ID A0A3B6FSF9_WHEAT Unreviewed; 850 AA.
AC A0A3B6FSF9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAF7031491.1, ECO:0000313|EnsemblPlants:TraesCS3B02G386600.1};
GN ORFNames=CFC21_042811 {ECO:0000313|EMBL:KAF7031491.1};
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:TraesCS3B02G386600.1};
RN [1] {ECO:0000313|EMBL:KAF7031491.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7031491.1};
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:TraesCS3B02G386600.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3B02G386600.1};
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:TraesCS3B02G386600.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7031491.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7031491.1};
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; CM022218; KAF7031491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6FSF9; -.
DR SMR; A0A3B6FSF9; -.
DR STRING; 4565.A0A3B6FSF9; -.
DR PaxDb; 4565-Traes_3B_FF5B3D6BB-1; -.
DR EnsemblPlants; TraesCS3B02G386600.1; TraesCS3B02G386600.1; TraesCS3B02G386600.
DR Gramene; TraesCLE_scaffold_022383_01G000400.1; TraesCLE_scaffold_022383_01G000400.1; TraesCLE_scaffold_022383_01G000400.
DR Gramene; TraesCS3B02G386600.1; TraesCS3B02G386600.1; TraesCS3B02G386600.
DR Gramene; TraesCS3B03G0967100.2; TraesCS3B03G0967100.2.CDS; TraesCS3B03G0967100.
DR Gramene; TraesKAR3B01G0403860.1; cds.TraesKAR3B01G0403860.1; TraesKAR3B01G0403860.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000019116; Chromosome 3B.
DR Proteomes; UP000815260; Chromosome 3B.
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 300..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..685
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 176..211
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 534..662
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 95661 MW; 8FD7D1FC3A9800A8 CRC64;
MASPGRGYAD RAAPPLDGIT VDGGGGRTPP PAGLPRPPGF RGLMQQPSRL ASGVRQFASR
VSMKVPEVVP GIRPGGGRMT RMQSSAQMGL KGLRFLDKTS GSKEGWKAVE RRFDEMSKAS
GRLPKESFGK CIGMGDSKEF AGELFVTLSR RRSIEPEQGI TKEQLREFWT EMTDQNFDSR
LRIFFDMCDK NGDGMLTEDE VKEVIILSAS ANKLAKLKSH AATYSSLIME ELDPDDRGYI
EIWQLETLLR GMVSAQAPEV KLKRTTSSLA RTMIPMRYRS PLKRHVTRTM DFIHENWKRI
WLVTLWLAAN LALFVYKFEQ YKHRSSFQVM GNCVCVAKGA AETLKLNMAL ILLPVCRNTL
TTLRSTALSH VIPFDDNINF HKVLAGAIAV GTVVHTLAHV TCDFPRLISC PSDKFMALLG
PNFGFRQPTY PDLLASAPGV TGILMIIIMT FSFTLAMHTF RRSVVKLPSP LHHLAGFNAF
WYAHHLLLLV YVLLVVHSYF IFLTRIWYKK TTWMFLIVPV LFYACERIIR KVRENNYHVN
ILKAAIYPGN VLSLHMKKPP GFKYKSGMYL FVKCPDVSPF EWHPFSITSA PGDDYLSVHI
RTLGDWTSEL RSLFGKCCEA QVTSKKATLS RLETTVVADS ATEDTRFPKV FIDGPYGAPA
QNYKKYDILL LIGLGIGATP FISILKDLLN NIKSNDEVES IHGSEIGSFK NSGPGRAYFY
WVTREQGSFD WFKGVMNEVA DNDHSNVIEM HNYLTSVYEE GDARSALIAM VQSLQHAKNG
VDIVSGSKIR THFARPNWRK VFSDLANAHK NSRIGVFYCG SPTLTKQLKD LSKEFSQTTT
TRFHFHKENF
//
