NOXA1_RAT
ID NOXA1_RAT Reviewed; 446 AA.
AC A7E3N7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=NADPH oxidase activator 1;
GN Name=Noxa1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION.
RX PubMed=17612411; DOI=10.1186/1471-2148-7-109;
RA Kawahara B.T., Quinn M.T., Lambeth J.D.;
RT "Molecular evolution of the reactive oxygen-generating NADPH oxidase
RT (Nox/Duox) family of enzymes.";
RL BMC Evol. Biol. 7:109-109(2007).
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
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 (By similarity).
CC {ECO:0000250}.
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. Cell membrane. Note=Translocation to
CC membranes depends on NOXO1 or NCF1 and maybe RAC1. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in gastrum, spleen,
CC uterus, small intestine, colon, inner ear, and brain.
CC {ECO:0000269|PubMed:15326186}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic kidney.
CC {ECO:0000269|PubMed:15326186}.
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}.
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DR EMBL; AABR03024824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BR000299; FAA00366.1; -; mRNA.
DR RefSeq; NP_001093641.1; NM_001100171.1.
DR AlphaFoldDB; A7E3N7; -.
DR SMR; A7E3N7; -.
DR STRING; 10116.ENSRNOP00000012375; -.
DR iPTMnet; A7E3N7; -.
DR PhosphoSitePlus; A7E3N7; -.
DR PaxDb; A7E3N7; -.
DR Ensembl; ENSRNOT00000012375; ENSRNOP00000012375; ENSRNOG00000009286.
DR GeneID; 311793; -.
DR KEGG; rno:311793; -.
DR UCSC; RGD:1306687; rat.
DR CTD; 10811; -.
DR RGD; 1306687; Noxa1.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00530000063843; -.
DR HOGENOM; CLU_041290_1_0_1; -.
DR InParanoid; A7E3N7; -.
DR OMA; PYMARGP; -.
DR OrthoDB; 431898at2759; -.
DR PhylomeDB; A7E3N7; -.
DR TreeFam; TF329087; -.
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:A7E3N7; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000009286; Expressed in colon and 5 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043020; C:NADPH oxidase complex; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; ISS:UniProtKB.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; ISO:RGD.
DR GO; GO:0060263; P:regulation of respiratory burst; ISO:RGD.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; ISS: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 PRINTS; PR00452; SH3DOMAIN.
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; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Membrane; Reference proteome; Repeat; SH3 domain;
KW TPR repeat.
FT CHAIN 1..446
FT /note="NADPH oxidase activator 1"
FT /id="PRO_0000314611"
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 287..367
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 371..430
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..224
FT /note="Mediates interaction with RAC1"
FT /evidence="ECO:0000250"
FT REGION 213..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 49245 MW; 3463AD5FA4C38474 CRC64;
MSSLGDQIRD WHRGVLAVAR EDWDSALCFF SDVREPLAKM YFNMGCVHLM AGDPEAALRA
FDQAVTKDTC MAVGFLQRGV ANFQLQRLQE AVSDFQLALA QLRGNAAIDY TQLGLDFKLQ
AWEVLYNMAS VQCQAGLWTK AANTLVEAIS KRPEGAQDTL EAAMDKVQKQ VPLQLRQVPK
GEVFQPPRRY LKHLEPMDFL GKAKVVASVI PDDHNSDIQP QQSSQVEQAG LQSSSPVCKR
VLSTRGGHMS PGLWDSLLAT GGPVPGPSED SSSAEGTATK DPESLVTVTV QCHFTVPLKV
PRGTDLSSFR TLLSQALLQQ TQKGQFSYKA RGEDRAWVPI STEDSLQSVW RNVPVSPRGL
QLQCRGAWGR PVLYQVVAQY DYRAQRPEDL DFRQGDTVDV LCEVDEAWLE GHRDGRVGIF
PKCFVVPAAT CVEALPVPEP QPGEQH
