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O35305 (TNR11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor receptor superfamily member 11A
Alternative name(s):
Osteoclast differentiation factor receptor
Short name=ODFR
Receptor activator of NF-KB
CD_antigen=CD265
Gene names
Name:Tnfrsf11a
Synonyms:Rank
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length625 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis. Involved in the regulation of interactions between T-cells and dendritic cells. Ref.3 Ref.4

Subunit structure

Binds to the clefts between the subunits of the TNFSF11 ligand trimer to form a heterohexamer. Interacts with TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6 By similarity. Interacts (via cytoplasmic domain) with GAB2 By similarity. Ref.4

Subcellular location

Cell membrane By similarity; Single-pass type I membrane protein Potential.

Tissue specificity

Ubiquitous expression with high levels in trabecular bone, thymus, small intestine, lung, brain and kidney. Weakly expressed in spleen and bone marrow.

Sequence similarities

Contains 4 TNFR-Cys repeats.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandMetal-binding
Sodium
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadaptive immune response

Inferred from electronic annotation. Source: Ensembl

circadian temperature homeostasis

Inferred from mutant phenotype PubMed 19940926. Source: BHF-UCL

lymph node development

Inferred from mutant phenotype PubMed 10500098. Source: MGI

mammary gland alveolus development

Inferred from mutant phenotype PubMed 11051546. Source: MGI

multicellular organismal development

Inferred from mutant phenotype PubMed 10500098. Source: MGI

ossification

Inferred from mutant phenotype PubMed 10500098. Source: MGI

osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of fever generation by positive regulation of prostaglandin secretion

Inferred from mutant phenotype PubMed 19940926. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 19940926. Source: BHF-UCL

response to interleukin-1

Inferred from mutant phenotype PubMed 19940926. Source: BHF-UCL

response to lipopolysaccharide

Inferred from mutant phenotype PubMed 19940926. Source: BHF-UCL

response to radiation

Inferred from electronic annotation. Source: Ensembl

response to tumor necrosis factor

Inferred from mutant phenotype PubMed 19940926. Source: BHF-UCL

tumor necrosis factor-mediated signaling pathway

Inferred from mutant phenotype PubMed 19940926. Source: BHF-UCL

   Cellular_componentcell surface

Inferred from direct assay PubMed 21844205. Source: MGI

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 10097072PubMed 15102471. Source: IntAct

tumor necrosis factor-activated receptor activity

Inferred from mutant phenotype PubMed 19940926. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 625595Tumor necrosis factor receptor superfamily member 11A
PRO_0000034586

Regions

Topological domain31 – 214184Extracellular Potential
Transmembrane215 – 23420Helical; Potential
Topological domain235 – 625391Cytoplasmic Potential
Repeat35 – 6935TNFR-Cys 1
Repeat72 – 11342TNFR-Cys 2
Repeat115 – 15238TNFR-Cys 3
Repeat155 – 19541TNFR-Cys 4

Sites

Metal binding1341Sodium; via carbonyl oxygen
Metal binding1351Sodium; via carbonyl oxygen
Metal binding1381Sodium; via carbonyl oxygen
Metal binding1611Sodium; via carbonyl oxygen
Metal binding1631Sodium; via carbonyl oxygen

Amino acid modifications

Glycosylation1061N-linked (GlcNAc...) Ref.5
Glycosylation1751N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 47 Ref.4 Ref.5
Disulfide bond48 ↔ 61 Ref.4 Ref.5
Disulfide bond51 ↔ 69 Ref.4 Ref.5
Disulfide bond72 ↔ 87 Ref.4 Ref.5
Disulfide bond93 ↔ 113 Ref.4 Ref.5
Disulfide bond115 ↔ 128 Ref.4 Ref.5
Disulfide bond125 ↔ 127 Ref.4 Ref.5
Disulfide bond134 ↔ 152 Ref.4 Ref.5
Disulfide bond155 ↔ 170 Ref.4 Ref.5
Disulfide bond176 ↔ 195 Ref.4 Ref.5

Experimental info

Sequence conflict4941R → K in AAH19185. Ref.2

Secondary structure

........................................... 625
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O35305 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F8C1872E99511D8E

FASTA62566,621
        10         20         30         40         50         60 
MAPRARRRRQ LPAPLLALCV LLVPLQVTLQ VTPPCTQERH YEHLGRCCSR CEPGKYLSSK 

        70         80         90        100        110        120 
CTPTSDSVCL PCGPDEYLDT WNEEDKCLLH KVCDAGKALV AVDPGNHTAP RRCACTAGYH 

       130        140        150        160        170        180 
WNSDCECCRR NTECAPGFGA QHPLQLNKDT VCTPCLLGFF SDVFSSTDKC KPWTNCTLLG 

       190        200        210        220        230        240 
KLEAHQGTTE SDVVCSSSMT LRRPPKEAQA YLPSLIVLLL FISVVVVAAI IFGVYYRKGG 

