TF
Domain
Has a bilobed structure, each lobe binds a single Fe(3+) ion. Does not always bind 2 Fe(3+) ions.
(Microbial infection) Binds to Neisseria transferrin-binding proteins A and B via its C-terminal lobe only. The L3 helix finger of TbpA inserts into the C-terminal lobe of TF, altering its conformation and probably disturbing the coordination of iron 2. Electron microscopy suggests that in the TbpA-TbpB-TF complex, TF is captured directly above the loop domain of TbpA in a chamber of about 1000 Angstroms(3) formed by the 3 proteins, where interactions between the proteins serve to abstract iron 2 from TF (PubMed:22327295, PubMed:22343719). Binding to TbpB does not alter the conformation of the C-terminal lobe (PubMed:22343719).
Function
Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
(Microbial infection) Serves as an iron source for Neisseria species, which capture the protein and extract its iron for their own use.
(Microbial infection) Serves as an iron source for parasite T.brucei (strain 427), which capture TF via its own transferrin receptor ESAG6:ESAG7 and extract its iron for its own use.
Involvement in disease
Atransferrinemia
ATRAF
A rare autosomal recessive disorder characterized by abnormal synthesis of transferrin leading to iron overload and microcytic hypochromic anemia.
None
The disease is caused by variants affecting the gene represented in this entry.
Sequence Similarities
Belongs to the transferrin family.
Tissue Specificity
Expressed by the liver and secreted in plasma.
Cellular localization
- Secreted
Alternative names
PRO1400, TF, Serotransferrin, Transferrin, Beta-1 metal-binding globulin, Siderophilin