statC

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: STATc is a transcription factor that accumulates in the nucleus upon activation by DIF-1 or stress. Phylogenetic inference of nuclear localization is correct and independently supported by direct experimental evidence. Reason: Nuclear localization of activated STATc is directly demonstrated and is central to its transcription factor function. Supporting Evidence: PMID:12506009 Dd-STATc becomes tyrosine phosphorylated, dimerises and accumulates in the nuclei of Dictyostelium cells exposed to DIF
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: In unstimulated cells STATc is a latent cytoplasmic factor that translocates to the nucleus only upon activation. Cytoplasmic localization is correct. Reason: STATc shuttles between cytoplasm and nucleus and is predominantly cytoplasmic in the resting state, consistent with the STAT activation paradigm. Supporting Evidence: PMID:18305004 STATc becomes tyrosine phosphorylated and accumulates in the nucleus when Dictyostelium cells are exposed to the prestalk cell inducer Differentiation inducing factor 1 (DIF-1), or are subjected to hyper-osmotic stress
GO:0006357 regulation of transcription by RNA polymerase II	IBA GO_REF:0000033	ACCEPT	Summary: STATc is a sequence-specific transcription factor that both represses and activates specific genes; regulation of RNA polymerase II transcription is its core biological role. Reason: Directly supported by experimental evidence that STATc regulates ecmA (repression) and stress-response genes (activation). Supporting Evidence: PMID:11336701 Dd-STATc also functions as a repressor, which directs graded expression of the ecmA gene in different prestalk cell populations
GO:0006952 defense response	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Retain the ancestral defense-response inference as non-core, without treating oxidative-stress signaling as direct pathogen-defense evidence. Reason: PTHR11801 places GO:0006952 at PTN000927860. The live definition concerns restriction of damage after a foreign body or injury and does not require metazoan cytokines, interferons or JAK. PMID:17673666 and PMID:26927887 establish TirA/NADPH-oxidase defense mechanisms, but their positive roles do not exclude STATc-dependent transcriptional regulation. The focused report explicitly states that STATc bacterial-clearance involvement is untested rather than experimentally excluded. Its missing-target-assay and other-effector arguments do not establish loss from the ancestral node. Retain the curated inheritance separately from the directly demonstrated stress-response core. Supporting Evidence: file:interpro/panther/PTHR11801/PTHR11801-paint.tsv PTHR11801 PTN000927860 GO:0006952 P IBD false FB:FBgn0016917\|MGI:MGI:103038\|MGI:MGI:103039\|MGI:MGI:103063\|RGD:3772\|RGD:3774\|UniProtKB:P42224\|UniProtKB:P52630\|WB:WBGene00010251\|ZFIN:ZDB-GENE-030131-9359 taxon: 20260828
GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding	IBA GO_REF:0000033	ACCEPT	Summary: STATs are sequence-specific DNA-binding transcription factors; STATc contains a STAT DNA-binding region and functions as a transcriptional regulator, so sequence-specific DNA binding is a reasonable core molecular function. Reason: Consistent with the STAT family DNA-binding domain and with STATc's documented sequence-specific transcriptional regulation of target genes. Supporting Evidence: PMID:11336701 Dd-STATc also functions as a repressor, which directs graded expression of the ecmA gene in different prestalk cell populations
GO:0042127 regulation of cell population proliferation	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Retain the inherited proliferation-regulation process as non-core; the source STATb growth phenotype is genuine but is not a STATc experiment. Reason: The IBD at PTN000927860 in PTHR11801 includes dictyBase:DDB_G0268638 (STATb) and animal STAT experimental descendants. PMID:14701681 demonstrates a subtle competitive-growth role for STATb despite its noncanonical activation. A paralog contributing descendant evidence does not itself invalidate an ancestral function inference. The focused report states that STATc was not tested and found negative for proliferation; it lacks a discriminating loss experiment. Broad proliferation regulation also does not require a JAK/cytokine pathway. Retain this phylogenetic assertion as non-core without converting developmental timing or stress fitness into direct proliferation evidence. Supporting Evidence: PMID:14701681 It has a subtle role in growth, so that Dd-STATb-null cells are gradually lost from the population when they are co-cultured with parental cells file:DICDI/statC/statC-hypotheses/proliferation-and-defense-response/openscientist.md The gap is not that statC was tested and found negative for proliferation
GO:0007259 cell surface receptor signaling pathway via JAK-STAT	IBA GO_REF:0000033	MODIFY	Summary: STATc participates in STAT signaling, but Dictyostelium has no JAK orthologs; STATc is instead phosphorylated by tyrosine-kinase-like enzymes (Pyk2/Pyk3). The JAK-STAT-specific term is therefore inappropriate and should be generalized to STAT signaling. Reason: There are no Dictyostelium homologs of the metazoan JAK family; STATc activation is catalyzed by TKL enzymes. The parent term GO:0097696 (cell surface receptor signaling pathway via STAT), which does not require a JAK, more accurately captures STATc signaling. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: LINEAGE OR TAXON MISMATCH Sources checked: PANTHER:PTN000927860 · PTN000927860 SUPPORTS SOURCE BUT NOT TARGET The cached PTHR11801 PAINT table places the JAK-dependent pathway at this ancestor. The GO definition explicitly requires receptor-associated JAK activation, whereas Dictyostelium STAT activation uses non-JAK kinases. The mechanistic mismatch concerns this pathway term, not a general exclusion of amoebal STAT signaling. Proposed replacements: cell surface receptor signaling pathway via STAT Supporting Evidence: PMID:22699506 There are no orthologs of the animal tyrosine kinases, but there are very many tyrosine kinase-like kinases (TKLs)
GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific	IBA GO_REF:0000033	ACCEPT	Summary: STATc is a bona fide DNA-binding transcription factor that regulates RNA polymerase II transcription of developmental and stress-response genes. This is a core molecular function. Reason: Well supported by experimental evidence that STATc acts as a sequence-specific transcriptional repressor and activator of target genes. Supporting Evidence: PMID:12771188 These data show that Dd-STATc functions as a transcriptional activator in a stress-response pathway
GO:0003677 DNA binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: Generic DNA binding is correct but uninformative given the more specific transcription-factor DNA-binding annotations already present. Reason: DNA binding is subsumed by the more specific molecular functions (DNA-binding transcription factor activity, RNA polymerase II-specific); retained as a correct but general parent term.
GO:0003700 DNA-binding transcription factor activity	IEA GO_REF:0000002	ACCEPT	Summary: STATc is a DNA-binding transcription factor. This InterPro2GO annotation is correct; the RNA polymerase II-specific child term is more precise. Reason: Correct general molecular function for a STAT transcription factor, consistent with the experimental evidence for transcriptional regulation. Supporting Evidence: PMID:11336701 Dd-STATc also functions as a repressor, which directs graded expression of the ecmA gene in different prestalk cell populations
GO:0005634 nucleus	IEA GO_REF:0000120	ACCEPT	Summary: Nuclear localization is correct and directly demonstrated. Reason: Consistent with direct experimental evidence for nuclear accumulation of activated STATc. Supporting Evidence: PMID:12506009 Dd-STATc becomes tyrosine phosphorylated, dimerises and accumulates in the nuclei of Dictyostelium cells exposed to DIF
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: Cytoplasmic localization is correct; STATc is a latent cytoplasmic factor in the resting state. Reason: Consistent with UniProt subcellular location and with the STAT cytoplasm-to-nucleus shuttling mechanism. Supporting Evidence: PMID:18305004 STATc becomes tyrosine phosphorylated and accumulates in the nucleus when Dictyostelium cells are exposed to the prestalk cell inducer Differentiation inducing factor 1 (DIF-1), or are subjected to hyper-osmotic stress
GO:0006355 regulation of DNA-templated transcription	IEA GO_REF:0000002	ACCEPT	Summary: Correct general biological process for a transcription factor; subsumed by the more specific regulation of transcription by RNA polymerase II. Reason: STATc regulates transcription of developmental and stress-response genes; the general term is correct. Supporting Evidence: PMID:12771188 These data show that Dd-STATc functions as a transcriptional activator in a stress-response pathway
GO:0007165 signal transduction	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: STATc is an effector of DIF-1 and stress signaling. Signal transduction is correct but very general. Reason: A high-level parent process that is correct but uninformative relative to the more specific STAT signaling and stress-response annotations.
