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DELLA protein RGL2 (GRAS family protein 15) (AtGRAS-15) (RGA-like protein 2) (Scarecrow-like protein 19) (AtSCL19)

 RGL2_ARATH              Reviewed;         547 AA.
Q8GXW1; Q9SRP9;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
22-NOV-2005, sequence version 2.
22-NOV-2017, entry version 107.
RecName: Full=DELLA protein RGL2;
AltName: Full=GRAS family protein 15;
Short=AtGRAS-15;
AltName: Full=RGA-like protein 2;
AltName: Full=Scarecrow-like protein 19;
Short=AtSCL19;
Name=RGL2; Synonyms=SCL19; OrderedLocusNames=At3g03450;
ORFNames=T21P5.13;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[4]
IDENTIFICATION.
PubMed=10341448; DOI=10.1046/j.1365-313X.1999.00431.x;
Pysh L.D., Wysocka-Diller J.W., Camilleri C., Bouchez D., Benfey P.N.;
"The GRAS gene family in Arabidopsis: sequence characterization and
basic expression analysis of the SCARECROW-LIKE genes.";
Plant J. 18:111-119(1999).
[5]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11877383; DOI=10.1101/gad.969002;
Lee S., Cheng H., King K.E., Wang W., He Y., Hussain A., Lo J.,
Harberd N.P., Peng J.;
"Gibberellin regulates Arabidopsis seed germination via RGL2, a
GAI/RGA-like gene whose expression is up-regulated following
imbibition.";
Genes Dev. 16:646-658(2002).
[6]
FUNCTION.
PubMed=12610625; DOI=10.1038/nature01387;
Fu X., Harberd N.P.;
"Auxin promotes Arabidopsis root growth by modulating gibberellin
response.";
Nature 421:740-743(2003).
[7]
FUNCTION.
PubMed=14615596; DOI=10.1105/tpc.015685;
Achard P., Vriezen W.H., Van Der Straeten D., Harberd N.P.;
"Ethylene regulates Arabidopsis development via the modulation of
DELLA protein growth repressor function.";
Plant Cell 15:2816-2825(2003).
[8]
FUNCTION.
PubMed=14973286; DOI=10.1242/dev.00992;
Cheng H., Qin L., Lee S., Fu X., Richards D.E., Cao D., Luo D.,
Harberd N.P., Peng J.;
"Gibberellin regulates Arabidopsis floral development via suppression
of DELLA protein function.";
Development 131:1055-1064(2004).
[9]
PROBABLE UBIQUITINATION, DEGRADATION, AND INTERACTION WITH GID2.
PubMed=15173565; DOI=10.1104/pp.104.039578;
Tyler L., Thomas S.G., Hu J., Dill A., Alonso J.M., Ecker J.R.,
Sun T.-P.;
"Della proteins and gibberellin-regulated seed germination and floral
development in Arabidopsis.";
Plant Physiol. 135:1008-1019(2004).
[10]
FUNCTION.
PubMed=15128937; DOI=10.1073/pnas.0402377101;
Yu H., Ito T., Zhao Y., Peng J., Kumar P., Meyerowitz E.M.;
"Floral homeotic genes are targets of gibberellin signaling in flower
development.";
Proc. Natl. Acad. Sci. U.S.A. 101:7827-7832(2004).
[11]
FUNCTION.
PubMed=16034591; DOI=10.1007/s00425-005-0057-3;
Cao D., Hussain A., Cheng H., Peng J.;
"Loss of function of four DELLA genes leads to light- and gibberellin-
independent seed germination in Arabidopsis.";
Planta 223:105-113(2005).
[12]
PROBABLE UBIQUITINATION, DEGRADATION, PHOSPHORYLATION, AND MUTAGENESIS
OF 48-ASP--ALA-52; TYR-52; SER-57; SER-86; SER-103; SER-212; THR-271;
THR-319; SER-381; THR-411; SER-436; SER-437; SER-441; SER-456;
THR-481; SER-501; SER-508; THR-535 AND SER-542.
PubMed=16167898; DOI=10.1111/j.1365-313X.2005.02512.x;
Hussain A., Cao D., Cheng H., Wen Z., Peng J.;
"Identification of the conserved serine/threonine residues important
for gibberellin-sensitivity of Arabidopsis RGL2 protein.";
Plant J. 44:88-99(2005).
[13]
FUNCTION.
PubMed=17141619; DOI=10.1016/j.cub.2006.10.057;
Penfield S., Gilday A.D., Halliday K.J., Graham I.A.;
"DELLA-mediated cotyledon expansion breaks coat-imposed seed
dormancy.";
Curr. Biol. 16:2366-2370(2006).
[14]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY GLUCOSE.
PubMed=16916886; DOI=10.1093/jxb/erl096;
Yuan K., Wysocka-Diller J.;
"Phytohormone signalling pathways interact with sugars during seed
germination and seedling development.";
J. Exp. Bot. 57:3359-3367(2006).
[15]
INTERACTION WITH GID1A; GID1B AND GID1C.
PubMed=16709201; DOI=10.1111/j.1365-313X.2006.02748.x;
Nakajima M., Shimada A., Takashi Y., Kim Y.C., Park S.H.,
Ueguchi-Tanaka M., Suzuki H., Katoh E., Iuchi S., Kobayashi M.,
Maeda T., Matsuoka M., Yamaguchi I.;
"Identification and characterization of Arabidopsis gibberellin
receptors.";
Plant J. 46:880-889(2006).
[16]
FUNCTION.
PubMed=16400150; DOI=10.1126/science.1118642;
Achard P., Cheng H., De Grauwe L., Decat J., Schoutteten H.,
Moritz T., Van Der Straeten D., Peng J., Harberd N.P.;
"Integration of plant responses to environmentally activated
phytohormonal signals.";
Science 311:91-94(2006).
[17]
FUNCTION, AND INDUCTION.
PubMed=17384169; DOI=10.1105/tpc.106.048009;
Ariizumi T., Steber C.M.;
"Seed germination of GA-insensitive sleepy1 mutants does not require
RGL2 protein disappearance in Arabidopsis.";
Plant Cell 19:791-804(2007).
[18]
FUNCTION.
PubMed=17704233; DOI=10.1104/pp.107.104794;
Gan Y., Yu H., Peng J., Broun P.;
"Genetic and molecular regulation by DELLA proteins of trichome
development in Arabidopsis.";
Plant Physiol. 145:1031-1042(2007).
[19]
PHOSPHORYLATION OF TYR RESIDUES, AND MUTAGENESIS OF TYR-52; TYR-89;
TYR-223; TYR-259 AND TYR-435.
PubMed=17333251; DOI=10.1007/s00425-007-0497-z;
Hussain A., Cao D., Peng J.;
"Identification of conserved tyrosine residues important for
gibberellin sensitivity of Arabidopsis RGL2 protein.";
Planta 226:475-483(2007).
[20]
FUNCTION.
STRAIN=cv. Landsberg erecta;
PubMed=18450451; DOI=10.1016/j.cub.2008.03.060;
Navarro L., Bari R., Achard P., Lison P., Nemri A., Harberd N.P.,
Jones J.D.G.;
"DELLAs control plant immune responses by modulating the balance of
jasmonic acid and salicylic acid signaling.";
Curr. Biol. 18:650-655(2008).
[21]
FUNCTION, AND INDUCTION BY SALT AND MANNITOL TREATMENT.
PubMed=18450450; DOI=10.1016/j.cub.2008.04.034;
Achard P., Renou J.-P., Berthome R., Harberd N.P., Genschik P.;
"Plant DELLAs restrain growth and promote survival of adversity by
reducing the levels of reactive oxygen species.";
Curr. Biol. 18:656-660(2008).
[22]
FUNCTION, INDUCTION BY ABA, AND TISSUE SPECIFICITY.
PubMed=18941053; DOI=10.1105/tpc.108.061515;
Piskurewicz U., Jikumaru Y., Kinoshita N., Nambara E., Kamiya Y.,
Lopez-Molina L.;
"The gibberellic acid signaling repressor RGL2 inhibits Arabidopsis
seed germination by stimulating abscisic acid synthesis and ABI5
activity.";
Plant Cell 20:2729-2745(2008).
[23]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY IMBIBITION.
PubMed=18162586; DOI=10.1104/pp.107.113738;
Toh S., Imamura A., Watanabe A., Nakabayashi K., Okamoto M.,
Jikumaru Y., Hanada A., Aso Y., Ishiyama K., Tamura N., Iuchi S.,
Kobayashi M., Yamaguchi S., Kamiya Y., Nambara E., Kawakami N.;
"High temperature-induced abscisic acid biosynthesis and its role in
the inhibition of gibberellin action in Arabidopsis seeds.";
Plant Physiol. 146:1368-1385(2008).
[24]
DEGRADATION BY PROTEASOME.
PubMed=19717618; DOI=10.1105/tpc.108.065433;
Wang F., Zhu D., Huang X., Li S., Gong Y., Yao Q., Fu X., Fan L.-M.,
Deng X.W.;
"Biochemical insights on degradation of Arabidopsis DELLA proteins
gained from a cell-free assay system.";
Plant Cell 21:2378-2390(2009).
[25]
TISSUE SPECIFICITY, AND INTERACTION WITH GID1A; GID1B AND GID1C.
PubMed=19500306; DOI=10.1111/j.1365-313X.2009.03936.x;
Suzuki H., Park S.-H., Okubo K., Kitamura J., Ueguchi-Tanaka M.,
Iuchi S., Katoh E., Kobayashi M., Yamaguchi I., Matsuoka M., Asami T.,
Nakajima M.;
"Differential expression and affinities of Arabidopsis gibberellin
receptors can explain variation in phenotypes of multiple knock-out
mutants.";
Plant J. 60:48-55(2009).
[26]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION
WITH PIF1; PIF4; PIF6 AND SPT.
STRAIN=cv. Landsberg erecta;
PubMed=20093430; DOI=10.1093/molbev/msq012;
Gallego-Bartolome J., Minguet E.G., Marin J.A., Prat S.,
Blazquez M.A., Alabadi D.;
"Transcriptional diversification and functional conservation between
DELLA proteins in Arabidopsis.";
Mol. Biol. Evol. 27:1247-1256(2010).
[27]
FUNCTION, INDUCTION DURING IMBIBITION, AND TISSUE SPECIFICITY.
PubMed=20956298; DOI=10.1073/pnas.1012896107;
Lee K.P., Piskurewicz U., Tureckova V., Strnad M., Lopez-Molina L.;
"A seed coat bedding assay shows that RGL2-dependent release of
abscisic acid by the endosperm controls embryo growth in Arabidopsis
dormant seeds.";
Proc. Natl. Acad. Sci. U.S.A. 107:19108-19113(2010).
[28]
INTERACTION WITH BOI; BRG1; BRG2 AND BRG3, AND DISRUPTION PHENOTYPE.
PubMed=23482857; DOI=10.1105/tpc.112.108951;
Park J., Nguyen K.T., Park E., Jeon J.S., Choi G.;
"DELLA proteins and their interacting RING Finger proteins repress
gibberellin responses by binding to the promoters of a subset of
gibberellin-responsive genes in Arabidopsis.";
Plant Cell 25:927-943(2013).
-!- FUNCTION: Probable transcriptional regulator that acts as a
repressor of the gibberellin (GA) signaling pathway. No effect of
the BOI proteins on its stability. Probably acts by participating
in large multiprotein complexes that repress transcription of GA-
inducible genes. Upon GA application, it is degraded by the
proteasome, allowing the GA signaling pathway. Acts as a major GA-
response repressor of seed germination, including seed
thermoinhibition. Promotes the biosynthesis of abscisic acid
(ABA), especially in seed coats to maintain seed dormancy. Delays
flowering and adult leaf production. Also regulates the floral
development, petal, stamen and anther development, by repressing
the continued growth of floral organs. Its activity is probably
regulated by other phytohormones such as auxin and ethylene.
