##gff-version 3
P24623	UniProtKB	Chain	1	196	.	.	.	ID=PRO_0000125883;Note=Alpha-crystallin A chain	
P24623	UniProtKB	Chain	1	191	.	.	.	ID=PRO_0000423505;Note=Alpha-crystallin A(1-168)	
P24623	UniProtKB	Chain	1	188	.	.	.	ID=PRO_0000423506;Note=Alpha-crystallin A(1-165)	
P24623	UniProtKB	Chain	1	186	.	.	.	ID=PRO_0000423507;Note=Alpha-crystallin A(1-163)	
P24623	UniProtKB	Chain	1	185	.	.	.	ID=PRO_0000423508;Note=Alpha-crystallin A(1-162)	
P24623	UniProtKB	Chain	1	180	.	.	.	ID=PRO_0000423509;Note=Alpha-crystallin A(1-157)	
P24623	UniProtKB	Chain	1	179	.	.	.	ID=PRO_0000423510;Note=Alpha-crystallin A(1-156)	
P24623	UniProtKB	Chain	1	174	.	.	.	ID=PRO_0000423511;Note=Alpha-crystallin A(1-151)	
P24623	UniProtKB	Domain	76	185	.	.	.	Note=SHSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00285	
P24623	UniProtKB	Region	1	63	.	.	.	Note=Required for complex formation with BFSP1 and BFSP2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02489	
P24623	UniProtKB	Region	168	196	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P24623	UniProtKB	Binding site	123	123	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02470	
P24623	UniProtKB	Binding site	125	125	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02470	
P24623	UniProtKB	Binding site	130	130	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02470	
P24623	UniProtKB	Binding site	177	177	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02470	
P24623	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:699911,ECO:0000269|Ref.5;Dbxref=PMID:699911	
P24623	UniProtKB	Modified residue	6	6	.	.	.	Note=Deamidated glutamine%3B partial;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P24623	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02489	
P24623	UniProtKB	Modified residue	50	50	.	.	.	Note=Deamidated glutamine%3B partial;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P24623	UniProtKB	Modified residue	93	93	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02489	
P24623	UniProtKB	Modified residue	122	122	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02489	
P24623	UniProtKB	Modified residue	124	124	.	.	.	Note=Deamidated asparagine%3B partial;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P24623	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02470	
P24623	UniProtKB	Modified residue	146	146	.	.	.	Note=Deamidated asparagine%3B partial;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P24623	UniProtKB	Modified residue	170	170	.	.	.	Note=Deamidated glutamine%3B partial;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P24623	UniProtKB	Glycosylation	185	185	.	.	.	Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P24623	UniProtKB	Alternative sequence	64	86	.	.	.	ID=VSP_011917;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:1429679,ECO:0000303|PubMed:2294971,ECO:0000303|PubMed:6171772,ECO:0000303|PubMed:8875649;Dbxref=PMID:1429679,PMID:2294971,PMID:6171772,PMID:8875649	
P24623	UniProtKB	Sequence conflict	147	147	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305