NOXA1_MOUSE
ID NOXA1_MOUSE Reviewed; 444 AA.
AC Q8CJ00; A2AJA1; Q80SY2; Q8BU68;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=NADPH oxidase activator 1;
GN Name=Noxa1;
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 1), FUNCTION AS NOX1 ACTIVATOR, AND
RP TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Colon;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=FVB/N; TISSUE=Colon;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=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 FUNCTION.
RX PubMed=15326186; DOI=10.1074/jbc.m403046200;
RA Banfi B., Malgrange B., Knisz J., Steger K., Dubois-Dauphin M.,
RA Krause K.-H.;
RT "NOX3, a superoxide-generating NADPH oxidase of the inner ear.";
RL J. Biol. Chem. 279:46065-46072(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15949904; DOI=10.1016/j.gene.2005.03.008;
RA Cheng G., Lambeth J.D.;
RT "Alternative mRNA splice forms of NOXO1: differential tissue expression and
RT regulation of Nox1 and Nox3.";
RL Gene 356:118-126(2005).
RN [8]
RP FUNCTION, INTERACTION WITH NOX1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16814099; DOI=10.1016/j.freeradbiomed.2005.12.035;
RA Ambasta R.K., Schreiber J.G., Janiszewski M., Busse R., Brandes R.P.;
RT "Noxa1 is a central component of the smooth muscle NADPH oxidase in mice.";
RL Free Radic. Biol. Med. 41:193-201(2006).
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:12473664, ECO:0000269|PubMed:15326186,
CC ECO:0000269|PubMed:16814099}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16814099}. Cell
CC membrane {ECO:0000269|PubMed:16814099}. Note=Translocation to membranes
CC depends on NOXO1 or NCF1 and maybe RAC1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CJ00-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CJ00-2; Sequence=VSP_030337;
CC -!- TISSUE SPECIFICITY: Widely expressed with a tissue distribution similar
CC to the one of NOX1. Detected in colon, uterus, prostate, small
CC intestine, stomach, lung, thyroid, aorta, inner ear and salivary
CC glands. Expressed in colon, small intestine and aortic smooth muscle
CC cells (at protein level). {ECO:0000269|PubMed:12473664,
CC ECO:0000269|PubMed:12657628, ECO:0000269|PubMed:15949904,
CC ECO:0000269|PubMed:16814099}.
CC -!- DOMAIN: The SH3 domain mediates interaction with NOXO1 and NCF1 and has
CC autoregulatory function. {ECO:0000250}.
CC -!- DOMAIN: The TPR repeats mediate interaction with RAC1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NCF2/NOXA1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF539798; AAN75143.1; -; mRNA.
DR EMBL; AY255770; AAP13481.1; -; mRNA.
DR EMBL; AK087263; BAC39832.1; -; mRNA.
DR EMBL; AL732585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047532; AAH47532.1; -; mRNA.
DR CCDS; CCDS15749.1; -. [Q8CJ00-1]
DR CCDS; CCDS50524.1; -. [Q8CJ00-2]
DR RefSeq; NP_001157098.1; NM_001163626.1. [Q8CJ00-2]
DR RefSeq; NP_757341.3; NM_172204.4. [Q8CJ00-1]
DR AlphaFoldDB; Q8CJ00; -.
DR SMR; Q8CJ00; -.
DR BioGRID; 232301; 2.
DR STRING; 10090.ENSMUSP00000037423; -.
DR iPTMnet; Q8CJ00; -.
DR PhosphoSitePlus; Q8CJ00; -.
DR PaxDb; Q8CJ00; -.
DR PeptideAtlas; Q8CJ00; -.
DR PRIDE; Q8CJ00; -.
DR ProteomicsDB; 293875; -. [Q8CJ00-1]
DR ProteomicsDB; 293876; -. [Q8CJ00-2]
DR Antibodypedia; 32446; 142 antibodies from 28 providers.
DR DNASU; 241275; -.
DR Ensembl; ENSMUST00000044018; ENSMUSP00000037423; ENSMUSG00000036805. [Q8CJ00-1]
DR Ensembl; ENSMUST00000114373; ENSMUSP00000110014; ENSMUSG00000036805. [Q8CJ00-2]
DR GeneID; 241275; -.
DR KEGG; mmu:241275; -.
DR UCSC; uc008iqh.2; mouse. [Q8CJ00-1]
DR UCSC; uc008iqi.2; mouse. [Q8CJ00-2]
DR CTD; 10811; -.
DR MGI; MGI:2449980; Noxa1.
DR VEuPathDB; HostDB:ENSMUSG00000036805; -.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00530000063843; -.
DR HOGENOM; CLU_041290_1_0_1; -.
DR InParanoid; Q8CJ00; -.
DR OMA; PYMARGP; -.
DR OrthoDB; 431898at2759; -.
DR PhylomeDB; Q8CJ00; -.
DR TreeFam; TF329087; -.
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; 241275; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q8CJ00; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CJ00; protein.
DR Bgee; ENSMUSG00000036805; Expressed in ileum and 12 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043020; C:NADPH oxidase complex; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IDA:MGI.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; ISO:MGI.
DR GO; GO:0060263; P:regulation of respiratory burst; ISO:MGI.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; IDA:MGI.
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 Pfam; PF13174; TPR_6; 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; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome; Repeat; SH3 domain; TPR repeat.
FT CHAIN 1..444
FT /note="NADPH oxidase activator 1"
FT /id="PRO_0000314610"
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 285..365
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 369..428
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..223
FT /note="Mediates interaction with RAC1"
FT /evidence="ECO:0000250"
FT REGION 215..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 237..244
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030337"
FT CONFLICT 235
FT /note="M -> T (in Ref. 2; AAP13481 and 5; AAH47532)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="R -> G (in Ref. 2; AAP13481 and 5; AAH47532)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="F -> S (in Ref. 3; BAC39832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 48880 MW; FD46EB298CD2E48F CRC64;
MSSLGDQIRD WHRGVLAVAR EDWDSALCFF SDVREPLARM YFNRGCVHLM AGDPEAALRA
FDQAVTKDTC MAVGFLQRGV ANFQLQRFQE AVSDFQLALA QLRDNAVIDY TQLGLNFKLQ
AWEVLYNMAS AQCQAGLWTK AANTLVEAIS KWPEGAQDIL DIAMDKVQKQ VPLQLQQVPK
GEVFQPPRRY LKHLEPMDFL GKAKVVASVI PDDHNAQPQQ RSQAEHAGHQ PSSSMCKRVL
STTGGHTSPG LYDSLLASRR PGPGPSEVSS GSEGAATKDP ESLVTVTVQC HFTVPLKVPR
GTGLSSFQTL LAQALLHQTQ TGQLSYKAPG EERSWIPIST EESLQSIWRN VPVGPGGLQL
QCQGVWGRPV LYQVVAQYNY RAQRPEDLDF HQGDTVDVLC EVDEAWLEGH RDGCVGIFPK
CFVVPAGAYV EAMLVLGPQP GDQN
