ERG7 lanosterol synthase ERG7 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: ERG7
Official Full Name: lanosterol synthase ERG7
Primary source: SGD:S000001114
Locus tag: YHR072W
See related: AllianceGenome:SGD:S000001114; FungiDB:YHR072W; VEuPathDB:YHR072W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: 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). [provided by Alliance of Genome Resources, Oct 2024]
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Genomic context

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See ERG7 in Genome Data Viewer

Location:: chromosome: VIII

Exon count:: 1

Sequence:: Chromosome: VIII; NC_001140.6 (239098..241293)

Chromosome VIII - NC_001140.6 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001140.6

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

A bicyclic intermediate with two altered deprotonation products, in conjunction with lanosterol, were isolated from the ERG7(Y707X) mutants
Title: Importance of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase tyrosine 707 residue for chair-boat bicyclic ring formation and deprotonation reactions.
This study provides new insights into the role of Erg27p in sterol biosynthesis.
Title: Genetic analyses involving interactions between the ergosterol biosynthetic enzymes, lanosterol synthase (Erg7p) and 3-ketoreductase (Erg27p), in the yeast Saccharomyces cerevisiae.
The Lanosterol synthase and cycloartenol synthase are a critical component of the catalytic distinction Oxidosqualene cyclase second-sphere residues.
Title: Oxidosqualene cyclase second-sphere residues profoundly influence the product profile.
Site-saturated mutagenesis experiments were carried out on the His234 residue of ERG7 to characterize its functional role in ERG7 activity and to determine its effect on the oxidosqualene cyclization/rearrangement reaction.
Title: Site-saturated mutagenesis of histidine 234 of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase demonstrates dual functions in cyclization and rearrangement reactions.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables intramolecular transferase activity	IEA Inferred from Electronic Annotation more info
enables isomerase activity	IEA Inferred from Electronic Annotation more info
enables lanosterol synthase activity	IBA Inferred from Biological aspect of Ancestor more info
enables lanosterol synthase activity	IDA Inferred from Direct Assay more info	PubMed
enables lanosterol synthase activity	IEA Inferred from Electronic Annotation more info
enables lanosterol synthase activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in ergosterol biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in ergosterol biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in ergosterol biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in lipid biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in sterol biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in triterpenoid biosynthetic process	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
located_in endoplasmic reticulum membrane	IEA Inferred from Electronic Annotation more info
is_active_in lipid droplet	IBA Inferred from Biological aspect of Ancestor more info
located_in lipid droplet	IDA Inferred from Direct Assay more info	PubMed
located_in lipid droplet	IEA Inferred from Electronic Annotation more info
located_in membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: lanosterol synthase ERG7

NP_011939.2

EC 5.4.99.7

Lanosterol synthase; an essential enzyme that catalyzes the cyclization of squalene 2,3-epoxide, a step in ergosterol biosynthesis; human LSS functionally complements the lethality of the erg7 null mutation

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001140.6 Reference assembly

Range

239098..241293

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179202.2 → NP_011939.2 TPA: lanosterol synthase ERG7 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_011939.2

Status: REVIEWED

UniProtKB/Swiss-Prot

D3DL21, P38604, Q92327

UniProtKB/TrEMBL

A6ZSX8, B5VK00, C7GWT3, G2WFE4, N1P9D7

Conserved Domains (1) summary

cd02892
Location:77 → 722

SQCY_1; Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization ...