PROSITE documentation PDOC00181 [for PROSITE entry PS00540]

Ferritin iron-binding regions signatures





Description

Ferritin [1,2] is one of the major non-heme iron storage proteins. It consists of a mineral core of hydrated ferric oxide, and a multi-subunit protein shell which englobes 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 encodes for 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 [3].

There are a number of well conserved region in the sequence of ferritins. We have selected two of these regions to develop signature patterns. The first pattern is located in the central part of the sequence of ferritin and it contains three conserved glutamate which are thought to be involved in the binding of iron. The second pattern is located in the C-terminal section, it corresponds to a region which forms a hydrophilic channel through which small molecules and ions can gain access to the central cavity of the molecule; this pattern also includes conserved acidic residues which are potential metal binding sites.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

FERRITIN_1, PS00540; Ferritin iron-binding regions signature 1  (PATTERN)

FERRITIN_2, PS00204; Ferritin iron-binding regions signature 2  (PATTERN)


References

1AuthorsCrichton R.R., Charloteaux-Wauters M.
TitleIron transport and storage.
SourceEur. J. Biochem. 164:485-506(1987).
PubMed ID3032619

2AuthorsTheil E.C.
TitleFerritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms.
SourceAnnu. Rev. Biochem. 56:289-315(1987).
PubMed ID3304136
DOI10.1146/annurev.bi.56.070187.001445

3AuthorsRagland M., Briat J.-F., Gagnon J., Laulhere J.-P., Massenet O., Theil E.C.
TitleEvidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean.
SourceJ. Biol. Chem. 265:18339-18344(1990).
PubMed ID2211706



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