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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
 
 
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