Q8GXW1 (RGL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DELLA protein RGL2

Alternative name(s):
GRAS family protein 15
Short name=AtGRAS-15
RGA-like protein 2
Scarecrow-like protein 19
Short name=AtSCL19

Gene names

Name:	RGL2
Synonyms:	SCL19
Ordered Locus Names:	At3g03450
ORF Names:	T21P5.13

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	547 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. 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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.26 Ref.27
Subunit structure	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. Ref.9 Ref.15 Ref.25 Ref.26
Subcellular location	Nucleus Ref.26.
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. Ref.5 Ref.22 Ref.25 Ref.26 Ref.27
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. Ref.5 Ref.14 Ref.17 Ref.21 Ref.22 Ref.23 Ref.27
Domain	The DELLA motif is required for its GA-induced degradation but not for the interaction with GID2.
Post-translational modification	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. Ref.12 Ref.19 Ubiquitinated Probable. Upon GA application or seed imbibation, it is ubiquitinated by the SCF(GID2) complex, leading to its subsequent degradation. Ref.9 Ref.12 Ref.24
Disruption phenotype	Higher germination rate in the presence of glucose and at supraoptimal temperature conditions. Ref.14 Ref.23
Sequence similarities	Belongs to the GRAS family. DELLA subfamily.

Ontologies

Keywords
Biological process	Differentiation Flowering Gibberellin signaling pathway Plant defense Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Developmental protein Repressor
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW defense response Inferred from electronic annotation. Source: UniProtKB-KW flower development Inferred from electronic annotation. Source: UniProtKB-KW gibberellic acid mediated signaling pathway Traceable author statement Ref.5. Source: TAIR hyperosmotic salinity response Inferred from genetic interaction Ref.16. Source: TAIR jasmonic acid mediated signaling pathway Inferred from genetic interaction Ref.20. Source: TAIR negative regulation of gibberellic acid mediated signaling pathway Traceable author statement Ref.12. Source: TAIR negative regulation of seed germination Inferred from mutant phenotype Ref.5. Source: TAIR regulation of gene expression, epigenetic Inferred from electronic annotation. Source: EnsemblPlants/Gramene regulation of reactive oxygen species metabolic process Inferred from genetic interaction Ref.21. Source: TAIR regulation of seed dormancy process Inferred from genetic interaction Ref.13. Source: TAIR response to abscisic acid stimulus Inferred from genetic interaction Ref.16. Source: TAIR response to ethylene stimulus Inferred from genetic interaction Ref.16. Source: TAIR salicylic acid mediated signaling pathway Inferred from genetic interaction Ref.20. Source: TAIR transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay Ref.12. Source: TAIR
Molecular_function	sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity PubMed 11118137Ref.5. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GID1A	Q9MAA7	3	EBI-963665,EBI-963597
GID1C	Q940G6	3	EBI-963665,EBI-963794

