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Q9FIJ0 (RBOHD_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Respiratory burst oxidase homolog protein D

EC=1.11.1.-
EC=1.6.3.-
Alternative name(s):
NADPH oxidase RBOHD
Short name=AtRBOHD
Gene names
Name:RBOHD
Ordered Locus Names:At5g47910
ORF Names:MCA23.25
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length921 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-dependent NADPH oxidase that generates superoxide. Involved in the generation of reactive oxygen species (ROS) during incompatible interactions with pathogens and in UV-B and abscisic acid ROS-dependent signaling. Might be required for ROS signal amplification during light stress. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11

Enzyme regulation

Inhibited by diphenylene iodinium (DPI). Ref.11

Subunit structure

Monomer and homodimer By similarity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

More abundant in roots than in leaves, stems or inflorescences. Expressed in mesophyll and guard cells. Ref.1 Ref.6

Induction

Up-regulated by pathogen infection and by abscisic acid. Ref.6 Ref.11

Disruption phenotype

Plants do not accumulate reactive oxygen species during disease-resistance reactions, do not up-regulate UV-B-dependent gene expression and are impaired in abscisic acid-induced stomatal closing and in root growth and seed germination inhibitions. Ref.7

Sequence similarities

Belongs to the RBOH (TC 5.B.1.3) family. [View classification]

Contains 2 EF-hand domains.

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 921921Respiratory burst oxidase homolog protein D
PRO_0000313756

Regions

Topological domain1 – 376376Cytoplasmic Potential
Transmembrane377 – 39721Helical; Name=1; Potential
Topological domain398 – 46164Extracellular Potential
Transmembrane462 – 48221Helical; Name=2; By similarity
Topological domain483 – 51634Cytoplasmic Potential
Transmembrane517 – 53721Helical; Name=3; Potential
Topological domain538 – 55922Extracellular Potential
Transmembrane560 – 58021Helical; Name=4; Potential
Topological domain581 – 5888Cytoplasmic Potential
Transmembrane589 – 60618Helical; Name=5; By similarity
Topological domain607 – 734128Extracellular Potential
Transmembrane735 – 75521Helical; Name=6; Potential
Topological domain756 – 921166Cytoplasmic Potential
Domain253 – 28836EF-hand 1
Domain297 – 33236EF-hand 2
Domain415 – 572158Ferric oxidoreductase
Domain611 – 732122FAD-binding FR-type
Calcium binding266 – 27712 Potential
Region193 – 20311EF-hand-like 1 By similarity
Region230 – 24112EF-hand-like 2 By similarity
Compositional bias98 – 1014Poly-Gly

Sites

Metal binding2661Calcium By similarity
Metal binding2681Calcium By similarity
Metal binding2701Calcium By similarity
Metal binding2721Calcium; via carbonyl oxygen By similarity
Metal binding2771Calcium By similarity

Amino acid modifications

Modified residue261Phosphoserine Ref.12
Modified residue391Phosphoserine Ref.13 Ref.14
Modified residue3431Phosphoserine Ref.12
Modified residue3471Phosphoserine Ref.12

Sequences

Sequence LengthMass (Da)Tools
Q9FIJ0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 1A822569A7AB1817

FASTA921103,909
        10         20         30         40         50         60 
MKMRRGNSSN DHELGILRGA NSDTNSDTES IASDRGAFSG PLGRPKRASK KNARFADDLP 

        70         80         90        100        110        120 
KRSNSVAGGR GDDDEYVEIT LDIRDDSVAV HSVQQAAGGG GHLEDPELAL LTKKTLESSL 

       130        140        150        160        170        180 
NNTTSLSFFR STSSRIKNAS RELRRVFSRR PSPAVRRFDR TSSAAIHALK GLKFIATKTA 

       190        200        210        220        230        240 
AWPAVDQRFD KLSADSNGLL LSAKFWECLG MNKESKDFAD QLFRALARRN NVSGDAITKE 

       250        260        270        280        290        300 
QLRIFWEQIS DESFDAKLQV FFDMVDKDED GRVTEEEVAE IISLSASANK LSNIQKQAKE 

       310        320        330        340        350        360 
YAALIMEELD PDNAGFIMIE NLEMLLLQAP NQSVRMGDSR ILSQMLSQKL RPAKESNPLV 

       370        380        390        400        410        420 
RWSEKIKYFI LDNWQRLWIM MLWLGICGGL FTYKFIQYKN KAAYGVMGYC VCVAKGGAET 

       430        440        450        460        470        480 
LKFNMALILL PVCRNTITWL RNKTKLGTVV PFDDSLNFHK VIASGIVVGV LLHAGAHLTC 

       490        500        510        520        530        540 
DFPRLIAADE DTYEPMEKYF GDQPTSYWWF VKGVEGWTGI VMVVLMAIAF TLATPWFRRN 

       550        560        570        580        590        600 
KLNLPNFLKK LTGFNAFWYT HHLFIIVYAL LIVHGIKLYL TKIWYQKTTW MYLAVPILLY 

