Search by BoMiProt ID - Bomi5706


Primary Information

BoMiProt ID Bomi5706
Protein Name FAS-associated death domain protein/FAS-associating death domain-containing protein
Organism Bos taurus
Uniprot IDQ645M6
Milk FractionExosomes
Ref Sequence ID NP_001007817.1
Aminoacid Length 209
Molecular Weight 23002
FASTA Sequence Download
Gene Name FADD
Gene ID 493720
Protein Existence Status Reviewed

Secondary Information

Presence in other biological fluids/tissue/cells placenta 
Protein Function Fas-associated death domain protein (FADD), which is the pivotal adaptor of the apoptotic signal mediated by death receptors of the TNF family.
Biochemical Properties FADD is the key transducer of the apoptotic signal triggered by all death receptors of the TNF family, such as Fas, TNF receptor 1 (TNF-R1), death receptor 3 (DR3), TNF-related apoptosis-inducing ligand TRAIL-R1 (DR4) and TRAIL-R2 (DR5).FADD binds directly or indirectly to the intracellular domain of these receptors via its death domain (DD) and transduces the signal to pro-caspase-8 via a homotypic interaction of their respective DEDs. The binding of FADD to the death receptors and to pro-caspase-8 gives rise to the DISC. Consequently, pro-caspase-8 is cleaved into active caspase-8 that will in turn activate effector caspases like caspase-3 to induce apoptosis. 
PTMs Phosphorylation at Ser
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
NA
Predicted Disorder Regions 89-91, 182-209
DisProt Annotation
TM Helix Prediction No TM helices
Bibliography 1.Vilmont V, Tourneur L, Chiocchia G. Fas-associated death domain protein and adenosine partnership: fad in RA. Rheumatology (Oxford). 2012 Jun;51(6):964-75. doi: 10.1093/rheumatology/ker402. Epub 2012 Jan 16. PMID: 22253026. 2. Chinnaiyan AM, O'Rourke K, Tewari M, et al. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis, Cell, 1995, vol. 81 (pg. 505-12). 3.Chaudhary PM, Eby M, Jasmin A, et al. Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-κB pathway, Immunity, 1997, vol. 7 (pg. 821-30). 4.Schneider-Brachert W, Tchikov V, Neumeyer J, et al. Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles, Immunity, 2004, vol. 21 (pg. 415-28). 5.Schneider P, Thome M, Burns K, et al. TRAIL receptors 1 (DR4) and 2 (DR5) signal FADD-dependent apoptosis and activate NF-κB, Immunity, 1997, vol. 7 (pg. 831-6). 6. Chinnaiyan AM, O'Rourke K, Yu GL, et al. Signal transduction by DR3, a death domain-containing receptor related to TNFR-1 and CD95, Science, 1996, vol. 274 (pg. 990-2). 7.Nagata S. Apoptosis by death factor, Cell, 1997, vol. 88 (pg. 355-65). 8.Tourneur L, Chiocchia G. FADD: a regulator of life and death, Trends Immunol, vol. 31 (pg. 260-9).