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CD40 ligand (CD40-L) (T-cell antigen Gp39) (TNF-related activation protein) (TRAP) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)]

 CD40L_HUMAN             Reviewed;         261 AA.
P29965;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
17-JUN-2020, entry version 216.
RecName: Full=CD40 ligand;
Short=CD40-L;
AltName: Full=T-cell antigen Gp39;
AltName: Full=TNF-related activation protein;
Short=TRAP;
AltName: Full=Tumor necrosis factor ligand superfamily member 5;
AltName: CD_antigen=CD154;
Contains:
RecName: Full=CD40 ligand, membrane form;
Contains:
RecName: Full=CD40 ligand, soluble form {ECO:0000303|PubMed:8626375};
Short=sCD40L {ECO:0000303|PubMed:31331973};
Name=CD40LG; Synonyms=CD40L, TNFSF5, TRAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=1280226; DOI=10.1002/eji.1830221226;
Graf D., Korthaeuer U., Mages H.W., Senger G., Kroczek R.A.;
"Cloning of TRAP, a ligand for CD40 on human T cells.";
Eur. J. Immunol. 22:3191-3194(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1385114; DOI=10.1002/j.1460-2075.1992.tb05530.x;
Hollenbaugh D., Grosmaire L.S., Kullas C.D., Chalupny J.N.,
Braesch-Andersen S., Noelle R.J., Stamenkovic I., Ledbetter J.A.,
Aruffo A.;
"The human T cell antigen gp39, a member of the TNF gene family, is a
ligand for the CD40 receptor: expression of a soluble form of gp39 with B
cell co-stimulatory activity.";
EMBO J. 11:4313-4321(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIGM1 128-ARG-GLY-129 AND PRO-235.
PubMed=7678782; DOI=10.1016/0092-8674(93)90668-g;
Aruffo A., Farrington M., Hollenbaugh D., Li X., Milatovich A.,
Nonoyama S., Bajorath J., Grosmaire L.S., Stenkamp R., Neubauer M.,
Roberts R.L., Noelle R.J., Ledbetter J.A., Francke U., Ochs H.D.;
"The CD40 ligand, gp39, is defective in activated T cells from patients
with X-linked hyper-IgM syndrome.";
Cell 72:291-300(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1281209; DOI=10.1084/jem.176.6.1543;
Spriggs M.K., Armitage R.J., Strockbine L., Clifford K.N., Macduff B.M.,
Sato T.A., Maliszewski C.R., Fanslow W.C.;
"Recombinant human CD40 ligand stimulates B cell proliferation and
immunoglobulin E secretion.";
J. Exp. Med. 176:1543-1550(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=7678552; DOI=10.1016/0014-5793(93)81175-y;
Gauchat J.-F., Aubry J.-P., Mazzei G.J., Life P., Jomotte T., Elson G.,
Bonnefoy J.-Y.;
"Human CD40-ligand: molecular cloning, cellular distribution and regulation
of expression by factors controlling IgE production.";
FEBS Lett. 315:259-266(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7999797; DOI=10.1016/0167-4781(94)00179-7;
Shimadzu M., Nunoi H., Terasaki H., Ninomiya R., Iwata M., Kanegasaka S.,
Matsuda I.;
"Structural organization of the gene for CD40 ligand: molecular analysis
for diagnosis of X-linked hyper-IgM syndrome.";
Biochim. Biophys. Acta 1260:67-72(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 113-117, PROTEOLYTIC PROCESSING, SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=8626375; DOI=10.1074/jbc.271.11.5965;
Pietravalle F., Lecoanet-Henchoz S., Blasey H., Aubry J.-P., Elson G.,
Edgerton M.D., Bonnefoy J.-Y., Gauchat J.-F.;
"Human native soluble CD40L is a biologically active trimer, processed
inside microsomes.";
J. Biol. Chem. 271:5965-5967(1996).
[9]
FUNCTION.
