RBOHB_ARATH
ID RBOHB_ARATH Reviewed; 843 AA.
AC Q9SBI0; O04020; O04021; Q84TJ9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Respiratory burst oxidase homolog protein B;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHB;
DE Short=AtRBOHB;
GN Name=RBOHB; OrderedLocusNames=At1g09090; ORFNames=F7G19.3, F7G19.4;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION.
RX PubMed=9490748; DOI=10.2307/3870703;
RA Keller T., Damude H.G., Werner D., Doerner P., Dixon R.A., Lamb C.;
RT "A plant homolog of the neutrophil NADPH oxidase gp91phox subunit gene
RT encodes a plasma membrane protein with Ca2+ binding motifs.";
RL Plant Cell 10:255-266(1998).
RN [6]
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=2;
CC Name=1;
CC IsoId=Q9SBI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SBI0-2; Sequence=VSP_030130, VSP_030131;
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70398.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAB70399.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF055354; AAC39476.1; -; Genomic_DNA.
DR EMBL; AC000106; AAB70398.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC000106; AAB70399.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28394.1; -; Genomic_DNA.
DR EMBL; BT005716; AAO64136.1; -; mRNA.
DR PIR; A86223; A86223.
DR PIR; B86223; B86223.
DR RefSeq; NP_172383.3; NM_100780.3.
DR RefSeq; NP_973799.1; NM_202070.1. [Q9SBI0-1]
DR AlphaFoldDB; Q9SBI0; -.
DR SMR; Q9SBI0; -.
DR STRING; 3702.AT1G09090.2; -.
DR PeroxiBase; 3283; AtRboh02.
DR PaxDb; Q9SBI0; -.
DR PRIDE; Q9SBI0; -.
DR ProteomicsDB; 236525; -. [Q9SBI0-1]
DR EnsemblPlants; AT1G09090.2; AT1G09090.2; AT1G09090. [Q9SBI0-1]
DR GeneID; 837430; -.
DR Gramene; AT1G09090.2; AT1G09090.2; AT1G09090. [Q9SBI0-1]
DR KEGG; ath:AT1G09090; -.
DR Araport; AT1G09090; -.
DR TAIR; locus:2036104; AT1G09090.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; Q9SBI0; -.
DR OMA; FIRGTHV; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; Q9SBI0; -.
DR BioCyc; ARA:AT1G09090-MON; -.
DR PRO; PR:Q9SBI0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SBI0; baseline and differential.
DR Genevisible; Q9SBI0; 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; IMP:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR011992; EF-hand-dom_pair.
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; IPR029654; RBOHB.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF64; PTHR11972:SF64; 1.
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; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; FAD; Flavoprotein; Membrane; Metal-binding;
KW NADP; Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..843
FT /note="Respiratory burst oxidase homolog protein B"
FT /id="PRO_0000313754"
FT TOPO_DOM 1..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..529
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..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..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 171..206
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 215..250
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 336..495
FT /note="Ferric oxidoreductase"
FT DOMAIN 534..657
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..122
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 148..159
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIJ0"
FT VAR_SEQ 618..621
FT /note="CQLP -> TIFQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_030130"
FT VAR_SEQ 622..843
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_030131"
SQ SEQUENCE 843 AA; 96390 MW; EBA11C6C74FED340 CRC64;
MREEEMESSS EGETNKISRC KATGSDNPDE DYVEITLEVR DETINTMKAK ATLRSVLSGR
LKTMVKSLSF ASRRLDRSKS FGAMFALRGL RFIAKNDAVG RGWDEVAMRF DKLAVEGKLP
KSKFGHCIGM VESSEFVNEL FEALVRRRGT TSSSITKTEL FEFWEQITGN SFDDRLQIFF
DMVDKNLDGR ITGDEVKEII ALSASANKLS KIKENVDEYA ALIMEELDRD NLGYIELHNL
ETLLLQVPSQ SNNSPSSANK RALNKMLSQK LIPTKDRNPV KRFAMNISYF FLENWKRIWV
LTLWISICIT LFTWKFLQYK RKTVFEVMGY CVTVAKGSAE TLKFNMALIL LPVCRNTITW
LRTKSKLIGS VVPFDDNINF HKVVAFGIAV GIGLHAISHL ACDFPRLLHA KNVEFEPMKK
FFGDERPENY GWFMKGTDGW TGVTMVVLML VAYVLAQSWF RRNRANLPKS LKRLTGFNAF
WYSHHLFVIV YVLLIVHGYF VYLSKEWYHK TTWMYLAVPV LLYAFERLIR AFRPGAKAVK
VLKVAVYPGN VLSLYMSKPK GFKYTSGQYI YINCSDVSPL QWHPFSITSA SGDDYLSVHI
RTLGDWTSQL KSLYSKVCQL PSTSQSGLFI ADIGQANNIT RFPRLLIDGP YGAPAQDYRN
YDVLLLVGLG IGATPLISII RDVLNNIKNQ NSIERGTNQH IKNYVATKRA YFYWVTREQG
SLEWFSEVMN EVAEYDSEGM IELHNYCTSV YEEGDARSAL ITMLQSLHHA KSGIDIVSGT
RVRTHFARPN WRSVFKHVAV NHVNQRVGVF YCGNTCIIGE LKRLAQDFSR KTTTKFEFHK
ENF
