Bioinformatic prediction of characteristics of ferredoxin 1,a key factor of cell death induced by copper ionophore
Objective To predict the protein structure,post-translational modification and tissue expression of Ferredoxin 1(Fdx1)by analyzing the amino acid sequence.Methods Amino acid sequences of human Fdx1 protein obtained from UniProt were analyzed.Using various data mining tools,the basic properties,characteristic structures,spatial structures,post-translational modification,biological function and tissue expression of Fdx1 were predicted using the ProtParam,SMART,SOPMA,NetPhos 3.1,STRING and ProteomicsDB,respectively.Results Basic properties.There were 184 amino acids in Fdx1,with the molecular mass of 19 kDa,and the molecular formula of C819H1341N251O275S9.Alanine and glycine accounted for the highest proportion of the amino acid composition(10.9%).It was predicted as a hydrophilic protein.No transmembrane structure and signal peptide were found.Mitochondria were the subcellular structures with the highest localization probability.Characteristic structure.A highly conservative structural functional domain,FER2,was present at positions 72-157.Spatial structure.The most abundant form of the secondary structure of human Fdx1 protein was the α-helix(36.96%).Post-translational modification.Ten post-translational modification sites,such as phosphorylation,glycosylation,and methylation were predicted.Biological function.Fdx1 interacted with multiple proteins like the iron-sulfur cluster assembling enzyme(P=0.0008).More than twenty signaling pathways were enriched in Fdx1,especially those related to diseases and metabolism.Tissue expression.Fdx1 was mostly overexpressed in the normal tissue of the nasal respiratory epithelium of the visceral system(log10 650 ppm)and the model organism of the brain cancer cell line U251(log10 557 ppm).Conclusion The bioinformatic analysis of the structure and function of the human Fdxl protein provides important references for exploring the mechanism of copper-induced programmed cell death.
cuproptosisferredoxin 1bioinformaticsprogrammed cell death