PubMed=8617933;
Blotta M.H., Marshall J.D., DeKruyff R.H., Umetsu D.T.;
"Cross-linking of the CD40 ligand on human CD4+ T lymphocytes generates a
costimulatory signal that up-regulates IL-4 synthesis.";
J. Immunol. 156:3133-3140(1996).
[10]
GLYCOSYLATION AT ASN-240, STRUCTURE OF CARBOHYDRATE ON ASN-240,
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
PubMed=11676606; DOI=10.1006/prep.2001.1501;
Khandekar S.S., Silverman C., Wells-Marani J., Bacon A.M., Birrell H.,
Brigham-Burke M., DeMarini D.J., Jonak Z.L., Camilleri P.,
Fishman-Lobell J.;
"Determination of carbohydrate structures N-linked to soluble CD154 and
characterization of the interactions of CD40 with CD154 expressed in Pichia
pastoris and Chinese hamster ovary cells.";
Protein Expr. Purif. 23:301-310(2001).
[11]
FUNCTION.
PubMed=15193700; DOI=10.1016/j.jacc.2003.12.055;
Furman M.I., Krueger L.A., Linden M.D., Barnard M.R., Frelinger A.L. III,
Michelson A.D.;
"Release of soluble CD40L from platelets is regulated by glycoprotein
IIb/IIIa and actin polymerization.";
J. Am. Coll. Cardiol. 43:2319-2325(2004).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15067037; DOI=10.1084/jem.20031705;
Mikolajczak S.A., Ma B.Y., Yoshida T., Yoshida R., Kelvin D.J., Ochi A.;
"The modulation of CD40 ligand signaling by transmembrane CD28 splice
variant in human T cells.";
J. Exp. Med. 199:1025-1031(2004).
[13]
FUNCTION AS CD40 AND INTEGRIN LIGAND, CHARACTERIZATION OF VARIANTS HIGM1
CYS-170; ARG-174; ILE-176; ASP-208; TYR-224; ALA-226; VAL-227 AND SER-258,
AND MUTAGENESIS OF TYR-170; HIS-224; GLY-226 AND GLY-252.
PubMed=31331973; DOI=10.4049/jimmunol.1801630;
Takada Y.K., Yu J., Shimoda M., Takada Y.;
"Integrin Binding to the Trimeric Interface of CD40L Plays a Critical Role
in CD40/CD40L Signaling.";
J. Immunol. 203:1383-1391(2019).
[14]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 116-261, AND SUBUNIT.
PubMed=8589998; DOI=10.1016/s0969-2126(01)00239-8;
Karpsusas M., Hsu Y.-M., Wang J.-H., Thompson J., Lederman S., Chess L.,
Thomas D.;
"2-A crystal structure of an extracellular fragment of human CD40 ligand.";
Structure 3:1031-1039(1995).
[15]
3D-STRUCTURE MODELING OF COMPLEX WITH CD40.
PubMed=9605317; DOI=10.1002/pro.5560070506;
Singh J., Garber E., van Vlijmen H., Karpsusas M., Hsu Y.-M., Zheng Z.,
Naismith J.H., Thomas D.;
"The role of polar interactions in the molecular recognition of CD40L with
its receptor CD40.";
Protein Sci. 7:1124-1135(1998).
[16]
VARIANTS HIGM1 ARG-36 AND GLY-140.
PubMed=7679206; DOI=10.1038/361539a0;
Korthaeuer U., Graf D., Mages H.W., Briere F., Padayachee M., Malcolm S.,
Ugazio A.G., Notarangelo L.D., Levinsky R.J., Kroczek R.A.;
"Defective expression of T-cell CD40 ligand causes X-linked
immunodeficiency with hyper-IgM.";
Nature 361:539-541(1993).
[17]
VARIANT HIGM1 GLU-123.
PubMed=8094231; DOI=10.1038/361541a0;
Disanto J.P., Bonnefoy J.-Y., Gauchat J.-F., Fischer A.,
de Saint Basile G.;
"CD40 ligand mutations in X-linked immunodeficiency with hyper-IgM.";
Nature 361:541-543(1993).
[18]
VARIANTS HIGM1 PRO-155; ASN-211 AND VAL-227.
PubMed=7679801; DOI=10.1126/science.7679801;
Allen R.C., Armitage R.J., Conley M.E., Rosenblatt H., Jenkins N.A.,
Copeland N.G., Bedell M.A., Edelhoff S., Disteche C.M., Simoneaux D.K.,
Fanslow W.C., Belmont J.W., Spriggs M.K.;
"CD40 ligand gene defects responsible for X-linked hyper-IgM syndrome.";
Science 259:990-993(1993).
[19]
VARIANTS HIGM1 ALA-126; ARG-140 AND GLU-144.
PubMed=7717401;
Macchi P., Villa A., Strina D., Sacco M.G., Morali F., Brugnoni D.,
Giliani S., Mantuano E., Fasth A., Andersson B., Zegers B.J.M., Cavagni G.,
Reznick I., Levy J., Zan-Bar I., Porat Y., Airo P., Plebani A., Vezzoni P.,
Notarangelo L.D.;
"Characterization of nine novel mutations in the CD40 ligand gene in
patients with X-linked hyper IgM syndrome of various ancestry.";
Am. J. Hum. Genet. 56:898-906(1995).
[20]
VARIANT HIGM1 GLU-237.
PubMed=7532185; DOI=10.1172/jci117692;
Saiki O., Tanaka T., Wada Y., Uda H., Inoue A., Katada Y., Izeki M.,
Iwata M., Nunoi H., Matsuda I.;
"Signaling through CD40 rescues IgE but not IgG or IgA secretion in X-
linked immunodeficiency with hyper-IgM.";
J. Clin. Invest. 95:510-514(1995).
[21]
VARIANTS HIGM1 ARG-38; ARG-125; ARG-174 AND SER-257.
PubMed=8889581;
DOI=10.1002/(sici)1098-1004(1996)8:3<223::aid-humu5>3.0.co;2-a;
Katz F., Hinshelwood S., Rutland P., Jones A., Kinnon C., Morgan G.;
"Mutation analysis in CD40 ligand deficiency leading to X-linked
hypogammaglobulinemia with hyper IgM syndrome.";
Hum. Mutat. 8:223-228(1996).
[22]
VARIANTS HIGM1 PRO-155 AND VAL-227, AND VARIANT ARG-219.
PubMed=8550833; DOI=10.1172/jci118389;
Lin Q., Rohrer J., Allen R.C., Larche M., Greene J.M., Shigeoka A.O.,
Gatti R.A., Derauf D.C., Belmont J.W., Conley M.E.;
"A single strand conformation polymorphism study of CD40 ligand. Efficient
mutation analysis and carrier detection for X-linked hyper IgM syndrome.";
J. Clin. Invest. 97:196-201(1996).
[23]
VARIANTS HIGM1 ARG-36; CYS-140; GLY-227 DEL; SER-231 AND MET-254.
PubMed=9150729; DOI=10.1007/s004390050417;
Nonoyama S., Shimadzu M., Toru H., Seyama K., Nunoi H., Neubauer M.,
Yata J., Och H.D.;
"Mutations of the CD40 ligand gene in 13 Japanese patients with X-linked
hyper-IgM syndrome.";
Hum. Genet. 99:624-627(1997).
[24]
VARIANTS HIGM1 SER-116; ASN-147; CYS-170; VAL-227; SER-231; PRO-235;
MET-254 AND SER-258.
PubMed=9746782;
Seyama K., Nonoyama S., Gangsaas I., Hollenbaugh D., Pabst H.F., Aruffo A.,
Ochs H.D.;
"Mutations of the CD40 ligand gene and its effect on CD40 ligand expression
in patients with X-linked hyper IgM syndrome.";
Blood 92:2421-2434(1998).
[25]
VARIANT HIGM1 SER-116.
PubMed=26545377; DOI=10.1007/s00251-015-0878-6;
Ouadani H., Ben-Mustapha I., Ben-ali M., Ben-khemis L., Largueche B.,
Boussoffara R., Maalej S., Fetni I., Hassayoun S., Mahfoudh A.,
Mellouli F., Yalaoui S., Masmoudi H., Bejaoui M., Barbouche M.R.;
"Novel and recurrent AID mutations underlie prevalent autosomal recessive
form of HIGM in consanguineous patients.";
Immunogenetics 68:19-28(2016).
