STV1/YMR054W Summary Help

Standard Name STV1 1
Systematic Name YMR054W
Feature Type ORF, Verified
Description Subunit a of the vacuolar-ATPase V0 domain; one of two isoforms (Stv1p and Vph1p); Stv1p is located in V-ATPase complexes of the Golgi and endosomes while Vph1p is located in V-ATPase complexes of the vacuole (1, 2, 3, 4 and see Summary Paragraph)
Name Description Similar To VPH1 1
Chromosomal Location
ChrXIII:383303 to 385975 | ORF Map | GBrowse
Gene Ontology Annotations All STV1 GO evidence and references
  View Computational GO annotations for STV1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 2 genes
Classical genetics
Large-scale survey
130 total interaction(s) for 90 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 4
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 10
  • Co-purification: 1
  • PCA: 5
  • Two-hybrid: 27

Genetic Interactions
  • Dosage Rescue: 2
  • Negative Genetic: 58
  • Phenotypic Enhancement: 2
  • Positive Genetic: 7
  • Synthetic Growth Defect: 9
  • Synthetic Lethality: 2

Expression Summary
Length (a.a.) 890
Molecular Weight (Da) 101,660
Isoelectric Point (pI) 5.13
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIII:383303 to 385975 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2673 383303..385975 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
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
Primary SGDIDS000004658

STV1 is one of two yeast genes encoding isoforms of the a subunit of the yeast V-ATPase V0 domain (2, 1). 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, 3, 6 and 7.

Deletion of STV1 has little effect on cell growth, but deletion of both STV1 and VPH1, which encodes the second a subunit isoform, causes a more severe growth defect at neutral pH or in the presence of excess calcium (2). Overproduction of Stv1p partially complements a defect in vacuolar acidification in the vph1 null mutant (2). Stv1p and Vph1p show different localization patterns in indirect immunofluorescence assays, suggesting that they may be equivalent subunits for V-ATPases located on different organelles (2).

Stv1p and Vph1p are 55% identical and proteins similar to Vph1p have also been identified in rat, mouse, C. elegans and humans (8). Mutations in the isoforms of human V-ATPase most similar to Vph1p, a3 and a4, result in osteopetrosis and distal renal tubular acidosis, respectively (9, 10).

Last updated: 2000-05-17 Contact SGD

References cited on this page View Complete Literature Guide for STV1
1) Manolson MF, et al.  (1992) The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H(+)-ATPase. J Biol Chem 267(20):14294-303
2) Manolson MF, et al.  (1994) STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p. J Biol Chem 269(19):14064-74
3) Graham LA and Stevens TH  (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47
4) Kawasaki-Nishi S, et al.  (2001) Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation. J Biol Chem 276(21):17941-8
5) Forgac M  (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4
6) Kane PM  (1999) Biosynthesis and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr 31(1):49-56
7) Stevens TH and Forgac M  (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808
8) Manolson MF, et al.  (1992) Evidence for a conserved 95-120 kDa subunit associated with and essential for activity of V-ATPases. J Exp Biol 172():105-12
9) Ochotny NM, et al.  (2006) Effects of Human a3 and a4 Mutations That Result in Osteopetrosis and Distal Renal Tubular Acidosis on Yeast V-ATPase Expression and Activity. J Biol Chem 281(36):26102-11
10) Kornak U, et al.  (2000) Mutations in the a3 subunit of the vacuolar H(+)-ATPase cause infantile malignant osteopetrosis. Hum Mol Genet 9(13):2059-63