Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADPH--cytochrome P450 reductase

Gene

Por

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • FADUniRule annotation1 PublicationNote: Binds 1 FAD per monomer.UniRule annotation1 Publication
  • FMNUniRule annotation1 PublicationNote: Binds 1 FMN per monomer.UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei208FMNUniRule annotation3 Publications1
Binding sitei298NADPUniRule annotation4 Publications1
Binding sitei424FADUniRule annotation4 Publications1
Binding sitei478FADUniRule annotation5 Publications1
Binding sitei535NADPUniRule annotation5 Publications1
Binding sitei639NADPUniRule annotation4 Publications1
Binding sitei677FADUniRule annotation5 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi86 – 91FMNUniRule annotation5 Publications6
Nucleotide bindingi138 – 141FMNUniRule annotation5 Publications4
Nucleotide bindingi173 – 182FMNUniRule annotation5 Publications10
Nucleotide bindingi454 – 457FADUniRule annotation5 Publications4
Nucleotide bindingi472 – 474FADUniRule annotation4 Publications3
Nucleotide bindingi488 – 491FADUniRule annotation5 Publications4
Nucleotide bindingi596 – 597NADPUniRule annotation5 Publications2
Nucleotide bindingi602 – 606NADPUniRule annotation5 Publications5

GO - Molecular functioni

  • [methionine synthase] reductase activity Source: GO_Central
  • cytochrome-b5 reductase activity, acting on NAD(P)H Source: RGD
  • electron carrier activity Source: RGD
  • enzyme binding Source: BHF-UCL
  • flavin adenine dinucleotide binding Source: RGD
  • FMN binding Source: RGD
  • hydrolase activity Source: RGD
  • iron-cytochrome-c reductase activity Source: RGD
  • NADP binding Source: RGD
  • NADPH-hemoprotein reductase activity Source: BHF-UCL
  • nitric oxide dioxygenase activity Source: RGD

GO - Biological processi

  • carnitine metabolic process Source: RGD
  • cellular organofluorine metabolic process Source: Ensembl
  • cellular response to follicle-stimulating hormone stimulus Source: RGD
  • cellular response to gonadotropin stimulus Source: RGD
  • cellular response to peptide hormone stimulus Source: RGD
  • demethylation Source: RGD
  • fatty acid oxidation Source: RGD
  • flavonoid metabolic process Source: RGD
  • internal peptidyl-lysine acetylation Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  • negative regulation of lipase activity Source: RGD
  • nitrate catabolic process Source: RGD
  • nitric oxide catabolic process Source: RGD
  • oxidation-reduction process Source: BHF-UCL
  • positive regulation of cholesterol biosynthetic process Source: RGD
  • positive regulation of chondrocyte differentiation Source: RGD
  • positive regulation of monooxygenase activity Source: Ensembl
  • positive regulation of smoothened signaling pathway Source: RGD
  • positive regulation of steroid hormone biosynthetic process Source: RGD
  • regulation of cholesterol metabolic process Source: RGD
  • regulation of growth plate cartilage chondrocyte proliferation Source: RGD
  • response to drug Source: RGD
  • response to nutrient Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14290.
BRENDAi1.6.2.4. 5301.
ReactomeiR-RNO-211897. Cytochrome P450 - arranged by substrate type.
SABIO-RKP00388.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductaseUniRule annotation (EC:1.6.2.4UniRule annotation)
Short name:
CPRUniRule annotation
Short name:
P450RUniRule annotation
Gene namesi
Name:PorUniRule annotation
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi68335. Por.

Subcellular locationi

  • Endoplasmic reticulum membrane UniRule annotation; Single-pass membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 22LumenalUniRule annotationAdd BLAST21
Transmembranei23 – 43HelicalUniRule annotationAdd BLAST21
Topological domaini44 – 678CytoplasmicUniRule annotationAdd BLAST635

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: RGD
  • membrane Source: RGD
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2817.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001676002 – 678NADPH--cytochrome P450 reductaseAdd BLAST677

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00388.
PRIDEiP00388.

PTM databases

iPTMnetiP00388.
PhosphoSitePlusiP00388.

Expressioni

Gene expression databases

BgeeiENSRNOG00000001442.
GenevisibleiP00388. RN.

Interactioni

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi248088. 1 interactor.
MINTiMINT-4564101.
STRINGi10116.ENSRNOP00000001961.

