Skip Header

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

P00388

- NCPR_RAT

UniProt

P00388 - NCPR_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

NADPH--cytochrome P450 reductase

Gene

Por

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

FAD.
FMN.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi170 – 20132FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi314 – 32512FADBy similarityAdd
BLAST
Nucleotide bindingi451 – 46111FADBy similarityAdd
BLAST
Nucleotide bindingi530 – 54819NADPBy similarityAdd
BLAST
Nucleotide bindingi625 – 64117NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. cytochrome-b5 reductase activity, acting on NAD(P)H Source: RGD
  2. electron carrier activity Source: RGD
  3. enzyme binding Source: BHF-UCL
  4. flavin adenine dinucleotide binding Source: RGD
  5. FMN binding Source: RGD
  6. hydrolase activity Source: RGD
  7. iron-cytochrome-c reductase activity Source: RGD
  8. iron ion binding Source: InterPro
  9. NADP binding Source: RGD
  10. NADPH-hemoprotein reductase activity Source: BHF-UCL
  11. nitric oxide dioxygenase activity Source: RGD
  12. 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 Source: RefGenome

GO - Biological processi

  1. carnitine metabolic process Source: RGD
  2. cellular organofluorine metabolic process Source: Ensembl
  3. cellular response to follicle-stimulating hormone stimulus Source: RGD
  4. cellular response to gonadotropin stimulus Source: RGD
  5. cellular response to peptide hormone stimulus Source: RGD
  6. demethylation Source: RGD
  7. fatty acid oxidation Source: RGD
  8. flavonoid metabolic process Source: RGD
  9. internal peptidyl-lysine acetylation Source: RGD
  10. negative regulation of apoptotic process Source: RGD
  11. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  12. negative regulation of lipase activity Source: RGD
  13. nitrate catabolic process Source: RGD
  14. nitric oxide catabolic process Source: RGD
  15. oxidation-reduction process Source: BHF-UCL
  16. positive regulation of cholesterol biosynthetic process Source: RGD
  17. positive regulation of chondrocyte differentiation Source: RGD
  18. positive regulation of monooxygenase activity Source: Ensembl
  19. positive regulation of smoothened signaling pathway Source: RGD
  20. positive regulation of steroid hormone biosynthetic process Source: RGD
  21. regulation of cholesterol metabolic process Source: RGD
  22. regulation of growth plate cartilage chondrocyte proliferation Source: RGD
  23. response to drug Source: RGD
  24. 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.
SABIO-RKP00388.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductase (EC:1.6.2.4)
Short name:
CPR
Short name:
P450R
Gene namesi
Name:Por
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 12

Organism-specific databases

RGDi68335. Por.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein
Note: Anchored to the ER membrane by its N-terminal hydrophobic region.

GO - Cellular componenti

  1. cytosol Source: RefGenome
  2. endoplasmic reticulum Source: UniProtKB-KW
  3. intracellular membrane-bounded organelle Source: RGD
  4. membrane Source: RGD
  5. mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 678677NADPH--cytochrome P450 reductasePRO_0000167600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00388.
PRIDEiP00388.

Expressioni

Gene expression databases

GenevestigatoriP00388.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1
678
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi69 – 768
Beta strandi80 – 856
Beta strandi87 – 893
Helixi90 – 10112
Helixi102 – 1054
Beta strandi109 – 1124
Helixi114 – 1163
Helixi119 – 1279
Beta strandi132 – 1409
Turni141 – 1433
Helixi147 – 1493
Helixi150 – 1589
Beta strandi167 – 1748
Beta strandi176 – 1805
Helixi183 – 19412
Beta strandi198 – 2014
Beta strandi204 – 2074
Turni208 – 2103
Helixi212 – 23120
Beta strandi244 – 2496
Helixi255 – 2573
Beta strandi258 – 2614
Beta strandi263 – 2653
Turni266 – 2705
Beta strandi278 – 2803
Beta strandi282 – 29110
Beta strandi294 – 2985
Beta strandi300 – 3067
Turni308 – 3114
Beta strandi319 – 3224
Helixi328 – 33710
Beta strandi345 – 3517
Beta strandi360 – 3667
Helixi367 – 3737
Helixi383 – 3897
Helixi390 – 3923
Beta strandi393 – 3953
Helixi396 – 4038
Helixi404 – 4063
Beta strandi408 – 4103
Helixi411 – 4199
Turni420 – 4245
Helixi427 – 4337
Helixi441 – 4477
Beta strandi454 – 4574
Turni462 – 4643
Beta strandi468 – 4747
Beta strandi477 – 4793
Beta strandi483 – 4875
Helixi489 – 4968
Beta strandi508 – 5147
Beta strandi528 – 5314
Helixi534 – 5374
Helixi538 – 55215
Beta strandi560 – 5678
Turni569 – 5713
Helixi576 – 5849
Beta strandi587 – 5959
Beta strandi598 – 6014
Helixi605 – 6117
Helixi613 – 6219
Beta strandi626 – 6327
Turni633 – 6353
Helixi636 – 65116
Helixi656 – 66813
Beta strandi671 – 6777

