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Tumor necrosis factor ligand superfamily member 6 (Apoptosis antigen ligand) (APTL) (CD95 ligand) (CD95-L) (Fas antigen ligand) (Fas ligand) (FasL) (CD antigen CD178) [Cleaved into: Tumor necrosis factor ligand superfamily member 6, membrane form; Tumor necrosis factor ligand superfamily member 6, soluble form (Receptor-binding FasL ectodomain) (Soluble Fas ligand) (sFasL); ADAM10-processed FasL form (APL); FasL intracellular domain (FasL ICD) (SPPL2A-processed FasL form) (SPA)]

 TNFL6_HUMAN             Reviewed;         281 AA.
P48023; Q9BZP9;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
02-JUN-2021, entry version 221.
RecName: Full=Tumor necrosis factor ligand superfamily member 6;
AltName: Full=Apoptosis antigen ligand;
Short=APTL;
AltName: Full=CD95 ligand;
Short=CD95-L;
AltName: Full=Fas antigen ligand;
Short=Fas ligand;
Short=FasL;
AltName: CD_antigen=CD178;
Contains:
RecName: Full=Tumor necrosis factor ligand superfamily member 6, membrane form;
Contains:
RecName: Full=Tumor necrosis factor ligand superfamily member 6, soluble form;
AltName: Full=Receptor-binding FasL ectodomain;
AltName: Full=Soluble Fas ligand;
Short=sFasL;
Contains:
RecName: Full=ADAM10-processed FasL form;
Short=APL;
Contains:
RecName: Full=FasL intracellular domain;
Short=FasL ICD;
AltName: Full=SPPL2A-processed FasL form;
Short=SPA;
Name=FASLG; Synonyms=APT1LG1, CD95L, FASL, TNFSF6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=7528780; DOI=10.1084/jem.181.1.71;
Alderson M.;
"Fas ligand mediates activation-induced cell death in human T
lymphocytes.";
J. Exp. Med. 181:71-77(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7826947; DOI=10.1093/intimm/6.10.1567;
Takahashi T., Tanaka M., Inazawa J., Abe T., Suda T., Nagata S.;
"Human Fas ligand: gene structure, chromosomal location and species
specificity.";
Int. Immunol. 6:1567-1574(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Schaetzlein C.E., Poehlmann R., Philippsen P., Eibel H.;
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7980502; DOI=10.1006/bbrc.1994.2483;
Mita E., Hayashi N., Iio S., Takehara T., Hijioka T., Kasahara A.,
Fusamoto H., Kamada T.;
"Role of Fas ligand in apoptosis induced by hepatitis C virus infection.";
Biochem. Biophys. Res. Commun. 204:468-474(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Leukocyte;
Zeytun A., Nagarkatti M., Nagarkatti P.S.;
"Isolation and characterization of a new naturally occurring variant of
human Fas ligand that is expressed only in membrane bound form.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
TISSUE=Blood;
Matsumura M., Nakanishi Y., Ohba Y.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[9]
INVOLVEMENT IN ALPS1B.
PubMed=8787672; DOI=10.1172/jci118892;
Wu J., Wilson J., He J., Xiang L., Schur P.H., Mountz J.D.;
"Fas ligand mutation in a patient with systemic lupus erythematosus and
lymphoproliferative disease.";
J. Clin. Invest. 98:1107-1113(1996).
[10]
CHARACTERIZATION, AND MUTAGENESIS OF PRO-206; TYR-218 AND PHE-275.
PubMed=9228058; DOI=10.1074/jbc.272.30.18827;
Schneider P., Bodmer J.-L., Holler N., Mattmann C., Scuderi P.,
Terskikh A., Peitsch M.C., Tschopp J.;
"Characterization of Fas (Apo-1, CD95)-Fas ligand interaction.";
J. Biol. Chem. 272:18827-18833(1997).
[11]
PROTEOLYTIC PROCESSING, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9427603; DOI=10.1038/nm0198-031;
Tanaka M., Itai T., Adachi M., Nagata S.;
"Downregulation of Fas ligand by shedding.";
Nat. Med. 4:31-36(1998).
[12]
FUNCTION OF FASL INTRACELLULAR DOMAIN, CLEAVAGE BY ADAM10 AND SPPL2A, AND
SUBCELLULAR LOCATION.