Involved in the regulation of seed dormancy and germination,
including glucose-induced delay of seed germination. Promotes salt
tolerance. Acts as a repressor of positive regulators of trichome
initiation. Required during the flagellin-derived peptide flg22-
mediated growth inhibition. Contributes to the susceptibility to
the biotrophic pathogen P.syringae pv. tomato and to the
resistance to the necrotrophic pathogens B.cinerea A.brassicicola,
probably by repressing the SA-defense pathway and preventing cell
death. Prevents stress-induced reactive oxygen species (ROS)
accumulation (e.g. salt stress) by acting on the ROS scavenging
system, and delays ROS-induced cell death, thus promoting stress
tolerance. {ECO:0000269|PubMed:11877383,
ECO:0000269|PubMed:12610625, ECO:0000269|PubMed:14615596,
ECO:0000269|PubMed:14973286, ECO:0000269|PubMed:15128937,
ECO:0000269|PubMed:16034591, ECO:0000269|PubMed:16400150,
ECO:0000269|PubMed:16916886, ECO:0000269|PubMed:17141619,
ECO:0000269|PubMed:17384169, ECO:0000269|PubMed:17704233,
ECO:0000269|PubMed:18162586, ECO:0000269|PubMed:18450450,
ECO:0000269|PubMed:18450451, ECO:0000269|PubMed:18941053,
ECO:0000269|PubMed:20093430, ECO:0000269|PubMed:20956298}.
-!- SUBUNIT: Interacts directly with the GID2/SLY1 component of the
SCF(GID2) complex. Interacts (via N-terminus) with GID1A, GID1B
and GID1C (via N-terminus). Binds to bHLH transcription factors
such as PIF1, PIF4, PIF6 and SPT. Interacts with the BOI proteins
BOI, BRG1, BRG2 and BRG3. {ECO:0000269|PubMed:15173565,
ECO:0000269|PubMed:16709201, ECO:0000269|PubMed:19500306,
ECO:0000269|PubMed:20093430, ECO:0000269|PubMed:23482857}.
-!- INTERACTION:
Q9MAA7:GID1A; NbExp=5; IntAct=EBI-963665, EBI-963597;
Q940G6:GID1C; NbExp=3; IntAct=EBI-963665, EBI-963794;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20093430}.
-!- TISSUE SPECIFICITY: Predominantly expressed in germinating seeds,
flowers and siliques. Only detectable in the inflorescence, with
high levels in young flower buds and significant levels in
siliques. In imbibed seeds, it is restricted to seed coats,
elongating regions of pre-emergent and recently emerged radicles,
endosperm (especially micropylar endosperm), and embryonic axis.
Not expressed in leaves, bolting stems or roots.
{ECO:0000269|PubMed:11877383, ECO:0000269|PubMed:18941053,
ECO:0000269|PubMed:19500306, ECO:0000269|PubMed:20093430,
ECO:0000269|PubMed:20956298}.
-!- INDUCTION: Up-regulated transiently following seed imbibition to
decline rapidly as germination proceeds; this induction is delayed
at supraoptimal temperature conditions (e.g. 34 degrees Celsius).
Accumulates in seed coats of dormant seeds where germination does
not occur after imbibition. Increased levels upon abscisic acid
(ABA) treatment. Down-regulated by norflurazon (NF), an ABA
biosynthesis inhibitor. Induced by stress such as glucose, salt or
mannitol treatment. {ECO:0000269|PubMed:11877383,
ECO:0000269|PubMed:16916886, ECO:0000269|PubMed:17384169,
ECO:0000269|PubMed:18162586, ECO:0000269|PubMed:18450450,
ECO:0000269|PubMed:18941053, ECO:0000269|PubMed:20956298}.
