##gff-version 3 P55087 UniProtKB Chain 1 323 . . . ID=PRO_0000063948;Note=Aquaporin-4 P55087 UniProtKB Topological domain 1 36 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Transmembrane 37 57 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Topological domain 58 69 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Transmembrane 70 89 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Topological domain 90 93 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Intramembrane 94 101 . . . Note=Discontinuously helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Topological domain 102 115 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Transmembrane 116 136 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Topological domain 137 155 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Transmembrane 156 176 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Topological domain 177 184 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Topological domain 206 208 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Intramembrane 209 222 . . . Note=Discontinuously helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Topological domain 223 231 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Topological domain 253 323 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Motif 97 99 . . . Note=NPA 1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Motif 213 215 . . . Note=NPA 2;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19383790;Dbxref=PMID:19383790 P55087 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine%3B by PKG;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55088 P55087 UniProtKB Modified residue 180 180 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47863 P55087 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47863 P55087 UniProtKB Modified residue 285 285 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55088 P55087 UniProtKB Modified residue 289 289 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55088 P55087 UniProtKB Modified residue 321 321 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47863 P55087 UniProtKB Lipidation 13 13 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47863 P55087 UniProtKB Lipidation 17 17 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47863 P55087 UniProtKB Glycosylation 153 153 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P55087 UniProtKB Glycosylation 206 206 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P55087 UniProtKB Alternative sequence 1 22 . . . ID=VSP_003232;Note=In isoform 1. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P55087 UniProtKB Natural variant 215 215 . . . ID=VAR_088778;Note=In MLC4%3B likely pathogenic%3B loss of function in cell volume regulation%3B does not localize to the cell membrane. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37143309;Dbxref=PMID:37143309 P55087 UniProtKB Sequence conflict 246 246 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P55087 UniProtKB Sequence conflict 287 288 . . . Note=VE->AK;Ontology_term=ECO:0000305;evidence=ECO:0000305 P55087 UniProtKB Sequence conflict 296 296 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P55087 UniProtKB Helix 33 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Turn 59 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Helix 70 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Helix 98 106 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Helix 112 136 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Helix 139 142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Turn 143 146 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Helix 156 177 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Helix 189 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Helix 214 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Turn 228 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8 P55087 UniProtKB Helix 232 250 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3GD8