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 (PubMed:11823419). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules (PubMed:27080106). Inositol polyphosphate binding promotes vacuolar polyphosphate synthesis (PubMed:27080106).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei22Important for inositol polyphosphate binding1 Publication1
Sitei26Important for inositol polyphosphate binding1 Publication1

GO - Molecular functioni

  • inositol hexakisphosphate binding Source: UniProtKB

GO - Biological processi

  • inositol phosphate-mediated signaling Source: UniProtKB
  • lysosomal microautophagy Source: SGD
  • polyphosphate biosynthetic process Source: UniProtKB
  • 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)DescriptionActionsGraphical viewLength
Topological domaini1 – 693CytoplasmicBy similarityAdd BLAST693
Transmembranei694 – 716HelicalSequence analysisAdd BLAST23
Topological domaini717 – 727VacuolarBy similarityAdd BLAST11
Transmembranei728 – 748HelicalSequence analysisAdd BLAST21
Topological domaini749 – 766CytoplasmicBy similarityAdd BLAST18
Transmembranei767 – 787HelicalSequence analysisAdd BLAST21
Topological domaini788 – 828VacuolarBy similarityAdd BLAST41

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi22Y → F: Decreases affinity for inositol polyphosphate. Strongly decreases affinity for inositol polyphosphate; when associated with A-26 and A-131. 1 Publication1
Mutagenesisi26K → A: Decreases affinity for inositol polyphosphate. Strongly decreases affinity for inositol polyphosphate; when associated with F-22 and A-131. 1 Publication1
Mutagenesisi127K → A: Abolishes inositol polyphosphate binding; when associated with A-130 and A-134. 1 Publication1
Mutagenesisi130K → A: Abolishes inositol polyphosphate binding; when associated with A-127 and A-134. 1 Publication1
Mutagenesisi131K → A: Decreases affinity for inositol polyphosphate. Strongly decreases affinity for inositol polyphosphate; when associated with F-22 and A-26. 1 Publication1
Mutagenesisi134K → A: Abolishes inositol polyphosphate binding; when associated with A-127 and A-130. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000659351 – 828Vacuolar transporter chaperone 2Add BLAST828

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei182PhosphoserineCombined sources1
Modified residuei187PhosphoserineCombined sources1
Modified residuei196PhosphoserineCombined sources1
Modified residuei264PhosphoserineCombined sources1
Modified residuei583PhosphoserineCombined sources1
Modified residuei615PhosphoserineCombined sources1
Modified residuei616PhosphoserineCombined sources1
Modified residuei620PhosphothreonineCombined sources1
Modified residuei626PhosphoserineCombined sources1
Modified residuei657PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP43585.
PRIDEiP43585.

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 interactors.
DIPiDIP-7596N.
IntActiP43585. 5 interactors.
MINTiMINT-1365292.

Structurei

Secondary structure

1828
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi204 – 210Combined sources7
Helixi212 – 223Combined sources12
Beta strandi278 – 284Combined sources7
Helixi289 – 296Combined sources8
Beta strandi303 – 310Combined sources8
Helixi312 – 314Combined sources3
Beta strandi318 – 325Combined sources8
Beta strandi336 – 343Combined sources8
Helixi345 – 347Combined sources3
Helixi348 – 353Combined sources6
Helixi358 – 370Combined sources13
Helixi374 – 393Combined sources20
Beta strandi397 – 409Combined sources13
Beta strandi416 – 429Combined sources14
Beta strandi434 – 437Combined sources4
Beta strandi444 – 446Combined sources3
Beta strandi452 – 455Combined sources4
Turni457 – 460Combined sources4
Helixi463 – 465Combined sources3
Beta strandi466 – 468Combined sources3
Beta strandi471 – 478Combined sources8
Helixi503 – 509Combined sources7
Helixi522 – 531Combined sources10
Helixi532 – 534Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP43585.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 146SPXPROSITE-ProRule annotationAdd BLAST146

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni127 – 134Important for inositol polyphosphate binding1 Publication8

Domaini

The SPX domain has very high affinity for inositol polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol pentakisphosphate (5-InsP7), and moderate affinity for inorganic pyrophosphate. Its affinity for inorganic phosphate is tow to three orders of magnitude lower.1 Publication

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.
OrthoDBiEOG092C0LBP.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3G3OX-ray2.10A183-553[»]
ProteinModelPortaliP43585.
SMRiP43585.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31142. 22 interactors.
DIPiDIP-7596N.
IntActiP43585. 5 interactors.
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.
PRIDEiP43585.

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.
OrthoDBiEOG092C0LBP.

Enzyme and pathway databases

BioCyciYEAST:YFL004W-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP43585.
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...

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: November 2, 2016
This is version 139 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.