TNR11_MOUSE
ID TNR11_MOUSE Reviewed; 625 AA.
AC O35305; Q8VCT7;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 11A;
DE AltName: Full=Osteoclast differentiation factor receptor;
DE Short=ODFR;
DE AltName: Full=Receptor activator of NF-KB;
DE AltName: CD_antigen=CD265;
DE Flags: Precursor;
GN Name=Tnfrsf11a; Synonyms=Rank;
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 TISSUE=Fetal liver;
RX PubMed=9367155; DOI=10.1038/36593;
RA Anderson D.M., Maraskovsky E., Billingsley W.L., Dougall W.C.,
RA Tometsko M.E., Roux E.R., Teepe M.C., DuBose R.F., Cosman D., Galibert L.;
RT "A homologue of the TNF receptor and its ligand enhance T-cell growth and
RT dendritic-cell function.";
RL Nature 390:175-179(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=9878548; DOI=10.1006/bbrc.1998.9788;
RA Nakagawa N., Kinosaki M., Yamaguchi K., Shima N., Yasuda H., Yano K.,
RA Morinaga T., Higashio K.;
RT "RANK is the essential signaling receptor for osteoclast differentiation
RT factor in osteoclastogenesis.";
RL Biochem. Biophys. Res. Commun. 253:395-400(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 26-210 ALONE AND IN COMPLEX WITH
RP TNFSF11, DISULFIDE BONDS, FUNCTION, SODIUM-BINDING SITE, AND SUBUNIT.
RX PubMed=20483727; DOI=10.4049/jimmunol.0904033;
RA Liu C., Walter T.S., Huang P., Zhang S., Zhu X., Wu Y., Wedderburn L.R.,
RA Tang P., Owens R.J., Stuart D.I., Ren J., Gao B.;
RT "Structural and functional insights of RANKL-RANK interaction and
RT signaling.";
RL J. Immunol. 184:6910-6919(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-198 IN COMPLEX WITH
RP TNFSF11/RANKL, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-106.
RX PubMed=23039992; DOI=10.1016/j.str.2012.08.030;
RA Nelson C.A., Warren J.T., Wang M.W., Teitelbaum S.L., Fremont D.H.;
RT "RANKL employs distinct binding modes to engage RANK and the
RT osteoprotegerin decoy receptor.";
RL Structure 20:1971-1982(2012).
CC -!- FUNCTION: Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-
CC mediated osteoclastogenesis. Involved in the regulation of interactions
CC between T-cells and dendritic cells. {ECO:0000269|PubMed:20483727,
CC ECO:0000269|PubMed:9878548}.
CC -!- SUBUNIT: Binds to the clefts between the subunits of the TNFSF11 ligand
CC trimer to form a heterohexamer. Interacts with TRAF1, TRAF2, TRAF3,
CC TRAF5 and TRAF6 (By similarity). Interacts (via cytoplasmic domain)
CC with GAB2 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O35305; Q9Z1R2: Bag6; NbExp=4; IntAct=EBI-647362, EBI-644645;
CC O35305; O35235-1: Tnfsf11; NbExp=6; IntAct=EBI-647362, EBI-15890886;
CC O35305; P39429: Traf2; NbExp=2; IntAct=EBI-647362, EBI-520016;
CC O35305; Q60803: Traf3; NbExp=3; IntAct=EBI-647362, EBI-520135;
CC O35305; P70196: Traf6; NbExp=2; IntAct=EBI-647362, EBI-448028;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous expression with high levels in
CC trabecular bone, thymus, small intestine, lung, brain and kidney.
CC Weakly expressed in spleen and bone marrow.
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DR EMBL; AF019046; AAB86810.1; -; mRNA.
DR EMBL; BC019185; AAH19185.1; -; mRNA.
DR CCDS; CCDS15207.1; -.
DR RefSeq; NP_033425.3; NM_009399.3.
DR PDB; 3ME2; X-ray; 2.80 A; R=26-210.
DR PDB; 3ME4; X-ray; 2.01 A; A/B=26-210.
DR PDB; 3QBQ; X-ray; 2.50 A; B/D=32-201.
DR PDB; 4GIQ; X-ray; 2.70 A; R=31-198.
DR PDB; 5BNQ; X-ray; 2.80 A; R=26-210.
DR PDBsum; 3ME2; -.
DR PDBsum; 3ME4; -.
DR PDBsum; 3QBQ; -.
DR PDBsum; 4GIQ; -.
DR PDBsum; 5BNQ; -.
DR AlphaFoldDB; O35305; -.
DR SMR; O35305; -.
DR BioGRID; 204246; 4.
DR DIP; DIP-48710N; -.
DR ELM; O35305; -.
DR IntAct; O35305; 11.
DR MINT; O35305; -.
DR STRING; 10090.ENSMUSP00000027559; -.
DR GlyGen; O35305; 2 sites.
DR iPTMnet; O35305; -.
DR PhosphoSitePlus; O35305; -.
DR MaxQB; O35305; -.
DR PaxDb; O35305; -.
DR PeptideAtlas; O35305; -.
DR PRIDE; O35305; -.
DR ProteomicsDB; 260632; -.
DR Antibodypedia; 4165; 812 antibodies from 43 providers.
DR DNASU; 21934; -.
