LOCUS       NP_445976                578 aa            linear   ROD 03-APR-2024
DEFINITION  NADPH oxidase 4 [Rattus norvegicus].
ACCESSION   NP_445976
VERSION     NP_445976.1
DBSOURCE    REFSEQ: accession NM_053524.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Li,S., Lyu,Q., Shi,Q., Bai,Y., Ren,X. and Ma,J.
  TITLE     Intermittent short-duration reoxygenation relieves high-altitude
            pulmonary hypertension via NOX4/H2O2/PPAR-gamma axis
  JOURNAL   Clin Sci (Lond) 138 (3), 103-115 (2024)
   PUBMED   38237016
  REMARK    GeneRIF: Intermittent short-duration reoxygenation relieves
            high-altitude pulmonary hypertension via NOX4/H2O2/PPAR-gamma axis.
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Naser,N., Lonj,C.K., Rikard-Bell,M., Sandow,S.L. and Murphy,T.V.
  TITLE     Advanced glycated end-products inhibit dilation through
            constitutive endothelial RAGE and Nox1/4 in rat isolated skeletal
            muscle arteries
  JOURNAL   Microcirculation 31 (1), e12837 (2024)
   PUBMED   37985248
  REMARK    GeneRIF: Advanced glycated end-products inhibit dilation through
            constitutive endothelial RAGE and Nox1/4 in rat isolated skeletal
            muscle arteries.
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Matsunaga,S., Kohda,A., Kamakura,S., Hayase,J., Miyano,K.,
            Shiose,A. and Sumimoto,H.
  TITLE     Hypoxia stabilizes the H2 O2 -producing oxidase Nox4 in
            cardiomyocytes via suppressing autophagy-related lysosomal
            degradation
  JOURNAL   Genes Cells 29 (1), 63-72 (2024)
   PUBMED   37985134
  REMARK    GeneRIF: Hypoxia stabilizes the H2 O2 -producing oxidase Nox4 in
            cardiomyocytes via suppressing autophagy-related lysosomal
            degradation.
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Zhang,Y., Shan,M., Ding,X., Sun,H., Qiu,F. and Shi,L.
  TITLE     Maternal exercise represses Nox4 via SIRT1 to prevent vascular
            oxidative stress and endothelial dysfunction in SHR offspring
  JOURNAL   Front Endocrinol (Lausanne) 14, 1219194 (2023)
   PUBMED   37501791
  REMARK    GeneRIF: Maternal exercise represses Nox4 via SIRT1 to prevent
            vascular oxidative stress and endothelial dysfunction in SHR
            offspring.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Sun,Z.H., Liu,F., Kong,L.L., Ji,P.M., Huang,L., Zhou,H.M., Sun,R.,
            Luo,J. and Li,W.Z.
  TITLE     Interruption of TRPC6-NFATC1 signaling inhibits NADPH oxidase 4 and
            VSMCs phenotypic switch in intracranial aneurysm
  JOURNAL   Biomed Pharmacother 161, 114480 (2023)
   PUBMED   37002575
  REMARK    GeneRIF: Interruption of TRPC6-NFATC1 signaling inhibits NADPH
            oxidase 4 and VSMCs phenotypic switch in intracranial aneurysm.
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Gorin,Y., Ricono,J.M., Kim,N.H., Bhandari,B., Choudhury,G.G. and
            Abboud,H.E.
  TITLE     Nox4 mediates angiotensin II-induced activation of Akt/protein
            kinase B in mesangial cells
  JOURNAL   Am J Physiol Renal Physiol 285 (2), F219-F229 (2003)
   PUBMED   12842860
  REMARK    GeneRIF: Nox4-based NAD(P)H oxidase and generation of reactive
            oxygen species mediate the effect of ANG II on Akt/PKB activation
            and protein synthesis in glomerular mesangial cells
REFERENCE   7  (residues 1 to 578)
  AUTHORS   Lassegue,B., Sorescu,D., Szocs,K., Yin,Q., Akers,M., Zhang,Y.,
            Grant,S.L., Lambeth,J.D. and Griendling,K.K.
  TITLE     Novel gp91(phox) homologues in vascular smooth muscle cells : nox1
            mediates angiotensin II-induced superoxide formation and
            redox-sensitive signaling pathways
  JOURNAL   Circ Res 88 (9), 888-894 (2001)
   PUBMED   11348997
REFERENCE   8  (residues 1 to 578)
  AUTHORS   Yang,S., Madyastha,P., Bingel,S., Ries,W. and Key,L.
