LOCUS       NM_004889                443 bp    mRNA    linear   PRI 21-SEP-2024
DEFINITION  Homo sapiens ATP synthase membrane subunit f (ATP5MF), transcript
            variant 1, mRNA; nuclear gene for mitochondrial product.
ACCESSION   NM_004889
VERSION     NM_004889.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 443)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (bases 1 to 443)
  AUTHORS   Solaini,G., Sgarbi,G. and Baracca,A.
  TITLE     The F1Fo-ATPase inhibitor, IF1, is a critical regulator of energy
            metabolism in cancer cells
  JOURNAL   Biochem Soc Trans 49 (2), 815-827 (2021)
   PUBMED   33929490
  REMARK    GeneRIF: The F1Fo-ATPase inhibitor, IF1, is a critical regulator of
            energy metabolism in cancer cells.
            Review article
REFERENCE   3  (bases 1 to 443)
  AUTHORS   Mnatsakanyan,N. and Jonas,E.A.
  TITLE     The new role of F1Fo ATP synthase in mitochondria-mediated
            neurodegeneration and neuroprotection
  JOURNAL   Exp Neurol 332, 113400 (2020)
   PUBMED   32653453
  REMARK    GeneRIF: The new role of F1Fo ATP synthase in mitochondria-mediated
            neurodegeneration and neuroprotection.
            Review article
REFERENCE   4  (bases 1 to 443)
  AUTHORS   Fujikawa,M., Sugawara,K., Tanabe,T. and Yoshida,M.
  TITLE     Assembly of human mitochondrial ATP synthase through two separate
            intermediates, F1-c-ring and b-e-g complex
  JOURNAL   FEBS Lett 589 (19 Pt B), 2707-2712 (2015)
   PUBMED   26297831
REFERENCE   5  (bases 1 to 443)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (bases 1 to 443)
  AUTHORS   Aggeler,R., Coons,J., Taylor,S.W., Ghosh,S.S., Garcia,J.J.,
            Capaldi,R.A. and Marusich,M.F.
  TITLE     A functionally active human F1F0 ATPase can be purified by
            immunocapture from heart tissue and fibroblast cell lines. Subunit
            structure and activity studies
  JOURNAL   J Biol Chem 277 (37), 33906-33912 (2002)
   PUBMED   12110673
REFERENCE   7  (bases 1 to 443)
  AUTHORS   Bosetti,F., Brizzi,F., Barogi,S., Mancuso,M., Siciliano,G.,
            Tendi,E.A., Murri,L., Rapoport,S.I. and Solaini,G.
  TITLE     Cytochrome c oxidase and mitochondrial F1F0-ATPase (ATP synthase)
            activities in platelets and brain from patients with Alzheimer's
            disease
  JOURNAL   Neurobiol Aging 23 (3), 371-376 (2002)
   PUBMED   11959398
REFERENCE   8  (bases 1 to 443)
  AUTHORS   Wang,H. and Oster,G.
  TITLE     Energy transduction in the F1 motor of ATP synthase
  JOURNAL   Nature 396 (6708), 279-282 (1998)
   PUBMED   9834036
REFERENCE   9  (bases 1 to 443)
  AUTHORS   Elston,T., Wang,H. and Oster,G.
  TITLE     Energy transduction in ATP synthase
  JOURNAL   Nature 391 (6666), 510-513 (1998)
   PUBMED   9461222
REFERENCE   10 (bases 1 to 443)
  AUTHORS   Boyer,P.D., Cross,R.L. and Momsen,W.
  TITLE     A new concept for energy coupling in oxidative phosphorylation
            based on a molecular explanation of the oxygen exchange reactions
  JOURNAL   Proc Natl Acad Sci U S A 70 (10), 2837-2839 (1973)
   PUBMED   4517936
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF047436.1.
            
            On Nov 30, 2019 this sequence version replaced NM_004889.4.
            
            Summary: Mitochondrial ATP synthase catalyzes ATP synthesis,
            utilizing an electrochemical gradient of protons across the inner
            membrane during oxidative phosphorylation. It is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, which comprises the proton
            channel. The catalytic portion of mitochondrial ATP synthase
            consists of five different subunits (alpha, beta, gamma, delta, and
            epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and
            single representatives of the gamma, delta, and epsilon subunits.
            The proton channel likely has nine subunits (a, b, c, d, e, f, g,
            F6 and 8). This gene encodes the f subunit of the Fo complex.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified for this gene. This gene has multiple
            pseudogenes. Naturally occurring read-through transcription also
            exists between this gene and the downstream pentatricopeptide
            repeat domain 1 (PTCD1) gene. [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript, and it encodes the longest isoform (2a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU960758.1, BU588238.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000292475.8/
                                                  ENSP00000292475.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-443               AF047436.1         2-444
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     gene            1..443
                     /gene="ATP5MF"
                     /gene_synonym="ATP5J2; ATP5JL"
                     /note="ATP synthase membrane subunit f"
                     /db_xref="GeneID:9551"
                     /db_xref="HGNC:HGNC:848"
                     /db_xref="MIM:619792"
     exon            1..57
                     /gene="ATP5MF"
                     /gene_synonym="ATP5J2; ATP5JL"
                     /inference="alignment:Splign:2.1.0"
     CDS             27..311
                     /gene="ATP5MF"
                     /gene_synonym="ATP5J2; ATP5JL"
                     /EC_number="3.6.1.14"
                     /note="isoform 2a is encoded by transcript variant 1;
                     F1Fo-ATPase synthase f subunit; ATP synthase, H+
                     transporting, mitochondrial F0 complex, subunit f; ATP
                     synthase f chain, mitochondrial; F1Fo-ATP synthase complex
                     Fo membrane domain f subunit; F1F0-type ATPase subunit f;
                     ATP synthase, H+ transporting, mitochondrial Fo complex
                     subunit F2"
                     /codon_start=1
                     /product="ATP synthase subunit f, mitochondrial isoform
                     2a"
                     /protein_id="NP_004880.1"
                     /db_xref="CCDS:CCDS5665.1"
                     /db_xref="GeneID:9551"
                     /db_xref="HGNC:HGNC:848"
                     /db_xref="MIM:619792"
                     /translation="MASVGECPAPVPVKDKKLLEVKLGELPSWILMRDFSPSGIFGAF
                     QRGYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLKHERLRKYH"
     exon            58..165
                     /gene="ATP5MF"
                     /gene_synonym="ATP5J2; ATP5JL"
                     /inference="alignment:Splign:2.1.0"
     exon            166..282
                     /gene="ATP5MF"
                     /gene_synonym="ATP5J2; ATP5JL"
                     /inference="alignment:Splign:2.1.0"
     exon            283..443
                     /gene="ATP5MF"
                     /gene_synonym="ATP5J2; ATP5JL"
                     /inference="alignment:Splign:2.1.0"
     regulatory      426..431
                     /regulatory_class="polyA_signal_sequence"
                     /gene="ATP5MF"
                     /gene_synonym="ATP5J2; ATP5JL"
                     /note="hexamer: AATAAA"
     polyA_site      443
                     /gene="ATP5MF"
                     /gene_synonym="ATP5J2; ATP5JL"
                     /note="major polyA site"
ORIGIN      
        1 ggcacagcgg acaccaggac tccaaaatgg cgtcagttgg tgagtgtccg gccccagtac
       61 cagtgaagga caagaaactt ctggaggtca aactggggga gctgccaagc tggatcttga
      121 tgcgggactt cagtcctagt ggcattttcg gagcgtttca aagaggttac taccggtact
      181 acaacaagta catcaatgtg aagaagggga gcatctcggg gattaccatg gtgctggcat
      241 gctacgtgct ctttagctac tccttttcct acaagcatct caagcacgag cggctccgca
      301 aataccactg aagaggacac actctgcacc cccccacccc acgaccttgg cccgagcccc
      361 tccgtgagga acacaatctc aatcgttgct gaatcctttc atatcctaat aggaattaac
      421 ctccaaataa aacatgactg gta
//
