Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9HBY0 (NOX3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NOX3
Synonyms:MOX2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Enzyme regulation

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. Ref.4 Ref.5

Subunit structure

Interacts with and stabilizes CYBA/p22phox. Ref.5

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Developmental stage

Expressed in fetal kidney and to a lower extent in liver, lung and spleen. Ref.1 Ref.3

Sequence similarities

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568NADPH oxidase 3
PRO_0000227596

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Helical; Potential
Topological domain35 – 5117Extracellular Potential
Transmembrane52 – 7221Helical; Potential
Topological domain73 – 10331Cytoplasmic Potential
Transmembrane104 – 12421Helical; Potential
Topological domain125 – 16743Extracellular Potential
Transmembrane168 – 18821Helical; Potential
Topological domain189 – 20113Cytoplasmic Potential
Transmembrane202 – 22221Helical; Potential
Topological domain223 – 395173Extracellular Potential
Transmembrane396 – 41621Helical; Potential
Topological domain417 – 568152Cytoplasmic Potential
Domain55 – 284230Ferric oxidoreductase
Domain285 – 395111FAD-binding FR-type

Amino acid modifications

Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential

Natural variations

Natural variant1711T → K.
Corresponds to variant rs3749930 [ dbSNP | Ensembl ].
VAR_049103

Experimental info

Mutagenesis4131P → H: Loss of catalytic activity. Ref.5
Sequence conflict3281P → S in AAG15435. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9HBY0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 10BCD6BEB18D0583

FASTA56864,935
        10         20         30         40         50         60 
MMGCWILNEG LSTILVLSWL GINFYLFIDT FYWYEEEESF HYTRVILGST LAWARASALC 

        70         80         90        100        110        120 
LNFNCMLILI PVSRNLISFI RGTSICCRGP WRRQLDKNLR FHKLVAYGIA VNATIHIVAH 

       130        140        150        160        170        180 
FFNLERYHWS QSEEAQGLLA ALSKLGNTPN ESYLNPVRTF PTNTTTELLR TIAGVTGLVI 

       190        200        210        220        230        240 
SLALVLIMTS STEFIRQASY ELFWYTHHVF IVFFLSLAIH GTGRIVRGQT QDSLSLHNIT 

       250        260        270        280        290        300 
FCRDRYAEWQ TVAQCPVPQF SGKEPSAWKW ILGPVVLYAC ERIIRFWRFQ QEVVITKVVS 

       310        320        330        340        350        360 
HPSGVLELHM KKRGFKMAPG QYILVQCPAI SSLEWHPFTL TSAPQEDFFS VHIRAAGDWT 

       370        380        390        400        410        420 
AALLEAFGAE GQALQEPWSL PRLAVDGPFG TALTDVFHYP VCVCVAAGIG VTPFAALLKS 

       430        440        450        460        470        480 
IWYKCSEAQT PLKLSKVYFY WICRDARAFE WFADLLLSLE TRMSEQGKTH FLSYHIFLTG 

       490        500        510        520        530        540 
WDENQALHIA LHWDENTDVI TGLKQKTFYG RPNWNNEFKQ IAYNHPSSSI GVFFCGPKAL 

       550        560 
SRTLQKMCHL YSSADPRGVH FYYNKESF

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF190122 mRNA. Translation: AAG17121.1.
AL031773 Genomic DNA. Translation: CAI19957.1.
AF229177 mRNA. Translation: AAG15435.1.
IPIIPI00024581.
RefSeqNP_056533.1. NM_015718.2.
UniGeneHs.247776.

3D structure databases

ProteinModelPortalQ9HBY0.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000159060.

Protein family/group databases

PeroxiBase5960. HsNOx03.
TCDB5.B.1.1.4. phagocyte (gp91phox) NADPH oxidase family.

PTM databases

PhosphoSiteQ9HBY0.

Polymorphism databases

DMDM74752785.

Proteomic databases

PaxDbQ9HBY0.
PRIDEQ9HBY0.

Protocols and materials databases

DNASU50508.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000159060; ENSP00000159060; ENSG00000074771.
GeneID50508.
KEGGhsa:50508.
UCSCuc003qqm.3. human.

Organism-specific databases

CTD50508.
GeneCardsGC06M155716.
HGNCHGNC:7890. NOX3.
MIM607105. gene.
neXtProtNX_Q9HBY0.
PharmGKBPA31691.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287712.
HOGENOMHOG000216669.
HOVERGENHBG003760.
InParanoidQ9HBY0.
KOK08008.
OMAIRGTSIC.
OrthoDBEOG47M1XJ.

Gene expression databases

CleanExHS_NOX3.
GenevestigatorQ9HBY0.
GermOnlineENSG00000074771. Homo sapiens.

Family and domain databases

InterProIPR000778. 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]
PfamPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSPR00466. GP91PHOX.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL1741216.
GenomeRNAi50508.
NextBio53074.
SOURCESearch...

Entry information

Entry nameNOX3_HUMAN
AccessionPrimary (citable) accession number: Q9HBY0
Secondary accession number(s): Q9HBJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents