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P31412

- VATC_YEAST

UniProt

P31412 - VATC_YEAST

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Protein

V-type proton ATPase subunit C

Gene

VMA5

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

Functioni

Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic activity of the catalytic sector. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. proton-transporting ATPase activity, rotational mechanism Source: SGD

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. vacuolar acidification Source: SGD
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31875-MONOMER.
ReactomeiREACT_189031. Phagosomal maturation (early endosomal stage).
REACT_189190. Transferrin endocytosis and recycling.
REACT_255567. Insulin receptor recycling.

Protein family/group databases

TCDBi3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit C
Short name:
V-ATPase subunit C
Alternative name(s):
V-ATPase 42 kDa subunit
Vacuolar proton pump subunit C
Gene namesi
Name:VMA5
Synonyms:VAT3, VATC
Ordered Locus Names:YKL080W
ORF Names:YKL410
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

SGDiS000001563. VMA5.

Subcellular locationi

Vacuole membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. fungal-type vacuole membrane Source: SGD
  2. vacuolar proton-transporting V-type ATPase, V1 domain Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi255 – 2551F → A: Is rapidly degraded and disrupts stable ATPase assembly. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 392391V-type proton ATPase subunit CPRO_0000209358Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP31412.
PaxDbiP31412.
PeptideAtlasiP31412.

Expressioni

Gene expression databases

GenevestigatoriP31412.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). Interacts directly with VMA4.2 Publications

Protein-protein interaction databases

BioGridi34052. 78 interactions.
DIPiDIP-4701N.
IntActiP31412. 16 interactions.
MINTiMINT-496270.
STRINGi4932.YKL080W.

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 179Combined sources
Helixi30 – 367Combined sources
Helixi38 – 414Combined sources
Beta strandi43 – 475Combined sources
Helixi58 – 603Combined sources
Helixi61 – 8828Combined sources
Beta strandi94 – 963Combined sources
Helixi107 – 1126Combined sources
Turni118 – 1203Combined sources
Helixi127 – 16539Combined sources
Turni170 – 1723Combined sources
Turni176 – 1783Combined sources
Helixi181 – 1833Combined sources
Beta strandi189 – 19911Combined sources
Helixi200 – 2023Combined sources
Helixi203 – 2097Combined sources
Helixi210 – 2123Combined sources
Beta strandi213 – 2175Combined sources
Beta strandi223 – 2275Combined sources
Beta strandi229 – 23911Combined sources
Helixi240 – 2423Combined sources
Helixi243 – 25210Combined sources
Beta strandi256 – 2583Combined sources
Helixi264 – 31956Combined sources
Beta strandi325 – 3328Combined sources
Helixi337 – 34812Combined sources
Helixi349 – 3524Combined sources
Beta strandi384 – 3929Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U7LX-ray1.75A1-392[»]
4DL0X-ray2.90C/I158-277[»]
4EFAX-ray2.82C158-277[»]
ProteinModelPortaliP31412.
SMRiP31412. Positions 5-392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31412.

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase C subunit family.Curated

Phylogenomic databases

eggNOGiCOG5127.
GeneTreeiENSGT00390000004263.
HOGENOMiHOG000207528.
InParanoidiP31412.
KOiK02148.
OMAiQRQYAPL.
OrthoDBiEOG7RRFJ7.

Family and domain databases

InterProiIPR004907. ATPase_V1-cplx_csu.
[Graphical view]
PANTHERiPTHR10137. PTHR10137. 1 hit.
PfamiPF03223. V-ATPase_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31412-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATALYTAND FILISLPQNA QPVTAPGSKT DSWFNETLIG GRAFVSDFKI
60 70 80 90 100
PEFKIGSLDT LIVESEELSK VDNQIGASIG KIIEILQGLN ETSTNAYRTL
110 120 130 140 150
PINNMPVPEY LENFQWQTRK FKLDKSIKDL ITLISNESSQ LDADVRATYA
160 170 180 190 200
NYNSAKTNLA AAERKKTGDL SVRSLHDIVK PEDFVLNSEH LTTVLVAVPK
210 220 230 240 250
SLKSDFEKSY ETLSKNVVPA SASVIAEDAE YVLFNVHLFK KNVQEFTTAA
260 270 280 290 300
REKKFIPREF NYSEELIDQL KKEHDSAASL EQSLRVQLVR LAKTAYVDVF
310 320 330 340 350
INWFHIKALR VYVESVLRYG LPPHFNIKII AVPPKNLSKC KSELIDAFGF
360 370 380 390
LGGNAFMKDK KGKINKQDTS LHQYASLVDT EYEPFVMYII NL
Length:392
Mass (Da):44,189
Last modified:January 23, 2007 - v4
Checksum:i0CD1B814046C377E
GO

Sequence cautioni

The sequence AAA34440.1 differs from that shown. Reason: Frameshift at position 25. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77143 Genomic DNA. Translation: AAA34440.1. Frameshift.
X75560 Genomic DNA. Translation: CAA53237.1.
Z28080 Genomic DNA. Translation: CAA81917.1.
BK006944 Genomic DNA. Translation: DAA09077.1.
PIRiS37905.
RefSeqiNP_012843.1. NM_001179646.1.

Genome annotation databases

EnsemblFungiiYKL080W; YKL080W; YKL080W.
GeneIDi853782.
KEGGisce:YKL080W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77143 Genomic DNA. Translation: AAA34440.1 . Frameshift.
X75560 Genomic DNA. Translation: CAA53237.1 .
Z28080 Genomic DNA. Translation: CAA81917.1 .
BK006944 Genomic DNA. Translation: DAA09077.1 .
PIRi S37905.
RefSeqi NP_012843.1. NM_001179646.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U7L X-ray 1.75 A 1-392 [» ]
4DL0 X-ray 2.90 C/I 158-277 [» ]
4EFA X-ray 2.82 C 158-277 [» ]
ProteinModelPortali P31412.
SMRi P31412. Positions 5-392.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34052. 78 interactions.
DIPi DIP-4701N.
IntActi P31412. 16 interactions.
MINTi MINT-496270.
STRINGi 4932.YKL080W.

Protein family/group databases

TCDBi 3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

MaxQBi P31412.
PaxDbi P31412.
PeptideAtlasi P31412.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL080W ; YKL080W ; YKL080W .
GeneIDi 853782.
KEGGi sce:YKL080W.

Organism-specific databases

SGDi S000001563. VMA5.

Phylogenomic databases

eggNOGi COG5127.
GeneTreei ENSGT00390000004263.
HOGENOMi HOG000207528.
InParanoidi P31412.
KOi K02148.
OMAi QRQYAPL.
OrthoDBi EOG7RRFJ7.

Enzyme and pathway databases

BioCyci YEAST:G3O-31875-MONOMER.
Reactomei REACT_189031. Phagosomal maturation (early endosomal stage).
REACT_189190. Transferrin endocytosis and recycling.
REACT_255567. Insulin receptor recycling.

Miscellaneous databases

EvolutionaryTracei P31412.
NextBioi 974900.

Gene expression databases

Genevestigatori P31412.

Family and domain databases

InterProi IPR004907. ATPase_V1-cplx_csu.
[Graphical view ]
PANTHERi PTHR10137. PTHR10137. 1 hit.
Pfami PF03223. V-ATPase_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and mutational analysis of the gene encoding subunit C of yeast vacuolar H(+)-ATPase."
    Beltran C., Kopecky J., Pan Y.-C.E., Nelson H., Nelson N.
    J. Biol. Chem. 267:774-779(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 99-117, SUBUNIT.
  2. "Isolation of vacuolar membrane H(+)-ATPase-deficient yeast mutants; the VMA5 and VMA4 genes are essential for assembly and activity of the vacuolar H(+)-ATPase."
    Ho M.N., Hill K.J., Lindorfer M.A., Stevens T.H.
    J. Biol. Chem. 268:221-227(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 99-111; 147-156; 242-251 AND 311-318.
  3. "Sequence analysis of a 10 kb fragment of yeast chromosome XI identifies the SMY1 locus and reveals sequences related to a pre-mRNA splicing factor and vacuolar ATPase subunit C plus a number of unidentified open reading frames."
    James C.M., Gent M.E., Indge K.J., Oliver S.G.
    Yeast 10:247-255(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-70; 82-98; 126-146; 157-164; 209-215; 242-251; 259-285; 319-328 AND 342-358, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding."
    Armbruester A., Hohn C., Hermesdorf A., Schumacher K., Boersch M., Grueber G.
    FEBS Lett. 579:1961-1967(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 106-115 AND 358-365, NUCLEOTIDE-BINDING.
  8. "The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes."
    Parra K.J., Keenan K.L., Kane P.M.
    J. Biol. Chem. 275:21761-21767(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Mutational analysis of the subunit C (Vma5p) of the yeast vacuolar H+-ATPase."
    Curtis K.K., Francis S.A., Oluwatosin Y., Kane P.M.
    J. Biol. Chem. 277:8979-8988(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PHE-255.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H(+)-ATPase."
    Jones R.P.O., Durose L.J., Findlay J.B.C., Harrison M.A.
    Biochemistry 44:3933-3941(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VMA4.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Crystal structure of yeast V-ATPase subunit C reveals its stator function."
    Drory O., Frolow F., Nelson N.
    EMBO Rep. 5:1148-1152(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

Entry informationi

Entry nameiVATC_YEAST
AccessioniPrimary (citable) accession number: P31412
Secondary accession number(s): D6VXK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 21114 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3