Binding Site

Transferrin family, iron binding site (IPR018195)

Short name: Transferrin_Fe_BS


Transferrins are a family of eukaryotic iron-binding glycoproteins that share the common function of controlling the level of free iron in biological fluids [PMID: 3032619]. The transferrin family currently includes:

  • Blood serotransferrin (siderophilin).
  • Milk lactotransferrin (lactoferrin).
  • Egg white ovotransferrin (conalbumin).
  • Membrane-associated melanotransferrin.
  • Inhibitor of carbonic anhydrase.

Transferrins are proteins of 650 to 700 residues which have evolved from the duplication of a domain of around 340 residues. Each of the duplicated domains binds one atom of iron. Each iron atom is bound by four conserved residues: an aspartic acid, two tyrosines, and a histidine [PMID: 2585506]. All of the cysteines in both domains are involved in intradomain disulphide bonds.

This entry contains three different signature patterns for transferrins. Each of them is centred on one of the iron-binding residue, respectively the two tyrosines and the histidine. Each of the signatures is present twice in each type of transferrins.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

No terms assigned in this category.

Cellular Component

GO:0005576 extracellular region

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns
PROSITE patterns
PROSITE patterns