Melanotransferrin is a protein that in humans is encoded by the MFI2gene. MFI2 has also recently been designated CD228 (cluster of differentiation 228).
The protein encoded by this gene is a cell-surface glycoprotein found on melanoma cells. The protein shares sequence similarity and iron-binding properties with members of the transferrin superfamily. The importance of the iron binding function has not yet been identified. This gene resides in the same region of chromosome 3 as members of the transferrin superfamily. Alternative splicing results in two transcript variants.[1] It is part of neural crest tissue, often present in melanotic neuroectodermal tumor of infancy.
Suryo Rahmanto Y, Dunn LL, Richardson DR (2007). "The melanoma tumor antigen, melanotransferrin (p97): a 25-year hallmark--from iron metabolism to tumorigenesis". Oncogene. 26 (42): 6113–24. doi:10.1038/sj.onc.1210442. PMID17452986.
Baker EN, Baker HM, Smith CA, et al. (1992). "Human melanotransferrin (p97) has only one functional iron-binding site". FEBS Lett. 298 (2–3): 215–8. doi:10.1016/0014-5793(92)80060-T. PMID1544447.
Garratt RC, Jhotí H (1992). "A molecular model for the tumour-associated antigen, p97, suggests a Zn-binding function". FEBS Lett. 305 (1): 55–61. doi:10.1016/0014-5793(92)80654-Y. PMID1633859.
Sciot R, de Vos R, van Eyken P, et al. (1989). "In situ localization of melanotransferrin (melanoma-associated antigen P97) in human liver. A light- and electronmicroscopic immunohistochemical study". Liver. 9 (2): 110–9. doi:10.1111/j.1600-0676.1989.tb00387.x. PMID2540389.
Le Beau MM, Diaz MO, Plowman GD, et al. (1986). "Chromosomal sublocalization of the human p97 melanoma antigen". Hum. Genet. 72 (4): 294–6. doi:10.1007/BF00290951. PMID3754536.
Plowman GD, Brown JP, Enns CA, et al. (1983). "Assignment of the gene for human melanoma-associated antigen p97 to chromosome 3". Nature. 303 (5912): 70–2. doi:10.1038/303070a0. PMID6843660.
Food MR, Rothenberger S, Gabathuler R, et al. (1994). "Transport and expression in human melanomas of a transferrin-like glycosylphosphatidylinositol-anchored protein". J. Biol. Chem. 269 (4): 3034–40. PMID8300636.
Rothenberger S, Food MR, Gabathuler R, et al. (1996). "Coincident expression and distribution of melanotransferrin and transferrin receptor in human brain capillary endothelium". Brain Res. 712 (1): 117–21. doi:10.1016/0006-8993(96)88505-2. PMID8705293.
Richardson DR (2000). "The role of the membrane-bound tumour antigen, melanotransferrin (p97), in iron uptake by the human malignant melanoma cell". Eur. J. Biochem. 267 (5): 1290–8. doi:10.1046/j.1432-1327.2000.01079.x. PMID10691965.
Sekyere E, Food MR, Richardson DR (2002). "A second melanotransferrin gene (MTf2) and a novel protein isoform: explanation for the membrane-bound and soluble forms of melanotransferrin?". FEBS Lett. 512 (1–3): 350–2. doi:10.1016/S0014-5793(02)02248-2. PMID11852110.
Food MR, Sekyere EO, Richardson DR (2002). "The soluble form of the membrane-bound transferrin homologue, melanotransferrin, inefficiently donates iron to cells via nonspecific internalization and degradation of the protein". Eur. J. Biochem. 269 (18): 4435–45. doi:10.1046/j.1432-1033.2002.03140.x. PMID12230555.