InterPro domain: IPR011030

Vitellinogen precursors provide the major egg yolk proteins that are a source of nutrients in the yolk of egg-laying animals. Vitellogenin is a large multidomain protein. In vertebrates, a complete vitellinogen is composed of an N-terminal signal peptide for export, followed by four regions that can be cleaved into yolk proteins: lipovitellin-1 (LV1), phosvitin (PV), lipovitellin-2 (LV2), and a von Willebrand factor type D domain (YGP40) [ 1 ].

The superhelical domain occurs at the N-terminal chain of lipovitellin-1 (LV1N) [ 2 ]. This domain is multihelical, forming two curved, alpha/alpha layers with an overall right-handed superhelix fold. This domain also occurs in other proteins, such as microsomal triglyceride transfer proteins, responsible for the assembly of low-density lipoproteins [ 3 ].

1. Vertebrate yolk proteins: a review. Mol. Reprod. Dev. 69, 109-16
2. Vertebrate yolk complexes and the functional implications of phosvitins and other subdomains in vitellogenins. Biol. Reprod. 76, 926-35
3. Lipid-protein interactions in lipovitellin. Biochemistry 41, 9398-409