RGA

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: RGA is a nuclear-localized protein. Both transient GFP-RGA in onion epidermis and stable GFP-RGA in transgenic Arabidopsis localize to the nucleus, and nuclear localization is required for its function as a transcriptional repressor. This electronic location annotation is well supported. Supporting Evidence: PMID:9490740 we demonstrated that a transiently expressed green fluorescent protein-RGA fusion protein is localized to the nucleus in onion epidermal cells.
GO:0009740 gibberellic acid mediated signaling pathway	IEA GO_REF:0000117	ACCEPT	Summary: RGA is a core repressor acting in the GA-mediated signaling pathway, immediately downstream of the GID1 receptor. This ARBA electronic annotation captures the central, defining role of RGA and is strongly supported by experimental literature. Reason: This is the central, defining biological process for RGA. While the bare pathway term is less specific than the negative-regulation child term, it is correct and is the core function. Retained as a core annotation. Supporting Evidence: PMID:9490740 This indicates that RGA is a negative regulator of the GA signal transduction pathway. file:ARATH/RGA/RGA-deep-research-falcon.md GA–GID1 signaling inactivates RGA primarily via SCF^SLY1-dependent ubiquitination and proteasomal degradation
GO:0005515 protein binding	IPI PMID:15155881 The Arabidopsis F-box protein SLEEPY1 targets gibberellin si...	MARK AS OVER ANNOTATED	Summary: This IPI captures the direct interaction of RGA (via its C-terminal GRAS domain) with the F-box protein SLY1/GID2, which recruits RGA to the SCF(SLY1) E3 ubiquitin ligase for GA-induced degradation. The bare 'protein binding' term is uninformative. Reason: Per curation guidelines, GO:0005515 protein binding is too generic and should be avoided in favor of an informative MF term. The real interaction (RGA GRAS domain binding the SLY1 F-box protein) is meaningful and central to RGA turnover, but is flagged rather than removed because the underlying interaction is genuine. Supporting Evidence: PMID:15155881 we demonstrated that SLY1 interacts directly with RGA and GA INSENSITIVE (GAI, a closely related DELLA protein) via their C-terminal GRAS domain.
GO:0005515 protein binding	IPI PMID:15161962 The Arabidopsis mutant sleepy1gar2-1 protein promotes plant ...	MARK AS OVER ANNOTATED	Summary: Documents the direct DELLA-SLY1 interaction (SCF(SLY1) E3 ligase binding its DELLA substrate), with the strength of interaction increased by RGA phosphorylation. The generic protein-binding term is uninformative. Reason: Generic 'protein binding' should be avoided. The genuine interaction (RGA as the substrate of the SCF(SLY1) E3 ligase via SLY1) is real and central to GA-induced degradation but is better captured by a specific term. Supporting Evidence: PMID:15161962 SLY1 (the wild-type form) and sly1gar2-1 both confer substrate specificity on this complex via specific binding to the DELLA proteins.
GO:0005515 protein binding	IPI PMID:16709201 Identification and characterization of Arabidopsis gibberell...	MARK AS OVER ANNOTATED	Summary: Documents the GA-dependent interaction between RGA (an AtDELLA) and the gibberellin receptors GID1A/B/C. This receptor binding is the key upstream regulatory step of RGA, but 'protein binding' is uninformative; the specific function is captured by a proposed gibberellin receptor binding term. Reason: Generic protein binding; the meaningful interaction (RGA binding the GA-GID1 receptor complex) is captured by a more specific proposed term. Supporting Evidence: PMID:16709201 A two-hybrid yeast system only showed in vivo interaction in the presence of GA(4) between each AtGID1 and the Arabidopsis DELLA proteins (AtDELLAs), negative regulators of GA signaling. file:ARATH/RGA/RGA-deep-research-falcon.md GA–GID1 binds the DELLA domain of RGA (conserved DELLA/LExLE/VHYNP motifs) to form a GA–GID1–RGA complex
GO:0005515 protein binding	IPI PMID:17194763 Genetic characterization and functional analysis of the GID1...	MARK AS OVER ANNOTATED	Summary: Yeast two-hybrid and pull-down assays show GA enhances the RGA-GID1 interaction (DELLA/VHYNP motif required) and that the GA-GID1 complex promotes RGA-SLY1 binding. Confirms RGA binding to the GA receptor; the generic term is uninformative. Reason: Generic protein binding; specific receptor binding captured by proposed term. Supporting Evidence: PMID:17194763 Yeast two-hybrid and in vitro pull-down assays confirmed that GA enhances the interaction between GID1 and DELLA proteins.
GO:0005515 protein binding	IPI PMID:17416730 The DELLA domain of GA INSENSITIVE mediates the interaction ...	MARK AS OVER ANNOTATED	Summary: Shows the DELLA domain functions as a receiver domain for the activated GID1A GA receptor (demonstrated for GAI with RGA as a close functional homolog and major co-repressor). Supports the RGA-GA receptor interaction; the generic term is uninformative. Reason: Generic protein binding; specific GA receptor binding captured by proposed term. Supporting Evidence: PMID:17416730 we propose that the DELLA domain functions as a receiver domain for activated GA receptors.
GO:0005515 protein binding	IPI PMID:18216856 Coordinated regulation of Arabidopsis thaliana development b...	MARK AS OVER ANNOTATED	Summary: Part of the light/GA framework establishing that DELLA proteins act through interaction with PIF transcription factors to coordinate light and GA control of development. Generic 'protein binding' is uninformative; the meaningful function is inhibitory binding of bHLH (PIF) transcription factors. Reason: Generic protein binding; the biologically meaningful DELLA-PIF inhibitory interaction is captured by the NEW DNA-binding transcription factor binding and transcription regulator inhibitor activity annotations. Supporting Evidence: PMID:18216857 DELLAs block PIF4 transcriptional activity by binding the DNA-recognition domain of this factor.
GO:0005515 protein binding	IPI PMID:18216857 A molecular framework for light and gibberellin control of c...	MARK AS OVER ANNOTATED	Summary: Demonstrates that DELLA proteins block PIF4 transcriptional activity by binding the DNA-recognition domain of this bHLH factor, integrating light and GA control of cell elongation. The generic term is uninformative. Reason: Generic protein binding; the DELLA-PIF4 inhibitory interaction is captured by NEW specific MF annotations. Supporting Evidence: PMID:18216857 DELLAs block PIF4 transcriptional activity by binding the DNA-recognition domain of this factor.
GO:0005515 protein binding	IPI PMID:18827182 Proteolysis-independent downregulation of DELLA repression i...	MARK AS OVER ANNOTATED	Summary: Shows GA-bound GID1 can block DELLA (RGA) repressor activity by direct protein-protein interaction with the DELLA domain, in a proteolysis-independent manner. Confirms RGA-GID1 receptor binding; the generic term is uninformative. Reason: Generic protein binding; specific GA receptor binding captured by proposed term. Supporting Evidence: PMID:18827182 GA-bound GID1 can block DELLA repressor activity by direct protein-protein interaction with the DELLA domain.
GO:0005515 protein binding	IPI PMID:19429606 FRIGIDA delays flowering in Arabidopsis via a cotranscriptio...	REMOVE	Summary: This paper is about FRIGIDA and the nuclear cap-binding complex (FLC regulation); it does not concern RGA function and provides no direct evidence for an informative RGA molecular function. The generic protein-binding term cannot be substantiated for RGA from this reference. Reason: The cited reference does not characterize an RGA interaction; the bare 'protein binding' term is both uninformative and unsupported by this publication for RGA. Supporting Evidence: PMID:19429606 FRIGIDA delays flowering in Arabidopsis via a cotranscriptional mechanism involving direct interaction with the nuclear cap-binding complex.
GO:0005515 protein binding	IPI PMID:19500306 Differential expression and affinities of Arabidopsis gibber...	MARK AS OVER ANNOTATED	Summary: Concerns differential expression and GA-binding affinities of the GID1 receptors and their interaction with DELLAs to explain knockout phenotypes. Supports RGA-GID1 receptor binding but the bare protein-binding term is uninformative. Reason: Generic protein binding; the meaningful RGA-GA receptor interaction is captured by a specific proposed term. Supporting Evidence: PMID:19500306 Differential expression and affinities of Arabidopsis gibberellin receptors can explain variation in phenotypes of multiple knock-out mutants.
GO:0005515 protein binding	IPI PMID:21245327 Scarecrow-like 3 promotes gibberellin signaling by antagoniz...	MARK AS OVER ANNOTATED	Summary: Shows RGA (DELLA) directly interacts with the GRAS protein SCL3, which acts as an attenuator of DELLA function; SCL3 and DELLA antagonize each other in controlling GA responses and GA homeostasis. The generic protein-binding term is uninformative. Reason: Generic protein binding; the genuine DELLA-SCL3 interaction is real and relevant to GA homeostasis but better captured by informative process/MF terms. Supporting Evidence: PMID:21245327 Transient expression, ChIP, and co-IP studies show that SCL3 autoregulates its own transcription by directly interacting with DELLA.
GO:0005515 protein binding	IPI PMID:21798944 Evidence for network evolution in an Arabidopsis interactome...	MARK AS OVER ANNOTATED	Summary: High-throughput binary interactome map (AI-1). Provides large-scale Y2H interaction data but no specific functional characterization of RGA; the generic protein-binding term is uninformative and low-specificity. Reason: Generic protein binding from a high-throughput interactome screen; not informative about RGA molecular function. Supporting Evidence: PMID:21798944 We describe a proteome-wide binary protein-protein interaction map for the interactome network of the plant Arabidopsis thaliana.
GO:0005515 protein binding	IPI PMID:22820377 Brassinosteroid, gibberellin and phytochrome impinge on a co...	MARK AS OVER ANNOTATED	Summary: Demonstrates RGA directly interacts with the brassinosteroid-activated transcription factor BZR1 and inhibits BZR1-DNA binding and transcriptional activity, defining a DELLA-BZR1-PIF4 module integrating GA, BR and light. The generic term is uninformative; the meaningful function is inhibitory TF binding. Reason: Generic protein binding; the DELLA-BZR1 inhibitory interaction is captured by NEW DNA-binding transcription factor binding and transcription regulator inhibitor activity annotations. Supporting Evidence: PMID:22820377 These results indicate that RGA specifically interacts with BZR1 to inhibit its abilities to bind DNA and regulate transcription.
GO:0005515 protein binding	IPI PMID:26801684 DELLA proteins physically interact with CONSTANS to regulate...	MARK AS OVER ANNOTATED	Summary: Shows DELLA proteins (RGA) physically interact with CONSTANS (CO) and that RGA inhibits the CO-NF-YB2 interaction, linking GA and photoperiod control of flowering. The generic protein-binding term is uninformative. Reason: Generic protein binding; the meaningful RGA-CO interaction is real but better captured by an informative TF-binding term. Supporting Evidence: PMID:26801684 the interaction of CO with NF-YB2 is inhibited by the DELLA protein, RGA.
GO:0005515 protein binding	IPI PMID:32612234 Extensive signal integration by the phytohormone protein net...	MARK AS OVER ANNOTATED	Summary: Systems-level phytohormone protein-protein interaction network. Provides large-scale binary interaction data placing DELLAs in a crosstalk hub, but no specific RGA molecular-function characterization. The generic term is uninformative. Reason: Generic protein binding from a high-throughput network screen; not informative about specific RGA molecular function. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions.
GO:0005515 protein binding	IPI PMID:40755058 A DELLA-ANAC106 reciprocal negative feedback circuit modulat...	MARK AS OVER ANNOTATED	Summary: Shows DELLA proteins physically interact with the NAC transcription factor ANAC106 and inhibit its transcriptional activation capacity, forming a reciprocal negative-feedback circuit regulating GA homeostasis and male fertility. The generic protein-binding term is uninformative. Reason: Generic protein binding; the DELLA-ANAC106 inhibitory interaction is real and relevant but better captured by an informative TF-binding term. Supporting Evidence: PMID:40755058 DELLA proteins physically interact with ANAC106 in a dose-dependent manner, inhibiting its transcriptional activation capacity to prevent GA over-accumulation.
GO:0005634 nucleus	IDA PMID:28412546 Prefoldins Negatively Regulate Cold Acclimation in Arabidops...	ACCEPT	Summary: Direct experimental evidence places RGA in the nucleus, where it accumulates in response to cold and mediates DELLA-dependent nuclear accumulation of prefoldins. Core localization for RGA function. Supporting Evidence: PMID:28412546 under cold conditions, PFDs accumulate into the nucleus through a DELLA-dependent mechanism
GO:0009409 response to cold	IDA PMID:28412546 Prefoldins Negatively Regulate Cold Acclimation in Arabidops...	KEEP AS NON CORE	Summary: RGA accumulates in the nucleus in response to cold and mediates the cold-induced nuclear accumulation of prefoldins, which in turn promote HY5 degradation to attenuate cold acclimation. This is one of many downstream, pleiotropic environmental responses integrated by DELLA, not the core GA-repressor function. Reason: RGA participates in cold responses as part of its role as a hormonal/environmental signal integrator, but this is a peripheral process for this pleiotropic repressor rather than its core function. Supporting Evidence: PMID:28412546 under cold conditions, PFDs accumulate into the nucleus through a DELLA-dependent mechanism, where they interact with HY5, triggering its ubiquitination and subsequent degradation.
