NOXA1_HUMAN
ID NOXA1_HUMAN Reviewed; 476 AA.
AC Q86UR1; O60533; Q29VU9; Q29VV0; Q2TAM1; Q8IUS3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=NADPH oxidase activator 1;
DE Short=NOX activator 1;
DE AltName: Full=Antigen NY-CO-31;
DE AltName: Full=NCF2-like protein;
DE AltName: Full=P67phox-like factor;
DE AltName: Full=p51-nox;
GN Name=NOXA1; Synonyms=P51NOX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS NOX1 ACTIVATOR.
RC TISSUE=Kidney;
RX PubMed=12657628; DOI=10.1074/jbc.m301289200;
RA Geiszt M., Lekstrom K., Witta J., Leto T.L.;
RT "Proteins homologous to p47phox and p67phox support superoxide production
RT by NAD(P)H oxidase 1 in colon epithelial cells.";
RL J. Biol. Chem. 278:20006-20012(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS NOX1 ACTIVATOR,
RP INTERACTION WITH NCF1; NOXO1 AND RAC1, MUTAGENESIS OF ARG-103 AND TRP-436,
RP AND TISSUE SPECIFICITY.
RX PubMed=12716910; DOI=10.1074/jbc.m212856200;
RA Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H.,
RA Sumimoto H.;
RT "Novel human homologues of p47phox and p67phox participate in activation of
RT superoxide-producing NADPH oxidases.";
RL J. Biol. Chem. 278:25234-25246(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION AS NOX1 ACTIVATOR,
RP MUTAGENESIS OF PRO-34; PRO-37 AND TRP-436, AND VARIANTS LEU-286 AND
RP NOXA1TRUNCATED.
RC TISSUE=Colon adenocarcinoma;
RX PubMed=17602954; DOI=10.1016/j.freeradbiomed.2007.04.022;
RA Valente A.J., Jamali A.E., Epperson T.K., Gamez M.J., Pearson D.W.,
RA Clark R.A.;
RT "NOX1 NADPH oxidase regulation by the NOXA1 SH3 domain.";
RL Free Radic. Biol. Med. 43:384-396(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 245-476 (ISOFORM 1).
RC TISSUE=Colon cancer;
RX PubMed=9610721;
RX DOI=10.1002/(sici)1097-0215(19980529)76:5<652::aid-ijc7>3.0.co;2-p;
RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT "Characterization of human colon cancer antigens recognized by autologous
RT antibodies.";
RL Int. J. Cancer 76:652-658(1998).
RN [7]
RP FUNCTION AS NOX1 ACTIVATOR.
RX PubMed=14617635; DOI=10.1074/jbc.m305968200;
RA Cheng G., Lambeth J.D.;
RT "NOXO1, regulation of lipid binding, localization, and activation of Nox1
RT by the Phox homology (PX) domain.";
RL J. Biol. Chem. 279:4737-4742(2004).
RN [8]
RP FUNCTION AS CYBB AND NOX3 ACTIVATOR, AND MUTAGENESIS OF VAL-205.
RX PubMed=15181005; DOI=10.1074/jbc.m400660200;
RA Cheng G., Ritsick D., Lambeth J.D.;
RT "Nox3 regulation by NOXO1, p47phox, and p67phox.";
RL J. Biol. Chem. 279:34250-34255(2004).
RN [9]
RP FUNCTION.
RX PubMed=14978110; DOI=10.4049/jimmunol.172.5.3051;
RA Kawahara T., Kuwano Y., Teshima-Kondo S., Takeya R., Sumimoto H., Kishi K.,
RA Tsunawaki S., Hirayama T., Rokutan K.;
RT "Role of nicotinamide adenine dinucleotide phosphate oxidase 1 in oxidative
RT burst response to Toll-like receptor 5 signaling in large intestinal
RT epithelial cells.";
RL J. Immunol. 172:3051-3058(2004).
RN [10]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15824103; DOI=10.1074/jbc.m414548200;
RA Ueno N., Takeya R., Miyano K., Kikuchi H., Sumimoto H.;
RT "The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-
RT dependent manner: its regulation by oxidase organizers and activators.";
RL J. Biol. Chem. 280:23328-23339(2005).
RN [11]
RP IDENTIFICATION IN A COMPLEX CONTAINING NOX1; NOXO1; NOXA1 AND RAC1, AND
RP MUTAGENESIS OF ASP-68 AND ARG-103.
RX PubMed=16636067; DOI=10.1074/jbc.m512751200;
RA Cheng G., Diebold B.A., Hughes Y., Lambeth J.D.;
RT "Nox1-dependent reactive oxygen generation is regulated by Rac1.";
RL J. Biol. Chem. 281:17718-17726(2006).
RN [12]
RP SUBCELLULAR LOCATION, INTERACTION WITH RAC1, AND MUTAGENESIS OF ARG-103 AND
RP TRP-436.
RX PubMed=16762923; DOI=10.1074/jbc.m513665200;
RA Miyano K., Ueno N., Takeya R., Sumimoto H.;
RT "Direct involvement of the small GTPase Rac in activation of the
RT superoxide-producing NADPH oxidase Nox1.";
RL J. Biol. Chem. 281:21857-21868(2006).
RN [13]
RP CHARACTERIZATION OF THE FUNCTIONAL NOX1 OXIDASE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16507994; DOI=10.1128/mcb.26.6.2160-2174.2006;
RA Ueyama T., Geiszt M., Leto T.L.;
RT "Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based
RT NADPH oxidases.";
RL Mol. Cell. Biol. 26:2160-2174(2006).
RN [14]
RP INTERACTION WITH NOXO1.
RX PubMed=17126813; DOI=10.1016/j.bbrc.2006.11.060;
RA Yamamoto A., Kami K., Takeya R., Sumimoto H.;
RT "Interaction between the SH3 domains and C-terminal proline-rich region in
RT NADPH oxidase organizer 1 (Noxo1).";
RL Biochem. Biophys. Res. Commun. 352:560-565(2007).
RN [15]
RP INTERACTION WITH YWHAZ, MUTAGENESIS OF SER-172 AND SER-461, AND
RP PHOSPHORYLATION AT SER-172 AND SER-461.
RX PubMed=17913709; DOI=10.1074/jbc.m704754200;
RA Kim J.-S., Diebold B.A., Babior B.M., Knaus U.G., Bokoch G.M.;
RT "Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1 and
RT 14-3-3 binding.";
RL J. Biol. Chem. 282:34787-34800(2007).
RN [16]
RP FUNCTION, AND INTERACTION WITH SH3PXD2A AND SH3PXD2B.
RX PubMed=19755710; DOI=10.1126/scisignal.2000370;
RA Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A., Bokoch G.M.;
RT "Novel p47(phox)-related organizers regulate localized NADPH oxidase 1
RT (Nox1) activity.";
RL Sci. Signal. 2:RA54-RA54(2009).
RN [17]
RP INTERACTION WITH SH3PXD2A AND SH3PXD2B.
RX PubMed=20609497; DOI=10.1016/j.ejcb.2010.05.007;
RA Gianni D., Dermardirossian C., Bokoch G.M.;
RT "Direct interaction between Tks proteins and the N-terminal proline-rich
RT region (PRR) of NoxA1 mediates Nox1-dependent ROS generation.";
RL Eur. J. Cell Biol. 90:164-171(2011).
CC -!- FUNCTION: Functions as an activator of NOX1, a superoxide-producing
CC NADPH oxidase. Functions in the production of reactive oxygen species
CC (ROS) which participate in a variety of biological processes including
CC host defense, hormone biosynthesis, oxygen sensing and signal
CC transduction. May also activate CYBB/gp91phox and NOX3.
CC {ECO:0000269|PubMed:12657628, ECO:0000269|PubMed:12716910,
CC ECO:0000269|PubMed:14617635, ECO:0000269|PubMed:14978110,
CC ECO:0000269|PubMed:15181005, ECO:0000269|PubMed:15824103,
CC ECO:0000269|PubMed:17602954, ECO:0000269|PubMed:19755710}.
CC -!- SUBUNIT: NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional
CC multimeric complex supporting ROS production. Interaction with YWHAZ
CC prevents the interaction of NOXA1 with NOXO1 and RAC1 and its targeting
CC to membranes, hence reducing its ability to activate NOX1. Interacts
CC (via N-terminus) with SH3PXD2A and SH3PXD2B; the interaction is direct.
CC {ECO:0000269|PubMed:12716910, ECO:0000269|PubMed:16636067,
CC ECO:0000269|PubMed:16762923, ECO:0000269|PubMed:17126813,
CC ECO:0000269|PubMed:17913709, ECO:0000269|PubMed:19755710,
CC ECO:0000269|PubMed:20609497}.
CC -!- INTERACTION:
CC Q86UR1; Q8NFA2-3: NOXO1; NbExp=5; IntAct=EBI-949814, EBI-20557410;
CC Q86UR1; Q9UFD9: RIMBP3; NbExp=4; IntAct=EBI-949814, EBI-10182375;
CC Q86UR1-2; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-12025760, EBI-14493093;
CC Q86UR1-2; Q5BKX5-3: C19orf54; NbExp=5; IntAct=EBI-12025760, EBI-11976299;
CC Q86UR1-2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-12025760, EBI-739624;
CC Q86UR1-2; P27918: CFP; NbExp=3; IntAct=EBI-12025760, EBI-9038570;
CC Q86UR1-2; P05813: CRYBA1; NbExp=3; IntAct=EBI-12025760, EBI-7043337;
CC Q86UR1-2; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-12025760, EBI-751587;
CC Q86UR1-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12025760, EBI-3867333;
CC Q86UR1-2; Q9H816: DCLRE1B; NbExp=3; IntAct=EBI-12025760, EBI-3508943;
CC Q86UR1-2; O95865: DDAH2; NbExp=3; IntAct=EBI-12025760, EBI-749139;
CC Q86UR1-2; Q13115: DUSP4; NbExp=3; IntAct=EBI-12025760, EBI-6591081;
CC Q86UR1-2; Q8WXI9: GATAD2B; NbExp=3; IntAct=EBI-12025760, EBI-923440;
CC Q86UR1-2; Q14005-2: IL16; NbExp=6; IntAct=EBI-12025760, EBI-17178971;
CC Q86UR1-2; Q96SI1-2: KCTD15; NbExp=3; IntAct=EBI-12025760, EBI-12382297;
CC Q86UR1-2; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-12025760, EBI-11992140;
CC Q86UR1-2; Q3LI73: KRTAP19-4; NbExp=3; IntAct=EBI-12025760, EBI-12958461;
CC Q86UR1-2; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-12025760, EBI-10241353;
CC Q86UR1-2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12025760, EBI-10261141;
CC Q86UR1-2; Q14847-2: LASP1; NbExp=3; IntAct=EBI-12025760, EBI-9088686;
CC Q86UR1-2; P25791-3: LMO2; NbExp=3; IntAct=EBI-12025760, EBI-11959475;
CC Q86UR1-2; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-12025760, EBI-8487781;
CC Q86UR1-2; Q6PF18: MORN3; NbExp=3; IntAct=EBI-12025760, EBI-9675802;
CC Q86UR1-2; Q8WY64: MYLIP; NbExp=5; IntAct=EBI-12025760, EBI-6952711;
CC Q86UR1-2; P41227: NAA10; NbExp=6; IntAct=EBI-12025760, EBI-747693;
CC Q86UR1-2; Q6IA69: NADSYN1; NbExp=3; IntAct=EBI-12025760, EBI-748610;
CC Q86UR1-2; O14561: NDUFAB1; NbExp=3; IntAct=EBI-12025760, EBI-1246261;
CC Q86UR1-2; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-12025760, EBI-12025760;
CC Q86UR1-2; Q99471: PFDN5; NbExp=3; IntAct=EBI-12025760, EBI-357275;
CC Q86UR1-2; O15496: PLA2G10; NbExp=3; IntAct=EBI-12025760, EBI-726466;
CC Q86UR1-2; P47897: QARS1; NbExp=3; IntAct=EBI-12025760, EBI-347462;
CC Q86UR1-2; Q04864-2: REL; NbExp=3; IntAct=EBI-12025760, EBI-10829018;
CC Q86UR1-2; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-12025760, EBI-10182375;
CC Q86UR1-2; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-12025760, EBI-10269322;
CC Q86UR1-2; Q53HV7-2: SMUG1; NbExp=4; IntAct=EBI-12025760, EBI-12275818;
CC Q86UR1-2; Q9Y242: TCF19; NbExp=3; IntAct=EBI-12025760, EBI-7413767;
CC Q86UR1-2; P15884-3: TCF4; NbExp=3; IntAct=EBI-12025760, EBI-13636688;
CC Q86UR1-2; Q96RS0: TGS1; NbExp=3; IntAct=EBI-12025760, EBI-949244;
CC Q86UR1-2; Q12933: TRAF2; NbExp=3; IntAct=EBI-12025760, EBI-355744;
CC Q86UR1-2; P36406: TRIM23; NbExp=3; IntAct=EBI-12025760, EBI-740098;
CC Q86UR1-2; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-12025760, EBI-2514383;
CC Q86UR1-2; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-12025760, EBI-7705033;
CC Q86UR1-2; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-12025760, EBI-14104088;
CC Q86UR1-2; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-12025760, EBI-17269964;
CC Q86UR1-2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-12025760, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocation to
CC membranes depends on NOXO1 or NCF1 and maybe RAC1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86UR1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86UR1-2; Sequence=VSP_030336;
CC Name=3; Synonyms=NOXA1inhib;
CC IsoId=Q86UR1-3; Sequence=VSP_030335, VSP_030336;
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in pancreas, liver,
CC kidney, spleen, prostate, small intestine and colon.
CC {ECO:0000269|PubMed:12716910}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal kidney.
CC {ECO:0000269|PubMed:15824103}.
CC -!- DOMAIN: The SH3 domain mediates interaction with NOXO1 and NCF1 and has
CC autoregulatory function.
CC -!- DOMAIN: The TPR repeats mediate interaction with RAC1.
CC -!- PTM: Interaction with YWHAZ depends on phosphorylation by PKA.
CC {ECO:0000269|PubMed:17913709}.
CC -!- MISCELLANEOUS: [Isoform 2]: Mostly inactive for NOX1 activation. Does
CC not interact with NOXO1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Inactive for NOX1 activation.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NCF2/NOXA1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY16126.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY255769; AAP13480.1; -; mRNA.
DR EMBL; AB095031; BAC76710.1; -; mRNA.
DR EMBL; AY927790; AAY16126.1; ALT_FRAME; mRNA.
DR EMBL; AY927791; AAY16127.1; -; mRNA.
DR EMBL; BX322799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041594; AAH41594.1; -; mRNA.
DR EMBL; BC110840; AAI10841.1; -; mRNA.
DR EMBL; AF039697; AAC18046.1; -; mRNA.
DR CCDS; CCDS59157.1; -. [Q86UR1-3]
DR CCDS; CCDS7042.1; -. [Q86UR1-2]
DR RefSeq; NP_001242996.1; NM_001256067.1. [Q86UR1-1]
DR RefSeq; NP_001242997.1; NM_001256068.1. [Q86UR1-3]
DR RefSeq; NP_006638.1; NM_006647.1. [Q86UR1-2]
DR PDB; 7CFZ; X-ray; 1.89 A; A/B=397-461.
DR PDBsum; 7CFZ; -.
DR AlphaFoldDB; Q86UR1; -.
DR SMR; Q86UR1; -.
DR BioGRID; 116025; 58.
DR ELM; Q86UR1; -.
DR IntAct; Q86UR1; 50.
DR MINT; Q86UR1; -.
DR STRING; 9606.ENSP00000342848; -.
DR iPTMnet; Q86UR1; -.
DR PhosphoSitePlus; Q86UR1; -.
DR BioMuta; NOXA1; -.
DR DMDM; 74759404; -.
DR EPD; Q86UR1; -.
DR jPOST; Q86UR1; -.
DR MassIVE; Q86UR1; -.
DR PaxDb; Q86UR1; -.
DR PeptideAtlas; Q86UR1; -.
DR PRIDE; Q86UR1; -.
DR ProteomicsDB; 69867; -. [Q86UR1-1]
DR ProteomicsDB; 69868; -. [Q86UR1-2]
DR ProteomicsDB; 69869; -. [Q86UR1-3]
DR Antibodypedia; 32446; 142 antibodies from 28 providers.
DR DNASU; 10811; -.
DR Ensembl; ENST00000341349.6; ENSP00000342848.2; ENSG00000188747.9. [Q86UR1-2]
DR Ensembl; ENST00000392815.2; ENSP00000376562.2; ENSG00000188747.9. [Q86UR1-3]
DR Ensembl; ENST00000683555.1; ENSP00000507846.1; ENSG00000188747.9. [Q86UR1-1]
DR GeneID; 10811; -.
DR KEGG; hsa:10811; -.
DR MANE-Select; ENST00000683555.1; ENSP00000507846.1; NM_001256067.2; NP_001242996.1.
DR UCSC; uc004cmu.4; human. [Q86UR1-1]
DR CTD; 10811; -.
DR DisGeNET; 10811; -.
DR GeneCards; NOXA1; -.
DR HGNC; HGNC:10668; NOXA1.
DR HPA; ENSG00000188747; Low tissue specificity.
DR MIM; 611255; gene.
DR neXtProt; NX_Q86UR1; -.
DR OpenTargets; ENSG00000188747; -.
DR PharmGKB; PA35598; -.
DR VEuPathDB; HostDB:ENSG00000188747; -.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00530000063843; -.
DR HOGENOM; CLU_041290_1_0_1; -.
DR InParanoid; Q86UR1; -.
DR OMA; PYMARGP; -.
DR OrthoDB; 431898at2759; -.
DR PhylomeDB; Q86UR1; -.
DR TreeFam; TF329087; -.
DR PathwayCommons; Q86UR1; -.
DR Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping.
DR SignaLink; Q86UR1; -.
DR SIGNOR; Q86UR1; -.
DR BioGRID-ORCS; 10811; 11 hits in 1059 CRISPR screens.
DR GeneWiki; NOXA1; -.
DR GenomeRNAi; 10811; -.
DR Pharos; Q86UR1; Tbio.
DR PRO; PR:Q86UR1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q86UR1; protein.
DR Bgee; ENSG00000188747; Expressed in pancreatic ductal cell and 164 other tissues.
DR Genevisible; Q86UR1; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043020; C:NADPH oxidase complex; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:BHF-UCL.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IDA:UniProtKB.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:BHF-UCL.
DR GO; GO:0060263; P:regulation of respiratory burst; IMP:BHF-UCL.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR034899; NOXA1.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR15175:SF4; PTHR15175:SF4; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; TPR repeat.
FT CHAIN 1..476
FT /note="NADPH oxidase activator 1"
FT /id="PRO_0000314609"
FT REPEAT 7..38
FT /note="TPR 1"
FT REPEAT 39..71
FT /note="TPR 2"
FT REPEAT 73..105
FT /note="TPR 3"
FT REPEAT 122..155
FT /note="TPR 4"
FT DOMAIN 315..395
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 399..458
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..224
FT /note="Mediates interaction with RAC1"
FT REGION 259..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:17913709"
FT MOD_RES 461
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:17913709"
FT VAR_SEQ 168..223
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17602954"
FT /id="VSP_030335"
FT VAR_SEQ 431
FT /note="E -> EEPDVPLA (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17602954"
FT /id="VSP_030336"
FT VARIANT 274..476
FT /note="Missing (found in a truncated form isolated from
FT Caco-2 cells treated with butyrate)"
FT /id="VAR_037985"
FT VARIANT 286
FT /note="P -> L (in dbSNP:rs34155071)"
FT /evidence="ECO:0000269|PubMed:17602954"
FT /id="VAR_037986"
FT MUTAGEN 34
FT /note="P->A: Partial loss of function."
FT /evidence="ECO:0000269|PubMed:17602954"
FT MUTAGEN 37
FT /note="P->A: Partial loss of function."
