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Q7TS55 (TNF18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 75. 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 ligand superfamily member 18
Alternative name(s):
GITR ligand
Short name=GITRL
Glucocorticoid-induced TNF-related ligand
Gene names
Name:Tnfsf18
Synonyms:Gitrl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.3 Ref.4 Ref.9

Subunit structure

Homotrimer. Homodimer. Ref.4 Ref.8 Ref.9 Ref.10

Subcellular location

Cell membrane; Single-pass type II membrane protein Ref.1 Ref.3.

Tissue specificity

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. Ref.1 Ref.2 Ref.3

Induction

Up-regulated by exposure to bacterial lipopolysaccharide (LPS). Ref.3

Post-translational modification

N-glycosylated. Ref.10

Sequence similarities

Belongs to the tumor necrosis factor family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Tnfrsf18O357143EBI-523345,EBI-523358

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 173173Tumor necrosis factor ligand superfamily member 18
PRO_0000415333

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4121Helical; Signal-anchor for type II membrane protein; Potential
Topological domain42 – 173132Extracellular Potential

Amino acid modifications

Glycosylation741N-linked (GlcNAc...) Potential
Disulfide bond52 ↔ 72 Ref.8 Ref.9 Ref.10

Experimental info

Sequence conflict481A → V in AAP96745. Ref.2
Sequence conflict1571T → N in AAP96745. Ref.2
Sequence conflict1571T → N in CAE12166. Ref.3
Sequence conflict1571T → N in CAE12167. Ref.3
Sequence conflict1571T → N in AAO89011. Ref.5
Sequence conflict1571T → N in AAI37815. Ref.7

Secondary structure

.......................... 173
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7TS55 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 0F08494CACF424D2

FASTA17319,732
        10         20         30         40         50         60 
MEEMPLRESS PQRAERCKKS WLLCIVALLL MLLCSLGTLI YTSLKPTAIE SCMVKFELSS 

        70         80         90        100        110        120 
SKWHMTSPKP HCVNTTSDGK LKILQSGTYL IYGQVIPVDK KYIKDNAPFV VQIYKKNDVL 

       130        140        150        160        170 
QTLMNDFQIL PIGGVYELHA GDNIYLKFNS KDHIQKTNTY WGIILMPDLP FIS 

« Hide

References

« Hide 'large scale' references
[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]"Cloning and characterization of GITR ligand."
Kim J.D., Choi B.K., Bae J.S., Lee U.H., Han I.S., Lee H.W., Youn B.S., Vinay D.S., Kwon B.S.
Genes Immun. 4:564-569(2003) [PubMed] [Europe PMC] [Abstract]
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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Structural basis for ligand-mediated mouse GITR activation."
Zhou Z., Tone Y., Song X., Furuuchi K., Lear J.D., Waldmann H., Tone M., Greene M.I., Murali R.
Proc. Natl. Acad. Sci. U.S.A. 105:641-645(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS15417.1.
RefSeqNP_899247.3. NM_183391.3.
UniGeneMm.276823.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q8OX-ray1.75A/B43-173[»]
2QDNX-ray2.09A/B46-173[»]
3B9IX-ray2.49A/B46-173[»]
3FC0X-ray1.76A/B46-173[»]
ProteinModelPortalQ7TS55.
SMRQ7TS55. Positions 51-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29663N.
IntActQ7TS55. 1 interaction.

Proteomic databases

PRIDEQ7TS55.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000086084; ENSMUSP00000083251; ENSMUSG00000066755.
GeneID240873.
KEGGmmu:240873.
UCSCuc007dfo.2. mouse.

Organism-specific databases

CTD8995.
MGIMGI:2673064. Tnfsf18.

Phylogenomic databases

eggNOGNOG39473.
GeneTreeENSGT00390000002560.
HOGENOMHOG000026597.
HOVERGENHBG061857.
InParanoidQ80YG2.
KOK05479.
OMATYKEPAP.
OrthoDBEOG7S7SG4.
PhylomeDBQ7TS55.
TreeFamTF338614.

Gene expression databases

GenevestigatorQ7TS55.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR006052. TNF_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamPF00229. TNF. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ7TS55.
NextBio384771.
PROQ7TS55.
SOURCESearch...

Entry information

Entry nameTNF18_MOUSE
AccessionPrimary (citable) accession number: Q7TS55
Secondary accession number(s): Q7TNY2, Q80YG2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 75 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