IED ID | IndEnz0018000326 |
Enzyme Type ID | peroxidase000326 |
Protein Name |
Respiratory burst oxidase homolog protein F EC 1.11.1.- EC 1.6.3.- Cytochrome b245 beta chain homolog RbohAp108 NADPH oxidase RBOHF AtRBOHF |
Gene Name | RBOHF RBOHAP108 At1g64060 F22C12.18 |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
Enzyme Sequence | MKPFSKNDRRRWSFDSVSAGKTAVGSASTSPGTEYSINGDQEFVEVTIDLQDDDTIVLRSVEPATAINVIGDISDDNTGIMTPVSISRSPTMKRTSSNRFRQFSQELKAEAVAKAKQLSQELKRFSWSRSFSGNLTTTSTAANQSGGAGGGLVNSALEARALRKQRAQLDRTRSSAQRALRGLRFISNKQKNVDGWNDVQSNFEKFEKNGYIYRSDFAQCIGMKDSKEFALELFDALSRRRRLKVEKINHDELYEYWSQINDESFDSRLQIFFDIVDKNEDGRITEEEVKEIIMLSASANKLSRLKEQAEEYAALIMEELDPERLGYIELWQLETLLLQKDTYLNYSQALSYTSQALSQNLQGLRGKSRIHRMSSDFVYIMQENWKRIWVLSLWIMIMIGLFLWKFFQYKQKDAFHVMGYCLLTAKGAAETLKFNMALILFPVCRNTITWLRSTRLSYFVPFDDNINFHKTIAGAIVVAVILHIGDHLACDFPRIVRATEYDYNRYLFHYFQTKQPTYFDLVKGPEGITGILMVILMIISFTLATRWFRRNLVKLPKPFDRLTGFNAFWYSHHLFVIVYILLILHGIFLYFAKPWYVRTTWMYLAVPVLLYGGERTLRYFRSGSYSVRLLKVAIYPGNVLTLQMSKPTQFRYKSGQYMFVQCPAVSPFEWHPFSITSAPEDDYISIHIRQLGDWTQELKRVFSEVCEPPVGGKSGLLRADETTKKSLPKLLIDGPYGAPAQDYRKYDVLLLVGLGIGATPFISILKDLLNNIVKMEEHADSISDFSRSSEYSTGSNGDTPRRKRILKTTNAYFYWVTREQGSFDWFKGVMNEVAELDQRGVIEMHNYLTSVYEEGDARSALITMVQALNHAKNGVDIVSGTRVRTHFARPNWKKVLTKLSSKHCNARIGVFYCGVPVLGKELSKLCNTFNQKGSTKFEFHKEHF |
Enzyme Length | 944 |
Uniprot Accession Number | O48538 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by diphenylene iodonium (DPI). {ECO:0000269|PubMed:16961732}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 1.11.1.-; 1.6.3.- |
Enzyme Function | FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide. Generates reactive oxygen species (ROS) during incompatible interactions with pathogens and is important in the regulation of the hypersensitive response (HR). Involved in abscisic acid-induced stomatal closing and in UV-B and abscisic acid ROS-dependent signaling. {ECO:0000269|PubMed:11756663, ECO:0000269|PubMed:12773379, ECO:0000269|PubMed:16428598, ECO:0000269|PubMed:16913867, ECO:0000269|PubMed:16961732}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Coiled coil (2); Domain (4); Erroneous gene model prediction (1); Initiator methionine (1); Metal binding (7); Modified residue (2); Region (2); Sequence caution (1); Sequence conflict (1); Topological domain (7); Transmembrane (6) |
Keywords | Calcium;Cell membrane;Coiled coil;Direct protein sequencing;FAD;Flavoprotein;Membrane;Metal-binding;NADP;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Repeat;Transmembrane;Transmembrane helix |
Interact With | Q940H6 |
Induction | INDUCTION: Up-regulated by abscisic acid. {ECO:0000269|PubMed:12773379}. |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:9490748}; Multi-pass membrane protein {ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:9490748}. |
Modified Residue | MOD_RES 354; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9FIJ0; MOD_RES 358; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9FIJ0 |
Post Translational Modification | PTM: Not glycosylated. Phosphorylated by CIPK26. {ECO:0000269|PubMed:23335733}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10381874; 14765119; 15705948; 16415066; 17317660; 18182433; 18212028; 18790995; 19690149; 19716822; 19726575; 20023407; 20736450; 20876608; 20951600; 21071853; 21421415; 21707649; 21746700; 21802603; 21984648; 21985584; 22001402; 22126965; 22422940; 22437147; 22652060; 22730426; 22751316; 22788984; 23064146; 23095998; 23162070; 23264520; 23341360; 23365132; 23400703; 23441575; 23448237; 23649257; 23748772; 23807482; 23952703; 23963673; 24033256; 24064768; 24444075; 24477528; 24699527; 24714570; 24733882; 25399352; 25462961; 25754244; 25826261; 26180024; 26765289; 26798024; 27246095; 27837091; 28254779; 28337518; 28412199; 28716423; 29163585; 29262318; 29301018; 29438048; 30013580; 30097007; 30218537; 30320882; 30796836; 30873191; 30963238; 31379894; 32005378; 32086363; 32234220; 32290990; 32519347; 32569316; 32605179; 32634860; 32695131; 32910883; 32938754; 33198167; 33213111; 33315520; |
Motif | |
Gene Encoded By | |
Mass | 108,418 |
Kinetics | |
Metal Binding | METAL 277; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 279; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 281; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 283; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 288; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 321; /note=Calcium 2; /evidence=ECO:0000305; METAL 327; /note=Calcium 2; /evidence=ECO:0000305 |
Rhea ID | |
Cross Reference Brenda |