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P43488 (TNFL4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor ligand superfamily member 4
Alternative name(s):
OX40 ligand
Short name=OX40L
CD_antigen=CD252
Gene names
Name:Tnfsf4
Synonyms:Ox40l, Txgp1l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytokine that binds to TNFRSF4. Co-stimulates T-cell proliferation and cytokine production.

Subunit structure

Homotrimer. Ref.2

Subcellular location

Membrane; Single-pass type II membrane protein.

Sequence similarities

Belongs to the tumor necrosis factor family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionCytokine
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCD4-positive, alpha-beta T cell costimulation

Inferred from direct assay PubMed 20639485. Source: BHF-UCL

T cell proliferation

Inferred from electronic annotation. Source: Ensembl

T-helper 2 cell activation

Inferred from mutant phenotype PubMed 12496423. Source: BHF-UCL

acute inflammatory response

Inferred from mutant phenotype PubMed 20844189. Source: BHF-UCL

blood vessel development

Non-traceable author statement PubMed 20584752. Source: BHF-UCL

cellular response to lipopolysaccharide

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to nitrogen dioxide

Inferred from mutant phenotype PubMed 20659336. Source: BHF-UCL

cellular response to prostaglandin E stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

chemokine (C-C motif) ligand 11 production

Inferred from mutant phenotype PubMed 12355440. Source: BHF-UCL

cholesterol metabolic process

Inferred from mutant phenotype PubMed 3473481. Source: MGI

defense response to nematode

Inferred from mutant phenotype PubMed 12496423. Source: BHF-UCL

inflammatory response

Inferred from physical interaction PubMed 14635034. Source: MGI

innate immune response

Non-traceable author statement PubMed 20844189. Source: BHF-UCL

memory T cell activation

Inferred from mutant phenotype PubMed 12496423. Source: BHF-UCL

negative regulation of T cell apoptotic process

Inferred by curator PubMed 11567634. Source: BHF-UCL

negative regulation of T-helper 1 cell differentiation

Inferred from direct assay PubMed 9670042. Source: BHF-UCL

negative regulation of activation-induced cell death of T cells

Inferred by curator PubMed 11567634. Source: BHF-UCL

negative regulation of cytokine secretion

Inferred from physical interaction PubMed 14635034. Source: MGI

negative regulation of extrinsic apoptotic signaling pathway

Inferred by curator PubMed 11567634. Source: BHF-UCL

negative regulation of interferon-gamma production

Inferred from direct assay PubMed 9670042. Source: BHF-UCL

negative regulation of interleukin-17 production

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of regulatory T cell differentiation

Inferred from mutant phenotype PubMed 18713990. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 7749983. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 7749983. Source: BHF-UCL

positive regulation of B cell activation

Inferred from direct assay PubMed 9670042. Source: BHF-UCL

positive regulation of CD4-positive, alpha-beta T cell costimulation

Inferred from direct assay PubMed 20639485. Source: BHF-UCL

positive regulation of CD4-positive, alpha-beta T cell differentiation

Inferred from direct assay PubMed 20639485. Source: BHF-UCL

positive regulation of T cell costimulation

Inferred from direct assay PubMed 20639485. Source: BHF-UCL

positive regulation of T cell cytokine production

Inferred from direct assay PubMed 18354165PubMed 9670042. Source: BHF-UCL

positive regulation of T cell migration

Non-traceable author statement PubMed 9670042. Source: BHF-UCL

positive regulation of T-helper 2 cell activation

Inferred from mutant phenotype PubMed 12496423. Source: BHF-UCL

positive regulation of T-helper 2 cell differentiation

Inferred from direct assay PubMed 18354165. Source: BHF-UCL

positive regulation of activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of alpha-beta T cell proliferation

Inferred from mutant phenotype PubMed 16670306. Source: BHF-UCL

positive regulation of immune effector process

Traceable author statement PubMed 18713990. Source: BHF-UCL

positive regulation of immunoglobulin mediated immune response

Inferred from mutant phenotype PubMed 12496423. Source: BHF-UCL

positive regulation of immunoglobulin secretion

Inferred from direct assay PubMed 7749983. Source: BHF-UCL

positive regulation of inflammatory response

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interferon-gamma production

Inferred from mutant phenotype PubMed 18713990. Source: BHF-UCL

positive regulation of interleukin-10 production

Inferred from mutant phenotype PubMed 20844189. Source: BHF-UCL

positive regulation of interleukin-12 production

Inferred from mutant phenotype PubMed 20844189. Source: BHF-UCL

positive regulation of interleukin-13 production

Inferred from direct assay PubMed 18354165. Source: BHF-UCL

positive regulation of interleukin-2 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-4 production