  TITLE     A new superoxide-generating oxidase in murine osteoclasts
  JOURNAL   J Biol Chem 276 (8), 5452-5458 (2001)
   PUBMED   11098048
REFERENCE   9  (residues 1 to 578)
  AUTHORS   Shiose,A., Kuroda,J., Tsuruya,K., Hirai,M., Hirakata,H., Naito,S.,
            Hattori,M., Sakaki,Y. and Sumimoto,H.
  TITLE     A novel superoxide-producing NAD(P)H oxidase in kidney
  JOURNAL   J Biol Chem 276 (2), 1417-1423 (2001)
   PUBMED   11032835
REFERENCE   10 (residues 1 to 578)
  AUTHORS   Geiszt,M., Kopp,J.B., Varnai,P. and Leto,T.L.
  TITLE     Identification of renox, an NAD(P)H oxidase in kidney
  JOURNAL   Proc Natl Acad Sci U S A 97 (14), 8010-8014 (2000)
   PUBMED   10869423
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY027527.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY027527.1, AB044086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..578
                     /product="NADPH oxidase 4"
                     /EC_number="1.6.3.1"
                     /note="kox-1; kidney superoxide-producing NADPH oxidase;
                     kidney oxidase-1"
                     /calculated_mol_wt=66338
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924V1.2)"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924V1.2)"
     Region          69..205
                     /region_name="Ferric_reduct"
                     /note="Ferric reductase like transmembrane component;
                     pfam01794"
                     /db_xref="CDD:426438"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924V1.2)"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q924V1.2)"
     Site            155..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924V1.2)"
     Site            189..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924V1.2)"
     Region          218..273
                     /region_name="E-loop, essential for H2O2 generating
                     catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:Q9NPH5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924V1.2)"
     Region          248..575
                     /region_name="Mediates interaction with TLR4.
                     /evidence=ECO:0000250|UniProtKB:Q9NPH5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924V1.2)"
     Region          311..577
                     /region_name="NOX_Duox_like_FAD_NADP"
                     /note="NADPH oxidase (NOX) catalyzes the generation of
                     reactive oxygen species (ROS) such as superoxide and
                     hydrogen peroxide. ROS were originally identified as
                     bactericidal agents in phagocytes, but are now also
                     implicated in cell signaling and metabolism. NOX...;
                     cd06186"
                     /db_xref="CDD:99783"
     Site            order(338,352..355,370..372,375..378,433)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99783"
     Site            order(352,354..355)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99783"
     Site            425..445
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924V1.2)"
     Site            428..438
                     /site_type="other"
                     /note="NAD pyrophosphate binding region [chemical
                     binding]"
                     /db_xref="CDD:99783"
     Site            order(428,432..435,437)
                     /site_type="other"
                     /note="beta-alpha-beta stucture motif"
                     /db_xref="CDD:99783"
     Site            order(433..434,462..464,548..549)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99783"
     Site            order(460..461,464)
                     /site_type="other"
                     /note="NADP ribose binding motif [chemical binding]"
                     /db_xref="CDD:99783"
     CDS             1..578
                     /gene="Nox4"
                     /coded_by="NM_053524.1:50..1786"
                     /db_xref="GeneID:85431"
                     /db_xref="RGD:620600"
ORIGIN      
        1 malswrswla negvkhlcll vwlslnvllf wktfllynqg peyyyihqml glglclsras
       61 asvlnlncsl illpmcrtvl aylrgsqkvp srrtrrlldk sktlhitcgi ticifsgvhv
      121 aahlvnalnf svnysehfla lnaaryqned prkllfttvp gltgvcmvvv lflmvtasty
      181 airvsnydif wythnlffvf ymllllhvsg gllkyqtnld thppgcisln rtpsqnmsia
      241 dyvsehfhgs lpggfskled hyqktlvkic leepkfqahf pqtwiwisgp lclycaerly
      301 rcirsnkpvt iisvinhpsd vmelrmiken fkarpgqyii lhcpsvsale nhpftltmcp
      361 tetkatfgvh fkvvgdwter frdlllppss qdseilpfiq srnypklyid gpfgspfees
      421 lnyevslcva ggigvtpfas ilntllddwk pyklrrlyfi wvcrdiqsfq wfadllyvlh
      481 nkfwqenrpd fvniqlylsq tdgiqkiige kyhtlnsrlf igrprwkllf deiakcnrgk
      541 tvgvfccgps sisktlhnls nrnnsygtkf eynkesfs
//
