@#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.