ABSTRACT
@#Objective To predict and analyze the physical and chemical properties,structure,function,protein interaction and homology of SLC33A1 gene based on bioinformatics so as to provide a reference for further study on the function of SLC33A1.Methods A variety of bioinformatics tools were used to predict the physical and chemical properties,hydrophilicity,hydrophobicity,signal peptide structure,transmembrane structure,subcellular localization,three dimensional spatial structure,post-translational modification sites and protein-protein interaction of SLC33A1.Results SLC33A1 was a neutral,stable and hydrophobic protein without signal peptide sequence,which was mainly distributed in cell membrane and membrane structural organelle,with a probability of 13. 0% in vesicle membrane. There were 11 transmembrane domains,6 extracellular domains and 6 intracellular domains in SLC33A1 sequence. The tertiary structure of SLC33A1 was elastic and stable,which had 2 N-glycosylation sites,2 O-glycosylation sites and 13 potential protein phosphorylation sites. SLC33A1 interacted with 7 proteins such as ATM with high confidence,which was mainly involved in the negative regulation of inositol-requiring enyzme 1(IRE1)-mediated unfolded protein response,the respon-ses of glycosphingolipid,sialylation and cells to γ ray as well as the negative regulation of endoplasmic reticulum stress response.Conclusion The nature and function of SLC33A1 were investigated by various software,which provided theoretical references and ideas for further research on new anticancer targets in the future.