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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.
27-SEP-2017, entry version 193.
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:
Q9DBG3:Ap2b1 (xeno); NbExp=2; IntAct=EBI-495538, EBI-775229;
Q14790:CASP8; NbExp=4; IntAct=EBI-495538, EBI-78060;
Q8IYA8:CCDC36; NbExp=4; IntAct=EBI-495538, EBI-8638439;
Q13158:FADD; NbExp=3; IntAct=EBI-495538, EBI-494804;
P25445:FAS; NbExp=4; IntAct=EBI-495538, EBI-494743;
Q96RU3:FNBP1; NbExp=4; IntAct=EBI-495538, EBI-1111248;
P06241:FYN; NbExp=2; IntAct=EBI-495538, EBI-515315;
Q08881:ITK; NbExp=3; IntAct=EBI-495538, EBI-968552;
Q6A162:KRT40; NbExp=3; IntAct=EBI-495538, EBI-10171697;
O43639:NCK2; NbExp=3; IntAct=EBI-495538, EBI-713635;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-495538, EBI-945833;
Q9BY11:PACSIN1; NbExp=4; IntAct=EBI-495538, EBI-721769;
Q9UNF0:PACSIN2; NbExp=4; IntAct=EBI-495538, EBI-742503;
Q9UKS6:PACSIN3; NbExp=4; IntAct=EBI-495538, EBI-77926;
P27986:PIK3R1; NbExp=2; IntAct=EBI-495538, EBI-79464;
O43586:PSTPIP1; NbExp=5; IntAct=EBI-495538, EBI-1050964;
O76081:RGS20; NbExp=3; IntAct=EBI-495538, EBI-1052678;
O76081-6:RGS20; NbExp=5; IntAct=EBI-495538, EBI-10178530;
Q91ZR2:Snx18 (xeno); NbExp=4; IntAct=EBI-495538, EBI-6879954;
Q8WV41:SNX33; NbExp=2; IntAct=EBI-495538, EBI-2481535;
Q9Y5X1:SNX9; NbExp=2; IntAct=EBI-495538, EBI-77848;
O75044:SRGAP2; NbExp=2; IntAct=EBI-495538, EBI-1051034;
Q15642:TRIP10; NbExp=4; IntAct=EBI-495538, EBI-739936;
Q15654:TRIP6; NbExp=3; IntAct=EBI-495538, EBI-742327;
-!- 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
mutations 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]
UniGene; Hs.2007; -.
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; -.
ProteinModelPortal; P48023; -.
SMR; P48023; -.
BioGrid; 106852; 83.
DIP; DIP-2997N; -.
ELM; P48023; -.
IntAct; P48023; 78.
MINT; MINT-238167; -.
STRING; 9606.ENSP00000356694; -.
ChEMBL; CHEMBL5714; -.
iPTMnet; P48023; -.
PhosphoSitePlus; P48023; -.
SwissPalm; P48023; -.
BioMuta; FASLG; -.
DMDM; 1345957; -.
PaxDb; P48023; -.
PeptideAtlas; P48023; -.
PRIDE; P48023; -.
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; -.
EuPathDB; HostDB:ENSG00000117560.7; -.
GeneCards; FASLG; -.
GeneReviews; FASLG; -.
HGNC; HGNC:11936; FASLG.
HPA; HPA054959; -.
MalaCards; FASLG; -.
MIM; 134638; gene.
MIM; 601859; phenotype.
neXtProt; NX_P48023; -.
OpenTargets; ENSG00000117560; -.
Orphanet; 3261; Autoimmune lymphoproliferative syndrome.
PharmGKB; PA56; -.
eggNOG; ENOG410IHZF; Eukaryota.
eggNOG; ENOG4112D9R; LUCA.
GeneTree; ENSGT00530000062992; -.
HOGENOM; HOG000290680; -.
HOVERGEN; HBG055128; -.
InParanoid; P48023; -.
KO; K04389; -.
OMA; WEDTYGI; -.
