Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

t-SNARE VTI1

Gene

VTI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Keywordsi

Biological processProtein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32884-MONOMER

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

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
PaxDbiQ04338
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

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi35375, 685 interactors
DIPiDIP-2145N
IntActiQ04338, 11 interactors
MINTiQ04338
STRINGi4932.YMR197C

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

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000116573
InParanoidiQ04338
KOiK08493
OMAiEELKYAP
OrthoDBiEOG092C4VGK

Family and domain databases

Gene3Di1.20.58.400, 1 hit
InterProiView protein in InterPro
IPR027027 GOSR2/Membrin/Bos1
IPR010989 SNARE
IPR000727 T_SNARE_dom
IPR038407 v-SNARE_N_sf
IPR007705 Vesicle_trsprt_v-SNARE_N
PfamiView protein in Pfam
PF05008 V-SNARE, 1 hit
PIRSFiPIRSF028865 Membrin-2, 1 hit
SMARTiView protein in SMART
SM00397 t_SNARE, 1 hit
SUPFAMiSSF47661 SSF47661, 1 hit
PROSITEiView protein in PROSITE
PS50192 T_SNARE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiVTI1_YEAST
AccessioniPrimary (citable) accession number: Q04338
Secondary accession number(s): D6W022
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 165 of the entry and version 3 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health