RBOHF_ARATH
ID RBOHF_ARATH Reviewed; 944 AA.
AC O48538; O80342; Q0WR97; Q9SH56;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Respiratory burst oxidase homolog protein F;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=Cytochrome b245 beta chain homolog RbohAp108;
DE AltName: Full=NADPH oxidase RBOHF;
DE Short=AtRBOHF;
GN Name=RBOHF; Synonyms=RBOHAP108; OrderedLocusNames=At1g64060;
GN ORFNames=F22C12.18;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9628030; DOI=10.1046/j.1365-313x.1998.00136.x;
RA Torres M.A., Onouchi H., Hamada S., Machida C., Hammond-Kosack K.E.,
RA Jones J.D.G.;
RT "Six Arabidopsis thaliana homologues of the human respiratory burst oxidase
RT (gp91phox).";
RL Plant J. 14:365-370(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-3, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, CALCIUM-BINDING DATA, AND LACK OF GLYCOSYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=9490748; DOI=10.2307/3870703;
RA Keller T., Damude H.G., Werner D., Doerner P., Dixon R.A., Lamb C.;
RT "A plant homolog of the neutrophil NADPH oxidase gp91phox subunit gene
RT encodes a plasma membrane protein with Ca2+ binding motifs.";
RL Plant Cell 10:255-266(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=11756663; DOI=10.1073/pnas.012452499;
RA Torres M.A., Dangl J.L., Jones J.D.G.;
RT "Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for
RT accumulation of reactive oxygen intermediates in the plant defense
RT response.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:517-522(2002).
RN [7]
RP FUNCTION, INDUCTION BY ABSCISIC ACID, AND TISSUE SPECIFICITY.
RX PubMed=12773379; DOI=10.1093/emboj/cdg277;
RA Kwak J.M., Mori I.C., Pei Z.-M., Leonhardt N., Torres M.A., Dangl J.L.,
RA Bloom R.E., Bodde S., Jones J.D.G., Schroeder J.I.;
RT "NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA
RT signaling in Arabidopsis.";
RL EMBO J. 22:2623-2633(2003).
RN [8]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=16961732; DOI=10.1111/j.1365-313x.2006.02842.x;
RA Desikan R., Last K., Harrett-Williams R., Tagliavia C., Harter K.,
RA Hooley R., Hancock J.T., Neill S.J.;
RT "Ethylene-induced stomatal closure in Arabidopsis occurs via AtrbohF-
RT mediated hydrogen peroxide synthesis.";
RL Plant J. 47:907-916(2006).
RN [9]
RP FUNCTION.
RX PubMed=16913867; DOI=10.1111/j.1365-3040.2006.01555.x;
RA Kalbina I., Strid A.;
RT "The role of NADPH oxidase and MAP kinase phosphatase in UV-B-dependent
RT gene expression in Arabidopsis.";
RL Plant Cell Environ. 29:1783-1793(2006).
RN [10]
RP FUNCTION.
RX PubMed=16428598; DOI=10.1104/pp.105.073072;
RA Song C.J., Steinebrunner I., Wang X., Stout S.C., Roux S.J.;
RT "Extracellular ATP induces the accumulation of superoxide via NADPH
RT oxidases in Arabidopsis.";
RL Plant Physiol. 140:1222-1232(2006).
RN [11]
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).
RN [12]
RP INTERACTION WITH SRC2.
RX PubMed=23872431; DOI=10.1016/j.bbamcr.2013.06.024;
RA Kawarazaki T., Kimura S., Iizuka A., Hanamata S., Nibori H., Michikawa M.,
RA Imai A., Abe M., Kaya H., Kuchitsu K.;
RT "A low temperature-inducible protein AtSRC2 enhances the ROS-producing
RT activity of NADPH oxidase AtRbohF.";
RL Biochim. Biophys. Acta 1833:2775-2780(2013).
RN [13]
RP INTERACTION WITH CIPK26, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=23335733; DOI=10.1093/mp/sst009;
RA Drerup M.M., Schluecking K., Hashimoto K., Manishankar P., Steinhorst L.,
RA Kuchitsu K., Kudla J.;
RT "The Calcineurin B-like calcium sensors CBL1 and CBL9 together with their
RT interacting protein kinase CIPK26 regulate the Arabidopsis NADPH oxidase
RT RBOHF.";
RL Mol. Plant 6:559-569(2013).
CC -!- FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide.
CC Generates reactive oxygen species (ROS) during incompatible
CC interactions with pathogens and is important in the regulation of the
CC hypersensitive response (HR). Involved in abscisic acid-induced
CC stomatal closing and in UV-B and abscisic acid ROS-dependent signaling.
CC {ECO:0000269|PubMed:11756663, ECO:0000269|PubMed:12773379,
CC ECO:0000269|PubMed:16428598, ECO:0000269|PubMed:16913867,
CC ECO:0000269|PubMed:16961732}.
CC -!- ACTIVITY REGULATION: Inhibited by diphenylene iodonium (DPI).
CC {ECO:0000269|PubMed:16961732}.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts (via N-
CC terminus) with CIPK26 (PubMed:23335733). Interacts (via N-terminus)
CC with SRC2 (PubMed:23872431). {ECO:0000250, ECO:0000269|PubMed:23335733,
CC ECO:0000269|PubMed:23872431}.
CC -!- INTERACTION:
CC O48538; Q940H6: SRK2E; NbExp=4; IntAct=EBI-7197253, EBI-782514;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23335733,
CC ECO:0000269|PubMed:9490748}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:9490748}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, seedlings,
CC inflorescences, leaves and guard cells. {ECO:0000269|PubMed:12773379,
CC ECO:0000269|PubMed:9490748, ECO:0000269|PubMed:9628030}.