-!- FUNCTION: Cytokine that acts as a ligand to CD40/TNFRSF5
(PubMed:1280226, PubMed:31331973). Costimulates T-cell proliferation
and cytokine production (PubMed:8617933). Its cross-linking on T-cells
generates a costimulatory signal which enhances the production of IL4
and IL10 in conjunction with the TCR/CD3 ligation and CD28
costimulation (PubMed:8617933). Induces the activation of NF-kappa-B
(PubMed:15067037, PubMed:31331973). Induces the activation of kinases
MAPK8 and PAK2 in T-cells (PubMed:15067037). Induces tyrosine
phosphorylation of isoform 3 of CD28 (PubMed:15067037). Mediates B-cell
proliferation in the absence of co-stimulus as well as IgE production
in the presence of IL4 (By similarity). Involved in immunoglobulin
class switching (By similarity). {ECO:0000250|UniProtKB:P27548,
ECO:0000269|PubMed:1280226, ECO:0000269|PubMed:15067037,
ECO:0000269|PubMed:31331973, ECO:0000269|PubMed:8617933}.
-!- FUNCTION: [CD40 ligand, soluble form]: Acts as a ligand for integrins,
specifically ITGA5:ITGB1 and ITGAV:ITGB3; both integrins and the CD40
receptor are required for activation of CD40-CD40LG signaling, which
have cell-type dependent effects, such as B-cell activation, NF-kappa-B
signaling and anti-apoptotic signaling. {ECO:0000269|PubMed:31331973}.
-!- SUBUNIT: Homotrimer (PubMed:8626375, PubMed:11676606, PubMed:8589998).
Interacts with isoform 3 of CD28 (PubMed:15067037). CD40 ligand,
soluble form: Exists as either a monomer or a homotrimer
(PubMed:8626375, PubMed:31331973). Forms a ternary complex between CD40
and integrins for CD40-CD40LG signaling (PubMed:31331973).
{ECO:0000269|PubMed:11676606, ECO:0000269|PubMed:15067037,
ECO:0000269|PubMed:31331973, ECO:0000269|PubMed:8589998,
ECO:0000269|PubMed:8626375}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8626375};
Single-pass type II membrane protein {ECO:0000303|PubMed:8626375}. Cell
surface {ECO:0000269|PubMed:15067037, ECO:0000269|PubMed:7678552}.
-!- SUBCELLULAR LOCATION: [CD40 ligand, soluble form]: Secreted
{ECO:0000269|PubMed:8626375}. Note=Release of soluble CD40L from
platelets is partially regulated by GP IIb/IIIa, actin polymerization,
and a matrix metalloproteinases (MMP) inhibitor-sensitive pathway.
{ECO:0000269|PubMed:15193700}.
-!- TISSUE SPECIFICITY: Specifically expressed on activated CD4+ T-
lymphocytes.
-!- PTM: The soluble form derives from the membrane form by proteolytic
processing. {ECO:0000269|PubMed:8626375}.
-!- PTM: N-linked glycan is a mixture of high mannose and complex type.
Glycan structure does not influence binding affinity to CD40.
{ECO:0000269|PubMed:11676606}.
-!- PTM: Not O-glycosylated.
-!- DISEASE: Immunodeficiency with hyper-IgM, type 1 (HIGM1) [MIM:308230]:
Immunoglobulin isotype switch defect characterized by elevated
concentrations of serum IgM and decreased amounts of all other
isotypes. Affected males present at an early age (usually within the
first year of life) recurrent bacterial and opportunistic infections,
including Pneumocystis carinii pneumonia and intractable diarrhea due
to cryptosporidium infection. Despite substitution treatment with
intravenous immunoglobulin, the overall prognosis is rather poor, with
a death rate of about 10% before adolescence.
