FSHβ plays an important role in the reproductive performance of pigs, but there are no studies on its protein structure and function. In this study, bioinformatics tools were used to predict the physicochemical properties, secondary and tertiary structure, hydrophobicity/hydrophilicity, transmembrane domain, and sites of phosphorylation and glycosylation of signal peptide FSHβ protein of sows. The results showed that the number of amino acids of FSHβ was 185, that is, the theoretical isoelectric amino acid point was 53.8, the instability index was 46.23, and the average hydrophilicity coefficient was 0.732. FSHβ protein was found to be a hydrophobic protein without a transmembrane domain, with 33 phosphorylation sites. None of the signal peptides was found to be distributed in the inner complete sequence. The secondary structure was mainly composed of α-helix, extended strand, β-turn, and random coil, with values of 29.97, 27.53, 10.10 and 32.40%, respectively. In summary, this study suggests that the amino acid sequence (988~1146aa) of FSHβ can be used to express antigens. It provides a reliable basis for further study of FSHβ protein function, purification of FSHβ protein, preparation of FSHβ antibody, and drug screening to improve reproductive performance of pigs.