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Protein

Vacuolar v-SNARE NYV1

Gene

NYV1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Vacuolar v-SNARE required for docking. Only involved in homotypic vacuole fusion. Required for Ca2+ efflux from the vacuolar lumen, a required signal for subsequent membrane fusion events, by inhibiting vacuolar Ca2+-ATPase PMC1 and promoting Ca2+ release when forming trans-SNARE assemblies during the docking step.4 Publications

GO - Molecular functioni

  • SNAP receptor activity Source: SGD
  • SNARE binding Source: GO_Central

GO - Biological processi

  • endocytosis Source: GO_Central
  • exocytosis Source: GO_Central
  • vacuole fusion, non-autophagic Source: SGD
  • vesicle fusion Source: SGD
  • vesicle-mediated transport Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-32243-MONOMER.

Protein family/group databases

TCDBi1.F.1.1.2. the synaptosomal vesicle fusion pore (svf-pore) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar v-SNARE NYV1
Short name:
R-SNARE NYV1
Alternative name(s):
New v-SNARE 1
Synaptobrevin NYV1
Gene namesi
Name:NYV1
Synonyms:MAM2
Ordered Locus Names:YLR093C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR093C.
SGDiS000004083. NYV1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 231231CytoplasmicSequence analysisAdd
BLAST
Transmembranei232 – 25221Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST
Topological domaini253 – 2531VacuolarSequence analysis

GO - Cellular componenti

  • fungal-type vacuole membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • SNARE complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 253253Vacuolar v-SNARE NYV1PRO_0000206780Add
BLAST

Proteomic databases

MaxQBiQ12255.
TopDownProteomicsiQ12255.

PTM databases

iPTMnetiQ12255.

Interactioni

Subunit structurei

Present in a pentameric cis-SNARE complex composed of the v-SNAREs NYV1, VTI1 and YKT6, and the t-SNAREs VAM3 and VAM7 on vacuolar membranes. Interacts in trans with the cognate t-SNARE VAM3 during the docking step of homotypic vacuolar fusion. Interacts with the vacuolar transporter chaperone (VTC) complex and the vacuolar Ca2+-ATPase PMC1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VAM3Q1224110EBI-35465,EBI-20227

GO - Molecular functioni

  • SNAP receptor activity Source: SGD
  • SNARE binding Source: GO_Central

Protein-protein interaction databases

BioGridi31366. 66 interactions.
DIPiDIP-2248N.
IntActiQ12255. 13 interactions.
MINTiMINT-4494777.

Structurei

Secondary structure

1
253
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1610Combined sources
Beta strandi20 – 223Combined sources
Beta strandi26 – 305Combined sources
Helixi43 – 5210Combined sources
Helixi55 – 573Combined sources
Beta strandi65 – 684Combined sources
Beta strandi74 – 818Combined sources
Beta strandi90 – 978Combined sources
Helixi104 – 1129Combined sources
Helixi124 – 14118Combined sources
Turni142 – 1443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FZ0NMR-A1-149[»]
ProteinModelPortaliQ12255.
SMRiQ12255. Positions 1-149, 171-227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12255.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini167 – 22761v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the synaptobrevin family.Curated
Contains 1 v-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000113898.
InParanoidiQ12255.
KOiK08564.
OMAiLIDGFDC.
OrthoDBiEOG722JMS.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
IPR019005. Vacuolar_R-SNAR_Nyv1_N_dom.
[Graphical view]
PfamiPF09426. Nyv1_N. 1 hit.
PF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS50892. V_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12255-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRFNVSYVE VIKNGETISS CFQPFQKNEN YGTITSANEQ ITPVIFHNLI
60 70 80 90 100
MDMVLPKVVP IKGNKVTKMS MNLIDGFDCF YSTDDHDPKT VYVCFTLVDM
110 120 130 140 150
PKILPIRILS GLQEYESNAT NELLSSHVGQ ILDSFHEELV EYRNQTLNSS
160 170 180 190 200
GNGQSSNGNG QNTISDIGDA TEDQIKDVIQ IMNDNIDKFL ERQERVSLLV
210 220 230 240 250
DKTSQLNSSS NKFRRKAVNI KEIMWWQKVK NITLLTFTII LFVSAAFMFF

