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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.
30-AUG-2017, entry version 189.
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]
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.
-!- FUNCTION: The TNF intracellular domain (ICD) form induces IL12
production in dendritic cells. {ECO:0000250}.
-!- 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; 12.
DIP; DIP-40029N; -.
IntAct; P06804; 1.
STRING; 10090.ENSMUSP00000025263; -.
ChEMBL; CHEMBL4984; -.
iPTMnet; P06804; -.
PhosphoSitePlus; 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; ENSGT00530000062992; -.
HOGENOM; HOG000048729; -.
HOVERGEN; HBG012516; -.
InParanoid; P06804; -.
KO; K03156; -.
OMA; PWYEPIY; -.
OrthoDB; EOG091G0HIG; -.
PhylomeDB; P06804; -.
TreeFam; TF332169; -.
Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
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; -.
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:0005622; C:intracellular; IDA: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: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:0097190; P:apoptotic signaling pathway; IDA: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: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:0090002; P:establishment of protein localization to plasma membrane; ISO: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: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: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: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 from RNA polymerase II promoter; 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: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: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: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:0031622; P:positive regulation of fever generation; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; 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:0032729; P:positive regulation of interferon-gamma production; IGI: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:0042346; P:positive regulation of NF-kappaB import into nucleus; IMP:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0051533; P:positive regulation of NFAT protein import into nucleus; ISO:MGI.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
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:0071803; P:positive regulation of podosome assembly; ISO:MGI.
GO; GO:0043068; P:positive regulation of programmed cell death; 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:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0051222; P:positive regulation of protein transport; ISO:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; 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:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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: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: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: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:0051384; P:response to glucocorticoid; 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:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:MGI.
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:SF46; PTHR11471:SF46; 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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