GO:0005515 protein binding	IPI PMID:33660280 A novel Arabidopsis gene RGAT1 is required for GA-mediated t...	MARK AS OVER ANNOTATED	Summary: Concerns RGAT1, a direct transcriptional target of RGA in anther development; the relevant relationship is RGA activating RGAT1 expression rather than a specific informative binary RGA protein-protein interaction. The generic protein-binding term is uninformative. Reason: Generic protein binding; the paper's relevant finding (RGA activates RGAT1 transcription, controlling tapetum/pollen development) is better captured by process annotations rather than a bare MF binding term. Supporting Evidence: PMID:33660280 RGAT1 is a direct target of RGA and plays an essential role in GA-mediated tapetum and pollen development.
GO:0000976 transcription cis-regulatory region binding	IPI PMID:22037706 Enhanced Y1H assays for Arabidopsis.	REMOVE	Summary: This annotation derives from a high-throughput enhanced yeast one-hybrid (eY1H) screen in which RGA scored as binding stele-expressed promoters. RGA lacks any recognizable DNA-binding domain and is well documented to associate with promoters only indirectly, via DNA-binding transcription factors (e.g. IDDs). eY1H readouts for GRAS/DELLA proteins reflect this indirect tethering or assay artifacts rather than intrinsic sequence-specific DNA binding. Reason: RGA has no DNA-binding domain; multiple primary studies state DELLAs lack DNA-binding motifs and associate with promoters only indirectly through partner transcription factors. A direct cis-regulatory-region-binding MF annotation mis-assigns DNA-binding activity to RGA. Supporting Evidence: PMID:25035403 a chromatin immunoprecipitation ( ChIP ) assay showed an in vivo association of DELLAs with promoters of several genes, although DELLAs lack known DNA binding motifs PMID:24821766 because DELLA lacks a DNA-binding domain, intermediate protein(s) mediating the DELLA/DNA interaction are believed to be necessary for activating DELLA target genes. file:ARATH/RGA/RGA-deep-research-falcon.md RGA does not bind DNA directly; instead, it acts through protein–protein interactions with transcription factors (TFs) and chromatin components, including histone H2A, to reprogram gene expression.
GO:0000976 transcription cis-regulatory region binding	IPI PMID:25352272 Promoter-based integration in plant defense regulation.	REMOVE	Summary: Derived from a large yeast one-hybrid screen of glucosinolate/defense promoters. As above, RGA is a non-DNA-binding GRAS/DELLA protein; any promoter binding is indirect (through partner TFs) and a direct DNA-binding MF annotation is mechanistically incorrect. Reason: RGA lacks a DNA-binding domain; direct cis-regulatory region binding is not a genuine RGA molecular function. Promoter association is indirect via partner transcription factors. Supporting Evidence: PMID:24821766 because DELLA lacks a DNA-binding domain, intermediate protein(s) mediating the DELLA/DNA interaction are believed to be necessary for activating DELLA target genes.
GO:0000976 transcription cis-regulatory region binding	IPI PMID:25533953 An Arabidopsis gene regulatory network for secondary cell wa...	REMOVE	Summary: From a Y1H-based secondary-cell-wall gene regulatory network, where GRAS family proteins (including RGA) appeared among promoter-binding factors. RGA lacks a DNA-binding domain; direct cis-regulatory region binding is not a genuine RGA molecular function. Reason: RGA has no DNA-binding domain; Y1H positives for DELLA/GRAS proteins reflect indirect/artifactual binding rather than intrinsic sequence-specific DNA binding. Supporting Evidence: PMID:25035403 a chromatin immunoprecipitation ( ChIP ) assay showed an in vivo association of DELLAs with promoters of several genes, although DELLAs lack known DNA binding motifs
GO:0005515 protein binding	IPI PMID:24989044 Arabidopsis DELLA and two HD-ZIP transcription factors regul...	MARK AS OVER ANNOTATED	Summary: Shows RGA (DELLA) directly interacts with the HD-ZIP transcription factors ATML1 and PDF2; GA-induced reduction of DELLA releases ATML1/PDF2 to activate L1-box epidermal genes (e.g. LIP1) and promote germination. The generic protein-binding term is uninformative; the meaningful function is inhibitory TF binding. Reason: Generic protein binding; the DELLA-ATML1/PDF2 inhibitory interaction is captured by NEW DNA-binding transcription factor binding annotation. Supporting Evidence: PMID:24989044 We show that DELLA proteins interact directly with ATML1 and its paralogue PDF2
GO:0010029 regulation of seed germination	IEP PMID:24989044 Arabidopsis DELLA and two HD-ZIP transcription factors regul...	KEEP AS NON CORE	Summary: RGA (with other DELLAs) negatively regulates seed germination; in the epidermis it represses L1-box genes by sequestering ATML1/PDF2, and increased GA on imbibition reduces DELLA to release germination. A genuine but non-core, partially redundant developmental role (RGL2 is the dominant DELLA in germination). Reason: Regulation of seed germination is one of many downstream developmental processes controlled by this pleiotropic repressor; RGA plays a minor/redundant role here relative to RGL2. Supporting Evidence: PMID:24989044 upon seed imbibition, increased GA levels reduce DELLA protein abundance and release ATML1/PDF2 to activate L1 box gene expression, thus enhancing germination potential.
GO:2000033 regulation of seed dormancy process	IEP PMID:24989044 Arabidopsis DELLA and two HD-ZIP transcription factors regul...	KEEP AS NON CORE	Summary: Consistent with UniProt's curated function, RGA is involved in regulation of seed dormancy/germination (including glucose-induced delay of germination). A genuine but non-core, partially redundant developmental role. Reason: Peripheral developmental process for this pleiotropic repressor. Supporting Evidence: PMID:24989044 blocking GA signaling in the epidermis represses the expression of L1 box-containing genes and negatively affects seed germination.
