LDH1 triacylglycerol lipase [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: LDH1
Official Full Name: triacylglycerol lipase
Primary source: SGD:S000000408
Locus tag: YBR204C
See related: AllianceGenome:SGD:S000000408; FungiDB:YBR204C; VEuPathDB:YBR204C
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 triacylglycerol lipase activity. Involved in lipid homeostasis. Located in lipid droplet. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See LDH1 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (632254..633381, complement)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Ldh1p is thought to play a role in maintaining the lipid homeostasis in yeast by regulating both phospholipid and nonpolar lipid levels
Title: Involvement of the Saccharomyces cerevisiae hydrolase Ldh1p in lipid homeostasis.
Ldh1p is not required for the function and biogenesis of peroxisomes, and targeting of Ldh1p to lipid droplets occurs independently of the PTS1 receptor Pex5p. [Ldh1p]
Title: The putative Saccharomyces cerevisiae hydrolase Ldh1p is localized to lipid droplets.

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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 hydrolase activity	IEA Inferred from Electronic Annotation more info
enables hydrolase activity, acting on ester bonds	IDA Inferred from Direct Assay more info	PubMed
enables monoacylglycerol lipase activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine hydrolase activity	HDA more info	PubMed
enables triacylglycerol lipase activity	IDA Inferred from Direct Assay more info	PubMed
enables triacylglycerol lipase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in acylglycerol catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in lipid catabolic process	IEA Inferred from Electronic Annotation more info
involved_in lipid homeostasis	IMP Inferred from Mutant Phenotype more info	PubMed

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

General protein information

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Preferred Names: triacylglycerol lipase

NP_009763.2

EC 3.1.1.3

Serine hydrolase; exhibits active esterase plus weak triacylglycerol lipase activities; proposed role in lipid homeostasis, regulating phospholipid and non-polar lipid levels and required for mobilization of LD-stored lipids; localizes to the lipid droplet (LD) surface; contains a classical serine containing catalytic triad (GxSxG motif)

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_001134.8 Reference assembly

Range

632254..633381 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178552.2 → NP_009763.2 TPA: triacylglycerol lipase [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009763.2

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VQK2, P38139

UniProtKB/TrEMBL

A6ZLE6, C7GKG7, G2W9K9, N1PAV0

Conserved Domains (1) summary

COG1075
Location:4 → 375

EstA; Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism]