ID VTC1_YEAST Reviewed; 129 AA. AC P40046; D3DLX7; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 180. DE RecName: Full=Vacuolar transporter chaperone complex subunit 1 {ECO:0000305}; DE AltName: Full=Negative regulator of CDC42 protein 1; DE AltName: Full=Phosphate metabolism protein 4 {ECO:0000303|PubMed:11102525}; DE AltName: Full=SPX-dependent polyphosphate polymerase VTC subunit 1 {ECO:0000305}; DE AltName: Full=Vacuolar membrane polyphosphate polymerase accessory subunit 1 {ECO:0000305}; DE Short=PolyP polymerase; GN Name=VTC1 {ECO:0000303|PubMed:10480897}; GN Synonyms=NRF1, PHM4 {ECO:0000303|PubMed:11102525}; GN OrderedLocusNames=YER072W; 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=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(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 PROTEIN SEQUENCE OF 2-9; 14-31 AND 91-98, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RA Bienvenut W.V., Peters C.; RL Submitted (MAY-2005) to UniProtKB. RN [4] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10480897; DOI=10.1074/jbc.274.38.26885; RA Cohen A., Perzov N., Nelson H., Nelson N.; RT "A novel family of yeast chaperons involved in the distribution of V-ATPase RT and other membrane proteins."; RL J. Biol. Chem. 274:26885-26893(1999). RN [5] RP INDUCTION. RX PubMed=11102525; DOI=10.1091/mbc.11.12.4309; RA Ogawa N., DeRisi J.L., Brown P.O.; RT "New components of a system for phosphate accumulation and polyphosphate RT metabolism in Saccharomyces cerevisiae revealed by genomic expression RT analysis."; RL Mol. Biol. Cell 11:4309-4321(2000). RN [6] RP FUNCTION, IDENTIFICATION IN VTC COMPLEX, SUBUNIT, AND INTERACTION WITH NYV1 RP AND VPH1. RX PubMed=11823419; DOI=10.1093/emboj/21.3.259; RA Mueller O., Bayer M.J., Peters C., Andersen J.S., Mann M., Mayer A.; RT "The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans- RT complex formation."; RL EMBO J. 21:259-269(2002). RN [7] RP FUNCTION, TOPOLOGY, AND SUBCELLULAR LOCATION. RX PubMed=12584253; DOI=10.1242/jcs.00328; RA Mueller O., Neumann H., Bayer M.J., Mayer A.; RT "Role of the Vtc proteins in V-ATPase stability and membrane trafficking."; RL J. Cell Sci. 116:1107-1115(2003). RN [8] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17079729; DOI=10.1091/mbc.e06-08-0664; RA Uttenweiler A., Schwarz H., Neumann H., Mayer A.; RT "The vacuolar transporter chaperone (VTC) complex is required for RT microautophagy."; RL Mol. Biol. Cell 18:166-175(2007). RN [10] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=19390046; DOI=10.1126/science.1168120; RA Hothorn M., Neumann H., Lenherr E.D., Wehner M., Rybin V., Hassa P.O., RA Uttenweiler A., Reinhardt M., Schmidt A., Seiler J., Ladurner A.G., RA Herrmann C., Scheffzek K., Mayer A.; RT "Catalytic core of a membrane-associated eukaryotic polyphosphate RT polymerase."; RL Science 324:513-516(2009). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP FUNCTION. RX PubMed=25315834; DOI=10.1242/jcs.159772; RA Gerasimaite R., Sharma S., Desfougeres Y., Schmidt A., Mayer A.; RT "Coupled synthesis and translocation restrains polyphosphate to RT acidocalcisome-like vacuoles and prevents its toxicity."; RL J. Cell Sci. 127:5093-5104(2014). RN [13] RP INTERACTION WITH VTC5. RX PubMed=27587415; DOI=10.1074/jbc.m116.746784; RA Desfougeres Y., Gerasimaite R.U., Jessen H.J., Mayer A.; RT "Vtc5, a novel subunit of the vacuolar transporter chaperone complex, RT regulates polyphosphate synthesis and phosphate homeostasis in yeast."; RL J. Biol. Chem. 291:22262-22275(2016). CC -!