Respiratory burst oxidase homolog protein D - Arabidopsis thaliana (Mouse-ear cress)

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Q9FIJ0 (RBOHD_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	921 AA.
Sequence status	Complete.
Protein existence	Evidence 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.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
Enzyme regulation	Inhibited by diphenylene iodinium (DPI). Ref.13
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.8
Induction	Up-regulated by pathogen infection and by abscisic acid. Ref.8 Ref.13
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
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.9
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.

Ontologies

Keywords
Cellular component	Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Calcium FAD Metal-binding NADP
Molecular function	Oxidoreductase Peroxidase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate homeostasis Inferred from mutant phenotype PubMed 22422940. Source: TAIR defense response to fungus Inferred from mutant phenotype PubMed 19726575. Source: TAIR negative regulation of programmed cell death Inferred from genetic interaction PubMed 16170317. Source: TAIR osmosensory signaling pathway Inferred from mutant phenotype PubMed 22422940. Source: TAIR reactive oxygen species metabolic process Inferred from mutant phenotype Ref.7. Source: TAIR response to heat Inferred from mutant phenotype PubMed 15923322. Source: TAIR response to wounding Inferred from expression pattern PubMed 21419340. Source: TAIR
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 22430844. Source: TAIR integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.5 PubMed 22923678. Source: TAIR
Molecular_function	NAD(P)H oxidase activity Inferred from mutant phenotype PubMed 19726575. Source: TAIR calcium ion binding Inferred from electronic annotation. Source: InterPro peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 921

921

Respiratory burst oxidase homolog protein D

PRO_0000313756

Regions

Topological domain

1 – 376

376

Cytoplasmic Potential

Transmembrane

377 – 397

Helical; Name=1; Potential

Topological domain

398 – 461

Extracellular Potential

Transmembrane

462 – 482

Helical; Name=2; By similarity

Topological domain

483 – 516

Cytoplasmic Potential

Transmembrane

517 – 537

Helical; Name=3; Potential

Topological domain

538 – 559

Extracellular Potential

Transmembrane

560 – 580

Helical; Name=4; Potential

Topological domain

581 – 588

Cytoplasmic Potential

Transmembrane

589 – 606

Helical; Name=5; By similarity

Topological domain

607 – 734

128

Extracellular Potential

Transmembrane

735 – 755

Helical; Name=6; Potential

Topological domain

756 – 921

166

Cytoplasmic Potential

Domain

253 – 288

EF-hand 1

Domain

297 – 332

EF-hand 2

Domain

415 – 572

158

Ferric oxidoreductase

Domain

611 – 732

122

FAD-binding FR-type

Calcium binding

266 – 277

Potential

Region

193 – 203

EF-hand-like 1 By similarity

Region

230 – 241

EF-hand-like 2 By similarity

Compositional bias

98 – 101

Poly-Gly

Sites

Metal binding

266

Calcium By similarity

Metal binding

268

Calcium By similarity

Metal binding

270

Calcium By similarity

Metal binding

272

Calcium; via carbonyl oxygen By similarity

Metal binding

277

Calcium By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.15

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.5 Ref.14 Ref.15

Modified residue

152

Phosphoserine Ref.5

Modified residue

163

Phosphoserine Ref.5

Modified residue

343

Phosphoserine Ref.5 Ref.6

Modified residue

347

Phosphoserine Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

Q9FIJ0 [UniParc].

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

FASTA

921

103,909

        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' referencesShow '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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-152; SER-163 AND SER-343, MASS SPECTROMETRY. Strain: cv. Columbia.
[6]	"Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses." Nuehse T.S., Bottrill A.R., Jones A.M.E., 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, MASS SPECTROMETRY.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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, MASS SPECTROMETRY. Strain: cv. Columbia.
[15]	"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-8 AND SER-39, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	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.
IPI	IPI00522047.
PIR	T51804.
RefSeq	NP_199602.1. NM_124165.2.
UniGene	At.23270.
3D structure databases
ProteinModelPortal	Q9FIJ0.
SMR	Q9FIJ0. Positions 161-328, 720-921.
ModBase	Search...
Protein family/group databases
PeroxiBase	3286. AtRboh04.
Proteomic databases
PaxDb	Q9FIJ0.
PRIDE	Q9FIJ0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G47910.1; AT5G47910.1; AT5G47910.
GeneID	834842.
KEGG	ath:AT5G47910.
Organism-specific databases
TAIR	At5g47910.
Phylogenomic databases
eggNOG	COG4097.
HOGENOM	HOG000216670.
InParanoid	Q9FIJ0.
KO	K13447.
OMA	FTYKFIQ.
PhylomeDB	Q9FIJ0.
ProtClustDB	CLSN2916327.
Gene expression databases
Genevestigator	Q9FIJ0.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR000778. Cyt_b245_heavy_chain. IPR011992. EF-hand-like_dom. 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]
Pfam	PF08022. FAD_binding_8. 1 hit. PF01794. Ferric_reduct. 1 hit. PF08030. NAD_binding_6. 1 hit. PF08414. NADPH_Ox. 1 hit. [Graphical view]
PRINTS	PR00466. GP91PHOX.
SUPFAM	SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 2 hits. PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBOHD_ARATH

Accession

Primary (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:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents