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O35305

- TNR11_MOUSE

UniProt

O35305 - TNR11_MOUSE

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
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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. protein binding Source: IntAct
    3. 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

    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

    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.
    GeneTreeiENSGT00740000115372.
    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

    MAPRARRRRQ LPAPLLALCV LLVPLQVTLQ VTPPCTQERH YEHLGRCCSR    50
    CEPGKYLSSK CTPTSDSVCL PCGPDEYLDT WNEEDKCLLH KVCDAGKALV 100
    AVDPGNHTAP RRCACTAGYH WNSDCECCRR NTECAPGFGA QHPLQLNKDT 150
    VCTPCLLGFF SDVFSSTDKC KPWTNCTLLG KLEAHQGTTE SDVVCSSSMT 200
    LRRPPKEAQA YLPSLIVLLL FISVVVVAAI IFGVYYRKGG KALTANLWNW 250
    VNDACSSLSG NKESSGDRCA GSHSATSSQQ EVCEGILLMT REEKMVPEDG 300
    AGVCGPVCAA GGPWAEVRDS RTFTLVSEVE TQGDLSRKIP TEDEYTDRPS 350
    QPSTGSLLLI QQGSKSIPPF QEPLEVGEND SLSQCFTGTE STVDSEGCDF 400
    TEPPSRTDSM PVSPEKHLTK EIEGDSCLPW VVSSNSTDGY TGSGNTPGED 450
    HEPFPGSLKC GPLPQCAYSM GFPSEAAASM AEAGVRPQDR ADERGASGSG 500
    SSPSDQPPAS GNVTGNSNST FISSGQVMNF KGDIIVVYVS QTSQEGPGSA 550
    EPESEPVGRP VQEETLAHRD SFAGTAPRFP DVCATGAGLQ EQGAPRQKDG 600
    TSRPVQEQGG AQTSLHTQGS GQCAE 625
    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 ENSGT00740000115372.
    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

    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 1, 2014
    This is version 115 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