ID NOX1_HUMAN Reviewed; 564 AA. AC Q9Y5S8; A8K836; O95691; Q2PP02; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 2. DT 27-MAR-2024, entry version 197. DE RecName: Full=NADPH oxidase 1; DE Short=NOX-1; DE EC=1.6.3.-; DE AltName: Full=Mitogenic oxidase 1; DE Short=MOX-1; DE AltName: Full=NADH/NADPH mitogenic oxidase subunit P65-MOX; DE AltName: Full=NOH-1; GN Name=NOX1; Synonyms=MOX1, NOH1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NOH-1L), FUNCTION (ISOFORM NOH-1L), RP CATALYTIC ACTIVITY (ISOFORM NOH-1L), AND TISSUE SPECIFICITY (ISOFORM RP NOH-1L). RC TISSUE=Colon epithelium; RX PubMed=10485709; DOI=10.1038/43459; RA Suh Y.-A., Arnold R.S., Lassegue B., Shi J., Xu X., Sorescu D., Chung A.B., RA Griendling K.K., Lambeth J.D.; RT "Cell transformation by the superoxide-generating oxidase Mox1."; RL Nature 401:79-82(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NOH-1L; NOH-1LV AND NOH-1S), FUNCTION RP (ISOFORM NOH-1S), AND TISSUE SPECIFICITY (ISOFORMS NOH-1L AND NOH-1S). RX PubMed=10615049; DOI=10.1126/science.287.5450.138; RA Banfi B., Maturana A., Jaconi S., Arnaudeau S., Laforge T., Sinha B., RA Ligeti E., Demaurex N., Krause K.-H.; RT "A mammalian H+ channel, generated through alternative splicing of the RT NADPH oxidase homolog NOH-1."; RL Science 287:138-142(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NOH-1L). RC TISSUE=Colon; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NOH-1L). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP ACTIVITY REGULATION, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR RP LOCATION. RX PubMed=14617635; DOI=10.1074/jbc.m305968200; RA Cheng G., Lambeth J.D.; RT "NOXO1, regulation of lipid binding, localization, and activation of Nox1 RT by the Phox homology (PX) domain."; RL J. Biol. Chem. 279:4737-4742(2004). RN [9] RP INTERACTION WITH NOXO1 AND ARHGEF7, ACTIVITY REGULATION, FUNCTION, AND RP CATALYTIC ACTIVITY. RX PubMed=16329988; DOI=10.1016/j.bbrc.2005.11.108; RA Park H.S., Park D., Bae Y.S.; RT "Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer RT 1."; RL Biochem. Biophys. Res. Commun. 339:985-990(2006). RN [10] RP IDENTIFICATION IN A COMPLEX CONTAINING NOX1; NOXO1; NOXA1 AND RAC1, RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=16636067; DOI=10.1074/jbc.m512751200; RA Cheng G., Diebold B.A., Hughes Y., Lambeth J.D.; RT "Nox1-dependent reactive oxygen generation is regulated by Rac1."; RL J. Biol. Chem. 281:17718-17726(2006). RN [11] RP SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19755710; DOI=10.1126/scisignal.2000370; RA Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A., Bokoch G.M.; RT "Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 RT (Nox1) activity."; RL Sci. Signal. 2:RA54-RA54(2009). RN [12] RP GLYCOSYLATION AT ASN-162 AND ASN-236. RX PubMed=24365146; DOI=10.1016/j.bbrc.2013.12.086; RA Miyano K., Sumimoto H.; RT "N-Linked glycosylation of the superoxide-producing NADPH oxidase Nox1."; RL Biochem. Biophys. Res. Commun. 443:1060-1065(2014). RN [13] RP POSSIBLE INVOLVEMENT IN INFLAMMATORY BOWEL DISEASE, VARIANTS SER-330 AND RP ASN-360, AND SUBCELLULAR LOCATION. RX PubMed=26301257; DOI=10.1016/j.jcmgh.2015.06.005; RA Hayes P., Dhillon S., O'Neill K., Thoeni C., Hui K.Y., Elkadri A., RA Guo C.H., Kovacic L., Aviello G., Alvarez L.A., Griffiths A.M., RA Snapper S.B., Brant S.R., Doroshow J.H., Silverberg M.S., Peter I., RA McGovern D.P., Cho J., Brumell J.H., Uhlig H.H., Bourke B., Muise A.A., RA Knaus U.G.; RT "Defects in NADPH oxidase genes NOX1 and DUOX2 in very early onset RT inflammatory bowel disease."; RL Cell. Mol. Gastroenterol. Hepatol. 