Abstract: The structure of SLITRK6 protein was predicted and analyzed through bioinformatics methods. The results revealed a molecular weight of approximately 95 109.61 Da and a theoretical isoelectric point （pI） of 6.07. Leucine （Leu） was the most abundant amino acid （15.5%）， followed by serine （Ser， 7.7%） and glutamic acid （Glu， 6.9%）， classifying it as a hydrophilic protein. A transmembrane domain was identified around position 600. Secondary structure composition comprised α-helices （10.46%）， β-turns （7.37%）， random coils（82.17%）.Random coils prevailed in the three-dimensional structure.Phylogenetic analysis identified homologous SLITRK6 family members across species. The evolutionary tree demonstrated vertebrate clustering into distinct branches： reptiles and birds， mammals， and a rapidly evolving amphibian clade， consistent with established phylogeny.