NYV1/YLR093C Summary Help

Standard Name NYV1 1
Systematic Name YLR093C
Alias MAM2 2
Feature Type ORF, Verified
Description v-SNARE component of the vacuolar SNARE complex; involved in vesicle fusion; inhibits ATP-dependent Ca(2+) transport activity of Pmc1p in the vacuolar membrane (3, 4 and see Summary Paragraph)
Name Description New Yeast V-SNARE 1
Chromosomal Location
ChrXII:327415 to 326513 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All NYV1 GO evidence and references
  View Computational GO annotations for NYV1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 3 genes
Classical genetics
Large-scale survey
126 total interaction(s) for 63 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 15
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 53
  • Biochemical Activity: 1
  • Co-fractionation: 5
  • Co-purification: 4
  • FRET: 1
  • PCA: 1
  • Reconstituted Complex: 19
  • Two-hybrid: 18

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 2
  • Phenotypic Enhancement: 2
  • Phenotypic Suppression: 1
  • Positive Genetic: 1
  • Synthetic Lethality: 1

Expression Summary
Length (a.a.) 253
Molecular Weight (Da) 28,964
Isoelectric Point (pI) 5.43
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXII:327415 to 326513 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 2000-07-14
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..16 327415..327400 2011-02-03 2000-07-14
Intron 17..157 327399..327259 2011-02-03 2000-07-14
CDS 158..903 327258..326513 2011-02-03 2000-07-14
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004083

NYV1 encodes a SNARE (soluble NSF attachment protein receptor) protein that is involved in homotypic vacuole fusion (1, 5). Nyv1p forms a SNARE complex with Vam7p, Vam3p, and Vti1p to mediate vacuole docking and fusion (5, 6, 3) but overexpression of Vam7p allows the SNARE Ykt6p to substitute for Nyv1p in this SNARE complex (7). Nyv1p-mediated fusion is positively regulated by phosphatidlyinositide phosphates (8). Functionally, Nyv1p is classified as a v-SNARE although by sequence it belongs to the R-SNARE family of proteins (reviewed in 9). Nyv1p is sorted to the vacuolar membrane by the (AP)3 adaptin pathway via a longin domain present in its N-terminus (10). In addition to its role in vacuolar fusion, Nyv1p is also involved in the negative regulation of the Ca(2+)-ATPase Pmc1p (4) and Vid (vacuole import and degradation) vesicle trafficking to the vacuole (11). nyv1 null mutants do not show the vaculolar fragmentation seen with other SNARE mutants, possibly due to the redundancy of Nyv1p and Ykt6p (7). Mutants lacking nyv1 do have a shortened lifespan (12) and NYV1 overproducing cells are sensitive to calcium (4).

Last updated: 2011-01-21 Contact SGD

References cited on this page View Complete Literature Guide for NYV1
1) Nichols BJ, et al.  (1997) Homotypic vacuolar fusion mediated by t- and v-SNAREs. Nature 387(6629):199-202
2) Entian KD, et al.  (1999) Functional analysis of 150 deletion mutants in Saccharomyces cerevisiae by a systematic approach. Mol Gen Genet 262(4-5):683-702
3) Ungermann C, et al.  (1999) Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. J Cell Biol 145(7):1435-42
4) Takita Y, et al.  (2001) Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p. J Biol Chem 276(9):6200-6
5) Fischer von Mollard G and Stevens TH  (1999) The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole. Mol Biol Cell 10(6):1719-32
6) Ungermann C, et al.  (1998) A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion. J Cell Biol 140(1):61-9
7) Thorngren N, et al.  (2004) A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion. EMBO J 23(14):2765-76
8) Xu H and Wickner W  (2010) Phosphoinositides Function Asymmetrically for Membrane Fusion, Promoting Tethering and 3Q-SNARE Subcomplex Assembly. J Biol Chem 285(50):39359-65
9) Hong W  (2005) SNAREs and traffic. Biochim Biophys Acta 1744(3):493-517
10) Wen W, et al.  (2006) Identification of the Yeast R-SNARE Nyv1p as a Novel Longin Domain-containing Protein. Mol Biol Cell 17(10):4282-99
11) Brown CR, et al.  (2003) The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery. J Biol Chem 278(28):25688-99
12) Tang F, et al.  (2008) A life-span extending form of autophagy employs the vacuole-vacuole fusion machinery. Autophagy 4(7):874-86