1:489-502(2015). CC -!- FUNCTION: NADPH oxidase that catalyzes the generation of superoxide CC from molecular oxygen utilizing NADPH as an electron donor. CC {ECO:0000269|PubMed:14617635, ECO:0000269|PubMed:16329988, CC ECO:0000269|PubMed:16636067, ECO:0000269|PubMed:19755710}. CC -!- FUNCTION: [Isoform NOH-1L]: NADPH oxidase that catalyzes the generation CC of superoxide from molecular oxygen utilizing NADPH as an electron CC donor. {ECO:0000269|PubMed:10485709}. CC -!- FUNCTION: [Isoform NOH-1S]: Voltage-gated proton channel that mediates CC the H(+) currents of resting phagocytes and other tissues. It CC participates in the regulation of cellular pH and is blocked by zinc. CC {ECO:0000269|PubMed:10615049}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADPH + 2 O2 = H(+) + NADP(+) + 2 superoxide; CC Xref=Rhea:RHEA:63180, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:18421, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC Evidence={ECO:0000269|PubMed:14617635, ECO:0000269|PubMed:16329988, CC ECO:0000269|PubMed:16636067, ECO:0000269|PubMed:19755710}; CC -!- CATALYTIC ACTIVITY: [Isoform NOH-1L]: CC Reaction=NADPH + 2 O2 = H(+) + NADP(+) + 2 superoxide; CC Xref=Rhea:RHEA:63180, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:18421, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC Evidence={ECO:0000269|PubMed:10485709}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305}; CC -!- ACTIVITY REGULATION: The oxidase activity is potentiated by NOXA1, CC NOXO1 and RAC1. {ECO:0000269|PubMed:14617635, CC ECO:0000269|PubMed:16329988, ECO:0000269|PubMed:16636067}. CC -!- SUBUNIT: NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional CC multimeric complex supporting reactive oxygen species (ROS) production CC (PubMed:16636067). Interacts with NOXO1 (PubMed:16329988). Interacts CC (via FAD-binding FR-type domain) with ARHGEF7 (via PH domain) CC (PubMed:16329988). The phosphorylated form at Thr-430 interacts with CC NOXA1 with greater affinity (By similarity). CC {ECO:0000250|UniProtKB:Q9WV87, ECO:0000269|PubMed:16329988, CC ECO:0000269|PubMed:16636067}. CC -!- INTERACTION: CC Q9Y5S8; Q0VAB0: TBXA2R; NbExp=3; IntAct=EBI-15795558, EBI-18271435; CC -!- SUBCELLULAR LOCATION: Cell projection, invadopodium membrane CC {ECO:0000269|PubMed:19755710}; Multi-pass membrane protein CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:14617635, CC ECO:0000269|PubMed:26301257}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=NOH-1L; CC IsoId=Q9Y5S8-1; Sequence=Displayed; CC Name=NOH-1S; CC IsoId=Q9Y5S8-2; Sequence=VSP_001577, VSP_001578; CC Name=NOH-1LV; CC IsoId=Q9Y5S8-3; Sequence=VSP_001579; CC -!- TISSUE SPECIFICITY: [Isoform NOH-1L]: Detected in colon, uterus, CC prostate, and colon carcinoma, but not in peripheral blood leukocytes. CC {ECO:0000269|PubMed:10485709, ECO:0000269|PubMed:10615049}. CC -!- TISSUE SPECIFICITY: [Isoform NOH-1S]: Detected only in colon and colon CC carcinoma cells. {ECO:0000269|PubMed:10615049}. CC -!- PTM: Phosphorylation at Thr-430 mediated by PKC/PRKBC positively CC regulates its interaction with NOXA1 and enzyme activity. CC {ECO:0000250|UniProtKB:Q9WV87}. CC -!