TLG1_YEAST
ID TLG1_YEAST Reviewed; 224 AA.
AC Q03322; D6VT92;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=t-SNARE affecting a late Golgi compartment protein 1;
DE AltName: Full=Syntaxin TLG1;
GN Name=TLG1; OrderedLocusNames=YDR468C; ORFNames=D8035.11;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, INTERACTION WITH SNARE PROTEINS, AND SUBCELLULAR LOCATION.
RX PubMed=9427746; DOI=10.1093/emboj/17.1.113;
RA Holthuis J.C.M., Nichols B.J., Dhruvakumar S., Pelham H.R.B.;
RT "Two syntaxin homologues in the TGN/endosomal system of yeast.";
RL EMBO J. 17:113-126(1998).
RN [5]
RP FUNCTION, INTERACTION WITH SNARE PROTEINS AND SEC17, STRAIN SPECIFIC
RP EFFECTS, AND SUBCELLULAR LOCATION.
RX PubMed=10397773; DOI=10.1091/mbc.10.7.2407;
RA Coe J.G., Lim A.C., Xu J., Hong W.;
RT "A role for Tlg1p in the transport of proteins within the Golgi apparatus
RT of Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 10:2407-2423(1999).
RN [6]
RP CLASSIFICATION.
RX PubMed=11237004; DOI=10.1038/35057024;
RA Bock J.B., Matern H.T., Peden A.A., Scheller R.H.;
RT "A genomic perspective on membrane compartment organization.";
RL Nature 409:839-841(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH VFT COMPLEX.
RX PubMed=11689439; DOI=10.1093/emboj/20.21.5991;
RA Siniossoglou S., Pelham H.R.B.;
RT "An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion
RT of vesicles with late Golgi membranes.";
RL EMBO J. 20:5991-5998(2001).
RN [8]
RP FUNCTION, AND INTERACTION SPECIFICITY WITH SNARE PROTEINS.
RX PubMed=11739407; DOI=10.1083/jcb.200104092;
RA Paumet F., Brugger B., Parlati F., McNew J.A., Sollner T.H., Rothman J.E.;
RT "A t-SNARE of the endocytic pathway must be activated for fusion.";
RL J. Cell Biol. 155:961-968(2001).
RN [9]
RP PHOSPHORYLATION AT THR-31, AND MUTAGENESIS OF THR-31.
RX PubMed=12006655; DOI=10.1091/mbc.01-11-0541;
RA Gurunathan S., Marash M., Weinberger A., Gerst J.E.;
RT "t-SNARE phosphorylation regulates endocytosis in yeast.";
RL Mol. Biol. Cell 13:1594-1607(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH VPS51.
RX PubMed=12377769; DOI=10.1074/jbc.m209428200;
RA Siniossoglou S., Pelham H.R.B.;
RT "Vps51p links the VFT complex to the SNARE Tlg1p.";
RL J. Biol. Chem. 277:48318-48324(2002).
RN [11]
RP FUNCTION, AND VFT COMPLEX IN RETROGRADE TRAFFIC FROM EARLY/LATE ENDOSOME TO
RP TGN.
RX PubMed=12686613; DOI=10.1091/mbc.e02-10-0654;
RA Conibear E., Cleck J.N., Stevens T.H.;
RT "Vps51p mediates the association of the GARP (Vps52/53/54) complex with the
RT late Golgi t-SNARE Tlg1p.";
RL Mol. Biol. Cell 14:1610-1623(2003).
RN [12]
RP REVIEW.
RX PubMed=14675424; DOI=10.1046/j.1600-0854.2003.00151.x;
RA Burri L., Lithgow T.;
RT "A complete set of SNAREs in yeast.";
RL Traffic 5:45-52(2004).
RN [13]
RP PALMITOYLATION AT CYS-205 AND CYS-206, AND MUTAGENESIS OF 205-CYS-CYS-206.