YLW
Length:253
Mass (Da):28,964
Last modified:October 17, 2006 - v2
Checksum:i494B587CF0F85997
GO

Sequence cautioni

The sequence AAB67537.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAT92805.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAA97654.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73265 Genomic DNA. Translation: CAA97654.1. Sequence problems.
U53876 Genomic DNA. Translation: AAB67537.1. Sequence problems.
AY692786 Genomic DNA. Translation: AAT92805.1. Sequence problems.
BK006945 Genomic DNA. Translation: DAA09409.1.
PIRiS64927.
RefSeqiNP_013194.2. NM_001181980.1.

Genome annotation databases

EnsemblFungiiYLR093C; YLR093C; YLR093C.
GeneIDi850782.
KEGGisce:YLR093C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73265 Genomic DNA. Translation: CAA97654.1. Sequence problems.
U53876 Genomic DNA. Translation: AAB67537.1. Sequence problems.
AY692786 Genomic DNA. Translation: AAT92805.1. Sequence problems.
BK006945 Genomic DNA. Translation: DAA09409.1.
PIRiS64927.
RefSeqiNP_013194.2. NM_001181980.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FZ0NMR-A1-149[»]
ProteinModelPortaliQ12255.
SMRiQ12255. Positions 1-149, 171-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31366. 66 interactions.
DIPiDIP-2248N.
IntActiQ12255. 13 interactions.
MINTiMINT-4494777.

Protein family/group databases

TCDBi1.F.1.1.2. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

iPTMnetiQ12255.

Proteomic databases

MaxQBiQ12255.
TopDownProteomicsiQ12255.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR093C; YLR093C; YLR093C.
GeneIDi850782.
KEGGisce:YLR093C.

Organism-specific databases

EuPathDBiFungiDB:YLR093C.
SGDiS000004083. NYV1.

Phylogenomic databases

HOGENOMiHOG000113898.
InParanoidiQ12255.
KOiK08564.
OMAiLIDGFDC.
OrthoDBiEOG722JMS.

Enzyme and pathway databases

BioCyciYEAST:G3O-32243-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12255.
PROiQ12255.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
IPR019005. Vacuolar_R-SNAR_Nyv1_N_dom.
[Graphical view]
PfamiPF09426. Nyv1_N. 1 hit.
PF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Bienvenut W.V., Peters C.
    Submitted (MAY-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 14-27; 108-143 AND 196-214, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Homotypic vacuolar fusion mediated by t- and v-SNAREs."
    Nichols B.J., Ungermann C., Pelham H.R.B., Wickner W.T., Haas A.
    Nature 387:199-202(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VAM3.
  6. "Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion."
    Ungermann C., Fischer von Mollard G., Jensen O.N., Margolis N., Stevens T.H., Wickner W.T.
    J. Cell Biol. 145:1435-1442(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  7. "Test of intron predictions reveals novel splice sites, alternatively spliced mRNAs and new introns in meiotically regulated genes of yeast."
    Davis C.A., Grate L., Spingola M., Ares M. Jr.
    Nucleic Acids Res. 28:1700-1706(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF INTRON.
  8. "Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p."
    Takita Y., Engstrom L., Ungermann C., Cunningham K.W.
    J. Biol. Chem. 276:6200-6206(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PMC1.
  9. "The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-complex formation."
    Mueller O., Bayer M.J., Peters C., Andersen J.S., Mann M., Mayer A.
    EMBO J. 21:259-269(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE VTC COMPLEX.
  10. "Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen."
    Merz A.J., Wickner W.T.
    J. Cell Biol. 164:195-206(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Identification of the yeast R-SNARE Nyv1p as a novel longin domain-containing protein."
    Wen W., Chen L., Wu H., Sun X., Zhang M., Banfield D.K.
    Mol. Biol. Cell 17:4282-4299(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-149.

Entry informationi

Entry nameiNYV1_YEAST
AccessioniPrimary (citable) accession number: Q12255
Secondary accession number(s): D6VY93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 17, 2006
Last modified: July 6, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1885 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.