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Protein

Lanosterol 14-alpha demethylase

Gene

ERG11

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

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.1 Publication

Catalytic activityi

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

Cofactori

hemeBy similarity

Pathwayi: zymosterol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes zymosterol from lanosterol.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Lanosterol 14-alpha demethylase (ERG11)
  2. Delta(14)-sterol reductase (ERG24)
  3. Methylsterol monooxygenase (ERG25)
  4. Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (ERG26)
  5. 3-keto-steroid reductase (ERG27)
  6. no protein annotated in this organism
This subpathway is part of the pathway zymosterol biosynthesis, which is itself part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes zymosterol from lanosterol, the pathway zymosterol biosynthesis and in Steroid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi470Iron (heme axial ligand)By similarity1

GO - Molecular functioni

  • heme binding Source: InterPro
  • iron ion binding Source: InterPro
  • sterol 14-demethylase activity Source: SGD

GO - Biological processi

  • ergosterol biosynthetic process Source: SGD

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandHeme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:YHR007C-MONOMER
YEAST:YHR007C-MONOMER
ReactomeiR-SCE-191273 Cholesterol biosynthesis
R-SCE-211976 Endogenous sterols
UniPathwayiUPA00770; UER00754

Names & Taxonomyi

Protein namesi
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 namesi
Name:ERG11
Synonyms:CYP51
Ordered Locus Names:YHR007C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR007C
SGDiS000001049 ERG11

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 20ExtracellularSequence analysisAdd BLAST20
Transmembranei21 – 41HelicalSequence analysisAdd BLAST21
Topological domaini42 – 530CytoplasmicSequence analysisAdd BLAST489

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

DrugBankiDB06890 (2R)-2-PHENYL-N-PYRIDIN-4-YLBUTANAMIDE
DB07572 3-{[(4-methylphenyl)sulfonyl]amino}propyl pyridin-4-ylcarbamate
DB07635 bis(4-hydroxyphenyl)methanone
DB07569 CIS-4-METHYL-N-[(1S)-3-(METHYLSULFANYL)-1-(PYRIDIN-4-YLCARBAMOYL)PROPYL]CYCLOHEXANECARBOXAMIDE
DB07560 N-[(1S)-2-methyl-1-(pyridin-4-ylcarbamoyl)propyl]cyclohexanecarboxamide

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000520121 – 530Lanosterol 14-alpha demethylaseAdd BLAST530

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki454Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei458PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP10614
PaxDbiP10614
PRIDEiP10614
TopDownProteomicsiP10614

PTM databases

iPTMnetiP10614

Interactioni

Subunit structurei

Interacts with ERG28.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ERG25P530453EBI-5127,EBI-6506

Protein-protein interaction databases

BioGridi36434, 484 interactors
DIPiDIP-7886N
IntActiP10614, 73 interactors
MINTiP10614
STRINGi4932.YHR007C

Structurei

Secondary structure

1530
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 23Combined sources15
Helixi27 – 49Combined sources23
Beta strandi53 – 55Combined sources3
Turni64 – 66Combined sources3
Helixi69 – 74Combined sources6
Helixi76 – 87Combined sources12
Beta strandi89 – 95Combined sources7
Beta strandi98 – 103Combined sources6
Helixi105 – 113Combined sources9
Turni117 – 119Combined sources3
Helixi122 – 134Combined sources13
Helixi144 – 155Combined sources12
Helixi160 – 180Combined sources21
Turni182 – 184Combined sources3
Turni186 – 188Combined sources3
Beta strandi190 – 195Combined sources6
Helixi196 – 212Combined sources17
Helixi215 – 220Combined sources6
Helixi225 – 234Combined sources10
Helixi238 – 242Combined sources5
Helixi249 – 274Combined sources26
Beta strandi280 – 282Combined sources3
Helixi283 – 289Combined sources7
Helixi301 – 331Combined sources31
Helixi334 – 347Combined sources14
Helixi349 – 351Combined sources3
Helixi357 – 360Combined sources4
Helixi364 – 376Combined sources13
Beta strandi383 – 387Combined sources5
Beta strandi405 – 408Combined sources4
Helixi410 – 413Combined sources4
Turni417 – 419Combined sources3
Turni421 – 424Combined sources4
Helixi428 – 431Combined sources4
Beta strandi444 – 449Combined sources6
Beta strandi451 – 454Combined sources4
Helixi466 – 468Combined sources3
Helixi473 – 490Combined sources18
Beta strandi491 – 494Combined sources4
Beta strandi507 – 510Combined sources4
Beta strandi518 – 525Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LXJX-ray1.90A1-530[»]
5EQBX-ray2.19A1-530[»]
ProteinModelPortaliP10614
SMRiP10614
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00910000144280
HOGENOMiHOG000042780
InParanoidiP10614
KOiK05917
OMAiAPIHSIM
OrthoDBiEOG092C1MV8