RX PubMed=15973437; DOI=10.1038/sj.emboj.7600724;
RA Valdez-Taubas J., Pelham H.R.B.;
RT "Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its
RT ubiquitination and degradation.";
RL EMBO J. 24:2524-2532(2005).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: SNARE protein (of Qc type) involved in membrane fusion
CC probably in retrograde traffic of cytosolic double-membrane vesicles
CC derived from both, early and possibly late endosomes/PVC (prevacuolar
CC compartment) back to the trans-Golgi network (TGN or late Golgi). It
CC has been reported to function both as a (target membrane) t-SNARE and
CC as a (vesicle) v-SNARE. Upon vesicle tethering to the target membrane,
CC which requires additional proteins, a SNARE-pin is formed. This is a
CC very stable 4 parallel alpha-helical coil bundle consisting of 4 SNARE
CC domains (usually one of each type: Qa, Qb, Qc, and R), of which at
CC least one is anchored in the opposite membrane. The formation of the
CC SNARE-pin is believed to bring the two membranes in close proximity and
CC to provide the energy to drive membrane fusion. Through its interaction
CC with the VFT (or GARP) complex, it may also contribute to vesicle
CC recognition specificity and tethering. Regulation of SNARE-pin
CC formation also seems to depend on the phosphorylation state of the
CC protein, phosphorylation by TPK1 causing inhibition and
CC dephosphorylation by SIT4 activation. {ECO:0000269|PubMed:10397773,
CC ECO:0000269|PubMed:11689439, ECO:0000269|PubMed:11739407,
CC ECO:0000269|PubMed:12377769, ECO:0000269|PubMed:12686613,
CC ECO:0000269|PubMed:9427746}.
CC -!- SUBUNIT: Interacts in a SNARE-pin with the SNAREs TLG2 (Qa), VTI1 (Qb),
CC and SNC1 or SNC2 (R). Interacts with VPS51 of the VFT (or GARP)
CC complex. {ECO:0000269|PubMed:10397773, ECO:0000269|PubMed:11689439,
CC ECO:0000269|PubMed:11739407, ECO:0000269|PubMed:12377769,
CC ECO:0000269|PubMed:9427746}.
CC -!- INTERACTION:
CC Q03322; P32602: SEC17; NbExp=3; IntAct=EBI-38705, EBI-16558;
CC Q03322; Q08144: TLG2; NbExp=3; IntAct=EBI-38705, EBI-19302;
CC Q03322; P38932: VPS45; NbExp=3; IntAct=EBI-38705, EBI-20444;
CC Q03322; P36116: VPS51; NbExp=6; IntAct=EBI-38705, EBI-26352;
CC Q03322; Q04338: VTI1; NbExp=8; IntAct=EBI-38705, EBI-20519;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
CC Early endosome membrane {ECO:0000305}; Single-pass type IV membrane
CC protein {ECO:0000305}. Late endosome membrane {ECO:0000305}; Single-
CC pass type IV membrane protein {ECO:0000305}. Note=Probably shuttling
CC between TGN and early/late endosome.
CC -!- PTM: Phosphorylated at Thr-31 by TPK1 and dephosphorylated by SIT4.
CC {ECO:0000269|PubMed:12006655}.
CC -!- PTM: Palmitoylated by SWF1, which prevents its recognition and
CC ubiquitination by TUL1 and its subsequent degradation.
CC {ECO:0000269|PubMed:15973437}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U33050; AAB64925.1; -; Genomic_DNA.
DR EMBL; AY558178; AAS56504.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12302.1; -; Genomic_DNA.
DR PIR; S69635; S69635.
DR RefSeq; NP_010756.3; NM_001180776.3.
DR PDB; 2C5I; X-ray; 2.30 A; T=1-101.
DR PDB; 2C5J; X-ray; 2.10 A; A/B=1-95.
DR PDB; 2C5K; X-ray; 2.05 A; T=1-95.
DR PDBsum; 2C5I; -.
