NOX5
entrez
79400
canonical
uniprot
Q96PH1
canonical
ensembl
ENSG00000255346
resolver
ensembl
ENSG00000290203
resolver
genesymbol
NOX5
resolver
hgnc
HGNC:14874
resolver
uniprot
A3QRJ0
resolver
uniprot
B2RBJ4
resolver
uniprot
Q08AN2
resolver
uniprot
Q08AN3
resolver
uniprot
Q8TEQ1
resolver
uniprot
Q8TER4
resolver
uniprot
Q96PH2
resolver
uniprot
Q96PJ8
resolver
uniprot
Q96PJ9
resolver
uniprot
Q9H6E0
resolver
uniprot
Q9HAM8
resolver
uniprot_entry
A3QRJ0_HUMAN
resolver
uniprot_entry
NOX5_HUMAN
resolver
uniprot_sec
B2RBJ4
resolver
uniprot_sec
Q08AN2
resolver
uniprot_sec
Q08AN3
resolver
uniprot_sec
Q8TEQ1
resolver
uniprot_sec
Q8TER4
resolver
uniprot_sec
Q96PH2
resolver
uniprot_sec
Q96PJ8
resolver
uniprot_sec
Q96PJ9
resolver
uniprot_sec
Q9H6E0
resolver
uniprot_sec
Q9HAM8
resolver
activity_regulation
ACTIVITY REGULATION: [Isoform v2]: Activated by calcium which induces conformational changes and interaction between the N-terminal regulatory region and the C-terminal catalytic region. Inhibited by diphenylene iodonium. {ECO:0000269|PubMed:14982937, ECO:0000269|PubMed:17587483, ECO:0000269|PubMed:36653838}.
uniprot
proteins
amino_acid_sequence
MNTSGDPAQTGPEGCRGTMSAEEDARWLRWVTQQFKTIAGEDGEISLQEFKAALHVKESFFAERFFALFDSDRSGTITLQELQEALTLLIHGSPMDKLKFLFQVYDIDVCARQGASAGTEWGAGAGPHWASSPLGTGSGSIDPDELRTVLQSCLRESAISLPDEKLDQLTLALFESADADGNGAITFEELRDELQRFPGVMENLTISAAHWLTAPAPRPRPRRPRQLTRAYWHNHRSQLFCLATYAGLHVLLFGLAASAHRDLGASVMVAKGCGQCLNFDCSFIAVLMLRRCLTWLRATWLAQVLPLDQNIQFHQLMGYVVVGLSLVHTVAHTVNFVLQAQAEASPFQFWELLLTTRPGIGWVHGSASPTGVALLLLLLLMFICSSSCIRRSGHFEVFYWTHLSYLLVWLLLIFHGPNFWKWLLVPGILFFLEKAIGLAVSRMAAVCIMEVNLLPSKVTHLLIKRPPFFHYRPGDYLYLNIPTIARYEWHPFTISSAPEQKDTIWLHIRSQGQWTNRLYESFKASDPLGRGSKRLSRSVTMRKSQRSSKGSEILLEKHKFCNIKCYIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMYRHQKRKHTCPSCQHSWIEGVQDNMKLHKVDFIWINRDQRSFEWFVSLLTKLEMDQAEEAQYGRFLELHMYMTSALGKNDMKAIGLQMALDLLANKEKKDSITGLQTRTQPGRPDWSKVFQKVAAEKKGKVQVFFCGSPALAKVLKGHCEKFGFRFFQENF
uniprot
proteins
ec_number
1.-.-.-
uniprot
proteins
ec_number
1.6.3.-
uniprot
proteins
function
FUNCTION: Calcium-dependent NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor (PubMed:12686516). Also synthesizes NAADP from its reduced NAADPH form which promotes Ca(2+) signaling during T cell activation (PubMed:34784249). May play a role in cell growth and apoptosis (PubMed:12686516). {ECO:0000269|PubMed:12686516, ECO:0000269|PubMed:34784249}.; FUNCTION: [Isoform v2]: Calcium-dependent NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor (PubMed:11483596, PubMed:14982937, PubMed:17275676, PubMed:17587483, PubMed:21642394, PubMed:22387196, PubMed:22427510, PubMed:24505490, PubMed:36653838). Involved in endothelial generation of reactive oxygen species (ROS), proliferation and angiogenesis and contributes to endothelial response to thrombin (PubMed:17275676). Regulates redox-dependent processes in lymphocytes and spermatozoa (PubMed:11483596). {ECO:0000269|PubMed:11483596, ECO:0000269|PubMed:14982937, ECO:0000269|PubMed:17275676, ECO:0000269|PubMed:17587483, ECO:0000269|PubMed:21642394, ECO:0000269|PubMed:22387196, ECO:0000269|PubMed:22427510, ECO:0000269|PubMed:24505490, ECO:0000269|PubMed:36653838}.; FUNCTION: [Isoform v1]: Calcium-dependent NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor. {ECO:0000269|PubMed:21319793, ECO:0000269|PubMed:22427510}.; FUNCTION: [Isoform v5]: This isoform lacks calcium-binding domains and was showed to present a NADPH oxidase activity in a calcium-independent manner (PubMed:17275676, PubMed:36653838). May be involved in endothelial generation of reactive oxygen species (ROS), proliferation and angiogenesis and contribute to endothelial response to thrombin (PubMed:17275676). However another study showed an absence of oxidase activity (PubMed:22427510). Subject to rapid degradation (PubMed:36653838). {ECO:0000269|PubMed:17275676, ECO:0000269|PubMed:22427510, ECO:0000269|PubMed:36653838}.; FUNCTION: [Isoform v3]: Lacks calcium-dependent NADPH oxidase activity. {ECO:0000269|PubMed:22427510}.; FUNCTION: [Isoform v4]: Lacks calcium-dependent NADPH oxidase activity. {ECO:0000269|PubMed:22427510}.
uniprot
proteins
mass_dalton
86439
uniprot
proteins
mutagenesis
MUTAGEN Q96PH1-3:277; /note="L->R: Loss of activity but no effect on protein levels."; /evidence="ECO:0000269|PubMed:21319793"; MUTAGEN Q96PH1-3:567; /note="P->H: Loss of activity but no effect on protein levels."; /evidence="ECO:0000269|PubMed:21319793"; MUTAGEN Q96PH1-3:656; /note="D->A: Loss of activity but no effect on protein levels."; /evidence="ECO:0000269|PubMed:21319793"; MUTAGEN Q96PH1-4:31; /note="E->Q: Loss of binding of 1 calcium molecule. No effect on catalytic activity."; /evidence="ECO:0000269|PubMed:14982937"; MUTAGEN Q96PH1-4:107; /note="C->S: Substantial loss of catalytic activity."; /evidence="ECO:0000269|PubMed:22387196"; MUTAGEN Q96PH1-4:110; /note="E->A: No effect on cell membrane localization and catalytic activity."; /evidence="ECO:0000269|PubMed:36653838"; MUTAGEN Q96PH1-4:111; /note="S->A: No effect on cell membrane localization and catalytic activity."; /evidence="ECO:0000269|PubMed:36653838"; MUTAGEN Q96PH1-4:112; /note="A->N: No effect on cell membrane localization and catalytic activity."; /evidence="ECO:0000269|PubMed:36653838"; MUTAGEN Q96PH1-4:113; /note="I->N: 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."; /evidence="ECO:0000269|PubMed:36653838"; MUTAGEN Q96PH1-4:114; /note="S->A: No effect on cell membrane localization and catalytic activity."; /evidence="ECO:0000269|PubMed:36653838"; MUTAGEN Q96PH1-4:115; /note="L->A: 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."; /evidence="ECO:0000269|PubMed:36653838"; MUTAGEN Q96PH1-4:116; /note="P->A: No effect on cell membrane localization and catalytic activity."; /evidence="ECO:0000269|PubMed:36653838"; MUTAGEN Q96PH1-4:475; /note="S->A: Loss of CaMK2-mediated activation of its activity."; /evidence="ECO:0000269|PubMed:21642394"; MUTAGEN Q96PH1-4:490; /note="S->A: Loss of PKC/PRKCA-mediated activation of its activity; when associated with A-494 and A-498."; /evidence="ECO:0000269|PubMed:24505490"; MUTAGEN Q96PH1-4:494; /note="T->A: No effect on CaMK2-mediated activation of its activity. Loss of PKC/PRKCA-mediated activation of its activity; when associated