##gff-version 3
O54957	UniProtKB	Chain	1	242	.	.	.	ID=PRO_0000083326;Note=Linker for activation of T-cells family member 1	
O54957	UniProtKB	Topological domain	1	4	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O54957	UniProtKB	Transmembrane	5	28	.	.	.	Note=Helical%3B Signal-anchor for type III membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O54957	UniProtKB	Topological domain	29	242	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O54957	UniProtKB	Region	78	118	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O54957	UniProtKB	Region	136	139	.	.	.	Note=Interaction with PLCG1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
O54957	UniProtKB	Region	175	178	.	.	.	Note=Interaction with GRB2%2C GRAP2 and PIK3R1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
O54957	UniProtKB	Region	176	242	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O54957	UniProtKB	Region	195	198	.	.	.	Note=Interaction with GRB2%2C GRAP2 and PIK3R1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
O54957	UniProtKB	Compositional bias	93	116	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O54957	UniProtKB	Compositional bias	195	213	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O54957	UniProtKB	Compositional bias	216	242	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O54957	UniProtKB	Modified residue	40	40	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43561	
O54957	UniProtKB	Modified residue	41	41	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
O54957	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
O54957	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43561	
O54957	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43561	
O54957	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
O54957	UniProtKB	Modified residue	112	112	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
O54957	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43561	
O54957	UniProtKB	Modified residue	199	199	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
O54957	UniProtKB	Modified residue	212	212	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
O54957	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
O54957	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43561	
O54957	UniProtKB	Lipidation	27	27	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19592663;Dbxref=PMID:19592663	
O54957	UniProtKB	Lipidation	30	30	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19592663;Dbxref=PMID:19592663