##gff-version 3 Q96PH1 UniProtKB Chain 1 765 . . . ID=PRO_0000224995;Note=NADPH oxidase 5 Q96PH1 UniProtKB Topological domain 1 238 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Transmembrane 239 259 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Topological domain 260 266 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Transmembrane 267 289 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Topological domain 290 317 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Transmembrane 318 338 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Topological domain 339 362 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Transmembrane 363 383 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Topological domain 384 394 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Transmembrane 395 417 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Topological domain 418 434 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Transmembrane 435 455 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Topological domain 456 583 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Transmembrane 584 604 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Topological domain 605 765 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PH1 UniProtKB Domain 26 56 . . . Note=EF-hand 1;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Domain 57 92 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Domain 93 156 . . . Note=EF-hand 3%3B atypical%3B contains an insert of 28 residues;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Domain 165 200 . . . Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Domain 293 440 . . . Note=Ferric oxidoreductase Q96PH1 UniProtKB Domain 441 577 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 Q96PH1 UniProtKB Region 122 141 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q96PH1 UniProtKB Binding site 42 42 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Binding site 44 44 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Binding site 49 49 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Binding site 70 70 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Binding site 72 72 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Binding site 74 74 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Binding site 76 76 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Binding site 81 81 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Binding site 106 106 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Binding site 108 108 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Binding site 138 138 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Binding site 140 140 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Binding site 145 145 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Binding site 178 178 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Binding site 180 180 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Binding site 182 182 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Binding site 189 189 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q96PH1 UniProtKB Alternative sequence 1 200 . . . ID=VSP_017326;Note=In isoform v5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.2 Q96PH1 UniProtKB Alternative sequence 1 18 . . . ID=VSP_017327;Note=In isoform v2 and isoform v4. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:11483596,ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:11483596,PMID:14702039,PMID:15489334 Q96PH1 UniProtKB Alternative sequence 1 17 . . . ID=VSP_041619;Note=In isoform v6. MNTSGDPAQTGPEGCRG->MAFVCAGLSD;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q96PH1 UniProtKB Alternative sequence 109 136 . . . ID=VSP_017328;Note=In isoform v1%2C isoform v2 and isoform v6. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:11483596,ECO:0000303|PubMed:15489334;Dbxref=PMID:11483596,PMID:15489334 Q96PH1 UniProtKB Natural variant 576 576 . . . ID=VAR_055820;Note=R->H;Dbxref=dbSNP:rs2277552 Q96PH1 UniProtKB Natural variant 759 759 . . . ID=VAR_055821;Note=R->G;Dbxref=dbSNP:rs7168025 Q96PH1 UniProtKB Sequence conflict 208 208 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Sequence conflict 272 272 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Sequence conflict 375 375 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Sequence conflict 380 380 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PH1 UniProtKB Helix 721 728 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6SZ5 Q96PH1 UniProtKB Region 416 737 . . . Note=C-terminal catalytic dehydrogenase domain;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21319793;Dbxref=PMID:21319793 Q96PH1 UniProtKB Mutagenesis 277 277 . . . Note=Loss of activity but no effect on protein levels. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319793;Dbxref=PMID:21319793 Q96PH1 UniProtKB Mutagenesis 567 567 . . . Note=Loss of activity but no effect on protein levels. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319793;Dbxref=PMID:21319793 Q96PH1 UniProtKB Mutagenesis 656 656 . . . Note=Loss of activity but no effect on protein levels. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319793;Dbxref=PMID:21319793 Q96PH1 UniProtKB Region 1 161 . . . Note=N-terminal regulatory EF domain;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:14982937,ECO:0000305|PubMed:31785178;Dbxref=PMID:14982937,PMID:31785178 Q96PH1 UniProtKB Region 1 77 . . . Note=N-terminal lobe of N-terminal regulatory EF domain;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:31785178;Dbxref=PMID:31785178 Q96PH1 UniProtKB Region 78 161 . . . Note=C-terminal lobe of N-terminal regulatory EF domain;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:31785178;Dbxref=PMID:31785178 Q96PH1 UniProtKB Region 398 719 . . . Note=C-terminal catalytic dehydrogenase domain;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:31785178;Dbxref=PMID:31785178 Q96PH1 UniProtKB Modified residue 107 107 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22387196;Dbxref=PMID:22387196 Q96PH1 UniProtKB Modified residue 246 246 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22387196;Dbxref=PMID:22387196 Q96PH1 UniProtKB Modified residue 475 475 . . . Note=Phosphoserine%3B by CaMK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21642394;Dbxref=PMID:21642394 Q96PH1 UniProtKB Modified residue 490 490 . . . Note=Phosphothreonine%3B by PKC/PRKCA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22387196,ECO:0000269|PubMed:24505490;Dbxref=PMID:22387196,PMID:24505490 Q96PH1 UniProtKB Modified residue 494 494 . . . Note=Phosphothreonine%3B by CaMK2 and PKC/PRKCA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21642394,ECO:0000269|PubMed:22387196,ECO:0000269|PubMed:24505490;Dbxref=PMID:21642394,PMID:22387196,PMID:24505490 Q96PH1 UniProtKB Modified residue 498 498 . . . Note=Phosphoserine%3B by CaMK2 and PKC/PRKCA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21642394,ECO:0000269|PubMed:22387196,ECO:0000269|PubMed:24505490;Dbxref=PMID:21642394,PMID:22387196,PMID:24505490 Q96PH1 UniProtKB Modified residue 502 502 . . . Note=Phosphoserine%3B by CaMK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21642394;Dbxref=PMID:21642394 Q96PH1 UniProtKB Modified residue 519 519 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22387196;Dbxref=PMID:22387196 Q96PH1 UniProtKB Modified residue 659 659 . . . Note=Phosphoserine%3B by CaMK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21642394;Dbxref=PMID:21642394 Q96PH1 UniProtKB Modified residue 694 694 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22387196;Dbxref=PMID:22387196 Q96PH1 UniProtKB Mutagenesis 31 31 . . . Note=Loss of binding of 1 calcium molecule. No effect on catalytic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14982937;Dbxref=PMID:14982937 Q96PH1 UniProtKB Mutagenesis 107 107 . . . Note=Substantial loss of catalytic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22387196;Dbxref=PMID:22387196 Q96PH1 UniProtKB Mutagenesis 110 110 . . . Note=No effect on cell membrane localization and catalytic activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36653838;Dbxref=PMID:36653838 Q96PH1 UniProtKB Mutagenesis 111 111 . . . Note=No effect on cell membrane localization and catalytic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36653838;Dbxref=PMID:36653838 Q96PH1 UniProtKB Mutagenesis 112 112 . . . Note=No effect on cell membrane localization and catalytic activity. A->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36653838;Dbxref=PMID:36653838 Q96PH1 UniProtKB Mutagenesis 113 113 . . . Note=Significant reduction in cell membrane localization and catalytic activity. Reduced calcium-dependent interaction between the N-terminal regulatory region and the C-terminal catalytic region. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36653838;Dbxref=PMID:36653838 Q96PH1 UniProtKB Mutagenesis 114 114 . . . Note=No effect on cell membrane localization and catalytic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36653838;Dbxref=PMID:36653838 Q96PH1 UniProtKB Mutagenesis 115 115 . . . Note=Significant reduction in cell membrane localization and catalytic activity. No effect on calcium-dependent interaction between the N-terminal regulatory region and the C-terminal catalytic region. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36653838;Dbxref=PMID:36653838 Q96PH1 UniProtKB Mutagenesis 116 116 . . . Note=No effect on cell membrane localization and catalytic activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36653838;Dbxref=PMID:36653838 Q96PH1 UniProtKB Mutagenesis 475 475 . . . Note=Loss of CaMK2-mediated activation of its activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21642394;Dbxref=PMID:21642394 Q96PH1 UniProtKB Mutagenesis 490 490 . . . Note=Loss of PKC/PRKCA-mediated activation of its activity%3B when associated with A-494 and A-498. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24505490;Dbxref=PMID:24505490 Q96PH1 UniProtKB Mutagenesis 494 494 . . . Note=No effect on CaMK2-mediated activation of its activity. Loss of PKC/PRKCA-mediated activation of its activity%3B when associated with A-490 and A-498. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21642394,ECO:0000269|PubMed:24505490;Dbxref=PMID:21642394,PMID:24505490 Q96PH1 UniProtKB Mutagenesis 498 498 . . . Note=No effect on CaMK2-mediated activation of its activity. Loss of PKC/PRKCA-mediated activation of its activity%3B when associated with A-490 and A-494. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21642394,ECO:0000269|PubMed:24505490;Dbxref=PMID:21642394,PMID:24505490 Q96PH1 UniProtKB Mutagenesis 502 502 . . . Note=No effect on CaMK2-mediated activation of its activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21642394;Dbxref=PMID:21642394 Q96PH1 UniProtKB Mutagenesis 519 519 . . . Note=Very significant loss of catalytic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22387196;Dbxref=PMID:22387196 Q96PH1 UniProtKB Mutagenesis 549 549 . . . Note=No effect on cell membrane localization but loss of catalytic activity. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36653838;Dbxref=PMID:36653838 Q96PH1 UniProtKB Mutagenesis 659 659 . . . Note=No effect on CaMK2-mediated activation of its activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21642394;Dbxref=PMID:21642394 Q96PH1 UniProtKB Mutagenesis 694 694 . . . Note=Reduced nitrosylation. Very significant loss of catalytic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22387196;Dbxref=PMID:22387196