##gff-version 3
Q9V2V6	UniProtKB	Chain	1	252	.	.	.	ID=PRO_0000124171;Note=Proteasome subunit alpha 1	
Q9V2V6	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16950923;Dbxref=PMID:16950923	
Q9V2V6	UniProtKB	Chain	2	252	.	.	.	ID=PRO_0000397604;Note=Proteasome subunit alpha 1%2C N-terminally processed	
Q9V2V6	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16950923;Dbxref=PMID:16950923	
Q9V2V6	UniProtKB	Mutagenesis	2	12	.	.	.	Note=Prevents acetylation of Met-1. Enhances peptidase activity of the proteasome. Renders the cells less tolerant of hypoosmotic stress than the wild-type. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19376868;Dbxref=PMID:19376868	
Q9V2V6	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Enhances cleavage of PsmA1 by methionine aminopeptidase (MAP)%2C resulting in acetylation of the N-terminal alanine. Enhances peptidase activity of the proteasome. Renders the cells less tolerant of hypoosmotic stress than the wild-type. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19376868;Dbxref=PMID:19376868	
Q9V2V6	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Does not alter the prevalence of the alpha1 subunit in N-acetylated form in proteasomes. Renders the cells more tolerant of hypoosmotic and high-temperature stress than the wild-type. Q->D%2CP%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19376868;Dbxref=PMID:19376868	
Q9V2V6	UniProtKB	Sequence conflict	96	96	.	.	.	Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305