Reviewed, UniProtKB/Swiss-Prot P10614 (CP51_YEAST)

Names and origin

Protein names

Recommended name:
    Cytochrome P450 51
    EC=1.14.13.70
Alternative name(s):
    CYPLI
    P450-LIA1
    Sterol 14-alpha demethylase
    Lanosterol 14-alpha demethylase
    P450-14DM

Gene names

Name:	ERG11
Synonyms:	CYP51
Ordered Locus Names:	YHR007C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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	Obtusifoliol + 3 O(2) + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP(+) + 4 H(2)O.
Cofactor	Heme group By similarity.
Pathway	Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6.
Subunit structure	Interacts with ERG28.
Subcellular location	Membrane; Multi-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 synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Membrane
Domain	Transmembrane
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from direct assay. 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 electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 530	530	Cytochrome P450 51		PRO_0000052012
Regions
	Topological domain	1 – 20	20	Extracellular Potential
	Transmembrane	21 – 41	21	Potential
	Topological domain	42 – 530	489	Cytoplasmic Potential
Sites
	Metal binding	470	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Modified residue	458	1	Phosphoserine
Experimental info
	Sequence conflict	433	1	K → N in AAA34546 and AAA34547. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P10614-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 646960BBA0E17979	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

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: 3322742] [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: 3046615] [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. , 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: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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: 3542713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-530.
[5]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex." Mo C., Bard M. J. Lipid Res. 46:1991-1998(2005) [PubMed: 15995173] [Abstract] Cited for: INTERACTION WITH ERG28.
[7]	"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: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
[8]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, MASS SPECTROMETRY.
[9]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	A27491.
RefSeq	NP_011871.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:7886N.
IntAct	P10614.
Proteomic databases
PeptideAtlas	P10614.
Genome annotation databases
Ensembl	YHR007C. Saccharomyces cerevisiae. [Contig view]
GeneID	856398.
GenomeReviews	Gene locus YHR007C in contig U00093_GR.
KEGG	sce:YHR007C.
NMPDR	fig|4932.3.peg.3015.
Organism-specific databases
CYGD	YHR007c.
SGD	S000001049. ERG11.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P10614.
Enzyme and pathway databases
BioCyc	MetaCyc:YHR007C-MON.
Gene expression databases
ArrayExpress	P10614.
GermOnline	YHR007C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR002403. Cyt_P450_E_grp-IV. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00465. EP450IV. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00257. Clotrimazole. DB01127. Econazole. DB00196. Fluconazole. DB01026. Ketoconazole. DB01263. Posaconazole. DB01153. Sertaconazole. DB00251. Terconazole. DB01007. Tioconazole. DB00582. Voriconazole.
LinkHub	P10614.
NextBio	981925.

Entry information

Entry name

CP51_YEAST

Accession

Primary (citable) accession number: P10614

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	November 25, 2008
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)