Family and domain databases

Gene3Di1.10.630.10, 1 hit
InterProiView protein in InterPro
IPR001128 Cyt_P450
IPR017972 Cyt_P450_CS
IPR002403 Cyt_P450_E_grp-IV
IPR036396 Cyt_P450_sf
PfamiView protein in Pfam
PF00067 p450, 1 hit
PRINTSiPR00465 EP450IV
PR00385 P450
SUPFAMiSSF48264 SSF48264, 1 hit
PROSITEiView protein in PROSITE
PS00086 CYTOCHROME_P450, 1 hit

Sequencei

Sequence statusi: Complete.

P10614-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATKSIVGE ALEYVNIGLS HFLALPLAQR ISLIIIIPFI YNIVWQLLYS
60 70 80 90 100
LRKDRPPLVF YWIPWVGSAV VYGMKPYEFF EECQKKYGDI FSFVLLGRVM
110 120 130 140 150
TVYLGPKGHE FVFNAKLADV SAEAAYAHLT TPVFGKGVIY DCPNSRLMEQ
160 170 180 190 200
KKFVKGALTK EAFKSYVPLI AEEVYKYFRD SKNFRLNERT TGTIDVMVTQ
210 220 230 240 250
PEMTIFTASR SLLGKEMRAK LDTDFAYLYS DLDKGFTPIN FVFPNLPLEH
260 270 280 290 300
YRKRDHAQKA ISGTYMSLIK ERRKNNDIQD RDLIDSLMKN STYKDGVKMT
310 320 330 340 350
DQEIANLLIG VLMGGQHTSA ATSAWILLHL AERPDVQQEL YEEQMRVLDG
360 370 380 390 400
GKKELTYDLL QEMPLLNQTI KETLRMHHPL HSLFRKVMKD MHVPNTSYVI
410 420 430 440 450
PAGYHVLVSP GYTHLRDEYF PNAHQFNIHR WNKDSASSYS VGEEVDYGFG
460 470 480 490 500
AISKGVSSPY LPFGGGRHRC IGEHFAYCQL GVLMSIFIRT LKWHYPEGKT
510 520 530
VPPPDFTSMV TLPTGPAKII WEKRNPEQKI
Length:530
Mass (Da):60,720
Last modified:July 1, 1989 - v1
Checksum:i646960BBA0E17979
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti433K → N in AAA34546 (PubMed:3046615).Curated1
Sequence conflicti433K → N in AAA34547 (PubMed:3046615).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiA27491
RefSeqiNP_011871.1, NM_001179137.1

Genome annotation databases

EnsemblFungiiYHR007C; YHR007C; YHR007C
GeneIDi856398
KEGGisce:YHR007C

Similar proteinsi

Entry informationi

Entry nameiCP51_YEAST
AccessioniPrimary (citable) accession number: P10614
Secondary accession number(s): D3DKV1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 23, 2018
This is version 178 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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