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O35305

- TNR11_MOUSE

UniProt

O35305 - TNR11_MOUSE

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Protein

Tumor necrosis factor receptor superfamily member 11A

Gene

Tnfrsf11a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis. Involved in the regulation of interactions between T-cells and dendritic cells.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi134 – 1341Sodium; via carbonyl oxygen
Metal bindingi135 – 1351Sodium; via carbonyl oxygen
Metal bindingi138 – 1381Sodium; via carbonyl oxygen
Metal bindingi161 – 1611Sodium; via carbonyl oxygen
Metal bindingi163 – 1631Sodium; via carbonyl oxygen

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. tumor necrosis factor-activated receptor activity Source: BHF-UCL

GO - Biological processi

  1. adaptive immune response Source: Ensembl
  2. circadian temperature homeostasis Source: BHF-UCL
  3. lymph node development Source: MGI
  4. mammary gland alveolus development Source: MGI
  5. multicellular organismal development Source: MGI
  6. ossification Source: MGI
  7. osteoclast differentiation Source: Ensembl
  8. positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling Source: Ensembl
  9. positive regulation of fever generation by positive regulation of prostaglandin secretion Source: BHF-UCL
  10. positive regulation of JUN kinase activity Source: Ensembl
  11. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  12. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  13. response to interleukin-1 Source: BHF-UCL
  14. response to lipopolysaccharide Source: BHF-UCL
  15. response to radiation Source: Ensembl
  16. response to tumor necrosis factor Source: BHF-UCL
  17. tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Metal-binding, Sodium

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Tnfrsf11a
Synonyms:Rank
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1314891. Tnfrsf11a.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: MGI
  2. external side of plasma membrane Source: Ensembl
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 625595Tumor necrosis factor receptor superfamily member 11APRO_0000034586Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 47
Disulfide bondi48 ↔ 61
Disulfide bondi51 ↔ 69
Disulfide bondi72 ↔ 87
Disulfide bondi93 ↔ 113
Glycosylationi106 – 1061N-linked (GlcNAc...)1 Publication
Disulfide bondi115 ↔ 128
Disulfide bondi125 ↔ 127
Disulfide bondi134 ↔ 152
Disulfide bondi155 ↔ 170
Glycosylationi175 – 1751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi176 ↔ 195

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO35305.
PRIDEiO35305.

PTM databases

PhosphoSiteiO35305.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO35305.
GenevestigatoriO35305.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Bag6Q9Z1R24EBI-647362,EBI-644645
Traf2P394292EBI-647362,EBI-520016
Traf3Q608033EBI-647362,EBI-520135
Traf6P701962EBI-647362,EBI-448028

Protein-protein interaction databases

BioGridi204246. 4 interactions.
DIPiDIP-48710N.
IntActiO35305. 10 interactions.
STRINGi10090.ENSMUSP00000027559.

Structurei

Secondary structure

1
625
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni37 – 393
Beta strandi40 – 434
Beta strandi46 – 494
Beta strandi55 – 595
Beta strandi63 – 653
Beta strandi68 – 714
Beta strandi80 – 823
Helixi95 – 973
Beta strandi99 – 1035
Beta strandi107 – 1093
Beta strandi112 – 1154
Beta strandi119 – 1224
Turni123 – 1264
Beta strandi127 – 1304
Beta strandi138 – 1403
Beta strandi142 – 1454
Beta strandi146 – 1483
Beta strandi152 – 1543
Beta strandi165 – 1673
Helixi176 – 1794
Beta strandi183 – 1853
Beta strandi189 – 1913
Beta strandi194 – 1963

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ME2X-ray2.80R26-210[»]
3ME4X-ray2.01A/B26-210[»]
3QBQX-ray2.50B/D32-201[»]
4GIQX-ray2.70R31-198[»]
ProteinModelPortaliO35305.
SMRiO35305. Positions 33-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35305.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 214184ExtracellularSequence AnalysisAdd
BLAST
Topological domaini235 – 625391CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei215 – 23420HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati35 – 6935TNFR-Cys 1Add
BLAST
Repeati72 – 11342TNFR-Cys 2Add
BLAST
Repeati115 – 15238TNFR-Cys 3Add
BLAST
Repeati155 – 19541TNFR-Cys 4Add
BLAST

Sequence similaritiesi

Contains 4 TNFR-Cys repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG45473.
GeneTreeiENSGT00760000119204.
HOGENOMiHOG000154659.
HOVERGENiHBG079274.
InParanoidiO35305.
KOiK05147.
OMAiCPHWAAS.
OrthoDBiEOG786H2Q.
PhylomeDBiO35305.
TreeFamiTF331157.