PubMed=17557115; DOI=10.1038/sj.cdd.4402175;
Kirkin V., Cahuzac N., Guardiola-Serrano F., Huault S., Luckerath K.,
Friedmann E., Novac N., Wels W.S., Martoglio B., Hueber A.O., Zornig M.;
"The Fas ligand intracellular domain is released by ADAM10 and SPPL2a
cleavage in T-cells.";
Cell Death Differ. 14:1678-1687(2007).
[13]
UBIQUITINATION, PHOSPHORYLATION, INTERACTION WITH FGR; FYN AND LYN, AND
SUBCELLULAR LOCATION.
PubMed=17164290; DOI=10.1242/jcs.03315;
Zuccato E., Blott E.J., Holt O., Sigismund S., Shaw M., Bossi G.,
Griffiths G.M.;
"Sorting of Fas ligand to secretory lysosomes is regulated by mono-
ubiquitylation and phosphorylation.";
J. Cell Sci. 120:191-199(2007).
[14]
INTERACTION WITH ARHGAP9; BAIAP2L1; BTK; CACNB3; CACNB4; CRK; DLG2; DNMBP;
DOCK4; EPS8L3; FYB1; FYN; HCK; ITK; ITSN2; KALRN; LYN; MACC1; MIA; MPP4;
MYO15A; NCF1; NCK1; NCK2; NCKIPSD; OSTF1; PIK3R1; PSTPIP1; RIMBP3C; SAMSN1;
SH3GL3; SH3PXD2B; SH3PXD2A; SH3RF2; SKAP2; SNX33; SNX9; SORBS3; SPTA1; SRC;
SRGAP1; SRGAP2; SRGAP3; TEC; TJP3 AND YES1.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL (CD178) by
phage display screening.";
BMC Immunol. 10:53-53(2009).
[15]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 130-281 IN COMPLEX WITH TNFRSF6B,
FUNCTION, SUBUNIT, GLYCOSYLATION, AND DISULFIDE BOND.
PubMed=27806260; DOI=10.1016/j.str.2016.09.009;
Liu W., Ramagopal U., Cheng H., Bonanno J.B., Toro R., Bhosle R., Zhan C.,
Almo S.C.;
"Crystal structure of the complex of human FasL and its decoy receptor
DcR3.";
Structure 24:2016-2023(2016).
[16]
VARIANT ALPS1B SER-202, AND CHARACTERIZATION OF VARIANT ALPS1B SER-202.
PubMed=26334989; DOI=10.1038/pr.2015.170;
Ruiz-Garcia R., Mora S., Lozano-Sanchez G., Martinez-Lostao L.,
Paz-Artal E., Ruiz-Contreras J., Anel A., Gonzalez-Granado L.I.,
Moreno-Perez D., Allende L.M.;
"Decreased activation-induced cell death by EBV-transformed B-cells from a
patient with autoimmune lymphoproliferative syndrome caused by a novel
FASLG mutation.";
Pediatr. Res. 78:603-608(2015).
-!- FUNCTION: Cytokine that binds to TNFRSF6/FAS, a receptor that
transduces the apoptotic signal into cells (PubMed:26334989,
PubMed:9228058). Involved in cytotoxic T-cell-mediated apoptosis,
natural killer cell-mediated apoptosis and in T-cell development
(PubMed:9228058, PubMed:7528780, PubMed:9427603). Initiates
fratricidal/suicidal activation-induced cell death (AICD) in antigen-
activated T-cells contributing to the termination of immune responses
(By similarity). TNFRSF6/FAS-mediated apoptosis has also a role in the
induction of peripheral tolerance (By similarity). Binds to
TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis
(PubMed:27806260). {ECO:0000250|UniProtKB:P41047,
ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:27806260,
ECO:0000269|PubMed:7528780, ECO:0000269|PubMed:9228058,
ECO:0000269|PubMed:9427603}.
-!- FUNCTION: [Tumor necrosis factor ligand superfamily member 6, soluble
form]: Induces FAS-mediated activation of NF-kappa-B, initiating non-
apoptotic signaling pathways (By similarity). Can induce apoptosis but
does not appear to be essential for this process (PubMed:27806260).
{ECO:0000250|UniProtKB:P41047, ECO:0000269|PubMed:27806260}.