{ECO:0000269|PubMed:26545377, ECO:0000269|PubMed:31331973,
ECO:0000269|PubMed:7532185, ECO:0000269|PubMed:7678782,
ECO:0000269|PubMed:7679206, ECO:0000269|PubMed:7679801,
ECO:0000269|PubMed:7717401, ECO:0000269|PubMed:8094231,
ECO:0000269|PubMed:8550833, ECO:0000269|PubMed:8889581,
ECO:0000269|PubMed:9150729, ECO:0000269|PubMed:9746782}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
-!- WEB RESOURCE: Name=CD40Lbase; Note=CD40L defect database;
URL="http://structure.bmc.lu.se/idbase/CD40Lbase/";
---------------------------------------------------------------------------
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EMBL; X68550; CAA48554.1; -; mRNA.
EMBL; Z15017; CAA78737.1; -; mRNA.
EMBL; X67878; CAA48077.1; -; mRNA.
EMBL; L07414; AAA35662.1; -; mRNA.
EMBL; D31797; BAA06599.1; -; Genomic_DNA.
EMBL; BC071754; AAH71754.1; -; mRNA.
EMBL; BC074950; AAH74950.1; -; mRNA.
CCDS; CCDS14659.1; -.
PIR; S28017; I53476.
RefSeq; NP_000065.1; NM_000074.2.
PDB; 1ALY; X-ray; 2.00 A; A=116-261.
PDB; 1I9R; X-ray; 3.10 A; A/B/C=116-261.
PDB; 3LKJ; X-ray; 2.50 A; A/B/C=121-261.
PDB; 3QD6; X-ray; 3.50 A; A/B/C/D/E/F=116-261.
PDB; 6BRB; X-ray; 2.82 A; A=120-261.
PDBsum; 1ALY; -.
PDBsum; 1I9R; -.
PDBsum; 3LKJ; -.
PDBsum; 3QD6; -.
PDBsum; 6BRB; -.
SMR; P29965; -.
BioGRID; 107397; 9.
DIP; DIP-3013N; -.
STRING; 9606.ENSP00000359663; -.
ChEMBL; CHEMBL3580491; -.
DrugBank; DB06475; Ruplizumab.
GlyConnect; 610; -.
iPTMnet; P29965; -.
PhosphoSitePlus; P29965; -.
UniCarbKB; P29965; -.
BioMuta; CD40LG; -.
DMDM; 231718; -.
MassIVE; P29965; -.
MaxQB; P29965; -.
PaxDb; P29965; -.
PeptideAtlas; P29965; -.
PRIDE; P29965; -.
ProteomicsDB; 54611; -.
ABCD; P29965; 6 sequenced antibodies.
Antibodypedia; 16693; 1945 antibodies.
DNASU; 959; -.
Ensembl; ENST00000370629; ENSP00000359663; ENSG00000102245.
GeneID; 959; -.
KEGG; hsa:959; -.
UCSC; uc004faa.4; human.
CTD; 959; -.
DisGeNET; 959; -.
EuPathDB; HostDB:ENSG00000102245.7; -.
GeneCards; CD40LG; -.
GeneReviews; CD40LG; -.
HGNC; HGNC:11935; CD40LG.
HPA; ENSG00000102245; Group enriched (blood, intestine, lymphoid tissue).
MalaCards; CD40LG; -.
MIM; 300386; gene.
MIM; 308230; phenotype.
neXtProt; NX_P29965; -.
OpenTargets; ENSG00000102245; -.
Orphanet; 101088; X-linked hyper-IgM syndrome.
PharmGKB; PA36626; -.
eggNOG; ENOG410IVYF; Eukaryota.
eggNOG; ENOG4111TET; LUCA.
GeneTree; ENSGT00970000193396; -.
InParanoid; P29965; -.
KO; K03161; -.
OMA; MKMDKME; -.
OrthoDB; 1146113at2759; -.
PhylomeDB; P29965; -.
TreeFam; TF332169; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
SIGNOR; P29965; -.
BioGRID-ORCS; 959; 2 hits in 412 CRISPR screens.
EvolutionaryTrace; P29965; -.
GeneWiki; CD154; -.
GenomeRNAi; 959; -.
Pharos; P29965; Tbio.
PRO; PR:P29965; -.
Proteomes; UP000005640; Chromosome X.
RNAct; P29965; protein.
Bgee; ENSG00000102245; Expressed in leukocyte and 62 other tissues.
ExpressionAtlas; P29965; baseline and differential.
