RBOHA_SOLTU
ID RBOHA_SOLTU Reviewed; 963 AA.
AC Q948U0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Respiratory burst oxidase homolog protein A;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHA;
DE AltName: Full=StRBOHA;
GN Name=RBOHA;
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], AND FUNCTION.
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 PHOSPHORYLATION.
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 rapid and transient phase I oxidative burst induced by
CC pathogen infection. {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: Expressed constitutively. Not induced by fungal elicitor.
CC {ECO:0000269|PubMed:16551687}.
CC -!- PTM: Phosphorylated by CPK. {ECO:0000269|PubMed:17400895}.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
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DR EMBL; AB050660; BAB70750.1; -; mRNA.
DR RefSeq; NP_001275304.1; NM_001288375.1.
DR AlphaFoldDB; Q948U0; -.
DR SMR; Q948U0; -.
DR STRING; 4113.PGSC0003DMT400032088; -.
DR PeroxiBase; 4549; StRboh01.
DR GeneID; 102579392; -.
DR KEGG; sot:102579392; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; Q948U0; -.
DR OrthoDB; 936110at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q948U0; baseline.
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; 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 1: Evidence at protein level;
KW Calcium; Cell membrane; FAD; Flavoprotein; Membrane; Metal-binding; NADP;
KW Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..963
FT /note="Respiratory burst oxidase homolog protein A"
FT /id="PRO_0000313763"
FT TOPO_DOM 1..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 457..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 504..535
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..759
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..963
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 276..311
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 438..595
FT /note="Ferric oxidoreductase"
FT DOMAIN 634..754
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..227
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 253..264
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 963 AA; 109146 MW; 501BB92E1157A4F9 CRC64;
MRGLPGHERR WTSDTVSSGK DLSGESSPGT DSGNISGFAS EEFVEVILDL QDDDTIILRS
VEPATVINID ASDPATGVGI GGVSIETPAS LTSTSGTRSP TMRRSTSNKL RQFSQELKAE
AVAKAKHFSQ ELKAELRRFS WSHGHASRTF SPASFFQNAV VGTGNGVDSA LAARALRRQR
AQLDRTRSSA HKALRGLKFI SNNKTNGWNE VENNFAKLAK DGYLYRSDFA QCIGMKDSKE
FALELFDALS RRRRLKVDKI SKEELYEYWS QITDQSFDSR LQIFFDMVDK NEDGRIGEEE
VKEIIMLSAS ANKLSRLKEQ AEEYAALIME ELDPERLGYI ELWQLETLLL QKDTYLNYSQ
ALSYTSQALS QNLQGLRKRS PIRRMSTKLV YSLQENWKRI WVLVLWILIM IGLFLWKFYL
YKQKSAFQVM GYCLLTAKGA AETLKFNMAL ILLPVCRNTI TFLRSTKLSC FVPFDDNINF
HKTVAAAIVT GIILHAGNHL VCDFPKLIHA NNTNYQKYLV NDFGPSQPQY IDLVKGVEGV
TGIIMVILMA IAFTLATRWF RRSLIKFPKP FDRLTGFNAF WYSHHLLIIV YIVLIIHGTF
LYLVHNWYSK TTWMYLAVPV LLYAGERTLR FFRSGLYTVR LLKVAIYPGN VLTLQMSKPP
QFRYKSGQYM FVQCPAVSPF EWHPFSITSA PGDDYLSIHI RQLGDWTQEL KRVFSEACEQ
PEAGKSGLLR ADENTKTSLP KLLIDGPYGA PAQDYRKYDV LLLVGLGIGA TPFISILKDL
LKNIVTMEEQ ADLVSDFSGN SDMSAATSEQ PALNKISPKK RKSTLKTTNA YFYWVTREQG
SFDWFKGVMN EVAELDQRGV IEMHNYLTSV YEEGDARSAL ITMVQALNHA KNGVDIVSGT
SVRTHFARPN WRKVFSKTLT KHANARIGVF YCGAPILAKE LSKLCKEFNQ KGTTKFEFHK
EHF
