##gff-version 3
P56402	UniProtKB	Chain	1	271	.	.	.	ID=PRO_0000063936;Note=Aquaporin-2	
P56402	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P56402	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41181	
P56402	UniProtKB	Topological domain	33	40	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P56402	UniProtKB	Transmembrane	41	59	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41181	
P56402	UniProtKB	Topological domain	60	64	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P56402	UniProtKB	Intramembrane	65	74	.	.	.	Note=Discontinuously helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41181	
P56402	UniProtKB	Topological domain	75	85	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P56402	UniProtKB	Transmembrane	86	107	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41181	
P56402	UniProtKB	Topological domain	108	127	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P56402	UniProtKB	Transmembrane	128	148	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41181	
P56402	UniProtKB	Topological domain	149	156	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P56402	UniProtKB	Transmembrane	157	176	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41181	
P56402	UniProtKB	Topological domain	177	180	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P56402	UniProtKB	Intramembrane	181	193	.	.	.	Note=Discontinuously helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41181	
P56402	UniProtKB	Topological domain	194	201	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P56402	UniProtKB	Transmembrane	202	222	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41181	
P56402	UniProtKB	Topological domain	223	271	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P56402	UniProtKB	Region	251	271	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P56402	UniProtKB	Motif	68	70	.	.	.	Note=NPA 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41181	
P56402	UniProtKB	Motif	184	186	.	.	.	Note=NPA 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41181	
P56402	UniProtKB	Modified residue	256	256	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:16641094,ECO:0007744|PubMed:21183079;Dbxref=PMID:16641094,PMID:21183079	
P56402	UniProtKB	Modified residue	261	261	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P56402	UniProtKB	Glycosylation	124	124	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P56402	UniProtKB	Natural variant	256	256	.	.	.	Note=In cph%3B loss of a phosphorylation site and loss of trafficking to the apical cell membrane%3B causes aberrant location at the basolateral cell membrane. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16641094;Dbxref=PMID:16641094	
P56402	UniProtKB	Mutagenesis	126	126	.	.	.	Note=Does not cause loss of water channel activity%2C but impairs trafficking from cytoplasmic vesicles to the cell membrane. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10191086;Dbxref=PMID:10191086	
P56402	UniProtKB	Sequence conflict	9	10	.	.	.	Note=FS->YC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P56402	UniProtKB	Sequence conflict	213	213	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305