ID NDOR1_HUMAN Reviewed; 597 AA. AC Q9UHB4; D3YTG6; D3YTH9; Q5VSG4; Q86US9; Q96BC6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 22-FEB-2023, entry version 170. DE RecName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0000255|HAMAP-Rule:MF_03178}; DE EC=1.18.1.- {ECO:0000255|HAMAP-Rule:MF_03178, ECO:0000269|PubMed:23596212, ECO:0000269|PubMed:28648056}; DE AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase {ECO:0000255|HAMAP-Rule:MF_03178}; DE AltName: Full=Novel reductase 1 {ECO:0000303|PubMed:10625700}; GN Name=NDOR1 {ECO:0000255|HAMAP-Rule:MF_03178}; GN Synonyms=NR1 {ECO:0000303|PubMed:10625700}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR, RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION. RX PubMed=10625700; DOI=10.1074/jbc.275.2.1471; RA Paine M.J., Garner A.P., Powell D., Sibbald J., Sales M., Pratt N., RA Smith T., Tew D.G., Wolf C.R.; RT "Cloning and characterization of a novel human dual flavin reductase."; RL J. Biol. Chem. 275:1471-1478(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=12871939; DOI=10.1074/jbc.m306355200; RA Kwasnicka D.A., Krakowiak A., Thacker C., Brenner C., Vincent S.R.; RT "Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and RT Hint-related 7meGMP-directed hydrolase, DCS-1."; RL J. Biol. Chem. 278:39051-39058(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Hippocampus, and Umbilical vein endothelial cell; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-522. RC TISSUE=Brain, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 1-8, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12871938; DOI=10.1074/jbc.m306282200; RA Olteanu H., Banerjee R.; RT "Redundancy in the pathway for redox regulation of mammalian methionine RT synthase: reductive activation by the dual flavoprotein, novel reductase RT 1."; RL J. Biol. Chem. 278:38310-38314(2003). RN [7] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12631275; DOI=10.1046/j.1432-1033.2003.03474.x; RA Finn R.D., Basran J., Roitel O., Wolf C.R., Munro A.W., Paine M.J., RA Scrutton N.S.; RT "Determination of the redox potentials and electron transfer properties of RT the FAD- and FMN-binding domains of the human oxidoreductase NR1."; RL Eur. J. Biochem. 270:1164-1175(2003). RN [8] RP INTERACTION WITH DCPS, AND CYTOTOXICITY. RX PubMed=16140270; DOI=10.1016/j.bbrc.2005.08.129; RA Kwasnicka-Crawford D.A., Vincent S.R.; RT "Role of a novel dual flavin reductase (NR1) and an associated histidine RT triad protein (DCS-1) in menadione-induced cytotoxicity."; RL Biochem. Biophys. Res. Commun. 336:565-571(2005). RN [9] RP FUNCTION, AND INTERACTION WITH CIAPIN1. RX PubMed=20802492; DOI=10.1038/nchembio.432; RA Netz D.J., Stumpfig M., Dore C., Muhlenhoff U., Pierik A.J., Lill R.; RT "Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein RT biogenesis."; RL Nat. Chem. Biol. 6:758-765(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=28648056; DOI=10.1021/jacs.7b05003; RA Camponeschi F., Ciofi-Baffoni S., Banci L.; RT "Anamorsin/Ndor1 Complex Reduces [2Fe-2S]-MitoNEET via a Transient Protein- RT Protein Interaction."; RL J. Am. Chem. Soc. 139:9479-9482(2017). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-161 IN COMPLEX WITH FMN, RP FUNCTION, COFACTOR, INTERACTION WITH CIAPIN1, AND CATALYTIC ACTIVITY. RX PubMed=23596212; DOI=10.1073/pnas.1302378110; RA Banci L., Bertini I., Calderone V., Ciofi-Baffoni S., Giachetti A., RA Jaiswal D., Mikolajczyk M., Piccioli M., Winkelmann J.; RT "Molecular view of an electron transfer process essential for iron-sulfur RT protein biogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 110:7136-7141(2013). RN [13] RP VARIANT ILE-522, CHARACTERIZATION OF VARIANT ILE-522, FUNCTION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15900210; DOI=10.1097/01213011-200506000-00002; RA Finn R.D., Wilkie M., Smith G., Paine M.J.; RT "Identification of a functionally impaired allele of human novel RT oxidoreductase 1 (NDOR1), NDOR1*1."; RL Pharmacogenet. Genomics 15:381-386(2005). CC -!