ID A0A1J7G9L2_LUPAN Unreviewed; 945 AA.
AC A0A1J7G9L2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OIV97039.1};
GN ORFNames=TanjilG_11556 {ECO:0000313|EMBL:OIV97039.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV97039.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIV97039.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIV97039.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
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; CM007375; OIV97039.1; -; Genomic_DNA.
DR RefSeq; XP_019416280.1; XM_019560735.1.
DR AlphaFoldDB; A0A1J7G9L2; -.
DR STRING; 3871.A0A1J7G9L2; -.
DR EnsemblPlants; OIV97039; OIV97039; TanjilG_11556.
DR GeneID; 109327553; -.
DR Gramene; OIV97039; OIV97039; TanjilG_11556.
DR KEGG; lang:109327553; -.
DR OMA; TMHAGAH; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000188354; Chromosome LG15.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 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:UP000188354};
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 382..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 565..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 596..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 262..297
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 619..743
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 54..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 107143 MW; 44541DF4C80CE39C CRC64;
MEAYKVGVVS ASDLHPHESN IELIDTNQRV SHSEPLNKRV SRKNYKLNSS ALTSAIDNGH
SSNKSHNKEQ QHDDEEEEED HVEVTVEIKG DSVAVHSVKP VSTACNEDIS GEDENLILLG
KGMQKKSSFV GASVMRSASS KIKQVSQELK RFASLSKQGE SSKVVHFDRN KSAAAHALKG
LKFFTNGGVG WAQVEKQFDI LTASNDGYLH CSLFAKCIGM NKESEAFAGE LFDALCRRRE
IQGISINKAQ LKDFWDQISD QSFDSRLKTF FDMVDKDADG RITEEEIKEI ICLSATTNKL
SNIQKQAEEY AALIMEELDP DDTGFVMLDN LEILLLHGPS HSTRGYSKYL SQMLSVKLKL
IYEENPIKRW YRETMYFLQD NWQRSWVLLL WISVMLGLFA YKFTQYRRKA AYEVMGHCVC
MAKGAAETLK LNMAIILLPV CRNTITWLRN KTKLGIAVPF DDNLNFHKVI AVAVAIAVGI
HGIYHLACDF PRLLHADIEK YKLMQPFFGD QPQSYWFFVK SWEGVTGIIM VVLMAIAFTL
ASPWFRRGRI KLPKPLDSLT GFNAFWYSHH LFIIVYALLI VHGIKLYLSK EWYKKTTWMY
LAIPIIIYTL ERLVRALRST IKPVRILKVA VYPGNVLALH MSKPHGFRYK SGQYMFVNCA
AVSPFEWHPF SITSAPDDDY LSVHIRTLGD WTRSLRAKFS EVCQPPDNGK SGLLRAECLP
GDSSPSNLPK VLIDGPYGAP AQDYKQYEVV LLVGLGIGAT PMISILKDIM NNFKAMEEEE
EGTTIEEGVI NKSPRTPQNN KANLSNFKTR KAYFYWITRE QGSFDWFKGV MNEVAEDDHS
GVIELHNYCT SVYEEGDARS ALIAMLQSLN HAKNGVDIVS GTRVKSHFAK PNWRSVYKRI
ALNHSQARVG VFYCGPPALT QELRQLSSDF SRNTTTKYDF HKENF
//
