P25118 · TNR1A_MOUSE
- ProteinTumor necrosis factor receptor superfamily member 1A
- GeneTnfrsf1a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids454 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for TNFSF2/TNF-alpha 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 (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTumor necrosis factor receptor superfamily member 1A
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP25118
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Golgi apparatus membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 30-212 | Extracellular | ||||
Sequence: LVPSLGDREKRDSLCPQGKYVHSKNNSICCTKCHKGTYLVSDCPSPGRDTVCRECEKGTFTASQNYLRQCLSCKTCRKEMSQVEISPCQADKDTVCGCKENQFQRYLSETHFQCVDCSPCFNGTVTIPCKETQNTVCNCHAGFFLRESECVPCSHCKKNEECMKLCLPPPLANVTNPQDSGTA | ||||||
Transmembrane | 213-235 | Helical | ||||
Sequence: VLLPLVILLGLCLLSFIFISLMC | ||||||
Topological domain | 236-454 | Cytoplasmic | ||||
Sequence: RYPRWRPEVYSIICRDPVPVKEEKAGKPLTPAPSPAFSPTSGFNPTLGFSTPGFSSPVSSTPISPIFGPSNWHFMPPVSEVVPTQGADPLLYESLCSVPAPTSVQKWEDSAHPQRPDNADLAILYAVVDGVPPARWKEFMRFMGLSEHEIERLEMQNGRCLREAQYSMLEAWRRRTPRHEDTLEVVGLVLSKMNLAGCLENILEALRNPAPSSTTRLPR |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-29 | |||||
Sequence: MGLPTVPGLLLSLVLLALLMGIHPSGVTG | ||||||
Chain | PRO_0000034545 | 30-454 | Tumor necrosis factor receptor superfamily member 1A | |||
Sequence: LVPSLGDREKRDSLCPQGKYVHSKNNSICCTKCHKGTYLVSDCPSPGRDTVCRECEKGTFTASQNYLRQCLSCKTCRKEMSQVEISPCQADKDTVCGCKENQFQRYLSETHFQCVDCSPCFNGTVTIPCKETQNTVCNCHAGFFLRESECVPCSHCKKNEECMKLCLPPPLANVTNPQDSGTAVLLPLVILLGLCLLSFIFISLMCRYPRWRPEVYSIICRDPVPVKEEKAGKPLTPAPSPAFSPTSGFNPTLGFSTPGFSSPVSSTPISPIFGPSNWHFMPPVSEVVPTQGADPLLYESLCSVPAPTSVQKWEDSAHPQRPDNADLAILYAVVDGVPPARWKEFMRFMGLSEHEIERLEMQNGRCLREAQYSMLEAWRRRTPRHEDTLEVVGLVLSKMNLAGCLENILEALRNPAPSSTTRLPR | ||||||
Disulfide bond | 44↔58 | |||||
Sequence: CPQGKYVHSKNNSIC | ||||||
Glycosylation | 54 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 59↔72 | |||||
Sequence: CTKCHKGTYLVSDC | ||||||
Disulfide bond | 62↔81 | |||||
Sequence: CHKGTYLVSDCPSPGRDTVC | ||||||
Disulfide bond | 84↔99 | |||||
Sequence: CEKGTFTASQNYLRQC | ||||||
Disulfide bond | 102↔117 | |||||
Sequence: CKTCRKEMSQVEISPC | ||||||
Disulfide bond | 105↔125 | |||||
Sequence: CRKEMSQVEISPCQADKDTVC | ||||||
Disulfide bond | 127↔143 | |||||
Sequence: CKENQFQRYLSETHFQC | ||||||
Disulfide bond | 146↔158 | |||||
Sequence: CSPCFNGTVTIPC | ||||||
Disulfide bond | 149↔166 | |||||
Sequence: CFNGTVTIPCKETQNTVC | ||||||
Glycosylation | 151 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 168↔179 | |||||
Sequence: CHAGFFLRESEC | ||||||
Disulfide bond | 182↔195 | |||||
Sequence: CSHCKKNEECMKLC | ||||||
Disulfide bond | 185↔191 | |||||
Sequence: CKKNEEC | ||||||
Glycosylation | 202 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 376 | (Microbial infection) N-beta-linked (GlcNAc) arginine | ||||
Sequence: R |
Post-translational modification
(Microbial infection) Glycosylated at Arg-376 by S.typhimurium protein Ssek3: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
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. Interacts with DAB2IP (By similarity).
Interacts directly with NOL3 (via CARD domain); inhibits TNF-signaling pathway (PubMed:24440909).
Interacts with SH3RF2, TRADD and RIPK1. SH3RF2 facilitates the recruitment of RIPK1 and TRADD to TNFRSF1A in a TNF-alpha-dependent process (By similarity).
Interacts with PGLYRP1; this interaction is important for cell death induction (By similarity).
Interacts (via death domain) with MADD (via death domain) (By similarity).
Interacts directly with NOL3 (via CARD domain); inhibits TNF-signaling pathway (PubMed:24440909).
Interacts with SH3RF2, TRADD and RIPK1. SH3RF2 facilitates the recruitment of RIPK1 and TRADD to TNFRSF1A in a TNF-alpha-dependent process (By similarity).
Interacts with PGLYRP1; this interaction is important for cell death induction (By similarity).
Interacts (via death domain) with MADD (via death domain) (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P25118 | Ern1 Q9EQY0 | 2 | EBI-518014, EBI-5480799 | |
BINARY | P25118 | Ripk1 Q60855 | 4 | EBI-518014, EBI-529119 | |
BINARY | P25118 | Slc39a7 Q31125 | 3 | EBI-518014, EBI-644519 | |
XENO | P25118 | TNF P01375 | 4 | EBI-518014, EBI-359977 | |
BINARY | P25118 | Ubc P62991 | 2 | EBI-518014, EBI-413074 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 43-82 | TNFR-Cys 1 | ||||
Sequence: LCPQGKYVHSKNNSICCTKCHKGTYLVSDCPSPGRDTVCR | ||||||
Repeat | 83-125 | TNFR-Cys 2 | ||||
Sequence: ECEKGTFTASQNYLRQCLSCKTCRKEMSQVEISPCQADKDTVC | ||||||
Repeat | 126-166 | TNFR-Cys 3 | ||||
Sequence: GCKENQFQRYLSETHFQCVDCSPCFNGTVTIPCKETQNTVC | ||||||
Repeat | 167-196 | TNFR-Cys 4 | ||||
Sequence: NCHAGFFLRESECVPCSHCKKNEECMKLCL | ||||||
Region | 339-349 | N-SMase activation domain (NSD) | ||||
Sequence: VQKWEDSAHPQ | ||||||
Domain | 356-441 | Death | ||||
Sequence: LAILYAVVDGVPPARWKEFMRFMGLSEHEIERLEMQNGRCLREAQYSMLEAWRRRTPRHEDTLEVVGLVLSKMNLAGCLENILEAL |
Domain
Both the cytoplasmic membrane-proximal region and the C-terminal region containing the death domain are involved in the interaction with TRPC4AP.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length454
- Mass (Da)50,130
- Last updated1992-05-01 v1
- Checksum0710C2E8C3C2B6D9
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 394 | in Ref. 6; AAA40465 | ||||
Sequence: R → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M60468 EMBL· GenBank· DDBJ | AAA39751.1 EMBL· GenBank· DDBJ | mRNA | ||
M59377 EMBL· GenBank· DDBJ | AAA40464.1 EMBL· GenBank· DDBJ | mRNA | ||
X59238 EMBL· GenBank· DDBJ | CAA41922.1 EMBL· GenBank· DDBJ | mRNA | ||
X57796 EMBL· GenBank· DDBJ | CAA40936.1 EMBL· GenBank· DDBJ | mRNA | ||
L26349 EMBL· GenBank· DDBJ | AAA59361.1 EMBL· GenBank· DDBJ | mRNA | ||
M76656 EMBL· GenBank· DDBJ | AAA40465.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M88067 EMBL· GenBank· DDBJ | AAA40465.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M76655 EMBL· GenBank· DDBJ | AAA40465.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004599 EMBL· GenBank· DDBJ | AAH04599.1 EMBL· GenBank· DDBJ | mRNA | ||
BC052675 EMBL· GenBank· DDBJ | AAH52675.1 EMBL· GenBank· DDBJ | mRNA |