DRS2 aminophospholipid-translocating P4-type ATPase DRS2 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: DRS2
Official Full Name: aminophospholipid-translocating P4-type ATPase DRS2
Primary source: SGD:S000000024
Locus tag: YAL026C
See related: AllianceGenome:SGD:S000000024; FungiDB:YAL026C; VEuPathDB:YAL026C
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: FUN38; SWA3
Summary: Enables phosphatidylcholine flippase activity; phosphatidylethanolamine flippase activity; and phosphatidylserine flippase activity. Involved in several processes, including endocytic recycling; phospholipid translocation; and post-Golgi vesicle-mediated transport. Located in trans-Golgi network. Part of Cdc50p-Drs2p complex. Human ortholog(s) of this gene implicated in cerebellar ataxia, impaired intellectual development, and dysequilibrium syndrome 4. Orthologous to several human genes including ATP8A2 (ATPase phospholipid transporting 8A2). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs: all
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Genomic context

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See DRS2 in Genome Data Viewer

Location:: chromosome: I

Exon count:: 1

Sequence:: Chromosome: I; NC_001133.9 (95630..99697, complement)

Chromosome I - NC_001133.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001133.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

TRAPPIII requires Drs2 binding to transport Atg9 vesicles at cold temperatures.
Title: TRAPPIII requires Drs2 binding to transport Atg9 vesicles at cold temperatures.
The P4-ATPase Drs2 interacts with and stabilizes the multisubunit tethering complex TRAPPIII in yeast.
Title: The P4-ATPase Drs2 interacts with and stabilizes the multisubunit tethering complex TRAPPIII in yeast.
The Drs2 PS flippase activity is required to support neo1Delta any1Delta viability.
Title: The PQ-loop protein Any1 segregates Drs2 and Neo1 functions required for viability and plasma membrane phospholipid asymmetry.
cryo-electron microscopy structure of the P4-ATPase Drs2p-Cdc50p; three structures are presented that represent the complex in an autoinhibited, an intermediate and a fully activated state
Title: Structure and autoregulation of a P4-ATPase lipid flippase.
activation of the Drs2p-Cdc50p flippase follows a multistep mechanism, with preliminary release of a number of constraints, possibly through the binding of regulatory proteins in the trans-Golgi network, followed by full activation by PI4P
Title: High phosphatidylinositol 4-phosphate (PI4P)-dependent ATPase activity for the Drs2p-Cdc50p flippase after removal of its N- and C-terminal extensions.
Deletion of KES1 suppresses plasma membrane-missorting defects and the accumulation of intracellular ergosterol in drs2 mutants.
Title: Phosphatidylserine translocation at the yeast trans-Golgi network regulates protein sorting into exocytic vesicles.
we describe the overexpression of a yeast lipid flippase complex, namely the P4-ATPase Drs2p and its associated subunit Cdc50p, in a coordinated manner.
Title: Coordinated Overexpression in Yeast of a P4-ATPase and Its Associated Cdc50 Subunit: The Case of the Drs2p/Cdc50p Lipid Flippase Complex.
Imh1p and Drs2p modulate the activity of Gcs1p by timing its interaction with Arl1p, hence providing feedback regulation of Arl1p activity.
Title: Mechanism of action of the flippase Drs2p in modulating GTP hydrolysis of Arl1p.
Auto-inhibition of Drs2p, a yeast phospholipid flippase, by its carboxyl-terminal tail.
Title: Auto-inhibition of Drs2p, a yeast phospholipid flippase, by its carboxyl-terminal tail.
results demonstrate that activated Arl1p can promote the spatial modulation of membrane organization at the trans-Golgi network through interacting with the effectors Gea2p and Drs2p
Title: Arl1p regulates spatial membrane organization at the trans-Golgi network through interaction with Arf-GEF Gea2p and flippase Drs2p.

Submit: New GeneRIF Correction See all GeneRIFs (20)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

NCBI Orthologs

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATPase-coupled intramembrane lipid carrier activity	EXP Inferred from Experiment more info	PubMed
enables ATPase-coupled intramembrane lipid carrier activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATPase-coupled intramembrane lipid carrier activity	IEA Inferred from Electronic Annotation more info
enables magnesium ion binding	IEA Inferred from Electronic Annotation more info
enables nucleotide binding	IEA Inferred from Electronic Annotation more info
enables phosphatidylcholine flippase activity	IGI Inferred from Genetic Interaction more info	PubMed
enables phosphatidylethanolamine flippase activity	IGI Inferred from Genetic Interaction more info	PubMed
enables phosphatidylethanolamine flippase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables phosphatidylinositol-4-phosphate binding	IDA Inferred from Direct Assay more info	PubMed
enables phosphatidylserine flippase activity	IDA Inferred from Direct Assay more info	PubMed
enables phosphatidylserine flippase activity	IEA Inferred from Electronic Annotation more info
enables phosphatidylserine flippase activity	IGI Inferred from Genetic Interaction more info	PubMed
enables phosphatidylserine flippase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables phosphatidylserine floppase activity	EXP Inferred from Experiment more info	PubMed
enables phosphatidylserine floppase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in aminophospholipid translocation	IEA Inferred from Electronic Annotation more info
involved_in endocytic recycling	IBA Inferred from Biological aspect of Ancestor more info
involved_in endocytic recycling	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in endocytosis	IGI Inferred from Genetic Interaction more info	PubMed
involved_in phospholipid translocation	IBA Inferred from Biological aspect of Ancestor more info
involved_in phospholipid translocation	IDA Inferred from Direct Assay more info	PubMed
involved_in phospholipid translocation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in phospholipid translocation	NAS Non-traceable Author Statement more info	PubMed
involved_in phospholipid transport	IEA Inferred from Electronic Annotation more info
involved_in post-Golgi vesicle-mediated transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in post-Golgi vesicle-mediated transport	IGI Inferred from Genetic Interaction more info	PubMed
involved_in post-Golgi vesicle-mediated transport	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of Cdc50p-Drs2p complex	IPI Inferred from Physical Interaction more info	PubMed
located_in Golgi apparatus	IEA Inferred from Electronic Annotation more info
located_in endoplasmic reticulum	HDA more info	PubMed
located_in endosome membrane	EXP Inferred from Experiment more info	PubMed
located_in endosome membrane	IEA Inferred from Electronic Annotation more info
located_in membrane	IEA Inferred from Electronic Annotation more info
part_of phospholipid-translocating ATPase complex	NAS Non-traceable Author Statement more info	PubMed
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
is_active_in trans-Golgi network	IBA Inferred from Biological aspect of Ancestor more info
located_in trans-Golgi network	IDA Inferred from Direct Assay more info	PubMed
located_in trans-Golgi network	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: aminophospholipid-translocating P4-type ATPase DRS2

NP_009376.2

EC 7.6.2.1

Trans-golgi network aminophospholipid translocase (flippase); P4-type ATPase; maintains membrane lipid asymmetry in post-Golgi secretory vesicles; contributes to clathrin-coated vesicle formation, endocytosis, protein trafficking between the Golgi and endosomal system and the cellular response to mating pheromone; autoinhibited by its C-terminal tail; localizes to the trans-Golgi network

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_001133.9 Reference assembly

Range

95630..99697 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178171.2 → NP_009376.2 aminophospholipid-translocating P4-type ATPase DRS2

See identical proteins and their annotated locations for NP_009376.2

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VPJ2, P39524

UniProtKB/TrEMBL

B3LUW0, C8Z3K1, N1P9T3

Conserved Domains (1) summary

TIGR01652
Location:198 → 1240

ATPase-Plipid; phospholipid-translocating P-type ATPase, flippase