-!- FUNCTION: [FasL intracellular domain]: Cytoplasmic form induces gene
transcription inhibition. {ECO:0000269|PubMed:17557115}.
-!- SUBUNIT: Homotrimer (PubMed:27806260). Interacts with ARHGAP9,
BAIAP2L1, BTK, CACNB3, CACNB4, CRK, DLG2, DNMBP, DOCK4, EPS8L3, FGR,
FYB1, FYN, HCK, ITK, ITSN2, KALRN, LYN, MACC1, MIA, MPP4, MYO15A, NCF1,
NCK1, NCK2, NCKIPSD, OSTF1, PIK3R1, PSTPIP1, RIMBP3C, SAMSN1, SH3GL3,
SH3PXD2B, SH3PXD2A, SH3RF2, SKAP2, SNX33, SNX9, SORBS3, SPTA1, SRC,
SRGAP1, SRGAP2, SRGAP3, TEC, TJP3 and YES1.
{ECO:0000269|PubMed:17164290, ECO:0000269|PubMed:19807924,
ECO:0000269|PubMed:27806260, ECO:0000305}.
-!- INTERACTION:
P48023; Q14790: CASP8; NbExp=5; IntAct=EBI-495538, EBI-78060;
P48023; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-495538, EBI-3867333;
P48023; Q16610: ECM1; NbExp=3; IntAct=EBI-495538, EBI-947964;
P48023; Q13158: FADD; NbExp=4; IntAct=EBI-495538, EBI-494804;
P48023; P25445: FAS; NbExp=4; IntAct=EBI-495538, EBI-494743;
P48023; Q96RU3: FNBP1; NbExp=4; IntAct=EBI-495538, EBI-1111248;
P48023; P06241: FYN; NbExp=2; IntAct=EBI-495538, EBI-515315;
P48023; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-495538, EBI-8638439;
P48023; Q08881: ITK; NbExp=3; IntAct=EBI-495538, EBI-968552;
P48023; Q14525: KRT33B; NbExp=3; IntAct=EBI-495538, EBI-1049638;
P48023; Q6A162: KRT40; NbExp=3; IntAct=EBI-495538, EBI-10171697;
P48023; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-495538, EBI-1052037;
P48023; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-495538, EBI-11953334;
P48023; A0A0S2Z4D7: NCK1; NbExp=3; IntAct=EBI-495538, EBI-16429340;
P48023; P16333-1: NCK1; NbExp=4; IntAct=EBI-495538, EBI-15578122;
P48023; O43639: NCK2; NbExp=4; IntAct=EBI-495538, EBI-713635;
P48023; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-495538, EBI-945833;
P48023; Q9BY11: PACSIN1; NbExp=4; IntAct=EBI-495538, EBI-721769;
P48023; Q9UNF0: PACSIN2; NbExp=4; IntAct=EBI-495538, EBI-742503;
P48023; Q9UKS6: PACSIN3; NbExp=4; IntAct=EBI-495538, EBI-77926;
P48023; P27986: PIK3R1; NbExp=2; IntAct=EBI-495538, EBI-79464;
P48023; O43586: PSTPIP1; NbExp=5; IntAct=EBI-495538, EBI-1050964;
P48023; O76081: RGS20; NbExp=3; IntAct=EBI-495538, EBI-1052678;
P48023; O76081-6: RGS20; NbExp=6; IntAct=EBI-495538, EBI-10178530;
P48023; Q15436: SEC23A; NbExp=3; IntAct=EBI-495538, EBI-81088;
P48023; Q8WV41: SNX33; NbExp=3; IntAct=EBI-495538, EBI-2481535;
P48023; Q9Y5X1: SNX9; NbExp=2; IntAct=EBI-495538, EBI-77848;
P48023; O75044: SRGAP2; NbExp=2; IntAct=EBI-495538, EBI-1051034;
P48023; Q63HR2: TNS2; NbExp=3; IntAct=EBI-495538, EBI-949753;
P48023; Q15642: TRIP10; NbExp=4; IntAct=EBI-495538, EBI-739936;
P48023; Q15654: TRIP6; NbExp=3; IntAct=EBI-495538, EBI-742327;
P48023; Q9DBG3: Ap2b1; Xeno; NbExp=2; IntAct=EBI-495538, EBI-775229;
P48023; Q91ZR2: Snx18; Xeno; NbExp=4; IntAct=EBI-495538, EBI-6879954;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17557115,
ECO:0000269|PubMed:9427603}; Single-pass type II membrane protein
{ECO:0000255}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:17164290}.
