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Protein

Lanosterol synthase

Gene

ERG7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus.

Catalytic activityi

(3S)-2,3-epoxy-2,3-dihydrosqualene = lanosterol.

Enzyme regulationi

ERG27 is required for activity.1 Publication

pH dependencei

Optimum pH is 7.1 Publication

Temperature dependencei

Optimum temperature is 35 degrees Celsius.1 Publication

Pathwayi: lanosterol biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes lanosterol from farnesyl diphosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Squalene synthase (ERG9)
  2. Squalene monooxygenase (ERG1)
  3. Lanosterol synthase (ERG7)
This subpathway is part of the pathway lanosterol biosynthesis, which is itself part of Terpene metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes lanosterol from farnesyl diphosphate, the pathway lanosterol biosynthesis and in Terpene metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei234 – 2341Proton acceptorBy similarity
Active sitei456 – 4561Proton donorBy similarity

GO - Molecular functioni

  • lanosterol synthase activity Source: SGD

GO - Biological processi

  • ergosterol biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:YHR072W-MONOMER.
YEAST:YHR072W-MONOMER.
BRENDAi5.4.99.7. 984.
ReactomeiR-SCE-191273. Cholesterol biosynthesis.
SABIO-RKP38604.
UniPathwayiUPA00767; UER00753.

Names & Taxonomyi

Protein namesi
Recommended name:
Lanosterol synthase (EC:5.4.99.7)
Alternative name(s):
2,3-epoxysqualene--lanosterol cyclase
Oxidosqualene--lanosterol cyclase
Short name:
OSC
Gene namesi
Name:ERG7
Ordered Locus Names:YHR072W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR072W.
SGDiS000001114. ERG7.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • lipid particle Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi457 – 4571C → D: Reduces thermal stability and enzyme activity; when associated with A-526 or C-526. No effect; when associated with D-526 or Q-526. 1 Publication
Mutagenesisi526 – 5261E → A or C: Reduces thermal stability and enzyme activity; when associated with D-457. 1 Publication
Mutagenesisi526 – 5261E → D or Q: No effect; when associated with D-457. 1 Publication

Chemistry

ChEMBLiCHEMBL5355.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 731730Lanosterol synthasePRO_0000072657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP38604.
PRIDEiP38604.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ERG27Q124524EBI-6572,EBI-38132

Protein-protein interaction databases

BioGridi36505. 33 interactions.
DIPiDIP-8319N.
IntActiP38604. 19 interactions.
MINTiMINT-1365031.

Chemistry

BindingDBiP38604.

Structurei

3D structure databases

ProteinModelPortaliP38604.
SMRiP38604. Positions 12-731.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati125 – 16743PFTB 1Add
BLAST
Repeati566 – 60338PFTB 2Add
BLAST
Repeati615 – 66147PFTB 3Add
BLAST

Sequence similaritiesi

Belongs to the terpene cyclase/mutase family.Curated
Contains 3 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000011570.
HOGENOMiHOG000234317.
InParanoidiP38604.
KOiK01852.
OMAiGYHIEED.
OrthoDBiEOG70610B.

Family and domain databases

Gene3Di1.50.10.20. 2 hits.
InterProiIPR032696. SQ_cyclase_C.
IPR032697. SQ_cyclase_N.
IPR018333. Squalene_cyclase.
IPR002365. Terpene_synthase_CS.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamiPF13243. SQHop_cyclase_C. 1 hit.
PF13249. SQHop_cyclase_N. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 2 hits.
TIGRFAMsiTIGR01787. squalene_cyclas. 1 hit.
PROSITEiPS01074. TERPENE_SYNTHASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38604-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEFYSDTIG LPKTDPRLWR LRTDELGRES WEYLTPQQAA NDPPSTFTQW
60 70 80 90 100
LLQDPKFPQP HPERNKHSPD FSAFDACHNG ASFFKLLQEP DSGIFPCQYK
110 120 130 140 150
GPMFMTIGYV AVNYIAGIEI PEHERIELIR YIVNTAHPVD GGWGLHSVDK
160 170 180 190 200
STVFGTVLNY VILRLLGLPK DHPVCAKARS TLLRLGGAIG SPHWGKIWLS
210 220 230 240 250
ALNLYKWEGV NPAPPETWLL PYSLPMHPGR WWVHTRGVYI PVSYLSLVKF
260 270 280 290 300
SCPMTPLLEE LRNEIYTKPF DKINFSKNRN TVCGVDLYYP HSTTLNIANS
310 320 330 340 350
LVVFYEKYLR NRFIYSLSKK KVYDLIKTEL QNTDSLCIAP VNQAFCALVT
360 370 380 390 400
LIEEGVDSEA FQRLQYRFKD ALFHGPQGMT IMGTNGVQTW DCAFAIQYFF
410 420 430 440 450
VAGLAERPEF YNTIVSAYKF LCHAQFDTEC VPGSYRDKRK GAWGFSTKTQ
460 470 480 490 500
GYTVADCTAE AIKAIIMVKN SPVFSEVHHM ISSERLFEGI DVLLNLQNIG
510 520 530 540 550
SFEYGSFATY EKIKAPLAME TLNPAEVFGN IMVEYPYVEC TDSSVLGLTY
560 570 580 590 600
FHKYFDYRKE EIRTRIRIAI EFIKKSQLPD GSWYGSWGIC FTYAGMFALE
610 620 630 640 650
ALHTVGETYE NSSTVRKGCD FLVSKQMKDG GWGESMKSSE LHSYVDSEKS
660 670 680 690 700
LVVQTAWALI ALLFAEYPNK EVIDRGIDLL KNRQEESGEW KFESVEGVFN
710 720 730
HSCAIEYPSY RFLFPIKALG MYSRAYETHT L
Length:731
Mass (Da):83,460
Last modified:July 27, 2011 - v6
Checksum:i9CE85BE1A7F5F52A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611H → N in AAA16975 (PubMed:8134375).Curated
Sequence conflicti530 – 5301N → D in AAA16975 (PubMed:8134375).Curated
Sequence conflicti530 – 5301N → D in AAB68891 (PubMed:8091229).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti359 – 731373Missing in strain: SGL9; loss of activity. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04841 Unassigned DNA. Translation: AAA16975.1.
U23488 Genomic DNA. Translation: AAA64377.1.
U60996 Genomic DNA. Translation: AAB08472.1.
U10556 Genomic DNA. Translation: AAB68891.1.
AY693043 Genomic DNA. Translation: AAT93062.1.
BK006934 Genomic DNA. Translation: DAA06765.2.
PIRiS46813.
RefSeqiNP_011939.2. NM_001179202.2.

