##gff-version 3
P00920	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P00920	UniProtKB	Chain	2	260	.	.	.	ID=PRO_0000077419;Note=Carbonic anhydrase 2	
P00920	UniProtKB	Domain	3	259	.	.	.	Note=Alpha-carbonic anhydrase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01134	
P00920	UniProtKB	Active site	64	64	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P00920	UniProtKB	Active site	67	67	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P00920	UniProtKB	Active site	127	127	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P00920	UniProtKB	Binding site	94	94	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P00920	UniProtKB	Binding site	96	96	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P00920	UniProtKB	Binding site	119	119	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P00920	UniProtKB	Binding site	198	199	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P00920	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P00920	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27139	
P00920	UniProtKB	Modified residue	87	87	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P00920	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00918	
P00920	UniProtKB	Sequence conflict	39	39	.	.	.	Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P00920	UniProtKB	Sequence conflict	145	145	.	.	.	Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P00920	UniProtKB	Sequence conflict	213	213	.	.	.	Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305