M., Landgraf R., Tohge T., Boernke F.;
RT "A protein-protein interaction network linking the energy-sensor kinase
RT SnRK1 to multiple signaling pathways in Arabidopsis thaliana.";
RL Curr. Plant Biol. 5:36-44(2016).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 11-113 IN COMPLEX WITH GID1A AND
RP GIBBERELLIN.
RX PubMed=19037309; DOI=10.1038/nature07519;
RA Murase K., Hirano Y., Sun T.P., Hakoshima T.;
RT "Gibberellin-induced DELLA recognition by the gibberellin receptor GID1.";
RL Nature 456:459-463(2008).
CC -!- FUNCTION: Transcriptional regulator that acts as a repressor of the
CC gibberellin (GA) signaling pathway. Transcription coactivator of the
CC zinc finger transcription factors GAF1/IDD2 and ENY/IDD1 in regulation
CC of gibberellin homeostasis and signaling (PubMed:25035403). No effect
CC of the BOI proteins on its stability. Probably acts by participating in
CC large multiprotein complexes that repress transcription of GA-inducible
CC genes. Positively regulates XERICO expression. In contrast to RGA, it
CC is less sensitive to GA. Its activity is probably regulated by other
CC phytohormones such as auxin and ethylene. Involved in the regulation of
CC seed dormancy and germination, including glucose-induced delay of seed
CC germination (PubMed:24989044). Involved in the process leading to
CC microtubules (MTs) dissociation in response to gibberellic acid (GA)
CC probably by mediating the translocation of the prefoldin co-chaperone
CC complex from the cytoplasm to the nucleus (PubMed:23583555).
CC {ECO:0000269|PubMed:11487693, ECO:0000269|PubMed:11606551,
CC ECO:0000269|PubMed:11606552, ECO:0000269|PubMed:14973286,
CC ECO:0000269|PubMed:15128937, ECO:0000269|PubMed:16034591,
CC ECO:0000269|PubMed:17933900, ECO:0000269|PubMed:23583555,
CC ECO:0000269|PubMed:24989044, ECO:0000269|PubMed:25035403,
CC ECO:0000269|PubMed:9389651}.
CC -!- ACTIVITY REGULATION: Transcription activation is repressed by
CC gibberellic acid GA(3) in the presence of TPR4.
CC {ECO:0000269|PubMed:25035403}.
CC -!- SUBUNIT: Interacts directly with the GID2/SLY1 component of the
CC SCF(GID2) complex. Interacts (via N-terminus) with GID1A, GID1B and
CC GID1B (via N-terminus). Interacts with the BOI proteins BOI, BRG1,
CC BRG2, BRG3 and NUP58 (PubMed:15155881, PubMed:15161962,
CC PubMed:15173565, PubMed:16709201, PubMed:19037309, PubMed:23482857,
CC PubMed:23840761). Interacts with TOPP4 (PubMed:25010794,
CC PubMed:15155881, PubMed:15161962, PubMed:15173565, PubMed:16709201,
CC PubMed:19037309, PubMed:23482857, PubMed:23840761). Interacts with
CC TCP14 and TCP15 (PubMed:25655823). Interacts with FLZ5 (Ref.27). Binds
CC to and coactivates GAF1/IDD2 and ENY/IDD1 at the promoter of GA20OX2
CC gene (PubMed:25035403). Binds to PDF2 and ATML1 (PubMed:24989044).
CC Interacts with the prefoldin alpha subunits PFD3 and PFD5 in the
CC nucleus (PubMed:23583555). {ECO:0000269|PubMed:15155881,
CC ECO:0000269|PubMed:15161962, ECO:0000269|PubMed:15173565,
CC ECO:0000269|PubMed:16709201, ECO:0000269|PubMed:19037309,
CC ECO:0000269|PubMed:23482857, ECO:0000269|PubMed:23583555,
CC ECO:0000269|PubMed:23840761, ECO:0000269|PubMed:24989044,
CC ECO:0000269|PubMed:25010794, ECO:0000269|PubMed:25035403,
CC ECO:0000269|PubMed:25655823, ECO:0000269|Ref.27}.
