NDOR1_MOUSE
ID NDOR1_MOUSE Reviewed; 598 AA.
AC A2AI05; Q3TQZ6; Q80WC5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 115.
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};
DE AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase {ECO:0000255|HAMAP-Rule:MF_03178};
GN Name=Ndor1 {ECO:0000255|HAMAP-Rule:MF_03178};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
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).
CC -!- FUNCTION: NADPH-dependent reductase which is a central component of the
CC cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
CC Transfers electrons from NADPH via its FAD and FMN prosthetic groups to
CC the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA
CC machinery. In turn, this reduced cluster provides electrons for
CC assembly of cytosolic iron-sulfur cluster proteins. It can also reduce
CC the [2Fe-2S] cluster of CISD1 and activate this protein implicated in
CC Fe/S cluster repair (By similarity). In vitro can fully activate
CC methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A
CC (By similarity). {ECO:0000250|UniProtKB:Q9UHB4, ECO:0000255|HAMAP-
CC Rule:MF_03178}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67717;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03178};
CC -!- SUBUNIT: Interacts with CIAPIN1; as part of the cytosolic iron-sulfur
CC (Fe-S) protein assembly (CIA) machinery (By similarity). Interacts with
CC DCPS (By similarity). {ECO:0000250|UniProtKB:Q9UHB4, ECO:0000255|HAMAP-
CC Rule:MF_03178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000255|HAMAP-
CC Rule:MF_03178}. Note=Concentrated in perinuclear structure.
CC {ECO:0000255|HAMAP-Rule:MF_03178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2AI05-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AI05-2; Sequence=VSP_031489;
CC Name=3;
CC IsoId=A2AI05-3; Sequence=VSP_031488, VSP_031490, VSP_031491;
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; AK163207; BAE37235.1; -; mRNA.
DR EMBL; AK169885; BAE41435.1; -; mRNA.
DR EMBL; AL732309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049789; AAH49789.1; -; mRNA.
DR CCDS; CCDS38069.1; -. [A2AI05-1]
DR CCDS; CCDS57157.1; -. [A2AI05-2]
DR RefSeq; NP_001075945.1; NM_001082476.2. [A2AI05-1]
DR RefSeq; NP_001239470.1; NM_001252541.1. [A2AI05-2]
DR AlphaFoldDB; A2AI05; -.
DR SMR; A2AI05; -.
DR BioGRID; 219640; 6.
DR STRING; 10090.ENSMUSP00000109989; -.
DR iPTMnet; A2AI05; -.
DR PhosphoSitePlus; A2AI05; -.
DR EPD; A2AI05; -.
DR MaxQB; A2AI05; -.
DR PaxDb; A2AI05; -.
DR PeptideAtlas; A2AI05; -.
DR PRIDE; A2AI05; -.
DR ProteomicsDB; 253038; -. [A2AI05-1]
DR ProteomicsDB; 253039; -. [A2AI05-2]
DR ProteomicsDB; 253040; -. [A2AI05-3]
DR DNASU; 78797; -.
DR Ensembl; ENSMUST00000100329; ENSMUSP00000097903; ENSMUSG00000006471. [A2AI05-2]
DR Ensembl; ENSMUST00000114349; ENSMUSP00000109989; ENSMUSG00000006471. [A2AI05-1]
DR GeneID; 78797; -.
DR KEGG; mmu:78797; -.
DR UCSC; uc008iqw.2; mouse. [A2AI05-1]
DR UCSC; uc012brw.2; mouse. [A2AI05-2]
DR CTD; 27158; -.
DR MGI; MGI:1926047; Ndor1.
DR VEuPathDB; HostDB:ENSMUSG00000006471; -.
DR eggNOG; KOG1159; Eukaryota.
DR GeneTree; ENSGT00930000151050; -.
DR HOGENOM; CLU_001570_17_6_1; -.
DR InParanoid; A2AI05; -.
DR OMA; QLFEMMP; -.
DR OrthoDB; 318396at2759; -.
DR PhylomeDB; A2AI05; -.
DR TreeFam; TF105716; -.
DR BioGRID-ORCS; 78797; 23 hits in 73 CRISPR screens.
DR PRO; PR:A2AI05; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AI05; protein.
DR Bgee; ENSMUSG00000006471; Expressed in retinal neural layer and 161 other tissues.
DR ExpressionAtlas; A2AI05; baseline and differential.
DR Genevisible; A2AI05; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISO:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; ISO:MGI.
DR GO; GO:0050661; F:NADP binding; ISO:MGI.
DR GO; GO:0070402; F:NADPH binding; ISO:MGI.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; ISS:UniProtKB.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0036245; P:cellular response to menadione; ISS:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; ISO:MGI.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; FAD; Flavoprotein; FMN; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..598
FT /note="NADPH-dependent diflavin oxidoreductase 1"
FT /id="PRO_0000319540"
FT DOMAIN 6..150
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT DOMAIN 206..448
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 12..17
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 59..62
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 97..106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 132
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
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 461
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 516..517
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 522..526
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 559
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT BINDING 597
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03178"
FT VAR_SEQ 1..45
FT /note="MQVPQLLVLFGSQTGTAQDEAERLGREARRRRLGCRVQALDSYSV -> MRC
FT REGTDQGCQRPYIYLCLVLE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031488"
FT VAR_SEQ 104..171
FT /note="KFNFVAKKLHRRLLQLGGSALLPPCLGDDQHELGPDAAIDPWVGDLWEKIMV
FT MYPVPLDIPEIPHGVP -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031489"
FT VAR_SEQ 481..488
FT /note="NFLFFGCR -> EYWSSKAV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031490"
FT VAR_SEQ 489..598
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031491"
SQ SEQUENCE 598 AA; 67183 MW; 7B621663EEE85FED CRC64;
MQVPQLLVLF GSQTGTAQDE AERLGREARR RRLGCRVQAL DSYSVANLIR EPLVIFVCAT
TGQGDPPDNM KNFWRFIFRK SLPSSSLCQM DFAVLGLGDS SYAKFNFVAK KLHRRLLQLG
GSALLPPCLG DDQHELGPDA AIDPWVGDLW EKIMVMYPVP LDIPEIPHGV PLPSKFIFQF
LQEVPSIGAE ELNIASSAPQ TPPSELQPFL APVITNQRVT GPQHFQDVRL IEFDITDSNI
SFAAGDVVFI LPSNSEAHTQ QFCQVLCLDP NQFFTLKPRE PGVPDPPGLP QPCTVWNLVS
QYLDIASVPR RSFFELLACL SQHALEREKL LELSSARGQE ELWEYCSRPR RTILEVLCDF
PHTAGAIPPD YLLDLIPRIR PRAFSIASSL LAHPRRLQIL VAVVKYQTRL KEPRHGLCSS
WLASLNPGQA GPVRVPLWVR PGSLVFPKTP DTPIIMVGAG TGVAPFRAAI QERVAHGQTG
NFLFFGCRQR DQDFYWQTEW QKLEQKGWLT LVTAFSREQE QKVYVQHRLR ELGPLVWELL
DGQGAYFYLA GNAKYLPTDV SEALMSIFQE EGRLSTADAS AYLARLQQTL RFQTETWA
