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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_RAT                Reviewed;         235 AA.
P16599; Q6EE11; Q9JI26; Q9JI27;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
26-FEB-2020, entry version 181.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Shirai T., Shimizu N., Horiguchi S., Ito H.;
"Cloning and expression in Escherichia coli of the gene for rat tumor
necrosis factor.";
Agric. Biol. Chem. 53:1733-1736(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1627266; DOI=10.1515/bchm3.1992.373.1.271;
Estler H.C., Grewe M., Gaussling R., Pavlovic M., Decker K.F.;
"Rat tumor necrosis factor-alpha. Transcription in rat Kupffer cells and in
vitro posttranslational processing based on a PCR-derived cDNA.";
Biol. Chem. Hoppe-Seyler 373:271-281(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley; TISSUE=Testis;
PubMed=8224868; DOI=10.1016/0378-1119(93)90200-m;
Kwon J., Chung I.Y., Benveniste E.N.;
"Cloning and sequence analysis of the rat tumor necrosis factor-encoding
genes.";
Gene 132:227-236(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ACI/SegHsd, BB(DR)/Wor, Brown Norway/SsNHsd, DA/Bkl, F344/NHsd, and
LEW/NHsd;
PubMed=11477479; DOI=10.1038/sj.gene.6363761;
Furuya T., Joe B., Salstrom J.L., Hashiramoto A., Dobbins D.E.,
Wilder R.L., Remmers E.F.;
"Polymorphisms of the tumor necrosis factor alpha locus among autoimmune
disease susceptible and resistant inbred rat strains.";
Genes Immun. 2:229-232(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-122 AND GLU-190.
STRAIN=Dark agouti;
Seidel M.F., Junier M.-P., Vetter H.;
"TNF-alpha polymorphism in rats with collagen-induced arthritis.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=AUG/OlaHsd, PVG/OlaHsd, and WF/HanHsd;
PubMed=15935297; DOI=10.1016/j.trim.2005.04.002;
Warle M.C., van der Laan L.J., Kusters J.G., Pot R.G., Hop W.C.,
Segeren K.C., Ijzermans J.N., Metselaar H.J., Tilanus H.W.;
"No association between tumor necrosis factor-alpha production and gene
polymorphisms among inbred rat strains.";
Transpl. Immunol. 14:77-82(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15060004; DOI=10.1101/gr.1987704;
Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
"The genomic sequence and comparative analysis of the rat major
histocompatibility complex.";
Genome Res. 14:631-639(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-231.
TISSUE=Tail;
Kirisits M.J., Vardimon D., Kunz H.W., Gill T.J. III;
"Mapping of the TNF-alpha locus in the rat.";
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:P01375, ECO:0000250|UniProtKB:P06804}.
-!- FUNCTION: The TNF intracellular domain (ICD) form induces IL12
production in dendritic cells. {ECO:0000250|UniProtKB:P01375}.
-!- SUBUNIT: Homotrimer. Interacts with SPPL2B (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
membrane protein {ECO:0000250}.
-!- 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
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: [C-domain 1]: Secreted {ECO:0000250}.
-!- SUBCELLULAR LOCATION: [C-domain 2]: Secreted {ECO:0000250}.
-!- PTM: The soluble form derives from the membrane form by proteolytic
processing. 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). {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; D00475; BAA00367.1; -; Genomic_DNA.
EMBL; X66539; CAA47146.1; -; mRNA.
EMBL; AJ002278; CAA05290.1; -; mRNA.
EMBL; L00981; AAA16275.1; -; Genomic_DNA.
EMBL; AF329982; AAK53568.1; -; Genomic_DNA.
EMBL; AF329983; AAK53569.1; -; Genomic_DNA.
EMBL; AF329984; AAK53570.1; -; Genomic_DNA.
EMBL; AF329985; AAK53571.1; -; Genomic_DNA.
EMBL; AF329986; AAK53572.1; -; Genomic_DNA.
EMBL; AF329987; AAK53573.1; -; Genomic_DNA.
EMBL; AF269159; AAF82567.1; -; mRNA.
EMBL; AF269160; AAF82568.1; -; mRNA.
EMBL; AY427673; AAR91624.1; -; Genomic_DNA.
EMBL; AY427674; AAR91625.1; -; Genomic_DNA.
EMBL; AY427675; AAR91626.1; -; Genomic_DNA.
EMBL; BX883046; CAE84003.1; -; Genomic_DNA.
EMBL; BC107671; AAI07672.1; -; mRNA.
EMBL; L19123; AAA42255.1; -; Genomic_DNA.
PIR; JU0029; JU0029.
RefSeq; NP_036807.1; NM_012675.3.
RefSeq; XP_008770997.1; XM_008772775.2.
SMR; P16599; -.
DIP; DIP-39461N; -.
IntAct; P16599; 74.
STRING; 10116.ENSRNOP00000001110; -.
BindingDB; P16599; -.
PhosphoSitePlus; P16599; -.
PaxDb; P16599; -.
PRIDE; P16599; -.
Ensembl; ENSRNOT00000001110; ENSRNOP00000001110; ENSRNOG00000000837.
Ensembl; ENSRNOT00000079677; ENSRNOP00000074520; ENSRNOG00000055156.
GeneID; 103694380; -.
GeneID; 24835; -.
KEGG; rno:103694380; -.
KEGG; rno:24835; -.
UCSC; RGD:3876; rat.
CTD; 7124; -.
RGD; 3876; Tnf.
eggNOG; ENOG410ISAN; Eukaryota.
eggNOG; ENOG410YQC4; LUCA.
GeneTree; ENSGT00970000193380; -.
HOGENOM; CLU_070352_3_1_1; -.
InParanoid; P16599; -.
KO; K03156; -.
OMA; SPCHRET; -.
OrthoDB; 1124938at2759; -.
PhylomeDB; P16599; -.
TreeFam; TF332169; -.
Reactome; R-RNO-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-RNO-5357905; Regulation of TNFR1 signaling.
Reactome; R-RNO-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-RNO-5626978; TNFR1-mediated ceramide production.
Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-RNO-75893; TNF signaling.
PRO; PR:P16599; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000000837; Expressed in spleen and 1 other tissue.
Genevisible; P16599; RN.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
GO; GO:0045121; C:membrane raft; ISO:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0001891; C:phagocytic cup; ISO:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0055037; C:recycling endosome; ISO:RGD.
GO; GO:0005125; F:cytokine activity; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0002020; F:protease binding; ISO:RGD.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:RGD.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IDA:RGD.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:0000187; P:activation of MAPK activity; ISO:RGD.
GO; GO:0000185; P:activation of MAPKKK activity; ISO:RGD.
GO; GO:0002526; P:acute inflammatory response; IEP:RGD.
GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
GO; GO:0006915; P:apoptotic process; IDA:RGD.
GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
GO; GO:0019722; P:calcium-mediated signaling; IDA:RGD.
GO; GO:0001775; P:cell activation; IDA:RGD.
GO; GO:0045123; P:cellular extravasation; ISO:RGD.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0071316; P:cellular response to nicotine; ISO:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
GO; GO:0002439; P:chronic inflammatory response to antigenic stimulus; ISO:RGD.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD.
GO; GO:0006952; P:defense response; ISO:RGD.
GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:RGD.
GO; GO:0048566; P:embryonic digestive tract development; ISO:RGD.
GO; GO:0072577; P:endothelial cell apoptotic process; ISO:RGD.
GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; ISO:RGD.
GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
GO; GO:0006959; P:humoral immune response; ISO:RGD.
GO; GO:0006954; P:inflammatory response; ISO:RGD.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
GO; GO:0007254; P:JNK cascade; ISO:RGD.
GO; GO:0050900; P:leukocyte migration; ISO:RGD.
GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD.
GO; GO:0000165; P:MAPK cascade; ISO:RGD.
GO; GO:0001774; P:microglial cell activation; ISO:RGD.
GO; GO:0007275; P:multicellular organism development; ISO:RGD.
GO; GO:0097527; P:necroptotic signaling pathway; ISS:UniProtKB.
GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; ISO:RGD.
GO; GO:1900222; P:negative regulation of amyloid-beta clearance; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; ISO:RGD.
GO; GO:0061048; P:negative regulation of branching involved in lung morphogenesis; ISO:RGD.
GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
GO; GO:0002740; P:negative regulation of cytokine secretion involved in immune response; ISO:RGD.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:RGD.
GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
GO; GO:0046325; P:negative regulation of glucose import; IDA:RGD.
GO; GO:0010459; P:negative regulation of heart rate; IMP:RGD.
GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD.
GO; GO:0002037; P:negative regulation of L-glutamate import across plasma membrane; IDA:RGD.
GO; GO:0050995; P:negative regulation of lipid catabolic process; ISO:RGD.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:RGD.
GO; GO:0031642; P:negative regulation of myelination; IMP:RGD.
GO; GO:0045662; P:negative regulation of myoblast differentiation; ISO:RGD.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; ISO:RGD.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
GO; GO:0043242; P:negative regulation of protein-containing complex disassembly; ISO:RGD.
GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0045071; P:negative regulation of viral genome replication; ISO:RGD.
GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
GO; GO:0045760; P:positive regulation of action potential; IDA:RGD.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:2000334; P:positive regulation of blood microparticle formation; ISO:RGD.
GO; GO:0060559; P:positive regulation of calcidiol 1-monooxygenase activity; ISO:RGD.
GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:RGD.
GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISO:RGD.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; ISO:RGD.
GO; GO:0032722; P:positive regulation of chemokine production; ISO:RGD.
GO; GO:0090197; P:positive regulation of chemokine secretion; IDA:ARUK-UCL.
GO; GO:0002876; P:positive regulation of chronic inflammatory response to antigenic stimulus; ISO:RGD.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
GO; GO:0050715; P:positive regulation of cytokine secretion; ISO:RGD.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:RGD.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
GO; GO:0031622; P:positive regulation of fever generation; ISO:RGD.
GO; GO:0050754; P:positive regulation of fractalkine biosynthetic process; IDA:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:RGD.
GO; GO:0051798; P:positive regulation of hair follicle development; ISO:RGD.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:RGD.
GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; ISO:RGD.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:ARUK-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:RGD.
GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:RGD.
GO; GO:0032741; P:positive regulation of interleukin-18 production; IMP:RGD.
GO; GO:0045410; P:positive regulation of interleukin-6 biosynthetic process; IDA:ARUK-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IDA:ARUK-UCL.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; ISO:RGD.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:RGD.
GO; GO:1904999; P:positive regulation of leukocyte adhesion to arterial endothelial cell; ISO:RGD.
GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:RGD.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:RGD.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:ARUK-UCL.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:RGD.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IC:ARUK-UCL.
GO; GO:0051173; P:positive regulation of nitrogen compound metabolic process; ISO:RGD.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:ARUK-UCL.
GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:ARUK-UCL.
GO; GO:0071803; P:positive regulation of podosome assembly; ISO:RGD.
GO; GO:0043068; P:positive regulation of programmed cell death; ISO:RGD.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:RGD.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:ARUK-UCL.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:RGD.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:ARUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
GO; GO:0051222; P:positive regulation of protein transport; IDA:RGD.
GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; ISO:RGD.
GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:ARUK-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:RGD.
GO; GO:1901671; P:positive regulation of superoxide dismutase activity; ISO:RGD.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0045994; P:positive regulation of translational initiation by iron; ISO:RGD.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:ARUK-UCL.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; ISO:RGD.
GO; GO:0060557; P:positive regulation of vitamin D biosynthetic process; ISO:RGD.
GO; GO:0043491; P:protein kinase B signaling; ISO:RGD.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
GO; GO:0032800; P:receptor biosynthetic process; ISO:RGD.
GO; GO:0060693; P:regulation of branching involved in salivary gland morphogenesis; ISO:RGD.
GO; GO:0042127; P:regulation of cell population proliferation; IDA:RGD.
GO; GO:2000351; P:regulation of endothelial cell apoptotic process; ISO:RGD.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:RGD.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
GO; GO:0051023; P:regulation of immunoglobulin secretion; ISO:RGD.
GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
GO; GO:0050796; P:regulation of insulin secretion; ISO:RGD.
GO; GO:0045670; P:regulation of osteoclast differentiation; ISO:RGD.
GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
GO; GO:0050708; P:regulation of protein secretion; ISO:RGD.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
GO; GO:0050807; P:regulation of synapse organization; ISO:RGD.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; ISO:RGD.
GO; GO:1990268; P:response to gold nanoparticle; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0010033; P:response to organic substance; ISO:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0009615; P:response to virus; ISO:RGD.
GO; GO:0030730; P:sequestering of triglyceride; ISO:RGD.
