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UniProtKB/Swiss-Prot entry P16603


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NCPR_YEAST
Primary accession number P16603
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 102)
Name and origin of the protein
Protein name NADPH--cytochrome P450 reductase
Synonyms CPR
P450R
EC 1.6.2.4
Gene name
Name: NCP1
Synonyms: NCPR1, PRD1
OrderedLocusNames: YHR042W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13 AND 45-62.
PubMed=3139648 [NCBI, ExPASy, EBI, Israel, Japan]
Yabusaki Y., Murakami H., Ohkawa H.;
"Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 reductase deduced from nucleotide sequence of its cloned gene.";
J. Biochem. 103:1004-1010(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8091229 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.";
Science 265:2077-2082(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
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., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[5]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-666, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135500100; PubMed=14557538 [NCBI, ExPASy, EBI, Israel, Japan]
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
[6]
PHOSPHORYLATION, AND INTERACTION WITH PCL1.
DOI=10.1534/genetics.166.3.1177; PubMed=15082539 [NCBI, ExPASy, EBI, Israel, Japan]
Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.;
"The identification of Pcl1-interacting proteins that genetically interact with Cla4 may indicate a link between G1 progression and mitotic exit.";
Genetics 166:1177-1186(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 34-691 IN COMPLEX WITH FAD; FMN AND NADP.
DOI=10.1016/j.str.2005.09.015; PubMed=16407065 [NCBI, ExPASy, EBI, Israel, Japan]
Lamb D.C., Kim Y., Yermalitskaya L.V., Yermalitsky V.N., Lepesheva G.I., Kelly S.L., Waterman M.R., Podust L.M.;
"A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases.";
Structure 14:51-61(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D13788; BAA02936.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00062; AAB68904.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY693091; AAT93110.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S46735; S46735.
RefSeq NP_011908.1; -.
3D structure databases
PDB
2BF4; X-ray; 3.00 A; A/B=34-691.[ExPASy / RCSB / EBI]
2BN4; X-ray; 2.91 A; A/B=34-691.[ExPASy / RCSB / EBI]
2BPO; X-ray; 2.90 A; A/B=24-691.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2BF4; -.
2BN4; -.
2BPO; -.
ModBase P16603.
Protein-protein interaction databases
DIP DIP:8294N; -.
IntAct P16603; -.
Organism-specific databases
CYGD YHR042w; -.
SGD S000001084; NCP1.
Yeast-GFP YHR042W.
Gene expression databases
ArrayExpress P16603; -.
GermOnline YHR042W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005792; Cellular component: microsome (inferred from direct assay from SGD).
GO:0005741; Cellular component: mitochondrial outer membrane (inferred from direct assay from SGD).
GO:0009055; Molecular function: electron carrier activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006696; Biological process: ergosterol biosynthetic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR015702; NADPH_Cyt_Red.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.
PANTHER PTHR19384:SF17; NADPH_Cyt_Red; 1.
Pfam PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00369; FLAVODOXIN.
PR00371; FPNCR.
PROSITE PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P16603.
Proteomic databases
PeptideAtlas P16603; -.
Genome annotation databases
Ensembl YHR042W; Saccharomyces cerevisiae. [Contig view]
GeneID 856438; -.
GenomeReviews U00093_GR; YHR042W.
KEGG sce:YHR042W; -.
NMPDR fig|4932.3.peg.3057; -.
Phylogenomic databases
HOGENOM P16603; -.
Other
LinkHub P16603; -.
ProtoNet P16603.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP; Oxidoreductase; Phosphoprotein; Transmembrane; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   691  690     NADPH--cytochrome P450 reductase. PRO_0000167608
TRANSMEM   8    24  17     Potential. 
DOMAIN   61   204  144     Flavodoxin-like. 
DOMAIN   266   529  264     FAD-binding FR-type. 
NP_BIND   71    78  8     FMN; alternate. 
NP_BIND   116   119  4     FMN. 
NP_BIND   610   621  12     NADP. 
BINDING   67    67        FMN. 
BINDING   187   187        FMN; alternate. 
BINDING   441   441        FAD. 
BINDING   478   478        FAD. 
BINDING   646   646        NADP. 
CROSSLNK   666   666        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
VARIANT   474   474  1     V -> G. 
CONFLICT   423   423        T -> N (in Ref. 1; BAA02936). 
HELIX   50    56  7      
STRAND   60    66  7      
STRAND   68    70  3      
HELIX   71    87  17      
STRAND   91    95  5      
HELIX   96    98  3      
HELIX   103   106  4      
STRAND   109   116  8      
TURN   119   121  3      
HELIX   128   136  9      
TURN   139   144  6      
STRAND   146   153  8      
STRAND   157   159  3      
HELIX   162   173  12      
STRAND   183   186  4      
HELIX   187   189  3      
HELIX   192   211  20      
STRAND   223   231  9      
STRAND   234   239  6      
HELIX   243   245  3      
STRAND   271   278  8      
STRAND   287   293  7      
STRAND   306   309  4      
HELIX   315   325  11      
STRAND   332   339  8      
STRAND   345   351  7      
HELIX   352   358  7      
HELIX   368   374  7      
HELIX   375   377  3      
HELIX   381   392  12      
HELIX   394   400  7      
HELIX   402   404  3      
HELIX   408   416  9      
HELIX   426   432  7      
STRAND   439   443  5      
TURN   448   452  5      
STRAND   453   459  7      
STRAND   469   471  3      
HELIX   477   489  13      
TURN   494   496  3      
HELIX   508   510  3      
TURN   511   515  5      
STRAND   519   522  4      
STRAND   536   541  6      
HELIX   542   545  4      
HELIX   546   563  18      
STRAND   574   583  10      
TURN   587   590  4      
HELIX   591   599  9      
HELIX   600   602  3      
STRAND   603   610  8      
HELIX   620   626  7      
HELIX   628   636  9      
STRAND   640   645  6      
HELIX   650   665  16      
HELIX   670   682  13      
STRAND   685   690  6      
Sequence information
Length: 691 AA [This is the length of the unprocessed precursor] Molecular weight: 76772 Da [This is the MW of the unprocessed precursor] CRC64: 82BB847701E5438B [This is a checksum on the sequence]
        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 

P16603 in FASTA format

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View entry in raw text format (no links)
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