NOX1_RAT
ID NOX1_RAT Reviewed; 563 AA.
AC Q9WV87;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=NADPH oxidase 1;
DE Short=NOX-1;
DE EC=1.-.-.-;
DE AltName: Full=Mitogenic oxidase 1;
DE Short=MOX-1;
DE AltName: Full=NADH/NADPH mitogenic oxidase subunit P65-MOX;
DE AltName: Full=NOH-1;
GN Name=Nox1; Synonyms=Mox1, Noh1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon epithelium;
RX PubMed=10485709; DOI=10.1038/43459;
RA Suh Y.-A., Arnold R.S., Lassegue B., Shi J., Xu X., Sorescu D., Chung A.B.,
RA Griendling K.K., Lambeth J.D.;
RT "Cell transformation by the superoxide-generating oxidase Mox1.";
RL Nature 401:79-82(1999).
CC -!- FUNCTION: Pyridine nucleotide-dependent oxidoreductase that generates
CC superoxide and might conduct H(+) ions as part of its electron
CC transport mechanism.
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: The oxidase activity is potentiated by NOXA1 and
CC NOXO1. {ECO:0000250}.
CC -!- SUBUNIT: NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional
CC multimeric complex supporting ROS production. Interacts with NOXA1 and
CC NOXO1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, invadopodium membrane
CC {ECO:0000250|UniProtKB:Q9Y5S8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Y5S8}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Y5S8}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular smooth muscle cells.
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DR EMBL; AF152963; AAD39542.1; -; mRNA.
DR RefSeq; NP_446135.1; NM_053683.1.
DR AlphaFoldDB; Q9WV87; -.
DR SMR; Q9WV87; -.
DR STRING; 10116.ENSRNOP00000065995; -.
DR ChEMBL; CHEMBL1075231; -.
DR PeroxiBase; 5408; RnoNOx01.
DR GlyGen; Q9WV87; 2 sites.
DR iPTMnet; Q9WV87; -.
DR PhosphoSitePlus; Q9WV87; -.
DR PaxDb; Q9WV87; -.
DR GeneID; 114243; -.
DR KEGG; rno:114243; -.
DR CTD; 27035; -.
DR RGD; 620598; Nox1.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; Q9WV87; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; Q9WV87; -.
DR Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q9WV87; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0043020; C:NADPH oxidase complex; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IMP:CACAO.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0071455; P:cellular response to hyperoxia; ISO:RGD.
DR GO; GO:1990451; P:cellular stress response to acidic pH; ISO:RGD.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; ISO:RGD.
DR GO; GO:0051454; P:intracellular pH elevation; ISO:RGD.
DR GO; GO:0072592; P:oxygen metabolic process; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISO:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; ISO:RGD.
DR GO; GO:0000302; P:response to reactive oxygen species; IDA:RGD.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR GO; GO:0042554; P:superoxide anion generation; IMP:BHF-UCL.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR029650; NOX1.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF71; PTHR11972:SF71; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Cell projection; Electron transport; FAD;
KW Flavoprotein; Glycoprotein; Heme; Iron; Membrane; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..563
FT /note="NADPH oxidase 1"
FT /id="PRO_0000210149"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..395
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..282
FT /note="Ferric oxidoreductase"
FT DOMAIN 283..390
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 396..535
FT /note="Interaction with NOXO1"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 115
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 208
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 220
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 337..343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 563 AA; 65177 MW; 2B74BCA021CC3335 CRC64;
MGNWLVNHWL SVLFLVSWLG LNIFLFVYVF LNYEKSDKYY YTREILGTAL ALARASALCL
NFNSMVILIP VCRNLLSFLR GTCSFCNHTL RKPLDHNLTF HKLVAYMICI FTAIHIIAHL
FNFERYSRSQ QAMDGSLASV LSSLFHPEKE DSWLNPIQSP NVTVMYAAFT SIAGLTGVVA
TVALVLMVTS AMEFIRRNYF ELFWYTHHLF IIYIICLGIH GLGGIVRGQT EESMSESHPR
NCSYSFHEWD KYERSCRSPH FVGQPPESWK WILAPIAFYI FERILRFYRS RQKVVITKVV
MHPCKVLELQ MRKRGFTMGI GQYIFVNCPS ISFLEWHPFT LTSAPEEEFF SIHIRAAGDW
TENLIRTFEQ QHSPMPRIEV DGPFGTVSED VFQYEVAVLV GAGIGVTPFA SFLKSIWYKF
QRAHNKLKTQ KIYFYWICRE TGAFAWFNNL LNSLEQEMDE LGKPDFLNYR LFLTGWDSNI
AGHAALNFDR ATDVLTGLKQ KTSFGRPMWD NEFSRIATAH PKSVVGVFLC GPPTLAKSLR
KCCRRYSSLD PRKVQFYFNK ETF
