MCA1 Ca(2+)-dependent cysteine protease MCA1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: MCA1
Gene description: Ca(2+)-dependent cysteine protease MCA1
Primary source: FungiDB:YOR197W
Locus tag: YOR197W
See related: SGD:S000005723; AllianceGenome:SGD:S000005723; VEuPathDB:YOR197W
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: YCA1
Summary: Enables calcium-dependent cysteine-type endopeptidase activity. Involved in apoptotic process and protein quality control for misfolded or incompletely synthesized proteins. Located in cytosol and nucleus. [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See MCA1 in Genome Data Viewer

Location:: chromosome: XV

Exon count:: 1

Sequence:: Chromosome: XV; NC_001147.6 (717086..718384)

Chromosome XV - NC_001147.6 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001147.6

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Yca1 metacaspase: diverse functions determine how yeast live and let die.
Title: Yca1 metacaspase: diverse functions determine how yeast live and let die.
The polyunsaturated fatty acid-producing strain also showed great increase in metacaspase Yca1p activity, suggesting cells could die by caspase-mediated cell death.
Title: PUFA-induced cell death is mediated by Yca1p-dependent and -independent pathways, and is reduced by vitamin C in yeast.
The yeast metacaspase regulates both proteolytic activities through the ubiquitin-proteasome system and ceramide metabolism as revealed by proteome and metabolome profiling of YCA1-knock-out cells during acetic-acid induced programmed cell death.
Title: Proteome and metabolome profiling of wild-type and YCA1-knock-out yeast cells during acetic acid-induced programmed cell death.
Using a combination of proteomics and , it was shown that YCA1 deletion down-regulated glycolysis, the TCA cycle and alcoholic fermentation compared with WT cells.
Title: Differential proteome-metabolome profiling of YCA1-knock-out and wild type cells reveals novel metabolic pathways and cellular processes dependent on the yeast metacaspase.
Life-span extension and aggregate management by Mca1 was only partly dependent on its conserved catalytic cysteine, which suggests that Mca1 harbors both caspase-dependent and independent functions related to life-span control.
Title: Life-span extension by a metacaspase in the yeast Saccharomyces cerevisiae.
protein degradation factors such as Cdc48 co-localize with Yca1 to the insoluble fraction, supporting the hypothesis that Yca1 may act primarily to dissolve or reduce accumulated aggregates.
Title: The role of Yca1 in proteostasis. Yca1 regulates the composition of the insoluble proteome.
structural and biochemical characterization identifies Yca1 as a Ca(2+)-activated cysteine protease that may cleave specific substrates during stress response in yeast.
Title: Crystal structure of the yeast metacaspase Yca1.
Metacaspase is associated with mitochondrial respiration, intracellular redox control and genomic stability.
Title: The yeast metacaspase is implicated in oxidative stress response in frataxin-deficient cells.
the aggregation propensity of the potential yeast prion protein Mca1 in vivo is strongly accelerated by a short peptide segment preceding its Q/N-rich region
Title: Extra N-terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein Mca1.
Data show that Yca1 protein complexes are enriched for aggregate-remodeling chaperones that colocalize with Yca1-GFP fusions.
Title: Metacaspase Yca1 is required for clearance of insoluble protein aggregates.

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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 calcium-dependent cysteine-type endopeptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables calcium-dependent cysteine-type endopeptidase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables cysteine-type endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables cysteine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info
enables cysteine-type peptidase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in apoptotic process	IDA Inferred from Direct Assay more info	PubMed
involved_in apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in apoptotic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein quality control for misfolded or incompletely synthesized proteins	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Ca(2+)-dependent cysteine protease MCA1

NP_014840.4

Ca2+-dependent cysteine protease; may cleave specific substrates during the stress response; regulates apoptosis upon H2O2 treatment; required for clearance of insoluble protein aggregates during normal growth; implicated in cell cycle dynamics and lifespan extension; undergoes autocatalytic processing; similar to mammalian metacaspases, but exists as a monomer due to an extra pair of anti-parallel beta-strands that block potential dimerization