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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-ray2.20A62-678[»]
3OJXX-ray2.50A57-678[»]
3WKTX-ray4.30A/B58-678[»]
ProteinModelPortaliP00388.
SMRiP00388. Positions 63-678.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00388.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 224145Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini279 – 521243FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0369.
GeneTreeiENSGT00760000119403.
HOGENOMiHOG000282027.
HOVERGENiHBG000432.
InParanoidiP00388.
KOiK00327.
OMAiVYSENSI.
OrthoDBiEOG7HQN7J.
PhylomeDBiP00388.
TreeFamiTF105719.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti255 – 2551V → A in AAA41683. (PubMed:2125483)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M10068 mRNA. Translation: AAA41064.1 .
M12516 mRNA. Translation: AAA41067.1 .
M58937
, M58932 , M58933 , M58934 , M58935 , M58936 Genomic DNA. Translation: AAA41683.1 .
PIRi A36073. RDRTO4.
RefSeqi NP_113764.1. NM_031576.1.
UniGenei Rn.11359.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AMO X-ray 2.60 A/B 64-678 [» ]
1J9Z X-ray 2.70 A/B 57-676 [» ]
1JA0 X-ray 2.60 A/B 57-676 [» ]
1JA1 X-ray 1.80 A/B 57-678 [» ]
3ES9 X-ray 3.40 A/B/C 57-678 [» ]
3OJW X-ray 2.20 A 62-678 [» ]
3OJX X-ray 2.50 A 57-678 [» ]
3WKT X-ray 4.30 A/B 58-678 [» ]
ProteinModelPortali P00388.
SMRi P00388. Positions 63-678.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248088. 1 interaction.
MINTi MINT-4564101.
STRINGi 10116.ENSRNOP00000001961.

Chemistry

ChEMBLi CHEMBL2817.

Proteomic databases

PaxDbi P00388.
PRIDEi P00388.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000001961 ; ENSRNOP00000001961 ; ENSRNOG00000001442 .
GeneIDi 29441.
KEGGi rno:29441.
UCSCi RGD:68335. rat.

Organism-specific databases

CTDi 5447.
RGDi 68335. Por.

Phylogenomic databases

eggNOGi COG0369.
GeneTreei ENSGT00760000119403.
HOGENOMi HOG000282027.
HOVERGENi HBG000432.
InParanoidi P00388.
KOi K00327.
OMAi VYSENSI.
OrthoDBi EOG7HQN7J.
PhylomeDBi P00388.
TreeFami TF105719.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-14290.
SABIO-RK P00388.

Miscellaneous databases

EvolutionaryTracei P00388.
NextBioi 609193.
PROi P00388.

Gene expression databases

Genevestigatori P00388.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProi IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000208. P450R. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains."
    Porter T.D., Kasper C.B.
    Proc. Natl. Acad. Sci. U.S.A. 82:973-977(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Expression of rat NADPH-cytochrome P-450 reductase cDNA in Saccharomyces cerevisiae."
    Murakami H., Yabusaki Y., Ohkawa H.
    DNA 5:1-10(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "NADPH-cytochrome P-450 oxidoreductase gene organization correlates with structural domains of the protein."
    Porter T.D., Beck T.W., Kasper C.B.
    Biochemistry 29:9814-9818(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
    Tissue: Liver.
  4. "Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes."
    Wang M., Roberts D.L., Paschke R., Shea T.M., Masters B.S.S., Kim J.-J.P.
    Proc. Natl. Acad. Sci. U.S.A. 94:8411-8416(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  5. "NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer."
    Hubbard P.A., Shen A.L., Paschke R., Kasper C.B., Kim J.-J.P.
    J. Biol. Chem. 276:29163-29170(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS.

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: October 29, 2014
This is version 146 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

External Data

Dasty 3