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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_PANTR              Reviewed;         232 AA.
Q8HZD9; Q1XHZ6;
23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
23-MAY-2003, sequence version 2.
25-OCT-2017, entry version 118.
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;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12493009; DOI=10.1034/j.1600-065X.2002.19008.x;
Kulski J.K., Shiina T., Anzai T., Kohara S., Inoko H.;
"Comparative genomic analysis of the MHC: the evolution of class I
duplication blocks, diversity and complexity from shark to man.";
Immunol. Rev. 190:95-122(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12799463; DOI=10.1073/pnas.1230533100;
Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T.,
Meyer A., Ikeo K., Gojobori T., Bahram S., Inoko H.;
"Comparative sequencing of human and chimpanzee MHC class I regions
unveils insertions/deletions as the major path to genomic
divergence.";
Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16702430; DOI=10.1534/genetics.106.057034;
Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y.,
Meyer A., Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K.,
Gojobori T., Inoko H., Bahram S.;
"Rapid evolution of major histocompatibility complex class I genes in
primates generates new disease alleles in humans via hitchhiking
diversity.";
Genetics 173:1555-1570(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-186.
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).
{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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB054536; BAB83882.1; -; Genomic_DNA.
EMBL; BA000041; BAC78157.1; -; Genomic_DNA.
EMBL; AB210165; BAE92772.1; -; Genomic_DNA.
EMBL; AB210166; BAE92774.1; -; Genomic_DNA.
EMBL; AY091964; AAM76582.1; -; Genomic_DNA.
RefSeq; NP_001038976.1; NM_001045511.1.
RefSeq; XP_016810226.1; XM_016954737.1.
UniGene; Ptr.6340; -.
ProteinModelPortal; Q8HZD9; -.
SMR; Q8HZD9; -.
STRING; 9598.ENSPTRP00000054518; -.
PaxDb; Q8HZD9; -.
Ensembl; ENSPTRT00000061970; ENSPTRP00000054518; ENSPTRG00000017965.
GeneID; 494186; -.
KEGG; ptr:494186; -.
CTD; 7124; -.
eggNOG; ENOG410ISAN; Eukaryota.
eggNOG; ENOG410YQC4; LUCA.
GeneTree; ENSGT00530000062992; -.
HOGENOM; HOG000048729; -.
HOVERGEN; HBG012516; -.
InParanoid; Q8HZD9; -.
KO; K03156; -.
OMA; PWYEPIY; -.
OrthoDB; EOG091G0HIG; -.
TreeFam; TF332169; -.
Proteomes; UP000002277; Chromosome 6.
Bgee; ENSPTRG00000017965; -.
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:0097527; P:necroptotic signaling pathway; ISS:UniProtKB.
GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; 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: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:0044130; P:negative regulation of growth of symbiont in host; 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:0043242; P:negative regulation of protein complex disassembly; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
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: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:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
GO; GO:0031622; P:positive regulation of fever generation; 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:0032729; P:positive regulation of interferon-gamma production; 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:0043507; P:positive regulation of JUN kinase activity; ISS:UniProtKB.
GO; GO:1904999; P:positive regulation of leukocyte adhesion to arterial endothelial cell; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IEA:Ensembl.
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; IEA:Ensembl.
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:0043243; P:positive regulation of protein complex disassembly; ISS:UniProtKB.
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:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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:0000060; P:protein import into nucleus, translocation; 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: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: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.
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.
3: Inferred from homology;
Cell membrane; Complete proteome; Cytokine; Disulfide bond;
Glycoprotein; Lipoprotein; Membrane; Myristate; Phosphoprotein;
Reference proteome; Secreted; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 232 Tumor necrosis factor, membrane form.
/FTId=PRO_0000034437.
CHAIN 1 39 Intracellular domain 1. {ECO:0000250}.
/FTId=PRO_0000417259.
CHAIN 1 35 Intracellular domain 2. {ECO:0000250}.
/FTId=PRO_0000417260.
CHAIN 50 ? C-domain 1. {ECO:0000250}.
/FTId=PRO_0000417261.
CHAIN 52 ? C-domain 2. {ECO:0000250}.
/FTId=PRO_0000417262.
CHAIN 77 232 Tumor necrosis factor, soluble form.
{ECO:0000250}.
/FTId=PRO_0000034438.
TOPO_DOM 1 34 Cytoplasmic. {ECO:0000255}.
TRANSMEM 35 57 Helical; Signal-anchor for type II
membrane protein. {ECO:0000250}.
TOPO_DOM 58 232 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 19 19 N6-myristoyl lysine. {ECO:0000250}.
LIPID 20 20 N6-myristoyl lysine. {ECO:0000250}.
CARBOHYD 79 79 O-linked (GalNAc...) serine; in soluble
form. {ECO:0000250}.
DISULFID 144 176 {ECO:0000250}.
CONFLICT 77 77 G -> VR (in Ref. 3 and 4). {ECO:0000305}.
SEQUENCE 232 AA; 25446 MW; E4D71B19C6AE0D03 CRC64;
MSTESMIRDV ELAEEALPKK TGGPQGSRRC LFLSLFSFLI VAGATTLFCL LHFGVIGPQR
EEFPRDLSLI SPLAQAGSSS RTPSDKPVAH VVANPQAEGQ LQWLNRRANA LLANGVELRD
NQLVVPSEGL YLIYSQVLFK GQGCPSTHVL LTHTISRIAV SYQTKVNLLS AIKSPCQRET
PEGAEAKPWY EPIYLGGVFQ LEKGDRLSAE INRPDYLDFA ESGQVYFGII AL


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