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Tumor necrosis factor receptor superfamily member 1B (Tumor necrosis factor receptor 2) (TNF-R2) (Tumor necrosis factor receptor type II) (TNF-RII) (TNFR-II) (p75) (p80 TNF-alpha receptor) (CD antigen CD120b)

 TNR1B_MOUSE             Reviewed;         474 AA.
P25119; O88734; P97893;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
08-MAY-2019, entry version 166.
RecName: Full=Tumor necrosis factor receptor superfamily member 1B;
AltName: Full=Tumor necrosis factor receptor 2;
Short=TNF-R2;
AltName: Full=Tumor necrosis factor receptor type II;
Short=TNF-RII;
Short=TNFR-II;
AltName: Full=p75;
AltName: Full=p80 TNF-alpha receptor;
AltName: CD_antigen=CD120b;
Flags: Precursor;
Name=Tnfrsf1b; Synonyms=Tnfr-2, Tnfr2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1849278; DOI=10.1073/pnas.88.7.2830;
Lewis M., Tartaglia L.A., Lee A., Bennett G.L., Rice G.C., Wong G.H.,
Chen E.Y., Goeddel D.V.;
"Cloning and expression of cDNAs for two distinct murine tumor
necrosis factor receptors demonstrate one receptor is species
specific.";
Proc. Natl. Acad. Sci. U.S.A. 88:2830-2834(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1645445; DOI=10.1128/MCB.11.6.3020;
Goodwin R.G., Anderson D., Jerzy R., Davis T., Brannan C.I.,
Copeland N.G., Jenkins N.A., Smith C.A.;
"Molecular cloning and expression of the type 1 and type 2 murine
receptors for tumor necrosis factor.";
Mol. Cell. Biol. 11:3020-3026(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9740674; DOI=10.1006/geno.1998.5407;
Hurle B., Segade F., Rodriguez R., Ramos S.S., Lazo P.S.;
"The mouse tumor necrosis factor receptor 2 gene: genomic structure
and characterization of the two transcripts.";
Genomics 52:79-89(1998).
[4]
NUCLEOTIDE SEQUENCE OF 1-26.
STRAIN=NOD;
Jacob C.O., Liu J.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE OF 1-22.
TISSUE=Liver;
Kissonerghis M., Fellowes R., Feldmann M., Chernajovsky Y.;
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Receptor with high affinity for TNFSF2/TNF-alpha and
approximately 5-fold lower affinity for homotrimeric
TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the
apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Binds to TRAF2. Interacts with BMX. Interacts (activated
form) with XPNPEP3. {ECO:0000250|UniProtKB:P20333}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-----------------------------------------------------------------------
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EMBL; M60469; AAA39752.1; -; mRNA.
EMBL; M59378; AAA40463.1; -; mRNA.
EMBL; Y14619; CAA74969.1; -; Genomic_DNA.
EMBL; Y14620; CAA74969.1; JOINED; Genomic_DNA.
EMBL; Y14621; CAA74969.1; JOINED; Genomic_DNA.
EMBL; Y14622; CAA74969.1; JOINED; Genomic_DNA.
EMBL; Y14679; CAA74969.1; JOINED; Genomic_DNA.
EMBL; Y14623; CAA74969.1; JOINED; Genomic_DNA.
EMBL; U39488; AAA85021.1; -; Genomic_DNA.
EMBL; X87128; CAA60618.1; -; Genomic_DNA.
CCDS; CCDS18914.1; -.
PIR; B38634; B38634.
RefSeq; NP_035740.2; NM_011610.3.
SMR; P25119; -.
BioGrid; 204250; 4.
DIP; DIP-60902N; -.
IntAct; P25119; 4.
MINT; P25119; -.
STRING; 10090.ENSMUSP00000030336; -.
PhosphoSitePlus; P25119; -.
SwissPalm; P25119; -.
EPD; P25119; -.
PaxDb; P25119; -.
PeptideAtlas; P25119; -.
PRIDE; P25119; -.
Ensembl; ENSMUST00000030336; ENSMUSP00000030336; ENSMUSG00000028599.
GeneID; 21938; -.
KEGG; mmu:21938; -.
UCSC; uc008vrt.1; mouse.
CTD; 7133; -.
MGI; MGI:1314883; Tnfrsf1b.
eggNOG; ENOG410IJ06; Eukaryota.
eggNOG; ENOG410YPQW; LUCA.
GeneTree; ENSGT00940000161800; -.
HOGENOM; HOG000132845; -.
InParanoid; P25119; -.
KO; K05141; -.
OMA; CVIMTQV; -.
OrthoDB; 559890at2759; -.
PhylomeDB; P25119; -.
TreeFam; TF331157; -.
Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Tnfrsf1b; mouse.
PRO; PR:P25119; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028599; Expressed in 172 organ(s), highest expression level in bone marrow macrophage.
ExpressionAtlas; P25119; baseline and differential.
Genevisible; P25119; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0043196; C:varicosity; ISO:MGI.
GO; GO:0043120; F:tumor necrosis factor binding; ISO:MGI.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; IPI:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0003176; P:aortic valve development; IGI:BHF-UCL.
GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:MGI.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0150098; P:glial cell-neuron signaling; IMP:ARUK-UCL.
GO; GO:0006955; P:immune response; ISO:MGI.
GO; GO:0006954; P:inflammatory response; IMP:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IGI:BHF-UCL.
GO; GO:0060548; P:negative regulation of cell death; IMP:ARUK-UCL.
GO; GO:0003332; P:negative regulation of extracellular matrix constituent secretion; IGI:BHF-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
GO; GO:0150079; P:negative regulation of neuroinflammatory response; IMP:ARUK-UCL.
GO; GO:1901215; P:negative regulation of neuron death; IMP:ARUK-UCL.
GO; GO:1902339; P:positive regulation of apoptotic process involved in morphogenesis; IGI:BHF-UCL.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:MGI.
GO; GO:0031643; P:positive regulation of myelination; IMP:ARUK-UCL.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:ARUK-UCL.
GO; GO:0003177; P:pulmonary valve development; IGI:BHF-UCL.
GO; GO:0002739; P:regulation of cytokine secretion involved in immune response; IGI:ARUK-UCL.
GO; GO:0031641; P:regulation of myelination; IGI:ARUK-UCL.
GO; GO:0150077; P:regulation of neuroinflammatory response; IGI:ARUK-UCL.
GO; GO:2001141; P:regulation of RNA biosynthetic process; IMP:ARUK-UCL.
GO; GO:0002724; P:regulation of T cell cytokine production; IMP:ARUK-UCL.
GO; GO:0042129; P:regulation of T cell proliferation; IMP:ARUK-UCL.
GO; GO:0050779; P:RNA destabilization; IMP:MGI.
CDD; cd10577; TNFRSF1B; 1.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR020411; TNFR_1B.
InterPro; IPR033996; TNFRSF1B_N.
Pfam; PF00020; TNFR_c6; 2.
PRINTS; PR01919; TNFACTORR1B.
SMART; SM00208; TNFR; 4.
PROSITE; PS00652; TNFR_NGFR_1; 2.
PROSITE; PS50050; TNFR_NGFR_2; 3.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 22
CHAIN 23 474 Tumor necrosis factor receptor
superfamily member 1B.
/FTId=PRO_0000034550.
TOPO_DOM 23 258 Extracellular. {ECO:0000255}.
TRANSMEM 259 288 Helical. {ECO:0000255}.
TOPO_DOM 289 474 Cytoplasmic. {ECO:0000255}.
REPEAT 39 77 TNFR-Cys 1.
REPEAT 78 119 TNFR-Cys 2.
REPEAT 120 164 TNFR-Cys 3.
REPEAT 165 203 TNFR-Cys 4.
MOD_RES 331 331 Phosphoserine.
{ECO:0000250|UniProtKB:P20333}.
CARBOHYD 30 30 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:P20333}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 208 208 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:P20333}.
CARBOHYD 224 224 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:P20333}.
DISULFID 40 54 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 55 68 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 58 76 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 79 94 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 97 111 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 101 119 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 121 127 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 136 145 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 139 163 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 166 181 {ECO:0000255|PROSITE-ProRule:PRU00206}.
CONFLICT 78 78 D -> DSDTVCAD (in Ref. 3; CAA74969).
{ECO:0000305}.
CONFLICT 102 102 T -> S (in Ref. 3; CAA74969).
{ECO:0000305}.
CONFLICT 108 108 I -> T (in Ref. 3; CAA74969).
{ECO:0000305}.
CONFLICT 283 283 I -> F (in Ref. 3; CAA74969).
{ECO:0000305}.
CONFLICT 331 331 S -> SS (in Ref. 3; CAA74969).
{ECO:0000305}.
CONFLICT 360 360 F -> S (in Ref. 3; CAA74969).
{ECO:0000305}.
CONFLICT 436 436 C -> Y (in Ref. 3; CAA74969).
{ECO:0000305}.
SEQUENCE 474 AA; 50320 MW; 462EAE398C4D6563 CRC64;
MAPAALWVAL VFELQLWATG HTVPAQVVLT PYKPEPGYEC QISQEYYDRK AQMCCAKCPP
GQYVKHFCNK TSDTVCADCE ASMYTQVWNQ FRTCLSCSSS CTTDQVEIRA CTKQQNRVCA
CEAGRYCALK THSGSCRQCM RLSKCGPGFG VASSRAPNGN VLCKACAPGT FSDTTSSTDV
CRPHRICSIL AIPGNASTDA VCAPESPTLS AIPRTLYVSQ PEPTRSQPLD QEPGPSQTPS
ILTSLGSTPI IEQSTKGGIS LPIGLIVGVT SLGLLMLGLV NCIILVQRKK KPSCLQRDAK
VPHVPDEKSQ DAVGLEQQHL LTTAPSSSSS SLESSASAGD RRAPPGGHPQ ARVMAEAQGF
QEARASSRIS DSSHGSHGTH VNVTCIVNVC SSSDHSSQCS SQASATVGDP DAKPSASPKD
EQVPFSQEEC PSQSPCETTE TLQSHEKPLP LGVPDMGMKP SQAGWFDQIA VKVA


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