##gff-version 3 P70705 UniProtKB Chain 1 1492 . . . ID=PRO_0000046313;Note=Copper-transporting ATPase 1 P70705 UniProtKB Topological domain 1 645 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Transmembrane 646 667 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Topological domain 668 706 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Transmembrane 707 726 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Topological domain 727 733 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Transmembrane 734 754 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Topological domain 755 773 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Transmembrane 774 794 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Topological domain 795 927 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Transmembrane 928 951 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Topological domain 952 981 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Transmembrane 982 1003 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Topological domain 1004 1348 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Transmembrane 1349 1366 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Topological domain 1367 1377 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Transmembrane 1378 1397 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Topological domain 1398 1492 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70705 UniProtKB Domain 8 74 . . . Note=HMA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Domain 85 151 . . . Note=HMA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Domain 171 237 . . . Note=HMA 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Domain 277 343 . . . Note=HMA 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Domain 377 443 . . . Note=HMA 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Domain 480 546 . . . Note=HMA 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Domain 556 622 . . . Note=HMA 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Region 1478 1492 . . . Note=PDZD11-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70705 UniProtKB Motif 1459 1460 . . . Note=Endocytosis signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q64430 P70705 UniProtKB Motif 1479 1480 . . . Note=Endocytosis signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q64430 P70705 UniProtKB Active site 1036 1036 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70705 UniProtKB Binding site 18 18 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Binding site 19 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 22 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 182 182 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 185 185 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 288 288 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 291 291 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 388 388 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 391 391 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 491 491 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 494 494 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 567 567 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 570 570 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 P70705 UniProtKB Binding site 1073 1073 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Binding site 1293 1293 . . . . P70705 UniProtKB Binding site 1297 1297 . . . . P70705 UniProtKB Modified residue 152 152 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 327 327 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 353 353 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 P70705 UniProtKB Modified residue 357 357 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 362 362 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q64430 P70705 UniProtKB Modified residue 1204 1204 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:16641100;Dbxref=PMID:16641100 P70705 UniProtKB Modified residue 1422 1422 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 1424 1424 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 1452 1452 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 1455 1455 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 1458 1458 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 1461 1461 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04656 P70705 UniProtKB Modified residue 1465 1465 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 P70705 UniProtKB Modified residue 1468 1468 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q64430 P70705 UniProtKB Modified residue 1478 1478 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q64430 P70705 UniProtKB Glycosylation 678 678 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255