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 547	547	DELLA protein RGL2		PRO_0000132237
Regions
	Motif	44 – 48	5	DELLA motif
	Motif	66 – 70	5	LEXLE motif
	Motif	87 – 91	5	VHYNP motif
	Motif	286 – 290	5	VHIID
	Motif	385 – 389	5	LXXLL motif
Experimental info
	Mutagenesis	44 – 48	5	Missing: Induces a resistance to GA-mediated degradation.
	Mutagenesis	52	1	Y → A or E: Induces a resistance to GA-mediated degradation. Ref.12 Ref.19
	Mutagenesis	52	1	Y → F: Normal GA-mediated degradation. Ref.12 Ref.19
	Mutagenesis	57	1	S → D: No effect. Ref.12
	Mutagenesis	86	1	S → D: No effect. Ref.12
	Mutagenesis	89	1	Y → A or E: Induces a resistance to GA-mediated degradation. Ref.19
	Mutagenesis	89	1	Y → F: Normal GA-mediated degradation. Ref.19
	Mutagenesis	103	1	S → D: No effect. Ref.12
	Mutagenesis	212	1	S → D: No effect. Ref.12
	Mutagenesis	223	1	Y → A or E: Induces a resistance to GA-mediated degradation. Ref.19
	Mutagenesis	223	1	Y → F: Normal GA-mediated degradation. Ref.19
	Mutagenesis	259	1	Y → A: Induces a partial resistance to GA-mediated degradation. Ref.19
	Mutagenesis	271	1	T → C: Induces a decrease to GA-mediated degradation. Ref.12
	Mutagenesis	271	1	T → E: Null mutant; induces a resistance to GA-mediated degradation. Ref.12
	Mutagenesis	319	1	T → C: No effect. Ref.12
	Mutagenesis	319	1	T → E: Induces a resistance to GA-mediated degradation. Ref.12
	Mutagenesis	381	1	S → D: No effect. Ref.12
	Mutagenesis	411	1	T → C: No effect. Ref.12
	Mutagenesis	411	1	T → E: Induces a resistance to GA-mediated degradation. Ref.12
	Mutagenesis	435	1	Y → A or E: Induces a resistance to GA-mediated degradation. Ref.19
	Mutagenesis	435	1	Y → F: Induces a resistance to GA-mediated degradation. Ref.19
	Mutagenesis	436	1	S → D: No effect. Ref.12
	Mutagenesis	437	1	S → D: No effect. Ref.12
	Mutagenesis	441	1	S → C: No effect. Ref.12
	Mutagenesis	441	1	S → D: Induces a resistance to GA-mediated degradation. Ref.12
	Mutagenesis	456	1	S → D: No effect. Ref.12
	Mutagenesis	481	1	T → E: No effect. Ref.12
	Mutagenesis	501	1	S → D: No effect. Ref.12
	Mutagenesis	508	1	S → D: No effect. Ref.12
	Mutagenesis	535	1	T → C: No effect. Ref.12
	Mutagenesis	535	1	T → E: Induces a resistance to GA-mediated degradation. Ref.12
	Mutagenesis	542	1	S → C: No effect. Ref.12
	Mutagenesis	542	1	S → D: Induces a resistance to GA-mediated degradation. Ref.12
	Sequence conflict	210	1	A → T in BAC42642. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8GXW1 [UniParc]. Last modified November 22, 2005. Version 2. Checksum: C4D18D5951D95634	FASTA	547	60,494
	10 20 30 40 50 60 MKRGYGETWD PPPKPLPASR SGEGPSMADK KKADDDNNNS NMDDELLAVL GYKVRSSEMA 70 80 90 100 110 120 EVAQKLEQLE MVLSNDDVGS TVLNDSVHYN PSDLSNWVES MLSELNNPAS SDLDTTRSCV 130 140 150 160 170 180 DRSEYDLRAI PGLSAFPKEE EVFDEEASSK RIRLGSWCES SDESTRSVVL VDSQETGVRL 190 200 210 220 230 240 VHALVACAEA IHQENLNLAD ALVKRVGTLA GSQAGAMGKV ATYFAQALAR RIYRDYTAET 250 260 270 280 290 300 DVCAAVNPSF EEVLEMHFYE SCPYLKFAHF TANQAILEAV TTARRVHVID LGLNQGMQWP 310 320 330 340 350 360 ALMQALALRP GGPPSFRLTG IGPPQTENSD SLQQLGWKLA QFAQNMGVEF EFKGLAAESL 370 380 390 400 410 420 SDLEPEMFET RPESETLVVN SVFELHRLLA RSGSIEKLLN TVKAIKPSIV TVVEQEANHN 430 440 450 460 470 480 GIVFLDRFNE ALHYYSSLFD SLEDSYSLPS QDRVMSEVYL GRQILNVVAA EGSDRVERHE 490 500 510 520 530 540 TAAQWRIRMK SAGFDPIHLG SSAFKQASML LSLYATGDGY RVEENDGCLM IGWQTRPLIT TSAWKLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." 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. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Functional annotation of a full-length Arabidopsis cDNA collection." 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. Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"The GRAS gene family in Arabidopsis: sequence characterization and basic expression analysis of the SCARECROW-LIKE genes." Pysh L.D., Wysocka-Diller J.W., Camilleri C., Bouchez D., Benfey P.N. Plant J. 18:111-119(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[5]	"Gibberellin regulates Arabidopsis seed germination via RGL2, a GAI/RGA-like gene whose expression is up-regulated following imbibition." Lee S., Cheng H., King K.E., Wang W., He Y., Hussain A., Lo J., Harberd N.P., Peng J. Genes Dev. 16:646-658(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[6]	"Auxin promotes Arabidopsis root growth by modulating gibberellin response." Fu X., Harberd N.P. Nature 421:740-743(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Ethylene regulates Arabidopsis development via the modulation of DELLA protein growth repressor function." Achard P., Vriezen W.H., Van Der Straeten D., Harberd N.P. Plant Cell 15:2816-2825(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Gibberellin regulates Arabidopsis floral development via suppression of DELLA protein function." Cheng H., Qin L., Lee S., Fu X., Richards D.E., Cao D., Luo D., Harberd N.P., Peng J. Development 131:1055-1064(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Della proteins and gibberellin-regulated seed germination and floral development in Arabidopsis." Tyler L., Thomas S.G., Hu J., Dill A., Alonso J.M., Ecker J.R., Sun T.-P. Plant Physiol. 135:1008-1019(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROBABLE UBIQUITINATION, DEGRADATION, INTERACTION WITH GID2.
