RBOHB_SOLTU
ID RBOHB_SOLTU Reviewed; 867 AA.
AC Q948T9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 AltName: Full=StRBOHB;
GN Name=RBOHB;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND ACTIVITY REGULATION.
RC STRAIN=cv. Rishiri;
RX PubMed=11386368; DOI=10.1094/mpmi.2001.14.6.725;
RA Yoshioka H., Sugie K., Park H.-J., Maeda H., Tsuda N., Kawakita K.,
RA Doke N.;
RT "Induction of plant gp91 phox homolog by fungal cell wall, arachidonic
RT acid, and salicylic acid in potato.";
RL Mol. Plant Microbe Interact. 14:725-736(2001).
RN [2]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=cv. Rishiri;
RX PubMed=16551687; DOI=10.1093/jxb/erj113;
RA Kobayashi M., Kawakita K., Maeshima M., Doke N., Yoshioka H.;
RT "Subcellular localization of Strboh proteins and NADPH-dependent O2(-)-
RT generating activity in potato tuber tissues.";
RL J. Exp. Bot. 57:1373-1379(2006).
RN [3]
RP MUTAGENESIS OF SER-82; SER-89 AND SER-97, PHOSPHORYLATION AT SER-82 AND
RP SER-97, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17400895; DOI=10.1105/tpc.106.048884;
RA Kobayashi M., Ohura I., Kawakita K., Yokota N., Fujiwara M., Shimamoto K.,
RA Doke N., Yoshioka H.;
RT "Calcium-dependent protein kinases regulate the production of reactive
RT oxygen species by potato NADPH oxidase.";
RL Plant Cell 19:1065-1080(2007).
CC -!- FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide.
CC Involved in the massive phase II oxidative burst induced by pathogen
CC infection. {ECO:0000269|PubMed:11386368}.
CC -!- ACTIVITY REGULATION: Inhibited by diphenylene iodinium (DPI).
CC {ECO:0000269|PubMed:11386368}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16551687};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16551687}.
CC -!- INDUCTION: By fungal elicitor, arachidonic acid and salicylic acid.
CC {ECO:0000269|PubMed:11386368, ECO:0000269|PubMed:16551687}.
CC -!- PTM: Phosphorylation at Ser-82 and Ser-97 is required for full activity
CC of RBOHB. Not phosphorylated at Ser-89. Phosphorylation at Ser-82 is
CC induced by fungal elicitor treatment. {ECO:0000269|PubMed:17400895}.
CC -!- MISCELLANEOUS: K252a and staurosporine, two protein kinase inhibitors,
CC completely block the RBOHB induction by fungal elicitor.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
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DR EMBL; AB050661; BAB70751.1; -; mRNA.
DR RefSeq; NP_001274981.1; NM_001288052.1.
DR AlphaFoldDB; Q948T9; -.
DR SMR; Q948T9; -.
DR STRING; 4113.PGSC0003DMT400063688; -.
DR PeroxiBase; 4546; StRboh02.
DR iPTMnet; Q948T9; -.
DR GeneID; 102603596; -.
DR KEGG; sot:102603596; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; Q948T9; -.
DR OrthoDB; 936110at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q948T9; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:CACAO.
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; 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 SMART; SM00054; EFh; 1.
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 1: Evidence at protein level;
KW Calcium; Cell membrane; FAD; Flavoprotein; Membrane; Metal-binding; NADP;
KW Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..867
FT /note="Respiratory burst oxidase homolog protein B"
FT /id="PRO_0000313764"
FT TOPO_DOM 1..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 380..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..463
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..686
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..867
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 198..233
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 242..277
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 361..519
FT /note="Ferric oxidoreductase"
FT DOMAIN 558..681
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..149
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 175..186
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 217
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 MOD_RES 82
FT /note="Phosphoserine; by CPK"
FT /evidence="ECO:0000269|PubMed:17400895"
FT MOD_RES 97
FT /note="Phosphoserine; by CPK"
FT /evidence="ECO:0000269|PubMed:17400895"
FT MUTAGEN 82
FT /note="S->A: Decreased activity."
FT /evidence="ECO:0000269|PubMed:17400895"
FT MUTAGEN 89
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:17400895"
FT MUTAGEN 97
FT /note="S->A: Decreased activity."
FT /evidence="ECO:0000269|PubMed:17400895"
SQ SEQUENCE 867 AA; 99051 MW; F1D64A8DC6AC6E78 CRC64;
MEIENTRDSD SMRGSRVGFS GSLVSGKKSA RFKDDESYVE ITLDVRDDSV SVQNIKGADH
EAALLASRLE KRPNNTLGSQ LSFHLRQVSK ELKRMTSSNK FQKIDRSKSG AARALRGLQF
MNKNVGTEGW SEVESRFDQL AVNGMLTKSL FGQCIGMKES SEFAEELFDA LARKRCITSP
AVTKDELREF WEQITDTSFD ARLQTFFDMV DKDADGRITQ EEVKEIISLS ASANKLSKIQ
DNSDEYAALI MEELDPGNVG YIELYNLETL LLQAPSHSMN LSTNSRVLSR MLSQKLKPTK
ERNPFKRCKR RLDYFIEDNW KRIWVMALWL SICAGLFTWK FIQYKRRAVF DVMGYCVSVA
KGGAETTKFN MALVLLPVCR NTITWLRSRT KLGKIIPFDD NINFHKVIAF GIAVGVGLHA
ISHLTCDFPR LLHATDEEYE PMKPFFGDER PNNYWWFVKG TEGWTGVVMV VLMIIAYVLA
QPWFRRNRLN LPSTIKKLTG FNAFWYSHHL FVIVYVLFII HGYFLYLSKK WYKKTTWMYI
AVPMILYACE RLLRAFRSGY KAVKILKVAV YPGNVMAVHM SKPQGFKYTS GQYIFVNCSD
VSSFQWHPFT ISSAPGDDYL SMHIRTLGDW TSQLKTLFSK VCEPPTGDQS GLLRADVAKA
DYKPRLPKLL IDGPYGAPAQ DYKKYDVVLL VGLGIGATPL ISIVKDVLNN IKQQKNIEDG
TKGSKRSPFA TKRAYFYWVT REQGSFEWFK GVMDEVSEND QEGLIELHNY CTSVYEEGDA
RSALITMLQS IQQAKSGVDI VSGTRVKTHF ARPNWRQVFK RVTINHPDQR IGVFYCGPQG
LVGELRHLSQ DFSHKTGTKF EFHKENF
