TLG2_YEAST
ID TLG2_YEAST Reviewed; 397 AA.
AC Q08144; D6W248; E9P933;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=t-SNARE affecting a late Golgi compartment protein 2;
DE AltName: Full=Syntaxin TLG2;
GN Name=TLG2; OrderedLocusNames=YOL018C;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 CHARACTERIZATION.
RX PubMed=9565594; DOI=10.1074/jbc.273.19.11719;
RA Abeliovich H., Grote E., Novick P., Ferro-Novick S.;
RT "Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic
RT structures.";
RL J. Biol. Chem. 273:11719-11727(1998).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9763449; DOI=10.1091/mbc.9.10.2873;
RA Seron K., Tieaho V., Prescianotto-Baschong C., Aust T., Blondel M.O.,
RA Guillaud P., Devilliers G., Rossanese O.W., Glick B.S., Riezman H.,
RA Keranen S., Haguenauer-Tsapis R.;
RT "A yeast t-SNARE involved in endocytosis.";
RL Mol. Biol. Cell 9:2873-2889(1998).
RN [6]
RP INTERACTION WITH VPS45.
RX PubMed=9930650; DOI=10.1016/s0171-9335(98)80084-8;
RA Nichols B.J., Holthuis J.C., Pelham H.R.;
RT "The Sec1p homologue Vps45p binds to the syntaxin Tlg2p.";
RL Eur. J. Cell Biol. 77:263-268(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: t-SNARE that functions in transport from the endosome to the
CC late Golgi and on the endocytic pathway.
CC -!- SUBUNIT: Interacts with VPS45. {ECO:0000269|PubMed:9930650}.
CC -!- INTERACTION:
CC Q08144; P32602: SEC17; NbExp=2; IntAct=EBI-19302, EBI-16558;
CC Q08144; Q03322: TLG1; NbExp=3; IntAct=EBI-19302, EBI-38705;
CC Q08144; P38932: VPS45; NbExp=4; IntAct=EBI-19302, EBI-20444;
CC Q08144; Q04338: VTI1; NbExp=6; IntAct=EBI-19302, EBI-20519;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane;
CC Single-pass type IV membrane protein. Endosome membrane; Single-pass
CC type IV membrane protein.
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; Z74760; CAA99017.1; -; Genomic_DNA.
DR EMBL; AY693218; AAT93237.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10764.1; -; Genomic_DNA.
DR PIR; S66700; S66700.
DR RefSeq; NP_014624.1; NM_001183272.1.
DR AlphaFoldDB; Q08144; -.
DR SMR; Q08144; -.
DR BioGRID; 34385; 643.
DR ComplexPortal; CPX-5321; Endosomal SNARE complex TLG2-VTI1-TLG1-SNC2.
DR ComplexPortal; CPX-5322; Endosomal SNARE complex TLG2-VTI1-TLG1-SNC1.
DR DIP; DIP-4244N; -.
DR IntAct; Q08144; 10.
DR MINT; Q08144; -.
DR STRING; 4932.YOL018C; -.
DR iPTMnet; Q08144; -.
DR SwissPalm; Q08144; -.
DR MaxQB; Q08144; -.
DR PaxDb; Q08144; -.
DR PRIDE; Q08144; -.
DR EnsemblFungi; YOL018C_mRNA; YOL018C; YOL018C.
DR GeneID; 854142; -.
DR KEGG; sce:YOL018C; -.
DR SGD; S000005378; TLG2.
DR VEuPathDB; FungiDB:YOL018C; -.
DR eggNOG; KOG0809; Eukaryota.
DR GeneTree; ENSGT01050000244948; -.
DR HOGENOM; CLU_038177_0_1_1; -.
DR InParanoid; Q08144; -.
DR OMA; QTMIIDQ; -.
DR BioCyc; YEAST:G3O-33434-MON; -.
DR Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR PRO; PR:Q08144; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08144; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0031303; C:integral component of endosome membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0006896; P:Golgi to vacuole transport; IGI:SGD.
DR GO; GO:0006673; P:inositol phosphoceramide metabolic process; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006675; P:mannosyl-inositol phosphorylceramide metabolic process; IMP:SGD.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IGI:SGD.
DR GO; GO:0009306; P:protein secretion; IMP:SGD.
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; IPR028673; STX16.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR PANTHER; PTHR19957:SF83; PTHR19957:SF83; 1.
DR Pfam; PF05739; SNARE; 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 Coiled coil; Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..397
FT /note="t-SNARE affecting a late Golgi compartment protein
FT 2"
FT /id="PRO_0000210279"
FT TOPO_DOM 1..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..397
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 244..306
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 341..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 74..96
FT /evidence="ECO:0000255"
FT COMPBIAS 343..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 397
FT /note="L -> R (in Ref. 3; AAT93237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 45875 MW; CEBD6FE11278B1F0 CRC64;
MFRDRTNLFL SYRRTFPHNI TFSSGKAPLG DDQDIEMGTY PMMNMSHDIS ARLTDERKNK
HENHSDALPP IFIDIAQDVD DYLLEVRRLS EQLAKVYRKN SLPGFEDKSH DEALIEDLSF
KVIQMLQKCY AVMKRLKTIY NSQFVDGKQL SREELIILDN LQKIYAEKIQ TESNKFRVLQ
NNYLKFLNKD DLKPIRNKAS AENTLLLDDE EEEAAREKRE GLDIEDYSKR TLQRQQQLHD
TSAEAYLRER DEEITQLARG VLEVSTIFRE MQDLVVDQGT IVDRIDYNLE NTVVELKSAD
KELNKATHYQ KRTQKCKVIL LLTLCVIALF FFVMLKPHGG GSGGRNNGSN KYNNDDNKTV
NNSHDDGSNT HINDEESNLP SIVEVTESEN DALDDLL