Lysosome lumen {ECO:0000269|PubMed:17164290}. Note=Is internalized into
multivesicular bodies of secretory lysosomes after phosphorylation by
FGR and monoubiquitination (PubMed:17164290). Colocalizes with the
SPPL2A protease at the cell membrane (PubMed:17557115).
{ECO:0000269|PubMed:17164290, ECO:0000269|PubMed:17557115}.
-!- SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member
6, soluble form]: Secreted {ECO:0000269|PubMed:9427603}. Note=May be
released into the extracellular fluid by cleavage from the cell
surface. {ECO:0000269|PubMed:9427603}.
-!- SUBCELLULAR LOCATION: [FasL intracellular domain]: Nucleus
{ECO:0000269|PubMed:17557115}. Note=The FasL ICD cytoplasmic form is
translocated into the nucleus. {ECO:0000269|PubMed:17557115}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P48023-1; Sequence=Displayed;
Name=2;
IsoId=P48023-2; Sequence=VSP_006443, VSP_006444;
-!- PTM: The soluble form derives from the membrane form by proteolytic
processing. The membrane-bound form undergoes two successive
intramembrane proteolytic cleavages. The first one is processed by
ADAM10 producing an N-terminal fragment, which lacks the receptor-
binding extracellular domain. This ADAM10-processed FasL (FasL APL)
remnant form is still membrane anchored and further processed by SPPL2A
that liberates the FasL intracellular domain (FasL ICD). FasL shedding
by ADAM10 is a prerequisite for subsequent intramembrane cleavage by
SPPL2A in T-cells. {ECO:0000269|PubMed:17557115,
ECO:0000269|PubMed:9427603}.
-!- PTM: N-glycosylated (PubMed:9228058). Glycosylation enhances apoptotic
activity (PubMed:27806260). {ECO:0000269|PubMed:27806260,
ECO:0000269|PubMed:9228058}.
-!- PTM: Phosphorylated by FGR on tyrosine residues; this is required for
ubiquitination and subsequent internalization.
{ECO:0000269|PubMed:17164290}.
-!- PTM: Monoubiquitinated. {ECO:0000269|PubMed:17164290}.
-!- DISEASE: Autoimmune lymphoproliferative syndrome 1B (ALPS1B)
[MIM:601859]: A disorder of apoptosis that manifests in early childhood
and results in the accumulation of autoreactive lymphocytes. It is
characterized by non-malignant lymphadenopathy with hepatosplenomegaly,
and autoimmune hemolytic anemia, thrombocytopenia and neutropenia.
{ECO:0000269|PubMed:26334989, ECO:0000269|PubMed:8787672}. Note=The
disease is caused by variants affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
-!- WEB RESOURCE: Name=FASLGbase; Note=FASLG mutation db;
URL="http://structure.bmc.lu.se/idbase/FASLGbase/";
-!- WEB RESOURCE: Name=Wikipedia; Note=FAS-ligand entry;
URL="https://en.wikipedia.org/wiki/FAS_ligand";
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EMBL; U08137; AAC50071.1; -; mRNA.
EMBL; U11821; AAC50124.1; -; mRNA.
EMBL; X89102; CAA61474.1; -; mRNA.
EMBL; D38122; BAA07320.1; -; mRNA.
EMBL; AF288573; AAG60017.1; -; mRNA.
EMBL; Z96050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017502; AAH17502.1; -; mRNA.
EMBL; AB013303; BAA32542.1; -; Genomic_DNA.
CCDS; CCDS1304.1; -. [P48023-1]
CCDS; CCDS76243.1; -. [P48023-2]
PIR; I38707; I38707.
RefSeq; NP_000630.1; NM_000639.2. [P48023-1]
RefSeq; NP_001289675.1; NM_001302746.1. [P48023-2]
PDB; 1BZI; Model; -; B/C=1-281.
PDB; 4MSV; X-ray; 2.50 A; A=130-281.
