TNR1B_MOUSE
ID TNR1B_MOUSE Reviewed; 474 AA.
AC P25119; O88734; P97893;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 1B;
DE AltName: Full=Tumor necrosis factor receptor 2;
DE Short=TNF-R2;
DE AltName: Full=Tumor necrosis factor receptor type II;
DE Short=TNF-RII;
DE Short=TNFR-II;
DE AltName: Full=p75;
DE AltName: Full=p80 TNF-alpha receptor;
DE AltName: CD_antigen=CD120b;
DE Flags: Precursor;
GN Name=Tnfrsf1b; Synonyms=Tnfr-2, Tnfr2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1849278; DOI=10.1073/pnas.88.7.2830;
RA Lewis M., Tartaglia L.A., Lee A., Bennett G.L., Rice G.C., Wong G.H.,
RA Chen E.Y., Goeddel D.V.;
RT "Cloning and expression of cDNAs for two distinct murine tumor necrosis
RT factor receptors demonstrate one receptor is species specific.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2830-2834(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1645445; DOI=10.1128/mcb.11.6.3020-3026.1991;
RA Goodwin R.G., Anderson D., Jerzy R., Davis T., Brannan C.I., Copeland N.G.,
RA Jenkins N.A., Smith C.A.;
RT "Molecular cloning and expression of the type 1 and type 2 murine receptors
RT for tumor necrosis factor.";
RL Mol. Cell. Biol. 11:3020-3026(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9740674; DOI=10.1006/geno.1998.5407;
RA Hurle B., Segade F., Rodriguez R., Ramos S.S., Lazo P.S.;
RT "The mouse tumor necrosis factor receptor 2 gene: genomic structure and
RT characterization of the two transcripts.";
RL Genomics 52:79-89(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-26.
RC STRAIN=NOD;
RA Jacob C.O., Liu J.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE OF 1-22.
RC TISSUE=Liver;
RA Kissonerghis M., Fellowes R., Feldmann M., Chernajovsky Y.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor with high affinity for TNFSF2/TNF-alpha and
CC approximately 5-fold lower affinity for homotrimeric
CC TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the
CC apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to TRAF2. Interacts with BMX. Interacts (activated form)
CC with XPNPEP3. {ECO:0000250|UniProtKB:P20333}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M60469; AAA39752.1; -; mRNA.
DR EMBL; M59378; AAA40463.1; -; mRNA.
DR EMBL; Y14619; CAA74969.1; -; Genomic_DNA.
DR EMBL; Y14620; CAA74969.1; JOINED; Genomic_DNA.
DR EMBL; Y14621; CAA74969.1; JOINED; Genomic_DNA.
DR EMBL; Y14622; CAA74969.1; JOINED; Genomic_DNA.
DR EMBL; Y14679; CAA74969.1; JOINED; Genomic_DNA.
DR EMBL; Y14623; CAA74969.1; JOINED; Genomic_DNA.
DR EMBL; U39488; AAA85021.1; -; Genomic_DNA.
DR EMBL; X87128; CAA60618.1; -; Genomic_DNA.
DR CCDS; CCDS18914.1; -.
DR PIR; B38634; B38634.
DR RefSeq; NP_035740.2; NM_011610.3.
DR AlphaFoldDB; P25119; -.
DR SMR; P25119; -.
DR BioGRID; 204250; 4.
DR DIP; DIP-60902N; -.
DR IntAct; P25119; 4.
DR MINT; P25119; -.
DR STRING; 10090.ENSMUSP00000030336; -.
DR GlyGen; P25119; 5 sites.
DR PhosphoSitePlus; P25119; -.
DR SwissPalm; P25119; -.
DR EPD; P25119; -.
DR PaxDb; P25119; -.
DR PeptideAtlas; P25119; -.
DR PRIDE; P25119; -.
DR ProteomicsDB; 259480; -.
DR Antibodypedia; 1344; 1073 antibodies from 47 providers.
DR DNASU; 21938; -.
DR Ensembl; ENSMUST00000030336; ENSMUSP00000030336; ENSMUSG00000028599.
DR GeneID; 21938; -.
DR KEGG; mmu:21938; -.
