Vitellogenin
| Vitellogenin_N | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Vitellogenin_N | ||||||||
| Pfam | PF01347 | ||||||||
| Pfam clan | CL0020 | ||||||||
| InterPro | IPR001747 | ||||||||
| SCOP | 1llv | ||||||||
| SUPERFAMILY | 1llv | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
Vitellogenin (VTG or less popularly known as VG) (from latin vitellus, yolk, and gener, to produce) is a precursor protein of egg yolk normally in the blood or hemolymph only of females that is used as a biomarker in vertebrates of exposure to environmental estrogens which stimulate elevated levels in males as well as females. "Vitellogenin" is a synonymous term for the gene and the expressed protein. The protein product is classified as a glycolipoprotein, having properties of a sugar, fat and protein. It belongs to a family of several lipid transport proteins.
Vitellogenin is an egg yolk precursor protein expressed in the females of nearly all oviparous species including fish, amphibians, reptiles, birds, most invertebrates, and monotremes. Vitellogenin is the precursor of the lipoproteins and phosphoproteins that make up most of the protein content of yolk. In the presence of estrogenic endocrine disruptive chemicals (EDCs), male fish can express the Vg gene in a dose dependent manner. Vg gene expression in male fish can be used as a molecular marker of exposure to estrogenic EDCs.
Vitellinogen precursors provide the major egg yolk proteins that are a source of nutrients during early development of egg-laying (oviparous) vertebrates and invertebrates. Vitellogenin is the precursor of the lipoproteins and phosphoproteins that make up most of the protein content of yolk. More specifically, the N-terminal domain functions as a signal peptide which helps export. Vitellinogen precursors are multi-domain apolipoproteins (proteins that bind to lipids to form lipoproteins), that are cleaved into distinct yolk proteins. Different vitellinogen precursors exist, which are composed of variable combinations of yolk protein components; however, the cleavage sites are conserved.
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