Tumor necrosis factor receptor 1

Membrane receptor protein found in humans

TNFRSF1A
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1EXT, 1FT4, 1ICH, 1NCF, 1TNR

Identifiers
AliasesTNFRSF1A, CD120a, FPF, MS5, TBP1, TNF-R, TNF-R-I, TNF-R55, TNFAR, TNFR1, TNFR1-d2, TNFR55, TNFR60, p55, p55-R, p60, tumor necrosis factor receptor superfamily member 1A, TNF receptor superfamily member 1A
External IDsOMIM: 191190; MGI: 1314884; HomoloGene: 828; GeneCards: TNFRSF1A; OMA:TNFRSF1A - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for TNFRSF1A
Genomic location for TNFRSF1A
Band12p13.31Start6,328,757 bp[1]
End6,342,114 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for TNFRSF1A
Genomic location for TNFRSF1A
Band6 F3|6 59.32 cMStart125,326,325 bp[2]
End125,339,447 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • tendon of biceps brachii

  • gallbladder

  • left uterine tube

  • epithelium of colon

  • right coronary artery

  • upper lobe of left lung

  • left adrenal cortex

  • Descending thoracic aorta

  • pericardium

  • blood
Top expressed in
  • granulocyte

  • tibiofemoral joint

  • saccule

  • lip

  • stroma of bone marrow

  • otic placode

  • esophagus

  • calvaria

  • otic vesicle

  • ankle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein binding
  • tumor necrosis factor-activated receptor activity
  • tumor necrosis factor binding
  • identical protein binding
Cellular component
  • integral component of membrane
  • Golgi apparatus
  • membrane
  • Golgi membrane
  • receptor complex
  • plasma membrane
  • integral component of plasma membrane
  • extracellular region
  • cell surface
  • mitochondrion
  • membrane raft
  • extracellular space
  • tumor necrosis factor receptor superfamily complex
Biological process
  • regulation of apoptotic process
  • prostaglandin metabolic process
  • defense response
  • positive regulation of ceramide biosynthetic process
  • positive regulation of inflammatory response
  • regulation of tumor necrosis factor-mediated signaling pathway
  • tumor necrosis factor-mediated signaling pathway
  • response to lipopolysaccharide
  • cellular response to mechanical stimulus
  • death-inducing signaling complex assembly
  • regulation of cell population proliferation
  • defense response to bacterium
  • immune response
  • intrinsic apoptotic signaling pathway in response to DNA damage
  • positive regulation of I-kappaB kinase/NF-kappaB signaling
  • viral process
  • I-kappaB kinase/NF-kappaB signaling
  • negative regulation of inflammatory response
  • regulation of establishment of endothelial barrier
  • extrinsic apoptotic signaling pathway via death domain receptors
  • positive regulation of transcription by RNA polymerase II
  • signal transduction
  • apoptotic process
  • inflammatory response
  • cell surface receptor signaling pathway
  • positive regulation of tyrosine phosphorylation of STAT protein
  • protein localization to plasma membrane
  • cytokine-mediated signaling pathway
  • aortic valve development
  • pulmonary valve development
  • negative regulation of extracellular matrix constituent secretion
  • negative regulation of cardiac muscle hypertrophy
  • positive regulation of apoptotic process involved in morphogenesis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7132

21937

Ensembl

ENSG00000067182

ENSMUSG00000030341

UniProt

P19438

P25118

RefSeq (mRNA)

NM_001065
NM_001346091
NM_001346092

NM_011609

RefSeq (protein)

NP_001056
NP_001333020
NP_001333021

NP_035739

Location (UCSC)Chr 12: 6.33 – 6.34 MbChr 6: 125.33 – 125.34 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tumor necrosis factor receptor 1 (TNFR1), also known as tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) and CD120a, is a ubiquitous membrane receptor that binds tumor necrosis factor-alpha (TNFα).[5][6][7]

Function

The protein encoded by this gene is a member of the tumor necrosis factor receptor superfamily, which also contains TNFRSF1B. This protein is one of the major receptors for the tumor necrosis factor-alpha. This receptor can activate the transcription factor NF-κB, mediate apoptosis, and function as a regulator of inflammation. Antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with this receptor, and thus play regulatory roles in the signal transduction mediated by the receptor.[8]

Clinical significance

Germline mutations of the extracellular domains of this receptor were found to be associated with the human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS) or periodic fever syndrome.[9] Impaired receptor clearance is thought to be a mechanism of the disease.

