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Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]

 TNFA_MOUSE              Reviewed;         235 AA.
P06804; O35853; Q62326; Q91VF3;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
05-DEC-2018, entry version 201.
RecName: Full=Tumor necrosis factor;
AltName: Full=Cachectin;
AltName: Full=TNF-alpha;
AltName: Full=Tumor necrosis factor ligand superfamily member 2;
Short=TNF-a;
Contains:
RecName: Full=Tumor necrosis factor, membrane form;
AltName: Full=N-terminal fragment;
Short=NTF;
Contains:
RecName: Full=Intracellular domain 1;
Short=ICD1;
Contains:
RecName: Full=Intracellular domain 2;
Short=ICD2;
Contains:
RecName: Full=C-domain 1;
Contains:
RecName: Full=C-domain 2;
Contains:
RecName: Full=Tumor necrosis factor, soluble form;
Flags: Precursor;
Name=Tnf; Synonyms=Tnfa, Tnfsf2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2836146; DOI=10.1089/dna.1988.7.193;
Shirai T., Shimizu N., Shiojiri S., Horiguchi S., Ito H.;
"Cloning and expression in Escherichia coli of the gene for mouse
tumor necrosis factor.";
DNA 7:193-201(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3898078; DOI=10.1073/pnas.82.18.6060;
Pennica D., Hayflick J.S., Bringman T.S., Palladino M.A.,
Goeddel D.V.;
"Cloning and expression in Escherichia coli of the cDNA for murine
tumor necrosis factor.";
Proc. Natl. Acad. Sci. U.S.A. 82:6060-6064(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2419912; DOI=10.1073/pnas.83.6.1670;
Caput D., Beutler B., Hartog K., Thayer R., Brown-Shimer S.,
Cerami A.;
"Identification of a common nucleotide sequence in the 3'-untranslated
region of mRNA molecules specifying inflammatory mediators.";
Proc. Natl. Acad. Sci. U.S.A. 83:1670-1674(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2989794; DOI=10.1093/nar/13.12.4417;
Fransen L., Mueller R., Marmenout A., Tavernier J., van der Heyden J.,
Kawashima E., Chollet A., Tizard R., van Heuverswyn H., van Vliet A.,
Ruysschaert M.-R., Fiers W.;
"Molecular cloning of mouse tumour necrosis factor cDNA and its
eukaryotic expression.";
Nucleic Acids Res. 13:4417-4429(1985).
[5]
NUCLEOTIDE SEQUENCE.
PubMed=3040015;
Shakhov A.N., Nedospasov S.A.;
"Molecular cloning of genes coding for tumor necrosis factor. Complete
nucleotide sequence of the genome copy of TNF-alpha in mice.";
Bioorg. Khim. 13:701-705(1987).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3684584; DOI=10.1093/nar/15.21.9083;
Semon D., Kawashima E., Jongeneel C.V., Shakhov A.N., Nedospasov S.A.;
"Nucleotide sequence of the murine TNF locus, including the TNF-alpha
(tumor necrosis factor) and TNF-beta (lymphotoxin) genes.";
Nucleic Acids Res. 15:9083-9084(1987).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CTS, and NOD;
PubMed=7560085; DOI=10.1172/JCI118239;
Ikegami H., Makino S., Yamato E., Kawaguchi Y., Ueda H., Sakamoto T.,
Takekawa K., Ogihara T.;
"Identification of a new susceptibility locus for insulin-dependent
diabetes mellitus by ancestral haplotype congenic mapping.";
J. Clin. Invest. 96:1936-1942(1995).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-7 AND ALA-77.
STRAIN=A/J, BALB/cJ, and C57BL/6J;
PubMed=9089109; DOI=10.1007/s002510050233;
Iraqi F., Teale A.;
"Cloning and sequencing of the Tnfa genes of three inbred mouse
strains.";
Immunogenetics 45:459-461(1997).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129;
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[10]
NUCLEOTIDE SEQUENCE OF 1-96.
STRAIN=BFM/2Msf, BLG2/Msf, C57BL/10SnJ, CAST/EiJ, HMI/Msf, MSM/Msf,
NJL/Msf, pgn2, and SWN/Msf;
Liu Y., Kitano T., Koide T., Shiroishi T., Moriwaki K., Saitou N.;
"Conspicuous differences among gene genealogies of 21 nuclear genes of
five Mus musculus subspecies.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 70-87.
