Q04338 (VTI1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
t-SNARE VTI1

Alternative name(s):
Qb-SNARE VTI1
VPS10-interacting protein 1
Vesicle transport v-SNARE protein VTI1

Gene names

Name:	VTI1
Ordered Locus Names:	YMR197C
ORF Names:	YM9646.10C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	217 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.10 Ref.12
Subunit structure	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). Ref.8
Subcellular location	Prevacuolar compartment membrane; Single-pass type IV membrane protein. Golgi apparatus membrane; Single-pass type IV membrane protein. Note: A small portion is localized in the Golgi apparatus, the majority is localized in the PVC.
Sequence similarities	Belongs to the VTI1 family. Contains 1 t-SNARE coiled-coil homology domain.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Golgi apparatus Membrane
Domain	Coiled coil Transmembrane Transmembrane helix
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	Golgi to vacuole transport Inferred from mutant phenotype Ref.1. Source: SGD intra-Golgi vesicle-mediated transport Inferred from mutant phenotype Ref.5. Source: SGD intracellular protein transport Inferred from electronic annotation. Source: InterPro vacuole fusion, non-autophagic Inferred from mutant phenotype Ref.8. Source: SGD vesicle fusion Inferred from direct assay Ref.10. Source: SGD
Cellular component	integral to Golgi membrane Inferred from direct assay Ref.5. Source: SGD late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	SNAP receptor activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YKT6	P36015	6	EBI-20519,EBI-26982

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 217

216

t-SNARE VTI1

PRO_0000218232

Regions

Topological domain

2 – 194

193

Cytoplasmic Potential

Transmembrane

195 – 215

21

Helical; Anchor for type IV membrane protein; Potential

Topological domain

216 – 217

2

Vesicular Potential

Domain

124 – 186

63

t-SNARE coiled-coil homology

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.4

Modified residue

110

1

Phosphoserine Ref.13

Modified residue

149

1

Phosphoserine Ref.13

Experimental info

Mutagenesis

130

1

S → P in VTI1-2; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with T-151. Ref.7

Mutagenesis

141

1

A → 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. Ref.7

Mutagenesis

145

1

E → 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. Ref.7

Mutagenesis

145

1

E → K in VTI1-1; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with R-148. Ref.7

Mutagenesis

148

1

G → R in VTI1-1; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with K-145. Ref.7

Mutagenesis

151

1

I → T in VTI1-2; exhibits defects in TGN to PVC transport at nonpermissive temperature; when associated with P-130. Ref.7

Mutagenesis

155

1

L → 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. Ref.7

Mutagenesis

158

1

Q → 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. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

217

Helix Strand Turn

Details...

Helix

4 – 25

22

Helix

26 – 28

3

Helix

31 – 62

32

Helix

66 – 86

21

Helix

88 – 96

9

Sequences

	Sequence		Length	Mass (Da)
	Q04338 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E55B4DA3B40FAD67	FASTA	217	24,668
	10 20 30 40 50 60 MSSLLISYES DFKTTLEQAK ASLAEAPSQP LSQRNTTLKH VEQQQDELFD LLDQMDVEVN 70 80 90 100 110 120 NSIGDASERA TYKAKLREWK KTIQSDIKRP LQSLVDSGDR DRLFGDLNAS NIDDDQRQQL 130 140 150 160 170 180 LSNHAILQKS GDRLKDASRI ANETEGIGSQ IMMDLRSQRE TLENARQTLF QADSYVDKSI 190 200 210 KTLKTMTRRL VANKFISYAI IAVLILLILL VLFSKFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9199167] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SED5 AND PEP12.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, 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: 9398683] [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: 9427746] [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: 9446565] [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: 10385523] [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: 10359592] [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: 11739407] [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: 12453154] [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: 14981247] [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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-149, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF006074 mRNA. Translation: AAC49745.1.
Z47815 Genomic DNA. Translation: CAA87819.1.
BK006946 Genomic DNA. Translation: DAA10096.1.

PIR

S50926.

RefSeq

NP_013924.1. NM_001182704.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ONJ	X-ray	1.92	A	3-99	[»]
3ONL	X-ray	2.20	C	3-99	[»]

ProteinModelPortal

Q04338.

SMR

Q04338. Positions 3-99, 115-191.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2145N.

IntAct

Q04338. 10 interactions.

MINT

MINT-545063.

STRING

Q04338.

Proteomic databases

PeptideAtlas

Q04338.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YMR197C; YMR197C; YMR197C.

GeneID

855237.

KEGG

sce:YMR197C.

NMPDR

fig|4932.3.peg.4977.

Organism-specific databases

SGD

S000004810. VTI1.

Phylogenomic databases

eggNOG

fuNOG08849.

GeneTree

EFGT00050000005996.

HOGENOM

HBG384598.

OMA

KGMARRM.

OrthoDB

EOG44F9KK.

Gene expression databases

ArrayExpress

Q04338.

Genevestigator

Q04338.

GermOnline

YMR197C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
IPR007705. Vesicle_trsprt_v-SNARE_N.
[Graphical view]

KO

K08493.

Pfam

PF05008. V-SNARE. 1 hit.
[Graphical view]

SMART

SM00397. t_SNARE. 1 hit.
[Graphical view]

SUPFAM

SSF47661. t-snare. 1 hit.

PROSITE

PS50192. T_SNARE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

978783.

Entry information

Entry name

VTI1_YEAST

Accession

Primary (citable) accession number: Q04338
Secondary accession number(s): D6W022

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program