##gff-version 3
P16015	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07450	
P16015	UniProtKB	Chain	2	260	.	.	.	ID=PRO_0000077427;Note=Carbonic anhydrase 3	
P16015	UniProtKB	Domain	3	259	.	.	.	Note=Alpha-carbonic anhydrase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01134	
P16015	UniProtKB	Region	64	67	.	.	.	Note=Involved in proton transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07451	
P16015	UniProtKB	Binding site	94	94	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P16015	UniProtKB	Binding site	96	96	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P16015	UniProtKB	Binding site	119	119	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P16015	UniProtKB	Binding site	198	199	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P16015	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07450	
P16015	UniProtKB	Modified residue	29	29	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	48	48	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	127	127	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P16015	UniProtKB	Modified residue	182	182	.	.	.	Note=S-glutathionyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	187	187	.	.	.	Note=S-glutathionyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	216	216	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Modified residue	219	219	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14141	
P16015	UniProtKB	Sequence conflict	9	9	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P16015	UniProtKB	Sequence conflict	86	86	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P16015	UniProtKB	Sequence conflict	126	126	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P16015	UniProtKB	Sequence conflict	146	146	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305