TNFL9_HUMAN
ID TNFL9_HUMAN Reviewed; 254 AA.
AC P41273; Q2M3S2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 9;
DE AltName: Full=4-1BB ligand;
DE Short=4-1BBL;
GN Name=TNFSF9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8088337; DOI=10.1002/eji.1830240943;
RA Alderson M.R., Smith C.A., Tough T.W., Davis-Smith T., Armitage R.J.,
RA Falk B., Roux E., Baker E., Sutherland G.R., Din W.S., Goodwin R.G.;
RT "Molecular and biological characterization of human 4-1BB and its ligand.";
RL Eur. J. Immunol. 24:2219-2227(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 80-246, FUNCTION, AND SUBUNIT.
RX PubMed=20032458; DOI=10.1074/jbc.m109.084442;
RA Won E.Y., Cha K., Byun J.S., Kim D.U., Shin S., Ahn B., Kim Y.H.,
RA Rice A.J., Walz T., Kwon B.S., Cho H.S.;
RT "The structure of the trimer of human 4-1BB ligand is unique among members
RT of the tumor necrosis factor superfamily.";
RL J. Biol. Chem. 285:9202-9210(2010).
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. {ECO:0000269|PubMed:20032458}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:20032458}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in brain, placenta, lung, skeletal muscle
CC and kidney.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR EMBL; U03398; AAA53134.1; -; mRNA.
DR EMBL; BC104805; AAI04806.1; -; mRNA.
DR EMBL; BC104807; AAI04808.1; -; mRNA.
DR CCDS; CCDS12169.1; -.
DR PIR; I38427; I38427.
DR RefSeq; NP_003802.1; NM_003811.3.
DR PDB; 2X29; X-ray; 2.30 A; A=80-246.
DR PDB; 6A3V; X-ray; 3.39 A; A/C/E/G/I/K/M/O/Q/S/U/W=58-254.
DR PDB; 6BWV; X-ray; 2.40 A; A/B=89-242.
DR PDB; 6CPR; X-ray; 2.70 A; A/B/C=80-244.
DR PDB; 6CU0; X-ray; 3.20 A; A/B/C/D/E/F=80-244.
DR PDB; 6D3N; X-ray; 2.70 A; A=80-244.
DR PDB; 6FIB; X-ray; 2.70 A; A/B/C=71-248.
DR PDB; 6MGE; X-ray; 2.95 A; A/B/C=58-254.
DR PDB; 6MGP; X-ray; 2.13 A; A/B/C=58-254.
DR PDBsum; 2X29; -.
DR PDBsum; 6A3V; -.
DR PDBsum; 6BWV; -.
DR PDBsum; 6CPR; -.
DR PDBsum; 6CU0; -.
DR PDBsum; 6D3N; -.
DR PDBsum; 6FIB; -.
DR PDBsum; 6MGE; -.
DR PDBsum; 6MGP; -.
DR AlphaFoldDB; P41273; -.
DR SMR; P41273; -.
DR BioGRID; 114281; 145.
DR DIP; DIP-3020N; -.
DR IntAct; P41273; 32.
DR STRING; 9606.ENSP00000245817; -.
DR iPTMnet; P41273; -.
DR PhosphoSitePlus; P41273; -.
DR BioMuta; TNFSF9; -.
DR DMDM; 728739; -.
DR EPD; P41273; -.
DR jPOST; P41273; -.
DR MassIVE; P41273; -.
DR MaxQB; P41273; -.
DR PaxDb; P41273; -.
DR PeptideAtlas; P41273; -.
DR PRIDE; P41273; -.
DR ProteomicsDB; 55457; -.
DR Antibodypedia; 24211; 646 antibodies from 40 providers.
DR CPTC; P41273; 2 antibodies.
DR DNASU; 8744; -.
DR Ensembl; ENST00000245817.5; ENSP00000245817.2; ENSG00000125657.5.
DR GeneID; 8744; -.
DR KEGG; hsa:8744; -.
DR MANE-Select; ENST00000245817.5; ENSP00000245817.2; NM_003811.4; NP_003802.1.
DR UCSC; uc002mfh.2; human.
DR CTD; 8744; -.
DR DisGeNET; 8744; -.
DR GeneCards; TNFSF9; -.
DR HGNC; HGNC:11939; TNFSF9.
DR HPA; ENSG00000125657; Tissue enhanced (esophagus, vagina).
DR MIM; 606182; gene.
DR neXtProt; NX_P41273; -.
DR OpenTargets; ENSG00000125657; -.
DR PharmGKB; PA36629; -.
DR VEuPathDB; HostDB:ENSG00000125657; -.
DR eggNOG; ENOG502SSK0; Eukaryota.
DR GeneTree; ENSGT00390000006244; -.
DR HOGENOM; CLU_095541_0_0_1; -.
DR InParanoid; P41273; -.
DR OMA; YVFFQLE; -.
DR OrthoDB; 1431273at2759; -.
DR PhylomeDB; P41273; -.
DR TreeFam; TF338523; -.
DR PathwayCommons; P41273; -.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR SignaLink; P41273; -.
DR BioGRID-ORCS; 8744; 12 hits in 1084 CRISPR screens.
DR ChiTaRS; TNFSF9; human.
DR EvolutionaryTrace; P41273; -.
DR GenomeRNAi; 8744; -.
DR Pharos; P41273; Tbio.
DR PRO; PR:P41273; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P41273; protein.
DR Bgee; ENSG00000125657; Expressed in buccal mucosa cell and 112 other tissues.
DR ExpressionAtlas; P41273; baseline and differential.
DR Genevisible; P41273; HS.
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; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IBA:GO_Central.
DR GO; GO:0045585; P:positive regulation of cytotoxic T cell differentiation; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; TAS:GO_Central.
DR GO; GO:0042129; P:regulation of T cell proliferation; TAS:GO_Central.
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; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="Tumor necrosis factor ligand superfamily member 9"
FT /id="PRO_0000185501"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT VARIANT 17
FT /note="P -> A (in dbSNP:rs442511)"
FT /id="VAR_011928"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2X29"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6D3N"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2X29"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:2X29"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6MGP"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 139..151
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:6CPR"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6FIB"
FT STRAND 195..206
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 211..222
FT /evidence="ECO:0007829|PDB:6MGP"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:6MGP"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6MGP"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6CPR"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:6MGP"
SQ SEQUENCE 254 AA; 26625 MW; 827551F34563E508 CRC64;
MEYASDASLD PEAPWPPAPR ARACRVLPWA LVAGLLLLLL LAAACAVFLA CPWAVSGARA
SPGSAASPRL REGPELSPDD PAGLLDLRQG MFAQLVAQNV LLIDGPLSWY SDPGLAGVSL
TGGLSYKEDT KELVVAKAGV YYVFFQLELR RVVAGEGSGS VSLALHLQPL RSAAGAAALA
LTVDLPPASS EARNSAFGFQ GRLLHLSAGQ RLGVHLHTEA RARHAWQLTQ GATVLGLFRV
TPEIPAGLPS PRSE
