Tumor necrosis factor ligand superfamily member 4

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P43488 (TNFL4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Cytokine
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell proliferation Inferred from electronic annotation. Source: Compara 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 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 innate immune response Non-traceable author statement PubMed 20844189. Source: BHF-UCL interleukin-4-dependent isotype switching to IgE isotypes Inferred from mutant phenotype PubMed 12496423. 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 cytokine secretion Inferred from physical interaction PubMed 14635034. Source: MGI 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-dependent 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 T cell cytokine production Inferred from direct assay PubMed 18354165 PubMed 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 differentiation Inferred from direct assay PubMed 18354165. Source: BHF-UCL positive regulation of activated T cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of alpha-beta T cell proliferation Inferred from mutant phenotype PubMed 16670306. 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: Compara positive regulation of interleukin-4 production Inferred from direct assay PubMed 18354165 PubMed 9670042. Source: BHF-UCL positive regulation of interleukin-6 production Inferred from mutant phenotype PubMed 20844189. 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 response to virus Inferred from direct assay PubMed 20639485. Source: BHF-UCL
Cellular_component	cell surface Inferred from sequence or structural similarity. Source: BHF-UCL extracellular space Inferred from sequence or structural similarity. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 198

198

Tumor necrosis factor ligand superfamily member 4

PRO_0000185494

Regions

Topological domain

1 – 28

Cytoplasmic Potential

Transmembrane

29 – 50

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

51 – 198

148

Extracellular Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Ref.2

Disulfide bond

Disulfide bond

Secondary structure

198

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P43488 [UniParc].

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

FASTA

198

22,255

        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.

IPI

IPI00120558.

PIR

S48290.

RefSeq

NP_033478.1. NM_009452.2.

UniGene

Mm.4994.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HEW	X-ray	1.45	F	51-198	[»]
2HEY	X-ray	2.00	F/G	51-198	[»]

ProteinModelPortal

P43488.

SMR

P43488. Positions 57-191.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6238N.

IntAct

P43488. 1 interaction.

PTM databases

PhosphoSite

P43488.

Proteomic databases

PRIDE

P43488.

Protocols and materials databases

DNASU

22164.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000028024; ENSMUSP00000028024; ENSMUSG00000026700.

GeneID

22164.

KEGG

mmu:22164.

Organism-specific databases

CTD

7292.

MGI

MGI:104511. Tnfsf4.

Phylogenomic databases

eggNOG

NOG47572.

GeneTree

ENSGT00390000015127.

HOGENOM

HOG000076309.

HOVERGEN

HBG056457.

InParanoid

P43488.

K05469.

OMA

MEGVQPL.

OrthoDB

EOG4K3KXF.

Gene expression databases

ArrayExpress

P43488.

Bgee

P43488.

Genevestigator

P43488.

GermOnline

ENSMUSG00000026700. Mus musculus.

Family and domain databases

InterPro

IPR006052. TNF.
IPR021184. TNF_CS.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]

Pfam

PF00229. TNF. 1 hit.
[Graphical view]

SMART

SM00207. TNF. 1 hit.
[Graphical view]

SUPFAM

SSF49842. TNF_like. 1 hit.

PROSITE

PS00251. TNF_1. 1 hit.
PS50049. TNF_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P43488.

NextBio

302098.

SOURCE

Search...

Entry information

Entry name

TNFL4_MOUSE

Accession

Primary (citable) accession number: P43488

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents