ATP7/YKL016C Summary Help

Standard Name ATP7
Systematic Name YKL016C
Feature Type ORF, Verified
Description Subunit d of the stator stalk of mitochondrial F1F0 ATP synthase; F1F0 ATP synthase is a large, evolutionarily conserved enzyme complex required for ATP synthesis (1, 2 and see Summary Paragraph)
Name Description ATP synthase
Chromosomal Location
ChrXI:407989 to 407465 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All ATP7 GO evidence and references
  View Computational GO annotations for ATP7
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 15 genes
Resources
Classical genetics
null
Large-scale survey
null
Resources
73 total interaction(s) for 57 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 28
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 2
  • Co-purification: 5
  • Reconstituted Complex: 3
  • Two-hybrid: 8

Genetic Interactions
  • Dosage Lethality: 1
  • Negative Genetic: 5
  • Phenotypic Suppression: 2
  • Positive Genetic: 13
  • Synthetic Growth Defect: 4

Resources
Expression Summary
histogram
Resources
Length (a.a.) 174
Molecular Weight (Da) 19,809
Isoelectric Point (pI) 9.74
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXI:407989 to 407465 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
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..525 407989..407465 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 SGDIDS000001499
SUMMARY PARAGRAPH for ATP7

ATP7 encodes subunit d of mitochondrial ATP synthase (1). The ATP synthase complex utilizes proton motive force to generate ATP from ADP and Pi (3). 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. Subunit d is part of the stator stalk, a stationary structure necessary for the productive transmission of rotary motion from the F0 proton pump to the F1 catalytic core. Unlike most ATP synthase subunits, mitochondrial subunit d does not have a bacterial homolog (3 and 4 and references therein).

Although ATP7 is essential for ATP synthase function, it is not essential for life in yeast. Deletion of ATP7, 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 3 and 4. For a review that is specific to yeast, see reference 5.

Last updated: 2001-01-16 Contact SGD

References cited on this page View Complete Literature Guide for ATP7
1) Norais N, et al.  (1991) ATP synthase of yeast mitochondria. Characterization of subunit d and sequence analysis of the structural gene ATP7. J Biol Chem 266(25):16541-9
2) Soubannier V, et al.  (1999) The second stalk of the yeast ATP synthase complex: identification of subunits showing cross-links with known positions of subunit 4 (subunit b). Biochemistry 38(45):15017-24
3) Boyer PD  (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49
4) Nakamoto RK, et al.  (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28():205-34
5) 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