CC -!- INTERACTION:
CC Q9LQT8; Q9FMT4: At5g14170; NbExp=3; IntAct=EBI-963606, EBI-3387100;
CC Q9LQT8; A0A178VU28: AXX17_At2g44430; NbExp=3; IntAct=EBI-963606, EBI-25528007;
CC Q9LQT8; Q38897: BEL1; NbExp=3; IntAct=EBI-963606, EBI-1153783;
CC Q9LQT8; Q9FXG8: BLH10; NbExp=3; IntAct=EBI-963606, EBI-1153895;
CC Q9LQT8; Q94KL5: BLH4; NbExp=3; IntAct=EBI-963606, EBI-1153797;
CC Q9LQT8; B9DGI8: BZIP63; NbExp=3; IntAct=EBI-963606, EBI-942713;
CC Q9LQT8; Q8S307: BZR1; NbExp=9; IntAct=EBI-963606, EBI-1803261;
CC Q9LQT8; Q39057: CO; NbExp=4; IntAct=EBI-963606, EBI-1639724;
CC Q9LQT8; Q9MAI5: ERF8; NbExp=3; IntAct=EBI-963606, EBI-2000137;
CC Q9LQT8; Q9MAA7: GID1A; NbExp=14; IntAct=EBI-963606, EBI-963597;
CC Q9LQT8; Q9LYC1: GID1B; NbExp=8; IntAct=EBI-963606, EBI-963686;
CC Q9LQT8; Q940G6: GID1C; NbExp=8; IntAct=EBI-963606, EBI-963794;
CC Q9LQT8; Q9STX3: GID2; NbExp=7; IntAct=EBI-963606, EBI-619033;
CC Q9LQT8; Q9SND4: HEC2; NbExp=3; IntAct=EBI-963606, EBI-1536720;
CC Q9LQT8; Q9LVW2: HSFA9; NbExp=3; IntAct=EBI-963606, EBI-15200782;
CC Q9LQT8; Q8RXD6: HUB1; NbExp=3; IntAct=EBI-963606, EBI-2012188;
CC Q9LQT8; Q93WJ9: KAN1; NbExp=3; IntAct=EBI-963606, EBI-4426504;
CC Q9LQT8; P48000: KNAT3; NbExp=3; IntAct=EBI-963606, EBI-1153908;
CC Q9LQT8; Q9FFJ9: MJJ3.20; NbExp=3; IntAct=EBI-963606, EBI-15211238;
CC Q9LQT8; Q9C5C0: MPK18; NbExp=6; IntAct=EBI-963606, EBI-1238534;
CC Q9LQT8; Q9SJG9: MPK20; NbExp=3; IntAct=EBI-963606, EBI-2358896;
CC Q9LQT8; Q9FX36: MYB54; NbExp=3; IntAct=EBI-963606, EBI-25511270;
CC Q9LQT8; Q9LUA3: NIMIN-2; NbExp=3; IntAct=EBI-963606, EBI-541107;
CC Q9LQT8; Q9LD95: SIGF; NbExp=4; IntAct=EBI-963606, EBI-4455937;
CC Q9LQT8; B9DI20: SPL13A; NbExp=3; IntAct=EBI-963606, EBI-15206662;
CC Q9LQT8; Q9FUA4: SPT; NbExp=3; IntAct=EBI-963606, EBI-1536703;
CC Q9LQT8; Q9S7W5: TCP13; NbExp=4; IntAct=EBI-963606, EBI-4424877;
CC Q9LQT8; Q93Z00: TCP14; NbExp=3; IntAct=EBI-963606, EBI-4424563;
CC Q9LQT8; Q9LEZ9: TCP17; NbExp=3; IntAct=EBI-963606, EBI-15192327;
CC Q9LQT8; Q9LMA8: TIFY10A; NbExp=5; IntAct=EBI-963606, EBI-1388539;
CC Q9LQT8; Q9LVI4: TIFY6B; NbExp=3; IntAct=EBI-963606, EBI-1792431;
CC Q9LQT8; Q8W4J8: TIFY7; NbExp=10; IntAct=EBI-963606, EBI-1792583;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12492836,
CC ECO:0000269|PubMed:23583555, ECO:0000269|PubMed:25035403}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in rosette
CC leaves, roots, stems and inflorescences of greenhouse grown.
