Lanosterol 14-alpha demethylase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P10614 (CP51_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ergosterol biosynthetic process Inferred from mutant phenotype PubMed 200835. Source: SGD
Cellular_component	endoplasmic reticulum Inferred from direct assay PubMed 11914276 PubMed 15951236. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro sterol 14-demethylase activity Inferred from direct assay PubMed 9087488. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERG25	P53045	3	EBI-5127,EBI-6506

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 530

530

Lanosterol 14-alpha demethylase

PRO_0000052012

Regions

Topological domain

1 – 20

Extracellular Potential

Transmembrane

21 – 41

Helical; Potential

Topological domain

42 – 530

489

Cytoplasmic Potential

Sites

Metal binding

470

Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue

458

Phosphoserine Ref.9 Ref.10

Experimental info

Sequence conflict

433

K → N in AAA34546. Ref.2

Sequence conflict

433

K → N in AAA34547. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P10614 [UniParc].

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

530

60,720

        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

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References

	« Hide 'large scale' referencesShow '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. Vaudin M. Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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, MASS SPECTROMETRY. Strain: ADR376.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, MASS SPECTROMETRY.
+	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.
PIR	A27491.
RefSeq	NP_011871.1. NM_001179137.1.
3D structure databases
ProteinModelPortal	P10614.
SMR	P10614. Positions 52-525.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-7886N.
IntAct	P10614. 66 interactions.
MINT	MINT-1325794.
STRING	4932.YHR007C.
Proteomic databases
PaxDb	P10614.
PeptideAtlas	P10614.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR007C; YHR007C; YHR007C.
GeneID	856398.
KEGG	sce:YHR007C.
Organism-specific databases
CYGD	YHR007c.
SGD	S000001049. ERG11.
Phylogenomic databases
eggNOG	COG2124.
GeneTree	ENSGT00660000095370.
HOGENOM	HOG000042780.
KO	K05917.
OMA	DFTSMVT.
OrthoDB	EOG4QJVWH.
Enzyme and pathway databases
BioCyc	MetaCyc:YHR007C-MONOMER.
UniPathway	UPA00770; UER00754.
Gene expression databases
Genevestigator	P10614.
GermOnline	YHR007C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002403. Cyt_P450_E_grp-IV. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00465. EP450IV. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00257. Clotrimazole. DB01127. Econazole. DB00196. Fluconazole. DB01026. Ketoconazole. DB01263. Posaconazole. DB01153. Sertaconazole. DB00251. Terconazole. DB01007. Tioconazole. DB00582. Voriconazole.
NextBio	981925.

Entry information

Entry name

CP51_YEAST

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VIII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents