RBOHI_ARATH
ID RBOHI_ARATH Reviewed; 941 AA.
AC Q9SUT8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable respiratory burst oxidase homolog protein I;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHI;
DE Short=AtRBOHI;
GN Name=RBOHI; OrderedLocusNames=At4g11230; ORFNames=F8L21.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16760484; DOI=10.1104/pp.106.078089;
RA Sagi M., Fluhr R.;
RT "Production of reactive oxygen species by plant NADPH oxidases.";
RL Plant Physiol. 141:336-340(2006).
CC -!- FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB51407.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81224.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL096882; CAB51407.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161531; CAB81224.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82987.1; -; Genomic_DNA.
DR PIR; T13014; T13014.
DR RefSeq; NP_192862.2; NM_117194.4.
DR AlphaFoldDB; Q9SUT8; -.
DR SMR; Q9SUT8; -.
DR STRING; 3702.AT4G11230.1; -.
DR PeroxiBase; 3288; AtRboh09.
DR PaxDb; Q9SUT8; -.
DR PRIDE; Q9SUT8; -.
DR EnsemblPlants; AT4G11230.1; AT4G11230.1; AT4G11230.
DR GeneID; 826725; -.
DR Gramene; AT4G11230.1; AT4G11230.1; AT4G11230.
DR KEGG; ath:AT4G11230; -.
DR Araport; AT4G11230; -.
DR TAIR; locus:2128248; AT4G11230.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; Q9SUT8; -.
DR OMA; HSFSCLN; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; Q9SUT8; -.
DR BioCyc; ARA:AT4G11230-MON; -.
DR PRO; PR:Q9SUT8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUT8; baseline and differential.
DR Genevisible; Q9SUT8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000293; F:ferric-chelate reductase activity; 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; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR011992; EF-hand-dom_pair.
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; IPR013623; NADPH_Ox.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR Pfam; PF08414; NADPH_Ox; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Calcium; FAD; Flavoprotein; Membrane; Metal-binding; NADP; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..941
FT /note="Probable respiratory burst oxidase homolog protein
FT I"
FT /id="PRO_0000313761"
FT TOPO_DOM 1..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..407
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..557
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..604
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..731
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..752
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 753..941
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 254..289
FT /note="EF-hand"
FT DOMAIN 413..570
FT /note="Ferric oxidoreductase"
FT DOMAIN 609..729
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..204
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 232..243
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 103..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
SQ SEQUENCE 941 AA; 106952 MW; 9B0F3B9B15ED4F12 CRC64;
MSMSFSGGTH NDRWGSDLAS AGEFTQSFPS LPATYSPSPS SSSSSGEELL EVTIEFPSGV
IINIDSVTGT GTDISGTDLE ITSCSDSGSG SRSLSLGWSA SSERLTAGTN SKQQIQKISR
RGYGYSSRSA PEPVVPHRGE ITDSVNLPRA LSQRPTRPNR DGSGTERAIH GLKFISSKEN
GIVDWNDVQN NFAHLSKDGY LFKSDFAHCI GLENENSKEF ADELFDALCR RRRIMVDKIN
LQELYEFWYQ ITDESFDSRL QIFFNMVKNG DGRITENEVK EIIILSASAN NLSRLRERAE
EYAALIMEEL APDGLYSQYI ELKDLEILLL EKDISHSYSL PFSQTSRALS QNLKDRRWRM
SRNLLYSLQD NWKRIWVLTL WFVIMAWLFM WKCYQYKHKD AFHVMGYCLV MAKGAAETLK
FNMALILLPV CRNTITYLRS TALSHSVPFD DCINFHKTIS VAIISAMLLH ATSHLACDFP
RILASTDTDY KRYLVKYFGV TRPTYFGLVN TPVGITGIIM VAFMLIAFTL ASRRCRRNLT
KLPKPFDKLT GYNAFWYSHH LLLTVYVLLV IHGVSLYLEH KWYRKTVWMY LAVPVLLYVG
ERIFRFFRSR LYTVEICKVV IYPGNVVVLR MSKPTSFDYK SGQYVFVQCP SVSKFEWHPF
SITSSPGDDY LSIHIRQRGD WTEGIKKAFS VVCHAPEAGK SGLLRADVPN QRSFPELLID
GPYGAPAQDH WKYDVVLLVG LGIGATPFVS ILRDLLNNII KQQEQAECIS GSCSNSNISS
DHSFSCLNSE AASRIPQTQR KTLNTKNAYF YWVTREQGSF DWFKEIMNEI ADSDRKGVIE
MHNYLTSVYE EGDTRSNLLT MIQTLNHAKN GVDIFSGTKV RTHFGRPKWK KVLSKISTKH
RNARIGVFYC GVPSLGKELS TLCHEFNQTG ITRFDFHKEQ F