Description
Product Characteristics:
Proteins internalized into the endocytic pathway are usually degraded. Efficient proteolysis requires denaturation, induced by acidic conditions within lysosomes, and reduction of inter- and intrachain disulfide bonds. Cytosolic reduction is mediated enzymatically by thioredoxin. In the endocytic pathway, reduction of protein disulfide bonds is important for the generation of MHC class II-peptide complexes. This process is catalyzed by a gamma-interferon-inducible thiol reductase (GILT). GILT is synthesized as a precursor, and following delivery to MHC class II-containing compartments (MIICs), is processed to the mature form via cleavage of amino- and carboxy-terminal propeptides. A lysosomal thiol reductase, GILT, is optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitro. GILT is expressed constitutively in antigen-presenting cells and is induced by g-interferon in other cell types, suggesting a potentially important role in antigen processing. Additionally, T cell recognition of select exogenous and endogenous epitopes is dependent on tumor cell expression of GILT. The absence of GILT in melanomas alters antigen processing and the hierarchy of immunodominant epitope presentation.
Subcellular location: Cytoplasm, Secreted
Synonyms: Gamma interferon inducible lysosomal thiol reductase, Gamma interferon inducible protein IP 30, GILT, I 30, interferon gamma inducible protein 30, Interferon gamma inducible protein 30 preproprotein, IP30, Lysosomal thiol reductase, Lysosomal thiol reductase, gamma-interferon-inducible.
Target Information: The protein encoded by this gene is a lysosomal thiol reductase that at low pH can reduce protein disulfide bonds. The enzyme is expressed constitutively in antigen-presenting cells and induced by gamma-interferon in other cell types. This enzyme has an important role in MHC class II-restricted antigen processing. [provided by RefSeq, Jul 2008]