ID   TNR9_MOUSE              Reviewed;         256 AA.
AC   P20334;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   02-SEP-2026, entry version 193.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 9;
DE   AltName: Full=4-1BB ligand receptor;
DE   AltName: Full=T-cell antigen 4-1BB {ECO:0000303|PubMed:7678621};
DE   AltName: CD_antigen=CD137;
DE   Flags: Precursor;
GN   Name=Tnfrsf9; Synonyms=Cd137, Ila, Ly63;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2784565; DOI=10.1073/pnas.86.6.1963;
RA   Kwon B.S., Weissman S.M.;
RT   "cDNA sequences of two inducible T-cell genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1963-1967(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=8133039; DOI=10.4049/jimmunol.152.5.2256;
RA   Kwon B.S., Kozak C.A., Kim K.K., Pickard R.T.;
RT   "Genomic organization and chromosomal localization of the T-cell antigen 4-
RT   1BB.";
RL   J. Immunol. 152:2256-2262(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 24-29, HOMODIMERIZATION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=7678621; DOI=10.4049/jimmunol.150.3.771;
RA   Pollok K.E., Kim Y.-J., Zhou Z., Hurtado J., Kin K.K., Pickard R.T.,
RA   Kwon B.S.;
RT   "Inducible T cell antigen 4-1BB. Analysis of expression and function.";
RL   J. Immunol. 150:771-781(1993).
CC   -!- FUNCTION: Receptor for TNFSF9/4-1BBL. Conveys a signal that enhances
CC       CD8(+) T-cell survival, cytotoxicity, and mitochondrial activity,
CC       thereby promoting immunity against viruses and tumors (By similarity).
CC       {ECO:0000250|UniProtKB:Q07011}.
CC   -!- SUBUNIT: Predominantly homodimeric, but may also exist as a monomer
CC       (PubMed:7678621). Associates with p56-LCK. Interacts with TRAF1, TRAF2
CC       and TRAF3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:7678621}.
CC   -!- INTERACTION:
CC       P20334; Q12933: TRAF2; Xeno; NbExp=2; IntAct=EBI-520693, EBI-355744;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein {ECO:0000305|PubMed:7678621}.
CC   -!- TISSUE SPECIFICITY: Expressed in activated thymocytes, splenic T cells,
CC       CD4(+), and CD8(+) T-cells. {ECO:0000269|PubMed:7678621}.
CC   -!- INDUCTION: Up-regulated after cell treatment by PMA and ionomycin,
CC       suggesting that optimal expression requires both protein kinase C
CC       activation and increase in intracellular calcium.
CC       {ECO:0000269|PubMed:7678621}.
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DR   EMBL; J04492; AAA40167.1; -; mRNA.
DR   EMBL; U02567; AAA93113.1; -; Genomic_DNA.
DR   CCDS; CCDS18976.1; -.
DR   PIR; B32393; B32393.
DR   RefSeq; NP_001070977.1; NM_001077509.1.
DR   RefSeq; NP_035742.1; NM_011612.2.
DR   RefSeq; XP_011248530.1; XM_011250228.3.
DR   PDB; 1D0J; X-ray; 2.50 A; G/H/I/J/K=230-236.
DR   PDB; 5WI8; X-ray; 2.95 A; A/B/C/D=24-160.
DR   PDB; 5WIW; X-ray; 2.30 A; A/B=24-160.
DR   PDB; 5WJF; X-ray; 2.60 A; A/B=24-160.
DR   PDB; 6MKZ; X-ray; 2.65 A; B/D=24-160.
DR   AlphaFoldDB; P20334; -.
DR   SMR; P20334; -.
DR   BioGRID; 204254; 1.
DR   DIP; DIP-1154N; -.
DR   FunCoup; P20334; 657.
DR   IntAct; P20334; 4.
DR   STRING; 10090.ENSMUSP00000111961; -.
DR   GlyCosmos; P20334; 2 sites, No reported glycans.
DR   GlyGen; P20334; 2 sites.
DR   PhosphoSitePlus; P20334; -.
DR   PaxDb; 10090-ENSMUSP00000111961; -.
DR   PeptideAtlas; P20334; -.