GO:0000976 transcription cis-regulatory region binding	IPI PMID:31806676 A PXY-Mediated Transcriptional Network Integrates Signaling ...	REMOVE	Summary: From an eY1H-based PXY/vascular development transcriptional network. RGA appearing as a promoter-binding factor reflects indirect tethering, since RGA lacks a DNA-binding domain. Direct cis-regulatory region binding is not a genuine RGA molecular function. Reason: RGA has no DNA-binding domain; Y1H positives reflect indirect/artifactual DNA association rather than intrinsic sequence-specific binding. Supporting Evidence: PMID:24821766 because DELLA lacks a DNA-binding domain, intermediate protein(s) mediating the DELLA/DNA interaction are believed to be necessary for activating DELLA target genes.
GO:0005634 nucleus	ISM GO_REF:0000122	ACCEPT	Summary: Sequence-based (AtSubP) prediction of nuclear localization, consistent with abundant experimental evidence for nuclear RGA. Accept. Supporting Evidence: PMID:11449051 The green fluorescent protein (GFP)-RGA fusion protein was localized to nuclei in transgenic Arabidopsis.
GO:0005515 protein binding	IPI PMID:25035403 DELLAs function as coactivators of GAI-ASSOCIATED FACTOR1 in...	MARK AS OVER ANNOTATED	Summary: Shows RGA (DELLA) binds and coactivates the IDD transcription factor GAF1/IDD2 (and ENY/IDD1); DELLA acts as a coactivator of GAF1 (with TPR as corepressor) at GA feedback genes. This is the key coactivator interaction but the generic protein-binding term is uninformative. Reason: Generic protein binding; the coactivator interaction with IDD TFs is captured by NEW transcription coactivator and DNA-binding TF binding annotations. Supporting Evidence: PMID:25035403 DELLAs and TOPLESS-RELATED (TPR) act as coactivators and a corepressor of GAF1, respectively, in GA -mediated transcriptional regulation.
GO:0005515 protein binding	IPI PMID:24821766 DELLA protein functions as a transcriptional activator throu...	MARK AS OVER ANNOTATED	Summary: Identifies five INDETERMINATE DOMAIN (IDD) zinc-finger transcription factors that bind both RGA and the SCL3 promoter; RGA uses IDDs as DNA-binding scaffolds to coactivate target genes such as SCL3. The generic protein-binding term is uninformative; the function is DNA-binding TF binding and coactivation. Reason: Generic protein binding; the RGA-IDD coactivator interaction is captured by NEW specific MF annotations. Supporting Evidence: PMID:24821766 we identified five members of INDETERMINATE DOMAIN (IDD) protein family which bind physically to both DELLA and the promoter sequence of the GA-positive regulator SCARECROW-LIKE 3 ( SCL3 )
GO:0005634 nucleus	IDA PMID:24821766 DELLA protein functions as a transcriptional activator throu...	ACCEPT	Summary: RGA binds IDD zinc-finger proteins in the nucleus; direct evidence of nuclear localization consistent with its role as a nuclear transcriptional cofactor. Accept as core localization. Supporting Evidence: PMID:24821766 DELLA and SCL3, using IDDs as transcriptional scaffolds for DNA binding, antagonistically regulate the expression of their downstream targets to control the GA signaling pathway.
GO:0045893 positive regulation of DNA-templated transcription	IDA PMID:24821766 DELLA protein functions as a transcriptional activator throu...	ACCEPT	Summary: RGA additively transactivates an SCL3-promoter reporter together with IDD proteins, acting as a transcriptional coactivator. This is a genuine, mechanistically important molecular activity of RGA (it activates DELLA-induced genes such as SCL3 and GA biosynthetic/receptor genes via IDD/GAF1 scaffolds). Reason: DELLA proteins exert dual transcriptional effects; the positive (coactivation) arm at IDD-bound feedback genes is well documented. This is a core aspect of RGA's transcriptional cofactor function. Supporting Evidence: PMID:24821766 a luciferase reporter controlled by the SCL3 promoter was additively transactivated by REPRESSOR of ga1-3 (RGA) and IDDs. PMID:25035403 DELLAs promote the transcription of genes encoding GA biosynthetic enzymes and GA receptors as coactivators of a DNA binding transcription factor, GAF1. file:ARATH/RGA/RGA-deep-research-falcon.md This supports a modern view of DELLAs as context-dependent transcriptional regulators (coactivator/corepressor roles) rather than simple repressors.
GO:0005515 protein binding	IPI PMID:29255112 MLK1 and MLK2 Coordinate RGA and CCA1 Activity to Regulate H...	MARK AS OVER ANNOTATED	Summary: RGA interacts with the casein-kinase-like MLK1/MLK2 and with the MYB-type clock TF CCA1; RGA suppresses CCA1 activation of DWF4 and MLK1/2 antagonize this, coordinating GA and circadian control of hypocotyl elongation. The generic protein-binding term is uninformative; the meaningful function is inhibitory TF binding (CCA1). Reason: Generic protein binding; the RGA-CCA1 inhibitory interaction is captured by NEW DNA-binding transcription factor binding annotation. Supporting Evidence: PMID:29255112 RGA suppressed the ability of CCA1 to activate expression from the DWF4 promoter, but MLK1/2 reversed this suppression.
GO:1990841 promoter-specific chromatin binding	IDA PMID:29255112 MLK1 and MLK2 Coordinate RGA and CCA1 Activity to Regulate H...	MARK AS OVER ANNOTATED	Summary: RGA associates with the DWF4 promoter region in vivo (ChIP), but this association is mediated by the DNA-binding factor CCA1, since RGA lacks a DNA-binding domain. The chromatin association is real but indirect. Reason: RGA has no DNA-binding domain; its promoter/chromatin association is indirect (via CCA1). A direct promoter-specific chromatin-binding MF over-states intrinsic DNA/chromatin binding capacity. Flagged rather than removed because in vivo promoter occupancy was observed. Supporting Evidence: PMID:29255112 The deposition of CCA1 was enriched in rga-28, but reduced in mlk1 mlk2 double mutants PMID:24821766 because DELLA lacks a DNA-binding domain, intermediate protein(s) mediating the DELLA/DNA interaction are believed to be necessary for activating DELLA target genes.
GO:1990841 promoter-specific chromatin binding	IPI PMID:29255112 MLK1 and MLK2 Coordinate RGA and CCA1 Activity to Regulate H...	MARK AS OVER ANNOTATED	Summary: Duplicate of the preceding promoter-specific chromatin binding annotation (same reference, IPI evidence). RGA chromatin association at DWF4 is indirect, mediated by CCA1. Reason: RGA lacks a DNA-binding domain; promoter/chromatin association is indirect via partner TFs. Same rationale as the paired IDA annotation. Supporting Evidence: PMID:24821766 because DELLA lacks a DNA-binding domain, intermediate protein(s) mediating the DELLA/DNA interaction are believed to be necessary for activating DELLA target genes.
