Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADPH oxidase 1

Gene

Nox1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H+ ions as part of its electron transport mechanism.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

The oxidase activity is potentiated by NOXA1 and NOXO1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi129 – 1291Iron (heme axial ligand)Curated
Metal bindingi143 – 1431Iron (heme axial ligand)Curated
Metal bindingi236 – 2361Iron (heme axial ligand)Curated
Metal bindingi248 – 2481Iron (heme axial ligand)Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi365 – 3717FADSequence analysis

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: MGI
  • cell migration Source: MGI
  • cellular response to hyperoxia Source: MGI
  • cellular stress response to acidic pH Source: MGI
  • extracellular matrix organization Source: MGI
  • hydrogen peroxide metabolic process Source: MGI
  • intracellular pH elevation Source: MGI
  • oxidation-reduction process Source: MGI
  • oxygen metabolic process Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of integrin biosynthetic process Source: MGI
  • positive regulation of JNK cascade Source: MGI
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of vascular endothelial growth factor production Source: Ensembl
  • proton transport Source: MGI
  • regulation of systemic arterial blood pressure by renin-angiotensin Source: MGI
  • superoxide anion generation Source: MGI
  • superoxide metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BRENDAi1.6.3.1. 3474.
ReactomeiR-MMU-5668599. RHO GTPases Activate NADPH Oxidases.

Protein family/group databases

PeroxiBasei5963. MmNOx01.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH oxidase 1 (EC:1.-.-.-)
Short name:
NOX-1
Gene namesi
Name:Nox1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:2450016. Nox1.

Subcellular locationi

  • Cell projectioninvadopodium membrane By similarity; Multi-pass membrane protein By similarity
  • Cell membrane By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3636CytoplasmicSequence analysisAdd
BLAST
Transmembranei37 – 5923Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini60 – 7213ExtracellularSequence analysisAdd
BLAST
Transmembranei73 – 9725Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini98 – 13033CytoplasmicSequence analysisAdd
BLAST
Transmembranei131 – 15121Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini152 – 19544ExtracellularSequence analysisAdd
BLAST
Transmembranei196 – 21621Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini217 – 23418CytoplasmicSequence analysisAdd
BLAST
Transmembranei235 – 25521Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini256 – 423168ExtracellularSequence analysisAdd
BLAST
Transmembranei424 – 44421Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini445 – 591147CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: MGI
  • early endosome Source: MGI
  • endosome Source: MGI
  • invadopodium membrane Source: UniProtKB
  • NADPH oxidase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591NADPH oxidase 1PRO_0000322982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence analysis
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8CIZ9.
PRIDEiQ8CIZ9.

PTM databases

PhosphoSiteiQ8CIZ9.

Expressioni

Tissue specificityi

Isoform 2 expressed in colon and vascular smooth muscle cells (VSMC).1 Publication

Inductioni

Isoform 1 (c-type) induced in VSMC by angiotensin II and injury to the artery.1 Publication

Gene expression databases

BgeeiQ8CIZ9.
CleanExiMM_NOX1.
ExpressionAtlasiQ8CIZ9. baseline and differential.

Interactioni

Subunit structurei

NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional multimeric complex supporting ROS production. Interacts with NOXA1 and NOXO1.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033610.

Structurei

3D structure databases

ProteinModelPortaliQ8CIZ9.
SMRiQ8CIZ9. Positions 406-591.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 316235Ferric oxidoreductaseAdd
BLAST
Domaini317 – 418102FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni424 – 563140Interaction with NOXO1By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 ferric oxidoreductase domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000216669.
HOVERGENiHBG003760.
InParanoidiQ8CIZ9.
KOiK08008.
OMAiIATSHPK.
OrthoDBiEOG71P299.
PhylomeDBiQ8CIZ9.
TreeFamiTF105354.

