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O35714 (TNR18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor receptor superfamily member 18
Alternative name(s):
Glucocorticoid-induced TNFR-related protein
CD_antigen=CD357
Gene names
Name:Tnfrsf18
Synonyms:Gitr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway By similarity.

Subunit structure

Binds to TRAF1, TRAF2, and TRAF3, but not TRAF5 and TRAF6 By similarity. Binds through its C-terminus to SIVA1/SIVA. Ref.5

Subcellular location

Isoform A: Cell membrane; Single-pass type I membrane protein.

Isoform B: Cell membrane; Single-pass type I membrane protein.

Isoform C: Cell membrane; Single-pass type I membrane protein.

Isoform D: Secreted.

Tissue specificity

Preferentially expressed in activated T lymphocytes.

Induction

Up-regulated in peripherical mononuclear cells after antigen stimulation/lymphocyte activation.

Sequence similarities

Contains 3 TNFR-Cys repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Tnfsf18Q7TS553EBI-523358,EBI-523345

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: O35714-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: O35714-2)

The sequence of this isoform differs from the canonical sequence as follows:
     189-228: ETQPFAEVQL...EKCHLGGRWP → VLLQRPSHSR...RLGPMAAFLI
Isoform C (identifier: O35714-3)

The sequence of this isoform differs from the canonical sequence as follows:
     189-228: ETQPFAEVQLSAEDACSFQFPEEERGEQTEEKCHLGGRWP → GQLCPREGENVSQAPHLPQFYYRDPAIRGGAVVS
Isoform D (identifier: O35714-4)

The sequence of this isoform differs from the canonical sequence as follows:
     121-228: NCSQFGFLTM...EKCHLGGRWP → KDPAIRGGAVVS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 228209Tumor necrosis factor receptor superfamily member 18
PRO_0000034596

Regions

Topological domain20 – 153134Extracellular Potential
Transmembrane154 – 17421Helical; Potential
Topological domain175 – 22854Cytoplasmic Potential
Repeat28 – 6134TNFR-Cys 1
Repeat62 – 10140TNFR-Cys 2
Repeat102 – 14241TNFR-Cys 3

Amino acid modifications

Glycosylation361N-linked (GlcNAc...) Potential
Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 44 By similarity
Disulfide bond62 ↔ 74 By similarity
Disulfide bond69 ↔ 82 By similarity
Disulfide bond103 ↔ 122 By similarity
Disulfide bond116 ↔ 141 By similarity

Natural variations

Alternative sequence121 – 228108NCSQF…GGRWP → KDPAIRGGAVVS in isoform D.
VSP_006509
Alternative sequence189 – 22840ETQPF…GGRWP → VLLQRPSHSRRCSCQLRMLA ASSSLRRNAGSRQKKSVIWG VGGHEAWSSSVPQARRYKTC PAIPLVRAGAMLCTLPWAWP CSPQQWRKWVYESGELRLGP MAAFLI in isoform B.
VSP_006510
Alternative sequence189 – 22840ETQPF…GGRWP → GQLCPREGENVSQAPHLPQF YYRDPAIRGGAVVS in isoform C.
VSP_006511

Experimental info

Mutagenesis1991S → A: Does not bind to SIVA1. Ref.5
Mutagenesis2011E → R: No effect on binding to SIVA1; when associated with G-204. Ref.5
Mutagenesis2041C → G: No effect on binding to SIVA1; when associated with R-201. Ref.5
Mutagenesis2091P → A: Does not bind to SIVA1. Ref.5
Mutagenesis210 – 2123EEE → RVV: Does not bind to SIVA1. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 50D8C275D9C56259

FASTA22825,334
        10         20         30         40         50         60 
MGAWAMLYGV SMLCVLDLGQ PSVVEEPGCG PGKVQNGSGN NTRCCSLYAP GKEDCPKERC 

        70         80         90        100        110        120 
ICVTPEYHCG DPQCKICKHY PCQPGQRVES QGDIVFGFRC VACAMGTFSA GRDGHCRLWT 

       130        140        150        160        170        180 
NCSQFGFLTM FPGNKTHNAV CIPEPLPTEQ YGHLTVIFLV MAACIFFLTT VQLGLHIWQL 

       190        200        210        220 
RRQHMCPRET QPFAEVQLSA EDACSFQFPE EERGEQTEEK CHLGGRWP 

« Hide

Isoform B [UniParc].

Checksum: FE0D4AE6A007BA9A
Show »

FASTA29432,658
Isoform C [UniParc].

Checksum: 594932BA425A79CA
Show »

FASTA22224,450
Isoform D [UniParc].

Checksum: F586A5404B1DFEDE
Show »

FASTA13214,106

References

« Hide 'large scale' references
[1]"A new member of the tumor necrosis factor/nerve growth factor receptor family inhibits T cell receptor-induced apoptosis."
Nocentini G., Giunchi L., Ronchetti S., Krausz L.T., Bartoli A., Moraca R., Migliorati G., Riccardi C.
Proc. Natl. Acad. Sci. U.S.A. 94:6216-6221(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Strain: C3H.
[2]"Gene structure and chromosomal assignment of mouse GITR, a member of the tumor necrosis factor/nerve growth factor receptor family."
Nocentini G., Bartoli A., Ronchetti S., Giunchi L., Cupelli A., Delfino D., Migliorati G., Riccardi C.
DNA Cell Biol. 19:205-217(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM A).
Strain: BALB/c.
[3]"Identification of three novel mRNA splice variants of GITR."
Nocentini G., Ronchetti S., Bartoli A., Spinicelli S., Delfino D., Brunetti L., Migliorati G., Riccardi C.
Cell Death Differ. 7:408-410(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C AND D).
Tissue: Thymus.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: C57BL/6J.
Tissue: Thymus.
[5]"GITR interacts with the pro-apoptotic protein Siva and induces apoptosis."
Spinicelli S., Nocentini G., Ronchetti S., Krausz L.T., Bianchini R., Riccardi C.
Cell Death Differ. 9:1382-1384(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIVA1, MUTAGENESIS OF SER-199; GLU-201; CYS-204; PRO-209 AND 210-GLU--GLU-212.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82534 mRNA. Translation: AAB81243.1.
AF109216 Genomic DNA. Translation: AAF14231.1.
AF229432 mRNA. Translation: AAF61566.1.
AF229433 mRNA. Translation: AAF61567.1.
AF229434 mRNA. Translation: AAF61568.1.
AK020762 mRNA. Translation: BAC25639.1.
CCDSCCDS19056.1. [O35714-1]
CCDS19057.1. [O35714-4]
RefSeqNP_033426.1. NM_009400.2. [O35714-1]
NP_068820.1. NM_021985.2. [O35714-4]
UniGeneMm.3180.

3D structure databases

ProteinModelPortalO35714.
SMRO35714. Positions 27-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29666N.
IntActO35714. 1 interaction.

Proteomic databases

PRIDEO35714.

Protocols and materials databases

DNASU21936.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040274; ENSMUSP00000040035; ENSMUSG00000041954. [O35714-4]
ENSMUST00000103173; ENSMUSP00000099462; ENSMUSG00000041954. [O35714-1]
GeneID21936.
KEGGmmu:21936.
UCSCuc008wfx.1. mouse. [O35714-1]

Organism-specific databases

CTD8784.
MGIMGI:894675. Tnfrsf18.

Phylogenomic databases

eggNOGNOG46178.
GeneTreeENSGT00730000111424.
HOGENOMHOG000049155.
HOVERGENHBG054195.
KOK05154.
OrthoDBEOG7XH6QM.
TreeFamTF336151.

Gene expression databases

ArrayExpressO35714.
BgeeO35714.
GenevestigatorO35714.

Family and domain databases

InterProIPR000742. EG-like_dom.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022318. TNFR_18.
[Graphical view]
PRINTSPR01968. TNFACTORR18.
SMARTSM00181. EGF. 1 hit.
SM00208. TNFR. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNFRSF18. mouse.
NextBio301540.
PROO35714.
SOURCESearch...

Entry information

Entry nameTNR18_MOUSE
AccessionPrimary (citable) accession number: O35714
Secondary accession number(s): Q9JKR1, Q9JKR2, Q9JKR3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 125 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

MGD cross-references

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