Glycosylation, one of the most important post-translational modifications of proteins, plays an irreplaceable role in the whole process of spermatogenesis, sperm-egg recognition, and fertilization. Herein, we mapped the first bovine sperm N-linked glycoproteome and a total of 1188 N-glycosylated sites on 626 proteins were identified. Bioinformatics analysis revealed that bovine sperm N-glycosylated proteins were classified into "extracellular region" and "lysosome" groups based on cellular component annotation and enrichment of glycoproteins with proteolytic and reproductive functions. Notably, cysteines were highly enriched in the canonical N-glycosylation motifs N-!P-[S/T/C] and the conservative motifs N-C-[S/T] were also significantly enriched, indicating these modifications play extraordinary roles in bovine spermatogenesis and maturation. The percentage of cysteine at the second position relative to modified asparagine was 7.5%, much higher than that of the previously reported N-linked glycoproteome. A total of 120 cysteine enriched N-glycoproteins were identified, which had significantly upregulated metalloendopeptidase activity and metal ion binding compared with the whole bovine sperm glycoproteome. Strikingly, 15 of 58 N-C-[S/T] motif-containing glycoproteins had a disintegrin and metalloproteinase (ADAM) protein domain. Thus, we hypothesized that ADAM-containing conserved free cysteine residues in N-linked glycoprotein motifs may be key cysteine-switches and may have extraordinary roles in bovine spermatozoa. In conclusion, almost all bovine sperm glycoproteins have enzyme activity, participate in proteolysis, and play indispensable roles in spermatogenesis, sperm-egg recognition, and eventual fertilization. The mapping of N-glycosylation on bovine sperm may provide a new means to explore potential biomarkers for improving sperm quality and fertility.