RBOHE_ARATH
ID RBOHE_ARATH Reviewed; 952 AA.
AC O81211; F4IE24; F4IE25; Q9LMA3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Respiratory burst oxidase homolog protein E;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHE;
DE Short=AtRBOHE;
GN Name=RBOHE; OrderedLocusNames=At1g19230; ORFNames=T29M8.10;
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 [GENOMIC DNA], 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 [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 [3]
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 [4]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O81211-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, inflorescences, leaves and
CC stems. {ECO:0000269|PubMed:9628030}.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39478.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF82233.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE29820.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF055356; AAC39478.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069143; AAF82233.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29820.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29821.2; -; Genomic_DNA.
DR PIR; H86325; H86325.
DR RefSeq; NP_001319042.1; NM_001332388.1. [O81211-1]
DR RefSeq; NP_173357.1; NM_101781.2.
DR AlphaFoldDB; O81211; -.
DR SMR; O81211; -.
DR STRING; 3702.AT1G19230.2; -.
DR PaxDb; O81211; -.
DR PRIDE; O81211; -.
DR ProteomicsDB; 236526; -. [O81211-1]
DR EnsemblPlants; AT1G19230.2; AT1G19230.2; AT1G19230. [O81211-1]
DR GeneID; 838506; -.
DR Gramene; AT1G19230.2; AT1G19230.2; AT1G19230. [O81211-1]
DR KEGG; ath:AT1G19230; -.
DR Araport; AT1G19230; -.
DR TAIR; locus:2202210; AT1G19230.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; O81211; -.
DR OrthoDB; 936110at2759; -.
DR BioCyc; ARA:AT1G19230-MON; -.
DR PRO; PR:O81211; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O81211; baseline and differential.
DR Genevisible; O81211; 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; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; FAD; Flavoprotein; Membrane; Metal-binding;
KW NADP; Oxidoreductase; Peroxidase; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..952
FT /note="Respiratory burst oxidase homolog protein E"
FT /id="PRO_0000313757"
FT TOPO_DOM 1..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..475
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..574
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 596..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..621
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 622..750
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 751..771
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 772..952
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 268..303
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 312..347
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 431..587
FT /note="Ferric oxidoreductase"
FT DOMAIN 626..748
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 211..219
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 245..256
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 952 AA; 107703 MW; 720729D69DE68457 CRC64;
MKLSPLSFST SSSFSHADGI DDGVELISSP FAGGAMLPVF LNDLSRNSGE SGSGSSWERE
LVEVTLELDV GDDSILVCGM SEAASVDSRA RSVDLVTARL SRNLSNASTR IRQKLGKLLR
SESWKTTTSS TAGERDRDLE RQTAVTLGIL TARDKRKEDA KLQRSTSSAQ RALKGLQFIN
KTTRGNSCVC DWDCDCDQMW KKVEKRFESL SKNGLLARDD FGECVGMVDS KDFAVSVFDA
LARRRRQKLE KITKDELHDF WLQISDQSFD ARLQIFFDMA DSNEDGKITR EEIKELLMLS
ASANKLAKLK EQAEEYASLI MEELDPENFG YIELWQLETL LLQRDAYMNY SRPLSTTSGG
VSTPRRNLIR PRHVVQKCRK KLQCLILDNW QRSWVLLVWV MLMAILFVWK FLEYREKAAF
KVMGYCLTTA KGAAETLKLN MALVLLPVCR NTLTWLRSTR ARACVPFDDN INFHKIIACA
IAIGILVHAG THLACDFPRI INSSPEQFVL IASAFNGTKP TFKDLMTGAE GITGISMVIL
TTIAFTLAST HFRRNRVRLP APLDRLTGFN AFWYTHHLLV VVYIMLIVHG TFLFFADKWY
QKTTWMYISV PLVLYVAERS LRACRSKHYS VKILKVSMLP GEVLSLIMSK PPGFKYKSGQ
YIFLQCPTIS RFEWHPFSIT SAPGDDQLSV HIRTLGDWTE ELRRVLTVGK DLSTCVIGRS
KFSAYCNIDM INRPKLLVDG PYGAPAQDYR SYDVLLLIGL GIGATPFISI LKDLLNNSRD
EQTDNEFSRS DFSWNSCTSS YTTATPTSTH GGKKKAVKAH FYWVTREPGS VEWFRGVMEE
ISDMDCRGQI ELHNYLTSVY DEGDARSTLI KMVQALNHAK HGVDILSGTR VRTHFARPNW
KEVFSSIARK HPNSTVGVFY CGIQTVAKEL KKQAQDMSQK TTTRFEFHKE HF
