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Protein

NADPH oxidase 3

Gene

Nox3

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

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.2 Publications

Enzyme regulationi

Activated by the ototoxic drug cisplatin. 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.1 Publication

GO - Molecular functioni

  • superoxide-generating NADPH oxidase activity Source: MGI

GO - Biological processi

  • detection of gravity Source: MGI
  • otolith development Source: MGI
  • response to gravity Source: MGI
  • superoxide anion generation Source: MGI
  • temperature homeostasis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

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

Protein family/group databases

PeroxiBasei5959. MmNOx03.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH oxidase 3 (EC:1.6.3.-)
Gene namesi
Name:Nox3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2681162. Nox3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence analysisAdd
BLAST
Transmembranei13 – 3321HelicalSequence analysisAdd
BLAST
Topological domaini34 – 4916ExtracellularSequence analysisAdd
BLAST
Transmembranei50 – 7021HelicalSequence analysisAdd
BLAST
Topological domaini71 – 10333CytoplasmicSequence analysisAdd
BLAST
Transmembranei104 – 12421HelicalSequence analysisAdd
BLAST
Topological domaini125 – 16743ExtracellularSequence analysisAdd
BLAST
Transmembranei168 – 18821HelicalSequence analysisAdd
BLAST
Topological domaini189 – 20113CytoplasmicSequence analysisAdd
BLAST
Transmembranei202 – 22221HelicalSequence analysisAdd
BLAST
Topological domaini223 – 395173ExtracellularSequence analysisAdd
BLAST
Transmembranei396 – 41621HelicalSequence analysisAdd
BLAST
Topological domaini417 – 568152CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • NADPH oxidase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Mice display balance defects, a tilted position of the head and abnormal performances in motor coordination tests. This is associated with the absence of otoconia in both the utricle and saccule of the inner ear.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi408 – 4081G → R: Defects in otoconia biogenesis. 1 Publication
Mutagenesisi542 – 5421K → E: Defects in otoconia biogenesis. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 568568NADPH oxidase 3PRO_0000227597Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ672J9.
PRIDEiQ672J9.

PTM databases

iPTMnetiQ672J9.
PhosphoSiteiQ672J9.

Expressioni

Tissue specificityi

Specifically expressed in inner ear by the spiral glanglion neurons, the vestibular system and the sensory epithelial cell layer of the saccule. Weakly expressed in skull and brain.1 Publication

Developmental stagei

Expressed in fetal kidney.1 Publication

Gene expression databases

BgeeiQ672J9.
CleanExiMM_NOX3.

Interactioni

Subunit structurei

Interacts with and stabilizes CYBA/p22phox.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024565.

Structurei

3D structure databases

ProteinModelPortaliQ672J9.
SMRiQ672J9. Positions 383-568.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000216669.
HOVERGENiHBG003760.
InParanoidiQ672J9.
KOiK08008.
OMAiNATIHIA.
OrthoDBiEOG71P299.
PhylomeDBiQ672J9.
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.
IPR029653. NOX3.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR11972:SF12. PTHR11972:SF12. 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]

Sequencei

Sequence statusi: Complete.

Q672J9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVCWILNES GSFVVALLWL AVNAYLFIDT FFWYTEEEAF FYTRVILGSA
60 70 80 90 100
LAWARASAVC LNFNCMLILL PVSRNFISLV RGTSVCCRGP WRRQLDKNLN
110 120 130 140 150
FHKLVAYGIA VNSVIHIVAH LFNLERYHLG QAKDAEGLLA ALSKLGDAPN
160 170 180 190 200
ESYLNPVRTF DMGTTTELLM TVSGITGLGI SLALVFIMTS STEFIRRSSY
210 220 230 240 250
ELFWYTHHIF VFFFISLAIH GGGRIIRGQT PESLRLHNVT YCRDHYAEWQ
260 270 280 290 300
AAALCPVPQF SGKEPSAWKW ALGPVVLYAC ERIIRFWRSH QEVVITKVVS
310 320 330 340 350
HPSAVLELHM KKRDFKMAPG QYIFIQCPSV SPLEWHPFTL TSAPQEDFFS
360 370 380 390 400
VHIRASGDWT EALLKAFRVE GQAPSELCSM PRLAVDGPFG GSLADVFHYP
410 420 430 440 450
VSVCIATGIG VTPFASLLKS VWYKCCESQS LPELSKVYFY WICRDAGAFE
460 470 480 490 500
WFADLLLSLE TRMSEQGKAH LLSYHIYLTG WDENQAIHIA LHWDESLDVI
510 520 530 540 550
TGLKQKAFYG RPNWNDEFKQ IAYNHPSSSI GVFFCGSKAM SKTLQKMCRL
560
YSSVDPRGVH FYYNKENF
Length:568
Mass (Da):64,495
Last modified:March 21, 2006 - v2
Checksum:i345FD67494ADB8F2
GO

Sequence cautioni

The sequence AAI06863.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAO65981.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611D → Y in AAT80344 (PubMed:15326186).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY182377 mRNA. Translation: AAO65981.1. Different initiation.
AY573240 mRNA. Translation: AAT80344.1.
BC106862 mRNA. Translation: AAI06863.1. Different initiation.
CCDSiCCDS28364.2.
RefSeqiNP_945196.2. NM_198958.2.
UniGeneiMm.328756.

Genome annotation databases

EnsembliENSMUST00000115800; ENSMUSP00000111466; ENSMUSG00000023802.
GeneIDi224480.
KEGGimmu:224480.
UCSCiuc008aev.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY182377 mRNA. Translation: AAO65981.1. Different initiation.
AY573240 mRNA. Translation: AAT80344.1.
BC106862 mRNA. Translation: AAI06863.1. Different initiation.
CCDSiCCDS28364.2.
RefSeqiNP_945196.2. NM_198958.2.
UniGeneiMm.328756.

3D structure databases

ProteinModelPortaliQ672J9.
SMRiQ672J9. Positions 383-568.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024565.

Protein family/group databases

PeroxiBasei5959. MmNOx03.

PTM databases

iPTMnetiQ672J9.
PhosphoSiteiQ672J9.

Proteomic databases

PaxDbiQ672J9.
PRIDEiQ672J9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115800; ENSMUSP00000111466; ENSMUSG00000023802.
GeneIDi224480.
KEGGimmu:224480.
UCSCiuc008aev.2. mouse.

Organism-specific databases

CTDi50508.
MGIiMGI:2681162. Nox3.

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000216669.
HOVERGENiHBG003760.
InParanoidiQ672J9.
KOiK08008.
OMAiNATIHIA.
OrthoDBiEOG71P299.
PhylomeDBiQ672J9.
TreeFamiTF105354.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ672J9.
SOURCEiSearch...

Gene expression databases

BgeeiQ672J9.
CleanExiMM_NOX3.

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.
IPR029653. NOX3.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR11972:SF12. PTHR11972:SF12. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLY-408 AND LYS-542, DISRUPTION PHENOTYPE.
    Strain: C3Heb/FeJ.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, ENZYME REGULATION.
    Strain: C57BL/6J.
    Tissue: Inner ear.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiNOX3_MOUSE
AccessioniPrimary (citable) accession number: Q672J9
Secondary accession number(s): Q6Y4Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: June 8, 2016
This is version 81 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.