ID DUOX1_RAT Reviewed; 1551 AA. AC Q8CIY2; DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 02-SEP-2026, entry version 134. DE RecName: Full=Dual oxidase 1 {ECO:0000312|RGD:628760}; DE EC=1.-.-.- {ECO:0000250|UniProtKB:Q9NRD9}; DE EC=1.11.1.- {ECO:0000250|UniProtKB:Q9NRD9}; DE EC=1.6.3.1 {ECO:0000250|UniProtKB:Q9NRD9}; DE Flags: Precursor; GN Name=Duox1 {ECO:0000312|RGD:628760}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Fischer 344; RX PubMed=12538618; DOI=10.1210/en.2002-220824; RA Morand S., Dos Santos O.F., Ohayon R., Kaniewski J., Noel-Hudson M.-S., RA Virion A., Dupuy C.; RT "Identification of a truncated dual oxidase 2 (DUOX2) messenger ribonucleic RT acid (mRNA) in two rat thyroid cell lines. Insulin and forskolin regulation RT of DUOX2 mRNA levels in FRTL-5 cells and porcine thyrocytes."; RL Endocrinology 144:567-574(2003). RN [2] RP TISSUE SPECIFICITY. RX PubMed=10806195; DOI=10.1074/jbc.m000916200; RA De Deken X., Wang D., Many M.-C., Costagliola S., Libert F., Vassart G., RA Dumont J.E., Miot F.; RT "Cloning of two human thyroid cDNAs encoding new members of the NADPH RT oxidase family."; RL J. Biol. Chem. 275:23227-23233(2000). RN [3] RP FUNCTION. RX PubMed=17643428; DOI=10.1016/j.yexcr.2007.06.011; RA Rigutto S., Hoste C., Dumont J.E., Corvilain B., Miot F., De Deken X.; RT "Duox1 is the main source of hydrogen peroxide in the rat thyroid cell line RT PCCl3."; RL Exp. Cell Res. 313:3892-3901(2007). CC -!- FUNCTION: Generates hydrogen peroxide (H2O2) which is required for the CC activity of thyroid peroxidase/TPO and lactoperoxidase/LPO CC (PubMed:17643428). Plays a role in thyroid hormone synthesis (By CC similarity). Also required for lactoperoxidase-mediated antimicrobial CC defense at the surface of mucosa (By similarity). Antimicrobial agent CC hypothiocyanite (OSCN-), which is produced by LPO from DUOX1-derived CC H2O2, promotes influenza virus inactivation by reducing viral binding CC to and entry into host cells (By similarity). Promotes antiviral CC immunity by increasing airway cytokine levels, promoting innate immune CC cell recruitment and reducing airway epithelial cell apoptosis (By CC similarity). In response to bacterial stimuli, activated by ATP and CC promotes EGFR/ERK signaling, ADAM17 activation, and EGFR ligand CC shedding, leading to enhanced CXCL8/IL8 expression and secretion in CC airway epithelia (By similarity). Synthesizes NAADP from its reduced CC NAADPH form which promotes Ca(2+) signaling during T cell activation CC (By similarity). In addition to its oxidase activity, has also been CC shown to have peroxidase activity through its N-terminal peroxidase- CC like domain (By similarity). However, another study showed that the CC isolated peroxidase-like domain does not bind heme and has no intrinsic CC peroxidase activity (By similarity). {ECO:0000250|UniProtKB:A2AQ92, CC ECO:0000250|UniProtKB:Q9NRD9, ECO:0000269|PubMed:17643428}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADH + O2 + H(+) = H2O2 + NAD(+); Xref=Rhea:RHEA:11264, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1; CC Evidence={ECO:0000250|UniProtKB:Q9NRD9}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NADPH + O2 + H(+) = H2O2 + NADP(+); Xref=Rhea:RHEA:11260, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1; CC Evidence={ECO:0000250|UniProtKB:Q9NRD9}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAADPH + O2 + H(+) = NAADP(+) + H2O2; Xref=Rhea:RHEA:86235, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:75967, ChEBI:CHEBI:235461; CC Evidence={ECO:0000250|UniProtKB:Q9NRD9}; CC -!- ACTIVITY REGULATION: The NADPH oxidase activity is calcium-dependent. CC It is activated by release of cellular ATP which is promoted by CC bacterial infection. Peroxidase activity is inhibited by CC aminobenzohydrazide. {ECO:0000250|UniProtKB:Q9NRD9}. CC -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. CC -!- SUBUNIT: Heterotetramer with DUOXA1 consisting of 2 DUOX1-DUOXA1 CC heterodimers (By similarity). This may represent the inactive state. CC Has also been detected as a heterodimer with DUOXA1 which has been CC proposed to be the active state (By similarity). Interacts with CC TXNDC11, TPO and CYBA (By similarity). {ECO:0000250|UniProtKB:A2AQ92, CC ECO:0000250|UniProtKB:Q9NRD9}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000250|UniProtKB:Q9NRD9}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q9NRD9}. Note=Localizes to the apical membrane CC of epithelial cells. {ECO:0000250|UniProtKB:Q9NRD9}. CC -!- TISSUE SPECIFICITY: Expressed in thyrocytes (at protein level). CC {ECO:0000269|PubMed:10806195}. CC -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase CC family. {ECO:0000305}. CC -!- CAUTION: The role of the N-terminal peroxidase-like domain is unclear. CC The domain has been shown in one study to have peroxidase activity when CC expressed in E.coli. However, another study showed that the isolated CC domain does not bind heme and has no intrinsic peroxidase activity. CC {ECO:0000250|UniProtKB:Q9NRD9}. 