AYR1 acylglycerone-phosphate reductase [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: AYR1
Official Full Name: acylglycerone-phosphate reductase
Primary source: SGD:S000001386
Locus tag: YIL124W
See related: AllianceGenome:SGD:S000001386; FungiDB:YIL124W; VEuPathDB:YIL124W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: GBG1
Summary: Enables acylglycerone-phosphate reductase (NADP+) activity and triacylglycerol lipase activity. Involved in phosphatidic acid biosynthetic process and triglyceride catabolic process. Located in endoplasmic reticulum and lipid droplet. [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See AYR1 in Genome Data Viewer

Location:: chromosome: IX

Exon count:: 1

Sequence:: Chromosome: IX; NC_001141.2 (126204..127097)

Chromosome IX - NC_001141.2 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001141.2

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

short-chain dehydrogenase-related protein Ayr1 forms an NADPH-regulated channel in the outer mitochondrial membrane.
Title: Identification of new channels by systematic analysis of the mitochondrial outer membrane.
Study demonstrate that Rpa12p interacts with the transcription factor Msn4p and prevents its binding to the promoter of AYR1, a key enzyme involved in triacylglycerol biosynthesis and mobilization of nonpolar lipids. These results suggest that the deletion of RPA12 derepresses Msn4p, thus activating the transcription of AYR1, which leads to the accumulation of triacylglycerol in the rpa12D mutant.
Title: The RNA polymerase I subunit Rpa12p interacts with the stress-responsive transcription factor Msn4p to regulate lipid metabolism in budding yeast.
Ayr1p as a novel triacylglycerol lipase in Saccharomyces cerevisiae
Title: Screening for hydrolytic enzymes reveals Ayr1p as a novel triacylglycerol lipase in Saccharomyces cerevisiae.

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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 acylglycerone-phosphate reductase (NADP+) activity	IBA Inferred from Biological aspect of Ancestor more info
enables acylglycerone-phosphate reductase (NADP+) activity	IEA Inferred from Electronic Annotation more info
enables acylglycerone-phosphate reductase (NADP+) activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables triacylglycerol lipase activity	IBA Inferred from Biological aspect of Ancestor more info
enables triacylglycerol lipase activity	IDA Inferred from Direct Assay more info	PubMed
enables triacylglycerol lipase activity	IEA Inferred from Electronic Annotation more info
enables triacylglycerol lipase activity	IGI Inferred from Genetic Interaction more info	PubMed
enables triacylglycerol lipase activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in lipid catabolic process	IEA Inferred from Electronic Annotation more info
involved_in phosphatidic acid biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in phosphatidic acid biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in triglyceride catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in triglyceride catabolic process	IGI Inferred from Genetic Interaction more info	PubMed

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

General protein information

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Preferred Names: acylglycerone-phosphate reductase

NP_012142.3

EC 1.1.1.101

EC 3.1.1.3

Bifunctional triacylglycerol lipase and 1-acyl DHAP reductase; NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase involved in phosphatidic acid biosynthesis; lipid droplet triacylglycerol lipase involved in mobilization of non-polar lipids; found in lipid particles, endoplasmic reticulum and mitochondrial outer membrane; forms NADPH-regulated channel in mitochondrial outer membrane; required for spore germination; role in cell wall biosynthesis; capable of metabolizing steroid hormones

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_001141.2 Reference assembly

Range

126204..127097

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179472.3 → NP_012142.3 TPA: acylglycerone-phosphate reductase [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012142.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VVG3, P40471

UniProtKB/TrEMBL

A6ZVF2, B3LTX1, C8ZAY9, E9P9B4, G2WG27, N1P0V1

Conserved Domains (1) summary

cd05374
Location:10 → 256

17beta-HSD-like_SDR_c; 17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs