Ferritin-like diiron domain

Definition

This entry represents a group of proteins, containing ferritin-like domain, which is an about 145-residue domain made of a four-helix bundle surrounding a non-heme, non-sulphur, oxo-bridged diiron site. The diiron site is contained within a twisted, left-handed four-helix-bundle constituted of two anti-parallel helix pairs connected through a left-handed crossover connection. Known ligand residues at non-heme, non-sulphur diiron sites in proteins include His, Asp, Glu, and Tyr. Proteins containing a ferritin-like diiron domain possess the ability to catalyse oxidation of Fe2 to Fe3 by O2, i.e. ferroxidase activity. The ferritin-like diiron domain occurs in stand-alone form in ferritin and bacterioferritin or in association with the rubredoxin-like domain in rubrerythrin PMID:8646540. Proteins known to contain a ferritin-like diiron domain are listed below: Ferritin (Ftn), an eukaryotic intracellular protein that stores iron in a soluble, nontoxic, readily available form. Bacterioferritin (Bfr), a prokaryotic protein which may perform functions in iron detoxification and storage. Rubrerythrin (Rr), a non-heme protein isolated from anaerobic sulphate- reducing bacteria. Nigerythrin (Nr), a prokaryotic protein of unknown function.

5 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (5 proteins: gene, accession, name)

• FTH1
• FTH1P19
• FTHL17
• FTL
• FTMT