       610        620        630        640        650        660 
ASERLLRAFR SSIKPVKMIK VAVYPGNVLS LHMTKPQGFK YKSGQFMLVN CRAVSPFEWH 

       670        680        690        700        710        720 
PFSITSAPGD DYLSVHIRTL GDWTRKLRTV FSEVCKPPTA GKSGLLRADG GDGNLPFPKV 

       730        740        750        760        770        780 
LIDGPYGAPA QDYKKYDVVL LVGLGIGATP MISILKDIIN NMKGPDRDSD IENNNSNNNS 

       790        800        810        820        830        840 
KGFKTRKAYF YWVTREQGSF EWFKGIMDEI SELDEEGIIE LHNYCTSVYE EGDARVALIA 

       850        860        870        880        890        900 
MLQSLQHAKN GVDVVSGTRV KSHFAKPNWR QVYKKIAVQH PGKRIGVFYC GMPGMIKELK 

       910        920 
NLALDFSRKT TTKFDFHKEN F 

« Hide

References

« Hide 'large scale' references
[1]"Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91phox)."
Torres M.A., Onouchi H., Hamada S., Machida C., Hammond-Kosack K.E., Jones J.D.G.
Plant J. 14:365-370(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: cv. Landsberg erecta.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones."
Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S.
DNA Res. 5:379-391(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for accumulation of reactive oxygen intermediates in the plant defense response."
Torres M.A., Dangl J.L., Jones J.D.G.
Proc. Natl. Acad. Sci. U.S.A. 99:517-522(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA signaling in Arabidopsis."
Kwak J.M., Mori I.C., Pei Z.-M., Leonhardt N., Torres M.A., Dangl J.L., Bloom R.E., Bodde S., Jones J.D.G., Schroeder J.I.
EMBO J. 22:2623-2633(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY ABSCISIC ACID, TISSUE SPECIFICITY.
[7]"Cytosolic ascorbate peroxidase 1 is a central component of the reactive oxygen gene network of Arabidopsis."
Davletova S., Rizhsky L., Liang H., Shengqiang Z., Oliver D.J., Coutu J., Shulaev V., Schlauch K., Mittler R.
Plant Cell 17:268-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]"The role of NADPH oxidase and MAP kinase phosphatase in UV-B-dependent gene expression in Arabidopsis."
Kalbina I., Strid A.
Plant Cell Environ. 29:1783-1793(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Extracellular ATP induces the accumulation of superoxide via NADPH oxidases in Arabidopsis."
Song C.J., Steinebrunner I., Wang X., Stout S.C., Roux S.J.
Plant Physiol. 140:1222-1232(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Production of reactive oxygen species by plant NADPH oxidases."
Sagi M., Fluhr R.
Plant Physiol. 141:336-340(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[11]"Arabidopsis thaliana expresses multiple lines of defense to counterattack Erwinia chrysanthemi."
Fagard M., Dellagi A., Roux C., Perino C., Rigault M., Boucher V., Shevchik V.E., Expert D.
Mol. Plant Microbe Interact. 20:794-805(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, INDUCTION.
[12]"Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses."
Nuehse T.S., Bottrill A.R., Jones A.M., Peck S.C.
Plant J. 51:931-940(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-343 AND SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: cv. La-0.
[13]"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.
[14]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF055357 mRNA. Translation: AAC39479.1.
AB016886 Genomic DNA. Translation: BAB11338.1.
CP002688 Genomic DNA. Translation: AED95593.1.
AF424625 mRNA. Translation: AAL11618.1.
BT002651 mRNA. Translation: AAO11567.1.
PIRT51804.
RefSeqNP_199602.1. NM_124165.2.
UniGeneAt.23270.

3D structure databases

ProteinModelPortalQ9FIJ0.
SMRQ9FIJ0. Positions 161-328, 720-921.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

PeroxiBase3286. AtRboh04.

Proteomic databases

PaxDbQ9FIJ0.
PRIDEQ9FIJ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G47910.1; AT5G47910.1; AT5G47910.
GeneID834842.
KEGGath:AT5G47910.

Organism-specific databases

TAIRAT5G47910.

Phylogenomic databases

eggNOGCOG4097.
HOGENOMHOG000216670.
InParanoidQ9FIJ0.
KOK13447.
OMAFTYKFIQ.
PhylomeDBQ9FIJ0.
ProtClustDBCLSN2916327.

Enzyme and pathway databases

BioCycARA:AT5G47910-MONOMER.

Gene expression databases

GenevestigatorQ9FIJ0.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR000778. Cyt_b245_heavy_chain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR013623. NADPH_Ox.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
PF08414. NADPH_Ox. 1 hit.
[Graphical view]
PRINTSPR00466. GP91PHOX.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBOHD_ARATH
AccessionPrimary (citable) accession number: Q9FIJ0
Secondary accession number(s): O81212
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2001
Last modified: March 19, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names