NDOR1_HUMAN
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 03-AUG-2022, entry version 167.
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}.
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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; 47.
DR IntAct; Q9UHB4; 28.
DR STRING; 9606.ENSP00000360576; -.
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 PRIDE; Q9UHB4; -.
DR ProteomicsDB; 12813; -.
DR ProteomicsDB; 12819; -.
DR ProteomicsDB; 84294; -. [Q9UHB4-1]
DR ProteomicsDB; 84295; -. [Q9UHB4-2]
DR Antibodypedia; 18959; 224 antibodies from 26 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 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; 318396at2759; -.
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; 616 hits in 1060 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; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 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 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; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 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
