##gff-version 3
P41047	UniProtKB	Chain	1	279	.	.	.	ID=PRO_0000034508;Note=Tumor necrosis factor ligand superfamily member 6%2C membrane form	
P41047	UniProtKB	Chain	1	127	.	.	.	ID=PRO_0000417159;Note=ADAM10-processed FasL form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P41047	UniProtKB	Chain	1	80	.	.	.	ID=PRO_0000417160;Note=FasL intracellular domain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P41047	UniProtKB	Chain	128	279	.	.	.	ID=PRO_0000034509;Note=Tumor necrosis factor ligand superfamily member 6%2C soluble form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P41047	UniProtKB	Topological domain	1	78	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41047	UniProtKB	Transmembrane	79	100	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41047	UniProtKB	Topological domain	101	279	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41047	UniProtKB	Region	30	70	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P41047	UniProtKB	Region	126	150	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P41047	UniProtKB	Compositional bias	30	68	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P41047	UniProtKB	Site	79	80	.	.	.	Note=Cleavage%3B by SPPL2A;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P41047	UniProtKB	Site	127	128	.	.	.	Note=Cleavage%3B by ADAM10;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P41047	UniProtKB	Glycosylation	117	117	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41047	UniProtKB	Glycosylation	182	182	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41047	UniProtKB	Glycosylation	248	248	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41047	UniProtKB	Glycosylation	258	258	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P41047	UniProtKB	Disulfide bond	200	231	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48023	
P41047	UniProtKB	Alternative sequence	1	210	.	.	.	ID=VSP_006445;Note=In isoform FasLS. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:10552956;Dbxref=PMID:10552956	
P41047	UniProtKB	Natural variant	184	184	.	.	.	Note=In strain: BALB/c%2C DBA/1 and DBA/2%3B enhances cytotoxicity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9108079;Dbxref=PMID:9108079	
P41047	UniProtKB	Natural variant	218	218	.	.	.	Note=In strain: BALB/c%2C DBA/1 and DBA/2%3B enhances cytotoxicity. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9108079;Dbxref=PMID:9108079	
P41047	UniProtKB	Natural variant	273	273	.	.	.	Note=In gld%3B abolishes binding of FASL to its receptor. F->L