Genevisible; P29965; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005174; F:CD40 receptor binding; IMP:UniProtKB.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0005178; F:integrin binding; IMP:UniProtKB.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:UniProtKB.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:0042100; P:B cell proliferation; IDA:UniProtKB.
GO; GO:0023035; P:CD40 signaling pathway; IMP:UniProtKB.
GO; GO:0048305; P:immunoglobulin secretion; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0045190; P:isotype switching; ISS:UniProtKB.
GO; GO:0007159; P:leukocyte cell-cell adhesion; NAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; IDA:UniProtKB.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:UniProtKB.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0051023; P:regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0031295; P:T cell costimulation; TAS:UniProtKB.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
CDD; cd00184; TNF; 1.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR003263; CD40L.
InterPro; IPR021184; TNF_CS.
InterPro; IPR006052; TNF_dom.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
PANTHER; PTHR11471:SF5; PTHR11471:SF5; 1.
Pfam; PF00229; TNF; 1.
PIRSF; PIRSF016527; TNF_5; 1.
PRINTS; PR01702; CD40LIGAND.
SMART; SM00207; TNF; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS00251; TNF_1; 1.
PROSITE; PS50049; TNF_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Cytokine; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Membrane; Polymorphism;
Reference proteome; Secreted; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1..261
/note="CD40 ligand, membrane form"
/id="PRO_0000034484"
CHAIN 113..261
/note="CD40 ligand, soluble form"
/evidence="ECO:0000269|PubMed:8626375"
/id="PRO_0000034485"
TOPO_DOM 1..22
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 23..46
/note="Helical; Signal-anchor for type II membrane protein"
/evidence="ECO:0000255"
TOPO_DOM 47..261
/note="Extracellular"
/evidence="ECO:0000255"
SITE 112..113
/note="Cleavage"
CARBOHYD 240
/note="N-linked (GlcNAc...) (complex) asparagine;
alternate"
/evidence="ECO:0000269|PubMed:11676606"
CARBOHYD 240
/note="N-linked (GlcNAc...) (high mannose) asparagine;
alternate"
/evidence="ECO:0000269|PubMed:11676606"
DISULFID 178..218
/evidence="ECO:0000255"
VARIANT 36
/note="M -> R (in HIGM1; dbSNP:rs104894774)"
/evidence="ECO:0000269|PubMed:7679206,
ECO:0000269|PubMed:9150729"
/id="VAR_007513"
VARIANT 38
/note="G -> R (in HIGM1)"
/evidence="ECO:0000269|PubMed:8889581"
/id="VAR_017925"
VARIANT 116
/note="G -> R (in HIGM1)"
/id="VAR_017929"
VARIANT 116
/note="G -> S (in HIGM1)"
/evidence="ECO:0000269|PubMed:26545377,
ECO:0000269|PubMed:9746782"
/id="VAR_017930"
VARIANT 123
/note="A -> E (in HIGM1; dbSNP:rs104894778)"
/evidence="ECO:0000269|PubMed:8094231"
/id="VAR_007514"
VARIANT 125
/note="H -> R (in HIGM1)"
/evidence="ECO:0000269|PubMed:8889581"
/id="VAR_017926"
VARIANT 126
/note="V -> A (in HIGM1)"
/evidence="ECO:0000269|PubMed:7717401"
/id="VAR_007515"
VARIANT 126
/note="V -> D (in HIGM1)"
/id="VAR_017931"
VARIANT 128..129
/note="SE -> RG (in HIGM1)"
/id="VAR_007516"
VARIANT 140
/note="W -> C (in HIGM1)"
/evidence="ECO:0000269|PubMed:9150729"
/id="VAR_007517"
VARIANT 140
/note="W -> G (in HIGM1; dbSNP:rs104894777)"
/evidence="ECO:0000269|PubMed:7679206"
/id="VAR_007518"
VARIANT 140
/note="W -> R (in HIGM1)"
/evidence="ECO:0000269|PubMed:7717401"
/id="VAR_007519"
VARIANT 143
/note="K -> T (in HIGM1)"
/id="VAR_017932"
VARIANT 144
/note="G -> E (in HIGM1; dbSNP:rs886039326)"
/evidence="ECO:0000269|PubMed:7717401"
/id="VAR_007520"
VARIANT 147
/note="T -> N (in HIGM1; dbSNP:rs1057521127)"
/evidence="ECO:0000269|PubMed:9746782"
/id="VAR_017922"
VARIANT 155
/note="L -> P (in HIGM1; dbSNP:rs104894769)"
/evidence="ECO:0000269|PubMed:7679801,
ECO:0000269|PubMed:8550833"
/id="VAR_007521"
VARIANT 170
/note="Y -> C (in HIGM1; decreases ITGA5:ITGB1 and
ITGAV:ITGB3 binding of the soluble form; decreases
activation of NF-kappa-B signaling; slightly decreases CD40
binding of the soluble form; dbSNP:rs756468554)"
/evidence="ECO:0000269|PubMed:31331973,
ECO:0000269|PubMed:9746782"
/id="VAR_017923"
VARIANT 173
/note="A -> D (in HIGM1)"
/id="VAR_017933"
VARIANT 174
/note="Q -> R (in HIGM1; decreases ITGA5:ITGB1 and
ITGAV:ITGB3 binding of the soluble form; decreases
activation of NF-kappa-B signaling)"
/evidence="ECO:0000269|PubMed:31331973,
ECO:0000269|PubMed:8889581"
/id="VAR_017927"
VARIANT 176
/note="T -> I (in HIGM1; decreases ITGA5:ITGB1 and
ITGAV:ITGB3 binding of the soluble form; decreases
activation of NF-kappa-B signaling)"
/evidence="ECO:0000269|PubMed:31331973"
/id="VAR_017934"
VARIANT 195
/note="L -> P (in HIGM1)"
/id="VAR_017935"
VARIANT 208
/note="A -> D (in HIGM1; decreases ITGA5:ITGB1 and
ITGAV:ITGB3 binding of the soluble form; decreases
activation of NF-kappa-B signaling)"
/evidence="ECO:0000269|PubMed:31331973"
/id="VAR_017936"
VARIANT 211
/note="T -> N (in HIGM1)"
/evidence="ECO:0000269|PubMed:7679801"
/id="VAR_007522"
VARIANT 219
/note="G -> R (in dbSNP:rs148594123)"
/evidence="ECO:0000269|PubMed:8550833"
/id="VAR_007523"
VARIANT 224
/note="H -> Y (in HIGM1; no effect on ITGA5:ITGB1 and
ITGAV:ITGB3 binding of the soluble form; increases NF-
kappa-B signaling)"
/evidence="ECO:0000269|PubMed:31331973"
/id="VAR_017937"
VARIANT 226
/note="G -> A (in HIGM1; no effect on ITGA5:ITGB1 and
ITGAV:ITGB3 binding of the soluble form; slightly increases
NF-kappa-B signaling)"
/evidence="ECO:0000269|PubMed:31331973"
/id="VAR_017938"
VARIANT 227
/note="G -> V (in HIGM1; decreases ITGA5:ITGB1 and
ITGAV:ITGB3 binding of the soluble form; decreases
activation of NF-kappa-B signaling; dbSNP:rs104894768)"
/evidence="ECO:0000269|PubMed:31331973,
ECO:0000269|PubMed:7679801, ECO:0000269|PubMed:8550833,
ECO:0000269|PubMed:9746782"
/id="VAR_007524"
VARIANT 227
/note="Missing (in HIGM1)"
/evidence="ECO:0000269|PubMed:9150729"
/id="VAR_007525"
VARIANT 231
/note="L -> S (in HIGM1)"
/evidence="ECO:0000269|PubMed:9150729,
ECO:0000269|PubMed:9746782"
/id="VAR_007526"
VARIANT 235
/note="A -> P (in HIGM1; dbSNP:rs104894771)"
/evidence="ECO:0000269|PubMed:7678782,
ECO:0000269|PubMed:9746782"
/id="VAR_007527"
VARIANT 237
/note="V -> E (in HIGM1)"
/evidence="ECO:0000269|PubMed:7532185"
/id="VAR_017939"
VARIANT 254
/note="T -> M (in HIGM1; dbSNP:rs193922136)"
/evidence="ECO:0000269|PubMed:9150729,
ECO:0000269|PubMed:9746782"
/id="VAR_007528"
VARIANT 257
/note="G -> D (in HIGM1; dbSNP:rs1477466218)"
/id="VAR_017940"
VARIANT 257
/note="G -> S (in HIGM1)"
/evidence="ECO:0000269|PubMed:8889581"
/id="VAR_017928"
VARIANT 258
/note="L -> S (in HIGM1; decreases ITGA5:ITGB1 and
ITGAV:ITGB3 binding of the soluble form; decreases
activation of NF-kappa-B signaling)"
/evidence="ECO:0000269|PubMed:31331973,
ECO:0000269|PubMed:9746782"
/id="VAR_017924"
MUTAGEN 170
/note="Y->E: Decreases ITGA5:ITGB1 binding, B-cell
activation, activation of NF-kappa-B signaling, and anti-
apoptotic signaling; in soluble form. Slightly decreases
CD40 binding; in soluble form."
