ADRO_MOUSE
ID ADRO_MOUSE Reviewed; 494 AA.
AC Q61578;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=NADPH:adrenodoxin oxidoreductase, mitochondrial;
DE Short=AR;
DE Short=Adrenodoxin reductase;
DE EC=1.18.1.6 {ECO:0000250|UniProtKB:P08165};
DE AltName: Full=Ferredoxin--NADP(+) reductase;
DE Short=Ferredoxin reductase;
DE Flags: Precursor;
GN Name=Fdxr;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=7495857; DOI=10.1016/0167-4781(95)00172-d;
RA Itoh S., Iemura O., Yamada E., Yoshimura T., Tsujikawa K., Kohama Y.,
RA Mimura T.;
RT "cDNA cloning of mouse ferredoxin reductase from kidney.";
RL Biochim. Biophys. Acta 1264:159-162(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Serves as the first electron transfer protein in all the
CC mitochondrial P450 systems including cholesterol side chain cleavage in
CC all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal
CC cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-
CC 27 hydroxylation in the liver. {ECO:0000250|UniProtKB:P08165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized
CC [adrenodoxin]; Xref=Rhea:RHEA:42312, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC COMP:9999, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.6;
CC Evidence={ECO:0000250|UniProtKB:P08165};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P08165};
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC -!- SUBUNIT: Monomer. Interacts directly with FDX1.
CC {ECO:0000250|UniProtKB:P08165}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the adrenal, testis and ovary and to a
CC lesser extent in the liver and kidney. {ECO:0000269|PubMed:7495857}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; D49920; BAA08659.1; -; mRNA.
DR CCDS; CCDS25625.1; -.
DR PIR; S60028; S60028.
DR RefSeq; NP_032023.1; NM_007997.1.
DR AlphaFoldDB; Q61578; -.
DR SMR; Q61578; -.
DR BioGRID; 199627; 8.
DR STRING; 10090.ENSMUSP00000021078; -.
DR iPTMnet; Q61578; -.
DR PhosphoSitePlus; Q61578; -.
DR REPRODUCTION-2DPAGE; Q61578; -.
DR EPD; Q61578; -.
DR jPOST; Q61578; -.
DR MaxQB; Q61578; -.
DR PaxDb; Q61578; -.
DR PRIDE; Q61578; -.
DR ProteomicsDB; 296117; -.
DR DNASU; 14149; -.
DR Ensembl; ENSMUST00000021078; ENSMUSP00000021078; ENSMUSG00000018861.
DR GeneID; 14149; -.
DR KEGG; mmu:14149; -.
DR UCSC; uc007mgy.1; mouse.
DR CTD; 2232; -.
DR MGI; MGI:104724; Fdxr.
DR VEuPathDB; HostDB:ENSMUSG00000018861; -.
DR eggNOG; KOG1800; Eukaryota.
DR GeneTree; ENSGT00940000165377; -.
DR HOGENOM; CLU_024722_3_1_1; -.
DR InParanoid; Q61578; -.
DR OMA; RFNFIGN; -.
DR OrthoDB; 1324510at2759; -.
DR PhylomeDB; Q61578; -.
DR TreeFam; TF314193; -.
DR Reactome; R-MMU-196108; Pregnenolone biosynthesis.
DR Reactome; R-MMU-211976; Endogenous sterols.
DR Reactome; R-MMU-2395516; Electron transport from NADPH to Ferredoxin.
DR UniPathway; UPA00296; -.
DR BioGRID-ORCS; 14149; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Fdxr; mouse.
DR PRO; PR:Q61578; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61578; protein.
DR Bgee; ENSMUSG00000018861; Expressed in adrenal gland and 150 other tissues.
DR Genevisible; Q61578; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0070402; F:NADPH binding; ISO:MGI.
DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0070995; P:NADPH oxidation; ISO:MGI.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000362; FNR; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Electron transport; FAD; Flavoprotein;
KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NADP; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Steroid metabolism; Sterol metabolism; Transit peptide; Transport.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT CHAIN 35..494
FT /note="NADPH:adrenodoxin oxidoreductase, mitochondrial"
FT /id="PRO_0000019421"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 72
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 187..190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 231..232
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 243
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 401
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 408..410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 408
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22570"
SQ SEQUENCE 494 AA; 54202 MW; 4BD279DFC606A5C5 CRC64;
MAPRCWHWWR WSAWSGLRPS PSRSTPTPGF CQKFSTQEKT PQICVVGSGP AGFYTAQHLL
KHHTHAHVDI YEKQLVPFGL VRFGVAPDHP EVKNVINTFT QTARSDRCAF QGNVVVGRDV
SVPELREAYH AVVLSYGAED HQPLGIPGEE LPGVVSARAF VGWYNGLPEN QELAPDLSCD
TAVILGQGNV ALDVARILLT PPEHLEKTDI TEAALGALRQ SRVKTVWIVG RRGPLQVAFT
IKELREMIQL PGTRPILDPS DFLGLQDRIK DVPRPRRRLT ELLLRTATEK PGVEEAARQA
LASRAWGLRF FRSPQQVLPT PDGQRVAGIR LAVTSLEGVG ESTRAVPTGD VEDLPCGLLL
SSVGYKSRPI DPSVPFDPKL GVIPNTEGRV VNVPGLYCSG WVKRGPTGVI TTTMTDSFLT
SQALLEDLKA GLLPSGPRPG YVAIQALLSN RGVRPVSFSD WEKLDAEEVS RGQGTGKPRE
KLVDRREMLR LLGH