GO:0033206 meiotic cytokinesis	IMP PMID:27621423 Gibberellin Induces Diploid Pollen Formation by Interfering ...	KEEP AS NON CORE	Summary: rga gai double mutants (and GA treatment) cause defects in male meiotic cytokinesis and diploid pollen formation, with RGA expressed in somatic anther cell layers surrounding meiocytes. A peripheral, non-core developmental role mediated indirectly via downstream MYB33/MYB65. Reason: A specific downstream developmental output (anther/pollen development) of GA-DELLA signaling, not the core repressor function. The acts_upstream_of_or_within qualifier appropriately reflects the indirect relationship. Supporting Evidence: PMID:27621423 Similar defects in meiotic cell division and reproductive ploidy stability occur in Arabidopsis plants depleted of RGA and GAI, two members of the DELLA family that function as suppressor of GA signaling.
GO:0009739 response to gibberellin	IMP PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	ACCEPT	Summary: rga loss-of-function mutations partially suppress the GA-deficient ga1-3 phenotype and rga/gai together completely rescue many GA-response defects, establishing RGA as a central component of the response to gibberellin. Core involvement. Supporting Evidence: PMID:11606552 rga loss-of-function mutations were shown to partially suppress defects of the GA-deficient ga1-3 mutant.
GO:0009739 response to gibberellin	IGI PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	ACCEPT	Summary: Genetic-interaction (rga-24/gai-t6 synergy) evidence for RGA's central role in the response to gibberellin. Duplicate term with IGI evidence; both are valid. Supporting Evidence: PMID:11606552 the rga-24 and gai-t6 null mutations have a synergistic effect on plant growth.
GO:0010628 positive regulation of gene expression	IMP PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	KEEP AS NON CORE	Summary: RGA positively affects expression of GA-feedback-regulated genes; rga mutation reduces GA4 (GA biosynthetic gene) expression, and DELLA induces expression of its direct target genes. This positive (coactivation/feedback) arm of DELLA transcriptional regulation is genuine, though the term is generic. Reason: RGA does positively regulate expression of feedback and DELLA-target genes, but the bare 'positive regulation of gene expression' term is broad and represents one downstream consequence rather than its core function. The mechanistically specific positive role is better captured by the coactivator MF annotation. Supporting Evidence: PMID:11606552 rga-24 and rga-24/gai-t6 but not gai-t6 alone caused increased feedback inhibition of expression of a GA biosynthetic gene
GO:0010628 positive regulation of gene expression	IGI PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	KEEP AS NON CORE	Summary: Genetic-interaction evidence (rga/gai) for RGA's positive influence on GA-feedback gene expression. Duplicate term with IGI evidence; same rationale as the IMP version. Reason: Broad downstream term; genuine but non-core, and better captured mechanistically by the coactivator MF. Supporting Evidence: PMID:11606552 rga-24 and rga-24/gai-t6 but not gai-t6 alone caused increased feedback inhibition of expression of a GA biosynthetic gene
GO:0009909 regulation of flower development	IMP NOT PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	ACCEPT	Summary: A NOT annotation. Dill and Sun (2001) showed that removing RGA and GAI did NOT restore flower development defects of ga1-3, indicating RGA/GAI are not the DELLAs responsible for the flower development arm in this genetic context. The negated annotation is correctly supported. Reason: The paper explicitly states flower development defects were not rescued by rga gai, supporting the NOT qualifier for this RGA-with-GAI genetic context. Supporting Evidence: PMID:11606552 However, seed germination and flower development defects were not restored.
GO:0009909 regulation of flower development	IGI NOT PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	ACCEPT	Summary: Genetic-interaction NOT annotation paralleling the IMP version; rga gai double mutant does not restore ga1-3 flower development defects. Reason: Correctly negated; supported by the explicit statement that flower development defects were not restored. Supporting Evidence: PMID:11606552 However, seed germination and flower development defects were not restored.
GO:0009938 negative regulation of gibberellic acid mediated signaling pathway	IGI PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	ACCEPT	Summary: This is the precise, core function of RGA: it is a negative regulator of the GA-mediated signaling pathway, acting redundantly with GAI but more dominantly. Strongly supported genetic-interaction evidence. Reason: Most specific and accurate process term for RGA's defining role. Supporting Evidence: PMID:11606552 These results demonstrate that RGA and GAI have partially redundant functions in maintaining the repressive state of the GA-signaling pathway, but RGA plays a more dominant role than GAI.
GO:0010029 regulation of seed germination	IMP NOT PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	ACCEPT	Summary: A NOT annotation. Removing RGA and GAI did not restore the seed germination defect of ga1-3, indicating RGA/GAI are not the major DELLAs for germination (RGL2 is). Correctly negated and supported. Reason: Explicitly supported; germination defects were not rescued by rga gai. Supporting Evidence: PMID:11606552 However, seed germination and flower development defects were not restored.
GO:0010029 regulation of seed germination	IGI NOT PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	ACCEPT	Summary: Genetic-interaction NOT annotation paralleling the IMP version. rga gai does not restore germination defects of ga1-3. Reason: Correctly negated and supported. Supporting Evidence: PMID:11606552 However, seed germination and flower development defects were not restored.
GO:0080154 regulation of fertilization	IMP NOT PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	ACCEPT	Summary: A NOT annotation derived from the observation that rga gai does not rescue the reproductive (flower development/fertility) defects of ga1-3. The negation is consistent with the paper, though 'regulation of fertilization' is a somewhat loose mapping of the reported flower/fertility defect. Reason: Consistent with the explicit statement that flower development (and associated fertility) defects were not restored by rga gai; correctly negated. Supporting Evidence: PMID:11606552 However, seed germination and flower development defects were not restored.
GO:0080154 regulation of fertilization	IGI NOT PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	ACCEPT	Summary: Genetic-interaction NOT annotation paralleling the IMP version. Reason: Correctly negated; supported by the unrescued flower/fertility defects. Supporting Evidence: PMID:11606552 However, seed germination and flower development defects were not restored.
GO:1900033 negative regulation of trichome patterning	IMP PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	KEEP AS NON CORE	Summary: rga (and rga gai) rescue/restore abaxial trichome initiation defects of ga1-3, showing RGA represses GA-promoted trichome initiation. A genuine but non-core, specific developmental output of GA-DELLA signaling. Reason: A specific downstream developmental process repressed by RGA, not its core GA-repressor function; pleiotropic output. Supporting Evidence: PMID:11606552 Phenotypes rescued include abaxial trichome initiation, rosette radius, flowering time, stem elongation, and apical dominance.
