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O35714

- TNR18_MOUSE

UniProt

O35714 - TNR18_MOUSE

Protein

Tumor necrosis factor receptor superfamily member 18

Gene

Tnfrsf18

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor receptor superfamily member 18
    Alternative name(s):
    Glucocorticoid-induced TNFR-related protein
    CD_antigen: CD357
    Gene namesi
    Name:Tnfrsf18
    Synonyms:Gitr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:894675. Tnfrsf18.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: MGI
    2. extracellular region Source: UniProtKB-SubCell
    3. integral component of plasma membrane Source: InterPro

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi199 – 1991S → A: Does not bind to SIVA1. 1 Publication
    Mutagenesisi201 – 2011E → R: No effect on binding to SIVA1; when associated with G-204. 1 Publication
    Mutagenesisi204 – 2041C → G: No effect on binding to SIVA1; when associated with R-201. 1 Publication
    Mutagenesisi209 – 2091P → A: Does not bind to SIVA1. 1 Publication
    Mutagenesisi210 – 2123EEE → RVV: Does not bind to SIVA1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 228209Tumor necrosis factor receptor superfamily member 18PRO_0000034596Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 44By similarity
    Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi62 ↔ 74By similarity
    Disulfide bondi69 ↔ 82By similarity
    Disulfide bondi103 ↔ 122By similarity
    Disulfide bondi116 ↔ 141By similarity
    Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiO35714.

    Expressioni

    Tissue specificityi

    Preferentially expressed in activated T lymphocytes.

    Inductioni

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

    Gene expression databases

    ArrayExpressiO35714.
    BgeeiO35714.
    GenevestigatoriO35714.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Tnfsf18Q7TS553EBI-523358,EBI-523345

    Protein-protein interaction databases

    DIPiDIP-29666N.
    IntActiO35714. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliO35714.
    SMRiO35714. Positions 27-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 153134ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini175 – 22854CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei154 – 17421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati28 – 6134TNFR-Cys 1Add
    BLAST
    Repeati62 – 10140TNFR-Cys 2Add
    BLAST
    Repeati102 – 14241TNFR-Cys 3Add
    BLAST

    Sequence similaritiesi

    Contains 3 TNFR-Cys repeats.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG46178.
    GeneTreeiENSGT00730000111424.
    HOGENOMiHOG000049155.
    HOVERGENiHBG054195.
    KOiK05154.
    OrthoDBiEOG7XH6QM.
    TreeFamiTF336151.

    Family and domain databases

    InterProiIPR000742. EG-like_dom.
    IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR022318. TNFR_18.
    [Graphical view]
    PRINTSiPR01968. TNFACTORR18.
    SMARTiSM00181. EGF. 1 hit.
    SM00208. TNFR. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: O35714-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGAWAMLYGV SMLCVLDLGQ PSVVEEPGCG PGKVQNGSGN NTRCCSLYAP    50
    GKEDCPKERC ICVTPEYHCG DPQCKICKHY PCQPGQRVES QGDIVFGFRC 100
    VACAMGTFSA GRDGHCRLWT NCSQFGFLTM FPGNKTHNAV CIPEPLPTEQ 150
    YGHLTVIFLV MAACIFFLTT VQLGLHIWQL RRQHMCPRET QPFAEVQLSA 200
    EDACSFQFPE EERGEQTEEK CHLGGRWP 228
    Length:228
    Mass (Da):25,334
    Last modified:January 1, 1998 - v1
    Checksum:i50D8C275D9C56259
    GO
    Isoform B (identifier: O35714-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         189-228: ETQPFAEVQL...EKCHLGGRWP → VLLQRPSHSR...RLGPMAAFLI

    Show »
    Length:294
    Mass (Da):32,658
    Checksum:iFE0D4AE6A007BA9A
    GO
    Isoform C (identifier: O35714-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         189-228: ETQPFAEVQLSAEDACSFQFPEEERGEQTEEKCHLGGRWP → GQLCPREGENVSQAPHLPQFYYRDPAIRGGAVVS

    Show »
    Length:222
    Mass (Da):24,450
    Checksum:i594932BA425A79CA
    GO
    Isoform D (identifier: O35714-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:132
    Mass (Da):14,106
    Checksum:iF586A5404B1DFEDE
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei121 – 228108NCSQF…GGRWP → KDPAIRGGAVVS in isoform D. 1 PublicationVSP_006509Add
    BLAST
    Alternative sequencei189 – 22840ETQPF…GGRWP → VLLQRPSHSRRCSCQLRMLA ASSSLRRNAGSRQKKSVIWG VGGHEAWSSSVPQARRYKTC PAIPLVRAGAMLCTLPWAWP CSPQQWRKWVYESGELRLGP MAAFLI in isoform B. 1 PublicationVSP_006510Add
    BLAST
    Alternative sequencei189 – 22840ETQPF…GGRWP → GQLCPREGENVSQAPHLPQF YYRDPAIRGGAVVS in isoform C. 1 PublicationVSP_006511Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS19056.1. [O35714-1]
    CCDS19057.1. [O35714-4]
    RefSeqiNP_033426.1. NM_009400.2. [O35714-1]
    NP_068820.1. NM_021985.2. [O35714-4]
    UniGeneiMm.3180.

    Genome annotation databases

    EnsembliENSMUST00000040274; ENSMUSP00000040035; ENSMUSG00000041954. [O35714-4]
    ENSMUST00000103173; ENSMUSP00000099462; ENSMUSG00000041954. [O35714-1]
    GeneIDi21936.
    KEGGimmu:21936.
    UCSCiuc008wfx.1. mouse. [O35714-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS19056.1. [O35714-1 ]
    CCDS19057.1. [O35714-4 ]
    RefSeqi NP_033426.1. NM_009400.2. [O35714-1 ]
    NP_068820.1. NM_021985.2. [O35714-4 ]
    UniGenei Mm.3180.

    3D structure databases

    ProteinModelPortali O35714.
    SMRi O35714. Positions 27-146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29666N.
    IntActi O35714. 1 interaction.

    Proteomic databases

    PRIDEi O35714.

    Protocols and materials databases

    DNASUi 21936.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040274 ; ENSMUSP00000040035 ; ENSMUSG00000041954 . [O35714-4 ]
    ENSMUST00000103173 ; ENSMUSP00000099462 ; ENSMUSG00000041954 . [O35714-1 ]
    GeneIDi 21936.
    KEGGi mmu:21936.
    UCSCi uc008wfx.1. mouse. [O35714-1 ]

    Organism-specific databases

    CTDi 8784.
    MGIi MGI:894675. Tnfrsf18.

    Phylogenomic databases

    eggNOGi NOG46178.
    GeneTreei ENSGT00730000111424.
    HOGENOMi HOG000049155.
    HOVERGENi HBG054195.
    KOi K05154.
    OrthoDBi EOG7XH6QM.
    TreeFami TF336151.

    Miscellaneous databases

    ChiTaRSi TNFRSF18. mouse.
    NextBioi 301540.
    PROi O35714.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O35714.
    Bgeei O35714.
    Genevestigatori O35714.

    Family and domain databases

    InterProi IPR000742. EG-like_dom.
    IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR022318. TNFR_18.
    [Graphical view ]
    PRINTSi PR01968. TNFACTORR18.
    SMARTi SM00181. EGF. 1 hit.
    SM00208. TNFR. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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.

    Entry informationi

    Entry nameiTNR18_MOUSE
    AccessioniPrimary (citable) accession number: O35714
    Secondary accession number(s): Q9JKR1, Q9JKR2, Q9JKR3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 126 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

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3