Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9HBY0

- NOX3_HUMAN

UniProt

Q9HBY0 - NOX3_HUMAN

Protein

NADPH oxidase 3

Gene

NOX3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    NADPH oxidase which constitutively produces superoxide upon formation of a complex with CYBA/p22phox. Plays a role in the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity.1 Publication

    Enzyme regulationi

    Activated by the ototoxic drug cisplatin By similarity. Activated by NOXO1. Cooperatively activated by NCF1 and NCF2 or NOXA1 in a phorbol 12-myristate 13-acetate (PMA)-dependent manner. Inhibited by diphenyleneiodonium chloride.By similarity2 Publications

    GO - Molecular functioni

    1. superoxide-generating NADPH oxidase activity Source: Ensembl

    GO - Biological processi

    1. detection of gravity Source: Ensembl
    2. otolith development Source: Ensembl
    3. superoxide anion generation Source: Ensembl
    4. temperature homeostasis Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Protein family/group databases

    PeroxiBasei5960. HsNOx03.
    TCDBi5.B.1.1.4. the phagocyte (gp91(phox)) nadph oxidase family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH oxidase 3 (EC:1.6.3.-)
    Alternative name(s):
    Mitogenic oxidase 2
    Short name:
    MOX-2
    gp91phox homolog 3
    Short name:
    GP91-3
    Gene namesi
    Name:NOX3
    Synonyms:MOX2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:7890. NOX3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. NADPH oxidase complex Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi413 – 4131P → H: Loss of catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA31691.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 568568NADPH oxidase 3PRO_0000227596Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9HBY0.
    PRIDEiQ9HBY0.

    PTM databases

    PhosphoSiteiQ9HBY0.

    Expressioni

    Developmental stagei

    Expressed in fetal kidney and to a lower extent in liver, lung and spleen.2 Publications

    Gene expression databases

    CleanExiHS_NOX3.
    GenevestigatoriQ9HBY0.

    Interactioni

    Subunit structurei

    Interacts with and stabilizes CYBA/p22phox.1 Publication

    Protein-protein interaction databases

    STRINGi9606.ENSP00000159060.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HBY0.
    SMRiQ9HBY0. Positions 383-568.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini35 – 5117ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini73 – 10331CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini125 – 16743ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini189 – 20113CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini223 – 395173ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini417 – 568152CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei14 – 3421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei52 – 7221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei104 – 12421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei168 – 18821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei202 – 22221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei396 – 41621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 284230Ferric oxidoreductaseAdd
    BLAST
    Domaini285 – 395111FAD-binding FR-typePROSITE-ProRule annotationAdd
    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

    eggNOGiNOG287712.
    HOGENOMiHOG000216669.
    HOVERGENiHBG003760.
    InParanoidiQ9HBY0.
    KOiK08008.
    OMAiKCSEAQT.
    OrthoDBiEOG71P299.
    PhylomeDBiQ9HBY0.
    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.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9HBY0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMGCWILNEG LSTILVLSWL GINFYLFIDT FYWYEEEESF HYTRVILGST    50
    LAWARASALC LNFNCMLILI PVSRNLISFI RGTSICCRGP WRRQLDKNLR 100
    FHKLVAYGIA VNATIHIVAH FFNLERYHWS QSEEAQGLLA ALSKLGNTPN 150
    ESYLNPVRTF PTNTTTELLR TIAGVTGLVI SLALVLIMTS STEFIRQASY 200
    ELFWYTHHVF IVFFLSLAIH GTGRIVRGQT QDSLSLHNIT FCRDRYAEWQ 250
    TVAQCPVPQF SGKEPSAWKW ILGPVVLYAC ERIIRFWRFQ QEVVITKVVS 300
    HPSGVLELHM KKRGFKMAPG QYILVQCPAI SSLEWHPFTL TSAPQEDFFS 350
    VHIRAAGDWT AALLEAFGAE GQALQEPWSL PRLAVDGPFG TALTDVFHYP 400
    VCVCVAAGIG VTPFAALLKS IWYKCSEAQT PLKLSKVYFY WICRDARAFE 450
    WFADLLLSLE TRMSEQGKTH FLSYHIFLTG WDENQALHIA LHWDENTDVI 500
    TGLKQKTFYG RPNWNNEFKQ IAYNHPSSSI GVFFCGPKAL SRTLQKMCHL 550
    YSSADPRGVH FYYNKESF 568
    Length:568
    Mass (Da):64,935
    Last modified:March 1, 2001 - v1
    Checksum:i10BCD6BEB18D0583
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti328 – 3281P → S in AAG15435. (PubMed:10974555)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti171 – 1711T → K.
    Corresponds to variant rs3749930 [ dbSNP | Ensembl ].
    VAR_049103

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190122 mRNA. Translation: AAG17121.1.
    AL031773 Genomic DNA. Translation: CAI19957.1.
    AF229177 mRNA. Translation: AAG15435.1.
    CCDSiCCDS5250.1.
    RefSeqiNP_056533.1. NM_015718.2.
    UniGeneiHs.247776.

