| Primary Identifier | IPR033999 | Type | Domain |
| Short Name | TNFRSF6_N |
| description | Tumor necrosis factor receptor superfamily member 6 (TNFRSF6), also known as Fas cell surface death receptor (FasR), Fas, APT1, CD95, FAS1, APO-1, FASTM, or ALPS1A, contains a death domain and plays a central role in the physiological regulation of programmed cell death [, ]. It has been implicated in the pathogenesis of various malignancies and diseases of the immune system [, ]. The receptor interacts with the Fas ligand (FasL), allowing the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10; autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, leading to apoptosis. This receptor has also been shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is involved in transducing the proliferating signals in normal diploid fibroblast and T cells [, , ].This entry represents the N-terminal domain of FasR. TNF-receptors are modular proteins. The N-terminal extracellular part contains a cysteine-rich region responsible for ligand-binding. This region is composed of small modules of about 40 residues containing 6 conserved cysteines; the number and type of modules can vary in different members of the family [, , ]. |