OrthoDB; EOG091G0MFC; -.
PhylomeDB; P48023; -.
TreeFam; TF332169; -.
Reactome; R-HSA-140534; Ligand-dependent caspase activation.
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 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.
SIGNOR; P48023; -.
GeneWiki; Fas_ligand; -.
GenomeRNAi; 356; -.
PMAP-CutDB; P48023; -.
PRO; PR:P48023; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117560; -.
CleanEx; HS_FASLG; -.
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: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:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; TAS:Reactome.
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: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:0006955; P:immune response; IEA:InterPro.
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 from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell 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: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.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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;
Complete proteome; Cytokine; Cytoplasmic vesicle; Disulfide bond;
Glycoprotein; Lysosome; Membrane; Nucleus; Polymorphism;
Reference proteome; Repressor; Secreted; Signal-anchor; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1 281 Tumor necrosis factor ligand superfamily
member 6, membrane form.
/FTId=PRO_0000034500.
CHAIN 1 129 ADAM10-processed FasL form.
/FTId=PRO_0000417152.
CHAIN 1 81 FasL intracellular domain.
/FTId=PRO_0000416842.
CHAIN 130 281 Tumor necrosis factor ligand superfamily
member 6, soluble form.
/FTId=PRO_0000034501.
TOPO_DOM 1 80 Cytoplasmic. {ECO:0000255}.
TRANSMEM 81 102 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 103 281 Extracellular. {ECO:0000255}.
COMPBIAS 4 70 Pro-rich.
COMPBIAS 45 65 Poly-Pro.
SITE 81 82 Cleavage; by SPPL2A. {ECO:0000305}.
SITE 129 130 Cleavage; by ADAM10. {ECO:0000305}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 202 233 {ECO:0000244|PDB:4MSV,
ECO:0000244|PDB:5L19,
ECO:0000269|PubMed:27806260}.
VAR_SEQ 117 127 STSQMHTASSL -> ATPVHPLKKRS (in isoform
2). {ECO:0000303|Ref.5}.
/FTId=VSP_006443.
VAR_SEQ 128 281 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_006444.
VARIANT 189 189 Y -> S (in dbSNP:rs12079514).
/FTId=VAR_052583.
VARIANT 202 202 C -> S (in ALPS1B; significant reduction
in cytotoxicity and apoptosis and
inhibition of the shedding of the soluble
form). {ECO:0000269|PubMed:26334989}.
/FTId=VAR_075568.
MUTAGEN 206 206 P->D,F,R: Lowers binding to TNFRSF6 and
reduces cytotoxicity more than 100-fold.
{ECO:0000269|PubMed:9228058}.
MUTAGEN 218 218 Y->F,R: Lowers binding to TNFRSF6 and
abolishes cytotoxicity.
{ECO:0000269|PubMed:9228058}.
MUTAGEN 275 275 F->L: Abolishes binding to TNRFSF6 and
cytotoxicity.
{ECO:0000269|PubMed:9228058}.
HELIX 137 142 {ECO:0000244|PDB:5L19}.
STRAND 146 151 {ECO:0000244|PDB:5L19}.
STRAND 157 159 {ECO:0000244|PDB:4MSV}.
STRAND 165 168 {ECO:0000244|PDB:4MSV}.
STRAND 170 177 {ECO:0000244|PDB:5L19}.
STRAND 180 182 {ECO:0000244|PDB:5L19}.
STRAND 187 201 {ECO:0000244|PDB:5L19}.
STRAND 207 214 {ECO:0000244|PDB:5L19}.
STRAND 218 220 {ECO:0000244|PDB:4MSV}.
STRAND 222 229 {ECO:0000244|PDB:5L19}.
STRAND 239 251 {ECO:0000244|PDB:5L19}.
STRAND 256 262 {ECO:0000244|PDB:5L19}.
HELIX 264 266 {ECO:0000244|PDB:5L19}.
TURN 271 273 {ECO:0000244|PDB:5L19}.
STRAND 274 280 {ECO:0000244|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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