Primary Information |
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| BoMiProt ID | Bomi10145 |
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| 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 |
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| Organism | Bos taurus |
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| Uniprot ID | O19131 |
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| Milk Fraction | whey |
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| Ref Sequence ID | NP_777099.1 |
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| Aminoacid Length | 471 |
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| Molecular Weight | 51368 |
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| FASTA Sequence |
Download |
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| Gene Name | TNFRSF1A/TNFR1 |
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| Gene ID | 282527 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| 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. |
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| 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. |
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| Significance in milk | Milk synthesis |
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| PTMs | Glycosylation and Disulphide bond |
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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
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH; (210-232) |
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| 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. |
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| 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 |
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