NOX1_HUMAN
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 03-AUG-2022, entry version 188.
DE RecName: Full=NADPH oxidase 1;
DE Short=NOX-1;
DE EC=1.-.-.-;
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).
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).
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.
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 ACTIVITY REGULATION.
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.
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.
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: NOH-1S is a voltage-gated proton channel that mediates the
CC H(+) currents of resting phagocytes and other tissues. It participates
CC in the regulation of cellular pH and is blocked by zinc. NOH-1L is a
CC pyridine nucleotide-dependent oxidoreductase that generates superoxide
CC and might conduct H(+) ions as part of its electron transport
CC mechanism, whereas NOH-1S does not contain an electron transport chain.
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: The oxidase activity is potentiated by NOXA1 and
CC NOXO1. {ECO:0000269|PubMed:14617635, ECO:0000269|PubMed:16329988}.
CC -!- SUBUNIT: NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional
CC multimeric complex supporting reactive oxygen species (ROS) production.
CC Interacts with NOXA1 and NOXO1. {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:0000269|PubMed:19755710}. Cell membrane
CC {ECO:0000269|PubMed:26301257}.
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: NOH-1L is detected in colon, uterus, prostate, and
CC colon carcinoma, but not in peripheral blood leukocytes. NOH-1S is
CC detected only in colon and colon carcinoma cells.
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}.
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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 GlyGen; Q9Y5S8; 2 sites.
DR iPTMnet; Q9Y5S8; -.
DR PhosphoSitePlus; Q9Y5S8; -.
DR BioMuta; NOX1; -.
DR DMDM; 8134597; -.
DR jPOST; Q9Y5S8; -.
DR MassIVE; Q9Y5S8; -.
DR PaxDb; Q9Y5S8; -.
DR PeptideAtlas; Q9Y5S8; -.
DR PRIDE; Q9Y5S8; -.
DR ProteomicsDB; 86491; -. [Q9Y5S8-1]
DR ProteomicsDB; 86492; -. [Q9Y5S8-2]
DR ProteomicsDB; 86493; -. [Q9Y5S8-3]
DR Antibodypedia; 28538; 370 antibodies from 33 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 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; HRTYISK; -.
DR OrthoDB; 936110at2759; -.
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; 8 hits in 694 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 124 other tissues.
DR ExpressionAtlas; Q9Y5S8; baseline and differential.
DR Genevisible; Q9Y5S8; HS.
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:0043020; C:NADPH oxidase complex; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IMP:BHF-UCL.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
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: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:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.80; -; 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; IPR029650; NOX1.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF71; PTHR11972:SF71; 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 SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
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 Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW 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 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; unknown pathological
FT significance; no effect on subcellular location;
FT significantly reduced basal and phorbol ester-stimulated
FT ROS generation, which may decrease resistance to infection
FT by enteric pathogens, such 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; unknown pathological
FT significance; no effect on subcellular location;
FT significantly reduced basal and phorbol ester-stimulated
FT ROS generation, which may decrease resistance to infection
FT by enteric pathogens, such as Campylobacter jejuni;
FT 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
