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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_DELLE              Reviewed;         233 AA.
Q8WNR1;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
25-OCT-2017, entry version 88.
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;
Delphinapterus leucas (Beluga whale).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Cetacea;
Odontoceti; Monodontidae; Delphinapterus.
NCBI_TaxID=9749;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11768130;
Denis F., Archambault D.;
"Molecular cloning and characterization of beluga whale
(Delphinapterus leucas) interleukin-1beta and tumor necrosis factor-
alpha.";
Can. J. Vet. Res. 65:233-240(2001).
-!- 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).
{ECO:0000250}.
-!- 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; AF320323; AAL56946.1; -; mRNA.
ProteinModelPortal; Q8WNR1; -.
HOVERGEN; HBG012516; -.
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.
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; Secreted; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 233 Tumor necrosis factor, membrane form.
/FTId=PRO_0000034417.
CHAIN 1 39 Intracellular domain 1. {ECO:0000250}.
/FTId=PRO_0000417219.
CHAIN 1 35 Intracellular domain 2. {ECO:0000250}.
/FTId=PRO_0000417220.
CHAIN 50 ? C-domain 1. {ECO:0000250}.
/FTId=PRO_0000417221.
CHAIN 52 ? C-domain 2. {ECO:0000250}.
/FTId=PRO_0000417222.
CHAIN 78 233 Tumor necrosis factor, soluble form.
/FTId=PRO_0000034418.
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 49 50 Cleavage; by SPPL2A or SPPL2B.
{ECO:0000250}.
SITE 51 52 Cleavage; by SPPL2A or SPPL2B.
{ECO:0000250}.
SITE 77 78 Cleavage; by ADAM17. {ECO:0000250}.
MOD_RES 2 2 Phosphoserine; by CK1. {ECO:0000250}.
LIPID 19 19 N6-myristoyl lysine. {ECO:0000250}.
CARBOHYD 80 80 O-linked (GalNAc...) serine; in soluble
form. {ECO:0000250}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 145 177 {ECO:0000250}.
SEQUENCE 233 AA; 25420 MW; 2DF37DCB2BC9E961 CRC64;
MSTESMIRDV ELAEEALSKT AGGSQGSGRC LCLSLFSFFL VAGGTTLFCL LHFGVIGPQR
EEFPTGYSII SPLAQTLRSS SKTSSNKPVA HVVANLSAQG QLRWLNTYAN TLLANSVKLE
DNQLVVPTDG LYLIYSQVLF RGQGCPSTHL FLTHTISRIA VSYQTKVNLL SAIKSPCQRE
TPEGAEAKPW YEPIYQGGVF QLEKGDRLSA EINLPDYLDF AESGQVYFGI IAL


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