FT /evidence="ECO:0000269|PubMed:17602954"
FT MUTAGEN 68
FT /note="D->A: Loss of function and loss of interaction with
FT RAC1."
FT /evidence="ECO:0000269|PubMed:16636067"
FT MUTAGEN 103
FT /note="R->E: Loss of function and loss of interaction with
FT RAC1. Loss of localization to membranes."
FT /evidence="ECO:0000269|PubMed:12716910,
FT ECO:0000269|PubMed:16636067, ECO:0000269|PubMed:16762923"
FT MUTAGEN 172
FT /note="S->A: Loss of phosphorylation. Loss of interaction
FT with YHAWZ; when associated with A-461."
FT /evidence="ECO:0000269|PubMed:17913709"
FT MUTAGEN 172
FT /note="S->E: Constitutively interacts with YWHAZ; when
FT associated with E-461."
FT /evidence="ECO:0000269|PubMed:17913709"
FT MUTAGEN 205
FT /note="V->A: Unable to activate NOX2."
FT /evidence="ECO:0000269|PubMed:15181005"
FT MUTAGEN 436
FT /note="W->R: Loss of interaction with NOXO1 and NCF1. Loss
FT of localization to membranes. Partial loss of function."
FT /evidence="ECO:0000269|PubMed:12716910,
FT ECO:0000269|PubMed:16762923, ECO:0000269|PubMed:17602954"
FT MUTAGEN 461
FT /note="S->A: Loss of phosphorylation. Loss of interaction
FT with YHAWZ; when associated with A-172."
FT /evidence="ECO:0000269|PubMed:17913709"
FT MUTAGEN 461
FT /note="S->E: Constitutively interacts with YWHAZ; when
FT associated with E-172."
FT /evidence="ECO:0000269|PubMed:17913709"
FT CONFLICT 51
FT /note="A -> T (in Ref. 3; AAY16126)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="A -> T (in Ref. 3; AAY16127)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="V -> L (in Ref. 3; AAY16127)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="A -> T (in Ref. 3; AAY16127)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="T -> A (in Ref. 3; AAY16126)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="K -> E (in Ref. 3; AAY16126)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="Q -> V (in Ref. 6; AAC18046)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="C -> R (in Ref. 3; AAY16127)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="R -> G (in Ref. 6; AAC18046)"
FT /evidence="ECO:0000305"
FT CONFLICT 345..346
FT /note="LP -> FL (in Ref. 6; AAC18046)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="L -> F (in Ref. 6; AAC18046)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="S -> R (in Ref. 6; AAC18046)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="C -> R (in Ref. 5; AAI10841)"
FT /evidence="ECO:0000305"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:7CFZ"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:7CFZ"
FT STRAND 433..441
FT /evidence="ECO:0007829|PDB:7CFZ"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:7CFZ"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:7CFZ"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:7CFZ"
SQ SEQUENCE 476 AA; 50933 MW; 64DFBF64C59722AD CRC64;
MASLGDLVRA WHLGAQAVDR GDWARALHLF SGVPAPPARL CFNAGCVHLL AGDPEAALRA
FDQAVTKDTC MAVGFFQRGV ANFQLARFQE ALSDFWLALE QLRGHAAIDY TQLGLRFKLQ
AWEVLHNVAS AQCQLGLWTE AASSLREAMS KWPEGSLNGL DSALDQVQRR GSLPPRQVPR
GEVFRPHRWH LKHLEPVDFL GKAKVVASAI PDDQGWGVRP QQPQGPGANH DARSLIMDSP
RAGTHQGPLD AETEVGADRC TSTAYQEQRP QVEQVGKQAP LSPGLPAMGG PGPGPCEDPA
GAGGAGAGGS EPLVTVTVQC AFTVALRARR GADLSSLRAL LGQALPHQAQ LGQLSYLAPG
EDGHWVPIPE EESLQRAWQD AAACPRGLQL QCRGAGGRPV LYQVVAQHSY SAQGPEDLGF
RQGDTVDVLC EVDQAWLEGH CDGRIGIFPK CFVVPAGPRM SGAPGRLPRS QQGDQP
