RBOHG_ARATH
ID RBOHG_ARATH Reviewed; 849 AA.
AC Q9SW17; F4JRU6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Putative respiratory burst oxidase homolog protein G;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHG;
DE Short=AtRBOHG;
GN Name=RBOHG; OrderedLocusNames=At4g25090; ORFNames=F13M23.230;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SW17-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79418.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035523; CAB36751.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161562; CAB79418.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85005.1; -; Genomic_DNA.
DR PIR; T05530; T05530.
DR RefSeq; NP_194239.2; NM_118641.3. [Q9SW17-1]
DR AlphaFoldDB; Q9SW17; -.
DR SMR; Q9SW17; -.
DR STRING; 3702.AT4G25090.1; -.
DR PeroxiBase; 3285; AtRboh07.
DR PaxDb; Q9SW17; -.
DR PRIDE; Q9SW17; -.
DR ProteomicsDB; 225913; -. [Q9SW17-1]
DR EnsemblPlants; AT4G25090.1; AT4G25090.1; AT4G25090. [Q9SW17-1]
DR GeneID; 828612; -.
DR Gramene; AT4G25090.1; AT4G25090.1; AT4G25090. [Q9SW17-1]
DR KEGG; ath:AT4G25090; -.
DR Araport; AT4G25090; -.
DR TAIR; locus:2117258; AT4G25090.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; Q9SW17; -.
DR OrthoDB; 936110at2759; -.
DR BioCyc; ARA:AT4G25090-MON; -.
DR PRO; PR:Q9SW17; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SW17; baseline and differential.
DR Genevisible; Q9SW17; AT.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA: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; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Alternative splicing; Calcium; FAD; Flavoprotein; Membrane; Metal-binding;
KW NADP; Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..849
FT /note="Putative respiratory burst oxidase homolog protein
FT G"
FT /id="PRO_0000313759"
FT TOPO_DOM 1..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..409
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..489
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..536
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 537..659
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 176..211
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 220..255
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 342..502
FT /note="Ferric oxidoreductase"
FT DOMAIN 541..657
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..128
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 153..164
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
SQ SEQUENCE 849 AA; 96862 MW; 86AD68BB20C01876 CRC64;
MQRVSFEVKD TEAEKSSSEI LSGSLPSTYR NPAMENVGNA VDDGSSVKNN PKLDMQKQNG
LVKWFKKCLT MVSGESKAPR LDRSKSTAGQ ALKGLKIISK TDGNAAWTVV EKRYLKITAN
TDGLLLRSKF GECIGMNSKE FALELFDALA RKSHLKGDVI TETELKKFWE QINDKSFDSR
LITFFDLMDK DSDGRLTEDE VREIIKLSSS ANHLSCIQNK ADEYAAMIME ELDPDHMGYI
MMESLKKLLL QAETKSVSTD INSEERKELS DMLTESLKPT RDPNHLRRWY CQLRFFVLDS
WQRVWVIALW LTIMAILFAY KYIQYKNRAV YEVLGPCVCL AKGAAETLKL NMALILLPVC
RNTITWLRNK TRLGVFVPFD DNLNFHKVIA VGIAIGVAIH SVSHLACDFP LLIAATPAEY
MPLGKFFGEE QPKRYLHFVK STEGITGLVM VFLMVIAFTL AMPWFRRGKL EKKLPGPLKK
LASFNAFWYT HHLFVIVYIL LVLHGYYIYL NKEWYKKTTW MYLAVPVALY AYERLIRAFR
SSIRTVKVLK MAAYPGKVLT LQMSKPTNFK YMSGQYMFVN CPAVSPFEWH PFSITSTPQD
DYLSVHIKAL GDWTEAIQGV FSEVSKPPPV GDMLNGANSP RFPKIMIDGP YGAPAQDYKK
YEVVLLIGLG IGATPMISII KDIINNTETK EQLSQMEKGS PQEQQGNKET FKTRRAYFYW
VTKEQGTFDW FKNIMNEIAE RDKSKVIELH NHCTSVYEEG DVRSALIRML QSLNYAKNGL
DIVAGTRVMS HFARPNWKNV YKQIAMDHPG ANVGVFYCGA PVLTKELRQL ALEFTHKTST
RFSFHKENF
