VTI1_YEAST
ID VTI1_YEAST Reviewed; 217 AA.
AC Q04338; D6W022;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=t-SNARE VTI1;
DE AltName: Full=Qb-SNARE VTI1;
DE AltName: Full=VPS10-interacting protein 1;
DE AltName: Full=Vesicle transport v-SNARE protein VTI1;
GN Name=VTI1; OrderedLocusNames=YMR197C; ORFNames=YM9646.10C;
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 [MRNA], AND INTERACTION WITH SED5 AND PEP12.
RX PubMed=9199167; DOI=10.1083/jcb.137.7.1511;
RA Fischer von Mollard G., Nothwehr S.F., Stevens T.H.;
RT "The yeast v-SNARE Vti1p mediates two vesicle transport pathways through
RT interactions with the t-SNAREs Sed5p and Pep12p.";
RL J. Cell Biol. 137:1511-1524(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-13; 21-34; 82-129; 140-156 AND 167-181, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (OCT-2005) to UniProtKB.
RN [5]
RP CHARACTERIZATION.
RX PubMed=9398683; DOI=10.1091/mbc.8.12.2659;
RA Lupashin V.V., Pokrovskaya I.D., McNew J.A., Waters M.G.;
RT "Characterization of a novel yeast SNARE protein implicated in Golgi
RT retrograde traffic.";
RL Mol. Biol. Cell 8:2659-2676(1997).
RN [6]
RP INTERACTION WITH TLG1 AND TLG2.
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 [7]
RP MUTAGENESIS OF SER-130; ALA-141; GLU-145; GLY-148; ILE-151; LEU-155 AND
RP GLN-158.
RX PubMed=9446565; DOI=10.1074/jbc.273.5.2624;
RA Fischer von Mollard G., Stevens T.H.;
RT "A human homolog can functionally replace the yeast vesicle-associated
RT SNARE Vti1p in two vesicle transport pathways.";
RL J. Biol. Chem. 273:2624-2630(1998).
RN [8]
RP FUNCTION IN HOMOTYPIC VACUOLE FUSION, AND SUBUNIT.
RX PubMed=10385523; DOI=10.1083/jcb.145.7.1435;
RA Ungermann C., Fischer von Mollard G., Jensen O.N., Margolis N.,
RA Stevens T.H., Wickner W.T.;
RT "Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex
RT on isolated vacuoles, are essential for homotypic fusion.";
RL J. Cell Biol. 145:1435-1442(1999).
RN [9]
RP INVOLVEMENT IN MULTIPLE TRAFFICKING STEPS.
RX PubMed=10359592; DOI=10.1091/mbc.10.6.1719;
RA Fischer von Mollard G., Stevens T.H.;
RT "The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple
RT membrane transport pathways to the vacuole.";
RL Mol. Biol. Cell 10:1719-1732(1999).
RN [10]
RP FUNCTION, AND INTERACTION WITH SNC2; TLG1 AND TLG2.
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 [11]
RP INTERACTION WITH SYN8.
RX PubMed=12453154; DOI=10.1034/j.1600-0854.2002.31207.x;
RA Lewis M.J., Pelham H.R.B.;
RT "A new yeast endosomal SNARE related to mammalian syntaxin 8.";
RL Traffic 3:922-929(2002).
RN [12]
RP FUNCTION.
RX PubMed=14981247; DOI=10.1073/pnas.0400271101;
RA Paumet F., Rahimian V., Rothman J.E.;
RT "The specificity of SNARE-dependent fusion is encoded in the SNARE motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3376-3380(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, 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 found in various SNARE complexes involved in multiple
CC transport pathways. The composition of the t-SNARE complexes is
CC specific for a limited number of v-SNAREs and therefore allows only the
CC vesicles carrying the matching v-SNARE to fuse.
CC {ECO:0000269|PubMed:10385523, ECO:0000269|PubMed:11739407,
CC ECO:0000269|PubMed:14981247}.