DR   ProteomicsDB; 259147; -.
DR   ABCD; P20334; 4 sequenced antibodies.
DR   Antibodypedia; 3718; 1536 antibodies from 50 providers.
DR   DNASU; 21942; -.
DR   Ensembl; ENSMUST00000030808.10; ENSMUSP00000030808.4; ENSMUSG00000028965.14.
DR   Ensembl; ENSMUST00000105671.8; ENSMUSP00000101296.2; ENSMUSG00000028965.14.
DR   Ensembl; ENSMUST00000116257.8; ENSMUSP00000111961.2; ENSMUSG00000028965.14.
DR   GeneID; 21942; -.
DR   KEGG; mmu:21942; -.
DR   UCSC; uc008vya.1; mouse.
DR   AGR; MGI:1101059; -.
DR   CTD; 3604; -.
DR   MGI; MGI:1101059; Tnfrsf9.
DR   VEuPathDB; HostDB:ENSMUSG00000028965; -.
DR   eggNOG; ENOG502S017; Eukaryota.
DR   GeneTree; ENSGT00730000111279; -.
DR   InParanoid; P20334; -.
DR   OMA; YLFKQPF; -.
DR   OrthoDB; 9423210at2759; -.
DR   PhylomeDB; P20334; -.
DR   Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
DR   BioGRID-ORCS; 21942; 1 hit in 84 CRISPR screens.
DR   EvolutionaryTrace; P20334; -.
DR   PRO; PR:P20334; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P20334; protein.
DR   Bgee; ENSMUSG00000028965; Expressed in placenta labyrinth and 48 other cell types or tissues.
DR   ExpressionAtlas; P20334; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0038023; F:signaling receptor activity; IPI:MGI.
DR   GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IDA:MGI.
DR   CDD; cd13410; TNFRSF9; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 2.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR020413; TNFR_9.
DR   InterPro; IPR034020; TNFRSF9_N.
DR   PANTHER; PTHR47139; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 9; 1.
DR   PANTHER; PTHR47139:SF1; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 9; 1.
DR   Pfam; PF00020; TNFR_c6; 1.
DR   PRINTS; PR01924; TNFACTORR9.
DR   SMART; SM00208; TNFR; 2.
DR   SUPFAM; SSF57586; TNF receptor-like; 1.
DR   PROSITE; PS00652; TNFR_NGFR_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:7678621"
FT   CHAIN           24..256
FT                   /note="Tumor necrosis factor receptor superfamily member 9"
FT                   /id="PRO_0000034578"
FT   TOPO_DOM        24..187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        209..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          24..45
FT                   /note="TNFR-Cys 1"
FT   REPEAT          46..85
FT                   /note="TNFR-Cys 2"
FT   REPEAT          86..117
FT                   /note="TNFR-Cys 3"
FT   REPEAT          118..159
FT                   /note="TNFR-Cys 4"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..37
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..44
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..61
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        98..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        101..116
FT                   /evidence="ECO:0000250"
FT   DISULFID        119..133
FT                   /evidence="ECO:0000250"
FT   DISULFID        139..158
FT                   /evidence="ECO:0000250"
FT   HELIX           28..30
FT                   /evidence="ECO:0007829|PDB:5WJF"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:5WJF"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:5WJF"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:5WJF"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:5WJF"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          91..95
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          109..112
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          127..130
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   TURN            139..143
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:5WIW"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:5WIW"
SQ   SEQUENCE   256 AA;  27598 MW;  93A10D03C60813C4 CRC64;
     MGNNCYNVVV IVLLLVGCEK VGAVQNSCDN CQPGTFCRKY NPVCKSCPPS TFSSIGGQPN
     CNICRVCAGY FRFKKFCSST HNAECECIEG FHCLGPQCTR CEKDCRPGQE LTKQGCKTCS
     LGTFNDQNGT GVCRPWTNCS LDGRSVLKTG TTEKDVVCGP PVVSFSPSTT ISVTPEGGPG
     GHSLQVLTLF LALTSALLLA LIFITLLFSV LKWIRKKFPH IFKQPFKKTT GAAQEEDACS
     CRCPQEEEGG GGGYEL
//