with A-490 and A-498."; /evidence="ECO:0000269|PubMed:21642394, ECO:0000269|PubMed:24505490"; MUTAGEN Q96PH1-4:498; /note="S->A: No effect on CaMK2-mediated activation of its activity. Loss of PKC/PRKCA-mediated activation of its activity; when associated with A-490 and A-494."; /evidence="ECO:0000269|PubMed:21642394, ECO:0000269|PubMed:24505490"; MUTAGEN Q96PH1-4:502; /note="S->A: No effect on CaMK2-mediated activation of its activity."; /evidence="ECO:0000269|PubMed:21642394"; MUTAGEN Q96PH1-4:519; /note="C->S: Very significant loss of catalytic activity."; /evidence="ECO:0000269|PubMed:22387196"; MUTAGEN Q96PH1-4:549; /note="P->H: No effect on cell membrane localization but loss of catalytic activity."; /evidence="ECO:0000269|PubMed:36653838"; MUTAGEN Q96PH1-4:659; /note="S->A: No effect on CaMK2-mediated activation of its activity."; /evidence="ECO:0000269|PubMed:21642394"; MUTAGEN Q96PH1-4:694; /note="C->S: Reduced nitrosylation. Very significant loss of catalytic activity."; /evidence="ECO:0000269|PubMed:22387196
uniprot
proteins
post_translational_modification
PTM: [Isoform v2]: Phosphorylation at Ser-475 by CaMK2 and at Ser-490, Thr-494 and Ser-498 by PKC/PRKCA positively regulates its catalytic activity. {ECO:0000269|PubMed:21642394, ECO:0000269|PubMed:24505490}.; PTM: [Isoform v2]: S-nitrosylation in response to nitric oxide inhibits its catalytic activity. {ECO:0000269|PubMed:22387196}.
uniprot
proteins
pubmed
11376945
uniprot
proteins
pubmed
11483596
uniprot
proteins
pubmed
12686516
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14982937
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15994299
uniprot
proteins
pubmed
16179589
uniprot
proteins
pubmed
16339585
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
17275676
uniprot
proteins
pubmed
17587483
uniprot
proteins
pubmed
21319793
uniprot
proteins
pubmed
21642394
uniprot
proteins
pubmed
22387196
uniprot
proteins
pubmed
22427510
uniprot
proteins
pubmed
24505490
uniprot
proteins
pubmed
31785178
uniprot
proteins
pubmed
34784249
uniprot
proteins
pubmed
36653838
uniprot
proteins
sequence_length
765
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform v2]: Endoplasmic reticulum {ECO:0000269|PubMed:17275676, ECO:0000269|PubMed:17587483}. Cell membrane {ECO:0000269|PubMed:17587483, ECO:0000269|PubMed:36653838}; Multi-pass membrane protein {ECO:0000255}. Note=Calcium-sensitive association and dissociation between the N- and C-terminal domains appears to facilitate its localization to the cell membrane. {ECO:0000269|PubMed:36653838}.; SUBCELLULAR LOCATION: [Isoform v5]: Endoplasmic reticulum {ECO:0000269|PubMed:17275676}.
uniprot
proteins
transmembrane_region
TRANSMEM 239..259; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 267..289; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 318..338; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 363..383; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 395..417; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 435..455; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 584..604; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins