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    MRX3 Mrx3p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852181, updated on 28-Oct-2024

    Summary

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    Official Symbol
    MRX3
    Official Full Name
    Mrx3p
    Primary source
    SGD:S000000191
    Locus tag
    YBL095W
    See related
    AllianceGenome:SGD:S000000191; FungiDB:YBL095W; VEuPathDB:YBL095W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Located in mitochondrial inner membrane. Orthologous to human THEM4 (thioesterase superfamily member 4). [provided by Alliance of Genome Resources, Oct 2024]
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    Genomic context

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    See MRX3 in Genome Data Viewer
    Location:
    chromosome: II
    Exon count:
    1
    Sequence:
    Chromosome: II; NC_001134.8 (43277..44089)

    Chromosome II - NC_001134.8Genomic Context describing neighboring genes Neighboring gene kynurenine 3-monooxygenase Neighboring gene condensin subunit BRN1 Neighboring gene Rox3p Neighboring gene ribosomal 60S subunit protein L32

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001134.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Yeast mitochondrial protein-protein interactions reveal diverse complexes and disease-relevant functional relationships. Jin K, et al. J Proteome Res, 2015 Feb 6. PMID 25546499
    2. Organization of Mitochondrial Gene Expression in Two Distinct Ribosome-Containing Assemblies. Kehrein K, et al. Cell Rep, 2015 Feb 17. PMID 25683707
    3. MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization. Alkhaja AK, et al. Mol Biol Cell, 2012 Jan. PMID 22114354, Free PMC Article
    4. Genome-Wide Studies of Rho5-Interacting Proteins That Are Involved in Oxidant-Induced Cell Death in Budding Yeast. Singh K, et al. G3 (Bethesda), 2019 Mar 7. PMID 30670610, Free PMC Article
    5. Exo1 recruits Cdc5 polo kinase to MutLγ to ensure efficient meiotic crossover formation. Sanchez A, et al. Proc Natl Acad Sci U S A, 2020 Dec 1. PMID 33199619, Free PMC Article

    See all (29) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables molecular_function ND
    No biological Data available
    more info
    		  
    Process Evidence Code Pubs
    involved_in biological_process ND
    No biological Data available
    more info
    		  
    Component Evidence Code Pubs
    located_in mitochondrial inner membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrion HDA PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    Mrx3p
    NP_009457.1
    • Protein that associates with mitochondrial ribosome; likely functions in cristae junction formation; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies

    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

    1. NC_001134.8 Reference assembly

      Range
      43277..44089
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178335.1 → NP_009457.1  TPA: Mrx3p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_009457.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VPQ9, P38172
      UniProtKB/TrEMBL
      A6ZKK8, B3LNM6, B5VDP8, C7GSE9, C8Z3U9, N1P9B9
      Conserved Domains (1) summary
      cl00509
      Location:121 → 216
      hot_dog; The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P38172.1

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