ATP16/YDL004W Summary Help

Standard Name ATP16
Systematic Name YDL004W
Feature Type ORF, Verified
Description Delta subunit of the central stalk of mitochondrial F1F0 ATP synthase; F1F0 ATP synthase is a large, evolutionarily conserved enzyme complex required for ATP synthesis; F1 translationally regulates ATP6 and ATP8 expression to achieve a balanced output of ATP synthase genes encoded in nucleus and mitochondria; phosphorylated (1, 2, 3 and see Summary Paragraph)
Name Description ATP synthase
Chromosomal Location
ChrIV:443029 to 443511 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All ATP16 GO evidence and references
  View Computational GO annotations for ATP16
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 3 genes
Resources
Classical genetics
null
Large-scale survey
null
reduction of function
unspecified
Resources
13 total interaction(s) for 10 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 4
  • Affinity Capture-RNA: 2
  • Biochemical Activity: 1
  • Co-purification: 5
  • Reconstituted Complex: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 160
Molecular Weight (Da) 17,020
Isoelectric Point (pI) 6.54
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:443029 to 443511 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..483 443029..443511 2011-02-03 1996-07-31
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 SGDIDS000002162
SUMMARY PARAGRAPH for ATP16

ATP16 encodes the delta subunit of mitochondrial ATP synthase and is homologous to the epsilon subunit of bacterial ATP synthase (1). The ATP synthase complex utilizes proton motive force to generate ATP from ADP and Pi (4). 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. F1 and F0 are connected, both functionally and physically, via two additional multi-subunit structures, the central stalk and the stator stalk. The delta subunit is part of the central stalk, which, like a rotor shaft, transmits the movement of the F0 proton pump to the catalytic core of F1 (5 and references therein).

Although ATP16 is essential for ATP synthase function, it is not essential for life in yeast. Deletion of ATP16, like deletions in many genes necessary for the function or maintenance of mitochondria, leads to a "petite" phenotype that is slow-growing and unable to survive on nonfermentable carbon sources (1).

General ATP synthase structure and function are reviewed in references 4 and 5. For a review that is specific to yeast, see reference 6.

Last updated: 2001-01-16 Contact SGD

References cited on this page View Complete Literature Guide for ATP16
1) Giraud MF and Velours J  (1994) ATP synthase of yeast mitochondria. Isolation of the F1 delta subunit, sequence and disruption of the structural gene. Eur J Biochem 222(3):851-9
2) Reinders J, et al.  (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906
3) Rak M and Tzagoloff A  (2009) F1-dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase. Proc Natl Acad Sci U S A 106(44):18509-14
4) Boyer PD  (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49
5) Nakamoto RK, et al.  (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28():205-34
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