Mutations in the TNFRSF1A gene are associated with elevated risk of multiple sclerosis.[10]

Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder,[11] and high levels are associated with more severe psychotic symptoms.[12]

High serum levels are also associated with cognitive impairment and dementia.[13][14]

Interactions

TNFRSF1A has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000067182 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030341 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Baker E, Chen LZ, Smith CA, Callen DF, Goodwin R, Sutherland GR (November 1991). "Chromosomal location of the human tumor necrosis factor receptor genes". Cytogenetics and Cell Genetics. 57 (2–3): 117–118. doi:10.1159/000133127. PMID 1655358.
  6. ^ Schall TJ, Lewis M, Koller KJ, Lee A, Rice GC, Wong GH, et al. (April 1990). "Molecular cloning and expression of a receptor for human tumor necrosis factor". Cell. 61 (2): 361–370. doi:10.1016/0092-8674(90)90816-W. PMID 2158863. S2CID 36187863.
  7. ^ Offermanns S, Rosenthal W (2008). Encyclopedia of Molecular Pharmacology. Vol. 1 (2nd ed.). Heidelberg, Germany: Springer. p. 1248. ISBN 9783540389163.
  8. ^ "Entrez Gene: TNFRSF1A tumor necrosis factor receptor superfamily, member 1A".
  9. ^ Kümpfel T, Hohlfeld R (October 2009). "Multiple sclerosis. TNFRSF1A, TRAPS and multiple sclerosis". Nature Reviews. Neurology. 5 (10): 528–529. doi:10.1038/nrneurol.2009.154. PMID 19794511. S2CID 40665495.
  10. ^ International Multiple Sclerosis Genetics Consortium (April 2011). "The genetic association of variants in CD6, TNFRSF1A and IRF8 to multiple sclerosis: a multicenter case-control study". PLOS ONE. 6 (4): e18813. Bibcode:2011PLoSO...618813.. doi:10.1371/journal.pone.0018813. PMC 3084233. PMID 21552549.
  11. ^ Hope S, Melle I, Aukrust P, Steen NE, Birkenaes AB, Lorentzen S, et al. (November 2009). "Similar immune profile in bipolar disorder and schizophrenia: selective increase in soluble tumor necrosis factor receptor I and von Willebrand factor". Bipolar Disorders. 11 (7): 726–734. doi:10.1111/j.1399-5618.2009.00757.x. hdl:10852/34620. PMID 19839997.
  12. ^ Hope S, Ueland T, Steen NE, Dieset I, Lorentzen S, Berg AO, et al. (April 2013). "Interleukin 1 receptor antagonist and soluble tumor necrosis factor receptor 1 are associated with general severity and psychotic symptoms in schizophrenia and bipolar disorder". Schizophrenia Research. 145 (1–3): 36–42. doi:10.1016/j.schres.2012.12.023. PMID 23403415.
  13. ^ Buchhave P, Zetterberg H, Blennow K, Minthon L, Janciauskiene S, Hansson O (November 2010). "Soluble TNF receptors are associated with Aβ metabolism and conversion to dementia in subjects with mild cognitive impairment". Neurobiology of Aging. 31 (11): 1877–1884. doi:10.1016/j.neurobiolaging.2008.10.012. PMID 19070941. S2CID 34595960.
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  17. ^ a b Gajate C, Mollinedo F (March 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". The Journal of Biological Chemistry. 280 (12): 11641–11647. doi:10.1074/jbc.M411781200. PMID 15659383.
  18. ^ Vincenz C, Dixit VM (March 1997). "Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling". The Journal of Biological Chemistry. 272 (10): 6578–6583. doi:10.1074/jbc.272.10.6578. PMID 9045686.