Family and domain databases

InterProiIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022323. TNFR_11.
IPR022361. TNFR_11A.
[Graphical view]
PfamiPF00020. TNFR_c6. 1 hit.
[Graphical view]
PRINTSiPR01961. TNFACTORR11.
PR01974. TNFACTORR11A.
SMARTiSM00208. TNFR. 4 hits.
[Graphical view]
PROSITEiPS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35305-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPRARRRRQ LPAPLLALCV LLVPLQVTLQ VTPPCTQERH YEHLGRCCSR
60 70 80 90 100
CEPGKYLSSK CTPTSDSVCL PCGPDEYLDT WNEEDKCLLH KVCDAGKALV
110 120 130 140 150
AVDPGNHTAP RRCACTAGYH WNSDCECCRR NTECAPGFGA QHPLQLNKDT
160 170 180 190 200
VCTPCLLGFF SDVFSSTDKC KPWTNCTLLG KLEAHQGTTE SDVVCSSSMT
210 220 230 240 250
LRRPPKEAQA YLPSLIVLLL FISVVVVAAI IFGVYYRKGG KALTANLWNW
260 270 280 290 300
VNDACSSLSG NKESSGDRCA GSHSATSSQQ EVCEGILLMT REEKMVPEDG
310 320 330 340 350
AGVCGPVCAA GGPWAEVRDS RTFTLVSEVE TQGDLSRKIP TEDEYTDRPS
360 370 380 390 400
QPSTGSLLLI QQGSKSIPPF QEPLEVGEND SLSQCFTGTE STVDSEGCDF
410 420 430 440 450
TEPPSRTDSM PVSPEKHLTK EIEGDSCLPW VVSSNSTDGY TGSGNTPGED
460 470 480 490 500
HEPFPGSLKC GPLPQCAYSM GFPSEAAASM AEAGVRPQDR ADERGASGSG
510 520 530 540 550
SSPSDQPPAS GNVTGNSNST FISSGQVMNF KGDIIVVYVS QTSQEGPGSA
560 570 580 590 600
EPESEPVGRP VQEETLAHRD SFAGTAPRFP DVCATGAGLQ EQGAPRQKDG
610 620
TSRPVQEQGG AQTSLHTQGS GQCAE
Length:625
Mass (Da):66,621
Last modified:January 1, 1998 - v1
Checksum:iF8C1872E99511D8E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti494 – 4941R → K in AAH19185. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF019046 mRNA. Translation: AAB86810.1.
BC019185 mRNA. Translation: AAH19185.1.
CCDSiCCDS15207.1.
RefSeqiNP_033425.3. NM_009399.3.
UniGeneiMm.6251.

Genome annotation databases

EnsembliENSMUST00000027559; ENSMUSP00000027559; ENSMUSG00000026321.
GeneIDi21934.
KEGGimmu:21934.
UCSCiuc007cgp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF019046 mRNA. Translation: AAB86810.1 .
BC019185 mRNA. Translation: AAH19185.1 .
CCDSi CCDS15207.1.
RefSeqi NP_033425.3. NM_009399.3.
UniGenei Mm.6251.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ME2 X-ray 2.80 R 26-210 [» ]
3ME4 X-ray 2.01 A/B 26-210 [» ]
3QBQ X-ray 2.50 B/D 32-201 [» ]
4GIQ X-ray 2.70 R 31-198 [» ]
ProteinModelPortali O35305.
SMRi O35305. Positions 33-201.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204246. 4 interactions.
DIPi DIP-48710N.
IntActi O35305. 10 interactions.
STRINGi 10090.ENSMUSP00000027559.

PTM databases

PhosphoSitei O35305.

Proteomic databases

PaxDbi O35305.
PRIDEi O35305.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027559 ; ENSMUSP00000027559 ; ENSMUSG00000026321 .
GeneIDi 21934.
KEGGi mmu:21934.
UCSCi uc007cgp.1. mouse.

Organism-specific databases

CTDi 8792.
MGIi MGI:1314891. Tnfrsf11a.

Phylogenomic databases

eggNOGi NOG45473.
GeneTreei ENSGT00760000119204.
HOGENOMi HOG000154659.
HOVERGENi HBG079274.
InParanoidi O35305.
KOi K05147.
OMAi CPHWAAS.
OrthoDBi EOG786H2Q.
PhylomeDBi O35305.
TreeFami TF331157.

Miscellaneous databases

ChiTaRSi TNFRSF11A. mouse.
EvolutionaryTracei O35305.
NextBioi 301532.
PROi O35305.
SOURCEi Search...

Gene expression databases

Bgeei O35305.
Genevestigatori O35305.

Family and domain databases

InterProi IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022323. TNFR_11.
IPR022361. TNFR_11A.
[Graphical view ]
Pfami PF00020. TNFR_c6. 1 hit.
[Graphical view ]
PRINTSi PR01961. TNFACTORR11.
PR01974. TNFACTORR11A.
SMARTi SM00208. TNFR. 4 hits.
[Graphical view ]
PROSITEi PS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTNR11_MOUSE
AccessioniPrimary (citable) accession number: O35305
Secondary accession number(s): Q8VCT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3