ID A0A3B6GXT5_WHEAT Unreviewed; 847 AA.
AC A0A3B6GXT5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAF7038491.1, ECO:0000313|EnsemblPlants:TraesCS3D02G347900.2};
GN ORFNames=CFC21_048668 {ECO:0000313|EMBL:KAF7038491.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS3D02G347900.2};
RN [1] {ECO:0000313|EMBL:KAF7038491.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7038491.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS3D02G347900.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3D02G347900.2};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS3D02G347900.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7038491.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7038491.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM022219; KAF7038491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6GXT5; -.
DR SMR; A0A3B6GXT5; -.
DR STRING; 4565.A0A3B6GXT5; -.
DR EnsemblPlants; TraesCS3D02G347900.2; TraesCS3D02G347900.2; TraesCS3D02G347900.
DR Gramene; TraesCS3D02G347900.2; TraesCS3D02G347900.2; TraesCS3D02G347900.
DR Gramene; TraesCS3D03G0772900.1; TraesCS3D03G0772900.1.CDS; TraesCS3D03G0772900.
DR Gramene; TraesKAR3D01G0333560.1; cds.TraesKAR3D01G0333560.1; TraesKAR3D01G0333560.
DR OMA; CMEVGQY; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000019116; Chromosome 3D.
DR Proteomes; UP000815260; Chromosome 3D.
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; 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:SF54; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN J-RELATED; 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; 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:UP000019116};
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 297..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 665..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..208
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 531..659
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 847 AA; 95315 MW; 15D2C5695F0F1374 CRC64;
MASPGGGYAD RPAPPLDGIT VEGGGGRPAG LPRPPGFRGL MQQPSRLASG VRQFASRVSM
KVPEVVPGIR PGGGRMTRMQ SSAQMGLKGL RFLDKTSGSK EGWKAVERRF DEMSKASGRL
PKESFGKCIG MGDSKEFAGE LFVTLSRRRS IEPEQGITKE QLREFWTEMT DQNFDSRLRI
FFDMCDKNGD GMLTEDEVKE VIILSASANK LAKLKSHAAT YSSLIMEELD PDDRGYIEIW
QLETLLRGMV SAQAPEVKLK RTTSSLARTM IPMRYRSPLK RHVTRTMDFA HENWKRIWLV
TLWLAANLAL FVYKFEQYKR RSSFQVMGNC VCVAKGAAET LKLNMALILL PVCRNTLTTL
RSTALSHVIP FDDNINFHKV LAGAIAVGTV VHTLAHVTCD FPRLVSCPSD KFMALLGPNF
GFRQPTYPDL LASAPGVTGI LMIIIMTFSF TLAMHTFRRS VVKLPSPLHH LAGFNAFWYA
HHLLLLVYVL LVVHSYFIFL TRIWYKKTTW MFLIVPVLFY ACERIIRKVR ENNYHVNILK
AAIYPGNVLS LHMKKPPGFK YKSGMYLFVK CPDVSPFEWH PFSITSAPGD DYLSVHIRTL
GDWTSELRNL FGKCCEAQVT SKKATLSRLE TTVVADSATE DTRFPKVFID GPYGAPAQNY
KKYDILLLIG LGIGATPFIS ILKDLLNNIK SNDEVESMHG SEIGSFKNSG PGRAYFYWVT
REQGSFDWFK GVMNEVADND HSDVIEMHNY LTSVYEEGDA RSALIAMVQS LQHAKNGVDI
VSGSKIRTHF ARPNWRKVFS DLANAHKNSR IGVFYCGSPT LTKQLKDLSK EFSQTTTTRF
HFHKENF
//