PDB; 5L19; X-ray; 2.00 A; A=130-281.
PDB; 5L36; X-ray; 3.10 A; A=130-281.
PDBsum; 1BZI; -.
PDBsum; 4MSV; -.
PDBsum; 5L19; -.
PDBsum; 5L36; -.
SMR; P48023; -.
BioGRID; 106852; 91.
DIP; DIP-2997N; -.
ELM; P48023; -.
IntAct; P48023; 83.
MINT; P48023; -.
STRING; 9606.ENSP00000356694; -.
ChEMBL; CHEMBL5714; -.
GlyGen; P48023; 3 sites.
iPTMnet; P48023; -.
PhosphoSitePlus; P48023; -.
SwissPalm; P48023; -.
BioMuta; FASLG; -.
DMDM; 1345957; -.
MassIVE; P48023; -.
PaxDb; P48023; -.
PeptideAtlas; P48023; -.
PRIDE; P48023; -.
ProteomicsDB; 55831; -. [P48023-1]
ProteomicsDB; 55832; -. [P48023-2]
ABCD; P48023; 4 sequenced antibodies.
Antibodypedia; 4418; 1340 antibodies.
DNASU; 356; -.
Ensembl; ENST00000340030; ENSP00000344739; ENSG00000117560. [P48023-2]
Ensembl; ENST00000367721; ENSP00000356694; ENSG00000117560. [P48023-1]
GeneID; 356; -.
KEGG; hsa:356; -.
UCSC; uc001git.4; human. [P48023-1]
CTD; 356; -.
DisGeNET; 356; -.
GeneCards; FASLG; -.
GeneReviews; FASLG; -.
HGNC; HGNC:11936; FASLG.
HPA; ENSG00000117560; Tissue enhanced (blood, lymphoid tissue).
MalaCards; FASLG; -.
MIM; 134638; gene.
MIM; 601859; phenotype.
neXtProt; NX_P48023; -.
OpenTargets; ENSG00000117560; -.
Orphanet; 3261; Autoimmune lymphoproliferative syndrome.
PharmGKB; PA56; -.
VEuPathDB; HostDB:ENSG00000117560.7; -.
eggNOG; ENOG502S09I; Eukaryota.
GeneTree; ENSGT01030000234737; -.
HOGENOM; CLU_070352_2_0_1; -.
InParanoid; P48023; -.
OMA; PQIFWVD; -.
PhylomeDB; P48023; -.
TreeFam; TF332169; -.
PathwayCommons; P48023; -.
Reactome; R-HSA-140534; Caspase activation via Death Receptors in the presence of ligand.
Reactome; R-HSA-3371378; Regulation by c-FLIP.
Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-HSA-5218900; CASP8 activity is inhibited.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-69416; Dimerization of procaspase-8.
Reactome; R-HSA-75157; FasL/ CD95L signaling.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
Reactome; R-HSA-9614657; FOXO-mediated transcription of cell death genes.
SIGNOR; P48023; -.
BioGRID-ORCS; 356; 6 hits in 990 CRISPR screens.
ChiTaRS; FASLG; human.
GeneWiki; Fas_ligand; -.
GenomeRNAi; 356; -.
Pharos; P48023; Tbio.
PRO; PR:P48023; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; P48023; protein.
Bgee; ENSG00000117560; Expressed in granulocyte and 83 other tissues.
ExpressionAtlas; P48023; baseline and differential.
Genevisible; P48023; HS.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:AgBase.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0005123; F:death receptor binding; IEA:Ensembl.
GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:BHF-UCL.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0030644; P:cellular chloride ion homeostasis; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0048388; P:endosomal lumen acidification; IEA:Ensembl.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
GO; GO:0006925; P:inflammatory cell apoptotic process; IEA:Ensembl.
GO; GO:0070266; P:necroptotic process; IDA:BHF-UCL.
GO; GO:0097527; P:necroptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:BHF-UCL.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:1905782; P:positive regulation of phosphatidylserine exposure on apoptotic cell surface; IDA:UniProtKB.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:1903514; P:release of sequestered calcium ion into cytosol by endoplasmic reticulum; IDA:MGI.
GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0046666; P:retinal cell programmed cell death; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0070231; P:T cell apoptotic process; IDA:UniProtKB.