GO:1900033 negative regulation of trichome patterning	IGI PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	KEEP AS NON CORE	Summary: Genetic-interaction evidence (rga/gai synergy) for RGA repression of trichome initiation. Duplicate term with IGI; same non-core rationale. Reason: Specific downstream developmental output, non-core. Supporting Evidence: PMID:11606552 Phenotypes rescued include abaxial trichome initiation, rosette radius, flowering time, stem elongation, and apical dominance.
GO:1905613 regulation of developmental vegetative growth	IMP NOT PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	REMOVE	Summary: A NOT annotation. This is mechanistically questionable: RGA and GAI are in fact the major repressors of GA-promoted vegetative growth (rga gai rescues stem elongation, leaf expansion, rosette radius of ga1-3). The negation of an unsigned 'regulation of developmental vegetative growth' likely reflects a curation interpretation; the correctly-signed annotation (negative regulation, below) is the appropriate one. Reason: RGA clearly regulates (negatively) developmental vegetative growth; the negated unsigned 'regulation of developmental vegetative growth' is confusing and redundant given the correctly-signed positive (non-negated) 'negative regulation of developmental vegetative growth' annotation that follows. Remove to avoid contradiction. Supporting Evidence: PMID:11606552 they completely rescued the above defects of ga1-3 to wild-type or GA-overdose phenotype.
GO:1905614 negative regulation of developmental vegetative growth	IGI PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	ACCEPT	Summary: This is the correctly-signed, central vegetative function: RGA (with GAI) negatively regulates GA-promoted vegetative growth (stem elongation, leaf expansion, rosette radius). Core developmental output of RGA's repressor activity. Reason: Accurately captures RGA's dominant role in repressing GA-promoted vegetative growth, strongly supported by the rga/gai synergy genetics. Supporting Evidence: PMID:11606552 when combined with rga-24, they completely rescued the above defects of ga1-3 to wild-type or GA-overdose phenotype.
GO:1905622 negative regulation of leaf development	IMP PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	KEEP AS NON CORE	Summary: RGA (with GAI) represses GA-promoted leaf expansion; rga gai rescues the leaf/rosette defects of ga1-3. A genuine but non-core, specific developmental output. Reason: Specific downstream developmental output of the repressor function, non-core. Supporting Evidence: PMID:11606552 Phenotypes rescued include abaxial trichome initiation, rosette radius, flowering time, stem elongation, and apical dominance.
GO:1905622 negative regulation of leaf development	IGI PMID:11606552 Synergistic derepression of gibberellin signaling by removin...	KEEP AS NON CORE	Summary: Genetic-interaction evidence for RGA repression of leaf development/expansion. Duplicate term with IGI; same non-core rationale. Reason: Specific downstream developmental output, non-core. Supporting Evidence: PMID:11606552 Phenotypes rescued include abaxial trichome initiation, rosette radius, flowering time, stem elongation, and apical dominance.
GO:0005515 protein binding	IPI PMID:22942378 Gibberellin regulates the Arabidopsis floral transition thro...	MARK AS OVER ANNOTATED	Summary: Shows DELLA (RGA) directly binds miR156-targeted SPL transcription factors, interfering with SPL transcriptional activity to delay floral transition. The generic protein-binding term is uninformative; the meaningful function is inhibitory TF binding. Reason: Generic protein binding; the DELLA-SPL inhibitory interaction is captured by NEW DNA-binding transcription factor binding annotation. Supporting Evidence: PMID:22942378 DELLA directly binds to microRNA156 (miR156)-targeted SQUAMOSA PROMOTER BINDING-LIKE (SPL) transcription factors
GO:0006355 regulation of DNA-templated transcription	TAS PMID:11118137 Arabidopsis transcription factors: genome-wide comparative a...	ACCEPT	Summary: A broad transcriptional-regulation process term, derived from the genome-wide TF survey that classifies RGA among transcriptional regulators. RGA does function in transcriptional regulation (as a cofactor), so this broad term is acceptable, though more specific child terms are warranted. Reason: Correct but general; RGA acts in DNA-templated transcription regulation via its cofactor activities. Retained as a broadly accurate process annotation. Supporting Evidence: PMID:25035403 DELLAs simultaneously turn on or off two sets of GA-regulated genes via two mechanisms, namely titration and coactivation.
GO:0005515 protein binding	IPI PMID:20093430 Transcriptional diversification and functional conservation ...	MARK AS OVER ANNOTATED	Summary: Shows RGA interacts with PIF4 and other bHLH transcription factors (PIF1, PIF6, SPT) that control cell growth and seed germination; DELLA functional diversification largely reflects expression patterns rather than partner specificity. The generic protein-binding term is uninformative; the function is inhibitory bHLH-TF binding. Reason: Generic protein binding; the RGA-PIF/bHLH inhibitory interaction is captured by NEW DNA-binding transcription factor binding annotation. Supporting Evidence: PMID:20093430 both DELLA proteins display equivalent abilities to interact with PIF4 and with other bHLH transcription factors with a reported role in the control of cell growth and seed germination.
GO:0042176 regulation of protein catabolic process	IMP PMID:19717618 Biochemical insights on degradation of Arabidopsis DELLA pro...	REMOVE	Summary: This cell-free study characterizes how RGA (TAP-RGA substrate) is degraded via Lys-29-linked ubiquitin chains by SCF(SLY1); it dissects DELLA degradation, i.e. RGA is the regulated substrate, not a regulator of a protein catabolic process. Assigning RGA the role 'regulation of protein catabolic process' over-interprets RGA as an upstream controller of proteolysis. Reason: The evidence shows RGA being degraded (it is the target of ubiquitin-mediated catabolism), not RGA regulating a protein catabolic process. The annotation mis-assigns a regulatory role. RGA's own ubiquitination/degradation is a PTM captured by UniProt, not a function it enables on other proteins. Supporting Evidence: PMID:19717618 we used the cell-free degradation of TAP-RGA to test the competitive efficiencies of exogenously added mutant ubiquitins.
GO:0003700 DNA-binding transcription factor activity	IDA PMID:17933900 Global analysis of della direct targets in early gibberellin...	MODIFY	Summary: This annotation assigns intrinsic DNA-binding transcription factor activity to RGA based on ChIP evidence of in vivo DELLA-promoter association. However, RGA lacks any DNA-binding domain; its in vivo promoter association is mediated by partner DNA-binding TFs (IDDs, etc.). DELLAs act as transcriptional coactivators/corepressors, not as sequence-specific DNA-binding transcription factors. Reason: RGA has no DNA-binding domain and does not act as a sequence-specific DNA-binding transcription factor; multiple primary studies state DELLAs lack DNA-binding motifs. The accurate molecular function is transcription coregulator activity (acting through partner TFs). Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:17933900 These GA-signaling repressors are nuclear localized and likely function as transcriptional regulators. PMID:24821766 because DELLA lacks a DNA-binding domain, intermediate protein(s) mediating the DELLA/DNA interaction are believed to be necessary for activating DELLA target genes. file:ARATH/RGA/RGA-deep-research-falcon.md DELLAs are nucleus-localized regulators that generally do not bind DNA directly and instead control transcription by interacting with many TFs and transcriptional regulators, with chromatin association detectable by ChIP/ChIP-seq
GO:0010218 response to far red light	IEP PMID:17449805 PIL5, a phytochrome-interacting bHLH protein, regulates gibb...	KEEP AS NON CORE	Summary: RGA expression is regulated by the phytochrome-interacting factor PIL5/PIF1 (PIL5 binds RGA and GAI promoters), linking phytochrome/red-far-red light signaling to GA responsiveness in seeds. RGA participates in light-modulated GA responses, a non-core, downstream environmental integration role. Reason: RGA is downstream of light signaling (its abundance and transcription are light-regulated) and contributes to light-modulated germination; a peripheral environmental-integration role rather than its core function. Supporting Evidence: PMID:17449805 PIL5 increases the expression of two GA repressor (DELLA) genes, GA-INSENSITIVE ( GAI ) and REPRESSOR OF GA1-3 ( RGA/RGA1 ), in darkness.
GO:0009740 gibberellic acid mediated signaling pathway	TAS PMID:11449051 Repressing a repressor: gibberellin-induced rapid reduction ...	ACCEPT	Summary: RGA is a repressor of GA signaling whose protein level is rapidly reduced by GA, derepressing the pathway. Core involvement in the GA-mediated signaling pathway, with author-traceable statement support. Reason: Core process for RGA. Duplicate of the IEA GA-signaling annotation with TAS evidence; both valid. Supporting Evidence: PMID:11449051 the GA signal appears to derepress the GA signaling pathway by degrading the repressor protein RGA.
GO:0003700 DNA-binding transcription factor activity	TAS PMID:11449051 Repressing a repressor: gibberellin-induced rapid reduction ...	MODIFY	Summary: Based on the historical inference from sequence features that RGA is a 'transcriptional regulator'. This was interpreted as DNA-binding TF activity, but RGA lacks a DNA-binding domain and acts as a transcriptional cofactor through partner TFs. Reason: RGA has no DNA-binding domain; sequence-feature-based inference of TF activity predates the demonstration that DELLAs lack DNA binding and act via partner TFs. Replace with transcription coregulator activity. Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:11449051 This result supports the predicted function of RGA as a transcriptional regulator based on sequence analysis. PMID:25035403 However, the effect of GA on gene expression is predominantly repression, and DELLAs associate with the promoters of DELLA-induced genes even though DELLA proteins lack DNA binding motifs ( Zentella et al., 2007 ; Hirano et al., 2012 ; Lim et al., 2013 ; Park et al., 2013 ).
GO:0005634 nucleus	TAS PMID:11449051 Repressing a repressor: gibberellin-induced rapid reduction ...	ACCEPT	Summary: GFP-RGA localizes to nuclei in transgenic Arabidopsis. Core nuclear localization, author-statement supported. Duplicate location term with TAS evidence. Supporting Evidence: PMID:11449051 The green fluorescent protein (GFP)-RGA fusion protein was localized to nuclei in transgenic Arabidopsis.
GO:0003700 DNA-binding transcription factor activity	ISS PMID:11118137 Arabidopsis transcription factors: genome-wide comparative a...	MODIFY	Summary: Sequence-similarity-based assignment of DNA-binding TF activity from a genome-wide TF catalogue. RGA was classified as a transcription factor by the GRAS family, but it lacks a DNA-binding domain and functions as a transcription cofactor. Reason: RGA has no DNA-binding domain; the ISS-based DNA-binding TF activity assignment is incorrect at the molecular level. Replace with transcription coregulator activity. Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:24821766 because DELLA lacks a DNA-binding domain, intermediate protein(s) mediating the DELLA/DNA interaction are believed to be necessary for activating DELLA target genes.
GO:0005634 nucleus	IDA PMID:9490740 The Arabidopsis RGA gene encodes a transcriptional regulator...	ACCEPT	Summary: The original RGA characterization showed GFP-RGA localizes to the nucleus (onion epidermal cells). Core nuclear localization with direct experimental evidence. Duplicate location term. Supporting Evidence: PMID:9490740 a transiently expressed green fluorescent protein-RGA fusion protein is localized to the nucleus in onion epidermal cells.
GO:0003712 transcription coregulator activity	IDA PMID:24821766 DELLA protein functions as a transcriptional activator throu...	NEW	Summary: NEW annotation capturing RGA's accurate molecular function. RGA lacks a DNA-binding domain and acts as a transcriptional coregulator: it coactivates target genes (e.g. SCL3, GA biosynthetic/receptor genes) via IDD/GAF1 DNA-binding scaffolds, and represses growth-promoting genes by titrating/inhibiting DNA-binding TFs (PIFs, BZR1, SPL, CCA1). This replaces the incorrect DNA-binding transcription factor activity annotations. Reason: Provides the informative, mechanistically accurate MF for RGA in place of GO:0003700 (DNA-binding TF activity) and bare GO:0005515 (protein binding). Supporting Evidence: PMID:24821766 the coregulators DELLA and SCL3, using IDDs as transcriptional scaffolds for DNA binding, antagonistically regulate the expression of their downstream targets PMID:25035403 DELLAs and TOPLESS-RELATED (TPR) act as coactivators and a corepressor of GAF1, respectively, in GA -mediated transcriptional regulation. file:ARATH/RGA/RGA-deep-research-falcon.md RGA is described as a nuclear-localized transcription regulator that controls expression of GA-responsive and other genes via protein interactions rather than catalytic activity
GO:0140297 DNA-binding transcription factor binding	IPI PMID:22820377 Brassinosteroid, gibberellin and phytochrome impinge on a co...	NEW	Summary: NEW annotation. RGA's defining biochemical activity is direct binding to DNA-binding transcription factors. It physically interacts with the bHLH PIFs, BZR1, SPT, MYC2, the MYB factor CCA1, SPL factors, HD-ZIP ATML1/PDF2, NAC ANAC106, IDD zinc-finger factors, and CO, generally to inhibit (titrate) or, for IDDs, to coactivate them. This specific MF replaces the many generic GO:0005515 protein-binding annotations to these transcription factors. Reason: Captures the specific, well-documented class of partners (DNA-binding transcription factors) through which RGA acts, replacing uninformative 'protein binding'. Supporting Evidence: PMID:22820377 These results indicate that RGA specifically interacts with BZR1 to inhibit its abilities to bind DNA and regulate transcription. PMID:18216857 DELLAs block PIF4 transcriptional activity by binding the DNA-recognition domain of this factor. file:ARATH/RGA/RGA-deep-research-falcon.md RGA does not bind DNA directly; instead, it acts through protein–protein interactions with transcription factors (TFs) and chromatin components, including histone H2A, to reprogram gene expression.
