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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_MACFA              Reviewed;         233 AA.
P79337;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
26-FEB-2020, entry version 105.
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;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphocyte;
Tatsumi M.;
"Molecular cloning and expression of cynomolgus monkey TNF-alpha.";
Submitted (JAN-1997) 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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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AB000513; BAA19131.1; -; mRNA.
RefSeq; NP_001272206.1; NM_001285277.1.
SMR; P79337; -.
STRING; 9541.XP_005553619.1; -.
GeneID; 102139631; -.
KEGG; mcf:102139631; -.
CTD; 7124; -.
KO; K03156; -.
Proteomes; UP000233100; Unplaced.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0097527; P:necroptotic signaling pathway; ISS:UniProtKB.
GO; GO:0043242; P:negative regulation of protein-containing complex disassembly; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; ISS:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; ISS:UniProtKB.
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..233
/note="Tumor necrosis factor, membrane form"
/id="PRO_0000034429"
CHAIN 1..39
/note="Intracellular domain 1"
/evidence="ECO:0000250"
/id="PRO_0000417243"
CHAIN 1..35
/note="Intracellular domain 2"
/evidence="ECO:0000250"
/id="PRO_0000417244"
CHAIN 50..?
/note="C-domain 1"
/evidence="ECO:0000250"
/id="PRO_0000417245"
CHAIN 52..?
/note="C-domain 2"
/evidence="ECO:0000250"
/id="PRO_0000417246"
CHAIN 77..233
/note="Tumor necrosis factor, soluble form"
/id="PRO_0000034430"
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..233
/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 76..77
/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 80
/note="O-linked (GalNAc...) serine; in soluble form"
/evidence="ECO:0000250"
DISULFID 145..177
/evidence="ECO:0000250"
SEQUENCE 233 AA; 25558 MW; 6ABF2C3AB132C217 CRC64;
MSTESMIQDV ELAEEALPRK TAGPQGSRRC WFLSLFSFLL VAGAATLFCL LHFGVIGPQR
EEFPKDPSLI SPLAQAVRSS SRTPSDKPVA HVVANPQAEG QLQWLNRRAN ALVANGVELT
DNQLVVPSEG LYLIYSQVLF KGQGCPSNHV LLTHTISRIA VSYQTKVNLL SAIKSPCQRE
TPEGAEAKPW YEPIYLGGVF QLEKGDRLSA EINLPDYLDF AESGQVYFGI IAL


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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]
[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]
[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]

Bibliography :