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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.
22-NOV-2017, entry version 163.
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;
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.
-!- FUNCTION: The TNF intracellular domain (ICD) form induces IL12
production in dendritic cells. {ECO:0000250}.
-!- 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.
UniGene; Rn.2275; -.
ProteinModelPortal; P16599; -.
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; ENSGT00530000062992; -.
HOGENOM; HOG000048729; -.
HOVERGEN; HBG012516; -.
InParanoid; P16599; -.
KO; K03156; -.
OMA; PWYEPIY; -.
OrthoDB; EOG091G0HIG; -.
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; -.
Genevisible; P16599; RN.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
GO; GO:0005622; C:intracellular; ISO:RGD.
GO; GO:0045121; C:membrane raft; ISO: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:0071222; P:cellular response to lipopolysaccharide; ISO: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: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: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: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 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:0010629; P:negative regulation of gene expression; ISO:RGD.
GO; GO:0046325; P:negative regulation of glucose import; IDA:RGD.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; ISO:RGD.
GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD.
GO; GO:0002037; P:negative regulation of L-glutamate transport; 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 complex disassembly; ISO:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; 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: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: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: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:0031622; P:positive regulation of fever generation; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
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; IGI:RGD.
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:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
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:0042346; P:positive regulation of NF-kappaB import into nucleus; ISO:RGD.
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:RGD.
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:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
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:0031334; P:positive regulation of protein complex assembly; ISO:RGD.
GO; GO:0043243; P:positive regulation of protein complex disassembly; 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; ISO:RGD.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
GO; GO:0051222; P:positive regulation of protein transport; IDA:RGD.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:RGD.
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 from RNA polymerase II promoter; ISO:RGD.
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: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:0000060; P:protein import into nucleus, translocation; 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 proliferation; 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: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: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.
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; Complete proteome; Cytokine; Disulfide bond;
Glycoprotein; Lipoprotein; Membrane; Myristate; Phosphoprotein;
Reference proteome; Secreted; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 235 Tumor necrosis factor, membrane form.
/FTId=PRO_0000034451.
CHAIN 1 39 Intracellular domain 1. {ECO:0000250}.
/FTId=PRO_0000417287.
CHAIN 1 35 Intracellular domain 2. {ECO:0000250}.
/FTId=PRO_0000417288.
CHAIN 50 ? C-domain 1. {ECO:0000250}.
/FTId=PRO_0000417289.
CHAIN 52 ? C-domain 2. {ECO:0000250}.
/FTId=PRO_0000417290.
CHAIN 80 235 Tumor necrosis factor, soluble form.
/FTId=PRO_0000034452.
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 19 19 N6-myristoyl lysine. {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.
{ECO:0000255}.
DISULFID 148 179 {ECO:0000250}.
VARIANT 122 122 L -> P. {ECO:0000269|Ref.5}.
VARIANT 190 190 K -> E. {ECO:0000269|Ref.5}.
CONFLICT 39 39 L -> P (in Ref. 2; CAA05290/CAA47146).
{ECO:0000305}.
CONFLICT 163 163 I -> T (in Ref. 2; CAA05290/CAA47146).
{ECO:0000305}.
CONFLICT 202 202 F -> S (in Ref. 2; CAA05290/CAA47146).
{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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