CC {ECO:0000269|PubMed:11877383, ECO:0000269|PubMed:9237632,
CC ECO:0000269|PubMed:9490740}.
CC -!- INDUCTION: Upon seed imbibition, increased GA levels in the epidermis
CC reduce DELLA proteins (e.g. GAI/RGA2, RGA/RGA1/GRS and RGL2/SCL19)
CC abundance and release, in turn, ATML1 and PDF2 which activate LIP1
CC expression, thus enhancing germination potential.
CC {ECO:0000269|PubMed:24989044}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: Gibberellin (GA) induces dephosphorylation of GAI by TOPP4 and
CC subsequent degradation by the proteasomal pathway.
CC {ECO:0000269|PubMed:25010794}.
CC -!- PTM: May be ubiquitinated, as suggested by its interaction with GID2.
CC Ubiquitination is however unsure since in contrast to other DELLA
CC proteins, it is not ubiquitinated and degraded upon GA application.
CC Nevertheless, ubiquitination may be triggered by other processes.
CC -!- DISRUPTION PHENOTYPE: Rga, gai, rgl1, rgl2 and rgl3 pentuple mutant
CC displays constitutive GA responses even in the absence of GA treatment.
CC {ECO:0000269|PubMed:23482857}.
CC -!- SIMILARITY: Belongs to the GRAS family. DELLA subfamily. {ECO:0000305}.
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DR EMBL; Y11337; CAA72178.1; -; mRNA.
DR EMBL; Y15193; CAA75492.1; -; Genomic_DNA.
DR EMBL; AC006917; AAF79228.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29242.1; -; Genomic_DNA.
DR EMBL; AY058194; AAL25607.1; -; mRNA.
DR EMBL; AY142002; AAM98266.1; -; mRNA.
DR PIR; H86282; H86282.
DR RefSeq; NP_172945.1; NM_101361.3.
DR PDB; 2ZSH; X-ray; 1.80 A; B=11-113.
DR PDB; 2ZSI; X-ray; 1.80 A; B=11-113.
DR PDBsum; 2ZSH; -.
DR PDBsum; 2ZSI; -.
DR AlphaFoldDB; Q9LQT8; -.
DR SMR; Q9LQT8; -.
DR BioGRID; 23297; 134.
DR DIP; DIP-32985N; -.
DR IntAct; Q9LQT8; 70.
DR MINT; Q9LQT8; -.
DR STRING; 3702.AT1G14920.1; -.
DR PaxDb; Q9LQT8; -.
DR PRIDE; Q9LQT8; -.
DR ProteomicsDB; 247386; -.
DR EnsemblPlants; AT1G14920.1; AT1G14920.1; AT1G14920.
DR GeneID; 838057; -.
DR Gramene; AT1G14920.1; AT1G14920.1; AT1G14920.
DR KEGG; ath:AT1G14920; -.
DR Araport; AT1G14920; -.
DR TAIR; locus:2006747; AT1G14920.
DR eggNOG; ENOG502QPMG; Eukaryota.
DR HOGENOM; CLU_011924_4_0_1; -.
DR InParanoid; Q9LQT8; -.
DR OMA; SQWRNRF; -.
DR OrthoDB; 559310at2759; -.
DR PhylomeDB; Q9LQT8; -.
DR EvolutionaryTrace; Q9LQT8; -.
DR PRO; PR:Q9LQT8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQT8; baseline and differential.
DR Genevisible; Q9LQT8; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0010336; P:gibberellic acid homeostasis; IDA:UniProtKB.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; TAS:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IBA:GO_Central.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0033206; P:meiotic cytokinesis; IMP:TAIR.
DR GO; GO:1905614; P:negative regulation of developmental vegetative growth; IGI:CAFA.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CAFA.
DR GO; GO:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:1905622; P:negative regulation of leaf development; IGI:CAFA.
DR GO; GO:0010187; P:negative regulation of seed germination; IBA:GO_Central.
DR GO; GO:1900033; P:negative regulation of trichome patterning; IGI:CAFA.