PubMed=2777790;
Cseh K., Beutler B.;
"Alternative cleavage of the cachectin/tumor necrosis factor
propeptide results in a larger, inactive form of secreted protein.";
J. Biol. Chem. 264:16256-16260(1989).
[12]
PROTEIN SEQUENCE OF 80-99.
PubMed=2268312; DOI=10.1016/S0006-291X(05)80895-2;
Sherry B., Juc D.-M., Zentella A., Cerami A.;
"Characterization of high molecular weight glycosylated forms of
murine tumor necrosis factor.";
Biochem. Biophys. Res. Commun. 173:1072-1078(1990).
[13]
IDENTIFICATION OF MEMBRANE-BOUND FORM.
PubMed=3349526; DOI=10.1016/0092-8674(88)90486-2;
Kriegler M., Perez X., Defay K., Albert I., Lu S.D.;
"A novel form of TNF/cachectin is a cell surface cytotoxic
transmembrane protein: ramifications for the complex physiology of
TNF.";
Cell 53:45-53(1988).
[14]
FUNCTION.
PubMed=25586176; DOI=10.1074/jbc.M114.624759;
Ando Y., Shinozawa Y., Iijima Y., Yu B.C., Sone M., Ooi Y.,
Watanaka Y., Chida K., Hakuno F., Takahashi S.;
"Tumor necrosis factor (TNF)-alpha-induced repression of GKAP42
protein levels through cGMP-dependent kinase (cGK)-Ialpha causes
insulin resistance in 3T3-L1 adipocytes.";
J. Biol. Chem. 290:5881-5892(2015).
[15]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 80-235.
PubMed=10089307; DOI=10.1107/S0907444998018435;
Baeyens K.J., De Bondt H.L., Raeymaekers A., Fiers W., De Ranter C.J.;
"The structure of mouse tumour-necrosis factor at 1.4 A resolution:
towards modulation of its selectivity and trimerization.";
Acta Crystallogr. D 55:772-778(1999).
-!- FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and
TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can
induce cell death of certain tumor cell lines. It is potent
pyrogen causing fever by direct action or by stimulation of
interleukin-1 secretion and is implicated in the induction of
cachexia, Under certain conditions it can stimulate cell
proliferation and induce cell differentiation (By similarity).
Induces insulin resistance in adipocytes via inhibition of
insulin-induced IRS1 tyrosine phosphorylation and insulin-induced
glucose uptake. Induces GKAP42 protein degradation in adipocytes
which is partially responsible for TNF-induced insulin resistance
(PubMed:25586176). {ECO:0000250|UniProtKB:P01375,
ECO:0000269|PubMed:25586176}.
-!- FUNCTION: The TNF intracellular domain (ICD) form induces IL12
production in dendritic cells. {ECO:0000250|UniProtKB:P01375}.
-!- SUBUNIT: Interacts with SPPL2B (By similarity). Homotrimer.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein.
-!- SUBCELLULAR LOCATION: Tumor necrosis factor, membrane form:
Membrane {ECO:0000250}; Single-pass type II membrane protein
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Tumor necrosis factor, soluble form:
Secreted.
-!- SUBCELLULAR LOCATION: C-domain 1: Secreted {ECO:0000250}.
-!- SUBCELLULAR LOCATION: C-domain 2: Secreted {ECO:0000250}.
-!- PTM: The membrane-bound form is further proteolytically processed
by SPPL2A or SPPL2B through regulated intramembrane proteolysis
producing TNF intracellular domains (ICD1 and ICD2) released in
the cytosol and TNF C-domain 1 and C-domain 2 secreted into the
extracellular space (By similarity). The soluble form derives from
the membrane form by proteolytic processing. {ECO:0000250}.
-!- PTM: The membrane form, but not the soluble form, is
phosphorylated on serine residues. Dephosphorylation of the
membrane form occurs by binding to soluble TNFRSF1A/TNFR1 (By
similarity). {ECO:0000250}.
-!- PTM: O-glycosylated; glycans contain galactose, N-
acetylgalactosamine and N-acetylneuraminic acid. {ECO:0000250}.
-!- SIMILARITY: Belongs to the tumor necrosis factor family.
{ECO:0000305}.
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EMBL; M20155; AAA40462.1; ALT_SEQ; Genomic_DNA.
EMBL; M11731; AAA40458.1; -; mRNA.
EMBL; M13049; AAA40457.1; -; mRNA.
EMBL; X02611; CAA26457.1; -; mRNA.
EMBL; M38296; AAA40459.1; -; Genomic_DNA.
EMBL; Y00467; CAA68530.1; -; Genomic_DNA.
EMBL; U06950; AAA18594.1; -; Unassigned_DNA.
EMBL; D84196; BAA19512.1; -; Genomic_DNA.
EMBL; D84199; BAA19513.1; -; Genomic_DNA.
EMBL; U68414; AAB65593.1; -; Genomic_DNA.
EMBL; AF109719; AAC82484.1; -; Genomic_DNA.
EMBL; AB039224; BAB68748.1; ALT_SEQ; Genomic_DNA.
EMBL; AB039225; BAB68749.1; ALT_SEQ; Genomic_DNA.
EMBL; AB039226; BAB68750.1; ALT_SEQ; Genomic_DNA.
EMBL; AB039227; BAB68751.1; ALT_SEQ; Genomic_DNA.
EMBL; AB039228; BAB68752.1; ALT_SEQ; Genomic_DNA.
EMBL; AB039229; BAB68753.1; ALT_SEQ; Genomic_DNA.
EMBL; AB039230; BAB68754.1; ALT_SEQ; Genomic_DNA.
EMBL; AB039231; BAB68755.1; ALT_SEQ; Genomic_DNA.
EMBL; AB039232; BAB68756.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS28691.1; -.
PIR; A22908; QWMSN.
RefSeq; NP_001265530.1; NM_001278601.1.
RefSeq; NP_038721.1; NM_013693.3.
UniGene; Mm.1293; -.
PDB; 2TNF; X-ray; 1.40 A; A/B/C=80-234.
PDBsum; 2TNF; -.
ProteinModelPortal; P06804; -.
SMR; P06804; -.
BioGrid; 204240; 13.
DIP; DIP-40029N; -.
IntAct; P06804; 2.
STRING; 10090.ENSMUSP00000025263; -.
ChEMBL; CHEMBL4984; -.
iPTMnet; P06804; -.
PhosphoSitePlus; P06804; -.
SwissPalm; P06804; -.
EPD; P06804; -.
PaxDb; P06804; -.
PRIDE; P06804; -.
Ensembl; ENSMUST00000025263; ENSMUSP00000025263; ENSMUSG00000024401.
GeneID; 21926; -.
KEGG; mmu:21926; -.
UCSC; uc008cgr.2; mouse.
CTD; 7124; -.
MGI; MGI:104798; Tnf.
eggNOG; ENOG410ISAN; Eukaryota.
eggNOG; ENOG410YQC4; LUCA.
GeneTree; ENSGT00940000153265; -.
HOGENOM; HOG000048729; -.
HOVERGEN; HBG012516; -.
InParanoid; P06804; -.
KO; K03156; -.
OMA; QLQWLSR; -.
OrthoDB; EOG091G0HIG; -.
PhylomeDB; P06804; -.
TreeFam; TF332169; -.
Reactome; R-MMU-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-MMU-5626978; TNFR1-mediated ceramide production.
Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-MMU-75893; TNF signaling.
EvolutionaryTrace; P06804; -.
PMAP-CutDB; P06804; -.
PRO; PR:P06804; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024401; Expressed in 74 organ(s), highest expression level in epididymal fat pad.
CleanEx; MM_TNF; -.
ExpressionAtlas; P06804; baseline and differential.
Genevisible; P06804; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0001891; C:phagocytic cup; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0055037; C:recycling endosome; IDA:BHF-UCL.
GO; GO:0030141; C:secretory granule; TAS:MGI.
GO; GO:0005125; F:cytokine activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IDA:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0000187; P:activation of MAPK activity; ISO:MGI.
GO; GO:0000185; P:activation of MAPKKK activity; ISO:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
GO; GO:0001775; P:cell activation; ISO:MGI.
GO; GO:0008283; P:cell proliferation; TAS:MGI.
GO; GO:0045123; P:cellular extravasation; IDA:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0071316; P:cellular response to nicotine; ISO:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
GO; GO:0002439; P:chronic inflammatory response to antigenic stimulus; ISO:MGI.
GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:MGI.
GO; GO:0006952; P:defense response; IMP:MGI.
GO; GO:0042742; P:defense response to bacterium; IDA:MGI.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IGI:MGI.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:MGI.
GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
GO; GO:0072577; P:endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; IDA:MGI.
GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IGI:MGI.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IGI:MGI.
GO; GO:0006006; P:glucose metabolic process; IDA:MGI.
