Search by BoMiProt ID - Bomi10145


Primary Information

BoMiProt ID Bomi10145
Protein Name Tumor necrosis factor receptor superfamily member 1A/Tumor necrosis factor receptor 1/TNF-R1/Tumor necrosis factor receptor type I/ TNF-RI/TNFR-I/p55/p60/CD_antigen: CD120a
Organism Bos taurus
Uniprot IdO19131
Milk Fractionwhey
Ref Sequence Id NP_777099.1
Aminoacid Length 471
Molecular Weight 51368
Fasta Sequence https://www.uniprot.org/uniprot/O19131.fasta
Gene Name TNFRSF1A/TNFR1
Gene Id 282527
Protein Existence Status Reviewed

Secondary Information

Protein Function It serves as a receptor for TNFSF2/TNF-α and homotrimeric TNFSF1/lymphotoxin-α. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis.
Biochemical Properties Upon binding with TNFα, the intracellular DD of TNFR1 recruits TNF receptor-associated DD protein (TRADD), which in turn recruits receptor-interacting protein kinase 1 (RIP1), cellular inhibitor of apoptosis proteins 1 and 2 (cIAP1 and 2), and TNF receptor-associated factor 2. TRADD is important for the TNF-induced NF-κB signaling pathway, as in TRADD-deficient MEFs, IκB phosphorylation and degradation are completely abolished. The N-terminal region of TRADD interacts with the trimeric TRAF domain of TRAF2 in a 3:3 stoichiometry, whereas the C-terminal DD-containing region of TRADD interacts with many other DD-containing proteins, such as FADD and RIP1.
Significance in milk Milk synthesis
PTMs Glycosylation and Disulphide bond
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|O19131|TNR1A_BOVIN Tumor necrosis factor receptor superfamily member 1A OS=Bos taurus OX=9913 GN=TNFRSF1A PE=2 SV=1 MGLPTVPGLLLPLVLPALLADVYPAGVQGLVPHPGDLEKRESPCPQGKYNHPQN*54STICCT KCHKGTYLYNDCPGPGRDTDCRVCAPGTYTALENHLRRCLSCSRCRDEMFQVEISPCVVD RDTVCGCRKNQYREYWGETGFRCLN*145CSLCPN*151GTVNIPCQERQDTICHCHMGFFLKGAKCI SCHDCKNKECEKLCPTRPSTGKDSQDPGTTVLLPLVIVFGLCLASFASVVLACRYQRWKP KLYSIICGQSTLVKEGEPELLVPAPGFNPTTTICFSSTPSSSPVSIPPYISCDRSNFGAV ASPSSETAPPHLKAGPILPGPPASTHLCTPGPPASTHLCTPGPPASTHLCTPVQKWEASA PSAPDQLADADPATLYAVVDGVPPSRWKELVRRLGLSEHEIERLELENGRHLREAQYSML AAWRRRTPRREATLELLGRVLRDMDLLGCLENIEEALGGAARLASEPRLLW
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction 1TMH; (210-232)
Significance of PTMs contain 3 N glycosylation sites.Inhibition of N-glycosylation of TNFRSF1A in microglial cells results in inhibition of ligand binding. In macrophages, α2,6-sialylation of TNFRSF1A protects from apoptosis.In Schwann cells stimulated by TNF, galactosyltransferase B4GALT1 triggers an autocrine loop in which the level of B4GALT1 expression regulates MAPK activation, the release of inflammatory mediators and apoptosis.A type of glycosylation, the addition of GlcNAc to arginine of the death domains of TNFRSF1A, TRADD and adaptor proteins,that is induced by a pathogenic bacterium. This modification disrupts the TNFA signaling, inhibiting apoptosis and necroptosis (a type of regulated necrotic cell death), and is a part of the bacterial defense against the host immune system.
Bibliography 1.Gomes Ferreira, I., Pucci, M., Venturi, G., Malagolini, N., Chiricolo, M., & Dall’Olio, F. (2018). Glycosylation as a main regulator of growth and death factor receptors signaling. International journal of molecular sciences, 19(2), 580. 2.Lee, E. K., Kehrli, M. E., Jr, & Taylor, M. J. (1998). Cloning and sequencing of cDNA encoding bovine tumor necrosis factor (TNF)-receptor I. Veterinary immunology and immunopathology, 61(2-4), 379–385. 3.Li, J., Yin, Q., & Wu, H. (2013). Structural basis of signal transduction in the TNF receptor superfamily. Advances in immunology, 119, 135–153. https://doi.org/10.1016/B978-0-12-407707-2.00005-9 https://doi.org/10.1016/s0165-2427(97)00136-0