NOX1_MOUSE
ID NOX1_MOUSE Reviewed; 591 AA.
AC Q8CIZ9; A2AEK5; Q0KKX3; Q0KKX5; Q811U2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=NADPH oxidase 1;
DE Short=NOX-1;
DE EC=1.-.-.-;
GN Name=Nox1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH NOXO1, AND
RP ACTIVITY REGULATION.
RC STRAIN=BALB/cJ;
RX PubMed=12473664; DOI=10.1074/jbc.c200613200;
RA Banfi B., Clark R.A., Steger K., Krause K.-H.;
RT "Two novel proteins activate superoxide generation by the NADPH oxidase
RT NOX1.";
RL J. Biol. Chem. 278:3510-3513(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-75 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 29-75 (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP AND INDUCTION.
RC TISSUE=Colon, and Vascular smooth muscle;
RX PubMed=16724959; DOI=10.1042/bj20060300;
RA Arakawa N., Katsuyama M., Matsuno K., Urao N., Tabuchi Y., Okigaki M.,
RA Matsubara H., Yabe-Nishimura C.;
RT "Novel transcripts of Nox1 are regulated by alternative promoters and
RT expressed under phenotypic modulation of vascular smooth muscle cells.";
RL Biochem. J. 398:303-310(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 116-565 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J;
RA Matsumoto Y., Blanchard T.G.;
RT "Nox1 expression in the gastric mucosa of Helicobacter-infected
RT gp91phox-/- mice.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pyridine nucleotide-dependent oxidoreductase that generates
CC superoxide and might conduct H(+) ions as part of its electron
CC transport mechanism. {ECO:0000269|PubMed:16724959}.
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:0000269|PubMed:12473664}.
CC -!- SUBUNIT: NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional
CC multimeric complex supporting ROS production. Interacts with NOXA1 and
CC NOXO1. {ECO:0000269|PubMed:12473664}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=f-type, c-type;
CC IsoId=Q8CIZ9-1; Sequence=Displayed;
CC Name=2; Synonyms=a-type;
CC IsoId=Q8CIZ9-2; Sequence=VSP_038574;
CC Name=3;
CC IsoId=Q8CIZ9-3; Sequence=VSP_038574, VSP_038575;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in colon and vascular smooth
CC muscle cells (VSMC). {ECO:0000269|PubMed:16724959}.
CC -!- INDUCTION: [Isoform 1]: (c-type) induced in VSMC by angiotensin II and
CC injury to the artery. {ECO:0000269|PubMed:16724959}.
CC -!- MISCELLANEOUS: [Isoform 1]: Product of f-type and c-type mRNA, which
CC differ only in 5'-UTR.
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DR EMBL; AF539799; AAN75144.1; -; mRNA.
DR EMBL; AK136432; BAE22974.1; -; mRNA.
DR EMBL; AL671915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB206383; BAF03561.1; -; mRNA.
DR EMBL; AB206384; BAF03562.1; -; mRNA.
DR EMBL; AB206385; BAF03563.1; -; mRNA.
DR EMBL; AY174116; AAO20852.1; -; mRNA.
DR CCDS; CCDS30390.1; -. [Q8CIZ9-2]
DR RefSeq; NP_757340.1; NM_172203.2. [Q8CIZ9-2]
DR RefSeq; XP_006528578.1; XM_006528515.3. [Q8CIZ9-1]
DR AlphaFoldDB; Q8CIZ9; -.
DR SMR; Q8CIZ9; -.
DR STRING; 10090.ENSMUSP00000033610; -.
DR PeroxiBase; 5963; MmNOx01.
DR GlyGen; Q8CIZ9; 2 sites.
DR iPTMnet; Q8CIZ9; -.
DR PhosphoSitePlus; Q8CIZ9; -.
DR MaxQB; Q8CIZ9; -.
DR PaxDb; Q8CIZ9; -.
DR PRIDE; Q8CIZ9; -.
DR ProteomicsDB; 252992; -. [Q8CIZ9-1]
DR ProteomicsDB; 252993; -. [Q8CIZ9-2]
DR ProteomicsDB; 252994; -. [Q8CIZ9-3]
DR Antibodypedia; 28538; 370 antibodies from 33 providers.
DR DNASU; 237038; -.
DR Ensembl; ENSMUST00000033610; ENSMUSP00000033610; ENSMUSG00000031257. [Q8CIZ9-2]
DR Ensembl; ENSMUST00000113275; ENSMUSP00000108900; ENSMUSG00000031257. [Q8CIZ9-3]
DR GeneID; 237038; -.
DR KEGG; mmu:237038; -.
DR UCSC; uc009ufl.2; mouse. [Q8CIZ9-1]
DR CTD; 27035; -.
DR MGI; MGI:2450016; Nox1.
DR VEuPathDB; HostDB:ENSMUSG00000031257; -.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000161632; -.
DR HOGENOM; CLU_005646_3_1_1; -.
DR InParanoid; Q8CIZ9; -.
DR OMA; HRTYISK; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; Q8CIZ9; -.
DR TreeFam; TF105354; -.
DR BRENDA; 1.6.3.1; 3474.
DR Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 237038; 1 hit in 76 CRISPR screens.
DR PRO; PR:Q8CIZ9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8CIZ9; protein.
DR Bgee; ENSMUSG00000031257; Expressed in ileum and 40 other tissues.
DR ExpressionAtlas; Q8CIZ9; baseline and differential.
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; IDA:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; IMP:MGI.
DR GO; GO:0043020; C:NADPH oxidase complex; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IMP:MGI.
DR GO; GO:0001525; P:angiogenesis; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0071455; P:cellular response to hyperoxia; IMP:MGI.
DR GO; GO:1990451; P:cellular stress response to acidic pH; ISO:MGI.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; ISO:MGI.
DR GO; GO:0051454; P:intracellular pH elevation; ISO:MGI.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI.
DR GO; GO:0007254; P:JNK cascade; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0072592; P:oxygen metabolic process; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IEA:Ensembl.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IMP:MGI.
DR GO; GO:0000302; P:response to reactive oxygen species; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0042554; P:superoxide anion generation; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Electron transport; FAD; Flavoprotein; Glycoprotein; Heme; Iron; Membrane;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..591
FT /note="NADPH oxidase 1"
FT /id="PRO_0000322982"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 82..316
FT /note="Ferric oxidoreductase"
FT DOMAIN 317..418
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 424..563
FT /note="Interaction with NOXO1"
FT /evidence="ECO:0000250"
FT BINDING 129
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 143
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 236
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 248
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 365..371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12473664,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:16724959"
FT /id="VSP_038574"
FT VAR_SEQ 460..508
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038575"
SQ SEQUENCE 591 AA; 68193 MW; B2D4AE54186A066B CRC64;
MAGELRGSRG PLQRIQIAPR EAPNLHLTMG NWLVNHWLSV LFLVSWLGLN IFLFVYAFLN
YEKSDKYYYT REILGTALAL ARASALCLNF NSMMILIPVC RNLLSFLRGT CSFCNRTLRK
PLDHNLTFHK LVAYMICIFT VIHIIAHLFN FERYRRSQQA MDGSLASVLS SLSHPEKEDS
WLNPIQSPNM TVMYAAFTSI AGLTGVIATV ALVLMVTSAM EFIRRNYFEL FWYTHHLFIV
YIICLGIHGL GGIVRGQTEE SLGESHPHNC SHSFHEWDDH KGSCRHPHFA GHPPESWKWI
LAPIAFYIFE RILRFYRSQQ KVVITKVVMH PSNVLELQMR KRGFSMEVGQ YIFVNCPSIS
FLEWHPFTLT SAPEEEFFSV HIRAAGDWTR NLIRTFEQQH SPMPRIEVDG PFGTVSEDVF
QYEVAVLVGA GIGVTPFASI LKSIWYKFQR ADNKLKTQKI YFYWICRETG AFAWFNNLLN
SLEQEMEELG KMDFLNYRLF LTGWDSNIAG HAALNFDRAT DILTGLKQKT SFGRPMWDNE
FSRIATAHPK SAVGVFLCGP RTLAKSLRKR CQRYSSLDPR KVQFYFNKET F
