InterPro : IPR018195

Name  Transferrin family, iron binding site Short Name  Transferrin_Fe_BS
Type  Binding_site Description  Transferrins are a family of eukaryotic iron-binding glycoproteins that share the common function of controlling the level of free iron in biological fluids []. The transferrin family currently includes: Blood serotransferrin (siderophilin). Milk lactotransferrin (lactoferrin). Egg white ovotransferrin (conalbumin). Membrane-associated melanotransferrin.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 []. 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.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

2 Found In

Id Name Short Name Type
IPR001156 Transferrin-like domain Transferrin-like_dom Domain
IPR016357 Transferrin Transferrin Family

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Crichton RR Iron transport and storage. 1987 Eur J Biochem 164 485-506
Anderson BF Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8 A resolution. 1989 J Mol Biol 209 711-34

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)