##gff-version 3
Q9HCR9	UniProtKB	Chain	1	933	.	.	.	ID=PRO_0000247040;Note=Dual 3'%2C5'-cyclic-AMP and -GMP phosphodiesterase 11A	
Q9HCR9	UniProtKB	Domain	217	370	.	.	.	Note=GAF 1	
Q9HCR9	UniProtKB	Domain	402	558	.	.	.	Note=GAF 2	
Q9HCR9	UniProtKB	Domain	588	912	.	.	.	Note=PDEase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01192	
Q9HCR9	UniProtKB	Region	42	125	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9HCR9	UniProtKB	Compositional bias	57	83	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9HCR9	UniProtKB	Active site	664	664	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O76083	
Q9HCR9	UniProtKB	Binding site	424	424	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q922S4	
Q9HCR9	UniProtKB	Binding site	668	668	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01192	
Q9HCR9	UniProtKB	Binding site	704	704	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01192	
Q9HCR9	UniProtKB	Binding site	705	705	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01192	
Q9HCR9	UniProtKB	Binding site	705	705	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01192	
Q9HCR9	UniProtKB	Binding site	816	816	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01192	
Q9HCR9	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0C1Q2	
Q9HCR9	UniProtKB	Modified residue	163	163	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0C1Q2	
Q9HCR9	UniProtKB	Modified residue	239	239	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332	
Q9HCR9	UniProtKB	Alternative sequence	1	444	.	.	.	ID=VSP_019898;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:10725373;Dbxref=PMID:10725373	
Q9HCR9	UniProtKB	Alternative sequence	1	358	.	.	.	ID=VSP_019899;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11050148;Dbxref=PMID:11050148	
Q9HCR9	UniProtKB	Alternative sequence	1	250	.	.	.	ID=VSP_019900;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10906126,ECO:0000303|PubMed:11050148;Dbxref=PMID:10906126,PMID:11050148	
Q9HCR9	UniProtKB	Alternative sequence	251	304	.	.	.	ID=VSP_019901;Note=In isoform 2. KTLVSKFFDVHAGTPLLPCSSTENSNEVQVPWGKGIIGYVGEHGETVNIPDAYQ->MLKQARRPLFRNVLSATQWKKVKITRLVQISGASLAEKQEKHQDFLIQRQTKTK;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10906126,ECO:0000303|PubMed:11050148;Dbxref=PMID:10906126,PMID:11050148	
Q9HCR9	UniProtKB	Natural variant	804	804	.	.	.	ID=VAR_027056;Note=R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16767104;Dbxref=dbSNP:rs75127279,PMID:16767104	
Q9HCR9	UniProtKB	Natural variant	867	867	.	.	.	ID=VAR_027057;Note=R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16767104;Dbxref=dbSNP:rs61306957,PMID:16767104	
Q9HCR9	UniProtKB	Mutagenesis	355	355	.	.	.	Note=Induces a decrease in enzyme activity due to the inability of cGMP to bind and stimulate enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16330539;Dbxref=PMID:16330539	
Q9HCR9	UniProtKB	Sequence conflict	184	184	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9HCR9	UniProtKB	Sequence conflict	921	921	.	.	.	Note=S->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305