ATP5J2

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; OMA:ATP5MF - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7q22.1 Start 99,448,475 bp End 99,466,186 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 G2 Start 145,120,508 bp End 145,128,872 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart right testis left testis mucosa of transverse colon muscle of thigh right frontal lobe right auricle prefrontal cortex left ventricle ganglionic eminence Top expressed in atrioventricular valve endocardial cushion intercostal muscle myocardium of ventricle cardiac muscles digastric muscle extraocular muscle soleus muscle thoracic diaphragm sternocleidomastoid muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ATPase activity 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 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 proton transmembrane transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9551 57423 Ensembl ENSG00000241468 ENSMUSG00000038690 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 Chr 5: 145.12 – 145.13 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

The ATP5MF gene encodes the ATP synthase subunit f, mitochondrial enzyme in humans.

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.

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. S2CID 218895820.
• 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. Bibcode:1998Natur.391..510E. doi:10.1038/35185. PMID 9461222. S2CID 4406161.
• Wang H, Oster G (Nov 1998). "Energy transduction in the F1 motor of ATP synthase". Nature. 396 (6708): 279–82. Bibcode:1998Natur.396..279W. doi:10.1038/24409. PMID 9834036. S2CID 4424498.
• 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. S2CID 5621542.
• Cross RL (Jan 2004). "Molecular motors: turning the ATP motor". Nature. 427 (6973): 407–8. Bibcode:2004Natur.427..407C. doi:10.1038/427407b. PMID 14749816. S2CID 52819856.
• 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.