InterPro domain: IPR008331

Ferritin is one of the major non-haem iron storage proteins in animals, plants, and microorganisms [ 1 ]. It consists of a mineral core of hydrated ferric oxide, and a multi-subunit protein shell that encloses the former and assures its solubility in an aqueous environment.

In animals the protein is mainly cytoplasmic and there are generally two or more genes that encode closely related subunits - in mammals there are two subunits which are known as H(eavy) and L(ight). In plants ferritin is found in the chloroplast [ 2 ].

This entry represents the main structural domain of ferritin. The domain is also found in other ferritin-like proteins such as members of the DNA protection during starvation (DPS) family [ 3 ] and bacterioferritins [ 4 ].

1. Iron and proteins for iron storage and detoxification. Biometals 17, 197-202
2. Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean. J. Biol. Chem. 265, 18339-44
3. Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states. Proc. Natl. Acad. Sci. U.S.A. 101, 13780-5
4. The binding of haem and zinc in the 1.9 A X-ray structure of Escherichia coli bacterioferritin. J. Biol. Inorg. Chem. 14, 201-7