    Genome annotation databases

    EnsembliENST00000159060; ENSP00000159060; ENSG00000074771.
    GeneIDi50508.
    KEGGihsa:50508.
    UCSCiuc003qqm.3. human.

    Polymorphism databases

    DMDMi74752785.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190122 mRNA. Translation: AAG17121.1 .
    AL031773 Genomic DNA. Translation: CAI19957.1 .
    AF229177 mRNA. Translation: AAG15435.1 .
    CCDSi CCDS5250.1.
    RefSeqi NP_056533.1. NM_015718.2.
    UniGenei Hs.247776.

    3D structure databases

    ProteinModelPortali Q9HBY0.
    SMRi Q9HBY0. Positions 383-568.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000159060.

    Chemistry

    ChEMBLi CHEMBL1741216.

    Protein family/group databases

    PeroxiBasei 5960. HsNOx03.
    TCDBi 5.B.1.1.4. the phagocyte (gp91(phox)) nadph oxidase family.

    PTM databases

    PhosphoSitei Q9HBY0.

    Polymorphism databases

    DMDMi 74752785.

    Proteomic databases

    PaxDbi Q9HBY0.
    PRIDEi Q9HBY0.

    Protocols and materials databases

    DNASUi 50508.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000159060 ; ENSP00000159060 ; ENSG00000074771 .
    GeneIDi 50508.
    KEGGi hsa:50508.
    UCSCi uc003qqm.3. human.

    Organism-specific databases

    CTDi 50508.
    GeneCardsi GC06M155716.
    HGNCi HGNC:7890. NOX3.
    MIMi 607105. gene.
    neXtProti NX_Q9HBY0.
    PharmGKBi PA31691.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287712.
    HOGENOMi HOG000216669.
    HOVERGENi HBG003760.
    InParanoidi Q9HBY0.
    KOi K08008.
    OMAi KCSEAQT.
    OrthoDBi EOG71P299.
    PhylomeDBi Q9HBY0.
    TreeFami TF105354.

    Miscellaneous databases

    GeneWikii NOX3.
    GenomeRNAii 50508.
    NextBioi 53074.
    PROi Q9HBY0.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_NOX3.
    Genevestigatori Q9HBY0.

    Family and domain databases

    InterProi IPR000778. Cyt_b245_heavy_chain.
    IPR013112. FAD-bd_8.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR013130. Fe3_Rdtase_TM_dom.
    IPR013121. Fe_red_NAD-bd_6.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF08022. FAD_binding_8. 1 hit.
    PF01794. Ferric_reduct. 1 hit.
    PF08030. NAD_binding_6. 1 hit.
    [Graphical view ]
    PRINTSi PR00466. GP91PHOX.
    SUPFAMi SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5."
      Cheng G., Cao Z., Xu X., van Meir E.G., Lambeth J.D.
      Gene 269:131-140(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
      Tissue: Fetal kidney.
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "NADPH oxidase subunit, gp91phox homologue, preferentially expressed in human colon epithelial cells."
      Kikuchi H., Hikage M., Miyashita H., Fukumoto M.
      Gene 254:237-243(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-497, DEVELOPMENTAL STAGE.
      Tissue: Fetal kidney.
    4. "Nox3 regulation by NOXO1, p47phox, and p67phox."
      Cheng G., Ritsick D., Lambeth J.D.
      J. Biol. Chem. 279:34250-34255(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    5. "The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators."
      Ueno N., Takeya R., Miyano K., Kikuchi H., Sumimoto H.
      J. Biol. Chem. 280:23328-23339(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF PRO-413, ENZYME REGULATION, INTERACTION WITH CYBA.

    Entry informationi

    Entry nameiNOX3_HUMAN
    AccessioniPrimary (citable) accession number: Q9HBY0
    Secondary accession number(s): Q9HBJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3