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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_MACMU              Reviewed;         233 AA.
P48094; Q5TM21; Q8HZD6;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
07-NOV-2018, entry version 133.
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 mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7561102;
Villinger F.J., Brar S.S., Mayne A.E., Chikkala N., Ansari A.A.;
"Comparative sequence analysis of cytokine genes from human and
nonhuman primates.";
J. Immunol. 155:3946-3954(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15269276; DOI=10.1093/molbev/msh216;
Kulski J.K., Anzai T., Shiina T., Inoko H.;
"Rhesus macaque class I duplicon structures, organization, and
evolution within the alpha block of the major histocompatibility
complex.";
Mol. Biol. Evol. 21:2079-2091(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-187.
O'Huigin C., Tichy H., Klein J.;
"Molecular evolution in higher primates; gene specific and organism
specific characteristics.";
Submitted (MAR-2002) 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
-----------------------------------------------------------------------
EMBL; U19850; AAA86712.1; -; mRNA.
EMBL; AB128049; BAD69724.1; -; Genomic_DNA.
EMBL; AY091967; AAM76585.1; -; Genomic_DNA.
RefSeq; NP_001040614.1; NM_001047149.1.
UniGene; Mmu.3364; -.
ProteinModelPortal; P48094; -.
SMR; P48094; -.
STRING; 9544.ENSMMUP00000011594; -.
Ensembl; ENSMMUT00000056699; ENSMMUP00000056761; ENSMMUG00000045654.
GeneID; 715467; -.
KEGG; mcc:715467; -.
CTD; 7124; -.
eggNOG; ENOG410ISAN; Eukaryota.
eggNOG; ENOG410YQC4; LUCA.
GeneTree; ENSGT00530000062992; -.
HOGENOM; HOG000048729; -.
HOVERGEN; HBG012516; -.
InParanoid; P48094; -.
KO; K03156; -.
OMA; QLQWLSR; -.
OrthoDB; EOG091G0HIG; -.
TreeFam; TF332169; -.
Proteomes; UP000006718; Chromosome 4.
Bgee; ENSMMUG00000008845; Expressed in 10 organ(s), highest expression level in CD4-positive helper T cell.
ExpressionAtlas; P48094; baseline.
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 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:0043243; P:positive regulation of protein complex disassembly; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; 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; Complete proteome; Cytokine; Disulfide bond;
Glycoprotein; Lipoprotein; Membrane; Myristate; Phosphoprotein;
Reference proteome; Secreted; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 233 Tumor necrosis factor, membrane form.
/FTId=PRO_0000034431.
CHAIN 1 39 Intracellular domain 1. {ECO:0000250}.
/FTId=PRO_0000417247.
CHAIN 1 35 Intracellular domain 2. {ECO:0000250}.
/FTId=PRO_0000417248.
CHAIN 50 ? C-domain 1. {ECO:0000250}.
/FTId=PRO_0000417249.
CHAIN 52 ? C-domain 2. {ECO:0000250}.
/FTId=PRO_0000417250.
CHAIN 77 233 Tumor necrosis factor, soluble form.
/FTId=PRO_0000034432.
TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.
TRANSMEM 36 56 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 57 233 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 76 77 Cleavage; by ADAM17. {ECO:0000250}.
MOD_RES 2 2 Phosphoserine; by CK1. {ECO:0000250}.
LIPID 20 20 N6-myristoyl lysine. {ECO:0000250}.
CARBOHYD 80 80 O-linked (GalNAc...) serine; in soluble
form. {ECO:0000250}.
DISULFID 145 177 {ECO:0000250}.
SEQUENCE 233 AA; 25630 MW; 9F6F85050595FD59 CRC64;
MSTESMIRDV ELAEEALPRK TAGPQGSRRC WFLSLFSFLL VAGATTLFCL LHFGVIGPQR
EEFPKDPSLI SPLAQAVRSS SRTPSDKPVA HVVANPQAEG QLQWLNRRAN ALLANGVELT
DNQLVVPSEG LYLIYSQVLF KGQGCPSNHV LLTHTISRIA VSYQTKVNLL SAIKSPCQRE
TPEGAEAKPW YEPIYLGGVF QLEKGDRLSA EINLPDYLDF AESGQVYFGI IAL


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