- DISEASE: Note=Defects in NOX1 may play a role in the pathogenesis of CC very early onset inflammatory bowel disease (VEOIBD), a chronic, CC relapsing inflammation of the gastrointestinal tract with a complex CC etiology diagnosed before 6 years of age. VEOIBD is subdivided into CC Crohn disease and ulcerative colitis phenotypes. Crohn disease may CC affect any part of the gastrointestinal tract from the mouth to the CC anus, but the phenotype of children with onset of Crohn disease CC occurring younger than the age of 10 is predominantly colonic, with a CC lower risk of ileal disease. Bowel inflammation is transmural and CC discontinuous; it may contain granulomas or be associated with CC intestinal or perianal fistulas. In contrast, in ulcerative colitis, CC the inflammation is continuous and limited to rectal and colonic CC mucosal layers; fistulas and granulomas are not observed. Both diseases CC include extraintestinal inflammation of the skin, eyes, or joints. CC {ECO:0000269|PubMed:26301257}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF127763; AAD38133.1; -; mRNA. DR EMBL; AF166326; AAF23232.1; -; mRNA. DR EMBL; AF166327; AAF23233.1; -; mRNA. DR EMBL; AF166328; AAF23234.1; -; mRNA. DR EMBL; DQ314883; ABC40742.1; -; Genomic_DNA. DR EMBL; AK292201; BAF84890.1; -; mRNA. DR EMBL; Z83819; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471115; EAX02820.1; -; Genomic_DNA. DR EMBL; BC075014; AAH75014.1; -; mRNA. DR EMBL; BC075015; AAH75015.1; -; mRNA. DR CCDS; CCDS14474.1; -. [Q9Y5S8-1] DR CCDS; CCDS14475.1; -. [Q9Y5S8-3] DR RefSeq; NP_001258744.1; NM_001271815.1. DR RefSeq; NP_008983.2; NM_007052.4. [Q9Y5S8-1] DR RefSeq; NP_039249.1; NM_013955.2. [Q9Y5S8-3] DR AlphaFoldDB; Q9Y5S8; -. DR SMR; Q9Y5S8; -. DR BioGRID; 117966; 11. DR DIP; DIP-60457N; -. DR IntAct; Q9Y5S8; 5. DR STRING; 9606.ENSP00000362057; -. DR BindingDB; Q9Y5S8; -. DR ChEMBL; CHEMBL1287628; -. DR DrugBank; DB09140; Oxygen. DR GuidetoPHARMACOLOGY; 3001; -. DR PeroxiBase; 5410; HsNOx01. DR TCDB; 5.B.1.1.3; the phagocyte (gp91(phox)) nadph oxidase family. DR GlyCosmos; Q9Y5S8; 2 sites, No reported glycans. DR GlyGen; Q9Y5S8; 2 sites. DR iPTMnet; Q9Y5S8; -. DR PhosphoSitePlus; Q9Y5S8; -. DR BioMuta; NOX1; -. DR DMDM; 8134597; -. DR jPOST; Q9Y5S8; -. DR MassIVE; Q9Y5S8; -. DR PaxDb; 9606-ENSP00000362057; -. DR PeptideAtlas; Q9Y5S8; -. DR ProteomicsDB; 86491; -. [Q9Y5S8-1] DR ProteomicsDB; 86492; -. [Q9Y5S8-2] DR ProteomicsDB; 86493; -. [Q9Y5S8-3] DR Antibodypedia; 28538; 412 antibodies from 34 providers. DR DNASU; 27035; -. DR Ensembl; ENST00000217885.5; ENSP00000217885.5; ENSG00000007952.18. [Q9Y5S8-3] DR Ensembl; ENST00000372966.8; ENSP00000362057.3; ENSG00000007952.18. [Q9Y5S8-1] DR GeneID; 27035; -. DR KEGG; hsa:27035; -. DR MANE-Select; ENST00000372966.8; ENSP00000362057.3; NM_007052.5; NP_008983.2. DR UCSC; uc004egj.3; human. [Q9Y5S8-1] DR AGR; HGNC:7889; -. DR CTD; 27035; -. DR DisGeNET; 27035; -. DR GeneCards; NOX1; -. DR HGNC; HGNC:7889; NOX1. DR HPA; ENSG00000007952; Tissue enriched (intestine). DR MIM; 300225; gene. DR neXtProt; NX_Q9Y5S8; -. DR OpenTargets; ENSG00000007952; -. DR PharmGKB; PA31690; -. DR VEuPathDB; HostDB:ENSG00000007952; -. DR eggNOG; KOG0039; Eukaryota. DR GeneTree; ENSGT00940000161632; -. DR HOGENOM; CLU_005646_3_1_1; -. DR InParanoid; Q9Y5S8; -. DR OMA; CMEVGQY; -. DR OrthoDB; 367877at2759; -. DR PhylomeDB; Q9Y5S8; -. DR TreeFam; TF105354; -. DR PathwayCommons; Q9Y5S8; -. DR Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping. DR SignaLink; Q9Y5S8; -. DR SIGNOR; Q9Y5S8; -. DR BioGRID-ORCS; 27035; 9 hits in 770 CRISPR screens. DR ChiTaRS; NOX1; human. DR GeneWiki; NOX1; -. DR GenomeRNAi; 27035; -. DR Pharos; Q9Y5S8; Tchem. DR PRO; PR:Q9Y5S8; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9Y5S8; Protein. DR Bgee; ENSG00000007952; Expressed in rectum and 126 other cell types or tissues. DR ExpressionAtlas; Q9Y5S8; baseline and differential. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell. DR GO; GO:0005769; C:early endosome; IDA:BHF-UCL. DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW. DR GO; GO:0043020; C:NADPH oxidase complex; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050661; F:NADP binding; IC:BHF-UCL. DR GO; GO:0031267; F:small GTPase binding; IPI:BHF-UCL. DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IDA:UniProtKB. DR GO; GO:0106292; F:superoxide-generating NADPH oxidase activity; IEA:RHEA. DR GO; GO:0001525; P:angiogenesis; IMP:BHF-UCL. DR GO; GO:0016477; P:cell migration; IMP:BHF-UCL. DR GO; GO:0071455; P:cellular response to hyperoxia; IEA:Ensembl. DR GO; GO:1990451; P:cellular stress response to acidic pH; IDA:BHF-UCL. DR GO; GO:0006952; P:defense response; IBA:GO_Central. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IDA:BHF-UCL. DR GO; GO:0006954; P:inflammatory response; TAS:BHF-UCL. DR GO; GO:0051454; P:intracellular pH elevation; IDA:BHF-UCL. DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl. DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl. DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW. DR GO; GO:0006739; P:NADP metabolic process; IC:BHF-UCL. DR GO; GO:0072592; P:oxygen metabolic process; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL. DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; IMP:BHF-UCL. DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl. DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:BHF-UCL. DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IEP:BHF-UCL. DR GO; GO:0008217; P:regulation of blood pressure; TAS:BHF-UCL. DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IEA:Ensembl. DR GO; GO:0045730; P:respiratory burst; TAS:BHF-UCL. DR GO; GO:0007165; P:signal transduction; TAS:BHF-UCL. DR GO; GO:0042554; P:superoxide anion generation; IDA:BHF-UCL. DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR InterPro; IPR000778; Cyt_b245_heavy_chain. DR InterPro; IPR013112; FAD-bd_8. DR InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR013130; Fe3_Rdtase_TM_dom. DR InterPro; IPR013121; Fe_red_NAD-bd_6. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR11972; NADPH OXIDASE; 1. DR PANTHER; PTHR11972:SF71; NADPH OXIDASE 1; 1. DR Pfam; PF08022; FAD_binding_8; 1. DR Pfam; PF01794; Ferric_reduct; 1. DR Pfam; PF08030; NAD_binding_6; 1. DR PRINTS; PR00466; GP91PHOX. DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1. DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51384; FAD_FR; 1. DR Genevisible; Q9Y5S8; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Cell membrane; Cell projection; KW Electron transport; FAD; Flavoprotein; Glycoprotein; Heme; Ion channel; KW Ion transport; Iron; Membrane; Metal-binding; NADP; Oxidoreductase; KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; KW Transport; Voltage-gated channel. FT CHAIN 1..564 FT /note="NADPH oxidase 1" FT /id="PRO_0000210148" FT TOPO_DOM 1..9 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 10..30 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 31..44 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 45..72 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 73..102 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 103..123 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 124..168 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 169..189 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 190..206 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 207..227 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 228..396 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 397..417 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 418..564 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 54..283 FT /note="Ferric oxidoreductase" FT DOMAIN 284..391 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT REGION 397..536 FT /note="Interaction with NOXO1" FT /evidence="ECO:0000269|PubMed:16329988" FT BINDING 101 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000305" FT BINDING 115 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000305" FT BINDING 209 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000305" FT BINDING 221 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000305" FT BINDING 338..344 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255" FT MOD_RES 430 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9WV87" FT CARBOHYD 162 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:24365146" FT CARBOHYD 236 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:24365146" FT VAR_SEQ 159..190 FT /note="QSRNTTVEYVTFTSIAGLTGVIMTIALILMVT -> HPHITPTVYMFTVTFD FT MVLSSVNSNLLFLLIK (in isoform NOH-1S)" FT /evidence="ECO:0000303|PubMed:10615049" FT /id="VSP_001577" FT VAR_SEQ 191..564 FT /note="Missing (in isoform NOH-1S)" FT /evidence="ECO:0000303|PubMed:10615049" FT /id="VSP_001578" FT VAR_SEQ 433..481 FT /note="Missing (in isoform NOH-1LV)" FT /evidence="ECO:0000303|PubMed:10615049" FT /id="VSP_001579" FT VARIANT 315 FT /note="R -> H (in dbSNP:rs2071756)" FT /id="VAR_049101" FT VARIANT 330 FT /note="P -> S (found in a patient with very early onset FT inflammatory bowel disease; uncertain significance; no FT effect on subcellular location; significantly reduced basal FT and phorbol ester-stimulated ROS generation, which may FT decrease resistance to infection by enteric pathogens, such FT as Campylobacter jejuni)" FT /evidence="ECO:0000269|PubMed:26301257" FT /id="VAR_075548" FT VARIANT 360 FT /note="D -> N (found in a patient with very early onset FT inflammatory bowel disease; uncertain significance; no FT effect on subcellular location; significantly reduced basal FT and phorbol ester-stimulated ROS generation, which may FT decrease resistance to infection by enteric pathogens, such FT as Campylobacter jejuni; dbSNP:rs34688635)" FT /evidence="ECO:0000269|PubMed:26301257" FT /id="VAR_061176" FT VARIANT 378 FT /note="R -> K (in dbSNP:rs35404864)" FT /id="VAR_049102" FT CONFLICT 173 FT /note="I -> V (in Ref. 2; AAD38133)" FT /evidence="ECO:0000305" SQ SEQUENCE 564 AA; 64871 MW; C3BE290F4E6DBC9A CRC64; MGNWVVNHWF SVLFLVVWLG LNVFLFVDAF LKYEKADKYY YTRKILGSTL ACARASALCL NFNSTLILLP VCRNLLSFLR GTCSFCSRTL RKQLDHNLTF HKLVAYMICL HTAIHIIAHL FNFDCYSRSR QATDGSLASI LSSLSHDEKK GGSWLNPIQS RNTTVEYVTF TSIAGLTGVI MTIALILMVT SATEFIRRSY FEVFWYTHHL FIFYILGLGI HGIGGIVRGQ TEESMNESHP RKCAESFEMW DDRDSHCRRP KFEGHPPESW KWILAPVILY ICERILRFYR SQQKVVITKV VMHPSKVLEL QMNKRGFSME VGQYIFVNCP SISLLEWHPF TLTSAPEEDF FSIHIRAAGD WTENLIRAFE QQYSPIPRIE VDGPFGTASE DVFQYEVAVL VGAGIGVTPF ASILKSIWYK FQCADHNLKT KKIYFYWICR ETGAFSWFNN LLTSLEQEME ELGKVGFLNY RLFLTGWDSN IVGHAALNFD KATDIVTGLK QKTSFGRPMW DNEFSTIATS HPKSVVGVFL CGPRTLAKSL RKCCHRYSSL DPRKVQFYFN KENF //