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Aconitase 1, also known as iron regulatory element binding protein 1 (IREB1), is a cytosolic protein which binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5' UTR of ferritin mRNA, and in the 3' UTR of transferrin receptor mRNA. The iron-induced binding to the IRE results in repression of translation of ferritin mRNA, and inhibition of degradation of the otherwise rapidly degrading transferrin receptor mRNA. Thus, IREB1 plays a central role in cellular iron homeostasis. It was also shown to have aconitase activity, and hence grouped with the aconitase family of enzymes. Protein function: Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding. [The UniProt Consortium]
Keywords:
Anti-IRP1, Anti-ACO1, Anti-IREB1, Anti-IRE-BP 1, Anti-Aconitase, EC=4.2.1.3, Anti-Citrate hydro-lyase, Anti-Iron regulatory protein 1, Anti-Ferritin repressor protein, Anti-Cytoplasmic aconitate hydratase, Anti-Iron-responsive element-binding protein 1, A
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