WIN1 (At1g80600), also known as TUMOR PRONE5 (TUP5), is a pyridoxal-phosphate-dependent acetylornithine aminotransferase of Arabidopsis arginine biosynthesis. It converts N-acetylglutamate semialdehyde and glutamate to N-acetylornithine and 2-oxoglutarate. Functional GFP experiments demonstrate chloroplast localization. Arginine deficiency in tup5 mutants causes a blue-light-dependent loss of root meristem maintenance, while null alleles impair gametophytes and embryos. WIN1 also interacts with the bacterial effector HopW1-1, and its overexpression modifies pathogen responses and salicylic-acid accumulation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003992 N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity | IBA GO_REF:0000033 | ACCEPT | Summary: The enzyme-specific activity is supported independently by curated reaction chemistry and target-specific experiments. Reason: The enzyme-specific activity is supported independently by curated reaction chemistry and target-specific experiments. Native mutant metabolite/rescue analysis and complementation of yeast ACOAT deficiency establish the biosynthetic role (PMID:23321422). The complementation evidence is not described as a purified-enzyme kinetic assay. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; PMID:23321422 a yeast (Saccharomyces cerevisiae) ACOAT mutant was complemented by TUP5. |
| GO:0003992 N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The enzyme-specific activity is supported independently by curated reaction chemistry and target-specific experiments. Reason: The enzyme-specific activity is supported independently by curated reaction chemistry and target-specific experiments. Native mutant metabolite/rescue analysis and complementation of yeast ACOAT deficiency establish the biosynthetic role (PMID:23321422). The complementation evidence is not described as a purified-enzyme kinetic assay. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; PMID:23321422 a yeast (Saccharomyces cerevisiae) ACOAT mutant was complemented by TUP5. |
| GO:0003992 N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity | IGI PMID:23321422 The Arabidopsis TUMOR PRONE5 gene encodes an acetylornithine... | ACCEPT | Summary: The enzyme-specific activity is supported independently by curated reaction chemistry and target-specific experiments. Reason: The enzyme-specific activity is supported independently by curated reaction chemistry and target-specific experiments. Native mutant metabolite/rescue analysis and complementation of yeast ACOAT deficiency establish the biosynthetic role (PMID:23321422). The complementation evidence is not described as a purified-enzyme kinetic assay. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; PMID:23321422 a yeast (Saccharomyces cerevisiae) ACOAT mutant was complemented by TUP5. |
| GO:0003992 N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity | IMP PMID:23321422 The Arabidopsis TUMOR PRONE5 gene encodes an acetylornithine... | ACCEPT | Summary: The enzyme-specific activity is supported independently by curated reaction chemistry and target-specific experiments. Reason: The enzyme-specific activity is supported independently by curated reaction chemistry and target-specific experiments. Native mutant metabolite/rescue analysis and complementation of yeast ACOAT deficiency establish the biosynthetic role (PMID:23321422). The complementation evidence is not described as a purified-enzyme kinetic assay. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; PMID:23321422 a yeast (Saccharomyces cerevisiae) ACOAT mutant was complemented by TUP5. |
| GO:0005507 copper ion binding | HDA PMID:20018591 Divalent metal ions in plant mitochondria and their role in ... | MARK AS OVER ANNOTATED | Summary: Retention on a Cu(2+)-charged IMAC column in a mitochondrial metal-binding screen does not establish copper ion binding as a function of this PLP-dependent aminotransferase. Reason: GO:0005507 is defined as "Binding to a copper (Cu) ion", and an MF annotation implies that this binding is part of what the protein does. PMID:20018591 used immobilized-metal affinity chromatography charged with several metals to capture proteins with metal-binding properties, an affinity screen that retains proteins with surface metal-coordinating residues. WIN1/TUP5 is a class-III pyridoxal-phosphate-dependent acetylornithine aminotransferase with no known copper cofactor or copper-dependent step. The over-annotation judgement rests on these two points, the nature of the assay and the enzyme's chemistry, and does not depend on the WIN1-specific capture data, which are not in the cached abstract. Retention on the column is not disputed, so the row is marked as an over-annotation of a screen hit rather than removed. Supporting Evidence: PMID:20018591 Immobilized metal affinity chromatography charged with Cu(2+), Zn(2+), and Co(2+) was used to identify over 100 mitochondrial proteins with metal-binding properties. file:ARATH/WIN1/WIN1-uniprot.txt Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. |
