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Protein

NADPH oxidase 1

Gene

Nox1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

The oxidase activity is potentiated by NOXA1 and NOXO1.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011Iron (heme axial ligand)Curated
Metal bindingi115 – 1151Iron (heme axial ligand)Curated
Metal bindingi208 – 2081Iron (heme axial ligand)Curated
Metal bindingi220 – 2201Iron (heme axial ligand)Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi337 – 3437FADSequence analysis

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • superoxide-generating NADPH oxidase activity Source: RGD

GO - Biological processi

  • positive regulation of reactive oxygen species metabolic process Source: RGD
  • positive regulation of smooth muscle cell proliferation Source: BHF-UCL
  • response to reactive oxygen species Source: RGD
  • signal transduction Source: RGD
  • superoxide anion generation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

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

Protein family/group databases

PeroxiBasei5408. RnoNOx01.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH oxidase 1 (EC:1.-.-.-)
Short name:
NOX-1
Alternative name(s):
Mitogenic oxidase 1
Short name:
MOX-1
NADH/NADPH mitogenic oxidase subunit P65-MOX
NOH-1
Gene namesi
Name:Nox1
Synonyms:Mox1, Noh1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620598. 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 – 88CytoplasmicSequence analysis
Transmembranei9 – 3123HelicalSequence analysisAdd
BLAST
Topological domaini32 – 4413ExtracellularSequence analysisAdd
BLAST
Transmembranei45 – 6925HelicalSequence analysisAdd
BLAST
Topological domaini70 – 10233CytoplasmicSequence analysisAdd
BLAST
Transmembranei103 – 12321HelicalSequence analysisAdd
BLAST
Topological domaini124 – 16744ExtracellularSequence analysisAdd
BLAST
Transmembranei168 – 18821HelicalSequence analysisAdd
BLAST
Topological domaini189 – 20618CytoplasmicSequence analysisAdd
BLAST
Transmembranei207 – 22721HelicalSequence analysisAdd
BLAST
Topological domaini228 – 395168ExtracellularSequence analysisAdd
BLAST
Transmembranei396 – 41621HelicalSequence analysisAdd
BLAST
Topological domaini417 – 563147CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • invadopodium membrane Source: UniProtKB-SubCell
  • NADPH oxidase complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075231.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 563563NADPH oxidase 1PRO_0000210149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9WV87.

PTM databases

iPTMnetiQ9WV87.
PhosphoSiteiQ9WV87.

Expressioni

Tissue specificityi

Expressed in vascular smooth muscle cells.

Interactioni

Subunit structurei

NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional multimeric complex supporting ROS production. Interacts with NOXA1 and NOXO1 (By similarity).By similarity

Protein-protein interaction databases

MINTiMINT-4998488.
STRINGi10116.ENSRNOP00000065995.

Structurei

3D structure databases

ProteinModelPortaliQ9WV87.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 282229Ferric oxidoreductaseAdd
BLAST
Domaini283 – 390108FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni396 – 535140Interaction 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.
HOVERGENiHBG003760.
InParanoidiQ9WV87.
KOiK08008.
PhylomeDBiQ9WV87.

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]

Sequencei

Sequence statusi: Complete.

Q9WV87-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNWLVNHWL SVLFLVSWLG LNIFLFVYVF LNYEKSDKYY YTREILGTAL
60 70 80 90 100
ALARASALCL NFNSMVILIP VCRNLLSFLR GTCSFCNHTL RKPLDHNLTF
110 120 130 140 150
HKLVAYMICI FTAIHIIAHL FNFERYSRSQ QAMDGSLASV LSSLFHPEKE
160 170 180 190 200
DSWLNPIQSP NVTVMYAAFT SIAGLTGVVA TVALVLMVTS AMEFIRRNYF
210 220 230 240 250
ELFWYTHHLF IIYIICLGIH GLGGIVRGQT EESMSESHPR NCSYSFHEWD
260 270 280 290 300
KYERSCRSPH FVGQPPESWK WILAPIAFYI FERILRFYRS RQKVVITKVV
310 320 330 340 350
MHPCKVLELQ MRKRGFTMGI GQYIFVNCPS ISFLEWHPFT LTSAPEEEFF
360 370 380 390 400
SIHIRAAGDW TENLIRTFEQ QHSPMPRIEV DGPFGTVSED VFQYEVAVLV
410 420 430 440 450
GAGIGVTPFA SFLKSIWYKF QRAHNKLKTQ KIYFYWICRE TGAFAWFNNL
460 470 480 490 500
LNSLEQEMDE LGKPDFLNYR LFLTGWDSNI AGHAALNFDR ATDVLTGLKQ
510 520 530 540 550
KTSFGRPMWD NEFSRIATAH PKSVVGVFLC GPPTLAKSLR KCCRRYSSLD
560
PRKVQFYFNK ETF
Length:563
Mass (Da):65,177
Last modified:November 1, 1999 - v1
Checksum:i2B74BCA021CC3335
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF152963 mRNA. Translation: AAD39542.1.
RefSeqiNP_446135.1. NM_053683.1.
UniGeneiRn.220465.

Genome annotation databases

GeneIDi114243.
KEGGirno:114243.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF152963 mRNA. Translation: AAD39542.1.
RefSeqiNP_446135.1. NM_053683.1.
UniGeneiRn.220465.

3D structure databases

ProteinModelPortaliQ9WV87.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4998488.
STRINGi10116.ENSRNOP00000065995.

Chemistry

ChEMBLiCHEMBL1075231.

Protein family/group databases

PeroxiBasei5408. RnoNOx01.

PTM databases

iPTMnetiQ9WV87.
PhosphoSiteiQ9WV87.

Proteomic databases

PaxDbiQ9WV87.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi114243.
KEGGirno:114243.

Organism-specific databases

CTDi27035.
RGDi620598. Nox1.

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
HOVERGENiHBG003760.
InParanoidiQ9WV87.
KOiK08008.
PhylomeDBiQ9WV87.

Miscellaneous databases

PROiQ9WV87.

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...

Entry informationi

Entry nameiNOX1_RAT
AccessioniPrimary (citable) accession number: Q9WV87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 97 of the entry and version 1 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. 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.