CC -!- SUBUNIT: Forms SNARE complexes with the t-SNAREs VAM3 and VAM7, and the
CC v-SNAREs NYV1 and YKT6 on vacuolar membranes, which are involved in
CC biosynthetic transport pathways to the vacuole and in homotypic vacuole
CC fusion. Forms SNARE complexes with the cis-Golgi t-SNARE SED5 and the
CC v-SNAREs SFT1 and YTK6, which are involved in retrograde traffic to the
CC cis-Golgi compartment. Forms SNARE complexes with the t-SNAREs TLG1 and
CC TLG2, and either the v-SNARE SNC1 or SNC2, which are involved in
CC traffic from early endosomes to the trans-Golgi network (TGN). Forms
CC SNARE complexes with the t-SNAREs PEP12 and either SYN8 or TLG1, and
CC the v-SNARE SNC1, which are involved in traffic from the TGN to the
CC prevacuolar compartment (PVC). {ECO:0000269|PubMed:10385523}.
CC -!- INTERACTION:
CC Q04338; P47160: ENT3; NbExp=7; IntAct=EBI-20519, EBI-25662;
CC Q04338; Q12255: NYV1; NbExp=11; IntAct=EBI-20519, EBI-35465;
CC Q04338; P32319: PEP1; NbExp=2; IntAct=EBI-20519, EBI-13123;
CC Q04338; Q01590: SED5; NbExp=2; IntAct=EBI-20519, EBI-16930;
CC Q04338; Q03322: TLG1; NbExp=8; IntAct=EBI-20519, EBI-38705;
CC Q04338; Q08144: TLG2; NbExp=6; IntAct=EBI-20519, EBI-19302;
CC Q04338; Q12241: VAM3; NbExp=13; IntAct=EBI-20519, EBI-20227;
CC Q04338; P36015: YKT6; NbExp=6; IntAct=EBI-20519, EBI-26982;
CC -!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane; Single-pass
CC type IV membrane protein. Golgi apparatus membrane; Single-pass type IV
CC membrane protein. Note=A small portion is localized in the Golgi
CC apparatus, the majority is localized in the PVC.
CC -!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
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DR EMBL; AF006074; AAC49745.1; -; mRNA.
DR EMBL; Z47815; CAA87819.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10096.1; -; Genomic_DNA.
DR PIR; S50926; S50926.
DR RefSeq; NP_013924.1; NM_001182704.1.
DR PDB; 3ONJ; X-ray; 1.92 A; A=3-99.
DR PDB; 3ONL; X-ray; 2.20 A; C=3-99.
DR PDBsum; 3ONJ; -.
DR PDBsum; 3ONL; -.
DR AlphaFoldDB; Q04338; -.
DR SMR; Q04338; -.
DR BioGRID; 35375; 705.
DR ComplexPortal; CPX-1887; Vacuolar SNARE complex VAM3-VTI1-VAM7-YKT6.
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-5401; Vacuolar SNARE complex VAM3-VTI1-VAM7-NYV1.
DR ComplexPortal; CPX-5421; Endosomal SNARE complex PEP12-VTI1-SYN8-YKT6.
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-5424; Endosomal SNARE complex PEP12-VTI1-SYN8-SNC1.
DR ComplexPortal; CPX-5461; Endosomal SNARE complex PEP12-VTI1-SYN8-SNC2.
DR ComplexPortal; CPX-5462; Endosomal SNARE complex PEP12-VTI1-TLG1-SNC2.
DR DIP; DIP-2145N; -.
DR IntAct; Q04338; 17.
DR MINT; Q04338; -.
DR STRING; 4932.YMR197C; -.
DR TCDB; 1.F.1.1.2; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; Q04338; -.
DR MaxQB; Q04338; -.
DR PaxDb; Q04338; -.
DR PRIDE; Q04338; -.
DR EnsemblFungi; YMR197C_mRNA; YMR197C; YMR197C.
DR GeneID; 855237; -.
DR KEGG; sce:YMR197C; -.
DR SGD; S000004810; VTI1.
DR VEuPathDB; FungiDB:YMR197C; -.
DR eggNOG; KOG1666; Eukaryota.
DR GeneTree; ENSGT00950000183192; -.
DR HOGENOM; CLU_075474_0_0_1; -.
DR InParanoid; Q04338; -.
DR OMA; RGRVESH; -.
DR BioCyc; YEAST:G3O-32884-MON; -.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR PRO; PR:Q04338; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04338; protein.
DR GO; GO:0000421; C:autophagosome membrane; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:SGD.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0031201; C:SNARE complex; IPI:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IDA:ComplexPortal.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0061911; P:amphisome-lysosome fusion; IC:ComplexPortal.
DR GO; GO:0006897; P:endocytosis; IC:ComplexPortal.
DR GO; GO:0006895; P:Golgi to endosome transport; IC:ComplexPortal.
DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IC:ComplexPortal.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0007036; P:vacuolar calcium ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:ComplexPortal.
DR GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
DR Gene3D; 1.20.58.400; -; 1.
DR InterPro; IPR027027; GOSR2/Membrin/Bos1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
DR InterPro; IPR038407; v-SNARE_N_sf.
DR InterPro; IPR007705; Vesicle_trsprt_v-SNARE_N.
DR Pfam; PF05008; V-SNARE; 1.
DR PIRSF; PIRSF028865; Membrin-2; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..217
FT /note="t-SNARE VTI1"
FT /id="PRO_0000218232"
FT TOPO_DOM 2..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..217
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 124..186
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 130
FT /note="S->P: In VTI1-2; exhibits defects in TGN to PVC
FT transport at nonpermissive temperature; when associated
FT with T-151."
FT /evidence="ECO:0000269|PubMed:9446565"
FT MUTAGEN 141
FT /note="A->S: In VTI1-12; blocks constitutively the traffic
FT from the late Golgi to the vacuole and blocks the transport
FT to the cis-Golgi compartment at nonpermissive temperature;
FT when associated with R-158."
FT /evidence="ECO:0000269|PubMed:9446565"
FT MUTAGEN 145
FT /note="E->G: In VTI1-11; displays a block in traffic to the
FT PVC and an additional defect in retrograde traffic to the
FT cis-Golgi; when associated with F-155."
FT /evidence="ECO:0000269|PubMed:9446565"
FT MUTAGEN 145
FT /note="E->K: In VTI1-1; exhibits defects in TGN to PVC
FT transport at nonpermissive temperature; when associated
FT with R-148."
FT /evidence="ECO:0000269|PubMed:9446565"
FT MUTAGEN 148
FT /note="G->R: In VTI1-1; exhibits defects in TGN to PVC
FT transport at nonpermissive temperature; when associated
FT with K-145."
FT /evidence="ECO:0000269|PubMed:9446565"
FT MUTAGEN 151
FT /note="I->T: In VTI1-2; exhibits defects in TGN to PVC
FT transport at nonpermissive temperature; when associated
FT with P-130."
FT /evidence="ECO:0000269|PubMed:9446565"
FT MUTAGEN 155
FT /note="L->F: In VTI1-11; displays a block in traffic to the
FT PVC and an additional defect in retrograde traffic to the
FT cis-Golgi; when associated with G-145."
FT /evidence="ECO:0000269|PubMed:9446565"
FT MUTAGEN 158
FT /note="Q->R: In VTI1-12; blocks constitutively the traffic
FT from the late Golgi to the vacuole and blocks the transport
FT to the cis-Golgi compartment at nonpermissive temperature;
FT when associated with S-141."
FT /evidence="ECO:0000269|PubMed:9446565"
FT HELIX 4..25
FT /evidence="ECO:0007829|PDB:3ONJ"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:3ONJ"
FT HELIX 31..62
FT /evidence="ECO:0007829|PDB:3ONJ"
FT HELIX 66..86
FT /evidence="ECO:0007829|PDB:3ONJ"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:3ONJ"
SQ SEQUENCE 217 AA; 24668 MW; E55B4DA3B40FAD67 CRC64;
MSSLLISYES DFKTTLEQAK ASLAEAPSQP LSQRNTTLKH VEQQQDELFD LLDQMDVEVN
NSIGDASERA TYKAKLREWK KTIQSDIKRP LQSLVDSGDR DRLFGDLNAS NIDDDQRQQL
LSNHAILQKS GDRLKDASRI ANETEGIGSQ IMMDLRSQRE TLENARQTLF QADSYVDKSI
KTLKTMTRRL VANKFISYAI IAVLILLILL VLFSKFK