DR Ensembl; ENSMUST00000027559; ENSMUSP00000027559; ENSMUSG00000026321.
DR GeneID; 21934; -.
DR KEGG; mmu:21934; -.
DR UCSC; uc007cgp.1; mouse.
DR CTD; 8792; -.
DR MGI; MGI:1314891; Tnfrsf11a.
DR VEuPathDB; HostDB:ENSMUSG00000026321; -.
DR eggNOG; ENOG502RWJI; Eukaryota.
DR GeneTree; ENSGT00940000161211; -.
DR HOGENOM; CLU_026571_0_0_1; -.
DR InParanoid; O35305; -.
DR OMA; CTCGLNF; -.
DR OrthoDB; 1038336at2759; -.
DR PhylomeDB; O35305; -.
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; 21934; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Tnfrsf11a; mouse.
DR EvolutionaryTrace; O35305; -.
DR PRO; PR:O35305; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O35305; protein.
DR Bgee; ENSMUSG00000026321; Expressed in left colon and 81 other tissues.
DR Genevisible; O35305; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019955; F:cytokine binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:MGI.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; IMP:BHF-UCL.
DR GO; GO:0002250; P:adaptive immune response; ISO:MGI.
DR GO; GO:0060086; P:circadian temperature homeostasis; IMP:BHF-UCL.
DR GO; GO:0048535; P:lymph node development; IMP:MGI.
DR GO; GO:0060749; P:mammary gland alveolus development; IMP:MGI.
DR GO; GO:0072674; P:multinuclear osteoclast differentiation; IMP:MGI.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; ISO:MGI.
DR GO; GO:0045780; P:positive regulation of bone resorption; IMP:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0071848; P:positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling; ISO:MGI.
DR GO; GO:0071812; P:positive regulation of fever generation by positive regulation of prostaglandin secretion; IMP:BHF-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:BHF-UCL.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; IMP:BHF-UCL.
DR GO; GO:0071847; P:TNFSF11-mediated signaling pathway; ISO:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:BHF-UCL.
DR CDD; cd13411; TNFRSF11A; 1.
DR InterPro; IPR041648; RANK_CRD_2.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR022323; TNFR_11.
DR InterPro; IPR022361; TNFR_11A.
DR InterPro; IPR034040; TNFRSF11A_N.
DR Pfam; PF18278; RANK_CRD_2; 1.
DR Pfam; PF00020; TNFR_c6; 1.
DR PRINTS; PR01961; TNFACTORR11.
DR PRINTS; PR01974; TNFACTORR11A.
DR SMART; SM00208; TNFR; 4.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Sodium; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..625
FT /note="Tumor necrosis factor receptor superfamily member
FT 11A"
FT /id="PRO_0000034586"
FT TOPO_DOM 31..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 35..69
FT /note="TNFR-Cys 1"
FT REPEAT 72..113
FT /note="TNFR-Cys 2"
FT REPEAT 115..152
FT /note="TNFR-Cys 3"
FT REPEAT 155..195
FT /note="TNFR-Cys 4"
FT REGION 331..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 135
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 138
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 161
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 163
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Q6"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23039992"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..47
FT DISULFID 48..61
FT DISULFID 51..69
FT DISULFID 72..87
FT DISULFID 93..113
FT DISULFID 115..128
FT DISULFID 125..127
FT DISULFID 134..152
FT DISULFID 155..170
FT DISULFID 176..195
FT CONFLICT 494
FT /note="R -> K (in Ref. 2; AAH19185)"
FT /evidence="ECO:0000305"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3QBQ"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3ME4"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3ME4"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4GIQ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3ME4"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3ME4"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3QBQ"
SQ SEQUENCE 625 AA; 66621 MW; F8C1872E99511D8E CRC64;
MAPRARRRRQ LPAPLLALCV LLVPLQVTLQ VTPPCTQERH YEHLGRCCSR CEPGKYLSSK
CTPTSDSVCL PCGPDEYLDT WNEEDKCLLH KVCDAGKALV AVDPGNHTAP RRCACTAGYH
WNSDCECCRR NTECAPGFGA QHPLQLNKDT VCTPCLLGFF SDVFSSTDKC KPWTNCTLLG
KLEAHQGTTE SDVVCSSSMT LRRPPKEAQA YLPSLIVLLL FISVVVVAAI IFGVYYRKGG
KALTANLWNW VNDACSSLSG NKESSGDRCA GSHSATSSQQ EVCEGILLMT REEKMVPEDG
AGVCGPVCAA GGPWAEVRDS RTFTLVSEVE TQGDLSRKIP TEDEYTDRPS QPSTGSLLLI
QQGSKSIPPF QEPLEVGEND SLSQCFTGTE STVDSEGCDF TEPPSRTDSM PVSPEKHLTK
EIEGDSCLPW VVSSNSTDGY TGSGNTPGED HEPFPGSLKC GPLPQCAYSM GFPSEAAASM
AEAGVRPQDR ADERGASGSG SSPSDQPPAS GNVTGNSNST FISSGQVMNF KGDIIVVYVS
QTSQEGPGSA EPESEPVGRP VQEETLAHRD SFAGTAPRFP DVCATGAGLQ EQGAPRQKDG
TSRPVQEQGG AQTSLHTQGS GQCAE
