Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Vacuolar transporter chaperone 2

Gene

VTC2

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.1 Publication

GO - Biological processi

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

Enzyme and pathway databases

BioCyciYEAST:YFL004W-MONOMER.

Protein family/group databases

TCDBi4.E.1.1.1. the vacuolar (acidocalcisome) polyphosphate polymerase (v-ppp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar transporter chaperone 2
Alternative name(s):
Phosphate metabolism protein 1
Gene namesi
Name:VTC2
Synonyms:PHM1
Ordered Locus Names:YFL004W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFL004W.
SGDiS000001890. VTC2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 693693CytoplasmicBy similarityAdd
BLAST
Transmembranei694 – 71623HelicalSequence analysisAdd
BLAST
Topological domaini717 – 72711VacuolarBy similarityAdd
BLAST
Transmembranei728 – 74821HelicalSequence analysisAdd
BLAST
Topological domaini749 – 76618CytoplasmicBy similarityAdd
BLAST
Transmembranei767 – 78721HelicalSequence analysisAdd
BLAST
Topological domaini788 – 82841VacuolarBy similarityAdd
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 – 828828Vacuolar transporter chaperone 2PRO_0000065935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei182 – 1821PhosphoserineCombined sources
Modified residuei187 – 1871PhosphoserineCombined sources
Modified residuei196 – 1961PhosphoserineCombined sources
Modified residuei264 – 2641PhosphoserineCombined sources
Modified residuei583 – 5831PhosphoserineCombined sources
Modified residuei615 – 6151PhosphoserineCombined sources
Modified residuei616 – 6161PhosphoserineCombined sources
Modified residuei620 – 6201PhosphothreonineCombined sources
Modified residuei626 – 6261PhosphoserineCombined sources
Modified residuei657 – 6571PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP43585.
PeptideAtlasiP43585.

PTM databases

iPTMnetiP43585.

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

BioGridi31142. 22 interactions.
DIPiDIP-7596N.
IntActiP43585. 5 interactions.
MINTiMINT-1365292.

Structurei

Secondary structure

1
828
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi204 – 2107Combined sources
Helixi212 – 22312Combined sources
Beta strandi278 – 2847Combined sources
Helixi289 – 2968Combined sources
Beta strandi303 – 3108Combined sources
Helixi312 – 3143Combined sources
Beta strandi318 – 3258Combined sources
Beta strandi336 – 3438Combined sources
Helixi345 – 3473Combined sources
Helixi348 – 3536Combined sources
Helixi358 – 37013Combined sources
Helixi374 – 39320Combined sources
Beta strandi397 – 40913Combined sources
Beta strandi416 – 42914Combined sources
Beta strandi434 – 4374Combined sources
Beta strandi444 – 4463Combined sources
Beta strandi452 – 4554Combined sources
Turni457 – 4604Combined sources
Helixi463 – 4653Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi471 – 4788Combined sources
Helixi503 – 5097Combined sources
Helixi522 – 53110Combined sources
Helixi532 – 5343Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G3OX-ray2.10A183-553[»]
ProteinModelPortaliP43585.
SMRiP43585. Positions 202-553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43585.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 146146SPXPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000014774.
HOGENOMiHOG000209413.
InParanoidiP43585.
OMAiHKFWVHP.
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.