DR UCSC; uc008vrt.1; mouse.
DR CTD; 7133; -.
DR MGI; MGI:1314883; Tnfrsf1b.
DR VEuPathDB; HostDB:ENSMUSG00000028599; -.
DR eggNOG; ENOG502RZ23; Eukaryota.
DR GeneTree; ENSGT00940000161800; -.
DR HOGENOM; CLU_047256_0_0_1; -.
DR InParanoid; P25119; -.
DR OMA; HKKCGKG; -.
DR OrthoDB; 559890at2759; -.
DR PhylomeDB; P25119; -.
DR TreeFam; TF331157; -.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 21938; 10 hits in 76 CRISPR screens.
DR ChiTaRS; Tnfrsf1b; mouse.
DR PRO; PR:P25119; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P25119; protein.
DR Bgee; ENSMUSG00000028599; Expressed in decidua and 161 other tissues.
DR ExpressionAtlas; P25119; baseline and differential.
DR Genevisible; P25119; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0043196; C:varicosity; ISO:MGI.
DR GO; GO:0043120; F:tumor necrosis factor binding; ISO:MGI.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; IPI:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0003176; P:aortic valve development; IGI:BHF-UCL.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0150098; P:glial cell-neuron signaling; IMP:ARUK-UCL.
DR GO; GO:0006955; P:immune response; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IGI:BHF-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:ARUK-UCL.
DR GO; GO:0003332; P:negative regulation of extracellular matrix constituent secretion; IGI:BHF-UCL.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0150079; P:negative regulation of neuroinflammatory response; IMP:ARUK-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:ARUK-UCL.
DR GO; GO:1902339; P:positive regulation of apoptotic process involved in morphogenesis; IGI:BHF-UCL.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:MGI.
DR GO; GO:0031643; P:positive regulation of myelination; IMP:ARUK-UCL.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:ARUK-UCL.
DR GO; GO:0003177; P:pulmonary valve development; IGI:BHF-UCL.
DR GO; GO:0002718; P:regulation of cytokine production involved in immune response; IGI:ARUK-UCL.
DR GO; GO:0031641; P:regulation of myelination; IGI:ARUK-UCL.
DR GO; GO:0150077; P:regulation of neuroinflammatory response; IGI:ARUK-UCL.
DR GO; GO:2001141; P:regulation of RNA biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:0002724; P:regulation of T cell cytokine production; IMP:ARUK-UCL.
DR GO; GO:0042129; P:regulation of T cell proliferation; IMP:ARUK-UCL.
DR GO; GO:0050779; P:RNA destabilization; IMP:MGI.
DR CDD; cd10577; TNFRSF1B; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020411; TNFR_1B.
DR InterPro; IPR033996; TNFRSF1B_N.
DR Pfam; PF00020; TNFR_c6; 2.
DR PRINTS; PR01919; TNFACTORR1B.
DR SMART; SM00208; TNFR; 4.
DR PROSITE; PS00652; TNFR_NGFR_1; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 3.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT CHAIN 23..474
FT /note="Tumor necrosis factor receptor superfamily member
FT 1B"
FT /id="PRO_0000034550"
FT TOPO_DOM 23..258
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 39..77
FT /note="TNFR-Cys 1"
FT REPEAT 78..119
FT /note="TNFR-Cys 2"
FT REPEAT 120..164
FT /note="TNFR-Cys 3"
FT REPEAT 165..203
FT /note="TNFR-Cys 4"
FT REGION 220..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20333"
FT CARBOHYD 30
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P20333"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P20333"
FT CARBOHYD 224
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P20333"
FT DISULFID 40..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 55..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 58..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 79..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 97..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 101..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 121..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 136..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 139..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 166..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT CONFLICT 78
FT /note="D -> DSDTVCAD (in Ref. 3; CAA74969)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="T -> S (in Ref. 3; CAA74969)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="I -> T (in Ref. 3; CAA74969)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="I -> F (in Ref. 3; CAA74969)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="S -> SS (in Ref. 3; CAA74969)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="F -> S (in Ref. 3; CAA74969)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="C -> Y (in Ref. 3; CAA74969)"
FT /evidence="ECO:0000305"
SQ 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
