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P10614 (CP51_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lanosterol 14-alpha demethylase

EC=1.14.13.70
Alternative name(s):
CYPLI
Cytochrome P450 51
Cytochrome P450-14DM
Cytochrome P450-LIA1
Sterol 14-alpha demethylase
Gene names
Name:ERG11
Synonyms:CYP51
Ordered Locus Names:YHR007C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.

Catalytic activity

A 14-alpha-methylsteroid + 3 O2 + 3 NADPH = a Delta(14)-steroid + formate + 3 NADP+ + 4 H2O.

Cofactor

Heme group By similarity.

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6.

Subunit structure

Interacts with ERG28. Ref.7

Subcellular location

Membrane; Single-pass membrane protein.

Miscellaneous

It is the main target for antifungal compounds of the triazole family like ketoconazole which inhibits by coordinating the iron atom at the sixth ligand position.

Present with 73200 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the cytochrome P450 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERG25P530453EBI-5127,EBI-6506

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Lanosterol 14-alpha demethylase
PRO_0000052012

Regions

Topological domain1 – 2020Extracellular Potential
Transmembrane21 – 4121Helical; Potential
Topological domain42 – 530489Cytoplasmic Potential

Sites

Metal binding4701Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue4581Phosphoserine Ref.9

Experimental info

Sequence conflict4331K → N in AAA34546. Ref.2
Sequence conflict4331K → N in AAA34547. Ref.2

Secondary structure

................................................................................ 530
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10614 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 646960BBA0E17979

FASTA53060,720
        10         20         30         40         50         60 
MSATKSIVGE ALEYVNIGLS HFLALPLAQR ISLIIIIPFI YNIVWQLLYS LRKDRPPLVF 

        70         80         90        100        110        120 
YWIPWVGSAV VYGMKPYEFF EECQKKYGDI FSFVLLGRVM TVYLGPKGHE FVFNAKLADV 

       130        140        150        160        170        180 
SAEAAYAHLT TPVFGKGVIY DCPNSRLMEQ KKFVKGALTK EAFKSYVPLI AEEVYKYFRD 

       190        200        210        220        230        240 
SKNFRLNERT TGTIDVMVTQ PEMTIFTASR SLLGKEMRAK LDTDFAYLYS DLDKGFTPIN 

       250        260        270        280        290        300 
FVFPNLPLEH YRKRDHAQKA ISGTYMSLIK ERRKNNDIQD RDLIDSLMKN STYKDGVKMT 

       310        320        330        340        350        360 
DQEIANLLIG VLMGGQHTSA ATSAWILLHL AERPDVQQEL YEEQMRVLDG GKKELTYDLL 

       370        380        390        400        410        420 
QEMPLLNQTI KETLRMHHPL HSLFRKVMKD MHVPNTSYVI PAGYHVLVSP GYTHLRDEYF 

       430        440        450        460        470        480 
PNAHQFNIHR WNKDSASSYS VGEEVDYGFG AISKGVSSPY LPFGGGRHRC IGEHFAYCQL 

       490        500        510        520        530 
GVLMSIFIRT LKWHYPEGKT VPPPDFTSMV TLPTGPAKII WEKRNPEQKI 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of the P450 lanosterol demethylase gene from Saccharomyces cerevisiae."
Kalb V.F., Woods C.W., Turi T.G., Dey C.R., Sutter T.R., Loper J.C.
DNA 6:529-537(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A single amino acid substitution converts cytochrome P450(14DM) to an inactive form, cytochrome P450SG1: complete primary structures deduced from cloned DNAS."
Ishida N., Aoyama Y., Hatanaka R., Oyama Y., Imajo S., Ishiguro M., Oshima T., Nakazato H., Noguchi T., Maitra U.S., Mohan V.P., Sprinson D.B., Yoshida Y.
Biochem. Biophys. Res. Commun. 155:317-323(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Isolation of a cytochrome P-450 structural gene from Saccharomyces cerevisiae."
Kalb V.F., Loper J.C., Dey C.R., Woods C.W., Sutter T.R.
Gene 45:237-245(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-530.
[6]"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].
[7]"Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex."
Mo C., Bard M.
J. Lipid Res. 46:1991-1998(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERG28.
[8]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18109 Genomic DNA. Translation: AAA34379.1.
M15663 Genomic DNA. Translation: AAA34837.1.
M21483 Genomic DNA. Translation: AAA34546.1.
M21484 Genomic DNA. Translation: AAA34547.1.
U10555 Genomic DNA. Translation: AAB68433.1.
BK006934 Genomic DNA. Translation: DAA06695.1.
PIRA27491.
RefSeqNP_011871.1. NM_001179137.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LXJX-ray1.90A1-530[»]
ProteinModelPortalP10614.
SMRP10614. Positions 52-525.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36434. 238 interactions.
DIPDIP-7886N.
IntActP10614. 68 interactions.
MINTMINT-1325794.
STRING4932.YHR007C.

Chemistry

DrugBankDB00257. Clotrimazole.
DB01127. Econazole.
DB00196. Fluconazole.
DB01026. Ketoconazole.
DB01263. Posaconazole.
DB01153. Sertaconazole.
DB00251. Terconazole.
DB01007. Tioconazole.
DB00582. Voriconazole.

Proteomic databases

PaxDbP10614.
PeptideAtlasP10614.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR007C; YHR007C; YHR007C.
GeneID856398.
KEGGsce:YHR007C.

Organism-specific databases

CYGDYHR007c.
SGDS000001049. ERG11.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00660000095370.
HOGENOMHOG000042780.
KOK05917.
OMAFRENRAK.
OrthoDBEOG7712HB.

Enzyme and pathway databases

BioCycMetaCyc:YHR007C-MONOMER.
YEAST:YHR007C-MONOMER.
UniPathwayUPA00770; UER00754.

Gene expression databases

GenevestigatorP10614.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00465. EP450IV.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio981925.
PROP10614.

Entry information

Entry nameCP51_YEAST
AccessionPrimary (citable) accession number: P10614
Secondary accession number(s): D3DKV1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 140 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways