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    ATP1 F1F0 ATP synthase subunit alpha [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852177, updated on 14-Nov-2024

    Summary

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    Official Symbol
    ATP1
    Official Full Name
    F1F0 ATP synthase subunit alpha
    Primary source
    SGD:S000000195
    Locus tag
    YBL099W
    See related
    AllianceGenome:SGD:S000000195; FungiDB:YBL099W; VEuPathDB:YBL099W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Contributes to ATP hydrolysis activity and proton-transporting ATP synthase activity, rotational mechanism. Involved in proton motive force-driven ATP synthesis. Located in mitochondrial nucleoid. Part of proton-transporting ATP synthase, catalytic core. Human ortholog(s) of this gene implicated in combined oxidative phosphorylation deficiency 22; mitochondrial complex V (ATP synthase) deficiency nuclear type 4A; and mitochondrial complex V (ATP synthase) deficiency nuclear type 4B. Orthologous to human ATP5F1A (ATP synthase F1 subunit alpha). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See ATP1 in Genome Data Viewer
    Location:
    chromosome: II
    Exon count:
    1
    Sequence:
    Chromosome: II; NC_001134.8 (37053..38690)

    Chromosome II - NC_001134.8Genomic Context describing neighboring genes Neighboring gene gag protein Neighboring gene gag-pol fusion protein Neighboring gene tRNA-Phe Neighboring gene kynurenine 3-monooxygenase Neighboring gene condensin subunit BRN1

    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. The mitochondrial F1ATPase alpha-subunit is necessary for efficient import of mitochondrial precursors. Yuan H, et al. J Biol Chem, 1992 Jul 25. PMID 1386080
    2. Alteration of apparent negative cooperativity of ATPase activity by alpha-subunit glutamine 173 mutation in yeast mitochondrial F1. Correlation with impaired nucleotide interaction at a regulatory site. Jault JM, et al. J Biol Chem, 1991 May 5. PMID 1827117
    3. Nuclear genes encoding the yeast mitochondrial ATPase complex. Analysis of ATP1 coding the F1-ATPase alpha-subunit and its assembly. Takeda M, et al. J Biol Chem, 1986 Nov 15. PMID 2876995
    4. Characterization of a protein serine kinase from yeast plasma membrane. Kolarov J, et al. J Biol Chem, 1988 Aug 5. PMID 2899078
    5. Three ATP1 genes are present on chromosome II in Saccharomyces cerevisiae. Takeda M, et al. J Biochem, 1995 Sep. PMID 8690725

    See all (176) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Dimerization of the F1F0-ATP synthase and the presence of the MICOS complex are necessary for the two pathways of mitochondrial crista formation.
      Title: An evidence based hypothesis on the existence of two pathways of mitochondrial crista formation.
    2. The structure of F-ATPase from Saccharomyces cerevisiae inhibited by the yeast IF has been determined at 2.5 A resolution.
      Title: The structure of F₁-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF₁.
    3. Measurement of chronological aging of yeast in culture reveals that ATP1 and ATP3 suppressor alleles in strains that contain mitochondrial DNA are longer lived than the isogenic wild-type strain.
      Title: Mutations in the Atp1p and Atp3p subunits of yeast ATP synthase differentially affect respiration and fermentation in Saccharomyces cerevisiae.
    Submit: New GeneRIF Correction

    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

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables ADP binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to ATP hydrolysis activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    contributes_to proton-transporting ATP synthase activity, rotational mechanism IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    contributes_to proton-transporting ATP synthase activity, rotational mechanism IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables proton-transporting ATP synthase activity, rotational mechanism IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to proton-transporting ATP synthase activity, rotational mechanism IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in ATP biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proton motive force-driven ATP synthesis IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in proton motive force-driven ATP synthesis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in proton motive force-driven ATP synthesis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proton motive force-driven ATP synthesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proton transmembrane transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in mitochondrial inner membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrial nucleoid IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrion HDA PubMed 
    located_in mitochondrion IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of proton-transporting ATP synthase complex, catalytic core F(1) IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of proton-transporting ATP synthase complex, catalytic core F(1) IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of proton-transporting ATP synthase, catalytic core IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of proton-transporting ATP synthase, catalytic core IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    F1F0 ATP synthase subunit alpha
    NP_009453.2
    • Alpha subunit of the F1 sector of mitochondrial F1F0 ATP synthase; which is a large, evolutionarily conserved enzyme complex required for ATP synthesis; F1 translationally regulates ATP6 and ATP8 expression to achieve a balanced output of ATP synthase genes encoded in nucleus and mitochondria; phosphorylated; N-terminally propionylated in vivo

    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
      37053..38690
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178339.2 → NP_009453.2  TPA: F1F0 ATP synthase subunit alpha [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_009453.2

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VPQ6, P07251, Q92449
      UniProtKB/TrEMBL
      A6ZKK5, B3LNM9, B5VDP5, C7GSE6, C8Z3U3, E9P981, F2Z6M8, G2W8R5, N1P9R2
      Conserved Domains (1) summary
      PRK09281
      Location:42 → 545
      PRK09281; F0F1 ATP synthase subunit alpha; Validated
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P07251.5

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