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Q03322

- TLG1_YEAST

UniProt

Q03322 - TLG1_YEAST

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Protein

T-SNARE affecting a late Golgi compartment protein 1

Gene

TLG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.6 Publications

GO - Molecular functioni

  1. SNAP receptor activity Source: SGD

GO - Biological processi

  1. endocytosis Source: SGD
  2. Golgi vesicle transport Source: InterPro
  3. intracellular protein transport Source: InterPro
  4. vesicle fusion Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29995-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
T-SNARE affecting a late Golgi compartment protein 1
Alternative name(s):
Syntaxin TLG1
Gene namesi
Name:TLG1
Ordered Locus Names:YDR468C
ORF Names:D8035.11
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR468c.
SGDiS000002876. TLG1.

Subcellular locationi

GO - Cellular componenti

  1. endosome Source: SGD
  2. integral component of membrane Source: UniProtKB-KW
  3. SNARE complex Source: SGD
  4. trans-Golgi network Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311T → A: Results in an aktivated t-SNARE that confers endocytosis, but not exocytosis. 1 Publication
Mutagenesisi205 – 2062CC → SS or LL: Not palmitoylated, rapidly degraded in a TUL1-dependent manner. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 224224T-SNARE affecting a late Golgi compartment protein 1PRO_0000210277Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphothreonine; by PKA1 Publication
Lipidationi205 – 2051S-palmitoyl cysteine1 Publication
Lipidationi206 – 2061S-palmitoyl cysteine1 Publication

Post-translational modificationi

Phosphorylated at Thr-31 by TPK1 and dephosphorylated by SIT4.1 Publication
Palmitoylated by SWF1, which prevents its recognition and ubiquitination by TUL1 and its subsequent degradation.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ03322.
PaxDbiQ03322.

Expressioni

Gene expression databases

GenevestigatoriQ03322.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VPS51P361166EBI-38705,EBI-26352

Protein-protein interaction databases

BioGridi32521. 50 interactions.
DIPiDIP-2058N.
IntActiQ03322. 7 interactions.
MINTiMINT-490335.
STRINGi4932.YDR468C.

Structurei

Secondary structure

1
224
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2822
Helixi38 – 6326
Helixi71 – 9222

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C5IX-ray2.30T1-101[»]
2C5JX-ray2.10A/B1-95[»]
2C5KX-ray2.05T1-95[»]
ProteinModelPortaliQ03322.
SMRiQ03322. Positions 6-94.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03322.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 203203CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei204 – 22421Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini132 – 19463t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 106106Interaction with VPS51Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili35 – 10167Sequence AnalysisAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG255019.
HOGENOMiHOG000248369.
InParanoidiQ03322.
KOiK08499.
OMAiRRQLEWV.
OrthoDBiEOG71GB6W.

Family and domain databases

InterProiIPR015260. Syntaxin-6_N.
IPR006012. Syntaxin/epimorphin_CS.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
PF09177. Syntaxin-6_N. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03322-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNSEDPFQQ VVKDTKEQLN RINNYITRHN TAGDDDQEEE IQDILKDVEE
60 70 80 90 100
TIVDLDRSII VMKRDENEDV SGREAQVKNI KQQLDALKLR FDRRIQESTQ
110 120 130 140 150
TTIPLEETVE NSTLNTSMAE NNDGGMSNPF QEQMLREQDV HLDGIHKTMQ
160 170 180 190 200
NLHIQAQTMG DELENQGQLL DNMDEGMDGV VNKLARGRRQ LEWVYEKNKE
210 220
KYDDCCIGLL IVVLIVLLVL AFIA
Length:224
Mass (Da):25,817
Last modified:November 1, 1996 - v1
Checksum:iB33251C18645EF74
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33050 Genomic DNA. Translation: AAB64925.1.
AY558178 Genomic DNA. Translation: AAS56504.1.
BK006938 Genomic DNA. Translation: DAA12302.1.
PIRiS69635.
RefSeqiNP_010756.3. NM_001180776.3.

Genome annotation databases

EnsemblFungiiYDR468C; YDR468C; YDR468C.
GeneIDi852079.
KEGGisce:YDR468C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33050 Genomic DNA. Translation: AAB64925.1 .
AY558178 Genomic DNA. Translation: AAS56504.1 .
BK006938 Genomic DNA. Translation: DAA12302.1 .
PIRi S69635.
RefSeqi NP_010756.3. NM_001180776.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C5I X-ray 2.30 T 1-101 [» ]
2C5J X-ray 2.10 A/B 1-95 [» ]
2C5K X-ray 2.05 T 1-95 [» ]
ProteinModelPortali Q03322.
SMRi Q03322. Positions 6-94.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32521. 50 interactions.
DIPi DIP-2058N.
IntActi Q03322. 7 interactions.
MINTi MINT-490335.
STRINGi 4932.YDR468C.

Proteomic databases

MaxQBi Q03322.
PaxDbi Q03322.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR468C ; YDR468C ; YDR468C .
GeneIDi 852079.
KEGGi sce:YDR468C.

Organism-specific databases

CYGDi YDR468c.
SGDi S000002876. TLG1.

Phylogenomic databases

eggNOGi NOG255019.
HOGENOMi HOG000248369.
InParanoidi Q03322.
KOi K08499.
OMAi RRQLEWV.
OrthoDBi EOG71GB6W.

Enzyme and pathway databases

BioCyci YEAST:G3O-29995-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q03322.
NextBioi 970385.
PROi Q03322.

Gene expression databases

Genevestigatori Q03322.

Family and domain databases

InterProi IPR015260. Syntaxin-6_N.
IPR006012. Syntaxin/epimorphin_CS.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view ]
Pfami PF05739. SNARE. 1 hit.
PF09177. Syntaxin-6_N. 1 hit.
[Graphical view ]
SMARTi SM00397. t_SNARE. 1 hit.
[Graphical view ]
SUPFAMi SSF47661. SSF47661. 1 hit.
PROSITEi PS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. 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].

Entry informationi

Entry nameiTLG1_YEAST
AccessioniPrimary (citable) accession number: Q03322
Secondary accession number(s): D6VT92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3