ID   TNFL4_MOUSE             Reviewed;         198 AA.
AC   P43488;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=Tumor necrosis factor ligand superfamily member 4;
DE   AltName: Full=OX40 ligand;
DE            Short=OX40L;
DE   AltName: CD_antigen=CD252;
GN   Name=Tnfsf4; Synonyms=Ox40l, Txgp1l;
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=8076595; DOI=10.1002/j.1460-2075.1994.tb06715.x;
RA   Baum P.R., Gayle R.B. III, Ramsdell F., Srinivasan S., Sorensen R.A.,
RA   Watson M.L., Seldin M.F., Baker E., Sutherland G.R., Clifford K.N.,
RA   Alderson M.R., Goodwin R.G., Fanslow W.C.;
RT   "Molecular characterization of murine and human OX40/OX40 ligand systems:
RT   identification of a human OX40 ligand as the HTLV-1-regulated protein
RT   gp34.";
RL   EMBO J. 13:3992-4001(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 50-198, DISULFIDE BONDS, SUBUNIT,
RP   AND GLYCOSYLATION AT ASN-91.
RX   PubMed=16905106; DOI=10.1016/j.str.2006.06.015;
RA   Compaan D.M., Hymowitz S.G.;
RT   "The crystal structure of the costimulatory OX40-OX40L complex.";
RL   Structure 14:1321-1330(2006).
CC   -!- FUNCTION: Cytokine that binds to TNFRSF4. Co-stimulates T-cell
CC       proliferation and cytokine production.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16905106}.
CC   -!- INTERACTION:
CC       P43488; P23510: TNFSF4; Xeno; NbExp=2; IntAct=EBI-519690, EBI-11724451;
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; U12763; AAA21871.1; -; mRNA.
DR   CCDS; CCDS15416.1; -.
DR   PIR; S48290; S48290.
DR   RefSeq; NP_033478.1; NM_009452.2.
DR   PDB; 2HEW; X-ray; 1.45 A; F=51-198.
DR   PDB; 2HEY; X-ray; 2.00 A; F/G=51-198.
DR   PDBsum; 2HEW; -.
DR   PDBsum; 2HEY; -.
DR   AlphaFoldDB; P43488; -.
DR   SMR; P43488; -.
DR   DIP; DIP-6238N; -.
DR   IntAct; P43488; 2.
DR   STRING; 10090.ENSMUSP00000028024; -.
DR   GlyCosmos; P43488; 1 site, No reported glycans.
DR   GlyGen; P43488; 1 site.
DR   iPTMnet; P43488; -.
DR   PhosphoSitePlus; P43488; -.
DR   PaxDb; 10090-ENSMUSP00000028024; -.
DR   ProteomicsDB; 258791; -.
DR   Antibodypedia; 34389; 817 antibodies from 40 providers.
DR   DNASU; 22164; -.
DR   Ensembl; ENSMUST00000028024.5; ENSMUSP00000028024.5; ENSMUSG00000026700.5.
DR   GeneID; 22164; -.
DR   KEGG; mmu:22164; -.
DR   UCSC; uc007dfn.2; mouse.
DR   AGR; MGI:104511; -.
DR   CTD; 7292; -.
DR   MGI; MGI:104511; Tnfsf4.
DR   VEuPathDB; HostDB:ENSMUSG00000026700; -.
DR   eggNOG; ENOG502ST4X; Eukaryota.
DR   GeneTree; ENSGT00390000015127; -.
DR   HOGENOM; CLU_091735_0_0_1; -.
DR   InParanoid; P43488; -.
DR   OMA; TTHNTSC; -.
DR   OrthoDB; 4334524at2759; -.
DR   PhylomeDB; P43488; -.
DR   TreeFam; TF336384; -.
DR   Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
DR   BioGRID-ORCS; 22164; 1 hit in 117 CRISPR screens.
DR   EvolutionaryTrace; P43488; -.
DR   PRO; PR:P43488; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P43488; Protein.
DR   Bgee; ENSMUSG00000026700; Expressed in scapula and 28 other cell types or tissues.
DR   ExpressionAtlas; P43488; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0005164; F:tumor necrosis factor receptor binding; IPI:MGI.
DR   GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; IPI:BHF-UCL.
DR   GO; GO:0002526; P:acute inflammatory response; IMP:BHF-UCL.
DR   GO; GO:0001568; P:blood vessel development; NAS:BHF-UCL.
DR   GO; GO:0035783; P:CD4-positive, alpha-beta T cell costimulation; IDA:BHF-UCL.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:BHF-UCL.
DR   GO; GO:0035714; P:cellular response to nitrogen dioxide; IMP:BHF-UCL.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISS:BHF-UCL.
DR   GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
DR   GO; GO:0002215; P:defense response to nematode; IMP:BHF-UCL.
DR   GO; GO:0006954; P:inflammatory response; IPI:MGI.
DR   GO; GO:0045087; P:innate immune response; NAS:BHF-UCL.
DR   GO; GO:0035709; P:memory T cell activation; IMP:BHF-UCL.
DR   GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IC:BHF-UCL.
DR   GO; GO:0001818; P:negative regulation of cytokine production; IPI:MGI.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IC:BHF-UCL.
DR   GO; GO:0032700; P:negative regulation of interleukin-17 production; ISS:BHF-UCL.
DR   GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0070233; P:negative regulation of T cell apoptotic process; IC:BHF-UCL.
DR   GO; GO:0045626; P:negative regulation of T-helper 1 cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0032689; P:negative regulation of type II interferon production; IDA:BHF-UCL.
DR   GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:MGI.
DR   GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0050871; P:positive regulation of B cell activation; IDA:BHF-UCL.
DR   GO; GO:1900281; P:positive regulation of CD4-positive, alpha-beta T cell costimulation; IDA:BHF-UCL.
DR   GO; GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0032722; P:positive regulation of chemokine production; IMP:BHF-UCL.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IBA:GO_Central.
DR   GO; GO:0002699; P:positive regulation of immune effector process; TAS:BHF-UCL.
DR   GO; GO:0002891; P:positive regulation of immunoglobulin mediated immune response; IMP:BHF-UCL.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; IDA:BHF-UCL.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:BHF-UCL.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:BHF-UCL.
DR   GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:BHF-UCL.
DR   GO; GO:0032736; P:positive regulation of interleukin-13 production; IDA:BHF-UCL.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:MGI.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:BHF-UCL.
DR   GO; GO:2000572; P:positive regulation of interleukin-4-dependent isotype switching to IgE isotypes; IMP:BHF-UCL.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:BHF-UCL.
DR   GO; GO:2000568; P:positive regulation of memory T cell activation; IMP:BHF-UCL.
DR   GO; GO:0043382; P:positive regulation of memory T cell differentiation; IDA:BHF-UCL.
DR   GO; GO:2000525; P:positive regulation of T cell costimulation; IDA:BHF-UCL.
DR   GO; GO:0002726; P:positive regulation of T cell cytokine production; IDA:BHF-UCL.
DR   GO; GO:2000406; P:positive regulation of T cell migration; NAS:BHF-UCL.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central.
DR   GO; GO:2000570; P:positive regulation of T-helper 2 cell activation; IMP:BHF-UCL.
DR   GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0002830; P:positive regulation of type 2 immune response; IDA:BHF-UCL.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; IMP:BHF-UCL.
DR   GO; GO:0002819; P:regulation of adaptive immune response; IDA:BHF-UCL.
DR   GO; GO:0050727; P:regulation of inflammatory response; IDA:BHF-UCL.
DR   GO; GO:0035713; P:response to nitrogen dioxide; IDA:BHF-UCL.
DR   GO; GO:0009615; P:response to virus; IDA:BHF-UCL.
DR   GO; GO:0042098; P:T cell proliferation; ISO:MGI.
DR   GO; GO:0035712; P:T-helper 2 cell activation; IMP:BHF-UCL.
DR   CDD; cd00184; TNF; 1.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR021184; TNF_CS.
DR   InterPro; IPR006052; TNF_dom.
DR   InterPro; IPR042338; TNFSF4.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR17534; OX40 LIGAND; 1.
DR   PANTHER; PTHR17534:SF4; TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 4; 1.
DR   SMART; SM00207; TNF; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS00251; TNF_1; 1.
DR   Genevisible; P43488; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytokine; Disulfide bond; Glycoprotein; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..198
FT                   /note="Tumor necrosis factor ligand superfamily member 4"
FT                   /id="PRO_0000185494"
FT   TOPO_DOM        1..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..50
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16905106"
FT   DISULFID        70..163
FT                   /evidence="ECO:0000269|PubMed:16905106"
FT   DISULFID        98..183
FT                   /evidence="ECO:0000269|PubMed:16905106"
FT   STRAND          62..71
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   STRAND          100..112
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   STRAND          135..146
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   STRAND          151..156
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   HELIX           160..165
FT                   /evidence="ECO:0007829|PDB:2HEW"
FT   STRAND          168..177
FT                   /evidence="ECO:0007829|PDB:2HEW"
SQ   SEQUENCE   198 AA;  22255 MW;  F4B23A7CC0590459 CRC64;
     MEGEGVQPLD ENLENGSRPR FKWKKTLRLV VSGIKGAGML LCFIYVCLQL SSSPAKDPPI
     QRLRGAVTRC EDGQLFISSY KNEYQTMEVQ NNSVVIKCDG LYIIYLKGSF FQEVKIDLHF
     REDHNPISIP MLNDGRRIVF TVVASLAFKD KVYLTVNAPD TLCEHLQIND GELIVVQLTP
     GYCAPEGSYH STVNQVPL
//