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Q7TS55

- TNF18_MOUSE

UniProt

Q7TS55 - TNF18_MOUSE

Protein

Tumor necrosis factor ligand superfamily member 18

Gene

Tnfsf18

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Cytokine that binds to TNFRSF18/AITR/GITR. Regulates T-cell responses. Can function as costimulator and lower the threshold for T-cell activation and T-cell proliferation. Important for interactions between activated T-lymphocytes and endothelial cells. Mediates activation of NF-kappa-B.5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. tumor necrosis factor receptor superfamily binding Source: UniProtKB

    GO - Biological processi

    1. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    2. regulation of T cell proliferation Source: UniProtKB
    3. T cell proliferation involved in immune response Source: UniProtKB
    4. tumor necrosis factor-mediated signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Cytokine

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor ligand superfamily member 18
    Alternative name(s):
    GITR ligand
    Short name:
    GITRL
    Glucocorticoid-induced TNF-related ligand
    Gene namesi
    Name:Tnfsf18
    Synonyms:Gitrl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:2673064. Tnfsf18.

    Subcellular locationi

    Cell membrane 2 Publications; Single-pass type II membrane protein 2 Publications

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. extracellular space Source: UniProtKB-KW
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 173173Tumor necrosis factor ligand superfamily member 18PRO_0000415333Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi52 ↔ 723 Publications
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ7TS55.

    Expressioni

    Tissue specificityi

    Detected in immature and mature dendritic cells and in macrophages (at protein level). Detected in spleen, lung, heart, thymus, monocytes, macrophages, B-cells and dendritic cells.3 Publications

    Inductioni

    Up-regulated by exposure to bacterial lipopolysaccharide (LPS).1 Publication

    Gene expression databases

    GenevestigatoriQ7TS55.

    Interactioni

    Subunit structurei

    Homotrimer. Homodimer.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Tnfrsf18O357143EBI-523345,EBI-523358

    Protein-protein interaction databases

    DIPiDIP-29663N.
    IntActiQ7TS55. 1 interaction.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi53 – 575
    Turni58 – 614
    Beta strandi62 – 698
    Beta strandi71 – 755
    Beta strandi81 – 833
    Beta strandi87 – 959
    Helixi100 – 1023
    Beta strandi109 – 1157
    Beta strandi118 – 12710
    Beta strandi130 – 1389
    Beta strandi143 – 1497
    Helixi151 – 1533
    Beta strandi160 – 1656
    Beta strandi171 – 1733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q8OX-ray1.75A/B43-173[»]
    2QDNX-ray2.09A/B46-173[»]
    3B9IX-ray2.49A/B46-173[»]
    3FC0X-ray1.76A/B46-173[»]
    ProteinModelPortaliQ7TS55.
    SMRiQ7TS55. Positions 51-173.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7TS55.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini42 – 173132ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei21 – 4121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tumor necrosis factor family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG39473.
    GeneTreeiENSGT00390000002560.
    HOGENOMiHOG000026597.
    HOVERGENiHBG061857.
    InParanoidiQ80YG2.
    KOiK05479.
    OMAiTYKEPAP.
    OrthoDBiEOG7S7SG4.
    PhylomeDBiQ7TS55.
    TreeFamiTF338614.

    Family and domain databases

    Gene3Di2.60.120.40. 1 hit.
    InterProiIPR006052. TNF_dom.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view]
    PfamiPF00229. TNF. 1 hit.
    [Graphical view]
    SUPFAMiSSF49842. SSF49842. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q7TS55-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEMPLRESS PQRAERCKKS WLLCIVALLL MLLCSLGTLI YTSLKPTAIE    50
    SCMVKFELSS SKWHMTSPKP HCVNTTSDGK LKILQSGTYL IYGQVIPVDK 100
    KYIKDNAPFV VQIYKKNDVL QTLMNDFQIL PIGGVYELHA GDNIYLKFNS 150
    KDHIQKTNTY WGIILMPDLP FIS 173
    Length:173
    Mass (Da):19,732
    Last modified:October 1, 2003 - v1
    Checksum:i0F08494CACF424D2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481A → V in AAP96745. (PubMed:14647196)Curated
    Sequence conflicti157 – 1571T → N in AAP96745. (PubMed:14647196)Curated
    Sequence conflicti157 – 1571T → N in CAE12166. (PubMed:14608036)Curated
    Sequence conflicti157 – 1571T → N in CAE12167. (PubMed:14608036)Curated
    Sequence conflicti157 – 1571T → N in AAO89011. 1 PublicationCurated
    Sequence conflicti157 – 1571T → N in AAI37815. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY359852 mRNA. Translation: AAQ55265.1.
    AY267900 mRNA. Translation: AAP96745.1.
    AJ577579 mRNA. Translation: CAE12166.1.
    AJ577580 mRNA. Translation: CAE12167.1.
    AY320040 mRNA. Translation: AAP70494.1.
    AY234223 mRNA. Translation: AAO89011.1.
    AC163268 Genomic DNA. No translation available.
    BC137814 mRNA. Translation: AAI37815.1.
    BC137815 mRNA. Translation: AAI37816.1.
    CCDSiCCDS15417.1.
    RefSeqiNP_899247.3. NM_183391.3.
    UniGeneiMm.276823.

    Genome annotation databases

    EnsembliENSMUST00000086084; ENSMUSP00000083251; ENSMUSG00000066755.
    GeneIDi240873.
    KEGGimmu:240873.
    UCSCiuc007dfo.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY359852 mRNA. Translation: AAQ55265.1 .
    AY267900 mRNA. Translation: AAP96745.1 .
    AJ577579 mRNA. Translation: CAE12166.1 .
    AJ577580 mRNA. Translation: CAE12167.1 .
    AY320040 mRNA. Translation: AAP70494.1 .
    AY234223 mRNA. Translation: AAO89011.1 .
    AC163268 Genomic DNA. No translation available.
    BC137814 mRNA. Translation: AAI37815.1 .
    BC137815 mRNA. Translation: AAI37816.1 .
    CCDSi CCDS15417.1.
    RefSeqi NP_899247.3. NM_183391.3.
    UniGenei Mm.276823.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q8O X-ray 1.75 A/B 43-173 [» ]
    2QDN X-ray 2.09 A/B 46-173 [» ]
    3B9I X-ray 2.49 A/B 46-173 [» ]
    3FC0 X-ray 1.76 A/B 46-173 [» ]
    ProteinModelPortali Q7TS55.
    SMRi Q7TS55. Positions 51-173.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29663N.
    IntActi Q7TS55. 1 interaction.

    Proteomic databases

    PRIDEi Q7TS55.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000086084 ; ENSMUSP00000083251 ; ENSMUSG00000066755 .
    GeneIDi 240873.
    KEGGi mmu:240873.
    UCSCi uc007dfo.2. mouse.

    Organism-specific databases

    CTDi 8995.
    MGIi MGI:2673064. Tnfsf18.

    Phylogenomic databases

    eggNOGi NOG39473.
    GeneTreei ENSGT00390000002560.
    HOGENOMi HOG000026597.
    HOVERGENi HBG061857.
    InParanoidi Q80YG2.
    KOi K05479.
    OMAi TYKEPAP.
    OrthoDBi EOG7S7SG4.
    PhylomeDBi Q7TS55.
    TreeFami TF338614.

    Miscellaneous databases

    EvolutionaryTracei Q7TS55.
    NextBioi 384771.
    PROi Q7TS55.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q7TS55.

    Family and domain databases

    Gene3Di 2.60.120.40. 1 hit.
    InterProi IPR006052. TNF_dom.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view ]
    Pfami PF00229. TNF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49842. SSF49842. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a ligand for glucocorticoid-induced tumor necrosis factor receptor constitutively expressed in dendritic cells."
      Yu K.Y., Kim H.S., Song S.Y., Min S.S., Jeong J.J., Youn B.S.
      Biochem. Biophys. Res. Commun. 310:433-438(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: 129/J.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Strain: BALB/c.
    3. "Mouse glucocorticoid-induced tumor necrosis factor receptor ligand is costimulatory for T cells."
      Tone M., Tone Y., Adams E., Yates S.F., Frewin M.R., Cobbold S.P., Waldmann H.
      Proc. Natl. Acad. Sci. U.S.A. 100:15059-15064(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
      Strain: CBA/Ca.
    4. "The natural ligand for glucocorticoid-induced TNF receptor-related protein abrogates regulatory T cell suppression."
      Ji H.B., Liao G., Faubion W.A., Abadia-Molina A.C., Cozzo C., Laroux F.S., Caton A., Terhorst C.
      J. Immunol. 172:5823-5827(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT.
      Strain: C57BL/6.
      Tissue: Spleen.
    5. "Cloning and characterization of the mouse ortholog of human GITR ligand (TNFSF18)."
      Bianchini R., Nocentini G., Ronchetti S., Ayroldi E., Riccardi C.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: DBA/2J.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    7. "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: Brain.
    8. "Evolution of GITRL immune function: murine GITRL exhibits unique structural and biochemical properties within the TNF superfamily."
      Chattopadhyay K., Ramagopal U.A., Brenowitz M., Nathenson S.G., Almo S.C.
      Proc. Natl. Acad. Sci. U.S.A. 105:635-640(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 46-173, SUBUNIT, DISULFIDE BOND.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 43-173, FUNCTION, SUBUNIT, DISULFIDE BOND.
    10. "1.8 A structure of murine GITR ligand dimer expressed in Drosophila melanogaster S2 cells."
      Chattopadhyay K., Ramagopal U.A., Nathenson S.G., Almo S.C.
      Acta Crystallogr. D 65:434-439(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 46-173, GLYCOSYLATION, SUBUNIT, DISULFIDE BOND.

    Entry informationi

    Entry nameiTNF18_MOUSE
    AccessioniPrimary (citable) accession number: Q7TS55
    Secondary accession number(s): Q7TNY2, Q80YG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 76 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