##gff-version 3
Q29495	UniProtKB	Chain	1	207	.	.	.	ID=PRO_0000074586;Note=Serotonin N-acetyltransferase	
Q29495	UniProtKB	Domain	35	196	.	.	.	Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532	
Q29495	UniProtKB	Region	1	29	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q29495	UniProtKB	Region	28	35	.	.	.	Note=YWHAZ-binding	
Q29495	UniProtKB	Binding site	124	126	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10319816,ECO:0000269|PubMed:11336675,ECO:0000269|PubMed:11902838;Dbxref=PMID:10319816,PMID:11336675,PMID:11902838	
Q29495	UniProtKB	Binding site	124	124	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11336675,ECO:0000269|PubMed:11884405,ECO:0000269|PubMed:11902838;Dbxref=PMID:11336675,PMID:11884405,PMID:11902838	
Q29495	UniProtKB	Binding site	132	137	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10319816,ECO:0000269|PubMed:11336675,ECO:0000269|PubMed:11902838;Dbxref=PMID:10319816,PMID:11336675,PMID:11902838	
Q29495	UniProtKB	Binding site	159	159	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11336675,ECO:0000269|PubMed:11884405,ECO:0000269|PubMed:11902838;Dbxref=PMID:11336675,PMID:11884405,PMID:11902838	
Q29495	UniProtKB	Binding site	168	170	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10319816,ECO:0000269|PubMed:11336675,ECO:0000269|PubMed:11902838;Dbxref=PMID:10319816,PMID:11336675,PMID:11902838	
Q29495	UniProtKB	Site	120	120	.	.	.	Note=Important for the catalytic mechanism%3B involved in substrate deprotonation;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10319816,ECO:0000269|PubMed:11884405;Dbxref=PMID:10319816,PMID:11884405	
Q29495	UniProtKB	Site	122	122	.	.	.	Note=Important for the catalytic mechanism%3B involved in substrate deprotonation;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10319816,ECO:0000269|PubMed:11884405;Dbxref=PMID:10319816,PMID:11884405	
Q29495	UniProtKB	Modified residue	31	31	.	.	.	Note=Phosphothreonine%3B by PKA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11427721,ECO:0000269|PubMed:14578935,ECO:0000269|PubMed:15644438;Dbxref=PMID:11427721,PMID:14578935,PMID:15644438	
Q29495	UniProtKB	Modified residue	205	205	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644438;Dbxref=PMID:15644438	
Q29495	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Loss of PKA-promoted YWHAZ-binding%3B when associated with G-205. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644438;Dbxref=PMID:15644438	
Q29495	UniProtKB	Mutagenesis	57	57	.	.	.	Note=No effect on enzymatic activity%3B when associated with A-59. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18362150;Dbxref=PMID:18362150	
Q29495	UniProtKB	Mutagenesis	59	59	.	.	.	Note=No effect on enzymatic activity%3B when associated with A-57. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18362150;Dbxref=PMID:18362150	
Q29495	UniProtKB	Mutagenesis	63	65	.	.	.	Note=Drastic loss of enzymatic activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18362150;Dbxref=PMID:18362150	
Q29495	UniProtKB	Mutagenesis	64	64	.	.	.	Note=Drastic loss of enzymatic activity. P->A%2CG%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18362150;Dbxref=PMID:18362150	
Q29495	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Reduces catalytic activity 270-fold and decreases affinity for acetyl-coenzyme A%3B when associated with A-122. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10319816,ECO:0000269|PubMed:11884405;Dbxref=PMID:10319816,PMID:11884405	
Q29495	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Decreases affinity for acetyl-coenzyme A and for substrate. H->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10319816,ECO:0000269|PubMed:11884405;Dbxref=PMID:10319816,PMID:11884405	
Q29495	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Reduces catalytic activity 270-fold and decreases affinity for acetyl-coenzyme A%3B when associated with A-120. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10319816,ECO:0000269|PubMed:11884405;Dbxref=PMID:10319816,PMID:11884405	
Q29495	UniProtKB	Mutagenesis	122	122	.	.	.	Note=Decreases affinity for acetyl-coenzyme A and for substrate. H->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10319816,ECO:0000269|PubMed:11884405;Dbxref=PMID:10319816,PMID:11884405	
Q29495	UniProtKB	Mutagenesis	160	160	.	.	.	Note=No effect on catalytic activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10024876,ECO:0000269|PubMed:11902838;Dbxref=PMID:10024876,PMID:11902838	
Q29495	UniProtKB	Mutagenesis	160	160	.	.	.	Note=Reduces catalytic activity. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10024876,ECO:0000269|PubMed:11902838;Dbxref=PMID:10024876,PMID:11902838	
Q29495	UniProtKB	Mutagenesis	161	161	.	.	.	Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11902838;Dbxref=PMID:11902838	
Q29495	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Reduces catalytic activity 30-fold. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10319816,ECO:0000269|PubMed:11884405;Dbxref=PMID:10319816,PMID:11884405	
Q29495	UniProtKB	Mutagenesis	205	205	.	.	.	Note=Loss of PKA-promoted YWHAZ-binding%3B when associated with A-31. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644438;Dbxref=PMID:15644438	
Q29495	UniProtKB	Beta strand	34	38	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Helix	42	44	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Helix	45	55	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Helix	57	60	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Helix	67	76	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Helix	78	80	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Beta strand	81	86	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Beta strand	89	99	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Beta strand	101	103	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Helix	106	110	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Beta strand	118	126	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Helix	128	130	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KUX	
Q29495	UniProtKB	Beta strand	132	134	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KUX	
Q29495	UniProtKB	Helix	135	148	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Beta strand	150	152	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1L0C	
Q29495	UniProtKB	Beta strand	155	160	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Helix	162	164	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Helix	165	169	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Turn	170	172	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Beta strand	173	178	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW	
Q29495	UniProtKB	Beta strand	189	194	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CJW