GO:0042802 identical protein binding	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Activated STATc homodimerizes through reciprocal SH2-phosphotyrosine interactions. Identical protein binding is correct and part of the activation mechanism, though not the core molecular function. Reason: STATc dimerizes upon tyrosine phosphorylation; homodimerization is a mechanistic feature rather than the primary evolved function. Supporting Evidence: PMID:11336701 Dd-STATc is tyrosine phosphorylated, dimerizes, and translocates to the nucleus when cells are exposed to DIF
GO:0045892 negative regulation of DNA-templated transcription	IEA GO_REF:0000117	ACCEPT	Summary: STATc acts as a transcriptional repressor, restricting graded ecmA expression in prestalk cells. Negative regulation of transcription is well supported. Reason: Independently supported by experimental evidence that STATc represses ecmA prestalk gene expression. Supporting Evidence: PMID:11336701 Dd-STATc also functions as a repressor, which directs graded expression of the ecmA gene in different prestalk cell populations
GO:0006970 response to osmotic stress	IMP PMID:22944283 The calcineurin dependent transcription factor TacA is invol...	ACCEPT	Summary: STATc is a well-established mediator of the transcriptional response to hyperosmotic (osmotic) stress in Dictyostelium. Reason: STATc's role in the osmotic stress response is documented across multiple studies; the TacA study explicitly contrasts its own pathway with the well-known STATc stress response. Supporting Evidence: PMID:22944283 TacA is involved in the stress response of D. discoideum during development in a separate pathway to the well-known stress response in Dictyostelium via STATc
GO:0043157 response to cation stress	IMP PMID:22944283 The calcineurin dependent transcription factor TacA is invol...	UNDECIDED	Summary: The cation-stress annotation is not resolved by the accessible TacA study abstract, which distinguishes TacA signaling from the known STATc stress pathway. Reason: STATc is an established osmotic-stress factor, but that broad role does not verify this particular cation-stress experiment. The source cache is abstract-only, so retain the curator's experimental assertion as unresolved pending full-text evidence rather than treating an unspecified stress association as sufficient.
GO:0010628 positive regulation of gene expression	IMP PMID:24587195 Identification of the protein kinases Pyk3 and Phg2 as regul...	ACCEPT	Summary: STATc positively regulates expression of its target genes, including a positive feedback loop that upregulates STATc and STATc-dependent genes during the stress response. Reason: Directly supported by mutant analyses showing STATc-dependent upregulation of stress-response genes. Supporting Evidence: PMID:24587195 The STATc stress signalling pathway feeds back on itself by upregulating the expression of STATc and STATc-regulated genes
GO:0080135 regulation of cellular response to stress	IMP PMID:24267687 The arrestin-domain containing protein AdcA is a response el...	ACCEPT	Summary: STATc-dependent transcription contributes to the cellular stress response, including the timely dephosphorylation of the stress element AdcA. Reason: Supported by evidence that STATc-dependent transcriptional activity is required for proper timing of the AdcA stress response. Supporting Evidence: PMID:24267687 STATc-dependent transcriptional activity is involved for the timely dephosphorylation of AdcA in
GO:1990782 protein tyrosine kinase binding	IPI PMID:22699506 Identification of the kinase that activates a nonmetazoan ST...	ACCEPT	Summary: STATc binds the tyrosine-kinase-like enzyme Pyk2 through its SH2 domain; the STATc-Pyk2 complex is formed constitutively and Pyk2 phosphorylates STATc on Tyr922. This is an informative molecular function central to STATc activation. Reason: Directly demonstrated physical interaction between STATc and its activating tyrosine kinase Pyk2 in vitro and in vivo. Supporting Evidence: PMID:22699506 the STATc-Pyk2 complex is formed constitutively by an interaction between the STATc SH2 domain and phosphotyrosine residues on Pyk2 PMID:22699506 Pyk2 phosphorylates STATc on Tyr922 in vitro and complexes with STATc both in vitro and in vivo
GO:0005634 nucleus	IDA PMID:11336701 Tyrosine phosphorylation-independent nuclear translocation o...	ACCEPT	Summary: Direct evidence that activated STATc translocates to and acts in the nucleus. Core localization. Reason: STATc translocates to the nucleus upon DIF-induced tyrosine phosphorylation and dimerization, where it exerts its transcription factor function. Supporting Evidence: PMID:11336701 Dd-STATc is tyrosine phosphorylated, dimerizes, and translocates to the nucleus when cells are exposed to DIF
GO:0005634 nucleus	IDA PMID:12506009 The Dictyostelium prestalk cell inducer DIF regulates nuclea...	ACCEPT	Summary: Direct evidence for nuclear accumulation of STATc; nuclear residence is controlled at the level of CRM1-dependent export. Reason: STATc accumulates in the nucleus of DIF-exposed cells, with DIF inhibiting its nuclear export. Supporting Evidence: PMID:12506009 Dd-STATc becomes tyrosine phosphorylated, dimerises and accumulates in the nuclei of Dictyostelium cells exposed to DIF
GO:0045892 negative regulation of DNA-templated transcription	IMP PMID:11336701 Tyrosine phosphorylation-independent nuclear translocation o...	ACCEPT	Summary: STATc functions as a repressor that restricts graded ecmA expression to specific prestalk cell populations. Core function. Reason: Mutant analysis demonstrates STATc acts as a transcriptional repressor of the ecmA prestalk marker. Supporting Evidence: PMID:11336701 Dd-STATc also functions as a repressor, which directs graded expression of the ecmA gene in different prestalk cell populations
GO:0005829 cytosol	IDA PMID:11336701 Tyrosine phosphorylation-independent nuclear translocation o...	ACCEPT	Summary: STATc is present in the cytosol in the resting (latent) state before activation-induced nuclear translocation. Reason: Consistent with the latent cytoplasmic nature of STATc prior to DIF/stress-induced nuclear accumulation. Supporting Evidence: PMID:11336701 Dd-STATc is tyrosine phosphorylated, dimerizes, and translocates to the nucleus when cells are exposed to DIF
GO:0005634 nucleus	IMP PMID:12771188 A STAT-regulated, stress-induced signalling pathway in Dicty...	ACCEPT	Summary: STATc localizes to the nucleus; nuclear accumulation is a hallmark of its activation by stress and DIF. Reason: Nuclear localization of activated STATc is consistent across multiple studies. Supporting Evidence: PMID:12771188 hyperosmotic stress, heat shock and oxidative stress also activate Dd-STATc
GO:0031288 sorocarp morphogenesis	IMP PMID:11336701 Tyrosine phosphorylation-independent nuclear translocation o...	KEEP AS NON CORE	Summary: STATc influences developmental timing and prestalk cell-type patterning during fruiting body (sorocarp) formation. This is a genuine but downstream developmental role rather than the core molecular function. Reason: statC null cells show altered developmental timing and prestalk patterning, and colonies form aberrant fruiting bodies; this developmental phenotype is a consequence of STATc's transcription factor activity. Supporting Evidence: PMID:11336701 which regulates the speed of early development and the timing of terminal differentiation
GO:0005515 protein binding	IPI PMID:12220630 OSBPa, a predicted oxysterol binding protein of Dictyosteliu...	UNDECIDED	Summary: The generic binding annotation is attributed to the OSBPa study, whose cached abstract does not resolve the STATc interaction. Reason: The abstract establishes OSBPa biology but does not identify the STATc binding assay or interaction partner. Without accessible supporting full text, neither a specific replacement nor a dismissal of the experimental observation is justified. Use UNDECIDED rather than retaining an uninterpretable generic annotation.
GO:0005515 protein binding	IPI PMID:18305004 Evidence that DIF-1 and hyper-osmotic stress activate a Dict...	MODIFY	Summary: This physical interaction is with the protein tyrosine phosphatase PTP3, which directly binds and dephosphorylates STATc. The bare protein binding term should be replaced by the more informative protein phosphatase binding. Reason: The interacting partner is identified as the phosphatase PTP3, so a more specific and informative molecular function is warranted instead of generic protein binding. Proposed replacements: protein phosphatase binding Supporting Evidence: PMID:18305004 the protein tyrosine phosphatase PTP3 interacts directly with STATc
GO:0005515 protein binding	IPI PMID:25143406 Two Dictyostelium tyrosine kinase-like kinases function in p...	MODIFY	Summary: This interaction is with the tyrosine-kinase-like enzymes Pyk2/Pyk3, which bind the STATc SH2 domain and phosphorylate it. The bare protein binding term should be replaced by protein tyrosine kinase binding. Reason: The interacting partners are the activating TKL kinases Pyk2/Pyk3, so the more informative protein tyrosine kinase binding term is warranted instead of generic protein binding. Proposed replacements: protein tyrosine kinase binding Supporting Evidence: PMID:25143406 The site(s) that are generated bind the SH2 domain of STATc, and then STATc becomes the target of further kinase action
GO:0042802 identical protein binding	IPI PMID:11336701 Tyrosine phosphorylation-independent nuclear translocation o...	KEEP AS NON CORE	Summary: Activated STATc homodimerizes; identical protein binding is directly supported and is part of the activation mechanism. Reason: STATc dimerizes upon tyrosine phosphorylation; homodimerization is a mechanistic step rather than the core evolved function. Supporting Evidence: PMID:11336701 Dd-STATc is tyrosine phosphorylated, dimerizes, and translocates to the nucleus when cells are exposed to DIF
GO:1903013 response to differentiation-inducing factor 1	HDA PMID:25518940 The Dictyostelium prestalk inducer differentiation-inducing ...	ACCEPT	Summary: STATc is rapidly tyrosine-phosphorylated in response to DIF-1, as confirmed by global phosphoproteomics. Response to DIF-1 is a defining feature of STATc. Reason: DIF-1-triggered activation of STATc is directly observed and is central to its role in prestalk cell differentiation. Supporting Evidence: PMID:25518940 STATc is rapidly phosphorylated after exposure to DIF-1
GO:0030587 sorocarp development	IEP PMID:25887420 Leaps and lulls in the developmental transcriptome of Dictyo...	KEEP AS NON CORE	Summary: STATc (dstC) is developmentally expressed with a graded trajectory during multicellular development. This expression-based annotation supports a developmental role but is non-core relative to the molecular function. Reason: An IEP (expression-pattern) inference; STATc's developmental involvement is genuine but is a downstream consequence of its transcription factor activity rather than a core function. Supporting Evidence: PMID:25887420 dstC continued on a more graded trajectory
GO:0006972 hyperosmotic response	IEP PMID:17517120 STATc is a key regulator of the transcriptional response to ...	ACCEPT	Summary: STATc is a key regulator of the transcriptional response to hyperosmotic shock, with roughly 20% of osmotically regulated genes dependent on STATc. Core stress-response role. Reason: Genome-wide analysis shows STATc controls a substantial subset of the hyperosmotic stress transcriptional program. Supporting Evidence: PMID:17517120 Approximately 20% of the differentially regulated genes were dependent on the presence of STATc
GO:0006972 hyperosmotic response	IDA PMID:12771188 A STAT-regulated, stress-induced signalling pathway in Dicty...	ACCEPT	Summary: STATc is directly activated by hyperosmotic stress and functions as a transcriptional activator in the stress-response pathway. Core role. Reason: Hyperosmotic stress directly activates STATc, which then drives stress-response gene expression (e.g. gapA, rtoA). Supporting Evidence: PMID:12771188 hyperosmotic stress, heat shock and oxidative stress also activate Dd-STATc
GO:0006979 response to oxidative stress	IDA PMID:12771188 A STAT-regulated, stress-induced signalling pathway in Dicty...	KEEP AS NON CORE	Summary: STATc is activated by oxidative stress, one of several stress stimuli that trigger its tyrosine phosphorylation and nuclear accumulation. Reason: Oxidative stress is one of multiple stress inputs that activate STATc; retained as a genuine but non-core stress response alongside the dominant osmotic response. Supporting Evidence: PMID:12771188 hyperosmotic stress, heat shock and oxidative stress also activate Dd-STATc
GO:0009408 response to heat	IDA PMID:12771188 A STAT-regulated, stress-induced signalling pathway in Dicty...	KEEP AS NON CORE	Summary: STATc is activated by heat shock, another of the stress stimuli that trigger its activation. Reason: Heat shock is one of several stresses that activate STATc; a genuine but non-core stress response relative to the dominant osmotic response. Supporting Evidence: PMID:12771188 hyperosmotic stress, heat shock and oxidative stress also activate Dd-STATc
GO:0047484 regulation of response to osmotic stress	IMP PMID:12771188 A STAT-regulated, stress-induced signalling pathway in Dicty...	ACCEPT	Summary: STATc regulates the transcriptional output of the osmotic stress response, controlling stress-induced genes such as gapA and rtoA. Reason: Mutant analysis shows osmotic-stress induction of STATc target genes is entirely dependent on STATc, placing it as a regulator of the osmotic stress response. Supporting Evidence: PMID:12771188 Osmotic stress induction of gapA and rtoA is entirely dependent on Dd-STATc

Gene Description

Existing Annotations Review

Core Functions

References

Deep Research

OpenScientist

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Notes

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