TNFL9_MOUSE
ID TNFL9_MOUSE Reviewed; 309 AA.
AC P41274;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 9;
DE AltName: Full=4-1BB ligand;
DE Short=4-1BBL;
GN Name=Tnfsf9; Synonyms=Cd137l, Cd157l, Ly63l;
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 [GENOMIC DNA].
RC TISSUE=T-cell;
RX PubMed=8405064; DOI=10.1002/eji.1830231037;
RA Goodwin R.G., Din W.S., Davis-Smith T., Anderson D.M., Gimpel S.D.,
RA Sato T.A., Maliszewski C.R., Brannan C.I., Copeland N.G., Jenkins N.A.,
RA Farrah T., Armitage R.J., Fanslow W.C., Smith C.A.;
RT "Molecular cloning of a ligand for the inducible T cell gene 4-1BB: a
RT member of an emerging family of cytokines with homology to tumor necrosis
RT factor.";
RL Eur. J. Immunol. 23:2631-2641(1993).
CC -!- FUNCTION: Cytokine that binds to TNFRSF9. Induces the proliferation of
CC activated peripheral blood T-cells. May have a role in activation-
CC induced cell death (AICD). May play a role in cognate interactions
CC between T-cells and B-cells/macrophages.
CC -!- SUBUNIT: Homotrimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR EMBL; L15435; AAA39435.1; -; Genomic_DNA.
DR CCDS; CCDS28926.1; -.
DR PIR; I53384; I53384.
DR RefSeq; NP_033430.1; NM_009404.3.
DR PDB; 6MKB; X-ray; 2.50 A; A/B/C/D=139-309.
DR PDB; 6MKZ; X-ray; 2.65 A; A/C=139-309.
DR PDBsum; 6MKB; -.
DR PDBsum; 6MKZ; -.
DR AlphaFoldDB; P41274; -.
DR SMR; P41274; -.
DR BioGRID; 204262; 1.
DR DIP; DIP-1153N; -.
DR STRING; 10090.ENSMUSP00000040412; -.
DR GlyGen; P41274; 3 sites.
DR iPTMnet; P41274; -.
DR PhosphoSitePlus; P41274; -.
DR SwissPalm; P41274; -.
DR PaxDb; P41274; -.
DR PeptideAtlas; P41274; -.
DR PRIDE; P41274; -.
DR ProteomicsDB; 258792; -.
DR Antibodypedia; 24211; 646 antibodies from 40 providers.
DR DNASU; 21950; -.
DR Ensembl; ENSMUST00000039490; ENSMUSP00000040412; ENSMUSG00000035678.
DR GeneID; 21950; -.
DR KEGG; mmu:21950; -.
DR UCSC; uc008ded.1; mouse.
DR CTD; 8744; -.
DR MGI; MGI:1101058; Tnfsf9.
DR VEuPathDB; HostDB:ENSMUSG00000035678; -.
DR eggNOG; ENOG502SSK0; Eukaryota.
DR GeneTree; ENSGT00390000006244; -.
DR HOGENOM; CLU_903042_0_0_1; -.
DR InParanoid; P41274; -.
DR OMA; VELFPCS; -.
DR OrthoDB; 942863at2759; -.
DR PhylomeDB; P41274; -.
DR TreeFam; TF338523; -.
DR Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
DR BioGRID-ORCS; 21950; 4 hits in 77 CRISPR screens.
DR PRO; PR:P41274; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P41274; protein.
DR Bgee; ENSMUSG00000035678; Expressed in gastrula and 94 other tissues.
DR ExpressionAtlas; P41274; baseline and differential.
DR Genevisible; P41274; MM.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; IPI:MGI.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; ISO:MGI.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:MGI.
DR GO; GO:0045585; P:positive regulation of cytotoxic T cell differentiation; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISO:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0033084; P:regulation of immature T cell proliferation in thymus; IDA:MGI.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR021184; TNF_CS.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR042373; TNFSF9.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR15153; PTHR15153; 1.
DR Pfam; PF00229; TNF; 1.
DR SMART; SM00207; TNF; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS00251; TNF_1; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Glycoprotein; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..309
FT /note="Tumor necrosis factor ligand superfamily member 9"
FT /id="PRO_0000185502"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6MKB"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 196..208
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 218..229
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:6MKB"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6MKZ"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 267..280
FT /evidence="ECO:0007829|PDB:6MKB"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6MKB"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:6MKB"
SQ SEQUENCE 309 AA; 33853 MW; 2A425829AD6B89C0 CRC64;
MDQHTLDVED TADARHPAGT SCPSDAALLR DTGLLADAAL LSDTVRPTNA ALPTDAAYPA
VNVRDREAAW PPALNFCSRH PKLYGLVALV LLLLIAACVP IFTRTEPRPA LTITTSPNLG
TRENNADQVT PVSHIGCPNT TQQGSPVFAK LLAKNQASLC NTTLNWHSQD GAGSSYLSQG
LRYEEDKKEL VVDSPGLYYV FLELKLSPTF TNTGHKVQGW VSLVLQAKPQ VDDFDNLALT
VELFPCSMEN KLVDRSWSQL LLLKAGHRLS VGLRAYLHGA QDAYRDWELS YPNTTSFGLF
LVKPDNPWE