CDD; cd00184; TNF; 1.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR028326; FASL.
InterPro; IPR006053; TNF.
InterPro; IPR021184; TNF_CS.
InterPro; IPR006052; TNF_dom.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
Pfam; PF00229; TNF; 1.
PRINTS; PR01681; FASLIGAND.
PRINTS; PR01234; TNECROSISFCT.
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; Alternative splicing; Apoptosis; Cell membrane; Cytokine;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Lysosome; Membrane;
Nucleus; Reference proteome; Repressor; Secreted; Signal-anchor;
Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1..281
/note="Tumor necrosis factor ligand superfamily member 6,
membrane form"
/id="PRO_0000034500"
CHAIN 1..129
/note="ADAM10-processed FasL form"
/id="PRO_0000417152"
CHAIN 1..81
/note="FasL intracellular domain"
/id="PRO_0000416842"
CHAIN 130..281
/note="Tumor necrosis factor ligand superfamily member 6,
soluble form"
/id="PRO_0000034501"
TOPO_DOM 1..80
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 81..102
/note="Helical; Signal-anchor for type II membrane protein"
/evidence="ECO:0000255"
TOPO_DOM 103..281
/note="Extracellular"
/evidence="ECO:0000255"
REGION 20..71
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 118..142
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 26..71
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
SITE 81..82
/note="Cleavage; by SPPL2A"
/evidence="ECO:0000305"
SITE 129..130
/note="Cleavage; by ADAM10"
/evidence="ECO:0000305"
CARBOHYD 184
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 250
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 260
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 202..233
/evidence="ECO:0000269|PubMed:27806260,
ECO:0007744|PDB:4MSV, ECO:0007744|PDB:5L19"
VAR_SEQ 117..127
/note="STSQMHTASSL -> ATPVHPLKKRS (in isoform 2)"
/evidence="ECO:0000303|Ref.5"
/id="VSP_006443"
VAR_SEQ 128..281
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|Ref.5"
/id="VSP_006444"
VARIANT 189
/note="Y -> S (in dbSNP:rs12079514)"
/id="VAR_052583"
VARIANT 202
/note="C -> S (in ALPS1B; significant reduction in
cytotoxicity and apoptosis and inhibition of the shedding
of the soluble form)"
/evidence="ECO:0000269|PubMed:26334989"
/id="VAR_075568"
MUTAGEN 206
/note="P->D,F,R: Lowers binding to TNFRSF6 and reduces
cytotoxicity more than 100-fold."
/evidence="ECO:0000269|PubMed:9228058"
MUTAGEN 218
/note="Y->F,R: Lowers binding to TNFRSF6 and abolishes
cytotoxicity."
/evidence="ECO:0000269|PubMed:9228058"
MUTAGEN 275
/note="F->L: Abolishes binding to TNRFSF6 and
cytotoxicity."
/evidence="ECO:0000269|PubMed:9228058"
HELIX 137..142
/evidence="ECO:0007829|PDB:5L19"
STRAND 146..151
/evidence="ECO:0007829|PDB:5L19"
STRAND 157..159
/evidence="ECO:0007829|PDB:4MSV"
STRAND 165..168
/evidence="ECO:0007829|PDB:4MSV"
STRAND 170..177
/evidence="ECO:0007829|PDB:5L19"
STRAND 180..182
/evidence="ECO:0007829|PDB:5L19"
STRAND 187..201
/evidence="ECO:0007829|PDB:5L19"
STRAND 207..214
/evidence="ECO:0007829|PDB:5L19"
STRAND 218..220
/evidence="ECO:0007829|PDB:4MSV"
STRAND 222..229
/evidence="ECO:0007829|PDB:5L19"
STRAND 239..251
/evidence="ECO:0007829|PDB:5L19"
STRAND 256..262
/evidence="ECO:0007829|PDB:5L19"
HELIX 264..266
/evidence="ECO:0007829|PDB:5L19"
TURN 271..273
/evidence="ECO:0007829|PDB:5L19"
STRAND 274..280
/evidence="ECO:0007829|PDB:5L19"
SEQUENCE 281 AA; 31485 MW; A8A6EB358246E9BB CRC64;
MQQPFNYPYP QIYWVDSSAS SPWAPPGTVL PCPTSVPRRP GQRRPPPPPP PPPLPPPPPP
PPLPPLPLPP LKKRGNHSTG LCLLVMFFMV LVALVGLGLG MFQLFHLQKE LAELRESTSQ
MHTASSLEKQ IGHPSPPPEK KELRKVAHLT GKSNSRSMPL EWEDTYGIVL LSGVKYKKGG