- FUNCTION: NADPH-dependent reductase which is a central component of the CC cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery CC (PubMed:10625700, PubMed:28648056, PubMed:23596212, PubMed:20802492, CC PubMed:15900210). Transfers electrons from NADPH via its FAD and FMN CC prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key CC component of the CIA machinery (PubMed:28648056, PubMed:23596212, CC PubMed:20802492). In turn, this reduced cluster provides electrons for CC assembly of cytosolic iron-sulfur cluster proteins (PubMed:23596212, CC PubMed:20802492). It can also reduce the [2Fe-2S] cluster of CISD1 and CC activate this protein implicated in Fe/S cluster repair CC (PubMed:28648056). In vitro can fully activate methionine synthase/MTR CC in the presence of soluble cytochrome b5/CYB5A (PubMed:12871938). CC {ECO:0000255|HAMAP-Rule:MF_03178, ECO:0000269|PubMed:10625700, CC ECO:0000269|PubMed:12871938, ECO:0000269|PubMed:15900210, CC ECO:0000269|PubMed:20802492, ECO:0000269|PubMed:23596212, CC ECO:0000269|PubMed:28648056}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2 CC reduced [2Fe-2S]-[protein]; Xref=Rhea:RHEA:67716, Rhea:RHEA- CC COMP:17327, Rhea:RHEA-COMP:17328, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; Evidence={ECO:0000255|HAMAP-Rule:MF_03178, CC ECO:0000269|PubMed:23596212, ECO:0000269|PubMed:28648056}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67717; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178, CC ECO:0000305|PubMed:23596212}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178, CC ECO:0000269|PubMed:10625700}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178, CC ECO:0000269|PubMed:10625700, ECO:0000269|PubMed:23596212}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=21 uM for cytochrome c {ECO:0000269|PubMed:10625700}; CC KM=1.08 uM for NADPH {ECO:0000269|PubMed:12631275, CC ECO:0000269|PubMed:15900210, ECO:0000269|PubMed:23596212}; CC Vmax=1.2 umol/min/ug enzyme for cytochrome c reduction CC {ECO:0000269|PubMed:10625700}; CC Vmax=1.98 umol/min/ug enzyme for cytochrome c reduction CC {ECO:0000269|PubMed:12871938}; CC Vmax=2.8 umol/min/ug enzyme for methionine synthase reductive CC activation {ECO:0000269|PubMed:12871938}; CC pH dependence: CC Optimum pH is about 8.0. {ECO:0000305|PubMed:10625700}; CC Redox potential: CC E(0) is -315 +/- 5 mV for the FAD oxidized/semiquinone couple, E(0) CC is -365 +/- 15 mV for the FAD semiquinone/dihydroquinone couple, E(0) CC is -146 +/- 5 mV for the FMN oxidized/semiquinone couple, and E(0) is CC -305 +/- 5 mV for the FMN semiquinone/dihydroquinone couple. CC {ECO:0000269|PubMed:12631275}; CC -!- SUBUNIT: Interacts with CIAPIN1; as part of the cytosolic iron-sulfur CC (Fe-S) protein assembly (CIA) machinery (By similarity) CC (PubMed:20802492, PubMed:23596212). Interacts with DCPS CC (PubMed:16140270). {ECO:0000255|HAMAP-Rule:MF_03178, CC ECO:0000269|PubMed:16140270, ECO:0000269|PubMed:20802492, CC ECO:0000269|PubMed:23596212}. CC -!