CUP5/YEL027W Summary Help

CUP5 BASIC INFORMATION

Standard Name CUP5 1
Systematic Name YEL027W
Alias CLS7 , GEF2 , VMA3
Feature Type ORF, Verified
Description Proteolipid subunit of the vacuolar H(+)-ATPase V0 sector (subunit c; dicyclohexylcarbodiimide binding subunit); required for vacuolar acidification and important for copper and iron metal ion homeostasis (2, 3 and see Summary Paragraph)
GO Annotations All CUP5 GO evidence and references
    View Computational GO annotations for CUP5
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All CUP5 Phenotype details and references
Classical genetics
null
unspecified
Large-scale survey
null
overexpression
Interactions CUP5 All interactions details and references
38 total interaction(s) for 30 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 6
  • Co-fractionation: 1
  • Protein-peptide: 1
  • Two-hybrid: 12
Genetic Interactions
  • Phenotypic Enhancement: 1
  • Synthetic Growth Defect: 9
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 3
Sequence Information
ChrV:100769 to 101251 | ORF Map | GBrowse
Gbrowse
Genetic position: -18 cM
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..483 100769..101251 1996-07-31 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000000753

CUP5 RESOURCES

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Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for CUP5

SUMMARY PARAGRAPH for CUP5

CUP5 encodes the c subunit of the yeast V-ATPase V0 domain (4). Vacuolar (H )-ATPases (V-ATPases) are ATP-dependent proton pumps that acidify intracellular vacuolar compartments. Vacuolar acidification is important for many cellular processes, including endocytosis, targeting of newly synthesized lysosomal enzymes, and other molecular targeting processes. The V-ATPase consists of two separable domains. The V1 domain has eight known subunits, is peripherally associated with the vacuolar membrane, and catalyzes ATP hydrolysis. The V0 domain is an integral membrane structure of five subunits, and transports protons across the membrane. The structure, function, and assembly of V-ATPases are reviewed in references 5, 6, 7 and 8.

The V0 c, c' (Tfp3p), and c'' (Ppa1p) subunits are highly hydrophobic integral membrane proteolipids, and have similar amino acid sequences; all three are required for V-ATPase activity (5, 8). Cup5p is also involved in copper and iron homeostasis (3, 2). The cup5 null mutant is viable but lacks vacuolar (H )-ATPase activity, and is defective in vacuolar acidification, vacuole biogenesis, vacuolar protein targeting, and endocytosis (4). The a and b V0 subunits do not assemble in the absence of Cup5p (4).

V-ATPases have been identified in numerous eukaryotes; c subunit homologs have been identified in Drosophila, Manduca sexta, and Nephrops norvegicus, and the Drosophila and Nephrops genes can rescue the cup5 null phenotype (9, 10).

Last updated: 2000-05-18

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for CUP5]

1) Welch, J.W. and Fogel, S.  (1985) Personal Communication, Mortimer Map Edition 9
2) Szczypka MS, et al.  (1997) Saccharomyces cerevisiae mutants altered in vacuole function are defective in copper detoxification and iron-responsive gene transcription. Yeast 13(15):1423-35
3) Eide DJ, et al.  (1993) The vacuolar H(+)-ATPase of Saccharomyces cerevisiae is required for efficient copper detoxification, mitochondrial function, and iron metabolism. Mol Gen Genet 241(3-4):447-56
4) Umemoto N, et al.  (1990) Roles of the VMA3 gene product, subunit c of the vacuolar membrane H(+)-ATPase on vacuolar acidification and protein transport. A study with VMA3-disrupted mutants of Saccharomyces cerevisiae. J Biol Chem 265(30):18447-53
5) Forgac M  (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4
6) Graham LA and Stevens TH  (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47
7) Kane PM  (1999) Biosynthesis and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr 31(1):49-56
8) Stevens TH and Forgac M  (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808
9) Finbow ME, et al.  (1994) Evidence that the 16 kDa proteolipid (subunit c) of the vacuolar H(+)-ATPase and ductin from gap junctions are the same polypeptide in Drosophila and Manduca: molecular cloning of the Vha16k gene from Drosophila. J Cell Sci 107 ( Pt 7):1817-24
10) Harrison MA, et al.  (1994) Functional properties of a hybrid vacuolar H(+)-ATPase in Saccharomyces cells expressing the Nephrops 16-kDa proteolipid. Eur J Biochem 221(1):111-20