  19. ^ a b c Hsu H, Shu HB, Pan MG, Goeddel DV (January 1996). "TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways". Cell. 84 (2): 299–308. doi:10.1016/S0092-8674(00)80984-8. PMID 8565075. S2CID 13171355.
  20. ^ Zhang SQ, Kovalenko A, Cantarella G, Wallach D (March 2000). "Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation". Immunity. 12 (3): 301–311. doi:10.1016/S1074-7613(00)80183-1. PMID 10755617.
  21. ^ Chaudhary PM, Eby MT, Jasmin A, Kumar A, Liu L, Hood L (September 2000). "Activation of the NF-kappaB pathway by caspase 8 and its homologs". Oncogene. 19 (39): 4451–4460. doi:10.1038/sj.onc.1203812. PMID 11002417.
  22. ^ a b Guo D, Dunbar JD, Yang CH, Pfeffer LM, Donner DB (March 1998). "Induction of Jak/STAT signaling by activation of the type 1 TNF receptor". Journal of Immunology. 160 (6): 2742–2750. doi:10.4049/jimmunol.160.6.2742. PMID 9510175.
  23. ^ Miscia S, Marchisio M, Grilli A, Di Valerio V, Centurione L, Sabatino G, et al. (January 2002). "Tumor necrosis factor alpha (TNF-alpha) activates Jak1/Stat3-Stat5B signaling through TNFR-1 in human B cells". Cell Growth & Differentiation. 13 (1): 13–18. PMID 11801527.
  24. ^ Castellino AM, Parker GJ, Boronenkov IV, Anderson RA, Chao MV (February 1997). "A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase". The Journal of Biological Chemistry. 272 (9): 5861–5870. doi:10.1074/jbc.272.9.5861. PMID 9038203.
  25. ^ Boldin MP, Mett IL, Wallach D (June 1995). "A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its 'death domain'". FEBS Letters. 367 (1): 39–44. Bibcode:1995FEBSL.367...39B. doi:10.1016/0014-5793(95)00534-G. PMID 7601280. S2CID 21442471.
  26. ^ Dunbar JD, Song HY, Guo D, Wu LW, Donner DB (May 1997). "Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a protein that interacts with the intracellular domain of the type 1 TNF receptor: identity with subunit 2 of the 26S protease". Journal of Immunology. 158 (9): 4252–4259. doi:10.4049/jimmunol.158.9.4252. PMID 9126987.
  27. ^ a b c Hsu H, Huang J, Shu HB, Baichwal V, Goeddel DV (April 1996). "TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex". Immunity. 4 (4): 387–396. doi:10.1016/S1074-7613(00)80252-6. PMID 8612133.
  28. ^ Kim JW, Choi EJ, Joe CO (September 2000). "Activation of death-inducing signaling complex (DISC) by pro-apoptotic C-terminal fragment of RIP". Oncogene. 19 (39): 4491–4499. doi:10.1038/sj.onc.1203796. PMID 11002422.
  29. ^ Duan H, Dixit VM (January 1997). "RAIDD is a new 'death' adaptor molecule". Nature. 385 (6611): 86–89. Bibcode:1997Natur.385...86D. doi:10.1038/385086a0. hdl:2027.42/62739. PMID 8985253. S2CID 4317538.
  30. ^ a b Blankenship JW, Varfolomeev E, Goncharov T, Fedorova AV, Kirkpatrick DS, Izrael-Tomasevic A, et al. (January 2009). "Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2(1)". The Biochemical Journal. 417 (1): 149–160. doi:10.1042/BJ20081885. PMID 18939944.
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  33. ^ Liou ML, Liou HC (April 1999). "The ubiquitin-homology protein, DAP-1, associates with tumor necrosis factor receptor (p60) death domain and induces apoptosis". The Journal of Biological Chemistry. 274 (15): 10145–10153. doi:10.1074/jbc.274.15.10145. PMID 10187798.
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Further reading

