Transferrin
| Gene Ontology | |
|---|---|
| Molecular function | • protein binding • ferric iron binding • ubiquitin protein ligase binding |
| Cellular component | • extracellular region • mitochondrion • early endosome • late endosome • coated pit • basal plasma membrane • endosome membrane • cytoplasmic membrane-bounded vesicle • apical plasma membrane • endocytic vesicle • secretory granule • basal part of cell • perinuclear region of cytoplasm • recycling endosome |
| Biological process | • platelet degranulation • cellular iron ion homeostasis • blood coagulation • platelet activation • transferrin transport • transmembrane transport |
| Sources: Amigo / QuickGO | |
133.46 – 133.5 Mb
103.2 – 103.23 Mb
| Transferrin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Transferrin | ||||||||
| Pfam | PF00405 | ||||||||
| InterPro | IPR001156 | ||||||||
| PROSITE | PDOC00182 | ||||||||
| SCOP | 1lcf | ||||||||
| SUPERFAMILY | 1lcf | ||||||||
| OPM superfamily | 161 | ||||||||
| OPM protein | 1lfc | ||||||||
Transferrins are iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. Human transferrin is encoded by the TF gene. Transferrin glycoproteins bind iron very tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of the total body iron, it is the most important iron pool, with the highest rate of turnover (25 mg/24 h). Transferrin has a molecular weight of around 80 KDa and contains two specific high-affinity Fe(III) binding sites. The affinity of transferrin for Fe(III) is extremely high (1023 M−1 at pH 7.4) but decreases progressively with decreasing pH below neutrality. When not bound to iron, it is known as "apotransferrin" (see also apoprotein). Read more about Transferrin: Transport Mechanism, Structure, Tissue Distribution, Immune System, Role in Disease, Other Effects, Pathology, Reference Ranges, Interactions, Related Proteins | |||||||||