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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)]

 TNFL6_MACFA             Reviewed;         280 AA.
P63308; Q9BDM5; Q9MYL6;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
12-SEP-2018, entry version 79.
RecName: Full=Tumor necrosis factor ligand superfamily member 6;
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=CD95L, FASL, TNFSF6;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12957408; DOI=10.1016/S0022-1759(03)00187-X;
Kirii Y., Inoue T., Yoshino K., Kayagaki N., Yagita H., Okumura K.,
Shibata H., Yoshikawa Y., Terao K.;
"Molecular cloning, functional characterization, and enzyme-linked
immunosorbent assay of cynomolgus monkey Fas ligand.";
J. Immunol. Methods 278:201-209(2003).
-!- FUNCTION: Cytokine that binds to TNFRSF6/FAS, a receptor that
transduces the apoptotic signal into cells. Involved in cytotoxic
T-cell-mediated apoptosis, natural killer cell-mediated apoptosis
and in T-cell development. Initiates fratricidal/suicidal
activation-induced cell death (AICD) in antigen-activated T-cells
contributing to the termination of immune responses. TNFRSF6/FAS-
mediated apoptosis has also a role in the induction of peripheral
tolerance. Binds to TNFRSF6B/DcR3, a decoy receptor that blocks
apoptosis. {ECO:0000250|UniProtKB:P41047,
ECO:0000250|UniProtKB:P48023}.
-!- FUNCTION: Tumor necrosis factor ligand superfamily member 6,
soluble form: Induces FAS-mediated activation of NF-kappa-B,
initiating non-apoptotic signaling pathways. Can induce apoptosis
but does not appear to be essential for this process.
{ECO:0000250|UniProtKB:P41047}.
-!- FUNCTION: FasL intracellular domain: Cytoplasmic form induces gene
transcription inhibition. {ECO:0000250|UniProtKB:P48023}.
-!- SUBUNIT: Homotrimer. 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:0000250|UniProtKB:P48023}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P48023}; Single-pass type II membrane
protein {ECO:0000255}. Cytoplasmic vesicle lumen
{ECO:0000250|UniProtKB:P48023}. Lysosome lumen
{ECO:0000250|UniProtKB:P48023}. Note=Colocalizes with the SPPL2A
protease at the cell membrane. Is internalized into multivesicular
bodies of secretory lysosomes after phosphorylation by FGR and
monoubiquitination. {ECO:0000250|UniProtKB:P48023}.
-!- SUBCELLULAR LOCATION: Tumor necrosis factor ligand superfamily
member 6, soluble form: Secreted {ECO:0000250|UniProtKB:P48023}.
Note=May be released into the extracellular fluid by cleavage from
the cell surface. {ECO:0000250|UniProtKB:P48023}.
-!- SUBCELLULAR LOCATION: FasL intracellular domain: Nucleus
{ECO:0000250|UniProtKB:P48023}. Note=The FasL ICD cytoplasmic form
is translocated into the nucleus. {ECO:0000250|UniProtKB:P48023}.
-!- 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:0000250|UniProtKB:P48023}.
-!- PTM: Phosphorylated by FGR on tyrosine residues; this is required
for ubiquitination and subsequent internalization.
{ECO:0000250|UniProtKB:P48023}.
-!- PTM: N-glycosylated. Glycosylation enhances apoptotic activity.
{ECO:0000250|UniProtKB:P48023}.
-!- PTM: Monoubiquitinated. {ECO:0000250|UniProtKB:P48023}.
-!- SIMILARITY: Belongs to the tumor necrosis factor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB035138; BAA90294.1; -; mRNA.
RefSeq; NP_001271479.1; NM_001284550.1.
UniGene; Mfa.6266; -.
ProteinModelPortal; P63308; -.
SMR; P63308; -.
Ensembl; ENSMFAT00000018217; ENSMFAP00000043926; ENSMFAG00000039338.
GeneID; 102139406; -.
KEGG; mcf:102139406; -.
CTD; 356; -.
GeneTree; ENSGT00530000062992; -.
HOVERGEN; HBG055128; -.
KO; K04389; -.
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; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:AgBase.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0097527; P:necroptotic signaling pathway; IEA:Ensembl.
GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:1903514; P:release of sequestered calcium ion into cytosol by endoplasmic reticulum; IEA:Ensembl.
GO; GO:0046666; P:retinal cell programmed cell death; IEA:Ensembl.
GO; GO:0070231; P:T cell apoptotic process; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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.
2: Evidence at transcript level;
Apoptosis; Cell membrane; Cytokine; Cytoplasmic vesicle;
Disulfide bond; Glycoprotein; Lysosome; Membrane; Nucleus; Repressor;
Secreted; Signal-anchor; Transcription; Transcription regulation;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 280 Tumor necrosis factor ligand superfamily
member 6, membrane form.
/FTId=PRO_0000034502.
CHAIN 1 128 ADAM10-processed FasL form.
{ECO:0000250}.
/FTId=PRO_0000417153.
CHAIN 1 81 FasL intracellular domain. {ECO:0000250}.
/FTId=PRO_0000417154.
CHAIN 129 280 Tumor necrosis factor ligand superfamily
member 6, soluble form. {ECO:0000250}.
/FTId=PRO_0000034503.
TOPO_DOM 1 80 Cytoplasmic. {ECO:0000255}.
TRANSMEM 81 101 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 102 280 Extracellular. {ECO:0000255}.
COMPBIAS 4 69 Pro-rich.
COMPBIAS 45 64 Poly-Pro.
SITE 80 81 Cleavage; by SPPL2A. {ECO:0000250}.
SITE 128 129 Cleavage; by ADAM10. {ECO:0000250}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 259 259 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 201 232 {ECO:0000250|UniProtKB:P48023}.
SEQUENCE 280 AA; 31368 MW; F0B284D61A132EB4 CRC64;
MQQPFNYPYP QIYWVDSSAS SPWAPPGTVL PCPTSVPRRP GQRRPPPPPP PPPLPPPPPS
PLPPLPLPPL KKRGNHSTGL CLLVMFFMVL VALVGLGLGM FQLFHLQKEL AELRESTSQK
HTASSLEKQI GHPSPPPEKK EQRKVAHLTG KPNSRSMPLE WEDTYGIVLL SGVKYKKGGL
VINETGLYFV YSKVYFRGQS CTNLPLSHKV YMRNSKYPQD LVMMEGKMMS YCTTGQMWAH
SSYLGAVFNL TSADHLYVNV SELSLVNFEE SQTFFGLYKL


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