Genome annotation databases

EnsemblFungiiYHR072W; YHR072W; YHR072W.
GeneIDi856470.
KEGGisce:YHR072W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04841 Unassigned DNA. Translation: AAA16975.1.
U23488 Genomic DNA. Translation: AAA64377.1.
U60996 Genomic DNA. Translation: AAB08472.1.
U10556 Genomic DNA. Translation: AAB68891.1.
AY693043 Genomic DNA. Translation: AAT93062.1.
BK006934 Genomic DNA. Translation: DAA06765.2.
PIRiS46813.
RefSeqiNP_011939.2. NM_001179202.2.

3D structure databases

ProteinModelPortaliP38604.
SMRiP38604. Positions 12-731.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36505. 33 interactions.
DIPiDIP-8319N.
IntActiP38604. 19 interactions.
MINTiMINT-1365031.

Chemistry

BindingDBiP38604.
ChEMBLiCHEMBL5355.

Proteomic databases

MaxQBiP38604.
PRIDEiP38604.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR072W; YHR072W; YHR072W.
GeneIDi856470.
KEGGisce:YHR072W.

Organism-specific databases

EuPathDBiFungiDB:YHR072W.
SGDiS000001114. ERG7.

Phylogenomic databases

GeneTreeiENSGT00390000011570.
HOGENOMiHOG000234317.
InParanoidiP38604.
KOiK01852.
OMAiGYHIEED.
OrthoDBiEOG70610B.

Enzyme and pathway databases

UniPathwayiUPA00767; UER00753.
BioCyciMetaCyc:YHR072W-MONOMER.
YEAST:YHR072W-MONOMER.
BRENDAi5.4.99.7. 984.
ReactomeiR-SCE-191273. Cholesterol biosynthesis.
SABIO-RKP38604.

Miscellaneous databases

PROiP38604.

Family and domain databases

Gene3Di1.50.10.20. 2 hits.
InterProiIPR032696. SQ_cyclase_C.
IPR032697. SQ_cyclase_N.
IPR018333. Squalene_cyclase.
IPR002365. Terpene_synthase_CS.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamiPF13243. SQHop_cyclase_C. 1 hit.
PF13249. SQHop_cyclase_N. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 2 hits.
TIGRFAMsiTIGR01787. squalene_cyclas. 1 hit.
PROSITEiPS01074. TERPENE_SYNTHASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, characterization, and overexpression of ERG7, the Saccharomyces cerevisiae gene encoding lanosterol synthase."
    Corey E.J., Matsuda S.P.T., Bartel B.
    Proc. Natl. Acad. Sci. U.S.A. 91:2211-2215(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 2-9.
  2. "Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae."
    Shi Z., Buntel C.J., Griffin J.H.
    Proc. Natl. Acad. Sci. U.S.A. 91:7370-7374(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Mutations in the oxidosqualene-lanosterol cyclase gene of Saccharomyces cerevisiae."
    Griffin J.H., Buntel C.J., Siregar J.J.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT 359-GLU--LEU-731 DEL.
    Strain: SGL9.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 530.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Characterization and partial purification of squalene-2,3-oxide cyclase from Saccharomyces cerevisiae."
    Balliano G., Viola F., Ceruti M., Cattel L.
    Arch. Biochem. Biophys. 293:122-129(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  9. "Yeast oxidosqualene cyclase (Erg7p) is a major component of lipid particles."
    Milla P., Athenstaedt K., Viola F., Oliaro-Bosso S., Kohlwein S.D., Daum G., Balliano G.
    J. Biol. Chem. 277:2406-2412(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "In yeast sterol biosynthesis the 3-keto reductase protein (Erg27p) is required for oxidosqualene cyclase (Erg7p) activity."
    Mo C., Milla P., Athenstaedt K., Ott R., Balliano G., Daum G., Bard M.
    Biochim. Biophys. Acta 1633:68-74(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Access of the substrate to the active site of yeast oxidosqualene cyclase: an inhibition and site-directed mutagenesis approach."
    Oliaro-Bosso S., Schulz-Gasch T., Balliano G., Viola F.
    ChemBioChem 6:2221-2228(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-457 AND GLU-526.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiERG7_YEAST
AccessioniPrimary (citable) accession number: P38604
Secondary accession number(s): D3DL21, Q92327
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 150 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2193 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.