Structural component of the egg vitelline envelope; forms long filaments. Functions as species-specific receptor for the sperm protein lysin; prevents fertilization by sperm from other species. Each VERL chain can bind multiple copies of the sperm protein lysin; this creates a 3 um hole in the egg vitelline envelope through which the sperm passes. May form disulfide-linked homodimers (PubMed:9192632, PubMed:28622512). Interacts (via VERL repeats) with sperm lysin (PubMed:9192632, PubMed:28622512). Each VERL chain can bind numerous lysin molecules (PubMed:9192632, PubMed:28622512). Detected on the egg vitelline envelope (at protein level). VERL repeat 2 is important for species-specific lysin binding, even if it has lower affinity for lysin than VERL repeat 3. VERL repeats 3 to 22 have high sequence similarity, indicating they all can bind lysin equally well, but they do not play a role in species-specific sperm selection. VERL repeat 1 does not bind lysin. N-glycosylated (PubMed:9192632, PubMed:28622512). About half of the glycoprotein mass corresponds to carbohydrate chains (PubMed:9192632). N-glycosylation is not required for lysin binding (PubMed:28622512). O-glycosylated. O-glycosylation is not required for lysin binding.