TNFRSF1B (Mus musculus)
Description [+]
- Synonyms: TNFRSF1B, TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 1B, CD120B, P75, P75 TNFR, TNF-ALPHAR2, TNF-R-II, TNF-R2, TNF-R75, TNFALPHA-R2, TNFBR, TNFR-1, TNFR2, TNFR80, TNFRII
- Species: Metazoa;Bilateria;Deuterostoma;Chordata;Vertebrata;Mammalia;Rodentia; Mus musculus
- Short gene description: Tumor necrosis factor receptor superfamily member 1B Precursor (Tumor necrosis factor receptor 2)(TNF-R2)(Tumor necrosis factor receptor type II)(p75)(p80 TNF-alpha receptor)(CD120b antigen) [Source:UniProtKB/Swiss-Prot;Acc:P25119]
- Family: death receptor
- Process: apoptosis, necroptosis,
- Pathways: extrinsic pathway, TNF/NF-kappaB signaling,
- Criteria: manually curated
- Curator comment:
- WIKI: TNFRSF1B-M_musculus
References [+]
- Molecular cloning and expression of the type 1 and type 2 murine receptors for tumor necrosis factor.
- Goodwin RG, Anderson D, Jerzy R, Davis T, Brannan CI, Copeland NG, Jenkins NA, Smith CA
- Clones encoding the type 1 (p80) and type 2 (p60) forms of the murine receptors for tumor necrosis factor (TNF) were isolated by cross-hybridization using probes derived from the cloned human TNF receptors. Each of the murine receptors shows strong sequence homology to the corresponding human receptor (approximately 65% amino acid identity) throughout the molecule but only modest homology, limited to ligand-binding domains, between themselves. The ligand-binding characteristics of the recombinant murine receptors mirror those of the human homologs: both receptor types bind TNF-alpha and -beta with multiple affinity classes, and the ligands cross-compete. Analysis of the murine transcripts encoding these receptors revealed the presence of RNAs for one or both forms of the receptors in all cells examined. It was also demonstrated that for both types of human TNF receptor, variably sized transcripts are observed in different cells. The murine cDNAs were further used to determine the chromosomal locations of the TNF receptor genes. They are not linked, in contrast to the ligands, and map to chromosomes 4 (type 1) and 6 (type 2). Mol Cell Biol. 1991 Jun;11(6):3020-6.
- A role for tumor necrosis factor receptor-2 and receptor-interacting protein in programmed necrosis and antiviral responses.
- Chan FK, Shisler J, Bixby JG, Felices M, Zheng L, Appel M, Orenstein J, Moss B, Lenardo MJ
- Members of the tumor necrosis factor (TNF) receptor (TNFR) superfamily are potent regulators of apoptosis, a process that is important for the maintenance of immune homeostasis. Recent evidence suggests that TNFR-1 and Fas and TRAIL receptors can also trigger an alternative form of cell death that is morphologically distinct from apoptosis. Because distinct molecular components including the serine/threonine protein kinase receptor-interacting protein (RIP) are required, we have referred to this alternative form of cell death as programmed necrosis. We show that TNFR-2 signaling can potentiate programmed necrosis via TNFR-1. When cells were pre-stimulated through TNFR-2 prior to subsequent activation of TNFR-1, enhanced cell death and recruitment of RIP to the TNFR-1 complex were observed. However, TNF-induced programmed necrosis was normally inhibited by caspase-8 cleavage of RIP. To ascertain the physiological significance of RIP and programmed necrosis, we infected Jurkat cells with vaccinia virus (VV) and found that VV-infected cells underwent programmed necrosis in response to TNF, but deficiency of RIP rescued the infected cells from TNF-induced cytotoxicity. Moreover, TNFR-2-/- mice exhibited reduced inflammation in the liver and defective viral clearance during VV infection. Interestingly, death effector domain-containing proteins such as MC159, E8, K13, and cellular FLIP, but not the apoptosis inhibitors Bcl-xL, p35, and XIAP, potently suppressed programmed necrosis. Thus, TNF-induced programmed necrosis is facilitated by TNFR-2 signaling and caspase inhibition and may play a role in controlling viral infection. J Biol Chem. 2003 Dec 19;278(51):51613-21. Epub 2003 Oct 7.
Structure & Sequence [+]
Pfam domains:
(Pfam is a large collection of protein families.)
