VTC1_YEAST
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 03-AUG-2022, entry version 172.
DE RecName: Full=Vacuolar transporter chaperone 1;
DE AltName: Full=Negative regulator of CDC42 protein 1;
DE AltName: Full=Phosphate metabolism protein 4;
GN Name=VTC1; Synonyms=NRF1, PHM4; 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 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).
CC -!- FUNCTION: Component of the vacuolar transporter chaperone (VTC)
CC complex, which plays a role in vacuolar membrane fusion. Required for
CC SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0)
CC trans-complex formation. {ECO:0000269|PubMed:10480897,
CC ECO:0000269|PubMed:11823419, ECO:0000269|PubMed:12584253}.
CC -!- SUBUNIT: The VTC complex is an integral membrane heterooligomer
CC composed of VTC1, VTC2, VTC3 and VTC4. The complex interacts with the
CC v-SNARE NYV1 and with the V(0) subunit of V-ATPase VPH1.
CC {ECO:0000269|PubMed:11823419}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10480897,
CC ECO:0000269|PubMed:12584253}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10480897, ECO:0000269|PubMed:12584253}.
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}.
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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 AlphaFoldDB; P40046; -.
DR BioGRID; 36815; 150.
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; P40046; -.
DR PRIDE; P40046; -.
DR TopDownProteomics; P40046; -.
DR DNASU; 856803; -.
DR EnsemblFungi; YER072W_mRNA; YER072W; YER072W.
DR GeneID; 856803; -.
DR KEGG; sce:YER072W; -.
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; YALITYH; -.
DR BioCyc; YEAST:G3O-30244-MON; -.
DR PRO; PR:P40046; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40046; protein.
DR GO; GO:0000421; C:autophagosome membrane; IC:ComplexPortal.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031310; C:intrinsic component of vacuolar membrane; IDA:SGD.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0031965; C:nuclear 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; IC:ComplexPortal.
DR GO; GO:0016237; P:lysosomal 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 Pfam; PF02656; DUF202; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Direct protein sequencing; 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 1"
FT /id="PRO_0000065934"
FT TOPO_DOM 2..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:12584253"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..59
FT /note="Vacuolar"
FT /evidence="ECO:0000269|PubMed:12584253"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|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"
SQ SEQUENCE 129 AA; 14371 MW; 3D170007240E50B5 CRC64;
MSSAPLLQRT PGKKIALPTR VEPKVFFANE RTFLSWLNFT VMLGGLGVGL LNFGDKIGRV
SAGLFTFVAM GTMIYALVTY HWRAAAIRRR GSGPYDDRLG PTLLCFFLLV AVIINFILRL
KYNDANTKL
