RBOHC_SOLTU
ID RBOHC_SOLTU Reviewed; 938 AA.
AC Q2HXL0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Respiratory burst oxidase homolog protein C;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHC;
DE AltName: Full=StRBOHC;
GN Name=RBOHC;
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].
RX PubMed=16407438; DOI=10.1104/pp.105.074906;
RA Yamamizo C., Kuchimura K., Kobayashi A., Katou S., Kawakita K.,
RA Jones J.D.G., Doke N., Yoshioka H.;
RT "Rewiring mitogen-activated protein kinase cascade by positive feedback
RT confers potato blight resistance.";
RL Plant Physiol. 140:681-692(2006).
RN [2]
RP PHOSPHORYLATION, AND TISSUE SPECIFICITY.
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 May be responsible for the oxidative burst in response to pathogen
CC attack in the leaves.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:17400895}.
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; AB198716; BAE79344.2; -; mRNA.
DR RefSeq; NP_001275453.1; NM_001288524.1.
DR AlphaFoldDB; Q2HXL0; -.
DR SMR; Q2HXL0; -.
DR STRING; 4113.PGSC0003DMT400036734; -.
DR PeroxiBase; 4547; StRboh03.
DR PRIDE; Q2HXL0; -.
DR GeneID; 102598898; -.
DR KEGG; sot:102598898; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; Q2HXL0; -.
DR OrthoDB; 936110at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q2HXL0; baseline.
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 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; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Calcium; Coiled coil; FAD; Flavoprotein; Membrane; Metal-binding; NADP;
KW Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..938
FT /note="Respiratory burst oxidase homolog protein C"
FT /id="PRO_0000313765"
FT TOPO_DOM 1..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..509
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 567..580
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..938
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 245..280
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 289..324
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 408..565
FT /note="Ferric oxidoreductase"
FT DOMAIN 599..727
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..195
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 222..233
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT REGION 762..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 115..141
FT /evidence="ECO:0000255"
FT COMPBIAS 767..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 938 AA; 105302 MW; 9189D640D118A35B CRC64;
MQNSENHHPH HHHHHSDTEI IGNDRASYSG PLSGPLNKRG GKKSARFNIP ESTDIGTSAG
AGAKSNDDAY VEITLDVRED SVAVHSVKTA GGADVEDPEL ALLAKGLEKK STLGASLVRN
ASSRIRQVSQ ELKRLASLNK RPIPTGRFDR NKSAAAHALK GLKFISKTDG GAGWAAVEKR
FDEITAPTTG LLPRAKFGEC IGMNKESKEF AGELYDALAR RRNITTDSIN KAQLKEFWDQ
VADQSFDTRL QTFFDMVDKD ADGRITEEEV REIIGLSASA NRLSTIQKQS DEYAAMIMEE
LDPNNLGYIM IENLEMLLLQ APNQSVQRGG ESRNLSQMLS QKLKHTQEPN PLVRWYKSFM
YFLLDNWQRV WVLLLWIGIM AVLFTWKYIQ YKQKAAYDVM GPCVCLAKGA AETIKLNMAI
ILLPVCRNTI TWLRNKTRLG SAVPFDDNLN FHKVIAVAIA LGVAIHGLAH LTCDFPKLLN
ASEEAYEPMI YYFGEQPESY WWFVRGVEGV TGIIMVVLMA IAFTLATPWF RRGRVSFPKP
FHKLTGFNAF WYSHHLFIIV YTLLIVHGEK LYITKDWYKR STWMYLTVPL VLYAGERLLR
AFRSSIKAVK ILKVAVYPGN VLALHMSKPQ GYKYKSGQYM FVNCAAVSPF EWHPFSITSA
PGDDHLSVHI RTLGDWTRQL KTVFSEVCQP PPNGKSGLLR ADYLQGENNP NFPRVLIDGP
YGAPAQDYKQ YEVVLLVGLG IGATPMISIV KDIVNNMKAM DEEENSLENG NGMSNAAQNA
SPNMAQKRGK SSSASGGNSF NTRRAYFYWV TREQGSFDWF KGIMNEAAEM DHKGVIEMHN
YCTSVYEEGD ARSALITMLQ SLHHAKSGVD IVSGTRVKSH FAKPNWRNVY KRIALNHPEA
KVGVFYCGAP ALTKELKQHA LNFSHKTSTK FDFHKENF
