ATP5J2

The ATP5MF gene [4][5] encodes the ATP synthase subunit f, mitochondrial enzyme in humans.

ATP5MF
Identifiers
Aliases	ATP5MF, ATP5JL, ATP synthase, H+ transporting, mitochondrial Fo complex subunit F2, ATP5J2, ATP synthase membrane subunit f
External IDs	MGI: 1927558 HomoloGene: 3594 GeneCards: ATP5MF
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7q22.1 Start 99,448,475 bp[1] End 99,466,331 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • ATPase activity • GO:0022891 transmembrane transporter activity Cellular component • integral component of membrane • mitochondrial inner membrane • mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) • mitochondrial proton-transporting ATP synthase complex • extracellular exosome • cell nucleus • membrane • proton-transporting ATP synthase complex, coupling factor F(o) • nucleoplasm • mitochondrion Biological process • ATP metabolic process • mitochondrial ATP synthesis coupled proton transport • ion transport • ATP biosynthetic process • cristae formation • transport • hydrogen ion transmembrane transport Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9551	57423
Ensembl	ENSG00000241468	n/a
UniProt	P56134	P56135
RefSeq (mRNA)	NM_004889 NM_001003713 NM_001003714 NM_001039178 NM_001190353 NM_001190354	NM_020582
RefSeq (protein)	NP_001003713 NP_001003714 NP_001034267 NP_004880	NP_065607
Location (UCSC)	Chr 7: 99.45 – 99.47 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

Function

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 5 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.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000241468 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Mao M, Fu G, Wu JS, Zhang QH, Zhou J, Kan LX, Huang QH, He KL, Gu BW, Han ZG, Shen Y, Gu J, Yu YP, Xu SH, Wang YX, Chen SJ, Chen Z (Jul 1998). "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning". Proceedings of the National Academy of Sciences of the United States of America. 95 (14): 8175–80. doi:10.1073/pnas.95.14.8175. PMC 20949. PMID 9653160.
5. "Entrez Gene: ATP5MF ATP synthase membrane subunit f".

External links

• Human ATP5MF genome location and ATP5MF gene details page in the UCSC Genome Browser.

Further reading

• Kinosita K, Yasuda R, Noji H (2003). "F1-ATPase: a highly efficient rotary ATP machine". Essays in Biochemistry. 35: 3–18. doi:10.1042/bse0350003. PMID 12471886.
• Oster G, Wang H (Mar 2003). "Rotary protein motors". Trends in Cell Biology. 13 (3): 114–21. doi:10.1016/S0962-8924(03)00004-7. PMID 12628343.
• Leyva JA, Bianchet MA, Amzel LM (2003). "Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)". Molecular Membrane Biology. 20 (1): 27–33. doi:10.1080/0968768031000066532. PMID 12745923.
• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Elston T, Wang H, Oster G (Jan 1998). "Energy transduction in ATP synthase". Nature. 391 (6666): 510–3. doi:10.1038/35185. PMID 9461222.
• Wang H, Oster G (Nov 1998). "Energy transduction in the F1 motor of ATP synthase". Nature. 396 (6708): 279–82. doi:10.1038/24409. PMID 9834036.
• Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Oct 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Research. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
• Bosetti F, Brizzi F, Barogi S, Mancuso M, Siciliano G, Tendi EA, Murri L, Rapoport SI, Solaini G (2002). "Cytochrome c oxidase and mitochondrial F1F0-ATPase (ATP synthase) activities in platelets and brain from patients with Alzheimer's disease". Neurobiology of Aging. 23 (3): 371–6. doi:10.1016/S0197-4580(01)00314-1. PMID 11959398.
• Cross RL (Jan 2004). "Molecular motors: turning the ATP motor". Nature. 427 (6973): 407–8. doi:10.1038/427407b. PMID 14749816.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.