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P10614

- CP51_YEAST

UniProt

P10614 - CP51_YEAST

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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: 5 out of 5- 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.

Catalytic activityi

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

Cofactori

hemeBy similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi470 – 4701Iron (heme axial ligand)By similarity

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. sterol 14-demethylase activity Source: SGD

GO - Biological processi

  1. demethylation Source: GOC
  2. ergosterol biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:YHR007C-MONOMER.
YEAST:YHR007C-MONOMER.
ReactomeiREACT_243755. Endogenous sterols.
REACT_253879. Cholesterol biosynthesis.
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
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

CYGDiYHR007c.
SGDiS000001049. ERG11.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020ExtracellularSequence AnalysisAdd
BLAST
Transmembranei21 – 4121HelicalSequence AnalysisAdd
BLAST
Topological domaini42 – 530489CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530Lanosterol 14-alpha demethylasePRO_0000052012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei458 – 4581Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP10614.
PaxDbiP10614.
PeptideAtlasiP10614.

Expressioni

Gene expression databases

GenevestigatoriP10614.

Interactioni

Subunit structurei

Interacts with ERG28.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi36434. 239 interactions.
DIPiDIP-7886N.
IntActiP10614. 68 interactions.
MINTiMINT-1325794.
STRINGi4932.YHR007C.

Structurei

Secondary structure

1
530
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 2315Combined sources
Helixi27 – 4923Combined sources
Beta strandi53 – 553Combined sources
Turni64 – 663Combined sources
Helixi69 – 746Combined sources
Helixi76 – 8712Combined sources
Beta strandi89 – 957Combined sources
Beta strandi98 – 1036Combined sources
Helixi105 – 1139Combined sources
Turni117 – 1193Combined sources
Helixi122 – 13413Combined sources
Helixi144 – 15512Combined sources
Helixi160 – 18021Combined sources
Turni182 – 1843Combined sources
Turni186 – 1883Combined sources
Beta strandi190 – 1956Combined sources
Helixi196 – 21217Combined sources
Helixi215 – 2206Combined sources
Helixi225 – 23410Combined sources
Helixi238 – 2425Combined sources
Helixi249 – 27426Combined sources
Beta strandi280 – 2823Combined sources
Helixi283 – 2897Combined sources
Helixi301 – 33131Combined sources
Helixi334 – 34714Combined sources
Helixi349 – 3513Combined sources
Helixi357 – 3604Combined sources
Helixi364 – 37613Combined sources
Beta strandi383 – 3875Combined sources
Beta strandi405 – 4084Combined sources
Helixi410 – 4134Combined sources
Turni417 – 4193Combined sources
Turni421 – 4244Combined sources
Helixi428 – 4314Combined sources
Beta strandi444 – 4496Combined sources
Beta strandi451 – 4544Combined sources
Helixi466 – 4683Combined sources
Helixi473 – 49018Combined sources
Beta strandi491 – 4944Combined sources
Beta strandi507 – 5104Combined sources
Beta strandi518 – 5258Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LXJX-ray1.90A1-530[»]
ProteinModelPortaliP10614.
SMRiP10614. Positions 6-530.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00660000095370.
HOGENOMiHOG000042780.
InParanoidiP10614.
KOiK05917.
OMAiDFTSMVT.
OrthoDBiEOG7712HB.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00465. EP450IV.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti433 – 4331K → N in AAA34546. (PubMed:3046615)Curated
Sequence conflicti433 – 4331K → N in AAA34547. (PubMed:3046615)Curated

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.

Cross-referencesi

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 .
PIRi A27491.
RefSeqi NP_011871.1. NM_001179137.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4LXJ X-ray 1.90 A 1-530 [» ]
ProteinModelPortali P10614.
SMRi P10614. Positions 6-530.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36434. 239 interactions.
DIPi DIP-7886N.
IntActi P10614. 68 interactions.
MINTi MINT-1325794.
STRINGi 4932.YHR007C.

Proteomic databases

MaxQBi P10614.
PaxDbi P10614.
PeptideAtlasi P10614.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YHR007C ; YHR007C ; YHR007C .
GeneIDi 856398.
KEGGi sce:YHR007C.

Organism-specific databases

CYGDi YHR007c.
SGDi S000001049. ERG11.

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00660000095370.
HOGENOMi HOG000042780.
InParanoidi P10614.
KOi K05917.
OMAi DFTSMVT.
OrthoDBi EOG7712HB.

Enzyme and pathway databases

UniPathwayi UPA00770 ; UER00754 .
BioCyci MetaCyc:YHR007C-MONOMER.
YEAST:YHR007C-MONOMER.
Reactomei REACT_243755. Endogenous sterols.
REACT_253879. Cholesterol biosynthesis.

Miscellaneous databases

NextBioi 981925.
PROi P10614.

Gene expression databases

Genevestigatori P10614.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00465. EP450IV.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. 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. 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].

Entry informationi

Entry nameiCP51_YEAST
AccessioniPrimary (citable) accession number: P10614
Secondary accession number(s): D3DKV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3