TIM11/YDR322C-A Summary Help

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
ChrIV:1112293 to 1112003 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All TIM11 GO evidence and references
  View Computational GO annotations for TIM11
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 3 genes
Resources
Classical genetics
null
reduction of function
repressible
Large-scale survey
null
Resources
58 total interaction(s) for 50 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 6
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 7
  • Co-purification: 2

Genetic Interactions
  • Negative Genetic: 33
  • Phenotypic Enhancement: 1
  • Positive Genetic: 7
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 96
Molecular Weight (Da) 10,875
Isoelectric Point (pI) 5.98
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:1112293 to 1112003 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1999-07-17
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..291 1112293..1112003 2011-02-03 1999-07-17
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000007255
SUMMARY PARAGRAPH for TIM11

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.

Last updated: 2001-01-18 Contact SGD

References cited on this page View Complete Literature Guide for TIM11
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