RBOHD_SOLTU
ID RBOHD_SOLTU Reviewed; 858 AA.
AC Q2HXK9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Respiratory burst oxidase homolog protein D;
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHD;
DE AltName: Full=StRBOHD;
GN Name=RBOHD;
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; AB198717; BAE79345.2; -; mRNA.
DR RefSeq; NP_001305507.1; NM_001318578.1.
DR AlphaFoldDB; Q2HXK9; -.
DR SMR; Q2HXK9; -.
DR PeroxiBase; 4548; StRboh04.
DR PRIDE; Q2HXK9; -.
DR GeneID; 102586476; -.
DR KEGG; sot:102586476; -.
DR InParanoid; Q2HXK9; -.
DR OrthoDB; 936110at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q2HXK9; 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; FAD; Flavoprotein; Membrane; Metal-binding; NADP; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..858
FT /note="Respiratory burst oxidase homolog protein D"
FT /id="PRO_0000313766"
FT TOPO_DOM 1..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..351
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..454
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..675
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 697..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 194..229
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 238..273
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 357..514
FT /note="Ferric oxidoreductase"
FT DOMAIN 548..670
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 134..144
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 171..182
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 858 AA; 97539 MW; 9414DDA428D6EBB9 CRC64;
MQNPEDHHSD RELSSPSNTT KSNDDKNVEI TLDIRDDTMA GQSVKNATKT KAEEAELEAL
GKNLQKKCSF GATIVRNVSM RMRLPSFKRQ PHPPQTFDRS STAAQNALKG FKFISKTDGG
SGWDTVQQRF DELTATSDSL LPRAKFGECI GMNRESEGFA LELFNALARR RNITSGCISK
EQLKEFWDQI ANQSFDSRLR TFFDMVDKDA DGRLTEEEVR EIICLSASAN KLSNIQKQAA
EYAALIMEEL DRDQKGYIML ENLEMLLLEA PIQPDGEKGL NRNLSHMLSM KLKPTLETNP
IKRWYNNLKY FLLDNWRRVW VLLLWIGVMA GLFAYKYVQY KNKAAFNVMG HCVCVAKGAA
EVLKLNMALI LLPVCRNTIT WLRNKTKLGG AVPFDDNINF HKVVAGAIAV GVGIHVLAHM
TCDFPRLLNA SPEKYKPMEP YFGDQPRNYW HFVKGVEGVS GIIMVVLMSI AFTLASQRFR
RNKIRLPRPL NKLTGFNAFW YSHHLFVIVY SLLIVHGIEL YLTKEWYKKT TWMYLAIPII
LYSGERLLRA FRSSVKDVKI LKVAMYTGNV LTLQMSKPQG FNYKSGQYMF VNCAAVSPFE
WHPFSITSAP GDEYLSVHIR IVGDWTTKLR DVFSEPSPTG RSGLVADYLQ DKINYPKVLI
DGPYGAPAQD YKEYEVLLLV GLGIGATPMI SIVKDIVNNM KEEKYDHDLE KKTVSGSGRS
NFKRVYFYWV TREQGSFDWF KGLMNELAVM DCDGIIEMHN YCTSVYEEGD ARSALIAMLQ
SINHAKNGVD IVSGTRVKTH FARPNWRNVY KRIALNHTDA RVGVFYCGAP ALTKVLGQLA
LDFSHKTSTK FDFHKENF
