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Protein

Vacuolar transporter chaperone 3

Gene

VTC3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the vacuolar transporter chaperone (VTC) complex, which plays a role in vacuolar membrane fusion. Required for LMA1 release prior to membrane fusion.1 Publication

GO - Biological processi

  • lysosomal microautophagy Source: SGD
  • polyphosphate metabolic process Source: SGD
  • vacuolar transport Source: SGD
  • vacuole fusion, non-autophagic Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:YPL019C-MONOMER.

Protein family/group databases

TCDBi4.E.1.1.2. the vacuolar (acidocalcisome) polyphosphate polymerase (v-ppp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar transporter chaperone 3
Alternative name(s):
Phosphate metabolism protein 2
Gene namesi
Name:VTC3
Synonyms:PHM2
Ordered Locus Names:YPL019C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL019C.
SGDiS000005940. VTC3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 709709CytoplasmicAdd
BLAST
Transmembranei710 – 72718HelicalSequence analysisAdd
BLAST
Topological domaini728 – 7358Vacuolar
Transmembranei736 – 75621HelicalSequence analysisAdd
BLAST
Topological domaini757 – 77822CytoplasmicAdd
BLAST
Transmembranei779 – 79921HelicalSequence analysisAdd
BLAST
Topological domaini800 – 83536VacuolarAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: SGD
  • fungal-type vacuole membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • vacuolar transporter chaperone complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 835835Vacuolar transporter chaperone 3PRO_0000065936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineCombined sources
Modified residuei45 – 451PhosphoserineCombined sources
Modified residuei50 – 501PhosphoserineCombined sources
Modified residuei183 – 1831PhosphothreonineCombined sources
Modified residuei195 – 1951PhosphoserineCombined sources
Modified residuei198 – 1981PhosphoserineCombined sources
Modified residuei270 – 2701PhosphoserineCombined sources
Modified residuei274 – 2741PhosphoserineCombined sources
Modified residuei589 – 5891PhosphoserineCombined sources
Modified residuei592 – 5921PhosphoserineCombined sources
Modified residuei621 – 6211PhosphoserineCombined sources
Modified residuei622 – 6221PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02725.
PeptideAtlasiQ02725.
PRIDEiQ02725.

PTM databases

iPTMnetiQ02725.

Expressioni

Inductioni

By low phosphate.1 Publication

Interactioni

Subunit structurei

The VTC complex is an integral membrane heterooligomer composed of VTC1, VTC2, VTC3 and VTC4. The complex interacts with the v-SNARE NYV1 and with the V0 subunit of V-ATPase VPH1.1 Publication

Protein-protein interaction databases

BioGridi36158. 27 interactions.
DIPiDIP-2000N.
IntActiQ02725. 6 interactions.
MINTiMINT-393829.

Structurei

3D structure databases

ProteinModelPortaliQ02725.
SMRiQ02725. Positions 206-559.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 145145SPXPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili385 – 41329Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the VTC2/3 family.Curated
Contains 1 SPX domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000014774.
HOGENOMiHOG000209413.
InParanoidiQ02725.
OMAiYNSAGER.
OrthoDBiEOG7W6WVG.

Family and domain databases

InterProiIPR003807. DUF202.
IPR004331. SPX_dom.
IPR018966. VTC_domain.
[Graphical view]
PfamiPF02656. DUF202. 1 hit.
PF09359. VTC. 1 hit.
[Graphical view]
PROSITEiPS51382. SPX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02725-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFGIKLAND VYPPWKDSYI DYERLKKLLK ESVIHDGRSS VDSWSERNES
60 70 80 90 100
DFVEALDKEL EKVYTFQISK YNAVLRKLDD LEENTKSAEK IQKINSEQFK
110 120 130 140 150
NTLEECLDEA QRLDNFDRLN FTGFIKIVKK HDKLHPNYPS VKSLLQVRLK
160 170 180 190 200
ELPFNNSEEY SPLLYRISYL YEFLRSNYDH PNTVSKSLAS TSKLSHFSNL
210 220 230 240 250
EDASFKSYKF WVHDDNIMEV KARILRHLPA LVYASVPNEN DDFVDNLESD
260 270 280 290 300
VRVQPEARLN IGSKSNSLSS DGNSNQDVEI GKSKSVIFPQ SYDPTITTLY
310 320 330 340 350
FDNDFFDLYN NRLLKISGAP TLRLRWIGKL LDKPDIFLEK RTFTENTETG
360 370 380 390 400
NSSFEEIRLQ MKAKFINNFI FKNDPSYKNY LINQLRERGT QKEELEKLSR
410 420 430 440 450
DFDNIQNFIV EEKLQPVLRA TYNRTAFQIP GDQSIRVTID SNIMYIREDS
460 470 480 490 500
LDKNRPIRNP ENWHRDDIDS NIPNPLRFLR AGEYSKFPYS VMEIKVINQD
510 520 530 540 550
NSQMPNYEWI KDLTNSHLVN EVPKFSLYLQ GVASLFGEDD KYVNILPFWL
560 570 580 590 600
PDLETDIRKN PQEAYEEEKK TLQKQKSIHD KLDNMRRLSK ISVPDGKTTE
610 620 630 640 650
RQGQKDQNTR HVIADLEDHE SSDEEGTALP KKSAVKKGKK FKTNAAFLKI
660 670 680 690 700
LAGKNISENG NDPYSDDTDS ASSFQLPPGV KKPVHLLKNA GPVKVEAKVW
710 720 730 740 750
LANERTFNRW LSVTTLLSVL TFSIYNSVQK AEFPQLADLL AYVYFFLTLF
760 770 780 790 800
CGVWAYRTYL KRLTLIKGRS GKHLDAPVGP ILVAVVLIVT LVVNFSVAFK
810 820 830
EAARRERGLV NVSSQPSLPR TLKPIQDFIF NLVGE
Length:835
Mass (Da):96,553
Last modified:November 1, 1996 - v1
Checksum:iF098B36A9D9B9C11
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36624 Genomic DNA. Translation: AAB68168.1.
BK006949 Genomic DNA. Translation: DAA11409.1.
PIRiS63463.
RefSeqiNP_015306.1. NM_001183833.1.

Genome annotation databases

EnsemblFungiiYPL019C; YPL019C; YPL019C.
GeneIDi856088.
KEGGisce:YPL019C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36624 Genomic DNA. Translation: AAB68168.1.
BK006949 Genomic DNA. Translation: DAA11409.1.
PIRiS63463.
RefSeqiNP_015306.1. NM_001183833.1.

3D structure databases

ProteinModelPortaliQ02725.
SMRiQ02725. Positions 206-559.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36158. 27 interactions.
DIPiDIP-2000N.
IntActiQ02725. 6 interactions.
MINTiMINT-393829.

Protein family/group databases

TCDBi4.E.1.1.2. the vacuolar (acidocalcisome) polyphosphate polymerase (v-ppp) family.

PTM databases

iPTMnetiQ02725.

Proteomic databases

MaxQBiQ02725.
PeptideAtlasiQ02725.
PRIDEiQ02725.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL019C; YPL019C; YPL019C.
GeneIDi856088.
KEGGisce:YPL019C.

Organism-specific databases

EuPathDBiFungiDB:YPL019C.
SGDiS000005940. VTC3.

Phylogenomic databases

GeneTreeiENSGT00390000014774.
HOGENOMiHOG000209413.
InParanoidiQ02725.
OMAiYNSAGER.
OrthoDBiEOG7W6WVG.

Enzyme and pathway databases

BioCyciYEAST:YPL019C-MONOMER.

Miscellaneous databases

NextBioi981110.
PROiQ02725.

Family and domain databases

InterProiIPR003807. DUF202.
IPR004331. SPX_dom.
IPR018966. VTC_domain.
[Graphical view]
PfamiPF02656. DUF202. 1 hit.
PF09359. VTC. 1 hit.
[Graphical view]
PROSITEiPS51382. SPX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 7-16; 28-62; 101-112; 149-175; 194-221; 227-252; 265-284; 330-340; 342-358; 363-386; 398-419; 425-447; 466-477; 481-495 AND 808-835, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "New components of a system for phosphate accumulation and polyphosphate metabolism in Saccharomyces cerevisiae revealed by genomic expression analysis."
    Ogawa N., DeRisi J.L., Brown P.O.
    Mol. Biol. Cell 11:4309-4321(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-complex formation."
    Mueller O., Bayer M.J., Peters C., Andersen J.S., Mann M., Mayer A.
    EMBO J. 21:259-269(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN VTC COMPLEX, SUBUNIT, INTERACTION WITH NYV1 AND VPH1.
  6. "Role of the Vtc proteins in V-ATPase stability and membrane trafficking."
    Mueller O., Neumann H., Bayer M.J., Mayer A.
    J. Cell Sci. 116:1107-1115(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY, SUBCELLULAR LOCATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-198; SER-270; SER-592; SER-621 AND SER-622, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183; SER-198; SER-274; SER-621 AND SER-622, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-45; SER-50; SER-195; SER-198; SER-270; SER-274; SER-621 AND SER-622, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVTC3_YEAST
AccessioniPrimary (citable) accession number: Q02725
Secondary accession number(s): D6W3Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2630 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.