LVINETGLYF VYSKVYFRGQ SCNNLPLSHK VYMRNSKYPQ DLVMMEGKMM SYCTTGQMWA
RSSYLGAVFN LTSADHLYVN VSELSLVNFE ESQTFFGLYK L


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WP2355: Corticotropin-releasing hormone
WP1825: GPCR ligand binding
WP247: Small Ligand GPCRs
WP161: Small Ligand GPCRs
WP853: Small Ligand GPCRs
WP1317: Small Ligand GPCRs
WP353: Small Ligand GPCRs
WP971: Small Ligand GPCRs
WP746: Small Ligand GPCRs
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WP1772: Apoptosis Modulation and Signaling
WP1254: Apoptosis
WP571: FAS pathway and Stress induction of HSP regulation
WP1834: Interactions of the immunoglobulin superfamily (IgSF) member proteins
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WP1046: Signaling of Hepatocyte Growth Factor Receptor
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Related Genes :
[Faslg Apt1Lg1 Cd95l Fasl Tnfsf6] Tumor necrosis factor ligand superfamily member 6 (CD95 ligand) (CD95-L) (Fas antigen ligand) (Fas ligand) (FasL) (CD antigen CD178) [Cleaved into: Tumor necrosis factor ligand superfamily member 6, membrane form; Tumor necrosis factor ligand superfamily member 6, soluble form (Receptor-binding FasL ectodomain) (Soluble Fas ligand) (sFasL); ADAM10-processed FasL form (APL); FasL intracellular domain (FasL ICD) (SPPL2A-processed FasL form) (SPA)]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[Fas Apt1 Tnfrsf6] Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95)
[FAS APT1 FAS1 TNFRSF6] Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95)
[Fas Apt1 Tnfrsf6] Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95)
[Tnf Tnfa Tnfsf2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[Tnfsf11 Opgl Rankl Trance] Tumor necrosis factor ligand superfamily member 11 (Osteoclast differentiation factor) (ODF) (Osteoprotegerin ligand) (OPGL) (Receptor activator of nuclear factor kappa-B ligand) (RANKL) (TNF-related activation-induced cytokine) (TRANCE) (CD antigen CD254) [Cleaved into: Tumor necrosis factor ligand superfamily member 11, membrane form; Tumor necrosis factor ligand superfamily member 11, soluble form]
[Tnf Tnfa Tnfsf2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[CD40LG CD40L TNFSF5 TRAP] 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)]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNFSF11 OPGL RANKL TRANCE] Tumor necrosis factor ligand superfamily member 11 (Osteoclast differentiation factor) (ODF) (Osteoprotegerin ligand) (OPGL) (Receptor activator of nuclear factor kappa-B ligand) (RANKL) (TNF-related activation-induced cytokine) (TRANCE) (CD antigen CD254) [Cleaved into: Tumor necrosis factor ligand superfamily member 11, membrane form; Tumor necrosis factor ligand superfamily member 11, soluble form]
[TNFSF13B BAFF BLYS TALL1 TNFSF20 ZTNF4 UNQ401/PRO738] Tumor necrosis factor ligand superfamily member 13B (B lymphocyte stimulator) (BLyS) (B-cell-activating factor) (BAFF) (Dendritic cell-derived TNF-like molecule) (TNF- and APOL-related leukocyte expressed ligand 1) (TALL-1) (CD antigen CD257) [Cleaved into: Tumor necrosis factor ligand superfamily member 13b, membrane form; Tumor necrosis factor ligand superfamily member 13b, soluble form]
[TNFSF14 HVEML LIGHT UNQ391/PRO726] Tumor necrosis factor ligand superfamily member 14 (Herpes virus entry mediator ligand) (HVEM-L) (Herpesvirus entry mediator ligand) (CD antigen CD258) [Cleaved into: Tumor necrosis factor ligand superfamily member 14, membrane form; Tumor necrosis factor ligand superfamily member 14, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]

Bibliography :