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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_PIG               Reviewed;         282 AA.
Q9BEA8; Q95M04; Q95N10;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 103.
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;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=11429161; DOI=10.1089/107999001300177493;
Muneta Y., Shimoji Y., Inumaru S., Mori Y.;
"Molecular cloning, characterization, and expression of porcine Fas
ligand (CD95 ligand).";
J. Interferon Cytokine Res. 21:305-312(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Landrace X Large Yorkshire white; TISSUE=Thymocyte;
PubMed=11792426; DOI=10.1016/S0161-5890(01)00098-0;
Motegi-Ishiyama Y., Nakajima Y., Hoka S., Takagaki Y.;
"Porcine Fas-ligand gene: genomic sequence analysis and comparison
with human gene.";
Mol. Immunol. 38:581-586(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Lymphoid tissue;
PubMed=12371937; DOI=10.1034/j.1399-3089.2002.01114.x;
Tsuyuki S., Kono M., Bloom E.T.;
"Cloning and potential utility of porcine Fas ligand: overexpression
in porcine endothelial cells protects them from attack by human
cytolytic cells.";
Xenotransplantation 9:410-421(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Guanxi bama miniature pig;
Zhu N., Young Y.;
"Molecular cloning and characterization of porcine Fas ligand cDNA.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Cytokine that binds to TNFRSF6/FAS, a receptor that
transduces the apoptotic signal into cells (PubMed:11429161,
PubMed:12371937). Involved in cytotoxic T-cell-mediated apoptosis,
natural killer cell-mediated apoptosis and in T-cell development
(PubMed:11429161, PubMed:12371937). 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 (By
similarity). {ECO:0000250|UniProtKB:P41047,
ECO:0000250|UniProtKB:P48023, ECO:0000269|PubMed:11429161,
ECO:0000269|PubMed:12371937}.
-!- 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:0000269|PubMed:11429161}.
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}.
-!- INDUCTION: By IL-18. {ECO:0000269|PubMed:11429161}.
-!- 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; AB027297; BAB40919.1; -; mRNA.
EMBL; AB069764; BAB64291.1; -; Genomic_DNA.
EMBL; AF397407; AAK84408.1; -; mRNA.
EMBL; AY033634; AAK56449.1; -; mRNA.
RefSeq; NP_998971.1; NM_213806.1.
UniGene; Ssc.15870; -.
ProteinModelPortal; Q9BEA8; -.
SMR; Q9BEA8; -.
STRING; 9823.ENSSSCP00000019767; -.
PaxDb; Q9BEA8; -.
PRIDE; Q9BEA8; -.
GeneID; 396726; -.
KEGG; ssc:396726; -.
CTD; 356; -.
eggNOG; ENOG410IHZF; Eukaryota.
eggNOG; ENOG4112D9R; LUCA.
HOVERGEN; HBG055128; -.
InParanoid; Q9BEA8; -.
KO; K04389; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
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; IEA:UniProtKB-SubCell.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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; Complete proteome; Cytokine;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Lysosome; Membrane;
Nucleus; Reference proteome; Repressor; Secreted; Signal-anchor;
Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 282 Tumor necrosis factor ligand superfamily
member 6, membrane form.
/FTId=PRO_0000034510.
CHAIN 1 130 ADAM10-processed FasL form.
{ECO:0000250}.
/FTId=PRO_0000417161.
CHAIN 1 83 FasL intracellular domain. {ECO:0000250}.
/FTId=PRO_0000417162.
CHAIN 131 282 Tumor necrosis factor ligand superfamily
member 6, soluble form. {ECO:0000250}.
/FTId=PRO_0000034511.
TOPO_DOM 1 82 Cytoplasmic. {ECO:0000255}.
TRANSMEM 83 103 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 104 282 Extracellular. {ECO:0000255}.
COMPBIAS 4 70 Pro-rich.
COMPBIAS 45 56 Poly-Pro.
SITE 82 83 Cleavage; by SPPL2A. {ECO:0000250}.
SITE 130 131 Cleavage; by ADAM10. {ECO:0000250}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 203 234 {ECO:0000250|UniProtKB:P48023}.
CONFLICT 5 5 F -> L (in Ref. 2; BAB64291).
{ECO:0000305}.
CONFLICT 57 57 T -> P (in Ref. 4; AAK56449).
{ECO:0000305}.
SEQUENCE 282 AA; 31756 MW; 6743DAA1145671FB CRC64;
MQQPFNYPYP QIFWVDSSAT SPWASPGSVF PCPASVPGRP GQRRPPPPPP PPPPPPTLLP
SRPLPPLPPP SLKKKRDHNA GLCLLVMFFM VLVALVGLGL GMFQLFHLQK ELTELRESAS
QRHTESSLEK QIGHPNLPSE KKELRKVAHL TGKPNSRSIP LEWEDTYGIA LVSGVKYMKG
SLVINDTGLY FVYSKVYFRG QYCNNQPLSH KVYTRNSRYP QDLVLMEGKM MNYCTTGQMW
ARSSYLGAVF NLTSADHLYV NVSELSLVNF EESKTFFGLY KL


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