- INTERACTION: CC Q9UHB4; Q86UT8: CENATAC; NbExp=3; IntAct=EBI-10249760, EBI-11028020; CC Q9UHB4; Q6FI81: CIAPIN1; NbExp=14; IntAct=EBI-10249760, EBI-750511; CC Q9UHB4; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-10249760, EBI-2349927; CC Q9UHB4; O95995: GAS8; NbExp=3; IntAct=EBI-10249760, EBI-1052570; CC Q9UHB4; Q13227: GPS2; NbExp=5; IntAct=EBI-10249760, EBI-713355; CC Q9UHB4; P14652: HOXB2; NbExp=3; IntAct=EBI-10249760, EBI-5329558; CC Q9UHB4; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-10249760, EBI-739493; CC Q9UHB4; P25791-3: LMO2; NbExp=3; IntAct=EBI-10249760, EBI-11959475; CC Q9UHB4; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-10249760, EBI-11742507; CC Q9UHB4; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10249760, EBI-739832; CC Q9UHB4; P50221: MEOX1; NbExp=3; IntAct=EBI-10249760, EBI-2864512; CC Q9UHB4; Q5JR59: MTUS2; NbExp=4; IntAct=EBI-10249760, EBI-742948; CC Q9UHB4; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-10249760, EBI-11522433; CC Q9UHB4; Q15742: NAB2; NbExp=3; IntAct=EBI-10249760, EBI-8641936; CC Q9UHB4; Q9UBE8: NLK; NbExp=3; IntAct=EBI-10249760, EBI-366978; CC Q9UHB4; P28072: PSMB6; NbExp=3; IntAct=EBI-10249760, EBI-359288; CC Q9UHB4; P15884: TCF4; NbExp=4; IntAct=EBI-10249760, EBI-533224; CC Q9UHB4; P15884-3: TCF4; NbExp=3; IntAct=EBI-10249760, EBI-13636688; CC Q9UHB4; Q9BT92: TCHP; NbExp=7; IntAct=EBI-10249760, EBI-740781; CC Q9UHB4; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-10249760, EBI-11139477; CC Q9UHB4; Q08117-2: TLE5; NbExp=3; IntAct=EBI-10249760, EBI-11741437; CC Q9UHB4; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10249760, EBI-741480; CC Q9UHB4; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-10249760, EBI-947187; CC Q9UHB4; B2RXF5: ZBTB42; NbExp=5; IntAct=EBI-10249760, EBI-12287587; CC Q9UHB4; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-10249760, EBI-14104088; CC Q9UHB4; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-10249760, EBI-4395669; CC Q9UHB4; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-10249760, EBI-10251462; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000255|HAMAP- CC Rule:MF_03178, ECO:0000269|PubMed:10625700, CC ECO:0000269|PubMed:12871939}. Note=Concentrated in perinuclear CC structure. {ECO:0000255|HAMAP-Rule:MF_03178, CC ECO:0000269|PubMed:12871939}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9UHB4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UHB4-2; Sequence=VSP_031487; CC Name=3; CC IsoId=Q9UHB4-3; Sequence=VSP_046313, VSP_046314; CC Name=4; CC IsoId=Q9UHB4-4; Sequence=VSP_053807; CC -!- TISSUE SPECIFICITY: Low expression in brain, heart, kidney, pancreas, CC prostate and skeletal muscle. Highest levels in the placenta. Expressed CC in cancer cell lines including promyelocytic leukemia, HeLaS3, chronic CC myelagenous leukemia, lymphoblastic leukemia, Burkitt's lymphoma, CC colorectal adenocarcinoma, lung carcinoma, and melanoma G-361. CC {ECO:0000269|PubMed:12871939}. CC -!- SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase CC NDOR1 family. {ECO:0000255|HAMAP-Rule:MF_03178}. CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin CC family. {ECO:0000255|HAMAP-Rule:MF_03178}. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP- CC Rule:MF_03178}. 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; AF199509; AAF25205.1; -; mRNA. DR EMBL; AY077845; AAL77754.1; -; mRNA. DR EMBL; AK074403; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK290026; BAF82715.1; -; mRNA. DR EMBL; AL929554; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX255925; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015735; AAH15735.1; -; mRNA. DR EMBL; BC093782; AAH93782.1; -; mRNA. DR EMBL; BC111943; AAI11944.1; -; mRNA. DR CCDS; CCDS48061.1; -. [Q9UHB4-2] DR CCDS; CCDS48062.1; -. [Q9UHB4-4] DR CCDS; CCDS48063.1; -. [Q9UHB4-3] DR CCDS; CCDS7036.1; -. [Q9UHB4-1] DR RefSeq; NP_001137498.1; NM_001144026.2. [Q9UHB4-2] DR RefSeq; NP_001137499.1; NM_001144027.2. [Q9UHB4-3] DR