  • Rath PC, Aggarwal BB (November 1999). "TNF-induced signaling in apoptosis". Journal of Clinical Immunology. 19 (6): 350–364. doi:10.1023/A:1020546615229. PMID 10634209. S2CID 23194856.
  • Chen G, Goeddel DV (May 2002). "TNF-R1 signaling: a beautiful pathway". Science. 296 (5573): 1634–1635. Bibcode:2002Sci...296.1634C. doi:10.1126/science.1071924. PMID 12040173. S2CID 25321662.
  • Kollias G, Kontoyiannis D (2003). "Role of TNF/TNFR in autoimmunity: specific TNF receptor blockade may be advantageous to anti-TNF treatments". Cytokine & Growth Factor Reviews. 13 (4–5): 315–321. doi:10.1016/S1359-6101(02)00019-9. PMID 12220546.
  • Dodé C, Cuisset L, Delpech M, Grateau G (2003). "TNFRSF1A-associated periodic syndrome (TRAPS), Muckle-Wells syndrome (MWS) and renal amyloidosis". Journal of Nephrology. 16 (3): 435–437. PMID 12832748.
  • Stojanov S, McDermott MF (October 2005). "The tumour necrosis factor receptor-associated periodic syndrome: current concepts". Expert Reviews in Molecular Medicine. 7 (22): 1–18. doi:10.1017/S1462399405009749. PMID 16216134. S2CID 35803989.
  • Rezaei N (November 2006). "TNF-receptor-associated periodic syndrome (TRAPS): an autosomal dominant multisystem disorder". Clinical Rheumatology. 25 (6): 773–777. doi:10.1007/s10067-005-0198-6. PMID 16447098. S2CID 41808394.
  • TNFRSF1A+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • Overview of all the structural information available in the PDB for UniProt: P19438 (Tumor necrosis factor receptor superfamily member 1A) at the PDBe-KB.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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  • 1ext: EXTRACELLULAR DOMAIN OF THE 55KDA TUMOR NECROSIS FACTOR RECEPTOR. CRYSTALLIZED AT PH3.7 IN P 21 21 21.
    1ext: EXTRACELLULAR DOMAIN OF THE 55KDA TUMOR NECROSIS FACTOR RECEPTOR. CRYSTALLIZED AT PH3.7 IN P 21 21 21.
  • 1ft4: PHOTOCHEMICALLY-ENHANCED BINDING OF SMALL MOLECULES TO THE TUMOR NECROSIS FACTOR RECEPTOR-1
    1ft4: PHOTOCHEMICALLY-ENHANCED BINDING OF SMALL MOLECULES TO THE TUMOR NECROSIS FACTOR RECEPTOR-1
  • 1ich: SOLUTION STRUCTURE OF THE TUMOR NECROSIS FACTOR RECEPTOR-1 DEATH DOMAIN
    1ich: SOLUTION STRUCTURE OF THE TUMOR NECROSIS FACTOR RECEPTOR-1 DEATH DOMAIN
  • 1ncf: A NEW PARADIGM FOR TUMOR NECROSIS FACTOR SIGNALLING
    1ncf: A NEW PARADIGM FOR TUMOR NECROSIS FACTOR SIGNALLING
  • 1tnr: CRYSTAL STRUCTURE OF THE SOLUBLE HUMAN 55 KD TNF RECEPTOR-HUMAN TNF-BETA COMPLEX: IMPLICATIONS FOR TNF RECEPTOR ACTIVATION
    1tnr: CRYSTAL STRUCTURE OF THE SOLUBLE HUMAN 55 KD TNF RECEPTOR-HUMAN TNF-BETA COMPLEX: IMPLICATIONS FOR TNF RECEPTOR ACTIVATION
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1–50
51–100
101–150
151–200
201–250
251–300
301–350
  • v
  • t
  • e
Chemokine receptor
(GPCRs)
CC
CXC
Other
TNF receptor
1-10
11-20
21-27
JAK-STAT
Type I
γ-chain
β-chain
gp130
IL12RB1
Other
Type II
Ig superfamily
IL 17 family
Enzyme-linked receptor
  • v
  • t
  • e
TNF receptor superfamily modulators
LTB (TNFβ)
  • Decoy receptors: Baminercept
TNF (TNFα)
TNFR1
TNFR2
Ungrouped
Others
  • Recombinant proteins: Ardenermin
  • Dulanermin
  • Decoy receptors: Briobacept
  • Unsorted: Tengonermin