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P16603 (NCPR_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH--cytochrome P450 reductase

Short name=CPR
Short name=P450R
EC=1.6.2.4
Gene names
Name:NCP1
Synonyms:CPR1, NCPR1, PRD1
Ordered Locus Names:YHR042W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length691 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane. Ref.5 Ref.6 Ref.7 Ref.8

Catalytic activity

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein. Ref.6 Ref.7 Ref.8

Cofactor

Binds 1 FAD per monomer. Ref.7 Ref.15

Binds 1 FMN per monomer. Ref.7

Subunit structure

Interacts with PCL1. Ref.12

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion outer membrane; Single-pass membrane protein. Cell membrane; Single-pass membrane protein. Microsome Ref.6 Ref.7 Ref.8 Ref.11 Ref.13 Ref.14.

Induction

By galactose and on the plasma membrane by iron or copper deficiency. Repressed by glucose. Ref.6

Post-translational modification

Phosphorylated by the cyclin-CDK PCL1-PHO85. Ref.12

Disruption phenotype

Accumulates 20% of ergosterol of wild type. Ref.7

Miscellaneous

Present with 46600 molecules/cell in log phase SD medium.

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.

Biophysicochemical properties

Kinetic parameters:

The Vmax of the reaction is 721 pmol/min/pmol enzyme towards cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH.

KM=1.59 µM for cytochrome c Ref.8

KM=1.46 µM for NADPH

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 691690NADPH--cytochrome P450 reductase
PRO_0000167608

Regions

Transmembrane8 – 2417Helical; Potential
Domain61 – 204144Flavodoxin-like
Domain266 – 529264FAD-binding FR-type
Nucleotide binding71 – 788FMN; alternate
Nucleotide binding116 – 1194FMN
Nucleotide binding610 – 62112NADP

Sites

Binding site671FMN
Binding site1871FMN; alternate
Binding site4411FAD
Binding site4781FAD
Binding site6461NADP

Amino acid modifications

Cross-link666Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Natural variations

Natural variant4741V → G.

Experimental info

Sequence conflict4231T → N in BAA02936. Ref.1

Secondary structure

.............................................................................................................. 691
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16603 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 82BB847701E5438B

FASTA69176,772
        10         20         30         40         50         60 
MPFGIDNTDF TVLAGLVLAV LLYVKRNSIK ELLMSDDGDI TAVSSGNRDI AQVVTENNKN 

        70         80         90        100        110        120 
YLVLYASQTG TAEDYAKKFS KELVAKFNLN VMCADVENYD FESLNDVPVI VSIFISTYGE 

       130        140        150        160        170        180 
GDFPDGAVNF EDFICNAEAG ALSNLRYNMF GLGNSTYEFF NGAAKKAEKH LSAAGAIRLG 

       190        200        210        220        230        240 
KLGEADDGAG TTDEDYMAWK DSILEVLKDE LHLDEQEAKF TSQFQYTVLN EITDSMSLGE 

       250        260        270        280        290        300 
PSAHYLPSHQ LNRNADGIQL GPFDLSQPYI APIVKSRELF SSNDRNCIHS EFDLSGSNIK 

       310        320        330        340        350        360 
YSTGDHLAVW PSNPLEKVEQ FLSIFNLDPE TIFDLKPLDP TVKVPFPTPT TIGAAIKHYL 

       370        380        390        400        410        420 
EITGPVSRQL FSSLIQFAPN ADVKEKLTLL SKDKDQFAVE ITSKYFNIAD ALKYLSDGAK 

       430        440        450        460        470        480 
WDTVPMQFLV ESVPQMTPRY YSISSSSLSE KQTVHVTSIV ENFPNPELPD APPVVGVTTN 

       490        500        510        520        530        540 
LLRNIQLAQN NVNIAETNLP VHYDLNGPRK LFANYKLPVH VRRSNFRLPS NPSTPVIMIG 