GO; GO:0006959; P:humoral immune response; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IGI:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
GO; GO:0007254; P:JNK cascade; IGI:MGI.
GO; GO:0050900; P:leukocyte migration; IDA:MGI.
GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:MGI.
GO; GO:0000165; P:MAPK cascade; ISO:MGI.
GO; GO:0007275; P:multicellular organism development; IMP:MGI.
GO; GO:0097527; P:necroptotic signaling pathway; IGI:MGI.
GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; IDA:BHF-UCL.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; ISO:MGI.
GO; GO:0061048; P:negative regulation of branching involved in lung morphogenesis; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0002740; P:negative regulation of cytokine secretion involved in immune response; ISO:MGI.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:BHF-UCL.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IDA:MGI.
GO; GO:0046325; P:negative regulation of glucose import; IDA:MGI.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IGI:MGI.
GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:MGI.
GO; GO:0002037; P:negative regulation of L-glutamate import across plasma membrane; ISO:MGI.
GO; GO:0050995; P:negative regulation of lipid catabolic process; ISO:MGI.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0031642; P:negative regulation of myelination; ISO:MGI.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:MGI.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; ISO:MGI.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:BHF-UCL.
GO; GO:0043242; P:negative regulation of protein complex disassembly; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
GO; GO:0030316; P:osteoclast differentiation; IGI:MGI.
GO; GO:0045760; P:positive regulation of action potential; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:2000334; P:positive regulation of blood microparticle formation; ISO:MGI.
GO; GO:0060559; P:positive regulation of calcidiol 1-monooxygenase activity; ISO:MGI.
GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:MGI.
GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:MGI.
GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISO:MGI.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; ISO:MGI.
GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
GO; GO:0090197; P:positive regulation of chemokine secretion; ISO:MGI.
GO; GO:0002876; P:positive regulation of chronic inflammatory response to antigenic stimulus; IGI:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
GO; GO:0050715; P:positive regulation of cytokine secretion; ISO:MGI.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0031622; P:positive regulation of fever generation; IDA:BHF-UCL.
GO; GO:0050754; P:positive regulation of fractalkine biosynthetic process; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
GO; GO:0051798; P:positive regulation of hair follicle development; IMP:UniProtKB.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IGI:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IGI:MGI.
GO; GO:0032741; P:positive regulation of interleukin-18 production; ISO:MGI.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:MGI.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; ISO:MGI.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
GO; GO:0043507; P:positive regulation of JUN kinase activity; ISS:UniProtKB.
GO; GO:1904999; P:positive regulation of leukocyte adhesion to arterial endothelial cell; ISO:MGI.
GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:MGI.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
GO; GO:0071803; P:positive regulation of podosome assembly; ISO:MGI.
GO; GO:0043068; P:positive regulation of programmed cell death; ISO:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
GO; GO:0031334; P:positive regulation of protein complex assembly; ISO:MGI.
GO; GO:0043243; P:positive regulation of protein complex disassembly; ISS:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:MGI.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:ARUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0051222; P:positive regulation of protein transport; ISO:MGI.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:1901671; P:positive regulation of superoxide dismutase activity; ISO:MGI.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:ARUK-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0045994; P:positive regulation of translational initiation by iron; IDA:MGI.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0060557; P:positive regulation of vitamin D biosynthetic process; ISO:MGI.
GO; GO:0000060; P:protein import into nucleus, translocation; ISO:MGI.
GO; GO:0043491; P:protein kinase B signaling; ISO:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
GO; GO:0032800; P:receptor biosynthetic process; ISO:MGI.
GO; GO:0060693; P:regulation of branching involved in salivary gland morphogenesis; IDA:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IDA:MGI.
GO; GO:2000351; P:regulation of endothelial cell apoptotic process; ISO:MGI.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:MGI.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0051023; P:regulation of immunoglobulin secretion; IDA:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IDA:MGI.
GO; GO:0050796; P:regulation of insulin secretion; ISO:MGI.
GO; GO:0045670; P:regulation of osteoclast differentiation; IDA:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; IDA:MGI.
GO; GO:0050708; P:regulation of protein secretion; IDA:MGI.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IDA:MGI.
GO; GO:0050807; P:regulation of synapse organization; IMP:ARUK-UCL.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
GO; GO:0010033; P:response to organic substance; IDA:MGI.
GO; GO:0009615; P:response to virus; ISO:MGI.
GO; GO:0030730; P:sequestering of triglyceride; ISO:MGI.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISO:MGI.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:MGI.
