InterPro domain: IPR012347

This entry represents ferritin and structurally related proteins. Ferritin is a major non-haem iron storage protein in animal, plants and microorganisms [ 1 ]. Iron is required by most organisms, but is potentially toxic due to its reactivity, which is counteracted by sequestering it into ferritin. Ferritin consists of a 4-helical bundle core, and contains a bimetal-ion centre in the middle of the bundle. Other proteins with this structure include: haem-containing bacteriferritins; rubrerythrin, which appears to have a role in anaerobic detoxification pathway for reactive oxygen species [ 2 ]; Dps (DNA-binding proteins from starved cells) used in bacteria for iron storage-detoxification; and CRD1 (AcsF), which is required for the maintenance of photosystem I [ 3 ].

1. Iron and proteins for iron storage and detoxification. Biometals 17, 197-202
2. Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase. J. Bacteriol. 186, 7888-95
3. The Crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii. EMBO J. 19, 2139-51