Family and domain databases

InterProiIPR000778. Cyt_b245_heavy_chain.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR029650. NOX1.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR11972:SF71. PTHR11972:SF71. 2 hits.
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00466. GP91PHOX.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CIZ9-1) [UniParc]FASTAAdd to basket

Also known as: f-type, c-type

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGELRGSRG PLQRIQIAPR EAPNLHLTMG NWLVNHWLSV LFLVSWLGLN
60 70 80 90 100
IFLFVYAFLN YEKSDKYYYT REILGTALAL ARASALCLNF NSMMILIPVC
110 120 130 140 150
RNLLSFLRGT CSFCNRTLRK PLDHNLTFHK LVAYMICIFT VIHIIAHLFN
160 170 180 190 200
FERYRRSQQA MDGSLASVLS SLSHPEKEDS WLNPIQSPNM TVMYAAFTSI
210 220 230 240 250
AGLTGVIATV ALVLMVTSAM EFIRRNYFEL FWYTHHLFIV YIICLGIHGL
260 270 280 290 300
GGIVRGQTEE SLGESHPHNC SHSFHEWDDH KGSCRHPHFA GHPPESWKWI
310 320 330 340 350
LAPIAFYIFE RILRFYRSQQ KVVITKVVMH PSNVLELQMR KRGFSMEVGQ
360 370 380 390 400
YIFVNCPSIS FLEWHPFTLT SAPEEEFFSV HIRAAGDWTR NLIRTFEQQH
410 420 430 440 450
SPMPRIEVDG PFGTVSEDVF QYEVAVLVGA GIGVTPFASI LKSIWYKFQR
460 470 480 490 500
ADNKLKTQKI YFYWICRETG AFAWFNNLLN SLEQEMEELG KMDFLNYRLF
510 520 530 540 550
LTGWDSNIAG HAALNFDRAT DILTGLKQKT SFGRPMWDNE FSRIATAHPK
560 570 580 590
SAVGVFLCGP RTLAKSLRKR CQRYSSLDPR KVQFYFNKET F
Note: Product of f-type and c-type mRNA, which differ only in 5'-UTR.
Length:591
Mass (Da):68,193
Last modified:January 19, 2010 - v2
Checksum:iB2D4AE54186A066B
GO
Isoform 2 (identifier: Q8CIZ9-2) [UniParc]FASTAAdd to basket

Also known as: a-type

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Show »
Length:563
Mass (Da):65,128
Checksum:i985620FDFBB75F65
GO
Isoform 3 (identifier: Q8CIZ9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
     460-508: Missing.

Note: Gene prediction based on human ortholog.
Show »
Length:514
Mass (Da):59,143
Checksum:i21F89266C87A1911
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform 2 and isoform 3. 3 PublicationsVSP_038574Add
BLAST
Alternative sequencei460 – 50849Missing in isoform 3. CuratedVSP_038575Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF539799 mRNA. Translation: AAN75144.1.
AK136432 mRNA. Translation: BAE22974.1.
AL671915 Genomic DNA. Translation: CAM16733.1.
AL671915 Genomic DNA. Translation: CAM16734.1.
AB206383 mRNA. Translation: BAF03561.1.
AB206384 mRNA. Translation: BAF03562.1.
AB206385 mRNA. Translation: BAF03563.1.
AY174116 mRNA. Translation: AAO20852.1.
CCDSiCCDS30390.1. [Q8CIZ9-2]
RefSeqiNP_757340.1. NM_172203.2. [Q8CIZ9-2]
XP_006528578.1. XM_006528515.2. [Q8CIZ9-1]
UniGeneiMm.233865.
Mm.455133.
Mm.67938.

