Hephaestin
| Hephaestin | |
|---|---|
| Identifiers | |
| Symbol | HEPH |
| Entrez | 9843 |
| HUGO | 4866 |
| OMIM | 300167 |
| UniProt | Q9BQS7 |
| Other data | |
| Locus | Chr. X q11-12 |
Hephaestin is a protein involved in the metabolism and homeostasis of iron and possibly copper. It is a transmembrane copper-dependent ferroxidase responsible for transporting dietary iron from intestinal enterocytes into the circulatory system. The highest expression of hephaestin is found in small intestine. It is limited to enterocytes of the villi (where the iron absorption takes place), being almost absent in crypt cells. Hephaestin may convert iron(II) state, Fe2+ to iron(III) state, Fe3+ and mediates iron efflux most likely in cooperation with the basolateral iron transporter, ferroportin 1. To a lesser extent hephaestin has been detected in colon, spleen, kidney, breast, placenta and bone trabecular cells but its role in these tissues remains to be established. Hephaestin presents homology with ceruloplasmin, a serum dehydrogenase protein involved in copper detoxification and storage.
Hephaestin is a protein of 1135 aminoacids formed from a precursor of 1158 aminoacids and 130,4 kDa. It binds 6 copper ions per monomer.
Hephaestin was first identified by Dr. Christopher D. Vulpe of the University of California et al. in 1999[1]. They named the new found protein after Hephaestus, the Greek god of metal working.