| Standard Name | TIM11 |
|---|---|
| Systematic Name | YDR322C-A |
| Alias | ATP21 |
| Feature Type | ORF, Verified |
| Description | Subunit e of mitochondrial F1F0-ATPase; ATPase is a large, evolutionarily conserved enzyme complex required for ATP synthesis; essential for the dimeric and oligomeric state of ATP synthase, which in turn determines the shape of inner membrane cristae (1, 2, 3, 4 and see Summary Paragraph) |
| Name Description | Translocase of the Inner Mitochondrial membrane |
| Chromosomal Location | |
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| Note: this feature is encoded on the Crick strand. | |
| View Computational GO annotations for TIM11 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Classical genetics | |
|---|---|
| null | |
| reduction of function | |
| repressible | |
| Large-scale survey | |
| null | |
| Resources |
| 57 total interaction(s) for 50 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1999-07-17 | ||||||||||||
| Subfeature details |
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000007255 |
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TIM11 encodes subunit e of mitochondrial ATP synthase (1). The ATP synthase complex utilizes proton motive force to generate ATP from ADP and Pi (5). The structure of this enzyme complex is highly conserved among diverse organisms and consists of two major components, soluble F1 and membrane-bound F0, each of which contains many subunits (6). Subunit e, like subunit g (Atp20p), is not essential for the basic function or assembly of the F1/F0 ATP synthase complex, but is required for complex dimerization and maximal enzyme stability. Deletion of TIM11 reduces the mitochondrial concentration of ATP synthase, but does not alter enzyme activity (2).
General ATP synthase structure and function are reviewed in references 5 and 7. For a review that is specific to yeast, see reference 6.
| 1) | Arnold I, et al. (1997) Yeast mitochondrial F1F0-ATPase: the novel subunit e is identical to Tim11. FEBS Lett 411(2-3):195-200 |
| 2) | Arnold I, et al. (1998) Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits. EMBO J 17(24):7170-8 |
| 3) | Arselin G, et al. (2003) The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane. Eur J Biochem 270(8):1875-84 |
| 4) | Davies KM, et al. (2012) Structure of the yeast F1Fo-ATP synthase dimer and its role in shaping the mitochondrial cristae. Proc Natl Acad Sci U S A 109(34):13602-7 |
| 5) | Boyer PD (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49 |
| 6) | Devenish RJ, et al. (2000) Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex. Biochim Biophys Acta 1458(2-3):428-42 |
| 7) | Nakamoto RK, et al. (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28:205-34 |