| GO:0005515 protein binding | IPI PMID:18266921 Arabidopsis proteins important for modulating defense respon... | REMOVE | Summary: WIN1 interaction with bacterial HopW1-1 is experimentally supported and retained in the biological summary. Reason: WIN1 interaction with bacterial HopW1-1 is experimentally supported and retained in the biological summary. Bare protein binding lacks a specific functional description and is removed under project policy; this does not mean the interaction is false or justify inventing a specialized binding function. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Interacts with the P.syringae pv. maculicola effector HopW1-1 (via C-terminus). {ECO:0000269|PubMed:18266921}. |
| GO:0005739 mitochondrion | HDA PMID:28887381 Global Analysis of Membrane-associated Protein Oligomerizati... | MARK AS OVER ANNOTATED | Summary: The cited fractionation study classifies WIN1 as a plastid protein and does not assign it to mitochondria; functional GFP localization places WIN1 in chloroplasts. Reason: PMID:28887381 profiled soluble and microsomal fractions of whole leaves, an assay that cannot resolve organelles, and its own supplement labels WIN1 as plastid with no dual-localization flag. A functional TUP5-GFP fusion localizes to chloroplasts (PMID:23321422), and plant ornithine synthesis is plastidic. No targeted assay shows a mitochondrial WIN1 pool, though dual targeting is not formally excluded, so the row is marked as an over-annotation rather than removed. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000250}. file:ARATH/WIN1/WIN1-source-analysis/README.md Subacon localization is plastid, and both True membrane and Dual Localized are empty. PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | MARK AS OVER ANNOTATED | Summary: This keyword-derived mitochondrion row rests on a by-similarity UniProt statement; experimental localization of WIN1 is chloroplastic. Reason: The IEA row is mapped from UniProt subcellular-location SL-0173, which the record supports only by similarity (ECO:0000250), whereas the chloroplast location is experimentally supported (PMID:18431481) and confirmed by a functional TUP5-GFP fusion (PMID:23321422). Plant arginine-pathway enzymes act in plastids, so a mitochondrial assignment transferred by similarity, plausibly from the fungal mitochondrial orthologue, is not supported for this target. Dual targeting is not formally excluded, so the row is marked as an over-annotation rather than removed. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000250}. PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization |
| GO:0006525 arginine metabolic process | IEA GO_REF:0000002 | MODIFY | Summary: The metabolic role is specifically arginine biosynthesis through acetylornithine, already asserted in this review; refine the broad metabolic term to that demonstrated process. Reason: The metabolic role is specifically arginine biosynthesis through acetylornithine, already asserted in this review; refine the broad metabolic term to that demonstrated process. Proposed replacements: L-arginine biosynthetic process Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; PMID:23321422 a yeast (Saccharomyces cerevisiae) ACOAT mutant was complemented by TUP5. |
| GO:0006526 L-arginine biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: The protein directly catalyzes an acetylated-intermediate reaction that produces an arginine/ornithine precursor, so it participates in the biosynthetic process. Reason: The protein directly catalyzes an acetylated-intermediate reaction that produces an arginine/ornithine precursor, so it participates in the biosynthetic process. Target-specific functional evidence supports the enzymatic role rather than reliance on knockout necessity alone. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; PMID:23321422 a yeast (Saccharomyces cerevisiae) ACOAT mutant was complemented by TUP5. file:ARATH/WIN1/WIN1-uniprot.txt Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 4/4. |
| GO:0006526 L-arginine biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: The protein directly catalyzes an acetylated-intermediate reaction that produces an arginine/ornithine precursor, so it participates in the biosynthetic process. Reason: The protein directly catalyzes an acetylated-intermediate reaction that produces an arginine/ornithine precursor, so it participates in the biosynthetic process. Target-specific functional evidence supports the enzymatic role rather than reliance on knockout necessity alone. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; PMID:23321422 a yeast (Saccharomyces cerevisiae) ACOAT mutant was complemented by TUP5. file:ARATH/WIN1/WIN1-uniprot.txt Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 4/4. |
