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Background
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Fas ligand is also known as FasL, CD178, CD95L, or TNFSF6, is a homotrimeric type-II transmembrane protein that belongs to the tumor necrosis factor (TNF) family. Its binding with its receptor induces apoptosis. Fas ligand/receptor interactions play an important role in the regulation of the immune system and the progression of cancer. Mature human Fas Ligand consists of a 179 amino acid (aa) extracellular domain (ECD), a 22 aa transmembrane segment, and a 80 aa cytoplasmic domain. Within the ECD, human Fas Ligand shares 81 % and 78 % aa sequence identity with mouse and rat Fas Ligand, respectively. Apoptosis triggered by Fas-Fas ligand binding plays a fundamental role in the regulation of the immune system. Its functions include:T-cell homeostasis, cytotoxic T-cell activity, immune privilege, maternal tolerance, tumor counterattack. Defective Fas-mediated apoptosis may lead to oncogenesis as well as drug resistance in existing tumors. Germline mutation of Fas is associated with autoimmune lymphoproliferative syndrome (ALPS), a childhood disorder of apoptosis.
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Molecular Weight
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17.7 kDa
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UniProt
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P48023
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Research Area
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Immunology, Adaptive Immunity, Hematopoietic Progenitors, Innate Immunity, Cytokines, Apoptosis/Necrosis, CD Antigens, Virology, Cancer, Surface Receptors of Immune Cells
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Pathways
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Apoptosis, EGFR Signaling Pathway, Production of Molecular Mediator of Immune Response, Positive Regulation of Endopeptidase Activity
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