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; AF542180; AAN33120.1; -; mRNA. DR RefSeq; NP_714961.2; NM_153739.3. DR AlphaFoldDB; Q8CIY2; -. DR SMR; Q8CIY2; -. DR FunCoup; Q8CIY2; 4. DR STRING; 10116.ENSRNOP00000045928; -. DR PeroxiBase; 3970; RnoDuOx01. DR GlyCosmos; Q8CIY2; 5 sites, No reported glycans. DR GlyGen; Q8CIY2; 5 sites. DR PhosphoSitePlus; Q8CIY2; -. DR PaxDb; 10116-ENSRNOP00000045928; -. DR GeneID; 266807; -. DR KEGG; rno:266807; -. DR UCSC; RGD:628760; rat. DR AGR; RGD:628760; -. DR CTD; 53905; -. DR RGD; 628760; Duox1. DR eggNOG; KOG0039; Eukaryota. DR InParanoid; Q8CIY2; -. DR PhylomeDB; Q8CIY2; -. DR Reactome; R-RNO-209968; Thyroxine biosynthesis. DR UniPathway; UPA00194; -. DR PRO; PR:Q8CIY2; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0031252; C:cell leading edge; ISO:RGD. DR GO; GO:0009986; C:cell surface; ISO:RGD. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0043020; C:NADPH oxidase complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISO:RGD. DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; ISS:UniProtKB. DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central. DR GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB. DR GO; GO:0042335; P:cuticle development; ISS:UniProtKB. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB. DR GO; GO:0006952; P:defense response; IBA:GO_Central. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:UniProtKB. DR GO; GO:2000147; P:positive regulation of cell motility; ISO:RGD. DR GO; GO:1900426; P:positive regulation of defense response to bacterium; ISS:UniProtKB. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB. DR GO; GO:0090303; P:positive regulation of wound healing; ISO:RGD. DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD. DR GO; GO:0051591; P:response to cAMP; ISS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central. DR GO; GO:0006590; P:thyroid hormone generation; IEA:UniProtKB-UniPathway. DR CDD; cd09820; dual_peroxidase_like; 1. DR CDD; cd00051; EFh; 2. DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1. DR FunFam; 2.40.30.10:FF:000043; dual oxidase 1; 1. DR FunFam; 1.10.640.10:FF:000004; Dual oxidase 2; 1. DR FunFam; 3.40.50.80:FF:000006; Dual oxidase 2; 1. DR FunFam; 1.10.238.10:FF:000095; dual oxidase 2; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 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; IPR034821; DUOX_peroxidase. 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; IPR019791; Haem_peroxidase_animal. DR InterPro; IPR010255; Haem_peroxidase_sf. DR InterPro; IPR037120; Haem_peroxidase_sf_animal. DR InterPro; IPR060053; PH_DUOX. DR InterPro; IPR050369; RBOH/FRE. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR11972:SF75; DUAL OXIDASE 1; 1. DR PANTHER; PTHR11972; NADPH OXIDASE; 1. DR Pfam; PF03098; An_peroxidase; 1. DR Pfam; PF00036; EF-hand_1; 1. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF08022; FAD_binding_8; 1. DR Pfam; PF01794; Ferric_reduct; 1. DR Pfam; PF08030; NAD_binding_6; 1. DR Pfam; PF26659; PH_DUOX; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1. DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1. DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1. DR SMART; SM00054; EFh; 2. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 3. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50292; PEROXIDASE_3; 1. PE 1: Evidence at protein level; KW Calcium; Cell membrane; Disulfide bond; FAD; Flavoprotein; Glycoprotein; KW Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding; NADP; KW Oxidoreductase; Peroxidase; Reference proteome; Repeat; Signal; KW Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..1551 FT /note="Dual oxidase 1" FT /id="PRO_0000223346" FT TOPO_DOM 22..591 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TRANSMEM 592..616 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TOPO_DOM 617..1043 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TRANSMEM 1044..1066 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TOPO_DOM 1067..1080 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TRANSMEM 1081..1105 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TOPO_DOM 1106..1127 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TRANSMEM 1128..1152 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TOPO_DOM 1153..1184 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TRANSMEM 1185..1210 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TOPO_DOM 1211..1222 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TRANSMEM 1223..1241 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TOPO_DOM 1242..1248 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TRANSMEM 1249..1262 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT TOPO_DOM 1263..1551 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT DOMAIN 815..850 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 851..886 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 895..930 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 1096..1236 FT /note="Ferric oxidoreductase" FT /evidence="ECO:0000255" FT DOMAIN 1270..1376 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT REGION 26..593 FT /note="Peroxidase-like" FT REGION 956..1248 FT /note="Interaction with TXNDC11" FT /evidence="ECO:0000250|UniProtKB:Q9MZF4" FT BINDING 109 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:A2AQ92" FT BINDING 170 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:A2AQ92" FT BINDING 172 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:A2AQ92" FT BINDING 174 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:A2AQ92" FT BINDING 176 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:A2AQ92" FT BINDING 828 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 830 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 832 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 834 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 839 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 864 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 866 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 868 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 870 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 875 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 1106 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1128 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1130 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1144 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1214 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1225 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1238 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1242 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1243 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1244 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1245 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1248 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1249 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1260 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:A2AQ92" FT BINDING 1264 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1320 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1322 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1335 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1337 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1342 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1343 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1390 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1391 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:A2AQ92" FT BINDING 1423 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:A2AQ92" FT BINDING 1424 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1455 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1495 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1520 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1524 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:A2AQ92" FT BINDING 1528 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1549 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT BINDING 1550 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT CARBOHYD 94 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 342 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 354 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 461 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 534 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 118..1165 FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT DISULFID 345..565 FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" FT DISULFID 364..579 FT /evidence="ECO:0000250|UniProtKB:Q9NRD9" SQ SEQUENCE 1551 AA; 177197 MW; 52B07F83EF4E1FE2 CRC64; MAVYSAVAWI LLFGVLASLG AQNPVSWEVQ RFDGWYNNLM EHRWGSKGSR LQRLVPASYA DGVYQPLREP YLPNPRHLSN RVMRGPAGQP SLRNRTVLGV FFGYHVLSDL VSVETPGCPA EFLNIYIPRG DPVFDPDKRG NVVLPFQRSR WDRSTGQSPS NPRDLTNQVT GWLDGSAIYG SSHSWSDTLR SFSGGQLASG PDPAFPRNSQ NSLLMWMAPD PATGQGGPQG LYAFGAQRGN REPFLQALGL LWFRYHNLCA KRLAQEHPHW GDEELFQHAR KRVIATYQNI AMYEWLPSFL KQTPPEYPGY HPFLDPSISP EFVVASEQFL STMVPPGVYM RNASCHFQGI ANRNSSVSGA LRVCNSYWSR ENPKLQRAED VDALLLGMAS QIAEREDHLV VEDVQDFWPG PLKFSRTDYL ASCLQRGRDL GLPSYTKARE ALGLPPVSHW QDINPALSRS NGTVLEATAA LYNQDLSRLE LLAGGLLESH GDPGPLFSAI VLDQFVRLRD GDRYWFENNR NGLFSKEEIA EIRNTSLRDI LVAVTNVDPS ALQPSVFFWL AGDPCPQPSQ LSTQGLPACA PLFVRDYFKG SGFGFGLTIG TLCCFPLVSL LSAWIVARLR MRNFKRLQRQ DRQSIMCEKL VGGVEALEWQ GRKEPCRPVL VHLQPGQIRV VDGRLTVLRT IQLRPPQQVN LILSSNRGRR TLLLKIPKEY DLVLLFNMEE ERQALVENIR AALKENGLSF QEWELREQEL MRAAVTRQQR GHLLETFFRH LFSQVLDINQ ADAGTLPLDS STKVREALTC ELSRAEFADS LGLKPQDMFV ESMFSLADKD GNGYLSFREF LDILVVFMKG SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKDQLAEVV ESMFRESGFQ DKEELTWEDF HFMLRDHDSD LRFTQLCVKG VEVPEVIKNL CRRASYISQE KICPSPRMSA HCARNNTKTA SSPQRLQCPV DTDPPQEIRR RFGKKVTSFQ PLLFTEAHRE KFQRSRRHQT VQQFKRFIEN YRRHIGCVAV FYTITGALFL ERAYYYAFAA HHSGITDTTR VGIILSRGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY IPFDAAVDFH RFIASTAIIL TVLHSAGHVV NVYLFSISPL SVLSCLFPDL FHDDGSEFPQ KYYWWFFQTV PGLTGVLLLL ALAIMYVFAS HHFRRRSFRG FWLTHHLYIF LYILLIIHGS FALIQMPRFH IFFLVPAIIY VGDKLVSLSR KKVEISVVKA ELLPSGVTHL RFQRPQGFEY KSGQWVRIAC LALGTTEYHP FTLTSAPHED TLSLHIRAAG PWTTRLREIY SPPTGDTCAR YPKLYLDGPF GEGHQEWHKF EVSVLVGAGI GVTPFASILK DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE ENDSRDLVSV HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSV THFGRPPFEP FFNSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINKQD RTHFSHHYEN F //