Annotation inferences using phylogenetic trees
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Phylogenetic annotation transfers urate oxidase activity, urate catabolic process, purine nucleobase catabolic process, and peroxisome annotations from conserved uricase orthologs.
"GOA IBA records cite PANTHER uricase orthologs and mouse/rat/zebrafish supporting entities for Uox."
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Keyword mapping supports a broad oxidoreductase annotation, but the more informative molecular function for Uox is urate oxidase activity.
"GOA maps the UniProt oxidoreductase keyword to GO:0016491 for Uox."
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
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Orthology transfer supports the same urate oxidase activity, urate catabolic process, and peroxisome terms that are directly supported by mouse evidence.
"GOA ISO records transfer experimentally verified rat uricase annotations to mouse Uox."
Combined Automated Annotation using Multiple IEA Methods
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Combined automated annotation supports urate oxidase activity and urate catabolic process; the broader purine nucleobase metabolic-process term is retained as non-core.
"GOA IEA records cite InterPro, Rhea, EC, ARBA, UniPathway, and UniProt keyword mappings for Uox."
UniProtKB record for mouse Uox (P25688)
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Uox catalyzes oxidation of urate to 5-hydroxyisourate with oxygen and water, producing hydrogen peroxide.
"FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin."
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UniProt places Uox in urate degradation and annotates peroxisome and mitochondrion localization.
"PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3. SUBCELLULAR LOCATION: Peroxisome. Mitochondrion."
Falcon deep research report for mouse Uox
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Falcon synthesizes mouse Uox as a uricase-family enzyme whose core reaction is cofactor-independent urate oxidation to 5-hydroxyisourate.
"Uox catalyzes the oxidation of uric acid to 5-hydroxyisourate using molecular oxygen, producing hydrogen peroxide as the reduced product of O2."
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Falcon emphasizes peroxisomal hepatic localization as the conserved primary site for mammalian uricase.
"In terrestrial vertebrates, including rodents, uricase resides in peroxisomes and forms a core peroxisomal crystalloid in hepatocytes."
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Falcon uses knockout and comparative literature to support Uox as a major determinant of systemic urate homeostasis.
"Uox knockout mice develop severe hyperuricemia and early lethality unless rescued, reinforcing Uox's essential role in controlling systemic urate."
Peroxisome proliferator-activated receptor alpha-responsive genes induced in the newborn but not prenatal liver of peroxisomal fatty acyl-CoA oxidase null mice.
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Uox is among PPARalpha-responsive peroxisome-related liver genes induced after birth in fatty acyl-CoA oxidase-null mice.
"High levels of expression of PPARalpha-responsive genes in the liver commenced on the day of birth and persisted throughout the postnatal period."
Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria.
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A high-throughput mitochondrial proteome survey reported mouse tissue mitochondrial proteins and underlies the HDA mitochondrion annotation.
"We performed a proteomic survey of mitochondria from mouse brain, heart, kidney, and liver and combined the results with existing gene annotations."
Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes.
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The uric acid degradation pathway proceeds from urate oxidation to 5-hydroxyisourate and then through two downstream mouse enzymes to allantoin.
"The two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU)."
On the compartmentalization of catalase, fatty acyl-CoA oxidase and urate oxidase in mammalian livers, and the influence of clofibrate treatment on this microlocalization.
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Digitonin extraction indicates mammalian liver urate oxidase is closely associated with the peroxisomal compartment.
"fatty acyl-CoA oxidase and urate oxidase both of which were indicated as showing a closer association with the peroxisomal compartment than was the case for catalase"
Developmental changes of adenosine deaminase, xanthine oxidase, and uricase in mouse tissues.
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The study separately assessed adenosine deaminase, xanthine oxidase, and uricase in mouse tissues, supporting uricase activity while not making Uox a xanthine oxidase.
"Developmental changes of adenosine deaminase, xanthine oxidase, and uricase in mouse tissues."
Pex5l binds Acox1 or Uox
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Reactome describes Pex5l binding monomeric Uox, consistent with peroxisome import context rather than stable cytosolic residence as a core location.
"Pex5l binds monomeric Acox1 and monomeric Uox in preference to dimeric Acox1 and tetrameric Uox."