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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-114608. Platelet degranulation.
R-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)DescriptionActionsGraphical viewLength
Topological domaini2 – 194CytoplasmicSequence analysisAdd BLAST193
Transmembranei195 – 215Helical; Anchor for type IV membrane proteinSequence analysisAdd BLAST21
Topological domaini216 – 217VesicularSequence analysis2

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)DescriptionActionsGraphical viewLength
Mutagenesisi130S → P in VTI1-2; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with T-151. 1 Publication1
Mutagenesisi141A → 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 Publication1
Mutagenesisi145E → 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 Publication1
Mutagenesisi145E → K in VTI1-1; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with R-148. 1 Publication1
Mutagenesisi148G → R in VTI1-1; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with K-145. 1 Publication1
Mutagenesisi151I → T in VTI1-2; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with P-130. 1 Publication1
Mutagenesisi155L → 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 Publication1
Mutagenesisi158Q → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002182322 – 217t-SNARE VTI1Add BLAST216

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei110PhosphoserineCombined sources1
Modified residuei149PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ04338.
PRIDEiQ04338.

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 interactors.
DIPiDIP-2145N.
IntActiQ04338. 10 interactors.
MINTiMINT-545063.

Structurei

Secondary structure

1217
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 25Combined sources22
Helixi26 – 28Combined sources3
Helixi31 – 62Combined sources32
Helixi66 – 86Combined sources21
Helixi88 – 96Combined sources9

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini124 – 186t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd BLAST63

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.
OrthoDBiEOG092C4VGK.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ONJX-ray1.92A3-99[»]
3ONLX-ray2.20C3-99[»]
ProteinModelPortaliQ04338.
SMRiQ04338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35375. 81 interactors.
DIPiDIP-2145N.
IntActiQ04338. 10 interactors.
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.
PRIDEiQ04338.

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.
OrthoDBiEOG092C4VGK.

Enzyme and pathway databases

BioCyciYEAST:G3O-32884-MONOMER.
ReactomeiR-SCE-114608. Platelet degranulation.
R-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...

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: November 2, 2016
This is version 154 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.