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P27548 (CD40L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. 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:
CD40 ligand

Short name=CD40-L
Alternative name(s):
T-cell antigen Gp39
TNF-related activation protein
Short name=TRAP
Tumor necrosis factor ligand superfamily member 5
CD_antigen=CD154

Cleaved into the following 2 chains:

  1. CD40 ligand, membrane form
  2. CD40 ligand, soluble form
Gene names
Name:Cd40lg
Synonyms:Cd40l, Tnfsf5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytokine that binds to TNFRSF5. Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL-4. Involved in immunoglobulin class switching By similarity.

Subunit structure

Homotrimer.

Subcellular location

Cell membrane; Single-pass type II membrane protein.

CD40 ligand, soluble form: Secreted.

Tissue specificity

Specifically expressed on activated CD4+ T-lymphocytes.

Post-translational modification

The soluble form derives from the membrane form by proteolytic processing By similarity.

Sequence similarities

Belongs to the tumor necrosis factor family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionCytokine
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from genetic interaction PubMed 14647274. Source: MGI

B cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

immunoglobulin secretion

Inferred from genetic interaction PubMed 15485634. Source: MGI

inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

isotype switching

Inferred from direct assay PubMed 7529792. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

platelet activation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of endothelial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-12 production

Inferred from electronic annotation. Source: Ensembl

regulation of immunoglobulin secretion

Inferred from direct assay PubMed 12958312. Source: MGI

signal transduction

Non-traceable author statement PubMed 7529792. Source: UniProtKB

   Cellular_componentexternal side of plasma membrane

Inferred from direct assay PubMed 17082577. Source: MGI

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionCD40 receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260CD40 ligand, membrane form
PRO_0000034490
Chain112 – 260149CD40 ligand, soluble form By similarity
PRO_0000034491

Regions

Topological domain1 – 2222Cytoplasmic Potential
Transmembrane23 – 4624Helical; Signal-anchor for type II membrane protein; Potential
Topological domain47 – 260214Extracellular Potential

Sites

Site111 – 1122Cleavage By similarity

Amino acid modifications

Glycosylation2391N-linked (GlcNAc...) Potential
Disulfide bond177 ↔ 217 Ref.5

Experimental info

Sequence conflict1981S → I in AAC13640. Ref.3

Secondary structure

..................... 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27548 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 7E1AC117473672AD

FASTA26029,370
        10         20         30         40         50         60 
MIETYSQPSP RSVATGLPAS MKIFMYLLTV FLITQMIGSV LFAVYLHRRL DKVEEEVNLH 

        70         80         90        100        110        120 
EDFVFIKKLK RCNKGEGSLS LLNCEEMRRQ FEDLVKDITL NKEEKKENSF EMQRGDEDPQ 

       130        140        150        160        170        180 
IAAHVVSEAN SNAASVLQWA KKGYYTMKSN LVMLENGKQL TVKREGLYYV YTQVTFCSNR 

       190        200        210        220        230        240 
EPSSQRPFIV GLWLKPSSGS ERILLKAANT HSSSQLCEQQ SVHLGGVFEL QAGASVFVNV 

       250        260 
TEASQVIHRV GFSSFGLLKL 

« Hide

References

[1]"Molecular and biological characterization of a murine ligand for CD40."
Armitage R., Fanslow W., Sato T.A., Clifford K.N., Strockbine L., Macduff B.M., Anderson D.M., Gimpel S.D., Davis-Smith T., Maliszewski C.R., Clark E.A., Smith C.A., Grabstein K.H., Cosman D., Spriggs M.K.
Nature 357:80-82(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Spriggs M.K.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 198.
[3]"Structure of the murine CD40 ligand gene."
Tsitsikov E.N., Ramesh N., Geha R.S.
Mol. Immunol. 31:895-900(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 AND 137-260.
Strain: 129/Sv.
Tissue: Liver.
[4]"Emerging cytokine family."
Farrah T., Smith C.A.
Nature 358:26-26(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO THE TNF FAMILY.
[5]"A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors."
Peitsch M.C., Jongeneel C.V.
Int. Immunol. 5:233-238(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 115-260, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65453 mRNA. Translation: CAA46448.2.
S71858 Genomic DNA. Translation: AAC13639.1.
S71861 Genomic DNA. Translation: AAC13640.1.
CCDSCCDS30152.1.
PIRS21738.
RefSeqNP_035746.2. NM_011616.2.
UniGeneMm.4861.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CDAmodel-A/B/C115-260[»]
ProteinModelPortalP27548.
SMRP27548. Positions 115-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000033466.

PTM databases

PhosphoSiteP27548.

Proteomic databases

PaxDbP27548.
PRIDEP27548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033466; ENSMUSP00000033466; ENSMUSG00000031132.
GeneID21947.
KEGGmmu:21947.
UCSCuc009thb.1. mouse.

Organism-specific databases

CTD959.
MGIMGI:88337. Cd40lg.

Phylogenomic databases

eggNOGNOG39330.
HOGENOMHOG000111291.
HOVERGENHBG079629.
InParanoidP27548.
KOK03161.
OMAFLITQMI.
OrthoDBEOG7ZPNKR.
PhylomeDBP27548.
TreeFamTF332169.

Gene expression databases

ArrayExpressP27548.
BgeeP27548.
CleanExMM_CD40LG.
GenevestigatorP27548.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR003263. TNF_ligand_5.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamPF00229. TNF. 1 hit.
[Graphical view]
PIRSFPIRSF016527. TNF_5. 1 hit.
PRINTSPR01702. CD40LIGAND.
SMARTSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301600.
PROP27548.
SOURCESearch...

Entry information

Entry nameCD40L_MOUSE
AccessionPrimary (citable) accession number: P27548
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 14, 2001
Last modified: July 9, 2014
This is version 132 of the entry and version 2 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