GID1C (GA INSENSITIVE DWARF1C; locus At5g27320) is one of three soluble gibberellin (GA) receptors in Arabidopsis thaliana, together with GID1A and GID1B. It has the alpha/beta-hydrolase fold of the hormone-sensitive lipase (GDXG) family but no hydrolase activity; the fold forms a pocket that binds bioactive GAs (highest affinity for GA4), after which an N-terminal lid closes over the hormone and creates a surface that binds the N-terminal DELLA domain of the DELLA growth repressors (GAI, RGA, RGL1, RGL2, RGL3). The GA-GID1-DELLA complex is recognized by the SCF(SLY1) E3 ubiquitin ligase, leading to DELLA polyubiquitination and proteasomal degradation; GA-GID1 binding can also inhibit DELLA activity without proteolysis. GID1C groups with GID1A in the eudicot GID1ac clade and acts mainly with GID1A: the gid1a gid1c double mutant is dwarfed, germinates poorly and has reduced pod elongation, and GID1C is expressed in stems, fruit valves and style. GID1C binds the floral DELLA RGL2 with much lower affinity than GID1A or GID1B, which helps explain why it cannot replace them in stamen development. Loss of all three GID1 receptors abolishes GA responses.
Definition: Binding to a gibberellin and, as a result, undergoing a conformational change that promotes gibberellin-dependent binding of DELLA repressor proteins, thereby transducing the gibberellin signal.
Justification: GID1 proteins, including GID1C, are bona fide soluble GA receptors but GO has no gibberellin receptor activity term (checked in GO via OAK/OLS); gibberellin binding (GO:0010331) captures ligand binding but not signal transduction. Same proposal as in the GID1A review.
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:16709201 Identification and characterization of Arabidopsis gibberell... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGL2 (Q8GXW1). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. 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 |
| GO:0005515 protein binding | IPI PMID:16709201 Identification and characterization of Arabidopsis gibberell... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGL1 (Q9C8Y3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. 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 |
| GO:0005515 protein binding | IPI PMID:16709201 Identification and characterization of Arabidopsis gibberell... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. 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 |
| GO:0005515 protein binding | IPI PMID:16709201 Identification and characterization of Arabidopsis gibberell... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. 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 |
| GO:0005515 protein binding | IPI PMID:17194763 Genetic characterization and functional analysis of the GID1... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:17194763 GA enhances the interaction between GID1 and DELLA proteins |
| GO:0005515 protein binding | IPI PMID:17194763 Genetic characterization and functional analysis of the GID1... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:17194763 GA enhances the interaction between GID1 and DELLA proteins |
| GO:0005515 protein binding | IPI PMID:18216856 Coordinated regulation of Arabidopsis thaliana development b... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGL1 (Q9C8Y3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005515 protein binding | IPI PMID:18216856 Coordinated regulation of Arabidopsis thaliana development b... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGL3 (Q9LF53). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005515 protein binding | IPI PMID:18216856 Coordinated regulation of Arabidopsis thaliana development b... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005515 protein binding | IPI PMID:18216856 Coordinated regulation of Arabidopsis thaliana development b... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005515 protein binding | IPI PMID:18827182 Proteolysis-independent downregulation of DELLA repression i... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18827182 Since DELLA shows increasing interaction with GID1 with increasing GA levels |
| GO:0005515 protein binding | IPI PMID:19500306 Differential expression and affinities of Arabidopsis gibber... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGL2 (Q8GXW1). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:19500306 We then evaluated the affinity of the AtGID1-DELLA interaction by a competitive yeast three-hybrid system and also by QCM apparatus |
| GO:0005515 protein binding | IPI PMID:19500306 Differential expression and affinities of Arabidopsis gibber... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGL1 (Q9C8Y3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:19500306 We then evaluated the affinity of the AtGID1-DELLA interaction by a competitive yeast three-hybrid system and also by QCM apparatus |
| GO:0005515 protein binding | IPI PMID:19500306 Differential expression and affinities of Arabidopsis gibber... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:19500306 We then evaluated the affinity of the AtGID1-DELLA interaction by a competitive yeast three-hybrid system and also by QCM apparatus |
| GO:0005515 protein binding | IPI PMID:19500306 Differential expression and affinities of Arabidopsis gibber... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:19500306 We then evaluated the affinity of the AtGID1-DELLA interaction by a competitive yeast three-hybrid system and also by QCM apparatus |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: High-throughput yeast two-hybrid interaction of GID1C with a non-DELLA protein (O64722) from the phytohormone interactome map. Reason: Generic protein binding from a large-scale screen, with no follow-up establishing a function for this partner in GA perception. Uninformative; removal does not mean the interaction is false. 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:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGL2 (Q8GXW1). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. 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:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGL1 (Q9C8Y3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. 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:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGL3 (Q9LF53). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. 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:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. 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:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: GA-dependent interaction of GID1C with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. 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:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: High-throughput yeast two-hybrid interaction of GID1C with a non-DELLA protein (Q9SYP2) from the phytohormone interactome map. Reason: Generic protein binding from a large-scale screen, with no follow-up establishing a function for this partner in GA perception. Uninformative; removal does not mean the interaction is false. 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:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: Nuclear localization of GID1C (IBA), consistent with GID1 being a soluble nuclear receptor that engages nuclear DELLA repressors. Reason: GID1 receptors act in the nucleus where DELLA proteins reside; consistent with UniProt (by similarity), the GID1 clade IBA and GA-GID1-DELLA interaction in the nucleus. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: Nuclear localization of GID1C (IEA), consistent with GID1 being a soluble nuclear receptor that engages nuclear DELLA repressors. Reason: GID1 receptors act in the nucleus where DELLA proteins reside; consistent with UniProt (by similarity), the GID1 clade IBA and GA-GID1-DELLA interaction in the nucleus. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005634 nucleus | ISM GO_REF:0000122 | ACCEPT | Summary: Nuclear localization of GID1C (ISM), consistent with GID1 being a soluble nuclear receptor that engages nuclear DELLA repressors. Reason: GID1 receptors act in the nucleus where DELLA proteins reside; consistent with UniProt (by similarity), the GID1 clade IBA and GA-GID1-DELLA interaction in the nucleus. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Cytoplasmic pool inferred from the GID1 clade (experimental nucleocytoplasmic localization of GID1A). Reason: GID1 proteins are soluble receptors distributed between nucleus and cytoplasm (GID1A-GFP is nucleocytoplasmic), so the clade IBA is plausible and not contradicted for this paralog. However, the nuclear pool is the functionally relevant one, where the GA-GID1 complex engages nuclear DELLA repressors; no cytoplasm-specific role is known, so the location is kept as non-core (consistent with the SLY1 review). Supporting Evidence: file:ARATH/GID1A/GID1A-deep-research-falcon.md GFP-tagged Arabidopsis GID1A localized to both nucleus and cytoplasm, and this distribution was not altered by GA or paclobutrazol treatment. |
| GO:0009739 response to gibberellin | IGI PMID:18827182 Proteolysis-independent downregulation of DELLA repression i... | ACCEPT | Summary: Genetic evidence (in combination with the GA1/ga1-3 locus and sly1 backgrounds): GID1C overexpression relieves DELLA repression in a GA-dependent way. Reason: Consistent with the receptor role in GA responses, including the proteolysis-independent inhibition of DELLA by GA-GID1. Supporting Evidence: PMID:18827182 GID1 overexpression rescued the sly1 dwarf and infertility phenotypes without decreasing the accumulation of the DELLA protein PMID:18827182 GA-bound GID1 can block DELLA repressor activity by direct protein-protein interaction with the DELLA domain |
| GO:0009739 response to gibberellin | IGI PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | ACCEPT | Summary: Genetic interaction with GID1A (Q9MAA7): the gid1a gid1c double mutant pistils show reduced GA responses. Reason: Supports the involvement of GID1C, redundantly with GID1A, in GA responses of the pistil/fruit. Supporting Evidence: PMID:24961590 the gid1a gid1c pistils displayed little or no GA response PMID:24961590 our data suggest that the three GID1 GA receptors act partially redundantly in pistil development |
| GO:0009739 response to gibberellin | IGI NOT PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | REMOVE | Summary: NOT involved in response to gibberellin (IGI, with Q9LYC1), based on the absence of a pistil/fruit phenotype in a gid1c single or double mutant in which another GID1 paralog remains. Reason: The negation is contradicted by direct evidence that GID1C is a functional GA receptor: recombinant GID1C binds GA and interacts with DELLAs only in the presence of GA, and it rescues the rice gid1 mutant. Lack of a phenotype in a mutant retaining a redundant paralog (the paper itself reports compensatory GID1A up-regulation) reflects genetic redundancy, not absence of involvement in GA responses. Supporting Evidence: PMID:16709201 These results demonstrate that all three AtGID1s functioned as GA receptors in Arabidopsis PMID:24961590 Elimination of two out of the three GA receptors in each double mutant combination may cause up-regulated expression of the remaining GID1 gene, which may alleviate reduced GA-response phenotype |
| GO:0009739 response to gibberellin | IMP NOT PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | REMOVE | Summary: NOT involved in response to gibberellin (IMP), based on the absence of a pistil/fruit phenotype in a gid1c single or double mutant in which another GID1 paralog remains. Reason: The negation is contradicted by direct evidence that GID1C is a functional GA receptor: recombinant GID1C binds GA and interacts with DELLAs only in the presence of GA, and it rescues the rice gid1 mutant. Lack of a phenotype in a mutant retaining a redundant paralog (the paper itself reports compensatory GID1A up-regulation) reflects genetic redundancy, not absence of involvement in GA responses. Supporting Evidence: PMID:16709201 These results demonstrate that all three AtGID1s functioned as GA receptors in Arabidopsis PMID:24961590 Elimination of two out of the three GA receptors in each double mutant combination may cause up-regulated expression of the remaining GID1 gene, which may alleviate reduced GA-response phenotype |
| GO:0010331 gibberellin binding | IBA GO_REF:0000033 | ACCEPT | Summary: GID1C binds bioactive gibberellins (highest affinity for GA4); IBA inferred from the GID1 clade (PTN000546395) seeded by Arabidopsis GID1A and rice GID1, and directly supported by in vitro GA-binding assays on recombinant GID1C. Reason: Core molecular function of a GA receptor. GID1C lies within the GID1 receptor clade, and its own GA-binding activity was demonstrated biochemically. Supporting Evidence: PMID:16709201 The GA-binding activities of the three recombinant proteins were confirmed by an in vitro assay PMID:16709201 These results demonstrate that all three AtGID1s functioned as GA receptors in Arabidopsis |
| GO:0010476 gibberellin mediated signaling pathway | IGI PMID:17521411 Multiple loss-of-function of Arabidopsis gibberellin recepto... | ACCEPT | Summary: The gid1a gid1b gid1c triple mutant completely loses GA responsiveness, placing all three GID1 receptors in the GA-mediated signaling pathway. Reason: Core process: GID1C is one of the three redundant GA receptors that initiate GA signaling. Supporting Evidence: PMID:17521411 the triple knockout seedlings completely lost their ability to respond to exogenously applied GA PMID:17194763 GID1a, GID1b, and GID1c function as positive regulators of the GA-signaling cascade in Arabidopsis |
| GO:0010629 negative regulation of gene expression | IGI PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | MARK AS OVER ANNOTATED | Summary: Genetic interaction annotation from PMID:24961590: in a double mutant lacking GID1C and its paralog (Q9LYC1), expression of the remaining GID1A receptor gene was enhanced. Reason: The observation reflects indirect GA/DELLA homeostatic feedback on GID1A transcription when receptor capacity is reduced, not a gene-expression regulatory activity of the receptor itself. The broad term "negative regulation of gene expression" overstates the evidence. Supporting Evidence: PMID:24961590 The up-regulation of GID1A in gid1b gid1c may be consequence of this feedback mechanism |
| GO:0016787 hydrolase activity | IBA GO_REF:0000033 | REMOVE | Summary: Hydrolase activity propagated by IBA from a deep PAINT node (PTN009058710) seeded by catalytically active carboxylesterases/arylacetamide deacetylases that share the alpha/beta-hydrolase (HSL/GDXG lipolytic enzyme) fold. Reason: GID1 receptors retain the hormone-sensitive-lipase fold but are not hydrolases; the fold has been repurposed into a GA-binding pocket. The GID1 clade diverged from the catalytic ancestral function, so the deep-node IBA and the fold-based IEA are over-propagated to a non-catalytic receptor (pseudoenzyme over-annotation). Propagation Review Root cause: PROPAGATION BAD Failure modes: PSEUDO OR SUBACTIVITY LOSS FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN009058710 · PTN009058710 SUPPORTS SOURCE BUT NOT TARGET Deep PTHR23024 node seeded by catalytically active carboxylesterases/arylacetamide deacetylases (e.g. AT1G49660, AT5G23530, human/mouse AADAC-like, bacterial esterases). The GID1 receptor subclade nested within it has lost hydrolase activity and was repurposed for GA binding; the IBD should carry a NOT/loss at the GID1 clade node. Supporting Evidence: PMID:24961590 GID1 was first described in rice as a nuclear localized protein similar to hormone-sensitive lipase family without hydrolase activity |
| GO:0016787 hydrolase activity | IEA GO_REF:0000002 | REMOVE | Summary: Hydrolase activity assigned by InterPro2GO mapping (IEA) from the alpha/beta-hydrolase (HSL/GDXG lipolytic enzyme) fold signatures IPR002168 and IPR013094. Reason: GID1 receptors retain the hormone-sensitive-lipase fold but are not hydrolases; the fold has been repurposed into a GA-binding pocket. The GID1 clade diverged from the catalytic ancestral function, so the fold-based InterPro mapping over-propagates hydrolase activity to a non-catalytic receptor (pseudoenzyme over-annotation). Supporting Evidence: PMID:24961590 GID1 was first described in rice as a nuclear localized protein similar to hormone-sensitive lipase family without hydrolase activity |
| GO:0048530 fruit morphogenesis | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA-predicted role in fruit morphogenesis, a downstream developmental output of GA signaling. Reason: GA perception by the GID1 receptors (partially redundantly, with GID1A predominant) controls fruit growth; GID1C contributes to pod elongation in valves. Pleiotropic downstream output, not the core function. Supporting Evidence: PMID:24961590 We show that GID1A plays a major role during fruit-set, whereas GID1B and GID1C have partially redundant function with GID1A in seed development and pod elongation, respectively |
| GO:0048530 fruit morphogenesis | IGI PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | KEEP AS NON CORE | Summary: Genetic interaction with GID1A (Q9MAA7): gid1a gid1c double mutants show stronger fruit defects than gid1a alone. Reason: Experimentally supported but a downstream developmental output of GA perception, revealed only in combination with gid1a because of receptor redundancy. Supporting Evidence: PMID:24961590 In contrast, gid1a gid1c showed a significant decrease in the slope, which suggested that this mutant has defects in pod elongation even in the presence of a significant number of seeds, possibly due to a reduced sensitivity to GAs |
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Download this section (compressed HTML)Q: What structural features of GID1C reduce its affinity for RGL2 relative to GID1A and GID1B, and does this DELLA preference shape tissue-specific GA responses?
Q: Do GID1A and GID1C have any non-redundant roles in stem elongation, or does GID1C act only as a dosage contributor?
Experiment: Measure GID1C affinity for each of the five DELLA proteins at physiological GA4 concentrations (e.g. quantitative yeast three-hybrid or purified-protein binding) to define its DELLA preference profile.
Experiment: Express GID1C from the GID1B promoter in gid1a gid1b to test whether its low RGL2 affinity prevents rescue of stamen elongation.
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