RefSeq; NP_001137500.1; NM_001144028.2. [Q9UHB4-4] DR RefSeq; NP_055249.1; NM_014434.3. [Q9UHB4-1] DR PDB; 4H2D; X-ray; 1.80 A; A/B=1-161. DR PDBsum; 4H2D; -. DR AlphaFoldDB; Q9UHB4; -. DR SMR; Q9UHB4; -. DR BioGRID; 118038; 51. DR IntAct; Q9UHB4; 28. DR STRING; 9606.ENSP00000360576; -. DR GlyCosmos; Q9UHB4; 2 sites, 1 glycan. DR GlyGen; Q9UHB4; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9UHB4; -. DR PhosphoSitePlus; Q9UHB4; -. DR BioMuta; NDOR1; -. DR DMDM; 74735011; -. DR EPD; Q9UHB4; -. DR jPOST; Q9UHB4; -. DR MassIVE; Q9UHB4; -. DR MaxQB; Q9UHB4; -. DR PaxDb; Q9UHB4; -. DR PeptideAtlas; Q9UHB4; -. DR ProteomicsDB; 12813; -. DR ProteomicsDB; 12819; -. DR ProteomicsDB; 84294; -. [Q9UHB4-1] DR ProteomicsDB; 84295; -. [Q9UHB4-2] DR Antibodypedia; 18959; 224 antibodies from 25 providers. DR DNASU; 27158; -. DR Ensembl; ENST00000371521.8; ENSP00000360576.4; ENSG00000188566.15. [Q9UHB4-2] DR Ensembl; ENST00000427047.6; ENSP00000394309.1; ENSG00000188566.15. [Q9UHB4-3] DR Ensembl; ENST00000458322.2; ENSP00000389905.1; ENSG00000188566.15. [Q9UHB4-4] DR Ensembl; ENST00000684003.1; ENSP00000507194.1; ENSG00000188566.15. [Q9UHB4-1] DR GeneID; 27158; -. DR KEGG; hsa:27158; -. DR MANE-Select; ENST00000684003.1; ENSP00000507194.1; NM_014434.4; NP_055249.1. DR UCSC; uc004clw.4; human. [Q9UHB4-1] DR AGR; HGNC:29838; -. DR CTD; 27158; -. DR DisGeNET; 27158; -. DR GeneCards; NDOR1; -. DR HGNC; HGNC:29838; NDOR1. DR HPA; ENSG00000188566; Low tissue specificity. DR MIM; 606073; gene. DR neXtProt; NX_Q9UHB4; -. DR OpenTargets; ENSG00000188566; -. DR PharmGKB; PA134885020; -. DR VEuPathDB; HostDB:ENSG00000188566; -. DR eggNOG; KOG1159; Eukaryota. DR GeneTree; ENSGT00930000151050; -. DR HOGENOM; CLU_001570_17_6_1; -. DR InParanoid; Q9UHB4; -. DR OMA; QLFEMMP; -. DR OrthoDB; 276396at2759; -. DR PhylomeDB; Q9UHB4; -. DR TreeFam; TF105716; -. DR BRENDA; 1.5.1.30; 2681. DR PathwayCommons; Q9UHB4; -. DR Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly. DR SignaLink; Q9UHB4; -. DR BioGRID-ORCS; 27158; 656 hits in 1148 CRISPR screens. DR ChiTaRS; NDOR1; human. DR GeneWiki; NDOR1; -. DR GenomeRNAi; 27158; -. DR Pharos; Q9UHB4; Tbio. DR PRO; PR:Q9UHB4; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9UHB4; protein. DR Bgee; ENSG00000188566; Expressed in granulocyte and 92 other tissues. DR Genevisible; Q9UHB4; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB. DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central. DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB. DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB. DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0016731; F:oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor; IDA:UniProtKB. DR GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IDA:UniProtKB. DR GO; GO:0008219; P:cell death; IDA:UniProtKB. DR GO; GO:0036245; P:cellular response to menadione; IDA:UniProtKB. DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB. DR GO; GO:0016226; P:iron-sulfur cluster assembly; TAS:ARUK-UCL. DR Gene3D; 3.40.50.360; -; 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 HAMAP; MF_03178; NDOR1; 1. DR InterPro; IPR003097; CysJ-like_FAD-binding. DR InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like_sf. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha. DR InterPro; IPR028879; NDOR1. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR19384:SF10; NADPH-DEPENDENT DIFLAVIN OXIDOREDUCTASE 1; 1. DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing; KW FAD; Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..597 FT /note="NADPH-dependent diflavin oxidoreductase 1" FT /id="PRO_0000319539" FT DOMAIN 6..150 FT /note="Flavodoxin-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178" FT DOMAIN 206..447 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178" FT REGION 188..207 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 12..17 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178, FT ECO:0000269|PubMed:23596212" FT BINDING 59..62 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178, FT ECO:0000269|PubMed:23596212" FT BINDING 97..106 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178, FT ECO:0000269|PubMed:23596212" FT BINDING 132 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178, FT ECO:0000269|PubMed:23596212" FT BINDING 350 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178" FT BINDING 382..385 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178" FT BINDING 416..419 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178" FT BINDING 460 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178" FT BINDING 515..516 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178" FT BINDING 521..525 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178" FT BINDING 558 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178" FT BINDING 596 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178" FT VAR_SEQ 138..171 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046313" FT VAR_SEQ 392..398 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_053807" FT VAR_SEQ 518 FT /note="Q -> QPPALFSALQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12871939" FT /id="VSP_031487" FT VAR_SEQ 543..597 FT /note="GAYFYLAGNAKSMPADVSEALMSIFQEEGGLCSPDAAAYLARLQQTRRFQTE FT TWA -> ATPSPCQRTSRKP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046314" FT VARIANT 522 FT /note="V -> I (in allele NDOR1*1; shows a decrease in FT affinity for NADPH and a reduction in ferricyanide FT reductase activity; dbSNP:rs62587579)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:15900210" FT /id="VAR_039010" FT STRAND 5..11 FT /evidence="ECO:0007829|PDB:4H2D" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:4H2D" FT HELIX 16..30 FT /evidence="ECO:0007829|PDB:4H2D" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:4H2D" FT TURN 40..42 FT /evidence="ECO:0007829|PDB:4H2D" FT HELIX 45..50 FT /evidence="ECO:0007829|PDB:4H2D" FT STRAND 52..59 FT /evidence="ECO:0007829|PDB:4H2D" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:4H2D" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:4H2D" FT HELIX 71..77 FT /evidence="ECO:0007829|PDB:4H2D" FT TURN 84..89 FT /evidence="ECO:0007829|PDB:4H2D" FT STRAND 91..98 FT /evidence="ECO:0007829|PDB:4H2D" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:4H2D" FT HELIX 107..118 FT /evidence="ECO:0007829|PDB:4H2D" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:4H2D" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:4H2D" FT TURN 135..138 FT /evidence="ECO:0007829|PDB:4H2D" FT HELIX 139..156 FT /evidence="ECO:0007829|PDB:4H2D" SQ SEQUENCE 597 AA; 66763 MW; 0D1340D7280A4D8F CRC64; MPSPQLLVLF GSQTGTAQDV SERLGREARR RRLGCRVQAL DSYPVVNLIN EPLVIFVCAT TGQGDPPDNM KNFWRFIFRK NLPSTALCQM DFAVLGLGDS SYAKFNFVAK KLHRRLLQLG GSALLPVCLG DDQHELGPDA AVDPWLRDLW DRVLGLYPPP PGLTEIPPGV PLPSKFTLLF LQEAPSTGSE GQRVAHPGSQ EPPSESKPFL APMISNQRVT GPSHFQDVRL IEFDILGSGI SFAAGDVVLI QPSNSAAHVQ RFCQVLGLDP DQLFMLQPRE PDVSSPTRLP QPCSMRHLVS HYLDIASVPR RSFFELLACL SLHELEREKL LEFSSAQGQE ELFEYCNRPR RTILEVLCDF PHTAAAIPPD YLLDLIPVIR PRAFSIASSL LTHPSRLQIL VAVVQFQTRL KEPRRGLCSS WLASLDPGQG PVRVPLWVRP GSLAFPETPD TPVIMVGPGT GVAPFRAAIQ ERVAQGQTGN FLFFGCRWRD QDFYWEAEWQ ELEKRDCLTL IPAFSREQEQ KVYVQHRLRE LGSLVWELLD RQGAYFYLAG NAKSMPADVS EALMSIFQEE GGLCSPDAAA YLARLQQTRR FQTETWA //