RBOHC_ARATH
ID RBOHC_ARATH Reviewed; 905 AA.
AC O81210; Q5VI40; Q8GZ82; Q9FI42;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Respiratory burst oxidase homolog protein C;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHC;
DE Short=AtRBOHC;
DE AltName: Full=Protein ROOT HAIR DEFECTIVE 2;
GN Name=RBOHC; Synonyms=RHD2; OrderedLocusNames=At5g51060; ORFNames=K3K7.25;
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].
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Jones M.A., Raymond M., Fu Y., Yang Z., Grierson C.S., Smirnoff N.;
RT "ROP2 regulates calcium-dependent root-hair reactive oxygen species
RT formation through AtrbohC/RHD2.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12660786; DOI=10.1038/nature01485;
RA Foreman J., Demidchik V., Bothwell J.H.F., Mylona P., Miedema H.,
RA Torres M.A., Linstead P., Costa S., Brownlee C., Jones J.D.G., Davies J.M.,
RA Dolan L.;
RT "Reactive oxygen species produced by NADPH oxidase regulate plant cell
RT growth.";
RL Nature 422:442-446(2003).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY POTASSIUM STARVATION.
RX PubMed=15173595; DOI=10.1073/pnas.0401707101;
RA Shin R., Schachtman D.P.;
RT "Hydrogen peroxide mediates plant root cell response to nutrient
RT deprivation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8827-8832(2004).
RN [8]
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 Required for H(2)O(2) production in response to K(+) deficiency and for
CC the generation of reactive oxygen species (ROS) that regulate cell
CC expansion through the activation of Ca(2+) channels.
CC {ECO:0000269|PubMed:12660786, ECO:0000269|PubMed:15173595}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In roots, expressed in the epidermis in the
CC proximal regions of the meristem, in the elongation zone, in the
CC differentiation zone and in elongating root hairs.
CC {ECO:0000269|PubMed:12660786, ECO:0000269|PubMed:15173595}.
CC -!- INDUCTION: By potassium starvation. {ECO:0000269|PubMed:15173595}.
CC -!- DISRUPTION PHENOTYPE: Plants have short root hairs and stunted roots.
CC {ECO:0000269|PubMed:12660786}.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39477.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF055355; AAC39477.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY452508; AAS15724.1; -; Genomic_DNA.
DR EMBL; AB017063; BAB08752.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96028.1; -; Genomic_DNA.
DR EMBL; AK117159; BAC41837.1; -; mRNA.
DR RefSeq; NP_199919.1; NM_124485.3.
DR AlphaFoldDB; O81210; -.
DR SMR; O81210; -.
DR BioGRID; 20424; 15.
DR IntAct; O81210; 15.
DR STRING; 3702.AT5G51060.1; -.
DR PeroxiBase; 3284; AtRboh03.
DR iPTMnet; O81210; -.
DR PaxDb; O81210; -.
DR PRIDE; O81210; -.
DR ProteomicsDB; 225973; -.
DR EnsemblPlants; AT5G51060.1; AT5G51060.1; AT5G51060.
DR GeneID; 835179; -.
DR Gramene; AT5G51060.1; AT5G51060.1; AT5G51060.
DR KEGG; ath:AT5G51060; -.
DR Araport; AT5G51060; -.
DR TAIR; locus:2157348; AT5G51060.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; O81210; -.
DR OMA; KGAMNEV; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; O81210; -.
DR BioCyc; ARA:AT5G51060-MON; -.
DR PRO; PR:O81210; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O81210; baseline and differential.
DR Genevisible; O81210; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:TAIR.
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; IMP:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IMP:TAIR.
DR GO; GO:0033198; P:response to ATP; IMP:TAIR.
DR GO; GO:0010053; P:root epidermal cell differentiation; IMP:TAIR.
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; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Calcium; FAD; Flavoprotein; Membrane; Metal-binding; NADP; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..905
FT /note="Respiratory burst oxidase homolog protein C"
FT /id="PRO_0000313755"
FT TOPO_DOM 1..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..536
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..583
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 584..713
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..905
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 226..261
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 270..305
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 390..549
FT /note="Ferric oxidoreductase"
FT DOMAIN 587..711
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..178
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 203..214
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
FT CONFLICT 676
FT /note="P -> L (in Ref. 5; BAC41837)"
FT /evidence="ECO:0000305"
FT CONFLICT 870
FT /note="G -> R (in Ref. 2; AAS15724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 905 AA; 102518 MW; FF797C0407E6944B CRC64;
MSRVSFEVSG GYHSDAEAGN SGPMSGGQLP PIYKKPGNSR FTAENSQRTR TAPYVDLTVD
VQDDTVSVHS LKMEGGSSVE ESPELTLLKR NRLEKKTTVV KRLASVSHEL KRLTSVSGGI
GGRKPPRPAK LDRTKSAASQ ALKGLKFISK TDGGAGWSAV EKRFNQITAT TGGLLLRTKF
GECIGMTSKD FALELFDALA RRRNITGEVI DGDQLKEFWE QINDQSFDSR LKTFFDMVDK
DADGRLTEDE VREIISLSAS ANNLSTIQKR ADEYAALIME ELDPDNIGYI MLESLETLLL
QAATQSVITS TGERKNLSHM MSQRLKPTFN RNPLKRWYRG LRFFLLDNWQ RCWVIVLWFI
VMAILFTYKY IQYRRSPVYP VMGDCVCMAK GAAETVKLNM ALILLPVCRN TITWLRNKTR
LGRVVPFDDN LNFHKVIAVG IIVGVTMHAG AHLACDFPRL LHATPEAYRP LRQFFGDEQP
KSYWHFVNSV EGITGLVMVL LMAIAFTLAT PWFRRGKLNY LPGPLKKLAS FNAFWYTHHL
FVIVYILLVA HGYYLYLTRD WHNKTTWMYL VVPVVLYACE RLIRAFRSSI KAVTIRKVAV
YPGNVLAIHL SRPQNFKYKS GQYMFVNCAA VSPFEWHPFS ITSAPQDDYL SVHIRVLGDW
TRALKGVFSE VCKPPPAGVS GLLRADMLHG ANNPDFPKVL IDGPYGAPAQ DYKKYEVVLL
VGLGIGATPM ISIVKDIVNN IKAKEQAQLN RMENGTSEPQ RSKKESFRTR RAYFYWVTRE
QGSFDWFKNI MNEVAERDAN RVIEMHNYCT SVYEEGDARS ALIHMLQSLN HAKNGVDIVS
GTRVMSHFAK PNWRNVYKRI AMDHPNTKVG VFYCGAPALT KELRHLALDF THKTSTRFSF
HKENF
