TNR3_MOUSE
ID TNR3_MOUSE Reviewed; 415 AA.
AC P50284;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 3;
DE AltName: Full=Lymphotoxin-beta receptor;
DE Flags: Precursor;
GN Name=Ltbr; Synonyms=Tnfcr, Tnfrsf3;
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].
RC STRAIN=CVB; TISSUE=Lung;
RX PubMed=7594541;
RA Force W.R., Walter B.N., Hession C., Tizard R., Kozak C.A., Browning J.L.,
RA Ware C.F.;
RT "Mouse lymphotoxin-beta receptor. Molecular genetics, ligand binding, and
RT expression.";
RL J. Immunol. 155:5280-5288(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8586432; DOI=10.1006/geno.1995.9872;
RA Nakamura T., Tashiro K., Nazarea M., Nakano T., Sasayama S., Honjo T.;
RT "The murine lymphotoxin-beta receptor cDNA: isolation by the signal
RT sequence trap and chromosomal mapping.";
RL Genomics 30:312-319(1995).
RN [3]
RP INTERACTION WITH TRAF5.
RC STRAIN=BALB/cJ;
RX PubMed=8663299; DOI=10.1074/jbc.271.25.14661;
RA Nakano H., Oshima H., Chung W., Williams-Abbott L., Ware C.F., Yagita H.,
RA Okumura K.;
RT "TRAF5, an activator of NF-kappaB and putative signal transducer for the
RT lymphotoxin-beta receptor.";
RL J. Biol. Chem. 271:14661-14664(1996).
CC -!- FUNCTION: Receptor for the heterotrimeric lymphotoxin containing LTA
CC and LTB, and for TNFS14/LIGHT. Promotes apoptosis via TRAF3 and TRAF5.
CC May play a role in the development of lymphoid organs (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Self-associates (By similarity). Associates with TRAF5.
CC Associates with TRAF3 and TRAF4 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P50284; P39429: Traf2; NbExp=3; IntAct=EBI-647023, EBI-520016;
CC P50284; O43557: TNFSF14; Xeno; NbExp=2; IntAct=EBI-647023, EBI-524131;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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DR EMBL; U29173; AAA68964.1; -; mRNA.
DR EMBL; L38423; AAB00846.1; -; mRNA.
DR EMBL; U30798; AAA81334.1; -; Genomic_DNA.
DR CCDS; CCDS20549.1; -.
DR RefSeq; NP_034866.1; NM_010736.3.
DR AlphaFoldDB; P50284; -.
DR SMR; P50284; -.
DR BioGRID; 201222; 5.
DR DIP; DIP-49695N; -.
DR IntAct; P50284; 7.
DR STRING; 10090.ENSMUSP00000032489; -.
DR GlyGen; P50284; 2 sites.
DR PhosphoSitePlus; P50284; -.
DR MaxQB; P50284; -.
DR PaxDb; P50284; -.
DR PRIDE; P50284; -.
DR ProteomicsDB; 258811; -.
DR Antibodypedia; 10740; 909 antibodies from 37 providers.
DR DNASU; 17000; -.
DR Ensembl; ENSMUST00000032489; ENSMUSP00000032489; ENSMUSG00000030339.
DR GeneID; 17000; -.
DR KEGG; mmu:17000; -.
DR UCSC; uc009duj.1; mouse.
DR CTD; 4055; -.
DR MGI; MGI:104875; Ltbr.
DR VEuPathDB; HostDB:ENSMUSG00000030339; -.
DR eggNOG; ENOG502S4WF; Eukaryota.
DR GeneTree; ENSGT00940000162178; -.
DR HOGENOM; CLU_052594_0_0_1; -.
DR InParanoid; P50284; -.
DR OMA; SPCGLAW; -.
DR OrthoDB; 1104669at2759; -.
DR PhylomeDB; P50284; -.
DR TreeFam; TF331157; -.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR BioGRID-ORCS; 17000; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Ltbr; mouse.
DR PRO; PR:P50284; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P50284; protein.
DR Bgee; ENSMUSG00000030339; Expressed in granulocyte and 214 other tissues.
DR ExpressionAtlas; P50284; baseline and differential.
DR Genevisible; P50284; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0048535; P:lymph node development; TAS:MGI.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR CDD; cd10578; TNFRSF3; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR017349; TNFR_3_LTBR.
DR InterPro; IPR033997; TNFRSF3_N.
DR PANTHER; PTHR47607; PTHR47607; 1.
DR Pfam; PF00020; TNFR_c6; 3.
DR PIRSF; PIRSF037999; TNFR_3_LTBR; 1.
DR PRINTS; PR01920; TNFACTORR3.
DR SMART; SM00208; TNFR; 3.
DR PROSITE; PS00652; TNFR_NGFR_1; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 3.
PE 1: Evidence at protein level;
KW Apoptosis; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..415
FT /note="Tumor necrosis factor receptor superfamily member 3"
FT /id="PRO_0000034553"
FT TOPO_DOM 31..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 42..81
FT /note="TNFR-Cys 1"
FT REPEAT 82..124
FT /note="TNFR-Cys 2"
FT REPEAT 125..170
FT /note="TNFR-Cys 3"
FT REPEAT 171..213
FT /note="TNFR-Cys 4"
FT REGION 261..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..384
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36941"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 59..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 62..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 83..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 101..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 104..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 126..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 139..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 142..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 172..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 415 AA; 44956 MW; 29B326A566AEF661 CRC64;
MRLPRASSPC GLAWGPLLLG LSGLLVASQP QLVPPYRIEN QTCWDQDKEY YEPMHDVCCS
RCPPGEFVFA VCSRSQDTVC KTCPHNSYNE HWNHLSTCQL CRPCDIVLGF EEVAPCTSDR
KAECRCQPGM SCVYLDNECV HCEEERLVLC QPGTEAEVTD EIMDTDVNCV PCKPGHFQNT
SSPRARCQPH TRCEIQGLVE AAPGTSYSDT ICKNPPEPGA MLLLAILLSL VLFLLFTTVL
ACAWMRHPSL CRKLGTLLKR HPEGEESPPC PAPRADPHFP DLAEPLLPMS GDLSPSPAGP
PTAPSLEEVV LQQQSPLVQA RELEAEPGEH GQVAHGANGI HVTGGSVTVT GNIYIYNGPV
LGGTRGPGDP PAPPEPPYPT PEEGAPGPSE LSTPYQEDGK AWHLAETETL GCQDL