       250        260        270        280        290        300 
KALTANLWNW VNDACSSLSG NKESSGDRCA GSHSATSSQQ EVCEGILLMT REEKMVPEDG 

       310        320        330        340        350        360 
AGVCGPVCAA GGPWAEVRDS RTFTLVSEVE TQGDLSRKIP TEDEYTDRPS QPSTGSLLLI 

       370        380        390        400        410        420 
QQGSKSIPPF QEPLEVGEND SLSQCFTGTE STVDSEGCDF TEPPSRTDSM PVSPEKHLTK 

       430        440        450        460        470        480 
EIEGDSCLPW VVSSNSTDGY TGSGNTPGED HEPFPGSLKC GPLPQCAYSM GFPSEAAASM 

       490        500        510        520        530        540 
AEAGVRPQDR ADERGASGSG SSPSDQPPAS GNVTGNSNST FISSGQVMNF KGDIIVVYVS 

       550        560        570        580        590        600 
QTSQEGPGSA EPESEPVGRP VQEETLAHRD SFAGTAPRFP DVCATGAGLQ EQGAPRQKDG 

       610        620 
TSRPVQEQGG AQTSLHTQGS GQCAE 

« Hide

References

« Hide 'large scale' references
[1]"A homologue of the TNF receptor and its ligand enhance T-cell growth and dendritic-cell function."
Anderson D.M., Maraskovsky E., Billingsley W.L., Dougall W.C., Tometsko M.E., Roux E.R., Teepe M.C., DuBose R.F., Cosman D., Galibert L.
Nature 390:175-179(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[3]"RANK is the essential signaling receptor for osteoclast differentiation factor in osteoclastogenesis."
Nakagawa N., Kinosaki M., Yamaguchi K., Shima N., Yasuda H., Yano K., Morinaga T., Higashio K.
Biochem. Biophys. Res. Commun. 253:395-400(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Structural and functional insights of RANKL-RANK interaction and signaling."
Liu C., Walter T.S., Huang P., Zhang S., Zhu X., Wu Y., Wedderburn L.R., Tang P., Owens R.J., Stuart D.I., Ren J., Gao B.
J. Immunol. 184:6910-6919(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 26-210 ALONE AND IN COMPLEX WITH TNFSF11, DISULFIDE BONDS, FUNCTION, SODIUM-BINDING SITE, SUBUNIT.
[5]"RANKL employs distinct binding modes to engage RANK and the osteoprotegerin decoy receptor."
Nelson C.A., Warren J.T., Wang M.W., Teitelbaum S.L., Fremont D.H.
Structure 20:1971-1982(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-198 IN COMPLEX WITH TNFSF11/RANKL, DISULFIDE BONDS, GLYCOSYLATION AT ASN-106.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF019046 mRNA. Translation: AAB86810.1.
BC019185 mRNA. Translation: AAH19185.1.
CCDSCCDS15207.1.
RefSeqNP_033425.3. NM_009399.3.
UniGeneMm.6251.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ME2X-ray2.80R26-210[»]
3ME4X-ray2.01A/B26-210[»]
3QBQX-ray2.50B/D32-201[»]
4GIQX-ray2.70R31-198[»]
ProteinModelPortalO35305.
SMRO35305. Positions 33-201.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204246. 4 interactions.
DIPDIP-48710N.
IntActO35305. 10 interactions.
STRING10090.ENSMUSP00000027559.

PTM databases

PhosphoSiteO35305.

Proteomic databases

PaxDbO35305.
PRIDEO35305.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027559; ENSMUSP00000027559; ENSMUSG00000026321.
GeneID21934.
KEGGmmu:21934.
UCSCuc007cgp.1. mouse.

Organism-specific databases

CTD8792.
MGIMGI:1314891. Tnfrsf11a.

Phylogenomic databases

eggNOGNOG45473.
GeneTreeENSGT00740000115372.
HOGENOMHOG000154659.
HOVERGENHBG079274.
InParanoidO35305.
KOK05147.
OMACPHWAAS.
OrthoDBEOG786H2Q.
PhylomeDBO35305.
TreeFamTF331157.

Gene expression databases

BgeeO35305.
GenevestigatorO35305.

Family and domain databases

InterProIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022323. TNFR_11.
IPR022361. TNFR_11A.
[Graphical view]
PfamPF00020. TNFR_c6. 1 hit.
[Graphical view]
PRINTSPR01961. TNFACTORR11.
PR01974. TNFACTORR11A.
SMARTSM00208. TNFR. 4 hits.
[Graphical view]
PROSITEPS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNFRSF11A. mouse.
EvolutionaryTraceO35305.
NextBio301532.
PROO35305.
SOURCESearch...

Entry information

Entry nameTNR11_MOUSE
AccessionPrimary (citable) accession number: O35305
Secondary accession number(s): Q8VCT7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot