SLM1 phosphatidylinositol 4,5-bisphosphate-binding protein [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: SLM1
Gene description: phosphatidylinositol 4,5-bisphosphate-binding protein
Primary source: FungiDB:YIL105C
Locus tag: YIL105C
See related: SGD:S000001367; AllianceGenome:SGD:S000001367; VEuPathDB:YIL105C
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: LIT2
Summary: Enables phosphatidylinositol-4,5-bisphosphate binding activity and sphingolipid binding activity. Involved in several processes, including TOR signaling; actin cytoskeleton organization; and eisosome assembly. Located in plasma membrane. Colocalizes with eisosome. [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See SLM1 in Genome Data Viewer

Location:: chromosome: IX

Exon count:: 1

Sequence:: Chromosome: IX; NC_001141.2 (167581..169641, complement)

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?

Plasma membrane tension regulates eisosome structure and function.
Title: Plasma membrane tension regulates eisosome structure and function.
Slm1/Slm2 and TORC2-dependent phosphorylation of Ypk1 is coupled to the biosynthesis of complex sphingolipids and to their levels within the plasma membrane.
Title: Plasma membrane proteins Slm1 and Slm2 mediate activation of the AGC kinase Ypk1 by TORC2 and sphingolipids in S. cerevisiae.
Slm proteins are required for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae.
Title: Requirements of Slm proteins for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae.
Slm proteins are subject to regulation by multiple signals, including PI4,5P(2), TORC2, and sphingolipids, and may thus integrate inputs from different signaling pathways to temporally and spatially control actin polarization
Title: The yeast PH domain proteins Slm1 and Slm2 are targets of sphingolipid signaling during the response to heat stress.
Slm1 and Slm2 integrate inputs from the Phosphatidylinositol-4,5-bisphosphate and TORC2 to modulate polarized actin assembly and growth
Title: The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2.
Data suggest that Slm1 and Slm2 define a molecular link between phosphoinositide and sphingolipid signaling and thereby regulate actin cytoskeleton organization.
Title: The phosphatidylinositol 4,5-biphosphate and TORC2 binding proteins Slm1 and Slm2 function in sphingolipid regulation.
calcineurin may modulate sphingolipid-dependent events through regulation of Slm1 and Slm2
Title: Slm1 and slm2 are novel substrates of the calcineurin phosphatase required for heat stress-induced endocytosis of the yeast uracil permease.

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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 phosphatidylinositol-4,5-bisphosphate binding	IDA Inferred from Direct Assay more info	PubMed
enables sphingolipid binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in TOR signaling	IPI Inferred from Physical Interaction more info	PubMed
involved_in actin cytoskeleton organization	IGI Inferred from Genetic Interaction more info	PubMed
involved_in actin filament bundle assembly	IGI Inferred from Genetic Interaction more info	PubMed
involved_in eisosome assembly	IGI Inferred from Genetic Interaction more info	PubMed
involved_in endosomal transport	IGI Inferred from Genetic Interaction more info	PubMed
involved_in establishment or maintenance of actin cytoskeleton polarity	IPI Inferred from Physical Interaction more info	PubMed
involved_in protein localization to plasma membrane	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of cell growth	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of cell growth	IPI Inferred from Physical Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in mitochondrion	HDA more info	PubMed
located_in plasma membrane	HDA more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: phosphatidylinositol 4,5-bisphosphate-binding protein

NP_012161.1

Phosphoinositide PI4,5P(2) binding protein, forms a complex with Slm2p; acts downstream of Mss4p in a pathway regulating actin cytoskeleton organization in response to stress; TORC2 complex substrate and effector; protein abundance increases in response to DNA replication stress; SLM1 has a paralog, SLM2, that arose from the whole genome duplication

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

167581..169641 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179453.1 → NP_012161.1 TPA: phosphatidylinositol 4,5-bisphosphate-binding protein [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012161.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VVI2, P40485

UniProtKB/TrEMBL

A0A8H4C0S3, B3LTV2, B5VKK5, C7GKN1

Conserved Domains (1) summary

cd13311
Location:467 → 581

PH_Slm1; Slm1 Pleckstrin homology (PH) domain