-!- DOMAIN: The DELLA motif is required for its GA-induced degradation
but not for the interaction with GID2.
-!- PTM: Phosphorylated. Phosphorylation on Tyr residues is required
for proteasome-mediated degradation in response to gibberellic
acid (GA). Dephosphorylation may be prerequisite for its
degradation by the proteasome. {ECO:0000269|PubMed:16167898,
ECO:0000269|PubMed:17333251}.
-!- PTM: Ubiquitinated (Probable). Upon GA application or seed
imbibation, it is ubiquitinated by the SCF(GID2) complex, leading
to its subsequent degradation. {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Higher germination rate in the presence of
glucose and at supraoptimal temperature conditions. Rga, gai,
rgl1, rgl2 and rgl3 pentuple mutant displays constitutive GA
responses even in the absence of GA treatment.
{ECO:0000269|PubMed:16916886, ECO:0000269|PubMed:18162586,
ECO:0000269|PubMed:23482857}.
-!- SIMILARITY: Belongs to the GRAS family. DELLA subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Kiss of life - Issue
137 of April 2012;
URL="https://web.expasy.org/spotlight/back_issues/137";
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EMBL; AC009895; AAF01590.1; -; Genomic_DNA.
EMBL; CP002686; AEE73945.1; -; Genomic_DNA.
EMBL; AK118009; BAC42642.1; -; mRNA.
RefSeq; NP_186995.1; NM_111216.3.
UniGene; At.18489; -.
UniGene; At.67027; -.
ProteinModelPortal; Q8GXW1; -.
SMR; Q8GXW1; -.
BioGrid; 6584; 18.
DIP; DIP-37661N; -.
IntAct; Q8GXW1; 5.
MINT; MINT-8069272; -.
STRING; 3702.AT3G03450.1; -.
PaxDb; Q8GXW1; -.
EnsemblPlants; AT3G03450.1; AT3G03450.1; AT3G03450.
GeneID; 821251; -.
Gramene; AT3G03450.1; AT3G03450.1; AT3G03450.
KEGG; ath:AT3G03450; -.
Araport; AT3G03450; -.
TAIR; locus:2099624; AT3G03450.
eggNOG; ENOG410IQYH; Eukaryota.
eggNOG; ENOG410YBFY; LUCA.
HOGENOM; HOG000238577; -.
InParanoid; Q8GXW1; -.
KO; K14494; -.
OMA; WRIRMKS; -.
OrthoDB; EOG0936075R; -.
PhylomeDB; Q8GXW1; -.
PRO; PR:Q8GXW1; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q8GXW1; baseline and differential.
Genevisible; Q8GXW1; AT.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:TAIR.
GO; GO:0000989; F:transcription factor activity, transcription factor binding; IEA:InterPro.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
GO; GO:0009740; P:gibberellic acid mediated signaling pathway; TAS:TAIR.
GO; GO:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; TAS:TAIR.
GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR.
GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR030006; TF_DELLA.
InterPro; IPR021914; TF_DELLA_N.
InterPro; IPR005202; TF_GRAS.
PANTHER; PTHR31636:SF47; PTHR31636:SF47; 1.
Pfam; PF12041; DELLA; 1.
Pfam; PF03514; GRAS; 1.
PROSITE; PS50985; GRAS; 1.
1: Evidence at protein level;
Complete proteome; Developmental protein; Differentiation; Flowering;
Gibberellin signaling pathway; Nucleus; Phosphoprotein; Plant defense;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 547 DELLA protein RGL2.
/FTId=PRO_0000132237.
MOTIF 44 48 DELLA motif.
MOTIF 66 70 LEXLE motif.
MOTIF 87 91 VHYNP motif.
MOTIF 286 290 VHIID.
MOTIF 385 389 LXXLL motif.
MUTAGEN 44 48 Missing: Induces a resistance to GA-
mediated degradation.
