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UniProtKB/Swiss-Prot entry P38626


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

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Entry information
Entry name NCB5R_YEAST
Primary accession number P38626
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on April 29, 2008 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 73)
Name and origin of the protein
Protein name NADH-cytochrome b5 reductase 1
Synonyms EC 1.6.2.2
Microsomal cytochrome b reductase
P35
Gene name
Name: CBR1
Synonyms: CBR, CBR5
OrderedLocusNames: YIL043C
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].
STRAIN=842;
PubMed=8307010 [NCBI, ExPASy, EBI, Israel, Japan]
Csukai M., Murray M., Orr E.;
"Isolation and complete sequence of CBR, a gene encoding a putative cytochrome b reductase in Saccharomyces cerevisiae.";
Eur. J. Biochem. 219:441-448(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169870 [NCBI, ExPASy, EBI, Israel, Japan]
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[3]
CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND SUBUNIT.
PubMed=14930 [NCBI, ExPASy, EBI, Israel, Japan]
Kubota S., Yoshida Y., Kumaoka H.;
"Studies on the microsomal electron-transport system of anaerobically grown yeast. IV. Purification and characterization of NADH-cytochrome b5 reductase.";
J. Biochem. 81:187-195(1977).
[4]
INDUCTION, AND ENZYME REGULATION.
DOI=10.1016/0300-9084(84)90155-X; PubMed=6442167 [NCBI, ExPASy, EBI, Israel, Japan]
Bertrand J.-C., Mattei G., Parra C., Giordani R., Gilewicz M.;
"Influence of oxygen on the microsomal electron transport system in Saccharomyces cerevisiae.";
Biochimie 66:583-588(1984).
[5]
FUNCTION.
DOI=10.1016/S0014-5793(99)01548-3; PubMed=10622712 [NCBI, ExPASy, EBI, Israel, Japan]
Lamb D.C., Kelly D.E., Manning N.J., Kaderbhai M.A., Kelly S.L.;
"Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction.";
FEBS Lett. 462:283-288(1999).
[6]
IDENTIFICATION OF PROBABLE INITIATION SITE.
DOI=10.1038/nature01644; PubMed=12748633 [NCBI, ExPASy, EBI, Israel, Japan]
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
"Sequencing and comparison of yeast species to identify genes and regulatory elements.";
Nature 423:241-254(2003).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[8]
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).
[9]
IDENTIFICATION OF PROBABLE INITIATION SITE.
DOI=10.1093/nar/gki583; PubMed=15905473 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Dietrich F.S.;
"Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE.";
Nucleic Acids Res. 33:2838-2851(2005).
[10]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1091/mbc.E05-08-0740; PubMed=16407407 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
"Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins.";
Mol. Biol. Cell 17:1436-1450(2006).
[11]
INTERACTION WITH STE20.
DOI=10.1242/jcs.009860; PubMed=17895367 [NCBI, ExPASy, EBI, Israel, Japan]
Tiedje C., Holland D.G., Just U., Hofken T.;
"Proteins involved in sterol synthesis interact with Ste20 and regulate cell polarity.";
J. Cell Sci. 120:3613-3624(2007).
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
Z28365; CAA82214.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46861; CAA86908.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S49935; S49935.
RefSeq NP_012221.2; -.
3D structure databases
HSSP P17571; 2CND. [HSSP ENTRY / PDB]
ModBase P38626.
Organism-specific databases
CYGD YIL043c; -.
SGD S000001305; CBR1.
Yeast-GFP YIL043C.
Gene expression databases
GermOnline YIL043C; 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:0004128; Molecular function: cytochrome-b5 reductase activity (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001834; Cyt_B5_reductase.
IPR001709; FPN_cyt_redctse.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.
Pfam PF00970; FAD_binding_6; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00406; CYTB5RDTASE.
PR00371; FPNCR.
PROSITE PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P38626.
ProtoNet P38626.
Proteomic databases
PeptideAtlas P38626; -.
Genome annotation databases
Ensembl YIL043C; Saccharomyces cerevisiae. [Contig view]
GeneID 854768; -.
GenomeReviews Z47047_GR; YIL043C.
KEGG sce:YIL043C; -.
NMPDR fig|4932.3.peg.1754; -.
Phylogenomic databases
HOGENOM P38626; -.
Other
LinkHub P38626; -.
NextBio 977526; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; NAD; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   284  284     NADH-cytochrome b5 reductase 1. PRO_0000167627
TRANSMEM   7    27  21     Potential. 
DOMAIN   38   142  105     FAD-binding FR-type. 
NP_BIND   122   137  16     FAD (By similarity). 
NP_BIND   148   180  33     FAD (By similarity). 
Sequence information
Length: 284 AA [This is the length of the unprocessed precursor] Molecular weight: 31494 Da [This is the MW of the unprocessed precursor] CRC64: 0E71E7AB083BB623 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAIDAQKLVV VIVIVVVPLL FKFIIGPKTK PVLDPKRNDF QSFPLVEKTI LTHNTSMYKF 

        70         80         90        100        110        120 
GLPHADDVLG LPIGQHIVIK ANINGKDITR SYTPTSLDGD TKGNFELLVK SYPTGNVSKM 

       130        140        150        160        170        180 
IGELKIGDSI QIKGPRGNYH YERNCRSHLG MIAGGTGIAP MYQIMKAIAM DPHDTTKVSL 

       190        200        210        220        230        240 
VFGNVHEEDI LLKKELEALV AMKPSQFKIV YYLDSPDRED WTGGVGYITK DVIKEHLPAA 

       250        260        270        280 
TMDNVQILIC GPPAMVASVR RSTVDLGFRR SKPLSKMEDQ VFVF 

P38626 in FASTA format

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View entry in raw text format (no links)
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