DR GO; GO:0010233; P:phloem transport; IMP:TAIR.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:CAFA.
DR GO; GO:0009939; P:positive regulation of gibberellic acid mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:1903508; P:positive regulation of nucleic acid-templated transcription; IDA:UniProtKB.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IMP:TAIR.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IBA:GO_Central.
DR GO; GO:2000033; P:regulation of seed dormancy process; IEP:UniProtKB.
DR GO; GO:0010029; P:regulation of seed germination; IEP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IBA:GO_Central.
DR GO; GO:0009723; P:response to ethylene; IBA:GO_Central.
DR GO; GO:0010218; P:response to far red light; IEP:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IMP:CAFA.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IBA:GO_Central.
DR DisProt; DP00724; -.
DR Gene3D; 1.10.10.1290; -; 1.
DR InterPro; IPR038088; DELLA_N_sf.
DR InterPro; IPR030006; TF_DELLA.
DR InterPro; IPR021914; TF_DELLA_N.
DR InterPro; IPR005202; TF_GRAS.
DR PANTHER; PTHR31636; PTHR31636; 1.
DR PANTHER; PTHR31636:SF245; PTHR31636:SF245; 1.
DR Pfam; PF12041; DELLA; 1.
DR Pfam; PF03514; GRAS; 1.
DR PROSITE; PS50985; GRAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Developmental protein;
KW Gibberellin signaling pathway; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..533
FT /note="DELLA protein GAI"
FT /id="PRO_0000132235"
FT DOMAIN 160..529
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..221
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 240..305
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 319..351
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 363..450
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 453..529
FT /note="SAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 28..32
FT /note="DELLA motif"
FT /evidence="ECO:0000255"
FT MOTIF 50..54
FT /note="LEXLE motif"
FT /evidence="ECO:0000255"
FT MOTIF 73..77
FT /note="VHYNP motif"
FT /evidence="ECO:0000255"
FT MOTIF 174..178
FT /note="LxCxE motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 271..275
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 371..375
FT /note="LXXLL motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MUTAGEN 28..44
FT /note="Missing: In gai; causes a dwarf phenotype."
FT /evidence="ECO:0000269|PubMed:9389651"
FT MUTAGEN 135..138
FT /note="Missing: Does not affect nuclear localization."
FT /evidence="ECO:0000269|PubMed:12492836"
FT MUTAGEN 219..223
FT /note="Missing: Does not affect nuclear localization."
FT /evidence="ECO:0000269|PubMed:12492836"
FT CONFLICT 10
FT /note="Missing (in Ref. 1; CAA72178 and 2; CAA75492)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="K -> Q (in Ref. 1; CAA72178)"
FT /evidence="ECO:0000305"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:2ZSH"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:2ZSH"
SQ SEQUENCE 533 AA; 58927 MW; 6464B8C129D79528 CRC64;
MKRDHHHHHH QDKKTMMMNE EDDGNGMDEL LAVLGYKVRS SEMADVAQKL EQLEVMMSNV
QEDDLSQLAT ETVHYNPAEL YTWLDSMLTD LNPPSSNAEY DLKAIPGDAI LNQFAIDSAS
SSNQGGGGDT YTTNKRLKCS NGVVETTTAT AESTRHVVLV DSQENGVRLV HALLACAEAV
QKENLTVAEA LVKQIGFLAV SQIGAMRKVA TYFAEALARR IYRLSPSQSP IDHSLSDTLQ
MHFYETCPYL KFAHFTANQA ILEAFQGKKR VHVIDFSMSQ GLQWPALMQA LALRPGGPPV
FRLTGIGPPA PDNFDYLHEV GCKLAHLAEA IHVEFEYRGF VANTLADLDA SMLELRPSEI
ESVAVNSVFE LHKLLGRPGA IDKVLGVVNQ IKPEIFTVVE QESNHNSPIF LDRFTESLHY
YSTLFDSLEG VPSGQDKVMS EVYLGKQICN VVACDGPDRV ERHETLSQWR NRFGSAGFAA
AHIGSNAFKQ ASMLLALFNG GEGYRVEESD GCLMLGWHTR PLIATSAWKL STN