/evidence="ECO:0000269|PubMed:31331973"
MUTAGEN 224
/note="H->E: Decreases ITGA5:ITGB1 binding, B-cell
activation, activation of NF-kappa-B signaling, and anti-
apoptotic signaling; when associated with E-226 in soluble
form. No effect on CD40 binding; when associated with E-226
in soluble form."
/evidence="ECO:0000269|PubMed:31331973"
MUTAGEN 226
/note="G->E: Decreases ITGA5:ITGB1 binding, B-cell
activation, activation of NF-kappa-B signaling, and anti-
apoptotic signaling; when associated with E-224 in soluble
form. No effect on CD40 binding; when associated with E-224
in soluble form."
/evidence="ECO:0000269|PubMed:31331973"
MUTAGEN 252
/note="G->E: Decreases ITGA5:ITGB1 binding, B-cell
activation, activation of NF-kappa-B signaling, and anti-
apoptotic signaling; in soluble form. No effect on CD40
binding; in soluble form."
/evidence="ECO:0000269|PubMed:31331973"
STRAND 123..128
/evidence="ECO:0000244|PDB:1ALY"
STRAND 132..134
/evidence="ECO:0000244|PDB:1ALY"
STRAND 135..137
/evidence="ECO:0000244|PDB:6BRB"
STRAND 140..142
/evidence="ECO:0000244|PDB:1ALY"
STRAND 153..156
/evidence="ECO:0000244|PDB:1ALY"
TURN 157..159
/evidence="ECO:0000244|PDB:1ALY"
STRAND 160..165
/evidence="ECO:0000244|PDB:1ALY"
STRAND 167..179
/evidence="ECO:0000244|PDB:1ALY"
TURN 181..183
/evidence="ECO:0000244|PDB:1ALY"
STRAND 186..195
/evidence="ECO:0000244|PDB:1ALY"
STRAND 203..211
/evidence="ECO:0000244|PDB:1ALY"
STRAND 218..232
/evidence="ECO:0000244|PDB:1ALY"
STRAND 237..242
/evidence="ECO:0000244|PDB:1ALY"
HELIX 244..246
/evidence="ECO:0000244|PDB:1ALY"
STRAND 251..260
/evidence="ECO:0000244|PDB:1ALY"
SEQUENCE 261 AA; 29274 MW; 16F5CEB093BCC2BB CRC64;
MIETYNQTSP RSAATGLPIS MKIFMYLLTV FLITQMIGSA LFAVYLHRRL DKIEDERNLH
EDFVFMKTIQ RCNTGERSLS LLNCEEIKSQ FEGFVKDIML NKEETKKENS FEMQKGDQNP
QIAAHVISEA SSKTTSVLQW AEKGYYTMSN NLVTLENGKQ LTVKRQGLYY IYAQVTFCSN
REASSQAPFI ASLCLKSPGR FERILLRAAN THSSAKPCGQ QSIHLGGVFE LQPGASVFVN
VTDPSQVSHG TGFTSFGLLK L


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