GO; GO:0007165; P:signal transduction; IDA:RGD.
GO; GO:0003009; P:skeletal muscle contraction; IEP:RGD.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IMP:UniProtKB.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
GO; GO:0042311; P:vasodilation; IMP:RGD.
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.
2: Evidence at transcript level;
Cell membrane; Cytokine; Disulfide bond; Glycoprotein; Lipoprotein;
Membrane; Myristate; Phosphoprotein; Reference proteome; Secreted;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1..235
/note="Tumor necrosis factor, membrane form"
/id="PRO_0000034451"
CHAIN 1..39
/note="Intracellular domain 1"
/evidence="ECO:0000250"
/id="PRO_0000417287"
CHAIN 1..35
/note="Intracellular domain 2"
/evidence="ECO:0000250"
/id="PRO_0000417288"
CHAIN 50..?
/note="C-domain 1"
/evidence="ECO:0000250"
/id="PRO_0000417289"
CHAIN 52..?
/note="C-domain 2"
/evidence="ECO:0000250"
/id="PRO_0000417290"
CHAIN 80..235
/note="Tumor necrosis factor, soluble form"
/id="PRO_0000034452"
TOPO_DOM 1..35
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 36..56
/note="Helical; Signal-anchor for type II membrane protein"
/evidence="ECO:0000255"
TOPO_DOM 57..235
/note="Extracellular"
/evidence="ECO:0000255"
SITE 34..35
/note="Cleavage; by SPPL2A or SPPL2B"
/evidence="ECO:0000250"
SITE 39..40
/note="Cleavage; by SPPL2A or SPPL2B"
/evidence="ECO:0000250"
SITE 49..50
/note="Cleavage; by SPPL2A or SPPL2B"
/evidence="ECO:0000250"
SITE 51..52
/note="Cleavage; by SPPL2A or SPPL2B"
/evidence="ECO:0000250"
SITE 79..80
/note="Cleavage; by ADAM17"
/evidence="ECO:0000250"
MOD_RES 2
/note="Phosphoserine; by CK1"
/evidence="ECO:0000250"
LIPID 19
/note="N6-myristoyl lysine"
/evidence="ECO:0000250"
LIPID 20
/note="N6-myristoyl lysine"
/evidence="ECO:0000250"
CARBOHYD 83
/note="O-linked (GalNAc...) serine; in soluble form"
/evidence="ECO:0000250"
CARBOHYD 86
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 148..179
/evidence="ECO:0000250"
VARIANT 122
/note="L -> P"
/evidence="ECO:0000269|Ref.5"
VARIANT 190
/note="K -> E"
/evidence="ECO:0000269|Ref.5"
CONFLICT 39
/note="L -> P (in Ref. 2; CAA05290/CAA47146)"
/evidence="ECO:0000305"
CONFLICT 163
/note="I -> T (in Ref. 2; CAA05290/CAA47146)"
/evidence="ECO:0000305"
CONFLICT 202
/note="F -> S (in Ref. 2; CAA05290/CAA47146)"
/evidence="ECO:0000305"
SEQUENCE 235 AA; 25806 MW; B808EC6D049C2F3B CRC64;
MSTESMIRDV ELAEEALPKK MGGLQNSRRC LCLSLFSFLL VAGATTLFCL LNFGVIGPNK
EEKFPNGLPL ISSMAQTLTL RSSSQNSSDK PVAHVVANHQ AEEQLEWLSQ RANALLANGM
DLKDNQLVVP ADGLYLIYSQ VLFKGQGCPD YVLLTHTVSR FAISYQEKVS LLSAIKSPCP
KDTPEGAELK PWYEPMYLGG VFQLEKGDLL SAEVNLPKYL DITESGQVYF GVIAL


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Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP2249: Metastatic brain tumor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP1983: Splicing factor NOVA regulated synpatic proteins
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP272: Blood Clotting Cascade
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP2148: Brain derived neurotrophic factor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP537: Translation Factors
WP32: Translation Factors
WP1566: Citrate cycle (TCA cycle)
WP149: Translation Factors
WP1486: Intracellular trafficking of CFTR
WP2256: Integrated Pancreatic Cancer Pathway
WP1948: Citrate cycle (TCA cycle)
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[TNF TNFA TNFSF2] 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] (Fragment)
[TNF TNFA TNFSF2] 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]

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