Tumor necrosis factor ligand superfamily member 18

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Q7TS55 (TNF18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Cell membrane Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Cytokine
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell proliferation involved in immune response Inferred from direct assay Ref.3. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from mutant phenotype Ref.1. Source: UniProtKB regulation of T cell proliferation Inferred from direct assay Ref.3. Source: UniProtKB tumor necrosis factor-mediated signaling pathway Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular_component	cell surface Inferred from direct assay Ref.1. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	tumor necrosis factor receptor superfamily binding Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Tnfrsf18	O35714	3	EBI-523345,EBI-523358

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 173

173

Tumor necrosis factor ligand superfamily member 18

PRO_0000415333

Regions

Topological domain

1 – 20

Cytoplasmic Potential

Transmembrane

21 – 41

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

42 – 173

132

Extracellular Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Disulfide bond

52 ↔ 72

Ref.8 Ref.9 Ref.10

Experimental info

Sequence conflict

A → V in AAP96745. Ref.2

Sequence conflict

157

T → N in AAP96745. Ref.2

Sequence conflict

157

T → N in CAE12166. Ref.3

Sequence conflict

157

T → N in CAE12167. Ref.3

Sequence conflict

157

T → N in AAO89011. Ref.5

Sequence conflict

157

T → N in AAI37815. Ref.7

Secondary structure

173

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q7TS55 [UniParc].

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

FASTA

173

19,732

        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' referencesShow '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. 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.

IPI

IPI00330855.

RefSeq

NP_899247.3. NM_183391.3.

UniGene

Mm.276823.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q7TS55.

SMR

Q7TS55. Positions 51-173.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29663N.

IntAct

Q7TS55. 1 interaction.

Proteomic databases

PRIDE

Q7TS55.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000086084; ENSMUSP00000083251; ENSMUSG00000066755.

GeneID

240873.

KEGG

mmu:240873.

UCSC

uc007dfo.2. mouse.

Organism-specific databases

CTD

8995.

MGI

MGI:2673064. Tnfsf18.

Phylogenomic databases

eggNOG

NOG39473.

GeneTree

ENSGT00390000002560.

HOGENOM

HOG000026597.

HOVERGEN

HBG061857.

InParanoid

Q80YG2.

K05479.

OMA

TYKEPAP.

OrthoDB

EOG40GCRS.

Gene expression databases

Genevestigator

Q7TS55.

Family and domain databases

Gene3D

2.60.120.40. 1 hit.

InterPro

IPR006052. TNF.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]

Pfam

PF00229. TNF. 1 hit.
[Graphical view]

SUPFAM

SSF49842. TNF_like. 1 hit.

PROSITE

PS00251. TNF_1. False negative.
PS50049. TNF_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q7TS55.

NextBio

384771.

SOURCE

Search...

Entry information

Entry name

TNF18_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents