TNR9_MOUSE
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 03-AUG-2022, entry version 175.
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;
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;
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 CHARACTERIZATION, AND PROTEIN SEQUENCE OF 24-29.
RX PubMed=7678621;
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. Possibly active during T cell
CC activation.
CC -!- SUBUNIT: Principally a homodimer, but also found as a monomer.
CC Associates with p56-LCK. Interacts with TRAF1, TRAF2 and TRAF3 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P20334; Q12933: TRAF2; Xeno; NbExp=2; IntAct=EBI-520693, EBI-355744;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed on the surface of activated T-cells.
CC -!- INDUCTION: Optimal by PMA and ionomycin.
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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_011250228.2.
DR PDB; 1D0J; X-ray; 2.50 A; G/H/I/J/K=231-236.
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 PDBsum; 1D0J; -.
DR PDBsum; 5WI8; -.
DR PDBsum; 5WIW; -.
DR PDBsum; 5WJF; -.
DR PDBsum; 6MKZ; -.
DR AlphaFoldDB; P20334; -.
DR SMR; P20334; -.
DR BioGRID; 204254; 1.
DR DIP; DIP-1154N; -.
DR IntAct; P20334; 4.
DR STRING; 10090.ENSMUSP00000030808; -.
DR GlyGen; P20334; 2 sites.
DR PhosphoSitePlus; P20334; -.
DR EPD; P20334; -.
DR PaxDb; P20334; -.
DR PeptideAtlas; P20334; -.
DR PRIDE; P20334; -.
DR ProteomicsDB; 259147; -.
DR ABCD; P20334; 4 sequenced antibodies.
DR Antibodypedia; 3718; 1365 antibodies from 47 providers.
DR DNASU; 21942; -.
DR Ensembl; ENSMUST00000030808; ENSMUSP00000030808; ENSMUSG00000028965.
DR Ensembl; ENSMUST00000105671; ENSMUSP00000101296; ENSMUSG00000028965.
DR Ensembl; ENSMUST00000116257; ENSMUSP00000111961; ENSMUSG00000028965.
DR GeneID; 21942; -.
DR KEGG; mmu:21942; -.
DR UCSC; uc008vya.1; mouse.
DR CTD; 3604; -.
DR MGI; MGI:1101059; Tnfrsf9.
DR VEuPathDB; HostDB:ENSMUSG00000028965; -.
DR eggNOG; ENOG502S017; Eukaryota.
DR GeneTree; ENSGT00730000111279; -.
DR InParanoid; P20334; -.
DR OMA; CISGFHC; -.
DR OrthoDB; 1102119at2759; -.
DR PhylomeDB; P20334; -.
DR TreeFam; TF336151; -.
DR Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
DR BioGRID-ORCS; 21942; 1 hit in 79 CRISPR screens.
DR ChiTaRS; Tnfrsf9; mouse.
DR EvolutionaryTrace; P20334; -.
DR PRO; PR:P20334; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P20334; protein.
DR Bgee; ENSMUSG00000028965; Expressed in placenta labyrinth and 47 other tissues.
DR ExpressionAtlas; P20334; baseline and differential.
DR Genevisible; P20334; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0033084; P:regulation of immature T cell proliferation in thymus; IDA:MGI.
DR CDD; cd13410; TNFRSF9; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020413; TNFR_9.
DR InterPro; IPR034020; TNFRSF9_N.
DR PANTHER; PTHR47139:SF1; PTHR47139:SF1; 1.
DR Pfam; PF00020; TNFR_c6; 1.
DR PRINTS; PR01924; TNFACTORR9.
DR SMART; SM00208; TNFR; 2.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW 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 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 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