RBOHJ_ARATH
ID RBOHJ_ARATH Reviewed; 912 AA.
AC Q9LZU9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Putative respiratory burst oxidase homolog protein J;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHJ;
DE Short=AtRBOHJ;
GN Name=RBOHJ; OrderedLocusNames=At3g45810; ORFNames=F16L2.20;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB82805.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162459; CAB82805.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78076.1; -; Genomic_DNA.
DR PIR; T47521; T47521.
DR RefSeq; NP_190167.2; NM_114450.3.
DR AlphaFoldDB; Q9LZU9; -.
DR SMR; Q9LZU9; -.
DR STRING; 3702.AT3G45810.1; -.
DR iPTMnet; Q9LZU9; -.
DR PaxDb; Q9LZU9; -.
DR PRIDE; Q9LZU9; -.
DR ProteomicsDB; 236528; -.
DR EnsemblPlants; AT3G45810.1; AT3G45810.1; AT3G45810.
DR GeneID; 823724; -.
DR Gramene; AT3G45810.1; AT3G45810.1; AT3G45810.
DR KEGG; ath:AT3G45810; -.
DR Araport; AT3G45810; -.
DR TAIR; locus:2077192; AT3G45810.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; Q9LZU9; -.
DR OMA; HRTYISK; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; Q9LZU9; -.
DR BioCyc; ARA:AT3G45810-MON; -.
DR PRO; PR:Q9LZU9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZU9; baseline and differential.
DR Genevisible; Q9LZU9; 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; 1.
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..912
FT /note="Putative respiratory burst oxidase homolog protein
FT J"
FT /id="PRO_0000313762"
FT TOPO_DOM 1..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..697
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..912
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 205..240
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 366..523
FT /note="Ferric oxidoreductase"
FT DOMAIN 562..695
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..155
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 181..193
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
SQ SEQUENCE 912 AA; 102937 MW; 7E49AB05F7D4399A CRC64;
MKNNKKVGTE DSTKWMLESV EIDPKGDSSV KQPESTINSN NPESSGAGGG ILKNVSKNLA
VGSIIRSMSV NKWRKSGNLG SPSTRKSGNL GPPLPVSQVK RPGPQRVERT TSSAARGLQS
LRFLDRTVTG RERDSWRSIE NRFNQFAVDG RLPKDKFGVC IGMGDTLEFA AKVYEALGRR
RQIKTENGID KEQLKLFWED MIKKDLDCRL QIFFDMCDKD GDGKLTEEEV KEVIVLSASA
NRLVNLKKNA ASYASLIMEE LDPNEQGYIE MWQLEVLLTG IVSNADSHKV VRKSQQLTRA
MIPKRYRTPT SKYVVVTAEL MYEHWKKIWV VTLWLAVNVV LFMWKYEEFT TSPLYNITGR
CLCAAKGTAE ILKLNMALIL VPVLRRTLTF LRSTFLNHLI PFDDNINFHK LIAVAIAVIS
LLHTALHMLC NYPRLSSCPY NFYSDYAGNL LGAKQPTYLG LMLTPVSVTG VLMIIFMGIS
FTLAMHYFRR NIVKLPIPFN RLAGFNSFWY AHHLLVIAYA LLIIHGYILI IEKPWYQKTT
WMYVAIPMVL YASERLFSRV QEHNHRVHII KAIVYSGNVL ALYMTKPQGF KYKSGMYMFV
KCPDISKFEW HPFSITSAPG DEYLSVHIRA LGDWTSELRN RFAETCEPHQ KSKPSPNDLI
RMETRARGAN PHVEESQALF PRIFIKGPYG APAQSYQKFD ILLLIGLGIG ATPFISILKD
MLNNLKPGIP KTGQKYEGSV GGESLGGSSV YGGSSVNGGG SVNGGGSVSG GGRKFPQRAY
FYWVTREQAS FEWFKGVMDD IAVYDKTNVI EMHNYLTSMY EAGDARSALI AMVQKLQHAK
NGVDIVSESR IRTHFARPNW RKVFSELSNK HETSRIGVFY CGSPTLVRPL KSLCQEFSLE
SSTRFTFHKE NF
