NCPR_MOUSE
ID NCPR_MOUSE Reviewed; 678 AA.
AC P37040;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212};
DE Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212};
DE Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212};
DE EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212};
GN Name=Por {ECO:0000255|HAMAP-Rule:MF_03212};
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].
RC STRAIN=ddY;
RX PubMed=8011664; DOI=10.1016/0005-2728(94)90146-5;
RA Ohgiya S., Ishizaki K., Kamataki T., Shinriki N.;
RT "Mouse NADPH-cytochrome P-450 oxidoreductase: molecular cloning and
RT functional expression in yeast.";
RL Biochim. Biophys. Acta 1186:137-141(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: This enzyme is required for electron transfer from NADP to
CC cytochrome P450 in microsomes. It can also provide electron transfer to
CC heme oxygenase and cytochrome B5. {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03212};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212};
CC Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212};
CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_03212}.
CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_03212}.
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; D17571; BAA04496.1; -; mRNA.
DR EMBL; BC031463; AAH31463.1; -; mRNA.
DR CCDS; CCDS39318.1; -.
DR RefSeq; NP_032924.1; NM_008898.2.
DR RefSeq; XP_006504461.1; XM_006504398.1.
DR RefSeq; XP_006504462.1; XM_006504399.1.
DR AlphaFoldDB; P37040; -.
DR SMR; P37040; -.
DR BioGRID; 202299; 8.
DR IntAct; P37040; 3.
DR MINT; P37040; -.
DR STRING; 10090.ENSMUSP00000005651; -.
DR ChEMBL; CHEMBL4105861; -.
DR iPTMnet; P37040; -.
DR PhosphoSitePlus; P37040; -.
DR SwissPalm; P37040; -.
DR SWISS-2DPAGE; P37040; -.
DR EPD; P37040; -.
DR jPOST; P37040; -.
DR MaxQB; P37040; -.
DR PaxDb; P37040; -.
DR PeptideAtlas; P37040; -.
DR PRIDE; P37040; -.
DR ProteomicsDB; 252930; -.
DR Antibodypedia; 2433; 454 antibodies from 35 providers.
DR DNASU; 18984; -.
DR Ensembl; ENSMUST00000005651; ENSMUSP00000005651; ENSMUSG00000005514.
DR GeneID; 18984; -.
DR KEGG; mmu:18984; -.
DR UCSC; uc008zyt.1; mouse.
DR CTD; 5447; -.
DR MGI; MGI:97744; Por.
DR VEuPathDB; HostDB:ENSMUSG00000005514; -.
DR eggNOG; KOG1158; Eukaryota.
DR GeneTree; ENSGT00940000156847; -.
DR HOGENOM; CLU_001570_17_3_1; -.
DR InParanoid; P37040; -.
DR OMA; QKRYQRD; -.
DR OrthoDB; 318396at2759; -.
DR PhylomeDB; P37040; -.
DR TreeFam; TF105719; -.
DR BioGRID-ORCS; 18984; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Por; mouse.
DR PRO; PR:P37040; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P37040; protein.
DR Bgee; ENSMUSG00000005514; Expressed in nasal cavity epithelium and 296 other tissues.
DR ExpressionAtlas; P37040; baseline and differential.
DR Genevisible; P37040; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; ISO:MGI.
DR GO; GO:0009055; F:electron transfer activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI.
DR GO; GO:0010181; F:FMN binding; ISO:MGI.
DR GO; GO:0016787; F:hydrolase activity; ISO:MGI.
DR GO; GO:0047726; F:iron-cytochrome-c reductase activity; ISO:MGI.
DR GO; GO:0050661; F:NADP binding; ISO:MGI.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; ISO:MGI.
DR GO; GO:0008941; F:nitric oxide dioxygenase activity; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IMP:MGI.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:Ensembl.
DR GO; GO:0090346; P:cellular organofluorine metabolic process; ISO:MGI.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
DR GO; GO:0070988; P:demethylation; ISO:MGI.
DR GO; GO:0022900; P:electron transport chain; ISO:MGI.
DR GO; GO:0019395; P:fatty acid oxidation; ISO:MGI.
DR GO; GO:0009812; P:flavonoid metabolic process; IEA:Ensembl.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0060192; P:negative regulation of lipase activity; ISO:MGI.
DR GO; GO:0043602; P:nitrate catabolic process; ISO:MGI.
DR GO; GO:0046210; P:nitric oxide catabolic process; ISO:MGI.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISO:MGI.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISO:MGI.
DR GO; GO:0032770; P:positive regulation of monooxygenase activity; ISO:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISO:MGI.
DR GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; ISO:MGI.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:MGI.
DR GO; GO:0003420; P:regulation of growth plate cartilage chondrocyte proliferation; ISO:MGI.
DR GO; GO:0071548; P:response to dexamethasone; ISO:MGI.
DR GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_03212; NCPR; 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; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR023208; P450R.
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 PIRSF; PIRSF000208; P450R; 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 Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P16435"
FT CHAIN 2..678
FT /note="NADPH--cytochrome P450 reductase"
FT /id="PRO_0000167597"
FT TOPO_DOM 2..22
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TOPO_DOM 44..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 80..224
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 279..521
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 86..91
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 138..141
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 173..182
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 208
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 298
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 424
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 454..457
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 472..474
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 478
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 488..491
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 535
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 596..597
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 602..606
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 639
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 677
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P16435"
SQ SEQUENCE 678 AA; 77044 MW; 060282A7A55483AF CRC64;
MGDSHEDTSA TVPEAVAEEV SLFSTTDIVL FSLIVGVLTY WFIFKKKKEE IPEFSKIQTT
APPVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA
DLSSLPEIDK SLVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLTGVKFAV FGLGNKTYEH
FNAMGKYVDQ RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEF FGVEATGEES
SIRQYELVVH EDMDTAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL
MHLELDISDS KIRYESGDHV AVYPANDSTL VNQIGEILGA DLDVIMSLNN LDEESNKKHP
FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE HLHKMASSSG EGKELYLSWV
VEARRHILAI LQDYPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVAVEYEA
KSGRVNKGVA TSWLRTKEPA GENGRRALVP MFVRKSQFRL PFKPTTPVIM VGPGTGVAPF
MGFIQERAWL REQGKEVGET LLYYGCRRSD EDYLYREELA RFHKDGALTQ LNVAFSREQA
HKVYVQHLLK RDKEHLWKLI HEGGAHIYVC GDARNMAKDV QNTFYDIVAE FGPMEHTQAV
DYVKKLMTKG RYSLDVWS
