Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tumor necrosis factor ligand superfamily member 6

Gene

FASLG

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells. May be involved in cytotoxic T-cell mediated apoptosis and in T-cell development. TNFRSF6/FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. Binding to the decoy receptor TNFRSF6B/DcR3 modulates its effects (By similarity).By similarity
The FasL intracellular domain (FasL ICD) cytoplasmic form induces gene transcription inhibition.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Repressor

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor ligand superfamily member 6
Alternative name(s):
CD95 ligand
Short name:
CD95-L
Fas antigen ligand
Short name:
Fas ligand
Short name:
FasL
CD_antigen: CD178
Cleaved into the following 4 chains:
Alternative name(s):
Receptor-binding FasL ectodomain
Soluble Fas ligand
Short name:
sFasL
FasL intracellular domain
Short name:
FasL ICD
Alternative name(s):
SPPL2A-processed FasL form
Short name:
SPA
Gene namesi
Name:FASLG
Synonyms:CD95L, FASL, TNFSF6
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Tumor necrosis factor ligand superfamily member 6, soluble form :
  • Secreted By similarity

  • Note: May be released into the extracellular fluid, probably by cleavage form the cell surface.By similarity
FasL intracellular domain :
  • Nucleus By similarity

  • Note: The FasL ICD cytoplasmic form is translocated into the nucleus.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 82CytoplasmicSequence analysisAdd BLAST82
Transmembranei83 – 103Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini104 – 282ExtracellularSequence analysisAdd BLAST179

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000345101 – 282Tumor necrosis factor ligand superfamily member 6, membrane formAdd BLAST282
ChainiPRO_00004171611 – 130ADAM10-processed FasL formBy similarityAdd BLAST130
ChainiPRO_00004171621 – 83FasL intracellular domainBy similarityAdd BLAST83
ChainiPRO_0000034511131 – 282Tumor necrosis factor ligand superfamily member 6, soluble formBy similarityAdd BLAST152

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi185N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi203 ↔ 234Sequence analysis
Glycosylationi251N-linked (GlcNAc...)Sequence analysis1
Glycosylationi261N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

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 (By similarity).By similarity
Phosphorylated by FGR on tyrosine residues; this is required for ubiquitination and subsequent internalization.By similarity
N-glycosylated.By similarity
Monoubiquitinated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei82 – 83Cleavage; by SPPL2ABy similarity2
Sitei130 – 131Cleavage; by ADAM10By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9BEA8.
PRIDEiQ9BEA8.

Expressioni

Inductioni

By IL-18.

Interactioni

Subunit structurei

Homotrimer (Probable). Interacts with ARHGAP9, BAIAP2L1, BTK, CACNB3, CACNB4, CRK, DLG2, DNMBP, DOCK4, EPS8L3, FGR, FYB, 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 (By similarity).By similarityCurated

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000019767.

Structurei

3D structure databases

ProteinModelPortaliQ9BEA8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 70Pro-richAdd BLAST67
Compositional biasi45 – 56Poly-ProAdd BLAST12

Sequence similaritiesi

Belongs to the tumor necrosis factor family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHZF. Eukaryota.
ENOG4112D9R. LUCA.
HOVERGENiHBG055128.
InParanoidiQ9BEA8.
KOiK04389.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR028326. FASL.
IPR006053. TNF.
IPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00229. TNF. 1 hit.
[Graphical view]
PRINTSiPR01681. FASLIGAND.
PR01234. TNECROSISFCT.
SMARTiSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9BEA8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQPFNYPYP QIFWVDSSAT SPWASPGSVF PCPASVPGRP GQRRPPPPPP
60 70 80 90 100
PPPPPPTLLP SRPLPPLPPP SLKKKRDHNA GLCLLVMFFM VLVALVGLGL
110 120 130 140 150
GMFQLFHLQK ELTELRESAS QRHTESSLEK QIGHPNLPSE KKELRKVAHL
160 170 180 190 200
TGKPNSRSIP LEWEDTYGIA LVSGVKYMKG SLVINDTGLY FVYSKVYFRG
210 220 230 240 250
QYCNNQPLSH KVYTRNSRYP QDLVLMEGKM MNYCTTGQMW ARSSYLGAVF
260 270 280
NLTSADHLYV NVSELSLVNF EESKTFFGLY KL
Length:282
Mass (Da):31,756
Last modified:June 1, 2001 - v1
Checksum:i6743DAA1145671FB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5F → L in BAB64291 (PubMed:11792426).Curated1
Sequence conflicti57T → P in AAK56449 (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027297 mRNA. Translation: BAB40919.1.
AB069764 Genomic DNA. Translation: BAB64291.1.
AF397407 mRNA. Translation: AAK84408.1.
AY033634 mRNA. Translation: AAK56449.1.
RefSeqiNP_998971.1. NM_213806.1.
UniGeneiSsc.15870.

Genome annotation databases

GeneIDi396726.
KEGGissc:396726.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027297 mRNA. Translation: BAB40919.1.
AB069764 Genomic DNA. Translation: BAB64291.1.
AF397407 mRNA. Translation: AAK84408.1.
AY033634 mRNA. Translation: AAK56449.1.
RefSeqiNP_998971.1. NM_213806.1.
UniGeneiSsc.15870.

3D structure databases

ProteinModelPortaliQ9BEA8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000019767.

Proteomic databases

PaxDbiQ9BEA8.
PRIDEiQ9BEA8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396726.
KEGGissc:396726.

Organism-specific databases

CTDi356.

Phylogenomic databases

eggNOGiENOG410IHZF. Eukaryota.
ENOG4112D9R. LUCA.
HOVERGENiHBG055128.
InParanoidiQ9BEA8.
KOiK04389.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR028326. FASL.
IPR006053. TNF.
IPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00229. TNF. 1 hit.
[Graphical view]
PRINTSiPR01681. FASLIGAND.
PR01234. TNECROSISFCT.
SMARTiSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTNFL6_PIG
AccessioniPrimary (citable) accession number: Q9BEA8
Secondary accession number(s): Q95M04, Q95N10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 1, 2001
Last modified: October 5, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.