Source | Domain Name | Start | End |
---|---|---|---|
PFAM A | TNFR_c6 | 40 | 76 |
PFAM A | TNFR_c6 | 79 | 119 |
Protein sequence [+]
Tnfrsf1b | Mus musculus | 10090 | length:474
MAPAALWVALVFELQLWATGHTVPAQVVLTPYKPEPGYECQISQEYYDRKAQMCCAKCPP
GQYVKHFCNKTSDTVCADCEASMYTQVWNQFRTCLSCSSSCTTDQVEIRACTKQQNRVCA
CEAGRYCALKTHSGSCRQCMRLSKCGPGFGVASSRAPNGNVLCKACAPGTFSDTTSSTDV
CRPHRICSILAIPGNASTDAVCAPESPTLSAIPRTLYVSQPEPTRSQPLDQEPGPSQTPS
ILTSLGSTPIIEQSTKGGISLPIGLIVGVTSLGLLMLGLVNCIILVQRKKKPSCLQRDAK
VPHVPDEKSQDAVGLEQQHLLTTAPSSSSSSLESSASAGDRRAPPGGHPQARVMAEAQGF
QEARASSRISDSSHGSHGTHVNVTCIVNVCSSSDHSSQCSSQASATVGDPDAKPSASPKD
EQVPFSQEECPSQSPCETTETLQSHEKPLPLGVPDMGMKPSQAGWFDQIAVKVA
GQYVKHFCNKTSDTVCADCEASMYTQVWNQFRTCLSCSSSCTTDQVEIRACTKQQNRVCA
CEAGRYCALKTHSGSCRQCMRLSKCGPGFGVASSRAPNGNVLCKACAPGTFSDTTSSTDV
CRPHRICSILAIPGNASTDAVCAPESPTLSAIPRTLYVSQPEPTRSQPLDQEPGPSQTPS
ILTSLGSTPIIEQSTKGGISLPIGLIVGVTSLGLLMLGLVNCIILVQRKKKPSCLQRDAK
VPHVPDEKSQDAVGLEQQHLLTTAPSSSSSSLESSASAGDRRAPPGGHPQARVMAEAQGF
QEARASSRISDSSHGSHGTHVNVTCIVNVCSSSDHSSQCSSQASATVGDPDAKPSASPKD
EQVPFSQEECPSQSPCETTETLQSHEKPLPLGVPDMGMKPSQAGWFDQIAVKVA
Structure links:
Evolution [+]
View protein alignment and tree with Jalview:  
Explore tree at phylomeDB:   Click here.
Homologs list [+]
Name | Relationship | Species |
---|
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Gene Ontology [+]
GO id | Name | Ontology type | Evidence |
---|---|---|---|
GO:0006955 | immune response | biological_proccess | IEA |
GO:0007166 | cell surface receptor linked signal transduction | biological_proccess | IMP |
GO:0008219 | cell death | biological_proccess | IMP |
GO:0008283 | cell proliferation | biological_proccess | TAS |
GO:0050728 | negative regulation of inflammatory response | biological_proccess | IMP |
GO:0050779 | RNA destabilization | biological_proccess | IMP |
GO:0006954 | inflammatory response | biological_proccess | IMP |
GO:0004872 | receptor activity | mollecular_function | IEA |
GO:0005031 | tumor necrosis factor receptor activity | mollecular_function | IPI |
GO:0005515 | protein binding | mollecular_function | IPI |
GO:0005515 | protein binding | mollecular_function | IEA |
GO:0005624 | membrane fraction | cell_component | IEA |
GO:0016020 | membrane | cell_component | IDA |
GO:0016021 | integral to membrane | cell_component | IEA |
GO:0045121 | membrane raft | cell_component | IDA |
GO:0045121 | membrane raft | cell_component | IEA |
Check GO Evidence Codes here
KEGG Pathways [+]
Curated Isoforms [+]
Transcript | Translation |
---|---|
OTTMUST00000023284 * | OTTMUSP00000010647 * |
OTTMUST00000023285 | OTTMUSP00000035231 |
Info from The Vertebrate Genome Annotation (VEGA) database.
(*) Canonical transcript and translation forms.
Information from other databases [+]
- Gene info from MGI [?] MGI:1314883
- Ensembl genome browser [?] : ENSMUSG00000028599
- Expression info from Arrayexpress [?] : ENSMUSG00000028599
- Protein expression from Protein Atlas: [?] ENSMUSG00000028599
- Community gene edition from Wikigenes: [?] 21938
Click on [?] for more information.