| GO:0006526 L-arginine biosynthetic process | IMP PMID:23321422 The Arabidopsis TUMOR PRONE5 gene encodes an acetylornithine... | ACCEPT | Summary: The protein directly catalyzes an acetylated-intermediate reaction that produces an arginine/ornithine precursor, so it participates in the biosynthetic process. Reason: The protein directly catalyzes an acetylated-intermediate reaction that produces an arginine/ornithine precursor, so it participates in the biosynthetic process. Target-specific functional evidence supports the enzymatic role rather than reliance on knockout necessity alone. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; PMID:23321422 a yeast (Saccharomyces cerevisiae) ACOAT mutant was complemented by TUP5. file:ARATH/WIN1/WIN1-uniprot.txt Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 4/4. |
| GO:0008483 transaminase activity | IEA GO_REF:0000002 | MODIFY | Summary: The generic catalytic class is true but the specific substrate reaction is established independently and already represented here. Reason: The generic catalytic class is true but the specific substrate reaction is established independently and already represented here. Refine the term to the demonstrated biosynthetic enzyme activity. Proposed replacements: N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; PMID:23321422 a yeast (Saccharomyces cerevisiae) ACOAT mutant was complemented by TUP5. |
| GO:0009507 chloroplast | HDA PMID:18431481 Sorting signals, N-terminal modifications and abundance of t... | MODIFY | Summary: Chloroplast localization is independently supported. Reason: Chloroplast localization is independently supported. Refine to the stromal compartment already represented in this review, using the convergent stromal proteomic assignments (PMID:16207701; PMID:20061580), consistent with functional GFP chloroplast localization (PMID:23321422). Proposed replacements: chloroplast stroma Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000250}. PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization |
| GO:0009507 chloroplast | HDA PMID:25293756 A proteomic strategy for global analysis of plant protein co... | MODIFY | Summary: Chloroplast localization is independently supported. Reason: Chloroplast localization is independently supported. Refine to the stromal compartment already represented in this review, using the convergent stromal proteomic assignments (PMID:16207701; PMID:20061580), consistent with functional GFP chloroplast localization (PMID:23321422). Proposed replacements: chloroplast stroma Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000250}. PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization |
| GO:0009507 chloroplast | IDA PMID:23321422 The Arabidopsis TUMOR PRONE5 gene encodes an acetylornithine... | MODIFY | Summary: Chloroplast localization is independently supported. Reason: Chloroplast localization is independently supported. Refine to the stromal compartment already represented in this review, using the convergent stromal proteomic assignments (PMID:16207701; PMID:20061580), consistent with functional GFP chloroplast localization (PMID:23321422). Proposed replacements: chloroplast stroma Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000250}. PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization |
| GO:0009507 chloroplast | IEA GO_REF:0000044 | MODIFY | Summary: Chloroplast localization is independently supported. Reason: Chloroplast localization is independently supported. Refine to the stromal compartment already represented in this review, using the convergent stromal proteomic assignments (PMID:16207701; PMID:20061580), consistent with functional GFP chloroplast localization (PMID:23321422). Proposed replacements: chloroplast stroma Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000250}. PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization |
| GO:0009507 chloroplast | ISM GO_REF:0000122 | MODIFY | Summary: Chloroplast localization is independently supported. Reason: Chloroplast localization is independently supported. Refine to the stromal compartment already represented in this review, using the convergent stromal proteomic assignments (PMID:16207701; PMID:20061580), consistent with functional GFP chloroplast localization (PMID:23321422). Proposed replacements: chloroplast stroma Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000250}. PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization |
| GO:0009570 chloroplast stroma | HDA PMID:16207701 The oligomeric stromal proteome of Arabidopsis thaliana chlo... | ACCEPT | Summary: Retain the stromal localization of this soluble chloroplast amino-acid-biosynthetic enzyme. Reason: Retain the stromal localization of this soluble chloroplast amino-acid-biosynthetic enzyme. Independent stromal proteomic assignments agree with the functional GFP chloroplast localization in PMID:23321422; the GFP experiment resolves chloroplasts, not the subplastid fraction. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000250}. PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization |
| GO:0009570 chloroplast stroma | HDA PMID:20061580 AT_CHLORO, a comprehensive chloroplast proteome database wit... | ACCEPT | Summary: Retain the stromal localization of this soluble chloroplast amino-acid-biosynthetic enzyme. Reason: Retain the stromal localization of this soluble chloroplast amino-acid-biosynthetic enzyme. Independent stromal proteomic assignments agree with the functional GFP chloroplast localization in PMID:23321422; the GFP experiment resolves chloroplasts, not the subplastid fraction. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000250}. PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization PMID:23321422 The TUP5-GFP signal colocalized with the autofluorescence of chloroplasts, indicating a chloroplastic localization |
| GO:0030170 pyridoxal phosphate binding | IEA GO_REF:0000002 | ACCEPT | Summary: The enzyme belongs to the class-III PLP-dependent aminotransferase family and conserves the PLP-binding catalytic machinery. Reason: The enzyme belongs to the class-III PLP-dependent aminotransferase family and conserves the PLP-binding catalytic machinery. Curated cofactor/site information and the ACOAT functional assignment support PLP binding; this is not a new direct cofactor assay claim. Supporting Evidence: file:ARATH/WIN1/WIN1-uniprot.txt Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; file:ARATH/WIN1/WIN1-uniprot.txt Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}. |
| GO:0042742 defense response to bacterium | IMP PMID:18266921 Arabidopsis proteins important for modulating defense respon... | KEEP AS NON CORE | Summary: WIN1 overexpression suppresses responses to HopW1-1 and other effectors and delays salicylic-acid induction (PMID:18266921). Reason: WIN1 overexpression suppresses responses to HopW1-1 and other effectors and delays salicylic-acid induction (PMID:18266921). Retain the defense-response contribution as contextual and non-core; the gene product is principally a metabolic enzyme, not demonstrated to be a pathogen receptor or direct immune signaling enzyme. Supporting Evidence: PMID:18266921 WIN1 is an essential protein, the overexpression of which over-rides the resistance response to HopW1-1 |
| GO:0048364 root development | IMP PMID:23321422 The Arabidopsis TUMOR PRONE5 gene encodes an acetylornithine... | MODIFY | Summary: The tup5-1 mutant loses primary-root meristem maintenance specifically under sufficient blue light, and arginine/metabolic-precursor supplementation rescues root growth (PMID:23321422). Reason: The tup5-1 mutant loses primary-root meristem maintenance specifically under sufficient blue light, and arginine/metabolic-precursor supplementation rescues root growth (PMID:23321422). Retain this demonstrated developmental consequence as non-core without recasting WIN1 as a light receptor or meristem signaling factor. Refine the general root-development claim to primary root development, already represented and directly resolved by the phenotype. Proposed replacements: primary root development Supporting Evidence: PMID:23321422 Roots of light-grown tup5-1 seedlings switch from indeterminate growth to determinate growth with arresting cell production and an exhausted root apical meristem. |
| GO:0080022 primary root development | IMP PMID:23321422 The Arabidopsis TUMOR PRONE5 gene encodes an acetylornithine... | KEEP AS NON CORE | Summary: The tup5-1 mutant loses primary-root meristem maintenance specifically under sufficient blue light, and arginine/metabolic-precursor supplementation rescues root growth (PMID:23321422). Reason: The tup5-1 mutant loses primary-root meristem maintenance specifically under sufficient blue light, and arginine/metabolic-precursor supplementation rescues root growth (PMID:23321422). Retain this demonstrated developmental consequence as non-core without recasting WIN1 as a light receptor or meristem signaling factor. Supporting Evidence: PMID:23321422 Roots of light-grown tup5-1 seedlings switch from indeterminate growth to determinate growth with arresting cell production and an exhausted root apical meristem. |
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