[10]	"Floral homeotic genes are targets of gibberellin signaling in flower development." Yu H., Ito T., Zhao Y., Peng J., Kumar P., Meyerowitz E.M. Proc. Natl. Acad. Sci. U.S.A. 101:7827-7832(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Loss of function of four DELLA genes leads to light- and gibberellin-independent seed germination in Arabidopsis." Cao D., Hussain A., Cheng H., Peng J. Planta 223:105-113(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Identification of the conserved serine/threonine residues important for gibberellin-sensitivity of Arabidopsis RGL2 protein." Hussain A., Cao D., Cheng H., Wen Z., Peng J. Plant J. 44:88-99(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROBABLE UBIQUITINATION, DEGRADATION, PHOSPHORYLATION, 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.
[13]	"DELLA-mediated cotyledon expansion breaks coat-imposed seed dormancy." Penfield S., Gilday A.D., Halliday K.J., Graham I.A. Curr. Biol. 16:2366-2370(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Phytohormone signalling pathways interact with sugars during seed germination and seedling development." Yuan K., Wysocka-Diller J. J. Exp. Bot. 57:3359-3367(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY GLUCOSE.
[15]	"Identification and characterization of Arabidopsis gibberellin receptors." 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. Plant J. 46:880-889(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GID1A; GID1B AND GID1C.
[16]	"Integration of plant responses to environmentally activated phytohormonal signals." Achard P., Cheng H., De Grauwe L., Decat J., Schoutteten H., Moritz T., Van Der Straeten D., Peng J., Harberd N.P. Science 311:91-94(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Seed germination of GA-insensitive sleepy1 mutants does not require RGL2 protein disappearance in Arabidopsis." Ariizumi T., Steber C.M. Plant Cell 19:791-804(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[18]	"Genetic and molecular regulation by DELLA proteins of trichome development in Arabidopsis." Gan Y., Yu H., Peng J., Broun P. Plant Physiol. 145:1031-1042(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Identification of conserved tyrosine residues important for gibberellin sensitivity of Arabidopsis RGL2 protein." Hussain A., Cao D., Peng J. Planta 226:475-483(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION OF TYR RESIDUES, MUTAGENESIS OF TYR-52; TYR-89; TYR-223; TYR-259 AND TYR-435.
[20]	"DELLAs control plant immune responses by modulating the balance of jasmonic acid and salicylic acid signaling." Navarro L., Bari R., Achard P., Lison P., Nemri A., Harberd N.P., Jones J.D.G. Curr. Biol. 18:650-655(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: cv. Landsberg erecta.
[21]	"Plant DELLAs restrain growth and promote survival of adversity by reducing the levels of reactive oxygen species." Achard P., Renou J.-P., Berthome R., Harberd N.P., Genschik P. Curr. Biol. 18:656-660(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION BY SALT AND MANNITOL TREATMENT.
[22]	"The gibberellic acid signaling repressor RGL2 inhibits Arabidopsis seed germination by stimulating abscisic acid synthesis and ABI5 activity." Piskurewicz U., Jikumaru Y., Kinoshita N., Nambara E., Kamiya Y., Lopez-Molina L. Plant Cell 20:2729-2745(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION BY ABA, TISSUE SPECIFICITY.
[23]	"High temperature-induced abscisic acid biosynthesis and its role in the inhibition of gibberellin action in Arabidopsis seeds." 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. Plant Physiol. 146:1368-1385(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY IMBIBITION.
[24]	"Biochemical insights on degradation of Arabidopsis DELLA proteins gained from a cell-free assay system." Wang F., Zhu D., Huang X., Li S., Gong Y., Yao Q., Fu X., Fan L.-M., Deng X.W. Plant Cell 21:2378-2390(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DEGRADATION BY PROTEASOME.
[25]	"Differential expression and affinities of Arabidopsis gibberellin receptors can explain variation in phenotypes of multiple knock-out mutants." 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. Plant J. 60:48-55(2009) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INTERACTION WITH GID1A; GID1B AND GID1C.
[26]	"Transcriptional diversification and functional conservation between DELLA proteins in Arabidopsis." Gallego-Bartolome J., Minguet E.G., Marin J.A., Prat S., Blazquez M.A., Alabadi D. Mol. Biol. Evol. 27:1247-1256(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH PIF1; PIF4; PIF6 AND SPT. Strain: cv. Landsberg erecta.
[27]	"A seed coat bedding assay shows that RGL2-dependent release of abscisic acid by the endosperm controls embryo growth in Arabidopsis dormant seeds." Lee K.P., Piskurewicz U., Tureckova V., Strnad M., Lopez-Molina L. Proc. Natl. Acad. Sci. U.S.A. 107:19108-19113(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION DURING IMBIBITION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Kiss of life - Issue 137 of April 2012

