Ferritin is the major intracellular iron storage protein in prokaryotes and eukaryotes. Ferritin is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in the light chain ferritin gene are associated with several neurodegenerative diseases and hyperferritinemia-cataract syndrome. The ferritin gene has multiple pseudogenes, and ferritin is a ubiquitous and highly conserved protein which plays a major role in iron homeostasis. Ferritin is a holoenzyme shell with a molecular weight of about 450 kDa, and consists of 24 subunits of two types, H(heavy) and L(light), and capable of storing up to 4,500 atoms of ferric iron.
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Protein Aliases: apoferritin; Cell proliferation-inducing gene 15 protein; Ferritin H subunit; Ferritin heavy chain; ferritin heavy chain 1; Ferritin heavy chain, N-terminally processed; Ferritin L subunit; Ferritin L subunit 1; ferritin L-chain; Ferritin light chain; Ferritin light chain 1; ferritin light polypeptide-like 3; Ferritin subunit H; ferritin, heavy polypeptide 1; ferritin, light polypeptide; frih; fril; H-ferritin; L apoferritin; MGC71996; placenta immunoregulatory factor; proliferation-inducing protein 15
Gene Aliases: FHC; FTH; FTH1; FTHL6; FTL; Ftl-1; Ftl1; HFE5; HFt; L-ferritin; LFTD; MFH; NBIA3; OK/SW-cl.84; PIG15; PLIF
Molecular Function: storage protein