TNR1B_RAT
ID TNR1B_RAT Reviewed; 474 AA.
AC Q80WY6; Q5YLP0;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=Tnfr2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Spleen;
RA Li Y., Ji A., Schafer M.K.;
RT "Molecular cloning and cellular expression of TNFR2 in rat dorsal root
RT ganglion.";
RL Submitted (JUL-2003) 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 {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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; AF498039; AAP33151.1; -; mRNA.
DR EMBL; AY191268; AAO61402.1; -; mRNA.
DR EMBL; AY191269; AAO61403.1; -; mRNA.
DR RefSeq; NP_569110.1; NM_130426.4.
DR AlphaFoldDB; Q80WY6; -.
DR SMR; Q80WY6; -.
DR IntAct; Q80WY6; 1.
DR STRING; 10116.ENSRNOP00000022478; -.
DR GlyGen; Q80WY6; 6 sites.
DR PaxDb; Q80WY6; -.
DR PRIDE; Q80WY6; -.
DR Ensembl; ENSRNOT00000022478; ENSRNOP00000022478; ENSRNOG00000016575.
DR GeneID; 156767; -.
DR KEGG; rno:156767; -.
DR CTD; 7133; -.
DR RGD; 621238; Tnfrsf1b.
DR eggNOG; ENOG502RZ23; Eukaryota.
DR GeneTree; ENSGT00940000161800; -.
DR HOGENOM; CLU_047256_0_0_1; -.
DR InParanoid; Q80WY6; -.
DR OMA; HKKCGKG; -.
DR OrthoDB; 559890at2759; -.
DR PhylomeDB; Q80WY6; -.
DR TreeFam; TF331157; -.
DR Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-RNO-5669034; TNFs bind their physiological receptors.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q80WY6; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016575; Expressed in spleen and 18 other tissues.
DR Genevisible; Q80WY6; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0043196; C:varicosity; IDA:RGD.
DR GO; GO:0043120; F:tumor necrosis factor binding; ISO:RGD.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; IDA:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0003176; P:aortic valve development; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0150098; P:glial cell-neuron signaling; ISO:RGD.
DR GO; GO:0006955; P:immune response; IDA:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:RGD.
DR GO; GO:0003332; P:negative regulation of extracellular matrix constituent secretion; ISO:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0150079; P:negative regulation of neuroinflammatory response; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:RGD.
DR GO; GO:1902339; P:positive regulation of apoptotic process involved in morphogenesis; ISO:RGD.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:RGD.
DR GO; GO:0031643; P:positive regulation of myelination; ISO:RGD.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:0003177; P:pulmonary valve development; ISO:RGD.
DR GO; GO:0002718; P:regulation of cytokine production involved in immune response; ISO:RGD.
DR GO; GO:0031641; P:regulation of myelination; ISO:RGD.
DR GO; GO:0150077; P:regulation of neuroinflammatory response; ISO:RGD.
DR GO; GO:2001141; P:regulation of RNA biosynthetic process; ISO:RGD.
DR GO; GO:0002724; P:regulation of T cell cytokine production; ISO:RGD.
DR GO; GO:0042129; P:regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0050779; P:RNA destabilization; ISO:RGD.
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 /evidence="ECO:0000250"
FT CHAIN 23..474
FT /note="Tumor necrosis factor receptor superfamily member
FT 1B"
FT /id="PRO_0000034551"
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..241
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..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..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 110
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"
SQ SEQUENCE 474 AA; 50148 MW; 298C6AB9E8C8D714 CRC64;
MAPAALWVAL VVELQLWATG HTVPAKVVLT PYKPEPGNQC QISQEYYDKK AQMCCAKCPP
GQYAKHFCNK TSDTVCADCA AGMFTQVWNH LHTCLSCSSS CSDDQVETHN CTKKQNRVCA
CNADSYCALK LHSGNCRQCM KLSKCGPGFG VARSRTSNGN VICSACAPGT FSDTTSSTDV
CRPHRICSIL AIPGNASTDA VCASESPTPS AVPRTIYVSQ PEPTRSQPMD QEPGPSQTPH
IPVSLGSTPI IEPSITGGIS LPIGLIVGLT TLGLLMLGLA NCFILVQRKK KPSCLQRETM
VPHLPDDKSQ DAIGLEQQHL LTTAPSSSSS SLESSASAGD RRAPPGGHPQ ARVTAEAQGS
QEACAGSRSS DSSHGSHGTH VNVTCIVNVC SSSDHSSQCS SQASTTVGDP DANPSGSPKD
EQVPFSQEEC PSQSQWETTE TLQNHDKPFP LGVPDVGMKP NQPGWYDQIA VKVP
