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Protein

NADPH oxidase 3

Gene

NOX3

Organism
Homo sapiens (Human)
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.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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BioCyciZFISH:HS01151-MONOMER.
ReactomeiR-HSA-5668599. RHO GTPases Activate NADPH Oxidases.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:7890. NOX3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 13CytoplasmicSequence analysisAdd BLAST13
Transmembranei14 – 34HelicalSequence analysisAdd BLAST21
Topological domaini35 – 51ExtracellularSequence analysisAdd BLAST17
Transmembranei52 – 72HelicalSequence analysisAdd BLAST21
Topological domaini73 – 103CytoplasmicSequence analysisAdd BLAST31
Transmembranei104 – 124HelicalSequence analysisAdd BLAST21
Topological domaini125 – 167ExtracellularSequence analysisAdd BLAST43
Transmembranei168 – 188HelicalSequence analysisAdd BLAST21
Topological domaini189 – 201CytoplasmicSequence analysisAdd BLAST13
Transmembranei202 – 222HelicalSequence analysisAdd BLAST21
Topological domaini223 – 395ExtracellularSequence analysisAdd BLAST173
Transmembranei396 – 416HelicalSequence analysisAdd BLAST21
Topological domaini417 – 568CytoplasmicSequence analysisAdd BLAST152

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • NADPH oxidase complex Source: Ensembl
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi413P → H: Loss of catalytic activity. 1 Publication1

Organism-specific databases

DisGeNETi50508.
OpenTargetsiENSG00000074771.
PharmGKBiPA31691.

Chemistry databases

ChEMBLiCHEMBL1741216.

Polymorphism and mutation databases

BioMutaiNOX3.
DMDMi74752785.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002275961 – 568NADPH oxidase 3Add BLAST568

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi163N-linked (GlcNAc...)Sequence analysis1
Glycosylationi238N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9HBY0.
PeptideAtlasiQ9HBY0.
PRIDEiQ9HBY0.

PTM databases

iPTMnetiQ9HBY0.
PhosphoSitePlusiQ9HBY0.

Expressioni

Developmental stagei

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

Gene expression databases

CleanExiHS_NOX3.
GenevisibleiQ9HBY0. HS.

Organism-specific databases

HPAiCAB008558.

Interactioni

Subunit structurei

Interacts with and stabilizes CYBA/p22phox.1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000159060.

Structurei

3D structure databases

ProteinModelPortaliQ9HBY0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 284Ferric oxidoreductaseAdd BLAST230
Domaini285 – 395FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST111

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.
InParanoidiQ9HBY0.
KOiK08008.
OMAiWICRDPS.
OrthoDBiEOG091G09RV.
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.
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.

Q9HBY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMGCWILNEG LSTILVLSWL GINFYLFIDT FYWYEEEESF HYTRVILGST
60 70 80 90 100
LAWARASALC LNFNCMLILI PVSRNLISFI RGTSICCRGP WRRQLDKNLR
110 120 130 140 150
FHKLVAYGIA VNATIHIVAH FFNLERYHWS QSEEAQGLLA ALSKLGNTPN
160 170 180 190 200
ESYLNPVRTF PTNTTTELLR TIAGVTGLVI SLALVLIMTS STEFIRQASY
210 220 230 240 250
ELFWYTHHVF IVFFLSLAIH GTGRIVRGQT QDSLSLHNIT FCRDRYAEWQ
260 270 280 290 300
TVAQCPVPQF SGKEPSAWKW ILGPVVLYAC ERIIRFWRFQ QEVVITKVVS
310 320 330 340 350
HPSGVLELHM KKRGFKMAPG QYILVQCPAI SSLEWHPFTL TSAPQEDFFS
360 370 380 390 400
VHIRAAGDWT AALLEAFGAE GQALQEPWSL PRLAVDGPFG TALTDVFHYP
410 420 430 440 450
VCVCVAAGIG VTPFAALLKS IWYKCSEAQT PLKLSKVYFY WICRDARAFE
460 470 480 490 500
WFADLLLSLE TRMSEQGKTH FLSYHIFLTG WDENQALHIA LHWDENTDVI
510 520 530 540 550
TGLKQKTFYG RPNWNNEFKQ IAYNHPSSSI GVFFCGPKAL SRTLQKMCHL
560
YSSADPRGVH FYYNKESF
Length:568
Mass (Da):64,935
Last modified:March 1, 2001 - v1
Checksum:i10BCD6BEB18D0583
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti328P → S in AAG15435 (PubMed:10974555).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049103171T → K.Corresponds to variant rs3749930dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9HBY0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000159060.

Chemistry databases

ChEMBLiCHEMBL1741216.

Protein family/group databases

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

PTM databases

iPTMnetiQ9HBY0.
PhosphoSitePlusiQ9HBY0.

Polymorphism and mutation databases

BioMutaiNOX3.
DMDMi74752785.

Proteomic databases

PaxDbiQ9HBY0.
PeptideAtlasiQ9HBY0.
PRIDEiQ9HBY0.

Protocols and materials databases

DNASUi50508.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000159060; ENSP00000159060; ENSG00000074771.
GeneIDi50508.
KEGGihsa:50508.
UCSCiuc003qqm.4. human.

Organism-specific databases

CTDi50508.
DisGeNETi50508.
GeneCardsiNOX3.
HGNCiHGNC:7890. NOX3.
HPAiCAB008558.
MIMi607105. gene.
neXtProtiNX_Q9HBY0.
OpenTargetsiENSG00000074771.
PharmGKBiPA31691.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000216669.
HOVERGENiHBG003760.
InParanoidiQ9HBY0.
KOiK08008.
OMAiWICRDPS.
OrthoDBiEOG091G09RV.
PhylomeDBiQ9HBY0.
TreeFamiTF105354.

Enzyme and pathway databases

BioCyciZFISH:HS01151-MONOMER.
ReactomeiR-HSA-5668599. RHO GTPases Activate NADPH Oxidases.

Miscellaneous databases

GeneWikiiNOX3.
GenomeRNAii50508.
PROiQ9HBY0.
SOURCEiSearch...

Gene expression databases

CleanExiHS_NOX3.
GenevisibleiQ9HBY0. HS.

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...

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: November 2, 2016
This is version 109 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

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.