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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_SHEEP              Reviewed;         234 AA.
P23383;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
17-JUN-2020, entry version 144.
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;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2251151; DOI=10.1093/nar/18.22.6723;
Young A.J., Hay J.B., Chan J.Y.C.;
"Primary structure of ovine tumor necrosis factor alpha cDNA.";
Nucleic Acids Res. 18:6723-6723(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Alveolar macrophage;
PubMed=1765267; DOI=10.1016/0378-1119(91)90610-n;
Green I.R., Sargan D.R.;
"Sequence of the cDNA encoding ovine tumor necrosis factor-alpha: problems
with cloning by inverse PCR.";
Gene 109:203-210(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1786996; DOI=10.1038/icb.1991.38;
Andrews A.E., Nash A.D., Barcham G.J., Brandon M.R.;
"Molecular cloning, expression and characterization of ovine TNF alpha.";
Immunol. Cell Biol. 69:273-283(1991).
-!- 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; X55966; CAA39437.1; -; mRNA.
EMBL; X55152; CAA38952.1; -; mRNA.
EMBL; X56756; CAA40076.1; -; mRNA.
PIR; JH0529; JH0529.
RefSeq; NP_001020031.1; NM_001024860.1.
RefSeq; XP_011955827.1; XM_012100437.2.
SMR; P23383; -.
STRING; 9940.ENSOARP00000008936; -.
PRIDE; P23383; -.
Ensembl; ENSOART00000009066; ENSOARP00000008936; ENSOARG00000008333.
GeneID; 443540; -.
KEGG; oas:443540; -.
CTD; 7124; -.
GeneTree; ENSGT00970000193380; -.
HOGENOM; CLU_070352_3_1_1; -.
KO; K03156; -.
OMA; GATMLFC; -.
OrthoDB; 1124938at2759; -.
Proteomes; UP000002356; Chromosome 20.
ExpressionAtlas; P23383; baseline.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0001891; C:phagocytic cup; IEA:Ensembl.
GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0044212; F:transcription regulatory region DNA binding; IEA:Ensembl.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0000185; P:activation of MAPKKK activity; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0071316; P:cellular response to nicotine; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0002439; P:chronic inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
GO; GO:0072577; P:endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
GO; GO:0097527; P:necroptotic signaling pathway; ISS:UniProtKB.
GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; IEA:Ensembl.
GO; GO:1900222; P:negative regulation of amyloid-beta clearance; IEA:Ensembl.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; IEA:Ensembl.
GO; GO:0061048; P:negative regulation of branching involved in lung morphogenesis; IEA:Ensembl.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0002740; P:negative regulation of cytokine secretion involved in immune response; IEA:Ensembl.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0046325; P:negative regulation of glucose import; IEA:Ensembl.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IEA:Ensembl.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IEA:Ensembl.
GO; GO:0043242; P:negative regulation of protein-containing complex disassembly; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IEA:Ensembl.
GO; GO:2000334; P:positive regulation of blood microparticle formation; IEA:Ensembl.
GO; GO:0060559; P:positive regulation of calcidiol 1-monooxygenase activity; IEA:Ensembl.
GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IEA:Ensembl.
GO; GO:0002876; P:positive regulation of chronic inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
GO; GO:0031622; P:positive regulation of fever generation; IEA:Ensembl.
GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
GO; GO:0051798; P:positive regulation of hair follicle development; IEA:Ensembl.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl.
GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; IEA:Ensembl.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0050725; P:positive regulation of interleukin-1 beta biosynthetic process; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; IEA:Ensembl.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IEA:Ensembl.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IEA:Ensembl.
GO; GO:1904999; P:positive regulation of leukocyte adhesion to arterial endothelial cell; IEA:Ensembl.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; IEA:Ensembl.
GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IEA:Ensembl.
GO; GO:0050806; P:positive regulation of synaptic transmission; IEA:Ensembl.
GO; GO:1901647; P:positive regulation of synoviocyte proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045994; P:positive regulation of translational initiation by iron; IEA:Ensembl.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0032800; P:receptor biosynthetic process; IEA:Ensembl.
GO; GO:0060693; P:regulation of branching involved in salivary gland morphogenesis; IEA:Ensembl.
GO; GO:2000351; P:regulation of endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl.
GO; GO:0051023; P:regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0009615; P:response to virus; IEA:Ensembl.
GO; GO:0030730; P:sequestering of triglyceride; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
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..234
/note="Tumor necrosis factor, membrane form"
/id="PRO_0000034455"
CHAIN 1..39
/note="Intracellular domain 1"
/evidence="ECO:0000250"
/id="PRO_0000417295"
CHAIN 1..35
/note="Intracellular domain 2"
/evidence="ECO:0000250"
/id="PRO_0000417296"
CHAIN 50..?
/note="C-domain 1"
/evidence="ECO:0000250"
/id="PRO_0000417297"
CHAIN 52..?
/note="C-domain 2"
/evidence="ECO:0000250"
/id="PRO_0000417298"
CHAIN 78..234
/note="Tumor necrosis factor, soluble form"
/id="PRO_0000034456"
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..234
/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 77..78
/note="Cleavage; by ADAM17"
/evidence="ECO:0000250"
MOD_RES 2
/note="Phosphoserine; by CK1"
/evidence="ECO:0000250"
LIPID 20
/note="N6-myristoyl lysine"
/evidence="ECO:0000250"
CARBOHYD 81
/note="O-linked (GalNAc...) serine; in soluble form"
/evidence="ECO:0000250"
CARBOHYD 96
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 146..178
/evidence="ECO:0000250"
CONFLICT 63
/note="Missing (in Ref. 1; CAA39437)"
/evidence="ECO:0000305"
SEQUENCE 234 AA; 25536 MW; 4BCF8CCAB7956B88 CRC64;
MSTKSMIRDV ELAEEVLSNK AGGPQGSRSC WCLSLFSFLL VAGATTLFCL LHFGVIGPQR
EEQSPAGPSF NRPLVQTLRS SSQASNNKPV AHVVANISAP GQLRWGDSYA NALMANGVEL
KDNQLVVPTD GLYLIYSQVL FRGHGCPSTP LFLTHTISRI AVSYQTKVNI LSAIKSPCHR
ETLEGAEAKP WYEPIYQGGV FQLEKGDRLS AEINLPEYLD YAESGQVYFG IIAL


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