Genome annotation databases

EnsembliENSMUST00000033610; ENSMUSP00000033610; ENSMUSG00000031257. [Q8CIZ9-2]
ENSMUST00000113275; ENSMUSP00000108900; ENSMUSG00000031257. [Q8CIZ9-3]
GeneIDi237038.
KEGGimmu:237038.
UCSCiuc009ufl.2. mouse. [Q8CIZ9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF539799 mRNA. Translation: AAN75144.1.
AK136432 mRNA. Translation: BAE22974.1.
AL671915 Genomic DNA. Translation: CAM16733.1.
AL671915 Genomic DNA. Translation: CAM16734.1.
AB206383 mRNA. Translation: BAF03561.1.
AB206384 mRNA. Translation: BAF03562.1.
AB206385 mRNA. Translation: BAF03563.1.
AY174116 mRNA. Translation: AAO20852.1.
CCDSiCCDS30390.1. [Q8CIZ9-2]
RefSeqiNP_757340.1. NM_172203.2. [Q8CIZ9-2]
XP_006528578.1. XM_006528515.2. [Q8CIZ9-1]
UniGeneiMm.233865.
Mm.455133.
Mm.67938.

3D structure databases

ProteinModelPortaliQ8CIZ9.
SMRiQ8CIZ9. Positions 406-591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033610.

Protein family/group databases

PeroxiBasei5963. MmNOx01.

PTM databases

PhosphoSiteiQ8CIZ9.

Proteomic databases

PaxDbiQ8CIZ9.
PRIDEiQ8CIZ9.

Protocols and materials databases

DNASUi237038.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033610; ENSMUSP00000033610; ENSMUSG00000031257. [Q8CIZ9-2]
ENSMUST00000113275; ENSMUSP00000108900; ENSMUSG00000031257. [Q8CIZ9-3]
GeneIDi237038.
KEGGimmu:237038.
UCSCiuc009ufl.2. mouse. [Q8CIZ9-1]

Organism-specific databases

CTDi27035.
MGIiMGI:2450016. Nox1.

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000216669.
HOVERGENiHBG003760.
InParanoidiQ8CIZ9.
KOiK08008.
OMAiIATSHPK.
OrthoDBiEOG71P299.
PhylomeDBiQ8CIZ9.
TreeFamiTF105354.

Enzyme and pathway databases

BRENDAi1.6.3.1. 3474.
ReactomeiR-MMU-5668599. RHO GTPases Activate NADPH Oxidases.

Miscellaneous databases

ChiTaRSiNox1. mouse.
NextBioi383203.
PROiQ8CIZ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CIZ9.
CleanExiMM_NOX1.
ExpressionAtlasiQ8CIZ9. baseline and differential.

Family and domain databases

InterProiIPR000778. Cyt_b245_heavy_chain.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR029650. NOX1.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR11972:SF71. PTHR11972:SF71. 2 hits.
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00466. GP91PHOX.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two novel proteins activate superoxide generation by the NADPH oxidase NOX1."
    Banfi B., Clark R.A., Steger K., Krause K.-H.
    J. Biol. Chem. 278:3510-3513(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH NOXO1, ENZYME REGULATION.
    Strain: BALB/cJ.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Colon.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "Novel transcripts of Nox1 are regulated by alternative promoters and expressed under phenotypic modulation of vascular smooth muscle cells."
    Arakawa N., Katsuyama M., Matsuno K., Urao N., Tabuchi Y., Okigaki M., Matsubara H., Yabe-Nishimura C.
    Biochem. J. 398:303-310(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-75 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 29-75 (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INDUCTION.
    Tissue: Colon and Vascular smooth muscle.
  5. "Nox1 expression in the gastric mucosa of Helicobacter-infected gp91phox-/- mice."
    Matsumoto Y., Blanchard T.G.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 116-565 (ISOFORMS 1/2).
    Strain: C57BL/6J.

Entry informationi

Entry nameiNOX1_MOUSE
AccessioniPrimary (citable) accession number: Q8CIZ9
Secondary accession number(s): A2AEK5
, Q0KKX3, Q0KKX5, Q811U2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: January 19, 2010
Last modified: March 16, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.