- FUNCTION: Accessory subunit of the vacuolar transporter chaperone (VTC) CC complex. The VTC complex acts as a vacuolar polyphosphate polymerase CC that catalyzes the synthesis of inorganic polyphosphate (polyP) via CC transfer of phosphate from ATP to a growing polyP chain, releasing ADP. CC VTC exposes its catalytic domain VTC4 to the cytosol, where the growing CC polyP chain winds through a tunnel-shaped pocket, integrating CC cytoplasmic polymer synthesis with polyP membrane translocation CC (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane CC domains, which are likely to constitute the translocation channel into CC the organelle lumen (PubMed:25315834, PubMed:19390046). PolyP synthesis CC is tightly coupled to its transport into the vacuole lumen, in order to CC avoid otherwise toxic intermediates in the cytosol, and it depends on CC the proton gradient across the membrane, formed by V-ATPase CC (PubMed:25315834). VTC1 contributes only 3 transmembrane domains to the CC complex (Probable). The VTC complex also plays a role in vacuolar CC membrane fusion (PubMed:10480897, PubMed:11102525, PubMed:11823419, CC PubMed:12584253). Required for SEC18/NSF activity in SNARE priming, CC membrane binding of LMA1 and V(0) trans-complex formation CC (PubMed:11823419). {ECO:0000269|PubMed:10480897, CC ECO:0000269|PubMed:11102525, ECO:0000269|PubMed:11823419, CC ECO:0000269|PubMed:12584253, ECO:0000269|PubMed:19390046, CC ECO:0000269|PubMed:25315834, ECO:0000305|PubMed:19390046}. CC -!- SUBUNIT: The VTC core complex is an integral membrane heterooligomer CC composed of the catalytic subunit VTC4 and the accessory subunits VTC1, CC VTC2 and VTC3. The complex exists in 2 different sub-complexes: VTC1- CC VTC2-VCT4 and VCT1-VTC3-VTC4. The VCT1-VTC3-VTC4 subcomplex is mostly CC found on the vacuolar membrane. The VTC1-VTC2-VCT4 subcomplex is CC observed in the cell periphery, probably ER and nuclear envelope, but CC localizes to the vacuole under phosphate starvation. Each subunit CC contains 3 transmembrane helices. VTC1 is a small membrane protein CC without hydrophilic domain. VTC2, VTC3 and VTC4 are related and have 2 CC hydrophilic domains that face the cytosol, an N-terminal SPX domain and CC the central core domain. The central core in VTC4 is the catalytic CC domain, with the essential catalytic lysine replaced by isoleucine and CC leucine in VTC2 and VTC3, respectively (PubMed:19390046). The core CC complex associates with the accessory subunit VTC5 (PubMed:27587415). CC The complex interacts with the v-SNARE NYV1 and with the V(0) subunit CC of V-ATPase VPH1 (PubMed:11823419). {ECO:0000269|PubMed:11823419, CC ECO:0000269|PubMed:19390046, ECO:0000269|PubMed:27587415}. CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10480897, CC ECO:0000269|PubMed:12584253, ECO:0000269|PubMed:19390046}; Multi-pass CC membrane protein {ECO:0000269|PubMed:10480897}. Cytoplasm, cell cortex CC {ECO:0000269|PubMed:17079729, ECO:0000269|PubMed:19390046}. Endoplasmic CC reticulum membrane {ECO:0000269|PubMed:17079729}; Multi-pass membrane CC protein {ECO:0000269|PubMed:10480897}. Cytoplasmic vesicle, CC autophagosome membrane {ECO:0000269|PubMed:17079729}; Multi-pass CC membrane protein {ECO:0000269|PubMed:10480897}. CC -!- INDUCTION: By low phosphate. {ECO:0000269|PubMed:11102525}. CC -!- MISCELLANEOUS: Present with 12074 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the VTC1 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; U18813; AAB64608.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07731.1; -; Genomic_DNA. DR PIR; S50575; S50575. DR RefSeq; NP_010995.1; NM_001178963.1. DR PDB; 7YTJ; EM; 3.00 A; A/B/C=2-129. DR PDB; 8I6V; EM; 3.06 A; A/B/C=1-129. DR PDBsum; 7YTJ; -. DR PDBsum; 8I6V; -. DR AlphaFoldDB; P40046; -. DR EMDB; EMD-35208; -. DR SMR; P40046; -. DR BioGRID; 36815; 181. DR ComplexPortal; CPX-784; Vacuolar transporter chaperone complex. DR IntAct; P40046; 16. DR MINT; P40046; -. DR STRING; 4932.YER072W; -. DR TCDB; 9.B.51.1.6; the uncharacterized duf202/yidh (yidh) family. DR iPTMnet; P40046; -. DR MaxQB; P40046; -. DR PaxDb; 4932-YER072W; -. DR PeptideAtlas; P40046; -. DR TopDownProteomics; P40046; -. DR DNASU; 856803; -. DR EnsemblFungi; YER072W_mRNA; YER072W; YER072W. DR GeneID; 856803; -. DR KEGG; sce:YER072W; -. DR AGR; SGD:S000000874; -. DR SGD; S000000874; VTC1. DR VEuPathDB; FungiDB:YER072W; -. DR eggNOG; KOG4580; Eukaryota. DR GeneTree; ENSGT00940000176488; -. DR HOGENOM; CLU_141247_1_0_1; -. DR InParanoid; P40046; -. DR OMA; MAIMIYA; -. DR OrthoDB; 11387at2759; -. DR BioCyc; YEAST:G3O-30244-MONOMER; -. DR BioGRID-ORCS; 856803; 2 hits in 10 CRISPR screens. DR PRO; PR:P40046; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P40046; Protein. DR GO; GO:0000421; C:autophagosome membrane; NAS:ComplexPortal. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD. DR GO; GO:0016020; C:membrane; NAS:ComplexPortal. DR GO; GO:0031965; C:nuclear membrane; IDA:SGD. DR GO; GO:0005774; C:vacuolar membrane; IDA:SGD. DR GO; GO:0033254; C:vacuolar transporter chaperone complex; IPI:SGD. DR GO; GO:0003729; F:mRNA binding; IDA:SGD. DR GO; GO:0061736; P:engulfment of target by autophagosome; NAS:ComplexPortal. DR GO; GO:0016237; P:microautophagy; IDA:SGD. DR GO; GO:0006799; P:polyphosphate biosynthetic process; IMP:SGD. DR GO; GO:0006797; P:polyphosphate metabolic process; IMP:SGD. DR GO; GO:0007034; P:vacuolar transport; IDA:SGD. DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD. DR InterPro; IPR003807; DUF202. DR PANTHER; PTHR46140; VACUOLAR TRANSPORTER CHAPERONE 1-RELATED; 1. DR PANTHER; PTHR46140:SF1; VACUOLAR TRANSPORTER CHAPERONE 4; 1. DR Pfam; PF02656; DUF202; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chaperone; Cytoplasm; Cytoplasmic vesicle; KW Direct protein sequencing; Endoplasmic reticulum; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Vacuole. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378" FT CHAIN 2..129 FT /note="Vacuolar transporter chaperone complex subunit 1" FT /id="PRO_0000065934" FT TOPO_DOM 2..32 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:12584253" FT TRANSMEM 33..53 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 54..59 FT /note="Vacuolar" FT /evidence="ECO:0000305|PubMed:12584253" FT TRANSMEM 60..80 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 81..98 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:12584253" FT TRANSMEM 99..119 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 120..129 FT /note="Vacuolar" FT /evidence="ECO:0000269|PubMed:12584253" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:7YTJ" FT HELIX 23..53 FT /evidence="ECO:0007829|PDB:7YTJ" FT HELIX 56..89 FT /evidence="ECO:0007829|PDB:7YTJ" FT HELIX 99..121 FT /evidence="ECO:0007829|PDB:7YTJ" SQ SEQUENCE 129 AA; 14371 MW; 3D170007240E50B5 CRC64; MSSAPLLQRT PGKKIALPTR VEPKVFFANE RTFLSWLNFT VMLGGLGVGL LNFGDKIGRV SAGLFTFVAM GTMIYALVTY HWRAAAIRRR GSGPYDDRLG PTLLCFFLLV AVIINFILRL KYNDANTKL //