IED Industry Enzyme Database

Detail Information for IndEnz0002010159
IED ID IndEnz0002010159
Enzyme Type ID protease010159
Protein Name 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
Gene Name Faslg Apt1lg1 Cd95l Fasl gld Tnfsf6
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MQQPMNYPCPQIFWVDSSATSSWAPPGSVFPCPSCGPRGPDQRRPPPPPPPVSPLPPPSQPLPLPPLTPLKKKDHNTNLWLPVVFFMVLVALVGMGLGMYQLFHLQKELAELREFTNQSLKVSSFEKQIANPSTPSEKKEPRSVAHLTGNPHSRSIPLEWEDTYGTALISGVKYKKGGLVINETGLYFVYSKVYFRGQSCNNQPLNHKVYMRNSKYPEDLVLMEEKRLNYCTTGQIWAHSSYLGAVFNLTSADHLYVNISQLSLINFEESKTFFGLYKL
Enzyme Length 279
Uniprot Accession Number P41047
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells (PubMed:7511063). Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development (PubMed:19794494, PubMed:7532682). Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses (PubMed:19794494). TNFRSF6/FAS-mediated apoptosis has also a role in the induction of peripheral tolerance (PubMed:10779162). Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis (By similarity). {ECO:0000250|UniProtKB:P48023, ECO:0000269|PubMed:19794494, ECO:0000269|PubMed:7511063, ECO:0000269|PubMed:7532682}.; FUNCTION: [Tumor necrosis factor ligand superfamily member 6, soluble form]: Induces FAS-mediated activation of NF-kappa-B, initiating non-apoptotic signaling pathways (PubMed:19794494). Can induce apoptosis but does not appear to be essential for this process (By similarity). {ECO:0000250|UniProtKB:P48023, ECO:0000269|PubMed:19794494}.; FUNCTION: [FasL intracellular domain]: Cytoplasmic form induces gene transcription inhibition. {ECO:0000250|UniProtKB:P48023}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (4); Compositional bias (1); Disulfide bond (1); Glycosylation (4); Natural variant (3); Region (2); Site (2); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Apoptosis;Cell membrane;Cytokine;Cytoplasmic vesicle;Disease variant;Disulfide bond;Glycoprotein;Lysosome;Membrane;Nucleus;Reference proteome;Repressor;Secreted;Signal-anchor;Transcription;Transcription regulation;Transmembrane;Transmembrane helix;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform FasL]: Cell membrane {ECO:0000269|PubMed:19794494, ECO:0000269|PubMed:7532682}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P48023}. Lysosome lumen {ECO:0000250|UniProtKB:P48023}. Note=Is internalized into multivesicular bodies of secretory lysosomes after phosphorylation by FGR and monoubiquitination. Colocalizes with the SPPL2A protease at the cell membrane. {ECO:0000250|UniProtKB:P48023}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 6, soluble form]: Secreted {ECO:0000269|PubMed:10552956, ECO:0000269|PubMed:19794494}. 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}.
Modified Residue
Post Translational Modification 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}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10049941; 10086384; 10190896; 10196250; 10209037; 10209045; 10235489; 10329594; 10352252; 10352283; 10370375; 10393694; 10395644; 10415034; 10417775; 10436160; 10452979; 10453074; 10477580; 10490975; 10510373; 10514014; 10515865; 10527913; 10550220; 10555993; 10585755; 10587362; 10588860; 10619357; 10620607; 10657610; 10679090; 10684974; 10712254; 10727450; 10728678; 10792025; 10875923; 10878381; 10898516; 10900166; 10903773; 10919598; 10932231; 10950807; 10993919; 11006240; 11035071; 11035735; 11046015; 11067900; 11086022; 11090183; 11106570; 11159055; 11197687; 11239407; 11241200; 11254710; 11292588; 11298345; 11312248; 11333140; 11359810; 11441070; 11457890; 11466351; 11489951; 11490027; 11497079; 11507223; 11536159; 11567045; 11581190; 11685458; 11695234; 11714837; 11714840; 11727760; 11739537; 11741599; 11752172; 11753206; 11781294; 11792426; 11829488; 11836634; 11881823; 11884544; 11922619; 11937135; 11937560; 11956070; 11978635; 11981816; 12021107; 12045257; 12050361; 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Motif
Gene Encoded By
Mass 31,442
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda