Structures of the IFNp gene and protein

The mature human IFNp is a glycoprotein of -23 kDa apparent molecular weight. The entire primary sequence as deduced from complementary DNA consists of 166 amino acids which are preceded by a signal peptide of 21 amino acids. An N-glycosylation site has been identified at position 80 of the mature protein (Asn80-Glu81-Thr82). A disulfide bond between cysteines 31 and 141 is essential for biological activity. The more hydrophobic character of the IFNp protein is in agreement with a high content of leucine, tyrosine and isoleucine. The physiological significance of the carbohydrate moiety is still unclear, since unglycosylated recombinant IFNp retains its biological activity, although it has been suggested that glycosylation may contribute to its stability.

The IFNp gene has been mapped to human chromosome 9 in the vicinity of the IFNa gene cluster. Like the IFNa genes, the IFNp gene lacks any intron. Only one IFNp gene has been identified in human and mouse, whereas at least three closely related IFNp genes have been found in cattle.

Native murine IFNp has an apparent molecular weight of 35-40 kDa. The primary sequence of the mature protein consists of 161 amino acids preceded by 21 amino acids of signal sequence. There are three potential sites for N-glycosylation (at positions 29, 69 and 76) and one single cysteine residue at position 17. Thus, unlike human IFNp, the murine species does not require intramolecular disulfide linkage for biological activity. Like the murine IFNa genes, the murine IFN|3 gene is devoid of introns and has been localized to chromosome 4.

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