       550        560        570        580        590        600 
PGTGVAPFRG FIRERVAFLE SQKKGGNNVS LGKHILFYGS RNTDDFLYQD EWPEYAKKLD 

       610        620        630        640        650        660 
GSFEMVVAHS RLPNTKKVYV QDKLKDYEDQ VFEMINNGAF IYVCGDAKGM AKGVSTALVG 

       670        680        690 
ILSRGKSITT DEATELIKML KTSGRYQEDV W 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 reductase deduced from nucleotide sequence of its cloned gene."
Yabusaki Y., Murakami H., Ohkawa H.
J. Biochem. 103:1004-1010(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13 AND 45-62.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Multiple regulatory elements control expression of the gene encoding the Saccharomyces cerevisiae cytochrome P450, lanosterol 14 alpha-demethylase (ERG11)."
Turi T.G., Loper J.C.
J. Biol. Chem. 267:2046-2056(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Cytochrome P-450 reductase is responsible for the ferrireductase activity associated with isolated plasma membranes of Saccharomyces cerevisiae."
Lesuisse E., Casteras-Simon M., Labbe P.
FEMS Microbiol. Lett. 156:147-152(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
[7]"The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity."
Venkateswarlu K., Lamb D.C., Kelly D.E., Manning N.J., Kelly S.L.
J. Biol. Chem. 273:4492-4496(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[8]"Activities and kinetic mechanisms of native and soluble NADPH-cytochrome P450 reductase."
Lamb D.C., Warrilow A.G., Venkateswarlu K., Kelly D.E., Kelly S.L.
Biochem. Biophys. Res. Commun. 286:48-54(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666.
[11]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]"The identification of Pcl1-interacting proteins that genetically interact with Cla4 may indicate a link between G1 progression and mitotic exit."
Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.
Genetics 166:1177-1186(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH PCL1.
[13]"Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[14]"Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins."
Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C.
Mol. Biol. Cell 17:1436-1450(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the surface is highly specific."
Ivanov A.S., Gnedenko O.V., Molnar A.A., Archakov A.I., Podust L.M.
ACS Chem. Biol. 5:767-776(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FMN-BINDING AND FAD-BINDING.
[16]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases."
Lamb D.C., Kim Y., Yermalitskaya L.V., Yermalitsky V.N., Lepesheva G.I., Kelly S.L., Waterman M.R., Podust L.M.
Structure 14:51-61(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 34-691 IN COMPLEX WITH FAD; FMN AND NADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13788 Genomic DNA. Translation: BAA02936.1.
U00062 Genomic DNA. Translation: AAB68904.1.
AY693091 Genomic DNA. Translation: AAT93110.1.
BK006934 Genomic DNA. Translation: DAA06734.1.
PIRS46735.
RefSeqNP_011908.1. NM_001179172.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BF4X-ray3.00A/B34-691[»]
2BN4X-ray2.91A/B34-691[»]
2BPOX-ray2.90A/B34-691[»]
3FJOX-ray2.50A44-211[»]
ProteinModelPortalP16603.
SMRP16603. Positions 47-691.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36474. 62 interactions.
DIPDIP-8294N.
IntActP16603. 8 interactions.
MINTMINT-2782506.
STRING4932.YHR042W.

Proteomic databases

PaxDbP16603.
PeptideAtlasP16603.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR042W; YHR042W; YHR042W.
GeneID856438.
KEGGsce:YHR042W.

Organism-specific databases

SGDS000001084. NCP1.

Phylogenomic databases

eggNOGCOG0369.
GeneTreeENSGT00620000087711.
HOGENOMHOG000282027.
KOK00327.
OMALGKHILF.
OrthoDBEOG744TKC.

Enzyme and pathway databases

BioCycYEAST:YHR042W-MONOMER.

Gene expression databases

GenevestigatorP16603.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
InterProIPR003097. 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]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000208. P450R. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16603.
NextBio982042.
PROP16603.

Entry information

Entry nameNCPR_YEAST
AccessionPrimary (citable) accession number: P16603
Secondary accession number(s): D3DKZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references