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Identification
NameT-SNARE affecting a late Golgi compartment protein 1
Synonyms
  • Syntaxin TLG1
Gene NameTLG1
Enzyme ClassNot Available
Biological Properties
General FunctionInvolved in SNAP receptor activity
Specific FunctionSNARE 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
Cellular LocationGolgi apparatus, trans-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).
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
GO Classification
Component
cell part
membrane
Function
protein binding
binding
SNAP receptor activity
Process
protein transport
intracellular protein transport
establishment of localization
transport
vesicle-mediated transport
Golgi vesicle transport
Gene Properties
Chromosome LocationNot Available
Locus
Gene Sequence>675 bp ATGAACAACAGTGAAGATCCGTTTCAACAAGTTGTTAAGGACACCAAGGAGCAATTGAAC CGCATAAACAATTACATAACTCGTCACAATACTGCTGGTGATGACGATCAAGAGGAGGAA ATACAAGATATTTTAAAGGATGTTGAGGAAACAATAGTTGATTTGGACAGAAGCATAATC GTAATGAAAAGGGATGAAAACGAAGACGTGAGTGGTAGGGAAGCACAAGTTAAAAATATA AAACAGCAACTTGATGCTCTGAAGTTGCGTTTTGATCGAAGAATACAGGAATCTACTCAA ACAACTATTCCTCTAGAAGAGACGGTGGAAAATTCAACACTTAACACCAGCATGGCTGAG AACAATGATGGTGGTATGTCCAATCCGTTTCAGGAACAAATGTTAAGAGAACAAGATGTT CATTTAGATGGTATTCACAAGACAATGCAAAATTTGCATATTCAAGCTCAAACAATGGGG GATGAATTAGAGAACCAGGGACAATTGTTGGATAATATGGACGAGGGTATGGACGGTGTT GTAAATAAGCTGGCTAGAGGTCGTAGGCAATTGGAATGGGTCTACGAAAAAAATAAAGAA AAATACGACGATTGTTGTATAGGACTTCTTATTGTCGTCTTGATAGTTTTATTAGTTTTG GCATTCATTGCTTGA
Protein Properties
Pfam Domain Function
Protein Residues224
Protein Molecular Weight25816.69922
Protein Theoretical pI4.23
Signalling Regions
  • None
Transmembrane Regions
  • 204-224
Protein Sequence>T-SNARE affecting a late Golgi compartment protein 1 MNNSEDPFQQVVKDTKEQLNRINNYITRHNTAGDDDQEEEIQDILKDVEETIVDLDRSII VMKRDENEDVSGREAQVKNIKQQLDALKLRFDRRIQESTQTTIPLEETVENSTLNTSMAE NNDGGMSNPFQEQMLREQDVHLDGIHKTMQNLHIQAQTMGDELENQGQLLDNMDEGMDGV VNKLARGRRQLEWVYEKNKEKYDDCCIGLLIVVLIVLLVLAFIA
References
External Links
ResourceLink
Saccharomyces Genome Database TLG1
Uniprot IDQ03322
Uniprot NameTLG1_YEAST
GenBank Gene IDAY558178
Genebank Protein ID45270246
General Reference
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, 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., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., 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., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Holthuis, J. C., Nichols, B. J., Dhruvakumar, S., Pelham, H. R. (1998). "Two syntaxin homologues in the TGN/endosomal system of yeast." EMBO J 17:113-126.9427746
  • Coe, J. G., Lim, A. C., Xu, J., Hong, W. (1999). "A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae." Mol Biol Cell 10:2407-2423.10397773
  • Bock, J. B., Matern, H. T., Peden, A. A., Scheller, R. H. (2001). "A genomic perspective on membrane compartment organization." Nature 409:839-841.11237004
  • Siniossoglou, S., Pelham, H. R. (2001). "An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes." EMBO J 20:5991-5998.11689439
  • Paumet, F., Brugger, B., Parlati, F., McNew, J. A., Sollner, T. H., Rothman, J. E. (2001). "A t-SNARE of the endocytic pathway must be activated for fusion." J Cell Biol 155:961-968.11739407
  • Gurunathan, S., Marash, M., Weinberger, A., Gerst, J. E. (2002). "t-SNARE phosphorylation regulates endocytosis in yeast." Mol Biol Cell 13:1594-1607.12006655
  • Siniossoglou, S., Pelham, H. R. (2002). "Vps51p links the VFT complex to the SNARE Tlg1p." J Biol Chem 277:48318-48324.12377769
  • Conibear, E., Cleck, J. N., Stevens, T. H. (2003). "Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p." Mol Biol Cell 14:1610-1623.12686613
  • Burri, L., Lithgow, T. (2004). "A complete set of SNAREs in yeast." Traffic 5:45-52.14675424
  • Valdez-Taubas, J., Pelham, H. (2005). "Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation." EMBO J 24:2524-2532.15973437