Structurei

Secondary structure

1678
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi69 – 76Combined sources8
Beta strandi80 – 85Combined sources6
Beta strandi87 – 89Combined sources3
Helixi90 – 101Combined sources12
Helixi102 – 105Combined sources4
Beta strandi109 – 112Combined sources4
Helixi114 – 116Combined sources3
Helixi119 – 127Combined sources9
Beta strandi132 – 140Combined sources9
Turni141 – 143Combined sources3
Helixi147 – 149Combined sources3
Helixi150 – 158Combined sources9
Beta strandi167 – 174Combined sources8
Beta strandi176 – 180Combined sources5
Helixi183 – 194Combined sources12
Beta strandi198 – 201Combined sources4
Beta strandi204 – 207Combined sources4
Turni208 – 210Combined sources3
Helixi212 – 231Combined sources20
Beta strandi244 – 249Combined sources6
Helixi255 – 257Combined sources3
Beta strandi258 – 261Combined sources4
Beta strandi263 – 265Combined sources3
Turni266 – 270Combined sources5
Beta strandi278 – 280Combined sources3
Beta strandi282 – 291Combined sources10
Beta strandi294 – 298Combined sources5
Beta strandi300 – 306Combined sources7
Turni308 – 311Combined sources4
Beta strandi319 – 322Combined sources4
Helixi328 – 337Combined sources10
Beta strandi345 – 351Combined sources7
Beta strandi360 – 366Combined sources7
Helixi367 – 373Combined sources7
Helixi383 – 389Combined sources7
Helixi390 – 392Combined sources3
Beta strandi393 – 395Combined sources3
Helixi396 – 403Combined sources8
Helixi404 – 406Combined sources3
Beta strandi408 – 410Combined sources3
Helixi411 – 419Combined sources9
Turni420 – 424Combined sources5
Helixi427 – 433Combined sources7
Helixi441 – 447Combined sources7
Beta strandi454 – 457Combined sources4
Turni462 – 464Combined sources3
Beta strandi468 – 474Combined sources7
Beta strandi477 – 479Combined sources3
Beta strandi483 – 487Combined sources5
Helixi489 – 496Combined sources8
Beta strandi508 – 514Combined sources7
Beta strandi528 – 531Combined sources4
Helixi534 – 537Combined sources4
Helixi538 – 552Combined sources15
Beta strandi560 – 567Combined sources8
Turni569 – 571Combined sources3
Helixi576 – 584Combined sources9
Beta strandi587 – 595Combined sources9
Beta strandi598 – 601Combined sources4
Helixi605 – 611Combined sources7
Helixi613 – 621Combined sources9
Beta strandi626 – 632Combined sources7
Turni633 – 635Combined sources3
Helixi636 – 651Combined sources16
Helixi656 – 668Combined sources13
Beta strandi671 – 677Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AMOX-ray2.60A/B64-678[»]
1J9ZX-ray2.70A/B57-676[»]
1JA0X-ray2.60A/B57-676[»]
1JA1X-ray1.80A/B57-678[»]
3ES9X-ray3.40A/B/C57-678[»]
3OJWX-ray2.20A57-678[»]
3OJXX-ray2.50A57-678[»]
3WKTX-ray4.30A/B58-678[»]
4Y7CX-ray2.20A/B57-678[»]
4Y9RX-ray2.40A/B57-678[»]
4Y9UX-ray1.95A/B57-678[»]
4YAFX-ray1.91A/B57-678[»]
4YALX-ray1.88A/B57-678[»]
4YAOX-ray2.50A/B57-678[»]
4YAUX-ray2.20A/B57-678[»]
4YAWX-ray2.00A/B57-678[»]
ProteinModelPortaliP00388.
SMRiP00388.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00388.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini80 – 224Flavodoxin-likeUniRule annotationAdd BLAST145
Domaini279 – 521FAD-binding FR-typeUniRule annotationAdd BLAST243

