YTA12 m-AAA protease subunit YTA12 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: YTA12
Official Full Name: m-AAA protease subunit YTA12
Primary source: SGD:S000004695
Locus tag: YMR089C
See related: AllianceGenome:SGD:S000004695; FungiDB:YMR089C; VEuPathDB:YMR089C
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: RCA1
Summary: Enables ATP binding activity; ATP hydrolysis activity; and metallopeptidase activity. Involved in protein-containing complex assembly and signal peptide processing. Located in mitochondrial inner boundary membrane. Part of m-AAA complex. Used to study hereditary spastic paraplegia; optic atrophy 12; and spinocerebellar ataxia type 28. Human ortholog(s) of this gene implicated in optic atrophy 12; spastic ataxia; spastic ataxia 5; and spinocerebellar ataxia type 28. Orthologous to human AFG3L2 (AFG3 like matrix AAA peptidase subunit 2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See YTA12 in Genome Data Viewer

Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (445609..448086, complement)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

that replacement of the Yta10 TM2 domain abolishes membrane dislocation for only a subset of substrates, whereas replacement of the Yta12 TM2 domain impairs membrane dislocation for all tested substrates, suggesting different roles of the TM domains in each m-AAA protease subunit
Title: Molecular insights into the m-AAA protease-mediated dislocation of transmembrane helices in the mitochondrial inner membrane.
Rca1p appears to regulate cellular metabolism in response to CO(2) availability in environments as diverse as the phagosome, yeast communities or liquid culture.
Title: The bZIP transcription factor Rca1p is a central regulator of a novel CO₂ sensing pathway in yeast.
Inactivation of either of the mitochondrial AAA proteases, Yme1 or Yta10/12, allows fermentative growth of hsc82 or hsp82 strains at 37 degrees C.
Title: Hsp90 and mitochondrial proteases Yme1 and Yta10/12 participate in ATP synthase assembly in Saccharomyces cerevisiae.
mechanism regarding how proteins are recognized and degraded by m-AAA proteases.
Title: Electron cryomicroscopy structure of a membrane-anchored mitochondrial AAA protease.
Results describe the localizations of the m-AAA protease, its subunits Yta10 and Yta12, and its substrate cytochrome c peroxidase (Ccp1) within yeast mitochondria.
Title: The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria.
transmembrane segments of m-AAA protease subunits have a direct role in the dislocation of membrane-embedded substrates
Title: Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits.

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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 ATP binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IDA Inferred from Direct Assay more info	PubMed
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables ATP-dependent H2AZ histone chaperone activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent H3-H4 histone complex chaperone activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent peptidase activity	IEA Inferred from Electronic Annotation more info
enables DNA clamp loader activity	IEA Inferred from Electronic Annotation more info
enables chromatin extrusion motor activity	IEA Inferred from Electronic Annotation more info
enables cohesin loader activity	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables metalloendopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metalloendopeptidase activity	IEA Inferred from Electronic Annotation more info
enables metallopeptidase activity	IEA Inferred from Electronic Annotation more info
enables metallopeptidase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables zinc ion binding	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in chromatin looping	IEA Inferred from Electronic Annotation more info
involved_in chromatin remodeling	IEA Inferred from Electronic Annotation more info
involved_in mitochondrial protein processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein-containing complex assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in signal peptide processing	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
part_of m-AAA complex	IBA Inferred from Biological aspect of Ancestor more info
part_of m-AAA complex	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in mitochondrial inner boundary membrane	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial inner membrane	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial inner 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: m-AAA protease subunit YTA12

NP_013807.1

Mitochondrial inner membrane m-AAA protease component; mediates degradation of misfolded or unassembled proteins; also required for correct assembly of mitochondrial enzyme complexes; overexpression of human AFG3L2 complements respiratory defect of yeast afg3 yta12 double null mutation, but overexpression of disease-associated AFG3L2 variants does not; expression of both human SPG7 (paraplegin) and AFG3L2 complements yeast yta12 afg3 double mutation

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_001145.3 Reference assembly

Range

445609..448086 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182589.1 → NP_013807.1 TPA: m-AAA protease subunit YTA12 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013807.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VZR2, E9P917, P40341

UniProtKB/TrEMBL

A6ZME6

Conserved Domains (2) summary

TIGR01241
Location:290 → 784

FtsH_fam; ATP-dependent metalloprotease FtsH

pfam06480
Location:205 → 282

FtsH_ext; FtsH Extracellular