CDD; cd00184; TNF; 1.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR006053; TNF.
InterPro; IPR002959; TNF_alpha.
InterPro; IPR021184; TNF_CS.
InterPro; IPR006052; TNF_dom.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
PANTHER; PTHR11471:SF23; PTHR11471:SF23; 1.
Pfam; PF00229; TNF; 1.
PRINTS; PR01234; TNECROSISFCT.
PRINTS; PR01235; TNFALPHA.
SMART; SM00207; TNF; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS00251; TNF_1; 1.
PROSITE; PS50049; TNF_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Glycoprotein; Lipoprotein;
Membrane; Myristate; Phosphoprotein; Polymorphism; Reference proteome;
Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 235 Tumor necrosis factor, membrane form.
/FTId=PRO_0000034435.
CHAIN 1 39 Intracellular domain 1. {ECO:0000250}.
/FTId=PRO_0000417255.
CHAIN 1 35 Intracellular domain 2. {ECO:0000250}.
/FTId=PRO_0000417256.
CHAIN 50 ? C-domain 1. {ECO:0000250}.
/FTId=PRO_0000417257.
CHAIN 52 ? C-domain 2. {ECO:0000250}.
/FTId=PRO_0000417258.
CHAIN 80 235 Tumor necrosis factor, soluble form.
/FTId=PRO_0000034436.
TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.
TRANSMEM 36 56 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 57 235 Extracellular. {ECO:0000255}.
SITE 34 35 Cleavage; by SPPL2A or SPPL2B.
{ECO:0000250}.
SITE 39 40 Cleavage; by SPPL2A or SPPL2B.
{ECO:0000250}.
SITE 49 50 Cleavage; by SPPL2A or SPPL2B.
{ECO:0000250}.
SITE 51 52 Cleavage; by SPPL2A or SPPL2B.
{ECO:0000250}.
SITE 79 80 Cleavage; by ADAM17. {ECO:0000250}.
MOD_RES 2 2 Phosphoserine; by CK1. {ECO:0000250}.
LIPID 20 20 N6-myristoyl lysine. {ECO:0000250}.
CARBOHYD 83 83 O-linked (GalNAc...) serine; in soluble
form. {ECO:0000250}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
DISULFID 148 179
VARIANT 7 7 I -> T (in strain: BALB/c and C57BL/6).
{ECO:0000269|PubMed:9089109}.
VARIANT 77 77 T -> A (in strain: BALB/c and C57BL/6).
{ECO:0000269|PubMed:9089109}.
CONFLICT 79 81 Missing (in Ref. 8; AAB65593).
{ECO:0000305}.
CONFLICT 231 231 G -> R (in Ref. 3 and 4). {ECO:0000305}.
STRAND 92 97 {ECO:0000244|PDB:2TNF}.
STRAND 99 101 {ECO:0000244|PDB:2TNF}.
STRAND 107 109 {ECO:0000244|PDB:2TNF}.
STRAND 115 117 {ECO:0000244|PDB:2TNF}.
STRAND 121 123 {ECO:0000244|PDB:2TNF}.
STRAND 126 128 {ECO:0000244|PDB:2TNF}.
STRAND 130 147 {ECO:0000244|PDB:2TNF}.
STRAND 154 161 {ECO:0000244|PDB:2TNF}.
TURN 163 165 {ECO:0000244|PDB:2TNF}.
STRAND 168 176 {ECO:0000244|PDB:2TNF}.
STRAND 191 204 {ECO:0000244|PDB:2TNF}.
STRAND 209 215 {ECO:0000244|PDB:2TNF}.
HELIX 217 219 {ECO:0000244|PDB:2TNF}.
STRAND 227 234 {ECO:0000244|PDB:2TNF}.
SEQUENCE 235 AA; 25896 MW; 16DD2A9676D68C5D CRC64;
MSTESMIRDV ELAEEALPQK MGGFQNSRRC LCLSLFSFLL VAGATTLFCL LNFGVIGPQR
DEKFPNGLPL ISSMAQTLTL RSSSQNSSDK PVAHVVANHQ VEEQLEWLSQ RANALLANGM
DLKDNQLVVP ADGLYLVYSQ VLFKGQGCPD YVLLTHTVSR FAISYQEKVN LLSAVKSPCP
KDTPEGAELK PWYEPIYLGG VFQLEKGDQL SAEVNLPKYL DFAESGQVYF GVIAL


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