DR PDBsum; 2C5J; -.
DR PDBsum; 2C5K; -.
DR AlphaFoldDB; Q03322; -.
DR SMR; Q03322; -.
DR BioGRID; 32521; 293.
DR ComplexPortal; CPX-5321; Endosomal SNARE complex TLG2-VTI1-TLG1-SNC2.
DR ComplexPortal; CPX-5322; Endosomal SNARE complex TLG2-VTI1-TLG1-SNC1.
DR ComplexPortal; CPX-5422; Endosomal SNARE complex PEP12-VTI1-TLG1-YKT6.
DR ComplexPortal; CPX-5423; Endosomal SNARE complex PEP12-VTI1-TLG1-SNC1.
DR ComplexPortal; CPX-5462; Endosomal SNARE complex PEP12-VTI1-TLG1-SNC2.
DR DIP; DIP-2058N; -.
DR IntAct; Q03322; 12.
DR MINT; Q03322; -.
DR STRING; 4932.YDR468C; -.
DR iPTMnet; Q03322; -.
DR SwissPalm; Q03322; -.
DR MaxQB; Q03322; -.
DR PaxDb; Q03322; -.
DR PRIDE; Q03322; -.
DR EnsemblFungi; YDR468C_mRNA; YDR468C; YDR468C.
DR GeneID; 852079; -.
DR KEGG; sce:YDR468C; -.
DR SGD; S000002876; TLG1.
DR VEuPathDB; FungiDB:YDR468C; -.
DR eggNOG; KOG3202; Eukaryota.
DR HOGENOM; CLU_061883_0_2_1; -.
DR InParanoid; Q03322; -.
DR OMA; DMKDHMV; -.
DR BioCyc; YEAST:G3O-29995-MON; -.
DR Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR EvolutionaryTrace; Q03322; -.
DR PRO; PR:Q03322; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03322; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0031201; C:SNARE complex; IPI:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0006895; P:Golgi to endosome transport; IC:ComplexPortal.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IC:ComplexPortal.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IC:ComplexPortal.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IC:ComplexPortal.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Endosome; Golgi apparatus; Isopeptide bond;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..224
FT /note="t-SNARE affecting a late Golgi compartment protein
FT 1"
FT /id="PRO_0000210277"
FT TOPO_DOM 1..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 132..194
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..106
FT /note="Interaction with VPS51"
FT /evidence="ECO:0000269|PubMed:12377769"
FT COILED 35..101
FT /evidence="ECO:0000255"
FT MOD_RES 31
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:12006655"
FT LIPID 205
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:15973437"
FT LIPID 206
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:15973437"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 31
FT /note="T->A: Results in an aktivated t-SNARE that confers
FT endocytosis, but not exocytosis."
FT /evidence="ECO:0000269|PubMed:12006655"
FT MUTAGEN 205..206
FT /note="CC->SS,LL: Not palmitoylated, rapidly degraded in a
FT TUL1-dependent manner."
FT /evidence="ECO:0000269|PubMed:15973437"
FT HELIX 7..28
FT /evidence="ECO:0007829|PDB:2C5K"
FT HELIX 38..63
FT /evidence="ECO:0007829|PDB:2C5K"
FT HELIX 71..92
FT /evidence="ECO:0007829|PDB:2C5K"
SQ SEQUENCE 224 AA; 25817 MW; B33251C18645EF74 CRC64;
MNNSEDPFQQ VVKDTKEQLN RINNYITRHN TAGDDDQEEE IQDILKDVEE TIVDLDRSII
VMKRDENEDV SGREAQVKNI KQQLDALKLR FDRRIQESTQ TTIPLEETVE NSTLNTSMAE
NNDGGMSNPF QEQMLREQDV HLDGIHKTMQ NLHIQAQTMG DELENQGQLL DNMDEGMDGV
VNKLARGRRQ LEWVYEKNKE KYDDCCIGLL IVVLIVLLVL AFIA
