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ferritin
Ferritin is a ubiquitous intracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including algae, bacteria, higher plants, and animals. In humans, it acts as a buffer against iron deficiency and iron overload.〔(Iron Use and Storage in the Body: Ferritin and Molecular Representations ), Rachel Casiday and Regina Frey, Department of Chemistry, Washington University, St. Louis.〕 Ferritin is found in most tissues as a cytosolic protein, but small amounts are secreted into the serum where it functions as an iron carrier. Plasma ferritin is also an indirect marker of the total amount of iron stored in the body, hence serum ferritin is used as a diagnostic test for iron deficiency anemia.
Ferritin is a globular protein complex consisting of 24 protein subunits and is the primary ''intracellular iron-storage protein'' in both prokaryotes and eukaryotes, keeping iron in a soluble and non-toxic form. Ferritin that is not combined with iron is called apoferritin.
== Gene ==
Ferritin genes are highly conserved between species. All vertebrate ferritin genes have three introns and four exons. In human ferritin, introns are present between amino acid residues 14 and 15, 34 and 35, and 82 and 83; in addition, there are one to two hundred untranslated bases at either end of the combined exons.〔 The tyrosine residue at amino acid position 27 is thought to be associated with biomineralization.
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