MUTAGEN 52 52 Y->A,E: Induces a resistance to GA-
mediated degradation.
{ECO:0000269|PubMed:16167898,
ECO:0000269|PubMed:17333251}.
MUTAGEN 52 52 Y->F: Normal GA-mediated degradation.
{ECO:0000269|PubMed:16167898,
ECO:0000269|PubMed:17333251}.
MUTAGEN 57 57 S->D: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 86 86 S->D: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 89 89 Y->A,E: Induces a resistance to GA-
mediated degradation.
{ECO:0000269|PubMed:17333251}.
MUTAGEN 89 89 Y->F: Normal GA-mediated degradation.
{ECO:0000269|PubMed:17333251}.
MUTAGEN 103 103 S->D: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 212 212 S->D: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 223 223 Y->A,E: Induces a resistance to GA-
mediated degradation.
{ECO:0000269|PubMed:17333251}.
MUTAGEN 223 223 Y->F: Normal GA-mediated degradation.
{ECO:0000269|PubMed:17333251}.
MUTAGEN 259 259 Y->A: Induces a partial resistance to GA-
mediated degradation.
{ECO:0000269|PubMed:17333251}.
MUTAGEN 271 271 T->C: Induces a decrease to GA-mediated
degradation.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 271 271 T->E: Null mutant; induces a resistance
to GA-mediated degradation.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 319 319 T->C: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 319 319 T->E: Induces a resistance to GA-mediated
degradation.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 381 381 S->D: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 411 411 T->C: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 411 411 T->E: Induces a resistance to GA-mediated
degradation.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 435 435 Y->A,E: Induces a resistance to GA-
mediated degradation.
{ECO:0000269|PubMed:17333251}.
MUTAGEN 435 435 Y->F: Induces a resistance to GA-mediated
degradation.
{ECO:0000269|PubMed:17333251}.
MUTAGEN 436 436 S->D: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 437 437 S->D: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 441 441 S->C: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 441 441 S->D: Induces a resistance to GA-mediated
degradation.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 456 456 S->D: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 481 481 T->E: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 501 501 S->D: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 508 508 S->D: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 535 535 T->C: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 535 535 T->E: Induces a resistance to GA-mediated
degradation.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 542 542 S->C: No effect.
{ECO:0000269|PubMed:16167898}.
MUTAGEN 542 542 S->D: Induces a resistance to GA-mediated
degradation.
{ECO:0000269|PubMed:16167898}.
CONFLICT 210 210 A -> T (in Ref. 3; BAC42642).
{ECO:0000305}.
SEQUENCE 547 AA; 60494 MW; C4D18D5951D95634 CRC64;
MKRGYGETWD PPPKPLPASR SGEGPSMADK KKADDDNNNS NMDDELLAVL GYKVRSSEMA
EVAQKLEQLE MVLSNDDVGS TVLNDSVHYN PSDLSNWVES MLSELNNPAS SDLDTTRSCV
DRSEYDLRAI PGLSAFPKEE EVFDEEASSK RIRLGSWCES SDESTRSVVL VDSQETGVRL
VHALVACAEA IHQENLNLAD ALVKRVGTLA GSQAGAMGKV ATYFAQALAR RIYRDYTAET
DVCAAVNPSF EEVLEMHFYE SCPYLKFAHF TANQAILEAV TTARRVHVID LGLNQGMQWP
ALMQALALRP GGPPSFRLTG IGPPQTENSD SLQQLGWKLA QFAQNMGVEF EFKGLAAESL
SDLEPEMFET RPESETLVVN SVFELHRLLA RSGSIEKLLN TVKAIKPSIV TVVEQEANHN
GIVFLDRFNE ALHYYSSLFD SLEDSYSLPS QDRVMSEVYL GRQILNVVAA EGSDRVERHE
TAAQWRIRMK SAGFDPIHLG SSAFKQASML LSLYATGDGY RVEENDGCLM IGWQTRPLIT
TSAWKLA


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