P43585-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFGVKLANE VYPPWKGSYI NYEGLKKFLK EDSVKDGSND KKARWDDSDE
60 70 80 90 100
SKFVEELDKE LEKVYGFQLK KYNNLMERLS HLEKQTDTEA AIKALDADAF
110 120 130 140 150
QRVLEELLSE STELDNFKRL NFTGFAKIVK KHDKLYPKYP SVKSLLEVRL
160 170 180 190 200
KELPSHSEEY SPLLYRISFL YNILRSNFNT ASEPLASASK FSSIVSNDID
210 220 230 240 250
MNFRSFKFWV HNDNLMEVKT RILRHLPVLV YANVPSENDD LVNRFESDIS
260 270 280 290 300
NNDEIVGSSS STSSVEHGLG ARSFDPLINT LYFDNEHFEL YNDKLLKLNS
310 320 330 340 350
APTLRLRWTG QLSDKPDIFL EKKTLIEDEA TGKSEFDLTK LQLKQKFING
360 370 380 390 400
FIFEGDKKFK EQTLKKLKES GTAGRDLERL EEDFSEIQNF IIKNELQPVF
410 420 430 440 450
RTVYTRTAFQ IPGDDKIRVT IDSNIVFIKE DSFDRERPIR DPNTWHRTDI
460 470 480 490 500
DANVANPLKF LRGGEYAKFP YSVMEIKVKS SLDSSMSASS MISNVKLPKK
510 520 530 540 550
HGQWLNDLTN SHLVKEIPKF SIFVQGVASL YGDDEKLDIL PFWLPDLETD
560 570 580 590 600
IRQDPKQAYE EEKKKLLKQK EIQKKIDGMR RLSNLKEPQH QAAVPVSQEE
610 620 630 640 650
NERITSQGDL EADGSSDEET EQEPHSKRSK KVRRRKPKAT FLRILAGRDP
660 670 680 690 700
KLMGVDSEEE EIELPPGVKK PLNLLKNAGP VNVEAKVWLA NERTFNRWLS
710 720 730 740 750
VTSLLSVLTF SIYNSVKKAE YPTLANYMAY VYFGLTIFCA LWSYSIYMKR
760 770 780 790 800
VDIIQQRSGQ HLDAPLGPVL VSIVLFVTLV VNFVMAFRNA AKSRQELQIQ
810 820
NLEVPERIPE VLRPLQNYLF KLMGPSSD
Length:828
Mass (Da):95,441
Last modified:November 1, 1995 - v1
Checksum:iBCEF34FDB2012ABD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50617 Genomic DNA. Translation: BAA09234.1.
BK006940 Genomic DNA. Translation: DAA12435.1.
PIRiS56250.
RefSeqiNP_116651.1. NM_001179962.1.

Genome annotation databases

EnsemblFungiiBAA09234; BAA09234; BAA09234.
YFL004W; YFL004W; YFL004W.
GeneIDi850544.
KEGGisce:YFL004W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50617 Genomic DNA. Translation: BAA09234.1.
BK006940 Genomic DNA. Translation: DAA12435.1.
PIRiS56250.
RefSeqiNP_116651.1. NM_001179962.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G3OX-ray2.10A183-553[»]
ProteinModelPortaliP43585.
SMRiP43585. Positions 202-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31142. 22 interactions.
DIPiDIP-7596N.
IntActiP43585. 5 interactions.
MINTiMINT-1365292.

Protein family/group databases

TCDBi4.E.1.1.1. the vacuolar (acidocalcisome) polyphosphate polymerase (v-ppp) family.

PTM databases

iPTMnetiP43585.

Proteomic databases

MaxQBiP43585.
PeptideAtlasiP43585.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09234; BAA09234; BAA09234.
YFL004W; YFL004W; YFL004W.
GeneIDi850544.
KEGGisce:YFL004W.

Organism-specific databases

EuPathDBiFungiDB:YFL004W.
SGDiS000001890. VTC2.

Phylogenomic databases

GeneTreeiENSGT00390000014774.
HOGENOMiHOG000209413.
InParanoidiP43585.
OMAiHKFWVHP.
OrthoDBiEOG7W6WVG.

Enzyme and pathway databases

BioCyciYEAST:YFL004W-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP43585.
NextBioi966310.
PROiP43585.

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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 7-27; 72-93; 103-127; 152-175; 208-219; 308-322; 324-340; 347-358; 448-477 AND 500-515, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "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.
  6. "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.
  7. "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.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  10. "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.
  11. "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-182; SER-196; SER-264; SER-583; SER-615; SER-616 AND SER-657, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  12. "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-583 AND SER-657, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 SER-182; SER-187; SER-615; SER-616 AND SER-657, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-182; SER-187; SER-196; SER-583; SER-615; SER-616; THR-620; SER-626 AND SER-657, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVTC2_YEAST
AccessioniPrimary (citable) accession number: P43585
Secondary accession number(s): D6VTM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 134 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 2915 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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