P37040 (NCPR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADPH--cytochrome P450 reductase
Short name=CPR
Short name=P450R
EC=1.6.2.4

Gene names

Name:

Por

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	678 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.
Catalytic activity	NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.
Cofactor	FAD. FMN.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Note: Anchored to the ER membrane by its N-terminal hydrophobic region.
Sequence similarities	In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Ligand	FAD FMN Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carnitine metabolic process Inferred from electronic annotation. Source: Compara cellular organofluorine metabolic process Inferred from electronic annotation. Source: Compara cellular response to follicle-stimulating hormone stimulus Inferred from electronic annotation. Source: Compara cellular response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara demethylation Inferred from electronic annotation. Source: Compara fatty acid oxidation Inferred from electronic annotation. Source: Compara flavonoid metabolic process Inferred from electronic annotation. Source: Compara internal peptidyl-lysine acetylation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of lipase activity Inferred from electronic annotation. Source: Compara nitrate catabolic process Inferred from electronic annotation. Source: Compara nitric oxide catabolic process Inferred from electronic annotation. Source: Compara positive regulation of cholesterol biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of chondrocyte differentiation Inferred from electronic annotation. Source: Compara positive regulation of monooxygenase activity Inferred from electronic annotation. Source: Compara positive regulation of smoothened signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of steroid hormone biosynthetic process Inferred from electronic annotation. Source: Compara regulation of growth plate cartilage chondrocyte proliferation Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	FMN binding Inferred from electronic annotation. Source: Compara NADP binding Inferred from electronic annotation. Source: Compara NADPH-hemoprotein reductase activity Inferred from Biological aspect of Ancestor. Source: RefGenome cytochrome-b5 reductase activity, acting on NAD(P)H Inferred from electronic annotation. Source: Compara electron carrier activity Inferred from electronic annotation. Source: Compara flavin adenine dinucleotide binding Inferred from electronic annotation. Source: Compara hydrolase activity Inferred from electronic annotation. Source: Compara iron ion binding Inferred from electronic annotation. Source: InterPro iron-cytochrome-c reductase activity Inferred from electronic annotation. Source: Compara oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 678	677	NADPH--cytochrome P450 reductase		PRO_0000167597
Regions
	Domain	80 – 224	145	Flavodoxin-like
	Domain	279 – 521	243	FAD-binding FR-type
	Nucleotide binding	170 – 201	32	FMN By similarity
	Nucleotide binding	314 – 325	12	FAD By similarity
	Nucleotide binding	451 – 461	11	FAD By similarity
	Nucleotide binding	530 – 548	19	NADP By similarity
	Nucleotide binding	625 – 641	17	NADP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylglycine By similarity
	Modified residue	575	1	Phosphotyrosine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P37040 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 060282A7A55483AF	FASTA	678	77,044
	10 20 30 40 50 60 MGDSHEDTSA TVPEAVAEEV SLFSTTDIVL FSLIVGVLTY WFIFKKKKEE IPEFSKIQTT 70 80 90 100 110 120 APPVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA 130 140 150 160 170 180 DLSSLPEIDK SLVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLTGVKFAV FGLGNKTYEH 190 200 210 220 230 240 FNAMGKYVDQ RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEF FGVEATGEES 250 260 270 280 290 300 SIRQYELVVH EDMDTAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL 310 320 330 340 350 360 MHLELDISDS KIRYESGDHV AVYPANDSTL VNQIGEILGA DLDVIMSLNN LDEESNKKHP 370 380 390 400 410 420 FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE HLHKMASSSG EGKELYLSWV 430 440 450 460 470 480 VEARRHILAI LQDYPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVAVEYEA 490 500 510 520 530 540 KSGRVNKGVA TSWLRTKEPA GENGRRALVP MFVRKSQFRL PFKPTTPVIM VGPGTGVAPF 550 560 570 580 590 600 MGFIQERAWL REQGKEVGET LLYYGCRRSD EDYLYREELA RFHKDGALTQ LNVAFSREQA 610 620 630 640 650 660 HKVYVQHLLK RDKEHLWKLI HEGGAHIYVC GDARNMAKDV QNTFYDIVAE FGPMEHTQAV 670 DYVKKLMTKG RYSLDVWS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse NADPH-cytochrome P-450 oxidoreductase: molecular cloning and functional expression in yeast." Ohgiya S., Ishizaki K., Kamataki T., Shinriki N. Biochim. Biophys. Acta 1186:137-141(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ddY.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[3]	"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-575, MASS SPECTROMETRY. Tissue: Teratocarcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D17571 mRNA. Translation: BAA04496.1. BC031463 mRNA. Translation: AAH31463.1.
IPI	IPI00621548.
RefSeq	NP_032924.1. NM_008898.1.
UniGene	Mm.3863.
3D structure databases
ProteinModelPortal	P37040.
SMR	P37040. Positions 63-678.
ModBase	Search...
Protein-protein interaction databases
IntAct	P37040. 2 interactions.
STRING	10090.ENSMUSP00000005651.
PTM databases
PhosphoSite	P37040.
2D gel databases
SWISS-2DPAGE	P37040.
Proteomic databases
PaxDb	P37040.
PRIDE	P37040.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005651; ENSMUSP00000005651; ENSMUSG00000005514.
GeneID	18984.
KEGG	mmu:18984.
UCSC	uc008zyt.1. mouse.
Organism-specific databases
CTD	5447.
MGI	MGI:97744. Por.
Phylogenomic databases
eggNOG	COG0369.
GeneTree	ENSGT00620000087711.
HOGENOM	HOG000282027.
HOVERGEN	HBG000432.
InParanoid	P37040.
KO	K00327.
OMA	KELHTHE.
OrthoDB	EOG46HG96.
Gene expression databases
ArrayExpress	P37040.
Bgee	P37040.
CleanEx	MM_POR.
Genevestigator	P37040.
GermOnline	ENSMUSG00000005514. Mus musculus.
Family and domain databases
Gene3D	1.20.990.10. 1 hit.
InterPro	IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR023173. NADPH_Cyt_P450_Rdtase_dom3. IPR001433. OxRdtase_FAD/NAD-bd. IPR023208. P450R. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF000208. P450R. 1 hit.
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
SUPFAM	SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	POR. mouse.
NextBio	295354.
SOURCE	Search...

Entry information

Entry name

NCPR_MOUSE

Accession

Primary (citable) accession number: P37040

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program