Q03322 (TLG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	224 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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. 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.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endosome Golgi apparatus Membrane
Domain	Coiled coil Transmembrane Transmembrane helix
PTM	Lipoprotein Palmitate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi vesicle transport Inferred from electronic annotation. Source: InterPro endocytosis Inferred from mutant phenotype Ref.4. Source: SGD intracellular protein transport Inferred from electronic annotation. Source: InterPro vesicle fusion Inferred from direct assay Ref.8. Source: SGD
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell SNARE complex Inferred from physical interaction Ref.5. Source: SGD early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endosome Inferred from direct assay Ref.4. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell trans-Golgi network Inferred from direct assay Ref.13. Source: SGD
Molecular_function	SNAP receptor activity Inferred from direct assay PubMed 14981247. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VPS51	P36116	6	EBI-38705,EBI-26352

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 224

224

T-SNARE affecting a late Golgi compartment protein 1

PRO_0000210277

Regions

Topological domain

1 – 203

203

Cytoplasmic Potential

Transmembrane

204 – 224

21

Helical; Anchor for type IV membrane protein; Potential

Domain

132 – 194

63

t-SNARE coiled-coil homology

Region

1 – 106

106

Interaction with VPS51

Coiled coil

35 – 101

67

Potential

Amino acid modifications

Modified residue

31

1

Phosphothreonine

Lipidation

205

1

S-palmitoyl cysteine Probable

Lipidation

206

1

S-palmitoyl cysteine Probable

Experimental info

Mutagenesis

205 – 206

2

CC → SS or LL: Not palmitoylated, rapidly degraded in a TUL1-dependent manner. Ref.13

Secondary structure

1

.

.

.

.

.

.

.

224

Helix Strand Turn

Details...

Helix

7 – 28

22

Helix

38 – 63

26

Helix

71 – 92

22

Sequences

	Sequence		Length	Mass (Da)
	Q03322 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B33251C18645EF74	FASTA	224	25,817
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
[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.
+	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.

PIR

S69635.

RefSeq

NP_010756.3. NM_001180776.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q03322.

SMR

Q03322. Positions 6-94.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2058N.

IntAct

Q03322. 5 interactions.

MINT

MINT-490335.

STRING

4932.YDR468C.

Proteomic databases

PaxDb

Q03322.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR468C; YDR468C; YDR468C.

GeneID

852079.

KEGG

sce:YDR468C.

Organism-specific databases

CYGD

YDR468c.

SGD

S000002876. TLG1.

Phylogenomic databases

eggNOG

NOG255019.

HOGENOM

HOG000248369.

KO

K08499.

OMA

RYNDCCI.

OrthoDB

EOG4X3MB5.

Enzyme and pathway databases

BioCyc

YEAST:G3O-29995-MONOMER.

Gene expression databases

Genevestigator

Q03322.

GermOnline

YDR468C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR015260. Syntaxin-6_N.
IPR006012. Syntaxin/epimorphin_CS.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]

Pfam

PF05739. SNARE. 1 hit.
PF09177. Syntaxin-6_N. 1 hit.
[Graphical view]

SMART

SM00397. t_SNARE. 1 hit.
[Graphical view]

SUPFAM

SSF47661. t-snare. 1 hit.

PROSITE

PS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q03322.

NextBio

970385.

Entry information

Entry name

TLG1_YEAST

Accession

Primary (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:	May 29, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program