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ERG7 - lanosterol synthase ERG7 (Saccharomyces cerevisiae S288C)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-02
Description
Enables lanosterol synthase activity. Involved in ergosterol biosynthetic process. Located in lipid droplet. Human ortholog(s) of this gene implicated in alopecia-mental retardation syndrome 4; cataract; cataract 44; and hypotrichosis 14. Orthologous to human LSS (lanosterol synthase).

1 Names and Identifiers

1.1 Other Identifiers

1.1.1 Alliance Gene ID

1.1.2 Enzyme Commission (EC) Number

1.1.3 SGD ID

1.1.4 VEuPathDB ID

1.1.5 Wikidata

2 Proteins

2.1 Protein Function

Lanosterol synthase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PMID: 12842197, PMID: 16235265, PMID: 1731628). ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core (PMID: 12842197, PMID: 1731628). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PMID: 32679672).

2.2 Protein 3D Structures

2.2.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

2.3 Protein Targets

3 Chemicals and Bioactivities

3.1 Tested Compounds

4 BioAssays

4.1 Small-Molecule BioAssays

5 Interactions and Pathways

5.1 Interactions

5.2 Pathways

6 Biochemical Reactions

7 Expression

8 Literature

8.1 Consolidated References

9 Classification

9.1 Gene Ontology: Biological Process

9.2 Gene Ontology: Cellular Component

9.3 Gene Ontology: Molecular Function

9.4 ChEMBL Target Tree

9.5 Enzyme Classification

10 Information Sources

  1. NCBI Gene
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. Alliance of Genome Resources
    LICENSE
    All annotations and data produced by Alliance members that are accessible from alliancegenome.org are distributed under a CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
    https://www.alliancegenome.org/privacy-warranty-licensing
  4. BioGRID
    LICENSE
    The MIT License (MIT); Copyright Mike Tyers Lab
    https://wiki.thebiogrid.org/doku.php/terms_and_conditions
  5. Database of Interacting Proteins (DIP)
    LICENSE
    All DIP database records available under the terms set by the Creative Commons Attribution-NoDerivs License.
    https://dip.doe-mbi.ucla.edu/dip/termsofuse.html
  6. STRING: functional protein association networks
  7. NCBI Gene Expression Omnibus (GEO)
  8. Saccharomyces Genome Database (SGD)
    LICENSE
    SGD operates under the Creative Commons Attribution 4.0 International license (CC BY 4.0).
    https://sites.google.com/view/yeastgenome-help/about
  9. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  10. VEuPathDB: The Eukaryotic Pathogen, Vector and Host Informatics Resource
    LICENSE
    All data on VEuPathDB websites are provided freely for public use.
    https://veupathdb.org/veupathdb/app/static-content/about.html
  11. Wikidata
  12. ChEMBL
    LICENSE
    Access to the web interface of ChEMBL is made under the EBI's Terms of Use (http://www.ebi.ac.uk/Information/termsofuse.html). The ChEMBL data is made available on a Creative Commons Attribution-Share Alike 3.0 Unported License (http://creativecommons.org/licenses/by-sa/3.0/).
    http://www.ebi.ac.uk/Information/termsofuse.html
  13. Swiss Institute of Bioinformatics ENZYME
    LICENSE
    Copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution (CC BY 4.0) License (https://creativecommons.org/licenses/by/4.0/).
    https://enzyme.expasy.org/enzyme.get
    Enzyme Classification
    https://enzyme.expasy.org/
  14. Gene Ontology (GO)
    LICENSE
    Gene Ontology Consortium data and data products are licensed under the Creative Commons Attribution 4.0 Unported License (https://creativecommons.org/licenses/by/4.0/legalcode)
    http://geneontology.org/docs/go-citation-policy/
  15. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
  16. Rhea - annotated reactions database
    LICENSE
    Rhea has chosen to apply the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). This means that you are free to copy, distribute, display and make commercial use of the database in all legislations, provided you credit (cite) Rhea.
    https://www.rhea-db.org/help/license-disclaimer
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