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Protein

t-SNARE VTI1

Gene

VTI1

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

t-SNARE found in various SNARE complexes involved in multiple transport pathways. The composition of the t-SNARE complexes is specific for a limited number of v-SNAREs and therefore allows only the vesicles carrying the matching v-SNARE to fuse.3 Publications

GO - Molecular functioni

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

GO - Biological processi

  • ER to Golgi vesicle-mediated transport Source: GO_Central
  • Golgi to vacuole transport Source: SGD
  • intra-Golgi vesicle-mediated transport Source: SGD
  • macroautophagy Source: SGD
  • protein targeting to vacuole Source: GO_Central
  • retrograde transport, endosome to Golgi Source: GO_Central
  • vacuole fusion, non-autophagic Source: SGD
  • vesicle fusion Source: SGD
  • vesicle fusion with Golgi apparatus Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32884-MONOMER.
ReactomeiR-SCE-6811440. Retrograde transport at the Trans-Golgi-Network.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
t-SNARE VTI1
Alternative name(s):
Qb-SNARE VTI1
VPS10-interacting protein 1
Vesicle transport v-SNARE protein VTI1
Gene namesi
Name:VTI1
Ordered Locus Names:YMR197C
ORF Names:YM9646.10C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR197C.
SGDiS000004810. VTI1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 194193CytoplasmicSequence analysisAdd
BLAST
Transmembranei195 – 21521Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST
Topological domaini216 – 2172VesicularSequence analysis

GO - Cellular componenti

  • cytosol Source: GOC
  • endoplasmic reticulum membrane Source: GO_Central
  • ER to Golgi transport vesicle membrane Source: GO_Central
  • integral component of Golgi membrane Source: SGD
  • late endosome membrane Source: GO_Central
  • SNARE complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi130 – 1301S → P in VTI1-2; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with T-151. 1 Publication
Mutagenesisi141 – 1411A → S in VTI1-12; blocks constitutively the traffic from the late Golgi to the vacuole and blocks the transport to the cis-Golgi compartment at nonpermissive temperature; when associated with R-158. 1 Publication
Mutagenesisi145 – 1451E → G in VTI1-11; displays a block in traffic to the PVC and an additional defect in retrograde traffic to the cis-Golgi; when associated with F-155. 1 Publication
Mutagenesisi145 – 1451E → K in VTI1-1; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with R-148. 1 Publication
Mutagenesisi148 – 1481G → R in VTI1-1; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with K-145. 1 Publication
Mutagenesisi151 – 1511I → T in VTI1-2; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with P-130. 1 Publication
Mutagenesisi155 – 1551L → F in VTI1-11; displays a block in traffic to the PVC and an additional defect in retrograde traffic to the cis-Golgi; when associated with G-145. 1 Publication
Mutagenesisi158 – 1581Q → R in VTI1-12; blocks constitutively the traffic from the late Golgi to the vacuole and blocks the transport to the cis-Golgi compartment at nonpermissive temperature; when associated with S-141. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 217216t-SNARE VTI1PRO_0000218232Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei149 – 1491PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ04338.

PTM databases

iPTMnetiQ04338.

Interactioni

Subunit structurei

Forms SNARE complexes with the t-SNAREs VAM3 and VAM7, and the v-SNAREs NYV1 and YKT6 on vacuolar membranes, which are involved in biosynthetic transport pathways to the vacuole and in homotypic vacuole fusion. Forms SNARE complexes with the cis-Golgi t-SNARE SED5 and the v-SNAREs SFT1 and YTK6, which are involved in retrograde traffic to the cis-Golgi compartment. Forms SNARE complexes with the t-SNAREs TLG1 and TLG2, and either the v-SNARE SNC1 or SNC2, which are involved in traffic from early endosomes to the trans-Golgi network (TGN). Forms SNARE complexes with the t-SNAREs PEP12 and either SYN8 or TLG1, and the v-SNARE SNC1, which are involved in traffic from the TGN to the prevacuolar compartment (PVC).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
YKT6P360156EBI-20519,EBI-26982

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi35375. 81 interactions.
DIPiDIP-2145N.
IntActiQ04338. 10 interactions.
MINTiMINT-545063.

Structurei

Secondary structure

1
217
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2522Combined sources
Helixi26 – 283Combined sources
Helixi31 – 6232Combined sources
Helixi66 – 8621Combined sources
Helixi88 – 969Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ONJX-ray1.92A3-99[»]
3ONLX-ray2.20C3-99[»]
ProteinModelPortaliQ04338.
SMRiQ04338. Positions 3-99, 117-191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 18663t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the VTI1 family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000063466.
HOGENOMiHOG000116573.
InParanoidiQ04338.
KOiK08493.
OMAiIRMANDQ.
OrthoDBiEOG7X0VV1.

Family and domain databases

InterProiIPR027027. GOSR2/Membrin/Bos1.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
IPR007705. Vesicle_trsprt_v-SNARE_N.
[Graphical view]
PfamiPF05008. V-SNARE. 1 hit.
[Graphical view]
PIRSFiPIRSF028865. Membrin-2. 1 hit.
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q04338-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSLLISYES DFKTTLEQAK ASLAEAPSQP LSQRNTTLKH VEQQQDELFD
60 70 80 90 100
LLDQMDVEVN NSIGDASERA TYKAKLREWK KTIQSDIKRP LQSLVDSGDR
110 120 130 140 150
DRLFGDLNAS NIDDDQRQQL LSNHAILQKS GDRLKDASRI ANETEGIGSQ
160 170 180 190 200
IMMDLRSQRE TLENARQTLF QADSYVDKSI KTLKTMTRRL VANKFISYAI
210
IAVLILLILL VLFSKFK
Length:217
Mass (Da):24,668
Last modified:January 23, 2007 - v3
Checksum:iE55B4DA3B40FAD67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006074 mRNA. Translation: AAC49745.1.
Z47815 Genomic DNA. Translation: CAA87819.1.
BK006946 Genomic DNA. Translation: DAA10096.1.
PIRiS50926.
RefSeqiNP_013924.1. NM_001182704.1.

Genome annotation databases

EnsemblFungiiYMR197C; YMR197C; YMR197C.
GeneIDi855237.
KEGGisce:YMR197C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006074 mRNA. Translation: AAC49745.1.
Z47815 Genomic DNA. Translation: CAA87819.1.
BK006946 Genomic DNA. Translation: DAA10096.1.
PIRiS50926.
RefSeqiNP_013924.1. NM_001182704.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ONJX-ray1.92A3-99[»]
3ONLX-ray2.20C3-99[»]
ProteinModelPortaliQ04338.
SMRiQ04338. Positions 3-99, 117-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35375. 81 interactions.
DIPiDIP-2145N.
IntActiQ04338. 10 interactions.
MINTiMINT-545063.

Protein family/group databases

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

PTM databases

iPTMnetiQ04338.

Proteomic databases

MaxQBiQ04338.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR197C; YMR197C; YMR197C.
GeneIDi855237.
KEGGisce:YMR197C.

Organism-specific databases

EuPathDBiFungiDB:YMR197C.
SGDiS000004810. VTI1.

Phylogenomic databases

GeneTreeiENSGT00530000063466.
HOGENOMiHOG000116573.
InParanoidiQ04338.
KOiK08493.
OMAiIRMANDQ.
OrthoDBiEOG7X0VV1.

Enzyme and pathway databases

BioCyciYEAST:G3O-32884-MONOMER.
ReactomeiR-SCE-6811440. Retrograde transport at the Trans-Golgi-Network.

Miscellaneous databases

PROiQ04338.

Family and domain databases

InterProiIPR027027. GOSR2/Membrin/Bos1.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
IPR007705. Vesicle_trsprt_v-SNARE_N.
[Graphical view]
PfamiPF05008. V-SNARE. 1 hit.
[Graphical view]
PIRSFiPIRSF028865. Membrin-2. 1 hit.
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p."
    Fischer von Mollard G., Nothwehr S.F., Stevens T.H.
    J. Cell Biol. 137:1511-1524(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SED5 AND PEP12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Bienvenut W.V., Peters C.
    Submitted (OCT-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 21-34; 82-129; 140-156 AND 167-181, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic."
    Lupashin V.V., Pokrovskaya I.D., McNew J.A., Waters M.G.
    Mol. Biol. Cell 8:2659-2676(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Two syntaxin homologues in the TGN/endosomal system of yeast."
    Holthuis J.C.M., Nichols B.J., Dhruvakumar S., Pelham H.R.B.
    EMBO J. 17:113-126(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TLG1 AND TLG2.
  7. "A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways."
    Fischer von Mollard G., Stevens T.H.
    J. Biol. Chem. 273:2624-2630(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-130; ALA-141; GLU-145; GLY-148; ILE-151; LEU-155 AND GLN-158.
  8. "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 IN HOMOTYPIC VACUOLE FUSION, SUBUNIT.
  9. "The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole."
    Fischer von Mollard G., Stevens T.H.
    Mol. Biol. Cell 10:1719-1732(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MULTIPLE TRAFFICKING STEPS.
  10. "A t-SNARE of the endocytic pathway must be activated for fusion."
    Paumet F., Brugger B., Parlati F., McNew J.A., Sollner T.H., Rothman J.E.
    J. Cell Biol. 155:961-968(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNC2; TLG1 AND TLG2.
  11. "A new yeast endosomal SNARE related to mammalian syntaxin 8."
    Lewis M.J., Pelham H.R.B.
    Traffic 3:922-929(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYN8.
  12. "The specificity of SNARE-dependent fusion is encoded in the SNARE motif."
    Paumet F., Rahimian V., Rothman J.E.
    Proc. Natl. Acad. Sci. U.S.A. 101:3376-3380(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVTI1_YEAST
AccessioniPrimary (citable) accession number: Q04338
Secondary accession number(s): D6W022
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.