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    NMA111 Nma111p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855600, updated on 9-Dec-2024

    Summary

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    Official Symbol
    NMA111
    Official Full Name
    Nma111p
    Primary source
    SGD:S000005067
    Locus tag
    YNL123W
    See related
    AllianceGenome:SGD:S000005067; FungiDB:YNL123W; VEuPathDB:YNL123W
    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
    YNM3
    Summary
    Enables serine-type endopeptidase activity. Involved in several processes, including apoptotic process; cellular response to heat; and stress-induced homeostatically regulated protein degradation pathway. Located in nucleus. Human ortholog(s) of this gene implicated in CADASIL (multiple); gastrointestinal system cancer (multiple); hypertension; lung adenocarcinoma; and macular degeneration (multiple). Orthologous to human HTRA1 (HtrA serine peptidase 1). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See NMA111 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (394685..397678)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene Esbp6p Neighboring gene RNA-binding snoRNP assembly protein Neighboring gene mitochondrial 54S ribosomal protein MRP35 Neighboring gene protein channel TOM70

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001146.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The S. cerevisiae HtrA-like protein Nma111p is a nuclear serine protease that mediates yeast apoptosis. Fahrenkrog B, et al. J Cell Sci, 2004 Jan 1. PMID 14657274
    2. Nuclear localisation is crucial for the proapoptotic activity of the HtrA-like serine protease Nma111p. Belanger KD, et al. J Cell Sci, 2009 Nov 1. PMID 19808885
    3. The yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress. Padmanabhan N, et al. Mol Biol Cell, 2009 Jan. PMID 18946088, Free PMC Article
    4. The inhibitor-of-apoptosis protein Bir1p protects against apoptosis in S. cerevisiae and is a substrate for the yeast homologue of Omi/HtrA2. Walter D, et al. J Cell Sci, 2006 May 1. PMID 16608876
    5. Mitochondrial impairment and oxidative stress mediated apoptosis induced by α-Fe(2)O(3) nanoparticles in Saccharomyces cerevisiae. Zhu S, et al. Toxicol Res (Camb), 2017 Sep 1. PMID 30090539, Free PMC Article

    See all (44) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Nuclear-localisation signal and catalytic serine 235 are necessary for the proapoptotic activity of Nma111.
      Title: Nuclear localisation is crucial for the proapoptotic activity of the HtrA-like serine protease Nma111p.
    2. Results suggest that the chaperone activity of Ynm3 may be important to improve the efficiency of proteolysis of aberrant proteins by averting the formation of nonproductive toxic aggregates and presenting them in a soluble state to its protease domain.
      Title: The yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress.
    3. Ynm3p modulates fatty acid metabolism and gene regulation through negative regulation of FAA1 activity
      Title: Direct interaction of Saccharomyces cerevisiae Faa1p with the Omi/HtrA protease orthologue Ynm3p alters lipid homeostasis.
    Submit: New GeneRIF Correction

    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 serine-type endopeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables serine-type endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables serine-type endopeptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables serine-type peptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables serine-type peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    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 cellular response to heat IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in cellular response to stress IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in lipid metabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in lipid metabolic process IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    involved_in positive regulation of apoptotic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in stress-induced homeostatically regulated protein degradation pathway IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in nucleus HDA PubMed 
    is_active_in nucleus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    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
    Nma111p
    NP_014276.1
    • Serine protease and general molecular chaperone; cleaves Roq1p, which modifies the substrate specificity of the Ubr1p Ub-ligase, promoting the stress-induced homeostatically-regulated protein degradation (SHRED) of misfolded and native ER-membrane and cytosolic proteins; chaperone activity involved in the heat stress response; promotes apoptosis through proteolysis of Bir1p; role in lipid homeostasis; mammalian Omi/HtrA2 serine protease family member

    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_001146.8 Reference assembly

      Range
      394685..397678
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182961.1 → NP_014276.1  TPA: Nma111p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014276.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      A6ZRW1, B0KZR3, B0KZU0, B0KZX6, B0L003, B0L021, D6W160, P53920
      UniProtKB/TrEMBL
      C7GKC3, G2WLY4, N1P4C0
      Conserved Domains (3) summary
      COG0265
      Location:48 → 391
      DegQ; Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]
      pfam12812
      Location:392 → 469
      PDZ_1; PDZ-like domain
      cl00117
      Location:869 → 944
      PDZ; PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P53920.1

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