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC009895 Genomic DNA. Translation: AAF01590.1. CP002686 Genomic DNA. Translation: AEE73945.1. AK118009 mRNA. Translation: BAC42642.1.
IPI	IPI00521981.
RefSeq	NP_186995.1. NM_111216.2.
UniGene	At.18489. At.67027.
3D structure databases
ProteinModelPortal	Q8GXW1.
SMR	Q8GXW1. Positions 44-106.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8GXW1. 3 interactions.
MINT	MINT-8069272.
STRING	3702.AT3G03450.1-P.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G03450.1; AT3G03450.1; AT3G03450.
GeneID	821251.
KEGG	ath:AT3G03450.
Organism-specific databases
GeneFarm	4240. 427.
TAIR	At3g03450.
Phylogenomic databases
eggNOG	NOG243696.
HOGENOM	HOG000238577.
InParanoid	Q8GXW1.
KO	K14494.
OMA	MLSELNN.
PhylomeDB	Q8GXW1.
ProtClustDB	CLSN2684085.
Gene expression databases
Genevestigator	Q8GXW1.
GermOnline	AT3G03450. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR021914. TF_DELLA_N. IPR005202. TF_GRAS. [Graphical view]
Pfam	PF12041. DELLA. 1 hit. PF03514. GRAS. 1 hit. [Graphical view]
PROSITE	PS50985. GRAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RGL2_ARATH

Accession

Primary (citable) accession number: Q8GXW1
Secondary accession number(s): Q9SRP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	November 22, 2005
Last modified:	May 29, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program