GO:0140416 transcription regulator inhibitor activity	IPI PMID:18216857 A molecular framework for light and gibberellin control of c...	NEW	Summary: NEW annotation. A major mode of RGA action is to inhibit the activity of transcription factors by direct binding - e.g. it binds the DNA-recognition domain of PIF4 and blocks its transcriptional activity, and likewise inhibits BZR1, CCA1, SPL and CO function. This transcription-regulator-inhibitor activity captures the 'titration/sequestration' arm of DELLA function that the generic protein-binding terms missed. Reason: Captures RGA's well-documented inhibitory effect on partner transcription factors (the titration mechanism), an informative MF distinct from coactivation. Supporting Evidence: PMID:18216857 DELLAs block PIF4 transcriptional activity by binding the DNA-recognition domain of this factor. PMID:25035403 DELLAs inhibit transcriptional activators by preventing DNA binding.
GO:0003700 DNA-binding transcription factor activity	IBA GO_REF:0000033	MODIFY	Summary: DNA-binding transcription factor activity inherited from the GRAS family root node PTN000780710. Reason: Same claim as this gene's other GO:0003700 rows and given the same action. DELLA proteins have no DNA-binding domain; they regulate transcription as coactivators of DNA-binding factors (IDD/GAF1) and by sequestering others (PIFs). The IBD at the GRAS root generalizes a DNA-binding activity that no DELLA has been shown to have. Propagation Review Root cause: SOURCE BAD Failure modes: ROLE CONFLATION Sources checked: PANTHER:PTN000780710 · PTN000780710 SOURCE BAD 2017 IBD at the root of the whole GRAS family, seeded by RGA, SCR and Medicago RAM1. The PTHR31636 family review rates it WRONG_NODE. DELLAs and SHR-SCR lack a DNA-binding domain and act as cofactors of DNA-binding partners (IDD/GAF1, JKD), so the seeds do not support a DNA-binding transcription factor activity for the ancestral GRAS protein. Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:17933900 These GA-signaling repressors are nuclear localized and likely function as transcriptional regulators. PMID:24821766 because DELLA lacks a DNA-binding domain, intermediate protein(s) mediating the DELLA/DNA interaction are believed to be necessary for activating DELLA target genes.
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: Nuclear localization inherited from the GRAS family root node PTN000780710. Reason: Matches this gene's experimental nuclear rows. The PTHR31636 family review rates this node SOUND, and every reviewed GRAS member accepts nucleus. Supporting Evidence: PMID:9490740 we demonstrated that a transiently expressed green fluorescent protein-RGA fusion protein is localized to the nucleus in onion epidermal cells. PMID:28412546 under cold conditions, PFDs accumulate into the nucleus through a DELLA-dependent mechanism
GO:0006355 regulation of DNA-templated transcription	IBA GO_REF:0000033	ACCEPT	Summary: Regulation of DNA-templated transcription inherited from the GRAS family root node PTN000780710. Reason: Correct when read as transcriptional regulation by any mechanism. DELLAs coactivate GAF1/IDD factors and sequester PIFs, so they regulate transcription without binding DNA themselves. The PTHR31636 family review rates this node SOUND. Supporting Evidence: PMID:25035403 DELLAs simultaneously turn on or off two sets of GA-regulated genes via two mechanisms, namely titration and coactivation.
GO:0009739 response to gibberellin	IBA GO_REF:0000033	ACCEPT	Summary: Response to gibberellin inherited from the eurosid GAI/RGA clade node PTN004849723. Reason: Matches this gene's experimental rows for the same term. GA triggers GID1-dependent, SCF(SLY1)-mediated degradation of the DELLA, which is the core of the GA response. The family review rates the node SOUND. Supporting Evidence: PMID:11606552 rga loss-of-function mutations were shown to partially suppress defects of the GA-deficient ga1-3 mutant. PMID:11606552 the rga-24 and gai-t6 null mutations have a synergistic effect on plant growth.
GO:0009938 negative regulation of gibberellic acid mediated signaling pathway	IBA GO_REF:0000033	ACCEPT	Summary: Negative regulation of gibberellin signaling inherited from the GAI/RGA clade node PTN004849723. Reason: Core DELLA function, matching this gene's experimental rows. The family review rates the placement SOUND (if anything conservative). Supporting Evidence: PMID:11606552 These results demonstrate that RGA and GAI have partially redundant functions in maintaining the repressive state of the GA-signaling pathway, but RGA plays a more dominant role than GAI.
GO:1900033 negative regulation of trichome patterning	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Negative regulation of trichome patterning inherited from the GAI/RGA clade node PTN004849723. Reason: Matches this gene's experimental rows, kept non-core as a pleiotropic developmental output of DELLA-mediated GA repression. Supporting Evidence: PMID:11606552 Phenotypes rescued include abaxial trichome initiation, rosette radius, flowering time, stem elongation, and apical dominance.
GO:2000033 regulation of seed dormancy process	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Regulation of seed dormancy inherited from the GAI/RGA clade node PTN004849723. Reason: Matches this gene's other row for the term, kept non-core (redundant DELLA control of dormancy and germination). Supporting Evidence: PMID:24989044 blocking GA signaling in the epidermis represses the expression of L1 box-containing genes and negatively affects seed germination.

Gene Description

Proposed New Ontology Terms

gibberellin receptor binding

Existing Annotations Review

Core Functions

Nuclear repressor of the gibberellin (GA) signaling pathway; RGA acts immediately downstream of the GID1 GA receptor as one of the major DELLA growth repressors, maintaining the repressed state of GA responses until GA triggers its degradation.

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

Falcon

📚 Additional Documentation

Notes

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