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Q03322 (TLG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-SNARE affecting a late Golgi compartment protein 1
Alternative name(s):
Syntaxin TLG1
Gene names
Name:TLG1
Ordered Locus Names:YDR468C
ORF Names:D8035.11
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

SNARE protein (of Qc type) involved in membrane fusion probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. Upon vesicle tethering to the target membrane, which requires additional proteins, a SNARE-pin is formed. This is a very stable 4 parallel alpha-helical coil bundle consisting of 4 SNARE domains (usually one of each type: Qa, Qb, Qc, and R), of which at least one is anchored in the opposite membrane. The formation of the SNARE-pin is believed to bring the two membranes in close proximity and to provide the energy to drive membrane fusion. Through its interaction with the VFT (or GARP) complex, it may also contribute to vesicle recognition specificity and tethering. Regulation of SNARE-pin formation also seems to depend on the phosphorylation state of the protein, phosphorylation by TPK1 causing inhibition and dephosphorylation by SIT4 activation. Ref.4 Ref.5 Ref.7 Ref.8 Ref.10 Ref.11

Subunit structure

Interacts in a SNARE-pin with the SNAREs TLG2 (Qa), VTI1 (Qb), and SNC1 or SNC2 (R). Interacts with VPS51 of the VFT (or GARP) complex. Ref.4 Ref.5 Ref.7 Ref.8 Ref.10

Subcellular location

Golgi apparatustrans-Golgi network membrane; Single-pass type IV membrane protein Probable. Early endosome membrane; Single-pass type IV membrane protein Probable. Late endosome membrane; Single-pass type IV membrane protein Probable. Note: Probably shuttling between TGN and early/late endosome. Ref.4 Ref.5

Post-translational modification

Phosphorylated at Thr-31 by TPK1 and dephosphorylated by SIT4. Ref.9

Palmitoylated by SWF1, which prevents its recognition and ubiquitination by TUL1 and its subsequent degradation. Ref.13

Sequence similarities

Belongs to the syntaxin family.

Contains 1 t-SNARE coiled-coil homology domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VPS51P361166EBI-38705,EBI-26352

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 224224T-SNARE affecting a late Golgi compartment protein 1
PRO_0000210277

Regions

Topological domain1 – 203203Cytoplasmic Potential
Transmembrane204 – 22421Helical; Anchor for type IV membrane protein; Potential
Domain132 – 19463t-SNARE coiled-coil homology
Region1 – 106106Interaction with VPS51
Coiled coil35 – 10167 Potential

Amino acid modifications

Modified residue311Phosphothreonine; by PKA Ref.9
Lipidation2051S-palmitoyl cysteine Probable
Lipidation2061S-palmitoyl cysteine Probable

Experimental info

Mutagenesis311T → A: Results in an aktivated t-SNARE that confers endocytosis, but not exocytosis. Ref.9 Ref.13
Mutagenesis205 – 2062CC → SS or LL: Not palmitoylated, rapidly degraded in a TUL1-dependent manner. Ref.13

Secondary structure

....... 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03322 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B33251C18645EF74

FASTA22425,817
        10         20         30         40         50         60 
MNNSEDPFQQ VVKDTKEQLN RINNYITRHN TAGDDDQEEE IQDILKDVEE TIVDLDRSII 

        70         80         90        100        110        120 
VMKRDENEDV SGREAQVKNI KQQLDALKLR FDRRIQESTQ TTIPLEETVE NSTLNTSMAE 

       130        140        150        160        170        180 
NNDGGMSNPF QEQMLREQDV HLDGIHKTMQ NLHIQAQTMG DELENQGQLL DNMDEGMDGV 

       190        200        210        220 
VNKLARGRRQ LEWVYEKNKE KYDDCCIGLL IVVLIVLLVL AFIA 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"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: FUNCTION, INTERACTION WITH SNARE PROTEINS, SUBCELLULAR LOCATION.
[5]"A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae."
Coe J.G., Lim A.C., Xu J., Hong W.
Mol. Biol. Cell 10:2407-2423(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SNARE PROTEINS AND SEC17, STRAIN SPECIFIC EFFECTS, SUBCELLULAR LOCATION.
[6]"A genomic perspective on membrane compartment organization."
Bock J.B., Matern H.T., Peden A.A., Scheller R.H.
Nature 409:839-841(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CLASSIFICATION.
[7]"An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes."
Siniossoglou S., Pelham H.R.B.
EMBO J. 20:5991-5998(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VFT COMPLEX.
[8]"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 SPECIFICITY WITH SNARE PROTEINS.
[9]"t-SNARE phosphorylation regulates endocytosis in yeast."
Gurunathan S., Marash M., Weinberger A., Gerst J.E.
Mol. Biol. Cell 13:1594-1607(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-31, MUTAGENESIS OF THR-31.
[10]"Vps51p links the VFT complex to the SNARE Tlg1p."
Siniossoglou S., Pelham H.R.B.
J. Biol. Chem. 277:48318-48324(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VPS51.
[11]"Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p."
Conibear E., Cleck J.N., Stevens T.H.
Mol. Biol. Cell 14:1610-1623(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VFT COMPLEX IN RETROGRADE TRAFFIC FROM EARLY/LATE ENDOSOME TO TGN.
[12]"A complete set of SNAREs in yeast."
Burri L., Lithgow T.
Traffic 5:45-52(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation."
Valdez-Taubas J., Pelham H.R.B.
EMBO J. 24:2524-2532(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-205 AND CYS-206, MUTAGENESIS OF 205-CYS-CYS-206.
[14]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33050 Genomic DNA. Translation: AAB64925.1.
AY558178 Genomic DNA. Translation: AAS56504.1.
BK006938 Genomic DNA. Translation: DAA12302.1.
PIRS69635.
RefSeqNP_010756.3. NM_001180776.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C5IX-ray2.30T1-101[»]
2C5JX-ray2.10A/B1-95[»]
2C5KX-ray2.05T1-95[»]
ProteinModelPortalQ03322.
SMRQ03322. Positions 6-94, 133-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32521. 49 interactions.
DIPDIP-2058N.
IntActQ03322. 7 interactions.
MINTMINT-490335.
STRING4932.YDR468C.

Proteomic databases

PaxDbQ03322.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR468C; YDR468C; YDR468C.
GeneID852079.
KEGGsce:YDR468C.

Organism-specific databases

CYGDYDR468c.
SGDS000002876. TLG1.

Phylogenomic databases

eggNOGNOG255019.
HOGENOMHOG000248369.
KOK08499.
OMARRQLEWV.
OrthoDBEOG71GB6W.

Enzyme and pathway databases

BioCycYEAST:G3O-29995-MONOMER.

Gene expression databases

GenevestigatorQ03322.

Family and domain databases

InterProIPR015260. Syntaxin-6_N.
IPR006012. Syntaxin/epimorphin_CS.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamPF05739. SNARE. 1 hit.
PF09177. Syntaxin-6_N. 1 hit.
[Graphical view]
SMARTSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMSSF47661. SSF47661. 1 hit.
PROSITEPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ03322.
NextBio970385.
PROQ03322.

Entry information

Entry nameTLG1_YEAST
AccessionPrimary (citable) accession number: Q03322
Secondary accession number(s): D6VT92
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references