NOXO1_MOUSE
ID NOXO1_MOUSE Reviewed; 349 AA.
AC Q8VCM2; Q3TZA4; Q8BH41; Q9D747;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=NADPH oxidase organizer 1;
DE Short=Nox organizer 1;
DE AltName: Full=Sorting nexin-28;
GN Name=Noxo1; Synonyms=Snx28;
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, AND 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 2).
RC STRAIN=C57BL/6J;
RA Hong W.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, and Thymus;
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 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 [5]
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16431374; DOI=10.1016/j.cub.2005.12.025;
RA Kiss P.J., Knisz J., Zhang Y., Baltrusaitis J., Sigmund C.D., Thalmann R.,
RA Smith R.J.H., Verpy E., Banfi B.;
RT "Inactivation of NADPH oxidase organizer 1 results in severe imbalance.";
RL Curr. Biol. 16:208-213(2006).
CC -!- FUNCTION: Constitutively potentiates the superoxide-generating activity
CC of NOX1 and NOX3 and is required for the biogenesis of
CC otoconia/otolith, which are crystalline structures of the inner ear
CC involved in the perception of gravity. Isoform 3 is more potent than
CC isoform 1 in activating NOX3. Together with NOXA1, may also substitute
CC to NCF1/p47phox and NCF2/p67phox in supporting the phagocyte
CC NOX2/gp91phox superoxide-generating activity.
CC {ECO:0000269|PubMed:12473664, ECO:0000269|PubMed:16431374}.
CC -!- SUBUNIT: Interacts with NOX1, NOXA1, CYBA/p22phox and NCF2/p67phox.
CC Interacts with SH3PXD2A and SH3PXD2B. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NFA2};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NFA2}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q8NFA2}. Note=Associates with the plasma
CC membrane in a lipid-dependent manner. {ECO:0000250|UniProtKB:Q8NFA2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VCM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VCM2-2; Sequence=VSP_017562, VSP_017563;
CC -!- TISSUE SPECIFICITY: Strongly expressed by colon epithelial cells and to
CC a lower extent in small intestine, uterus, stomach and testis.
CC Expressed in different parts of the inner ear including sensory and
CC nonsensory cell layers of the saccule, ampullae of the semicircular
CC canals, the stria vascularis and the spiral glanglion neurons.
CC {ECO:0000269|PubMed:12473664, ECO:0000269|PubMed:15949904,
CC ECO:0000269|PubMed:16431374}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in inner ear during
CC embryogenesis. {ECO:0000269|PubMed:16431374}.
CC -!- DOMAIN: The PX domain mediates lipid-binding, localization to the
CC plasma membrane and is required for NOX1 activation. {ECO:0000250}.
CC -!- DOMAIN: The SH3 domains mediate interaction with CYBA/p22phox.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice display balance defects being unable to
CC orient themselves with respect to the gravitational force. This is
CC associated with a defect in otoconia biogenesis in the inner ear.
CC {ECO:0000269|PubMed:16431374}.
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DR EMBL; AF539797; AAN75142.1; -; mRNA.
DR EMBL; AF399754; AAK94017.1; -; mRNA.
DR EMBL; AK009605; BAB26387.1; -; mRNA.
DR EMBL; AK088226; BAC40222.1; -; mRNA.
DR EMBL; AK157993; BAE34305.1; -; mRNA.
DR EMBL; BC019525; AAH19525.1; -; mRNA.
DR CCDS; CCDS50018.1; -. [Q8VCM2-1]
DR RefSeq; NP_082264.2; NM_027988.4. [Q8VCM2-1]
DR RefSeq; XP_006525012.1; XM_006524949.2.
DR RefSeq; XP_011244931.1; XM_011246629.2.
DR AlphaFoldDB; Q8VCM2; -.
DR SMR; Q8VCM2; -.
DR BioGRID; 215012; 2.
DR STRING; 10090.ENSMUSP00000019464; -.
DR iPTMnet; Q8VCM2; -.
DR PhosphoSitePlus; Q8VCM2; -.
DR PaxDb; Q8VCM2; -.
DR PRIDE; Q8VCM2; -.
DR ProteomicsDB; 293679; -. [Q8VCM2-1]
DR Antibodypedia; 23401; 212 antibodies from 33 providers.
DR DNASU; 71893; -.
DR Ensembl; ENSMUST00000019464; ENSMUSP00000019464; ENSMUSG00000019320. [Q8VCM2-1]
DR GeneID; 71893; -.
DR KEGG; mmu:71893; -.
DR UCSC; uc008axs.2; mouse. [Q8VCM2-1]
DR CTD; 124056; -.
DR MGI; MGI:1919143; Noxo1.
DR VEuPathDB; HostDB:ENSMUSG00000019320; -.
DR eggNOG; ENOG502QW5I; Eukaryota.
DR GeneTree; ENSGT00940000158812; -.
DR HOGENOM; CLU_030529_2_0_1; -.
DR InParanoid; Q8VCM2; -.
DR OMA; QQMAWFP; -.
DR OrthoDB; 601811at2759; -.
DR PhylomeDB; Q8VCM2; -.
DR TreeFam; TF329347; -.
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; 71893; 2 hits in 44 CRISPR screens.
DR PRO; PR:Q8VCM2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8VCM2; protein.
DR Bgee; ENSMUSG00000019320; Expressed in paneth cell and 111 other tissues.
DR Genevisible; Q8VCM2; MM.
DR GO; GO:0005737; C:cytoplasm; 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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IDA:MGI.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISS:UniProtKB.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; IDA:MGI.
DR CDD; cd12024; SH3_NoxO1_2; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR035758; NoxO1_SH3_2.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Lipid-binding; Membrane;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..349
FT /note="NADPH oxidase organizer 1"
FT /id="PRO_0000227595"
FT DOMAIN 1..126
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 160..219
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 231..290
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 315..324
FT /note="Proline-rich region; mediates mutually exclusive
FT interactions with itself and NOXA1"
FT /evidence="ECO:0000250"
FT VAR_SEQ 234..239
FT /note="RQFCTT -> MSPSLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_017562"
FT VAR_SEQ 240..349
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_017563"
FT CONFLICT 13
FT /note="V -> I (in Ref. 3; BAE34305)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="G -> S (in Ref. 2; AAK94017 and 3; BAB26387)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="T -> I (in Ref. 3; BAE34305)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="G -> A (in Ref. 4; AAH19525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38827 MW; 500F1E1247454101 CRC64;
MASPRHPVSA HAVALVQMDR LQTFAFSVCW SDNSDTFVRR SWDEFRQLQK TLKKTFPVEA
GLLRRSEQVL PKLPDAPLLT RRGHTGRGLV RLRLLDTYVQ ALLATSEHIL RSSALHGFFV
PKPLDLEPML PPGSLVILPT PEEPLSQPRG SLDIHSLEAQ SIPCVQPFHT LDIRDRPFHT
KAQEILDILL RHPSGWWLVE NKDQQVAWFP APYLEEVATC QGQESGLALQ GSGRQFCTTQ
AYEGSRSDEL SVPSGARVHV LETSDRGWWL CRYNGRTGLL PAMSLQPEGL GSLLGRPGFP
DSAGADKVAE DRTIPPVVPT RPCMSAIQSR CCSITRRALG QEQGTRVPR
