ID B9I440_POPTR Unreviewed; 909 AA.
AC B9I440;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 2.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=NAD(P)H oxidase (H(2)O(2)-forming) {ECO:0008006|Google:ProtNLM};
GN ORFNames=POPTR_012G111600 {ECO:0000313|EMBL:PNT10599.1};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT10599.1, ECO:0000313|Proteomes:UP000006729};
RN [1] {ECO:0000313|EMBL:PNT10599.1, ECO:0000313|Proteomes:UP000006729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.
CC {ECO:0000256|ARBA:ARBA00007975}.
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DR EMBL; CM009301; PNT10599.1; -; Genomic_DNA.
DR RefSeq; XP_002318793.2; XM_002318757.2.
DR AlphaFoldDB; B9I440; -.
DR STRING; 3694.B9I440; -.
DR EnsemblPlants; Potri.012G111600.1.v4.1; Potri.012G111600.1.v4.1; Potri.012G111600.v4.1.
DR GeneID; 7484354; -.
DR Gramene; Potri.012G111600.1.v4.1; Potri.012G111600.1.v4.1; Potri.012G111600.v4.1.
DR KEGG; pop:7484354; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; B9I440; -.
DR OMA; TMHAGAH; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000006729; Chromosome 12.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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 PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR PANTHER; PTHR11972:SF213; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN C; 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 SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR SMART; SM00054; EFh; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000006729};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 348..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..260
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 581..704
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 102997 MW; AA39810D6415A253 CRC64;
MQDMGREDHH SDSEMSGSER LAYSGPLSGP LNKRPGRKSA RFSIPGTTTS KDEQYVEITL
DVRNDSVAVH SVKAANGVEE DPEMALLAKG LEKRSASNVL RTASARIRQV SHEIKRLASF
SKRPPPGRLD RSKSAAAHAL KGLKFISKTD GGAGWAAVEK RFDEITASTD GLLPRARFCE
CIGMKESKDF AGELFNALAR KRNMHCDSIS KAELREFWDQ ISNQSFDSRL QTFFDMVDKD
ADGRITEEEV REIITLSASA NKLSNIQKQA EEYAALIMEE LDPENHGYIL IENLEMLLLQ
GSNQSVRGES RNLSHMLSQK LKPTLDSNPL NRWCRSTKYF LLDNWQRVWV MALWIVFMAS
LFAYKYIQYR RREAYEVMGH CVCMAKGAAE TLKLNMALIL LPVCRNTLTW LRNKTKLGVV
VPFDDNLNFH KVIAVGIAVG VGIHGISHLA CDFPRLLQAS EEKWELMQQF FGDQPSSYWH
FVKSKEGVTG IVMVVLMAIA FTLATPWFRR NKLNLPTWLK KLTGFNAFWY SHHLFVIVYT
LLVVHGYYLY LTHKWYKKTT WMYLAVPVIL YGSERLIRAL RSSIKAVTIQ KVAIYPGNVL
ALHMSKPQGF RYKSGQYMFV NCAAVSPFEW HPFSITSAPG DDYLSVHIRT LGDWTRQLRT
VFSEVCQPPP DGKSGLLRSD CFQGHNSNLP RVLIDGPYGA PAQDYKKYEV VLLVGLGIGA
TPMISIVKDI VSNIRTMEEE ENAVENGAGG IGNSPSTKIP SPYTQKRKEN FKTRRAYFYW
VTREQGSFDW FKGVMNEVAE IDHNHVIELH NYCTSVYEEG DARSALIAML QSINHAKNGV
DIVSGTRVKS HFAKPNWRNV YKRTALNHPD SRVGVFYCGA PALTKELRQL ALDFSHKTST
KFDFHKENF
//
