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NADPH oxidase 4 (EC 1.6.3.-) (Kidney oxidase-1) (KOX-1) (Kidney superoxide-producing NADPH oxidase)

 NOX4_RAT                Reviewed;         578 AA.
Q924V1; Q99M78;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 2.
18-JUL-2018, entry version 94.
RecName: Full=NADPH oxidase 4;
EC=1.6.3.-;
AltName: Full=Kidney oxidase-1;
Short=KOX-1;
AltName: Full=Kidney superoxide-producing NADPH oxidase;
Name=Nox4; Synonyms=Kox;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Vascular smooth muscle;
PubMed=11348997; DOI=10.1161/hh0901.090299;
Lassegue B., Sorescu D., Szoecs K., Yin Q., Akers M., Zhang Y.,
Grant S.L., Lambeth J.D., Griendling K.K.;
"Novel gp91(phox) homologues in vascular smooth muscle cells: nox1
mediates angiotensin II-induced superoxide formation and redox-
sensitive signaling pathways.";
Circ. Res. 88:888-894(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[3]
SUBCELLULAR LOCATION.
PubMed=14670934; DOI=10.1161/01.ATV.0000112024.13727.2c;
Hilenski L.L., Clempus R.E., Quinn M.T., Lambeth J.D.,
Griendling K.K.;
"Distinct subcellular localizations of Nox1 and Nox4 in vascular
smooth muscle cells.";
Arterioscler. Thromb. Vasc. Biol. 24:677-683(2004).
[4]
FUNCTION, INTERACTION WITH CYBA, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF HIS-119.
PubMed=15322091; DOI=10.1074/jbc.M406486200;
Ambasta R.K., Kumar P., Griendling K.K., Schmidt H.H.H.W., Busse R.,
Brandes R.P.;
"Direct interaction of the novel Nox proteins with p22phox is required
for the formation of a functionally active NADPH oxidase.";
J. Biol. Chem. 279:45935-45941(2004).
[5]
FUNCTION, AND INDUCTION.
PubMed=16135519; DOI=10.1074/jbc.M502412200;
Gorin Y., Block K., Hernandez J., Bhandari B., Wagner B., Barnes J.L.,
Abboud H.E.;
"Nox4 NAD(P)H oxidase mediates hypertrophy and fibronectin expression
in the diabetic kidney.";
J. Biol. Chem. 280:39616-39626(2005).
[6]
INTERACTION WITH PROTEIN DISULFIDE ISOMERASE, AND SUBCELLULAR
LOCATION.
PubMed=16150729; DOI=10.1074/jbc.M509255200;
Janiszewski M., Lopes L.R., Carmo A.O., Pedro M.A., Brandes R.P.,
Santos C.X.C., Laurindo F.R.M.;
"Regulation of NAD(P)H oxidase by associated protein disulfide
isomerase in vascular smooth muscle cells.";
J. Biol. Chem. 280:40813-40819(2005).
-!- 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.
{ECO:0000269|PubMed:15322091, ECO:0000269|PubMed:16135519}.
-!- ENZYME REGULATION: Activated by insulin. Inhibited by diphenylene
iodonium. Inhibited by plumbagin. Activated by phorbol 12-
myristate 13-acetate (PMA) (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with TLR4 (By similarity). Interacts with,
relocalizes and stabilizes CYBA/p22phox. Interacts with protein
disulfide isomerase. {ECO:0000250, ECO:0000269|PubMed:15322091,
ECO:0000269|PubMed:16150729}.
-!- 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.
-!- TISSUE SPECIFICITY: Expressed in vascular smooth muscle.
{ECO:0000269|PubMed:11348997}.
-!- INDUCTION: Up-regulated in diabetic kidney (at protein level).
{ECO:0000269|PubMed:16135519}.
-!- PTM: N-glycosylation is required for the function. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AY027527; AAK14799.1; -; mRNA.
EMBL; AB044086; BAB61724.1; -; mRNA.
RefSeq; NP_445976.1; NM_053524.1.
UniGene; Rn.14744; -.
ProteinModelPortal; Q924V1; -.
SMR; Q924V1; -.
BioGrid; 250101; 2.
STRING; 10116.ENSRNOP00000018990; -.
PeroxiBase; 5409; RnoNOx04.
PhosphoSitePlus; Q924V1; -.
PaxDb; Q924V1; -.
PRIDE; Q924V1; -.
Ensembl; ENSRNOT00000018990; ENSRNOP00000018990; ENSRNOG00000013925.
GeneID; 85431; -.
KEGG; rno:85431; -.
UCSC; RGD:620600; rat.
CTD; 50507; -.
RGD; 620600; Nox4.
eggNOG; KOG0039; Eukaryota.
eggNOG; ENOG410XNZY; LUCA.
GeneTree; ENSGT00550000074350; -.
HOGENOM; HOG000216669; -.
HOVERGEN; HBG003760; -.
InParanoid; Q924V1; -.
KO; K21423; -.
OMA; FCCGPNS; -.
OrthoDB; EOG091G09RV; -.
BRENDA; 1.6.3.1; 5301.
Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:Q924V1; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000013925; -.
Genevisible; Q924V1; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:ARUK-UCL.
GO; GO:0043020; C:NADPH oxidase complex; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:ARUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ARUK-UCL.
GO; GO:0072341; F:modified amino acid binding; IEA:Ensembl.
GO; GO:0016174; F:NAD(P)H oxidase activity; IDA:RGD.
GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IDA:RGD.
GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
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; IEP:RGD.
GO; GO:0071480; P:cellular response to gamma radiation; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
GO; GO:0010467; P:gene expression; IEA:Ensembl.
GO; GO:0003015; P:heart process; IEA:Ensembl.
GO; GO:0050667; P:homocysteine metabolic process; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
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:0061098; P:positive regulation of protein tyrosine kinase activity; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:RGD.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:RGD.
GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0042554; P:superoxide anion generation; ISS:UniProtKB.
GO; GO:0006801; P:superoxide metabolic process; IDA:RGD.
Gene3D; 3.40.50.80; -; 1.
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; IPR039261; FNR_nucleotide_bd.
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; SSF52343; SSF52343; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Membrane; NADP; Oxidoreductase;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 578 NADPH oxidase 4.
/FTId=PRO_0000238983.
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 84 104 Cytoplasmic. {ECO:0000255}.
TRANSMEM 105 125 Helical. {ECO:0000255}.
TOPO_DOM 126 154 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:0000250}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 119 119 H->L: Loss of interaction with
CYBA/p22phox.
{ECO:0000269|PubMed:15322091}.
CONFLICT 232 232 T -> P (in Ref. 2; BAB61724).
{ECO:0000305}.
SEQUENCE 578 AA; 66469 MW; 474347299F994D92 CRC64;
MALSWRSWLA NEGVKHLCLL VWLSLNVLLF WKTFLLYNQG PEYYYIHQML GLGLCLSRAS
ASVLNLNCSL ILLPMCRTVL AYLRGSQKVP SRRTRRLLDK SKTLHITCGI TICIFSGVHV
AAHLVNALNF SVNYSEHFLA LNAARYQNED PRKLLFTTVP GLTGVCMVVV LFLMVTASTY
AIRVSNYDIF WYTHNLFFVF YMLLLLHVSG GLLKYQTNLD THPPGCISLN RTPSQNMSIA
DYVSEHFHGS LPGGFSKLED HYQKTLVKIC LEEPKFQAHF PQTWIWISGP LCLYCAERLY
RCIRSNKPVT IISVINHPSD VMELRMIKEN FKARPGQYII LHCPSVSALE NHPFTLTMCP
TETKATFGVH FKVVGDWTER FRDLLLPPSS QDSEILPFIQ SRNYPKLYID GPFGSPFEES
LNYEVSLCVA GGIGVTPFAS ILNTLLDDWK PYKLRRLYFI WVCRDIQSFQ WFADLLYVLH
NKFWQENRPD FVNIQLYLSQ TDGIQKIIGE KYHTLNSRLF IGRPRWKLLF DEIAKCNRGK
TVGVFCCGPS SISKTLHNLS NRNNSYGTKF EYNKESFS


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