CC -!- INDUCTION: Up-regulated by abscisic acid.
CC {ECO:0000269|PubMed:12773379}.
CC -!- PTM: Not glycosylated. Phosphorylated by CIPK26.
CC {ECO:0000269|PubMed:23335733}.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
CC -!- CAUTION: Was originally called RBOHA. {ECO:0000305|PubMed:9490748}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24574.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF00352.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB008111; BAA28953.1; -; mRNA.
DR EMBL; AF015301; AAB87789.1; -; mRNA.
DR EMBL; AC007764; AAF24574.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34186.1; -; Genomic_DNA.
DR EMBL; AK228418; BAF00352.1; ALT_SEQ; mRNA.
DR PIR; T03826; T03826.
DR RefSeq; NP_564821.1; NM_105079.3.
DR AlphaFoldDB; O48538; -.
DR SMR; O48538; -.
DR BioGRID; 27931; 3.
DR IntAct; O48538; 1.
DR MINT; O48538; -.
DR STRING; 3702.AT1G64060.1; -.
DR TCDB; 5.B.1.1.9; the phagocyte (gp91(phox)) nadph oxidase family.
DR PaxDb; O48538; -.
DR PRIDE; O48538; -.
DR ProteomicsDB; 225975; -.
DR EnsemblPlants; AT1G64060.1; AT1G64060.1; AT1G64060.
DR GeneID; 842710; -.
DR Gramene; AT1G64060.1; AT1G64060.1; AT1G64060.
DR KEGG; ath:AT1G64060; -.
DR Araport; AT1G64060; -.
DR TAIR; locus:2024603; AT1G64060.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; O48538; -.
DR OMA; LFTWKFY; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; O48538; -.
DR BioCyc; ARA:AT1G64060-MON; -.
DR PRO; PR:O48538; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O48538; baseline and differential.
DR Genevisible; O48538; 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:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IMP:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0033500; P:carbohydrate homeostasis; IMP:TAIR.
DR GO; GO:0052542; P:defense response by callose deposition; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; TAS:TAIR.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:TAIR.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:TAIR.
DR GO; GO:0007231; P:osmosensory signaling pathway; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0002679; P:respiratory burst involved in defense response; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; 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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Coiled coil; Direct protein sequencing; FAD;
KW Flavoprotein; Membrane; Metal-binding; NADP; Oxidoreductase; Peroxidase;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9490748"
FT CHAIN 2..944
FT /note="Respiratory burst oxidase homolog protein F"
FT /id="PRO_0000313758"
FT TOPO_DOM 2..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..475
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..492
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 493..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..570
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..599
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..617
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..744
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 745..765
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 766..944
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 264..299
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 308..343
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 426..583
FT /note="Ferric oxidoreductase"
FT DOMAIN 622..742
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 207..215
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 241..252
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT COILED 102..126
FT /evidence="ECO:0000255"
FT COILED 157..184
FT /evidence="ECO:0000255"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
FT CONFLICT 908
FT /note="I -> T (in Ref. 1; BAA28953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 944 AA; 108418 MW; 1ABAEC316AE80F9B CRC64;
MKPFSKNDRR RWSFDSVSAG KTAVGSASTS PGTEYSINGD QEFVEVTIDL QDDDTIVLRS
VEPATAINVI GDISDDNTGI MTPVSISRSP TMKRTSSNRF RQFSQELKAE AVAKAKQLSQ
ELKRFSWSRS FSGNLTTTST AANQSGGAGG GLVNSALEAR ALRKQRAQLD RTRSSAQRAL
RGLRFISNKQ KNVDGWNDVQ SNFEKFEKNG YIYRSDFAQC IGMKDSKEFA LELFDALSRR
RRLKVEKINH DELYEYWSQI NDESFDSRLQ IFFDIVDKNE DGRITEEEVK EIIMLSASAN
KLSRLKEQAE EYAALIMEEL DPERLGYIEL WQLETLLLQK DTYLNYSQAL SYTSQALSQN
LQGLRGKSRI HRMSSDFVYI MQENWKRIWV LSLWIMIMIG LFLWKFFQYK QKDAFHVMGY
CLLTAKGAAE TLKFNMALIL FPVCRNTITW LRSTRLSYFV PFDDNINFHK TIAGAIVVAV
ILHIGDHLAC DFPRIVRATE YDYNRYLFHY FQTKQPTYFD LVKGPEGITG ILMVILMIIS
FTLATRWFRR NLVKLPKPFD RLTGFNAFWY SHHLFVIVYI LLILHGIFLY FAKPWYVRTT
WMYLAVPVLL YGGERTLRYF RSGSYSVRLL KVAIYPGNVL TLQMSKPTQF RYKSGQYMFV
QCPAVSPFEW HPFSITSAPE DDYISIHIRQ LGDWTQELKR VFSEVCEPPV GGKSGLLRAD
ETTKKSLPKL LIDGPYGAPA QDYRKYDVLL LVGLGIGATP FISILKDLLN NIVKMEEHAD
SISDFSRSSE YSTGSNGDTP RRKRILKTTN AYFYWVTREQ GSFDWFKGVM NEVAELDQRG
VIEMHNYLTS VYEEGDARSA LITMVQALNH AKNGVDIVSG TRVRTHFARP NWKKVLTKLS
SKHCNARIGV FYCGVPVLGK ELSKLCNTFN QKGSTKFEFH KEHF
