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NADPH oxidase 4 (EC 1.6.3.-) (Kidney oxidase-1) (KOX-1) (Kidney superoxide-producing NADPH oxidase) (Renal NAD(P)H-oxidase)

 NOX4_HUMAN              Reviewed;         578 AA.
Q9NPH5; A8K715; B7Z520; E7EMD7; Q5K3R4; Q5K3R5; Q5K3R6; Q5K3R8;
Q7Z7G3; Q86V92;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 2.
25-OCT-2017, entry version 136.
RecName: Full=NADPH oxidase 4;
EC=1.6.3.-;
AltName: Full=Kidney oxidase-1;
Short=KOX-1;
AltName: Full=Kidney superoxide-producing NADPH oxidase;
AltName: Full=Renal NAD(P)H-oxidase;
Name=NOX4; Synonyms=RENOX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND
VARIANT ILE-315.
TISSUE=Kidney;
PubMed=10869423; DOI=10.1073/pnas.130135897;
Geiszt M., Kopp J.B., Varnai P., Leto T.L.;
"Identification of renox, an NAD(P)H oxidase in kidney.";
Proc. Natl. Acad. Sci. U.S.A. 97:8010-8014(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND VARIANT ILE-315.
TISSUE=Fetal kidney;
PubMed=11376945; DOI=10.1016/S0378-1119(01)00449-8;
Cheng G., Cao Z., Xu X., van Meir E.G., Lambeth J.D.;
"Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4,
and Nox5.";
Gene 269:131-140(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND VARIANT ILE-315.
TISSUE=Kidney;
PubMed=11032835; DOI=10.1074/jbc.M007597200;
Shiose A., Kuroda J., Tsuruya K., Hirai M., Hirakata H., Naito S.,
Hattori M., Sakaki Y., Sumimoto H.;
"A novel superoxide-producing NAD(P)H oxidase in kidney.";
J. Biol. Chem. 276:1417-1423(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, AND
VARIANT ILE-315.
PubMed=15210697; DOI=10.1074/jbc.M404983200;
Schwarzer C., Machen T.E., Illek B., Fischer H.;
"NADPH oxidase-dependent acid production in airway epithelial cells.";
J. Biol. Chem. 279:36454-36461(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), FUNCTION,
SUBCELLULAR LOCATION, GLYCOSYLATION, AND VARIANT ILE-315.
TISSUE=Lung;
PubMed=15721269; DOI=10.1016/j.bbrc.2005.01.089;
Goyal P., Weissmann N., Rose F., Grimminger F., Schaefers H.J.,
Seeger W., Haenze J.;
"Identification of novel Nox4 splice variants with impact on ROS
levels in A549 cells.";
Biochem. Biophys. Res. Commun. 329:32-39(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 9), AND VARIANT
ILE-315.
TISSUE=Pulmonary artery;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7), AND VARIANT
ILE-315.
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION.
PubMed=15155719; DOI=10.1074/jbc.M400078200;
Vaquero E.C., Edderkaoui M., Pandol S.J., Gukovsky I.,
Gukovskaya A.S.;
"Reactive oxygen species produced by NAD(P)H oxidase inhibit apoptosis
in pancreatic cancer cells.";
J. Biol. Chem. 279:34643-34654(2004).
[10]
FUNCTION, AND INTERACTION WITH TLR4.
PubMed=15356101; DOI=10.4049/jimmunol.173.6.3589;
Park H.S., Jung H.Y., Park E.Y., Kim J., Lee W.J., Bae Y.S.;
"Direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is
essential for lipopolysaccharide-induced production of reactive oxygen
species and activation of NF-kappa B.";
J. Immunol. 173:3589-3593(2004).
[11]
FUNCTION, AND ENZYME REGULATION.
PubMed=14966267; DOI=10.1128/MCB.24.5.1844-1854.2004;
Mahadev K., Motoshima H., Wu X., Ruddy J.M., Arnold R.S., Cheng G.,
Lambeth J.D., Goldstein B.J.;
"The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated
generation of H2O2 and plays an integral role in insulin signal
transduction.";
Mol. Cell. Biol. 24:1844-1854(2004).
[12]
FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=15572675; DOI=10.1128/MCB.24.24.10703-10717.2004;
Pedruzzi E., Guichard C., Ollivier V., Driss F., Fay M., Prunet C.,
Marie J.-C., Pouzet C., Samadi M., Elbim C., O'dowd Y., Bens M.,
Vandewalle A., Gougerot-Pocidalo M.-A., Lizard G., Ogier-Denis E.;
"NAD(P)H oxidase Nox-4 mediates 7-ketocholesterol-induced endoplasmic
reticulum stress and apoptosis in human aortic smooth muscle cells.";
Mol. Cell. Biol. 24:10703-10717(2004).
[13]
FUNCTION.
PubMed=16230378; DOI=10.1158/0008-5472.CAN-05-2105;
Maranchie J.K., Zhan Y.;
"Nox4 is critical for hypoxia-inducible factor 2-alpha transcriptional
activity in von Hippel-Lindau-deficient renal cell carcinoma.";
Cancer Res. 65:9190-9193(2005).
[14]
FUNCTION.
PubMed=16179589; DOI=10.1161/01.RES.0000187457.24338.3D;
Cucoranu I., Clempus R., Dikalova A., Phelan P.J., Ariyan S.,
Dikalov S., Sorescu D.;
"NAD(P)H oxidase 4 mediates transforming growth factor-beta1-induced
differentiation of cardiac fibroblasts into myofibroblasts.";
Circ. Res. 97:900-907(2005).
[15]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ENZYME
REGULATION.
PubMed=16324151; DOI=10.1111/j.1365-2443.2005.00907.x;
Kuroda J., Nakagawa K., Yamasaki T., Nakamura K., Takeya R.,
Kuribayashi F., Imajoh-Ohmi S., Igarashi K., Shibata Y., Sueishi K.,
Sumimoto H.;
"The superoxide-producing NAD(P)H oxidase Nox4 in the nucleus of human
vascular endothelial cells.";
Genes Cells 10:1139-1151(2005).
[16]
FUNCTION, INTERACTION WITH CYBA, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF ARG-304 AND 575-GLU--SER-578.
PubMed=15927447; DOI=10.1016/j.cellsig.2005.03.023;
Martyn K.D., Frederick L.M., von Loehneysen K., Dinauer M.C.,
Knaus U.G.;
"Functional analysis of Nox4 reveals unique characteristics compared
to other NADPH oxidases.";
Cell. Signal. 18:69-82(2006).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=16019190; DOI=10.1016/j.cellsig.2005.05.025;
Lee Y.-M., Kim B.-J., Chun Y.-S., So I., Choi H., Kim M.-S.,
Park J.-W.;
"NOX4 as an oxygen sensor to regulate TASK-1 activity.";
Cell. Signal. 18:499-507(2006).
[18]
FUNCTION (ISOFORM 4), AND SUBCELLULAR LOCATION (ISOFORM 4).
PubMed=23393389; DOI=10.1161/ATVBAHA.112.300956;
Anilkumar N., San Jose G., Sawyer I., Santos C.X., Sand C.,
Brewer A.C., Warren D., Shah A.M.;
"A 28-kDa splice variant of NADPH oxidase-4 is nuclear-localized and
involved in redox signaling in vascular cells.";
Arterioscler. Thromb. Vasc. Biol. 33:E104-E112(2013).
-!- FUNCTION: Constitutive NADPH oxidase which generates superoxide
intracellularly upon formation of a complex with CYBA/p22phox.
Regulates signaling cascades probably through phosphatases
inhibition. May function as an oxygen sensor regulating the
KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate
insulin signaling cascade. May play a role in apoptosis, bone
resorption and lipolysaccharide-mediated activation of NFKB. May
produce superoxide in the nucleus and play a role in regulating
gene expression upon cell stimulation. Isoform 3 is not
functional. Isoform 5 and isoform 6 display reduced activity.
-!- FUNCTION: Isoform 4: Involved in redox signaling in vascular
cells. Constitutively and NADPH-dependently generates reactive
oxygen species (ROS). Modulates the nuclear activation of ERK1/2
and the ELK1 transcription factor, and is capable of inducing
nuclear DNA damage. Displays an increased activity relative to
isoform 1.
-!- ENZYME REGULATION: Inhibited by plumbagin (By similarity).
Activated by phorbol 12-myristate 13-acetate (PMA). Activated by
insulin. Inhibited by diphenylene iodonium. {ECO:0000250,
ECO:0000269|PubMed:14966267, ECO:0000269|PubMed:15572675,
ECO:0000269|PubMed:16019190, ECO:0000269|PubMed:16324151}.
-!- SUBUNIT: Interacts with protein disulfide isomerase (By
similarity). Interacts with, relocalizes and stabilizes
CYBA/p22phox. Interacts with TLR4. {ECO:0000250,
ECO:0000269|PubMed:15356101, ECO:0000269|PubMed:15927447}.
-!- INTERACTION:
O00206:TLR4; NbExp=4; IntAct=EBI-11301574, EBI-528701;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein. Cell membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Cell junction, focal adhesion
{ECO:0000305}. Note=May localize to plasma membrane and focal
adhesions. According to PubMed:15927447, may also localize to the
nucleus.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus
{ECO:0000269|PubMed:23393389}. Nucleus, nucleolus
{ECO:0000269|PubMed:23393389}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=1;
IsoId=Q9NPH5-1; Sequence=Displayed;
Name=2; Synonyms=Nox4A;
IsoId=Q9NPH5-2; Sequence=VSP_019052;
Name=3; Synonyms=Nox4E;
IsoId=Q9NPH5-3; Sequence=VSP_019053, VSP_019058;
Name=4; Synonyms=28 kDa, Nox4D;
IsoId=Q9NPH5-4; Sequence=VSP_019053;
Name=5; Synonyms=Nox4C;
IsoId=Q9NPH5-5; Sequence=VSP_019056, VSP_019057;
Name=6; Synonyms=Nox4B;
IsoId=Q9NPH5-6; Sequence=VSP_019058;
Name=7;
IsoId=Q9NPH5-7; Sequence=VSP_019054, VSP_019055;
Name=8;
IsoId=Q9NPH5-8; Sequence=VSP_053826;
Name=9;
IsoId=Q9NPH5-9; Sequence=VSP_053826, VSP_019058;
-!- TISSUE SPECIFICITY: Expressed by distal tubular cells in kidney
cortex and in endothelial cells (at protein level). Widely
expressed. Strongly expressed in kidney and to a lower extent in
heart, adipocytes, hepatoma, endothelial cells, skeletal muscle,
brain, several brain tumor cell lines and airway epithelial cells.
{ECO:0000269|PubMed:11032835, ECO:0000269|PubMed:11376945,
ECO:0000269|PubMed:15210697, ECO:0000269|PubMed:16324151}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal kidney and fetal liver.
{ECO:0000269|PubMed:10869423, ECO:0000269|PubMed:11032835,
ECO:0000269|PubMed:11376945}.
-!- INDUCTION: By 7-ketocholesterol (at protein level).
{ECO:0000269|PubMed:15572675}.
-!- PTM: Isoform 3 and isoform 4 are N-glycosylated. Isoform 4
glycosylation is required for its proper function.
{ECO:0000269|PubMed:15721269}.
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EMBL; AF261943; AAF87572.1; -; mRNA.
EMBL; AF254621; AAF68973.1; -; mRNA.
EMBL; AB041035; BAA95695.1; -; mRNA.
EMBL; AY288918; AAP41109.1; -; mRNA.
EMBL; AJ704725; CAG28807.1; -; mRNA.
EMBL; AJ704726; CAG28808.1; -; mRNA.
EMBL; AJ704727; CAG28809.1; -; mRNA.
EMBL; AJ704728; CAG28810.1; -; mRNA.
EMBL; AJ704729; CAG28811.1; -; mRNA.
EMBL; AK291830; BAF84519.1; -; mRNA.
EMBL; AK298323; BAH12756.1; -; mRNA.
EMBL; AP003400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC040105; AAH40105.1; -; mRNA.
EMBL; BC051371; AAH51371.1; -; mRNA.
CCDS; CCDS44695.1; -. [Q9NPH5-6]
CCDS; CCDS44696.1; -. [Q9NPH5-8]
CCDS; CCDS73361.1; -. [Q9NPH5-9]
CCDS; CCDS8285.1; -. [Q9NPH5-1]
RefSeq; NP_001137308.1; NM_001143836.2.
RefSeq; NP_001137309.1; NM_001143837.1.
RefSeq; NP_001278855.1; NM_001291926.1.
RefSeq; NP_001278856.1; NM_001291927.1.
RefSeq; NP_001287924.1; NM_001300995.1. [Q9NPH5-9]
RefSeq; NP_058627.1; NM_016931.4.
RefSeq; XP_011541159.1; XM_011542857.2. [Q9NPH5-8]
UniGene; Hs.371036; -.
ProteinModelPortal; Q9NPH5; -.
SMR; Q9NPH5; -.
BioGrid; 119078; 2.
IntAct; Q9NPH5; 1.
STRING; 9606.ENSP00000263317; -.
BindingDB; Q9NPH5; -.
ChEMBL; CHEMBL1250375; -.
PeroxiBase; 5967; HsNOx04.
TCDB; 5.B.1.1.2; the phagocyte (gp91(phox)) nadph oxidase family.
iPTMnet; Q9NPH5; -.
PhosphoSitePlus; Q9NPH5; -.
BioMuta; NOX4; -.
DMDM; 212276447; -.
PaxDb; Q9NPH5; -.
PeptideAtlas; Q9NPH5; -.
PRIDE; Q9NPH5; -.
DNASU; 50507; -.
Ensembl; ENST00000263317; ENSP00000263317; ENSG00000086991. [Q9NPH5-1]
Ensembl; ENST00000343727; ENSP00000344747; ENSG00000086991. [Q9NPH5-8]
Ensembl; ENST00000375979; ENSP00000365146; ENSG00000086991. [Q9NPH5-4]
Ensembl; ENST00000393282; ENSP00000376961; ENSG00000086991. [Q9NPH5-7]
Ensembl; ENST00000424319; ENSP00000412446; ENSG00000086991. [Q9NPH5-8]
Ensembl; ENST00000527956; ENSP00000433797; ENSG00000086991. [Q9NPH5-8]
Ensembl; ENST00000529343; ENSP00000435474; ENSG00000086991. [Q9NPH5-5]
Ensembl; ENST00000531342; ENSP00000435039; ENSG00000086991. [Q9NPH5-3]
Ensembl; ENST00000532825; ENSP00000434924; ENSG00000086991. [Q9NPH5-9]
Ensembl; ENST00000534731; ENSP00000436892; ENSG00000086991. [Q9NPH5-6]
GeneID; 50507; -.
KEGG; hsa:50507; -.
UCSC; uc001pct.4; human. [Q9NPH5-1]
CTD; 50507; -.
DisGeNET; 50507; -.
EuPathDB; HostDB:ENSG00000086991.12; -.
GeneCards; NOX4; -.
HGNC; HGNC:7891; NOX4.
HPA; HPA015475; -.
MIM; 605261; gene.
neXtProt; NX_Q9NPH5; -.
OpenTargets; ENSG00000086991; -.
PharmGKB; PA31692; -.
eggNOG; KOG0039; Eukaryota.
eggNOG; ENOG410XNZY; LUCA.
GeneTree; ENSGT00550000074350; -.
HOGENOM; HOG000216669; -.
HOVERGEN; HBG003760; -.
InParanoid; Q9NPH5; -.
KO; K21423; -.
OMA; FCCGPNS; -.
OrthoDB; EOG091G09RV; -.
PhylomeDB; Q9NPH5; -.
TreeFam; TF105354; -.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
SIGNOR; Q9NPH5; -.
GeneWiki; NOX4; -.
GenomeRNAi; 50507; -.
PRO; PR:Q9NPH5; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000086991; -.
CleanEx; HS_NOX4; -.
ExpressionAtlas; Q9NPH5; baseline and differential.
Genevisible; Q9NPH5; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043020; C:NADPH oxidase complex; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; TAS:UniProtKB.
GO; GO:0020037; F:heme binding; TAS:UniProtKB.
GO; GO:0072341; F:modified amino acid binding; IDA:UniProtKB.
GO; GO:0016174; F:NAD(P)H oxidase activity; TAS:UniProtKB.
GO; GO:0000166; F:nucleotide binding; TAS:UniProtKB.
GO; GO:0019826; F:oxygen sensor activity; TAS:UniProtKB.
GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; TAS:Reactome.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0007569; P:cell aging; ISS:UniProtKB.
GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0010467; P:gene expression; IMP:CACAO.
GO; GO:0050667; P:homocysteine metabolic process; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0042554; P:superoxide anion generation; ISS:UniProtKB.
GO; GO:0006801; P:superoxide metabolic process; IDA:CACAO.
InterPro; IPR000778; Cyt_b245_heavy_chain.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
PRINTS; PR00466; GP91PHOX.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane; NADP;
Nucleus; Oxidoreductase; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 578 NADPH oxidase 4.