Sequence similaritiesi

Belongs to the NADPH--cytochrome P450 reductase family.UniRule annotation
In the N-terminal section; belongs to the flavodoxin family.UniRule annotation
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation
Contains 1 FAD-binding FR-type domain.UniRule annotation
Contains 1 flavodoxin-like domain.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
GeneTreeiENSGT00840000129757.
HOGENOMiHOG000282027.
HOVERGENiHBG000432.
InParanoidiP00388.
KOiK00327.
OMAiVWYENDP.
OrthoDBiEOG091G02VT.
PhylomeDBiP00388.
TreeFamiTF105719.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_03212. NCPR. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00388-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDSHEDTSA TMPEAVAEEV SLFSTTDMVL FSLIVGVLTY WFIFRKKKEE
60 70 80 90 100
IPEFSKIQTT APPVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK
110 120 130 140 150
DAHRYGMRGM SADPEEYDLA DLSSLPEIDK SLVVFCMATY GEGDPTDNAQ
160 170 180 190 200
DFYDWLQETD VDLTGVKFAV FGLGNKTYEH FNAMGKYVDQ RLEQLGAQRI
210 220 230 240 250
FELGLGDDDG NLEEDFITWR EQFWPAVCEF FGVEATGEES SIRQYELVVH
260 270 280 290 300
EDMDVAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTANR KLNQGTERHL
310 320 330 340 350
MHLELDISDS KIRYESGDHV AVYPANDSAL VNQIGEILGA DLDVIMSLNN
360 370 380 390 400
LDEESNKKHP FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE
410 420 430 440 450
HLHKMASSSG EGKELYLSWV VEARRHILAI LQDYPSLRPP IDHLCELLPR
460 470 480 490 500
LQARYYSIAS SSKVHPNSVH ICAVAVEYEA KSGRVNKGVA TSWLRAKEPA
510 520 530 540 550
GENGGRALVP MFVRKSQFRL PFKSTTPVIM VGPGTGIAPF MGFIQERAWL
560 570 580 590 600
REQGKEVGET LLYYGCRRSD EDYLYREELA RFHKDGALTQ LNVAFSREQA
610 620 630 640 650
HKVYVQHLLK RDREHLWKLI HEGGAHIYVC GDARNMAKDV QNTFYDIVAE
660 670
FGPMEHTQAV DYVKKLMTKG RYSLDVWS
Length:678
Mass (Da):76,963
Last modified:January 23, 2007 - v3
Checksum:iAF3087E4D7A352D6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti255V → A in AAA41683 (PubMed:2125483).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10068 mRNA. Translation: AAA41064.1.
M12516 mRNA. Translation: AAA41067.1.
M58937
, M58932, M58933, M58934, M58935, M58936 Genomic DNA. Translation: AAA41683.1.
PIRiA36073. RDRTO4.
RefSeqiNP_113764.1. NM_031576.1.
UniGeneiRn.11359.

Genome annotation databases

EnsembliENSRNOT00000001961; ENSRNOP00000001961; ENSRNOG00000001442.
GeneIDi29441.
KEGGirno:29441.
UCSCiRGD:68335. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10068 mRNA. Translation: AAA41064.1.
M12516 mRNA. Translation: AAA41067.1.
M58937
, M58932, M58933, M58934, M58935, M58936 Genomic DNA. Translation: AAA41683.1.
PIRiA36073. RDRTO4.
RefSeqiNP_113764.1. NM_031576.1.
UniGeneiRn.11359.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AMOX-ray2.60A/B64-678[»]
1J9ZX-ray2.70A/B57-676[»]
1JA0X-ray2.60A/B57-676[»]
1JA1X-ray1.80A/B57-678[»]
3ES9X-ray3.40A/B/C57-678[»]
3OJWX-ray2.20A57-678[»]
3OJXX-ray2.50A57-678[»]
3WKTX-ray4.30A/B58-678[»]
4Y7CX-ray2.20A/B57-678[»]
4Y9RX-ray2.40A/B57-678[»]
4Y9UX-ray1.95A/B57-678[»]
4YAFX-ray1.91A/B57-678[»]
4YALX-ray1.88A/B57-678[»]
4YAOX-ray2.50A/B57-678[»]
4YAUX-ray2.20A/B57-678[»]
4YAWX-ray2.00A/B57-678[»]
ProteinModelPortaliP00388.
SMRiP00388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248088. 1 interactor.
MINTiMINT-4564101.
STRINGi10116.ENSRNOP00000001961.

Chemistry databases

ChEMBLiCHEMBL2817.

PTM databases

iPTMnetiP00388.
PhosphoSitePlusiP00388.

Proteomic databases

PaxDbiP00388.
PRIDEiP00388.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001961; ENSRNOP00000001961; ENSRNOG00000001442.
GeneIDi29441.
KEGGirno:29441.
UCSCiRGD:68335. rat.

Organism-specific databases

CTDi5447.
RGDi68335. Por.

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
GeneTreeiENSGT00840000129757.
HOGENOMiHOG000282027.
HOVERGENiHBG000432.
InParanoidiP00388.
KOiK00327.
OMAiVWYENDP.
OrthoDBiEOG091G02VT.
PhylomeDBiP00388.
TreeFamiTF105719.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14290.
BRENDAi1.6.2.4. 5301.
ReactomeiR-RNO-211897. Cytochrome P450 - arranged by substrate type.
SABIO-RKP00388.

Miscellaneous databases

EvolutionaryTraceiP00388.
PROiP00388.

Gene expression databases

BgeeiENSRNOG00000001442.
GenevisibleiP00388. RN.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_03212. NCPR. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNCPR_RAT
AccessioniPrimary (citable) accession number: P00388
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.