About TFRC / Transferrin:
Transferrin, known by the code TF, is a category of glycoproteins found in vertebrates, which are produced in the liver. While the liver is the main site of transferrin production, it is also synthesized in other tissues and organs, including the brain.
Transferrin binds to and manages the transport of iron through blood plasma, containing binding sites for two Fe ions. They have a reversible binding with iron, which allows them to bind and release as a means of transporting them from one part of the body to the next. Transferrins are also able to bind other metal ions.
Transferrin proteins work by loading themselves with iron in the liver. Then, when they travel through the body, they can come across cells that have transferrin receptors on their surface, which causes them to bind to the cell and release the iron ions based on pH levels, temperature, salt, and chelator, allowing transferrin to transport iron to certain cells under specific dontiions.
Transferrin interacts with MIS2 (MIS12 Kinetochore Complex Component), CALR (Calreticulin), CANX (Calnexin), TFRC (Transferrin Receptor), and TRF2 (Telomeric Repeat Binding Factor 2).
The structure of transferrin differs depending on the organism that it is present in. In humans, transferrin is made up of a polypeptide chain that contains 697 amino acids, as well as two carbohydrate chains. These amino acids play the key role in binding the iron ion and do this by having identical acids for each of the two lobes: two tyrosines, one histidine, and one aspartic acid.