Synonyms
Historical Background
In 1988, the laboratory of Dr. Jeffrey Ravetch characterized a gene which is upregulated upon exposure to the cytokine, interferon-γ (IFN-γ). The protein is produced in a precursor form of 35 kDa and processed into a mature form of 30 kDa. The protein was originally named inducible protein 30 (IP30) and the gene named IFI30. IP30 is constitutively expressed in many antigen-presenting cells (APCs) and induced in other cell types including fibroblasts, endothelial cells, and keratinocytes (Maric et al. 2001; Lackman and Cresswell 2006; Phipps-Yonas et al. 2013a; Nguyen et al. 2016).
Homology to protein folding patterns of a cellular thiol reductase, thioredoxin, suggested that IP30 may be capable of breaking disulfide bonds. Indeed, a thioredoxin-like motif, CXXC, is found in the IP30 protein sequence and is conserved across species with IP30 homologs. IP30 reduces disulfide bonds, and the cysteines in the CXXC motif...
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References
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Meador, L.R., Hastings, K.T. (2018). Gamma-Interferon-Inducible Lysosomal Thiol Reductase (GILT). In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101662
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