SPO14 phospholipase D [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SPO14
Official Full Name: phospholipase D
Primary source: SGD:S000001739
Locus tag: YKR031C
See related: AllianceGenome:SGD:S000001739; FungiDB:YKR031C; VEuPathDB:YKR031C
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: PLD1
Summary: Enables phosphatidylinositol-3-phosphate binding activity and phospholipase D activity. Involved in ascospore-type prospore assembly; cell morphogenesis involved in conjugation with cellular fusion; and phospholipid metabolic process. Located in endosome; nucleus; and prospore membrane. Used to study developmental cardiac valvular defect. Human ortholog(s) of this gene implicated in developmental cardiac valvular defect. Orthologous to several human genes including PLD2 (phospholipase D2). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See SPO14 in Genome Data Viewer

Location:: chromosome: XI

Exon count:: 1

Sequence:: Chromosome: XI; NC_001143.9 (501344..506395, complement)

Chromosome XI - NC_001143.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001143.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Yeast phospholipase D, Spo14, is not required for macroautophagy.
Title: Yeast phospholipase D, Spo14, is not required for macroautophagy.
PLD-generated phosphatidic acid and phosphatidylinositol-4,5-bisphosphate collaborate to promote SNARE-mediated fusion for prospore membrane formation.
Title: Phosphatidylinositol-4,5-bisphosphate and phospholipase D-generated phosphatidic acid specify SNARE-mediated vesicle fusion for prospore membrane formation.
These findings highlight the important interactions among PLD1, Cdc42p and Ste20p during polarized cell growth in S. cerevisiae.
Title: An upstream regulator and downstream target of phospholipase D1 activity during pheromone response in Saccharomyces cerevisiae.
Taken together, these results indicate that GCS1 is essential for sporulation and suggest that GCS1 positively regulates SPO14.
Title: The Arf-GTPase-activating protein Gcs1p is essential for sporulation and regulates the phospholipase D Spo14p.
During prospore membrane growth both Spo14 and Sma1 localize to the membrane, and localization of Spo14 is independent of Sma1.
Title: Differential requirement for phospholipase D/Spo14 and its novel interactor Sma1 for regulation of exocytotic vesicle fusion in yeast meiosis.

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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 phosphatidylinositol binding	IEA Inferred from Electronic Annotation more info
enables phosphatidylinositol-3-phosphate binding	IDA Inferred from Direct Assay more info	PubMed
enables phospholipase D activity	IBA Inferred from Biological aspect of Ancestor more info
enables phospholipase D activity	IDA Inferred from Direct Assay more info	PubMed
enables phospholipase D activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in ascospore-type prospore assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cell morphogenesis involved in conjugation with cellular fusion	IGI Inferred from Genetic Interaction more info	PubMed
involved_in cell morphogenesis involved in conjugation with cellular fusion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in intracellular signal transduction	IEA Inferred from Electronic Annotation more info
involved_in lipid catabolic process	IEA Inferred from Electronic Annotation more info
involved_in meiotic cell cycle	IEA Inferred from Electronic Annotation more info
involved_in phosphatidic acid biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in phospholipid catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in phospholipid metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in phospholipid metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in sporulation resulting in formation of a cellular spore	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in endosome	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in prospore membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: phospholipase D

NP_012956.3

EC 3.1.4.4

Phospholipase D; catalyzes the hydrolysis of phosphatidylcholine, producing choline and phosphatidic acid; involved in Sec14p-independent secretion; required for meiosis and spore formation; differently regulated in secretion and meiosis; participates in transcription initiation and/or early elongation of specific genes; interacts with 'foot domain' of RNA polymerase II; deletion results in abnormal CTD-Ser5 phosphorylation of RNA polymerase II at specific promoter regions

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_001143.9 Reference assembly

Range

501344..506395 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179821.3 → NP_012956.3 TPA: phospholipase D [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012956.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VX96, P36126

UniProtKB/TrEMBL

G2WI63, N1P2N9

Conserved Domains (3) summary

PLN02866
Location:638 → 1165

PLN02866; phospholipase D

cd01254
Location:473 → 660

PH_PLD; Phospholipase D pleckstrin homology (PH) domain

cl02563
Location:300 → 390

PX_domain; The Phox Homology domain, a phosphoinositide binding module