/FTId=PRO_0000238980.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 37 Helical. {ECO:0000255}.
TOPO_DOM 38 62 Extracellular. {ECO:0000255}.
TRANSMEM 63 83 Helical. {ECO:0000255}.
TOPO_DOM 84 103 Cytoplasmic. {ECO:0000255}.
TRANSMEM 104 124 Helical. {ECO:0000255}.
TOPO_DOM 125 154 Extracellular. {ECO:0000255}.
TRANSMEM 155 175 Helical. {ECO:0000255}.
TOPO_DOM 176 188 Cytoplasmic. {ECO:0000255}.
TRANSMEM 189 209 Helical. {ECO:0000255}.
TOPO_DOM 210 424 Extracellular. {ECO:0000255}.
TRANSMEM 425 445 Helical. {ECO:0000255}.
TOPO_DOM 446 578 Cytoplasmic. {ECO:0000255}.
DOMAIN 58 303 Ferric oxidoreductase.
DOMAIN 304 419 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
REGION 248 575 Mediates interaction with TLR4.
{ECO:0000269|PubMed:15356101}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 74 Missing (in isoform 2).
{ECO:0000303|PubMed:15721269}.
/FTId=VSP_019052.
VAR_SEQ 1 24 Missing (in isoform 8 and isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053826.
VAR_SEQ 52 358 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15721269}.
/FTId=VSP_019053.
VAR_SEQ 52 54 LGL -> ELS (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019054.
VAR_SEQ 55 578 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019055.
VAR_SEQ 211 224 GLLKYQTNLDTHPP -> VQLKPKQHLGFILK (in
isoform 5).
{ECO:0000303|PubMed:15721269}.
/FTId=VSP_019056.
VAR_SEQ 225 578 Missing (in isoform 5).
{ECO:0000303|PubMed:15721269}.
/FTId=VSP_019057.
VAR_SEQ 407 446 Missing (in isoform 3, isoform 6 and
isoform 9). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15210697,
ECO:0000303|PubMed:15721269}.
/FTId=VSP_019058.
VARIANT 315 315 M -> I (in dbSNP:rs317139).
{ECO:0000269|PubMed:10869423,
ECO:0000269|PubMed:11032835,
ECO:0000269|PubMed:11376945,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15210697,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15721269}.
/FTId=VAR_047114.
MUTAGEN 304 304 R->RGT: Partial loss of catalytic
activity. No effect on CYBA localization.
{ECO:0000269|PubMed:15927447}.
MUTAGEN 575 578 Missing: Partial loss of catalytic
activity. No effect on CYBA localization.
{ECO:0000269|PubMed:15927447}.
CONFLICT 286 286 W -> C (in Ref. 6; BAH12756).
{ECO:0000305}.
SEQUENCE 578 AA; 66932 MW; D150A92CC71DD40D CRC64;
MAVSWRSWLA NEGVKHLCLF IWLSMNVLLF WKTFLLYNQG PEYHYLHQML GLGLCLSRAS
ASVLNLNCSL ILLPMCRTLL AYLRGSQKVP SRRTRRLLDK SRTFHITCGV TICIFSGVHV
AAHLVNALNF SVNYSEDFVE LNAARYRDED PRKLLFTTVP GLTGVCMVVV LFLMITASTY
AIRVSNYDIF WYTHNLFFVF YMLLTLHVSG GLLKYQTNLD THPPGCISLN RTSSQNISLP
EYFSEHFHEP FPEGFSKPAE FTQHKFVKIC MEEPRFQANF PQTWLWISGP LCLYCAERLY
RYIRSNKPVT IISVMSHPSD VMEIRMVKEN FKARPGQYIT LHCPSVSALE NHPFTLTMCP
TETKATFGVH LKIVGDWTER FRDLLLPPSS QDSEILPFIQ SRNYPKLYID GPFGSPFEES
LNYEVSLCVA GGIGVTPFAS ILNTLLDDWK PYKLRRLYFI WVCRDIQSFR WFADLLCMLH
NKFWQENRPD YVNIQLYLSQ TDGIQKIIGE KYHALNSRLF IGRPRWKLLF DEIAKYNRGK
TVGVFCCGPN SLSKTLHKLS NQNNSYGTRF EYNKESFS


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