Inferred from direct assay PubMed 18354165PubMed 9670042. Source: BHF-UCL

positive regulation of interleukin-4-dependent isotype switching to IgE isotypes

Inferred from mutant phenotype PubMed 12496423. Source: BHF-UCL

positive regulation of interleukin-6 production

Inferred from mutant phenotype PubMed 20844189. Source: BHF-UCL

positive regulation of memory T cell activation

Inferred from mutant phenotype PubMed 12496423. Source: BHF-UCL

positive regulation of memory T cell differentiation

Inferred from direct assay PubMed 18713990. Source: BHF-UCL

positive regulation of type 2 immune response

Inferred from direct assay PubMed 18354165. Source: BHF-UCL

regulation of adaptive immune response

Inferred from direct assay PubMed 20844189. Source: BHF-UCL

regulation of inflammatory response

Inferred from direct assay PubMed 12355440. Source: BHF-UCL

response to nitrogen dioxide

Inferred from direct assay PubMed 20659336. Source: BHF-UCL

response to virus

Inferred from direct assay PubMed 20639485. Source: BHF-UCL

   Cellular_componentcell surface

Inferred from sequence or structural similarity. Source: BHF-UCL

extracellular space

Inferred from sequence or structural similarity. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiontumor necrosis factor receptor binding

Inferred from physical interaction PubMed 14635034. Source: MGI

tumor necrosis factor receptor superfamily binding

Inferred from physical interaction PubMed 7749983. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Tumor necrosis factor ligand superfamily member 4
PRO_0000185494

Regions

Topological domain1 – 2828Cytoplasmic Potential
Transmembrane29 – 5022Helical; Signal-anchor for type II membrane protein; Potential
Topological domain51 – 198148Extracellular Potential

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Ref.2
Disulfide bond70 ↔ 163 Ref.2
Disulfide bond98 ↔ 183 Ref.2

Secondary structure

......................... 198
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43488 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F4B23A7CC0590459

FASTA19822,255
        10         20         30         40         50         60 
MEGEGVQPLD ENLENGSRPR FKWKKTLRLV VSGIKGAGML LCFIYVCLQL SSSPAKDPPI 

        70         80         90        100        110        120 
QRLRGAVTRC EDGQLFISSY KNEYQTMEVQ NNSVVIKCDG LYIIYLKGSF FQEVKIDLHF 

       130        140        150        160        170        180 
REDHNPISIP MLNDGRRIVF TVVASLAFKD KVYLTVNAPD TLCEHLQIND GELIVVQLTP 

       190 
GYCAPEGSYH STVNQVPL 

« Hide

References

[1]"Molecular characterization of murine and human OX40/OX40 ligand systems: identification of a human OX40 ligand as the HTLV-1-regulated protein gp34."
Baum P.R., Gayle R.B. III, Ramsdell F., Srinivasan S., Sorensen R.A., Watson M.L., Seldin M.F., Baker E., Sutherland G.R., Clifford K.N., Alderson M.R., Goodwin R.G., Fanslow W.C.
EMBO J. 13:3992-4001(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The crystal structure of the costimulatory OX40-OX40L complex."
Compaan D.M., Hymowitz S.G.
Structure 14:1321-1330(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 50-198, DISULFIDE BONDS, SUBUNIT, GLYCOSYLATION AT ASN-91.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12763 mRNA. Translation: AAA21871.1.
CCDSCCDS15416.1.
PIRS48290.
RefSeqNP_033478.1. NM_009452.2.
UniGeneMm.4994.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HEWX-ray1.45F51-198[»]
2HEYX-ray2.00F/G51-198[»]
ProteinModelPortalP43488.
SMRP43488. Positions 57-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6238N.
IntActP43488. 1 interaction.

PTM databases

PhosphoSiteP43488.

Proteomic databases

PRIDEP43488.

Protocols and materials databases

DNASU22164.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028024; ENSMUSP00000028024; ENSMUSG00000026700.
GeneID22164.
KEGGmmu:22164.
UCSCuc007dfn.2. mouse.

Organism-specific databases

CTD7292.
MGIMGI:104511. Tnfsf4.

Phylogenomic databases

eggNOGNOG47572.
GeneTreeENSGT00390000015127.
HOGENOMHOG000076309.
HOVERGENHBG056457.
InParanoidP43488.
KOK05469.
OMAMEGVQPL.
OrthoDBEOG74BJVD.
PhylomeDBP43488.
TreeFamTF336384.

Gene expression databases

BgeeP43488.
GenevestigatorP43488.

Family and domain databases

InterProIPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamPF00229. TNF. 1 hit.
[Graphical view]
SMARTSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS00251. TNF_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP43488.
NextBio302098.
PROP43488.
SOURCESearch...

Entry information

Entry nameTNFL4_MOUSE
AccessionPrimary (citable) accession number: P43488
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot