RBOHH_ARATH
ID RBOHH_ARATH Reviewed; 886 AA.
AC Q9FJD6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Putative respiratory burst oxidase homolog protein H;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHH;
DE Short=AtRBOHH;
GN Name=RBOHH; OrderedLocusNames=At5g60010; ORFNames=MMN10.18;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [2]
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 [3]
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 -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
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DR EMBL; AB015475; BAB08369.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97266.1; -; Genomic_DNA.
DR RefSeq; NP_200809.4; NM_125394.5.
DR AlphaFoldDB; Q9FJD6; -.
DR SMR; Q9FJD6; -.
DR STRING; 3702.AT5G60010.1; -.
DR PeroxiBase; 3281; AtRboh08.
DR iPTMnet; Q9FJD6; -.
DR PaxDb; Q9FJD6; -.
DR PRIDE; Q9FJD6; -.
DR ProteomicsDB; 236527; -.
DR EnsemblPlants; AT5G60010.1; AT5G60010.1; AT5G60010.
DR GeneID; 836123; -.
DR Gramene; AT5G60010.1; AT5G60010.1; AT5G60010.
DR KEGG; ath:AT5G60010; -.
DR Araport; AT5G60010; -.
DR TAIR; locus:2168113; AT5G60010.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; Q9FJD6; -.
DR OMA; KPSMKYK; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; Q9FJD6; -.
DR BioCyc; ARA:AT5G60010-MON; -.
DR PRO; PR:Q9FJD6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJD6; baseline and differential.
DR Genevisible; Q9FJD6; 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 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; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Calcium; FAD; Flavoprotein; Membrane; Metal-binding; NADP; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..886
FT /note="Putative respiratory burst oxidase homolog protein
FT H"
FT /id="PRO_0000313760"
FT TOPO_DOM 1..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..421
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..546
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 547..688
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 195..230
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 239..274
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 355..512
FT /note="Ferric oxidoreductase"
FT DOMAIN 552..686
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..145
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 171..183
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
SQ SEQUENCE 886 AA; 100628 MW; C399E5FF4FB0863D CRC64;
MKSNTPTEDS TKWMLESVEI DSMGESSSKE PEINLNKNEG GLKKNASRNL GVGSIIRTLS
VSNWRKSGNL GSPSTRKSGN LGPPTNAVPK KTGPQRVERT TSSAARGLQS LRFLDRTVTG
RERDAWRSIE NRFNQFSVDG KLPKEKFGVC IGMGDTMEFA AEVYEALGRR RQIETENGID
KEQLKLFWED MIKKDLDCRL QIFFDMCDKN GDGKLTEEEV KEVIVLSASA NRLGNLKKNA
AAYASLIMEE LDPDHKGYIE MWQLEILLTG MVTNADTEKM KKSQTLTRAM IPERYRTPMS
KYVSVTAELM HENWKKLWVL ALWAIINVYL FMWKYEEFMR NPLYNITGRC VCAAKGAAET
LKLNMALILV PVCRKTLTIL RSTFLNRVVP FDDNINFHKV IAYMIAFQAL LHTALHIFCN
YPRLSSCSYD VFLTYAGAAL GNTQPSYLGL MLTSVSITGV LMIFFMGFSF TLAMHYFRRN
IVKLPKPFNV LAGFNAFWYA HHLLVLAYIL LIIHGYYLII EKPWYQKTTW MYLAVPMLFY
ASERLFSRLL QEHSHRVNVI KAIVYSGNVL ALYVTKPPGF KYKSGMYMFV KCPDLSKFEW
HPFSITSAPG DDYLSVHIRA LGDWTTELRS RFAKTCEPTQ AAAKPKPNSL MRMETRAAGV
NPHIEESQVL FPKIFIKGPY GAPAQNYQKF DILLLVGLGI GATPFISILK DMLNHLKPGI
PRSGQKYEGS VGGESIGGDS VSGGGGKKFP QRAYFFWVTR EQASFDWFKG VMDDIAEYDK
THVIEMHNYL TSMYEAGDAR SALIAMVQKL QHAKNGVDIV SESRIRTHFA RPNWRKVFSE
LSSKHEACRI GVFYCGSPTL VRPLKELCQE FSLESSTRFT FHKENF
