##gff-version 3
P60520	UniProtKB	Chain	1	116	.	.	.	ID=PRO_0000212373;Note=Gamma-aminobutyric acid receptor-associated protein-like 2	
P60520	UniProtKB	Propeptide	117	117	.	.	.	ID=PRO_0000423070;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169837;Dbxref=PMID:15169837	
P60520	UniProtKB	Site	116	117	.	.	.	Note=Cleavage%3B by ATG4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169837;Dbxref=PMID:15169837	
P60520	UniProtKB	Modified residue	24	24	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861	
P60520	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17525332;Dbxref=PMID:17525332	
P60520	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine%3B by TBK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31709703;Dbxref=PMID:31709703	
P60520	UniProtKB	Modified residue	88	88	.	.	.	Note=Phosphoserine%3B by TBK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31709703;Dbxref=PMID:31709703	
P60520	UniProtKB	Lipidation	116	116	.	.	.	Note=Phosphatidylethanolamine amidated glycine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:12507496,ECO:0000269|PubMed:33909989,ECO:0000305|PubMed:29458288;Dbxref=PMID:12507496,PMID:29458288,PMID:33909989	
P60520	UniProtKB	Lipidation	116	116	.	.	.	Note=Phosphatidylserine amidated glycine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33909989;Dbxref=PMID:33909989	
P60520	UniProtKB	Natural variant	51	51	.	.	.	ID=VAR_049756;Note=V->A;Dbxref=dbSNP:rs11556291	
P60520	UniProtKB	Mutagenesis	47	47	.	.	.	Note=Strongly reduced interaction with UBA5. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30990354;Dbxref=PMID:30990354	
P60520	UniProtKB	Mutagenesis	87	88	.	.	.	Note=Impaired phosphorylation by TBK1. SS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31709703;Dbxref=PMID:31709703	
P60520	UniProtKB	Mutagenesis	87	88	.	.	.	Note=Phospho-mimetic mutant%3B impaired interaction with ATG4 proteins%2C preventing cleavage at the C-terminus%2C conjugation to phosphatidylethanolamine. SS->DD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31709703;Dbxref=PMID:31709703	
P60520	UniProtKB	Mutagenesis	88	88	.	.	.	Note=Phospho-mimetic mutant%3B abolished localization to autophagosomes. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31709703;Dbxref=PMID:31709703	
P60520	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Impairs localization at the autophagosomal membrane. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169837;Dbxref=PMID:15169837	
P60520	UniProtKB	Sequence conflict	29	29	.	.	.	Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P60520	UniProtKB	Helix	5	8	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YO8	
P60520	UniProtKB	Helix	11	24	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YO8	
P60520	UniProtKB	Beta strand	28	35	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YO8	
P60520	UniProtKB	Beta strand	39	41	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6H8C	
P60520	UniProtKB	Beta strand	48	52	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YO8	
P60520	UniProtKB	Helix	57	68	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YO8	
P60520	UniProtKB	Beta strand	77	80	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YO8	
P60520	UniProtKB	Helix	91	98	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YO8	
P60520	UniProtKB	Beta strand	105	110	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YO8