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Details on Person UniProt:P19438 TNFRSF1A

Class:Id	ReferenceGeneProduct:66345
_chainChangeLog	signal peptide:1-21 added on Fri February 6 2015;chain:22-455 added on Fri February 6 2015;chain:41-201 added on Fri February 6 2015
_displayName	UniProt:P19438 TNFRSF1A
_timestamp	2026-02-20 22:50:22
chain	signal peptide:1-29 chain:30-455 chain:41-201
checksum	4CEFBA96D03B8225
comment	FUNCTION Receptor for TNFSF2/TNF and homotrimeric TNFSF1/lymphotoxin-alpha. 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. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.SUBUNIT Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling. Interacts with BAG4, BABAM2, FEM1B, GRB2, SQSTM1 and TRPC4AP (PubMed:10356400, PubMed:10359574, PubMed:10542291, PubMed:15465831, PubMed:8387891, PubMed:9915703). Interacts directly with NOL3 (via CARD domain); inhibits TNF-signaling pathway (By similarity). Interacts with SH3RF2, TRADD and RIPK1. SH3RF2 facilitates the recruitment of RIPK1 and TRADD to TNFRSF1A in a TNF-dependent process (PubMed:24130170). Interacts with PGLYRP1; this interaction is important for cell death induction (PubMed:26183779). Interacts (via death domain) with MADD (via death domain) (PubMed:9115275).SUBUNIT (Microbial infection) Interacts with mumps virus protein SH; this interaction inhibits downstream NF-kappa-B pathway activation.SUBUNIT (Microbial infection) Interacts with HCV core protein.SUBUNIT (Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein UL138.SUBUNIT (Microbial infection) Interacts with host TNFRSF1A; this interaction leads to the stimulation of both surface expression and shedding of TNFRSF1A.INTERACTION A secreted form is produced through proteolytic processing.SUBCELLULAR LOCATION Lacks a Golgi-retention motif, is not membrane bound and therefore is secreted.ALTERNATIVE PRODUCTS The domain that induces A-SMASE is probably identical to the death domain. The N-SMASE activation domain (NSD) is both necessary and sufficient for activation of N-SMASE.DOMAIN Both the cytoplasmic membrane-proximal region and the C-terminal region containing the death domain are involved in the interaction with TRPC4AP.PTM The soluble form is produced from the membrane form by proteolytic processing.PTM (Microbial infection) Glycosylated at Arg-376 by enteropathogenic E.coli protein NleB1 and S.typhimurium protein Ssek3: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE Disease susceptibility is associated with variants affecting the gene represented in this entry. An intronic mutation affecting alternative splicing and skipping of exon 6 directs increased expression of isoform 4 a transcript encoding a C-terminally truncated protein which is secreted and may function as a TNF antagonist.MISCELLANEOUS Disease-associated isoform. Isoform 4 splicing pattern is driven by a variation in the exon 6/intron 6 boundary region that alters exon 6 splicing. Exon 6 skipping introduces a frameshift and the translation of a protein lacking the intracellular, the transmembrane and part of the extracellular domain.ONLINE INFORMATION Repertory of FMF and hereditary autoinflammatory disorders mutations
description	recommendedName: Tumor necrosis factor receptor superfamily member 1A alternativeName: Tumor necrosis factor receptor 1 shortName: TNF-R1 alternativeName: Tumor necrosis factor receptor type I shortName: TNF-RI shortName: TNFR-I alternativeName: p55 alternativeName: p60 cdAntigenNameCD120a/cdAntigenName component recommendedName: Tumor necrosis factor receptor superfamily member 1A, membrane form /component component recommendedName: Tumor necrosis factor-binding protein 1 shortName: TBPI /component
geneName	TNFRSF1A TNFAR TNFR1
identifier	P19438
isSequenceChanged	FALSE
keyword	3D-structure Alternative splicing Amyloidosis Apoptosis Cell membrane Cleavage on pair of basic residues Direct protein sequencing Disease variant Disulfide bond Glycoprotein Golgi apparatus Host-virus interaction Membrane Proteomics identification Receptor Reference proteome Repeat Secreted Signal Transmembrane Transmembrane helix
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20
name	TNFRSF1A
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:6785075] ENSEMBL:ENSG00000067182 TNFRSF1A [Homo sapiens]
secondaryIdentifier	TNR1A_HUMAN A8K4X3 B2RDE4 B3KPQ1 B4DQB7 B4E309 B5M0B5 D3DUR1 Q9UCA4
sequenceLength	455
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:423550] UniProt:P19438-1 TNFRSF1A [Homo sapiens] [ReferenceIsoform:423551] UniProt:P19438-2 TNFRSF1A [Homo sapiens] [ReferenceIsoform:423552] UniProt:P19438-3 TNFRSF1A [Homo sapiens] [ReferenceIsoform:8978093] UniProt:P19438-4 TNFRSF1A [Homo sapiens] [ReferenceIsoform:8978094] UniProt:P19438-5 TNFRSF1A [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:5675738] TNFRSF1A(30-45) [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:6785048] TNFRSF1A(41-201) [extracellular region] [Homo sapiens]
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No pathways have been reviewed or authored by UniProt:P19438 TNFRSF1A (66345)