RBOHB_ORYSJ
ID RBOHB_ORYSJ Reviewed; 905 AA.
AC Q5ZAJ0; A0A0P0V2T2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=OsrbohB;
GN Name=RBOHB; OrderedLocusNames=Os01g0360200, LOC_Os01g25820;
GN ORFNames=B1164G11.26, OsJ_01746;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 138-313, AND HOMODIMERIZATION.
RX PubMed=18765925; DOI=10.1107/s1744309108026535;
RA Oda T., Hashimoto H., Kuwabara N., Hayashi K., Kojima C., Kawasaki T.,
RA Shimamoto K., Sato M., Shimizu T.;
RT "Crystallographic characterization of the N-terminal domain of a plant
RT NADPH oxidase.";
RL Acta Crystallogr. F 64:867-869(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 138-313 IN COMPLEX WITH CALCIUM
RP ION, HOMODIMERIZATION, MUTAGENESIS OF GLU-253; 260-LEU--ALA-274; ARG-273
RP AND TYR-277, EF-HAND DOMAINS, AND INTERACTION WITH RAC1.
RX PubMed=19864426; DOI=10.1074/jbc.m109.058909;
RA Oda T., Hashimoto H., Kuwabara N., Akashi S., Hayashi K., Kojima C.,
RA Wong H.L., Kawasaki T., Shimamoto K., Sato M., Shimizu T.;
RT "Structure of the N-terminal regulatory domain of a plant NADPH oxidase and
RT its functional implications.";
RL J. Biol. Chem. 285:1435-1445(2010).
CC -!- FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide.
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer, stabilized by swapping the EF-hand
CC motifs. Interacts with GTP-bound RAC1. {ECO:0000269|PubMed:19864426}.
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}.
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DR EMBL; AP003444; BAD53393.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04934.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS72095.1; -; Genomic_DNA.
DR EMBL; CM000138; EEE54557.1; -; Genomic_DNA.
DR EMBL; AY603975; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015620905.1; XM_015765419.1.
DR PDB; 3A8R; X-ray; 2.40 A; A/B=138-313.
DR PDBsum; 3A8R; -.
DR AlphaFoldDB; Q5ZAJ0; -.
DR SMR; Q5ZAJ0; -.
DR STRING; 4530.OS01T0360200-01; -.
DR PeroxiBase; 5564; OsRboh01.
DR PaxDb; Q5ZAJ0; -.
DR PRIDE; Q5ZAJ0; -.
DR EnsemblPlants; Os01t0360200-01; Os01t0360200-01; Os01g0360200.
DR EnsemblPlants; Os01t0360200-03; Os01t0360200-03; Os01g0360200.
DR GeneID; 4326027; -.
DR Gramene; Os01t0360200-01; Os01t0360200-01; Os01g0360200.
DR Gramene; Os01t0360200-03; Os01t0360200-03; Os01g0360200.
DR KEGG; osa:4326027; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; Q5ZAJ0; -.
DR OMA; HKITANT; -.
DR OrthoDB; 936110at2759; -.
DR PlantReactome; R-OSA-9611432; Recognition of fungal and bacterial pathogens and immunity response.
DR EvolutionaryTrace; Q5ZAJ0; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q5ZAJ0; OS.
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; IDA:UniProtKB.
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 GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
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:SF141; PTHR11972:SF141; 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; 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 3D-structure; Calcium; FAD; Flavoprotein; Membrane; Metal-binding; NADP;
KW Oxidoreductase; Peroxidase; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..905
FT /note="Respiratory burst oxidase homolog protein B"
FT /id="PRO_0000403420"
FT TOPO_DOM 1..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..539
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..560
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..586
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..717
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 739..905
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 229..264
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 273..308
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 395..551
FT /note="Ferric oxidoreductase"
FT DOMAIN 587..715
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..180
FT /note="EF-hand-like 1"
FT REGION 206..217
FT /note="EF-hand-like 2"
FT COMPBIAS 12..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MUTAGEN 253
FT /note="E->A: Impaired calcium binding."
FT /evidence="ECO:0000269|PubMed:19864426"
FT MUTAGEN 260..274
FT /note="Missing: Loss of RAC1-binding."
FT /evidence="ECO:0000269|PubMed:19864426"
FT MUTAGEN 273
FT /note="R->N: Reduced RAC1-binding."
FT /evidence="ECO:0000269|PubMed:19864426"
FT MUTAGEN 277
FT /note="Y->Q: Reduced RAC1-binding."
FT /evidence="ECO:0000269|PubMed:19864426"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:3A8R"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:3A8R"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3A8R"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:3A8R"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:3A8R"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:3A8R"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:3A8R"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:3A8R"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:3A8R"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:3A8R"
FT HELIX 266..285
FT /evidence="ECO:0007829|PDB:3A8R"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:3A8R"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:3A8R"
SQ SEQUENCE 905 AA; 101759 MW; CF3187424F7BA16A CRC64;
MADLEAGMVA AATDQGNSTR SQDDAATLIP NSGNLGSSNR STKTARFKDD DELVEITLDV
QRDSVAIQEV RGVDEGGSGH GTGFDGLPLV SPSSKSGKLT SKLRQVTNGL KMKSSSRKAP
SPQAQQSAKR VRKRLDRTKS SAAVALKGLQ FVTAKVGNDG WAAVEKRFNQ LQVDGVLLRS
RFGKCIGMDG SDEFAVQMFD SLARKRGIVK QVLTKDELKD FYEQLTDQGF DNRLRTFFDM
VDKNADGRLT AEEVKEIIAL SASANKLSKI KERADEYTAL IMEELDPTNL GYIEMEDLEA
LLLQSPSEAA ARSTTTHSSK LSKALSMKLA SNKEMSPVRH YWQQFMYFLE ENWKRSWVMT
LWISICIALF IWKFIQYRNR AVFGIMGYCV TTAKGAAETL KFNMALVLLP VCRNTITWIR
SKTQVGAVVP FNDNINFHKV IAAGVAVGVA LHAGAHLTCD FPRLLHASDA QYELMKPFFG
EKRPPNYWWF VKGTEGWTGV VMVVLMAIAF TLAQPWFRRN KLKDSNPLKK MTGFNAFWFT
HHLFVIVYTL LFVHGTCLYL SRKWYKKTTW MYLAVPVVLY VSERILRLFR SHDAVGIQKV
AVYPGNVLAL YMSKPPGFRY RSGQYIFIKC TAVSPYEWHP FSITSAPGDD YLSVHIRTRG
DWTSRLRTVF SEACRPPTEG ESGLLRADLS KGITDEKARF PKLLVDGPYG APAQDYREYD
VLLLIGLGIG ATPLISIVKD VLNHIQGEGS VGTTEPESSS KAKKKPFMTK RAYFYWVTRE
EGSFEWFRGV MNEVSEKDKD GVIELHNHCS SVYQEGDARS ALIVMLQELQ HAKKGVDILS
GTSVKTHFAR PNWRSVFKKV AVSHENQRVG VFYCGEPVLV PQLRQLSADF THKTNTRFDF
HKENF
