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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: 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

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • 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.
ReactomeiR-SCE-1222556. ROS, RNS production in response to bacteria.
R-SCE-77387. Insulin receptor recycling.
R-SCE-917977. Transferrin endocytosis and 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
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL080W.
SGDiS000001563. VMA5.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi255F → A: Is rapidly degraded and disrupts stable ATPase assembly. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002093582 – 392V-type proton ATPase subunit CAdd BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP31412.
PRIDEiP31412.

PTM databases

iPTMnetiP31412.

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. 79 interactors.
DIPiDIP-4701N.
IntActiP31412. 16 interactors.
MINTiMINT-496270.

Structurei

Secondary structure

1392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 17Combined sources9
Helixi30 – 36Combined sources7
Helixi38 – 41Combined sources4
Beta strandi43 – 47Combined sources5
Helixi58 – 60Combined sources3
Helixi61 – 88Combined sources28
Beta strandi94 – 96Combined sources3
Helixi107 – 112Combined sources6
Turni118 – 120Combined sources3
Helixi127 – 165Combined sources39
Turni170 – 172Combined sources3
Turni176 – 178Combined sources3
Helixi181 – 183Combined sources3
Beta strandi189 – 199Combined sources11
Helixi200 – 202Combined sources3
Helixi203 – 209Combined sources7
Helixi210 – 212Combined sources3
Beta strandi213 – 217Combined sources5
Beta strandi223 – 227Combined sources5
Beta strandi229 – 239Combined sources11
Helixi240 – 242Combined sources3
Helixi243 – 252Combined sources10
Beta strandi256 – 258Combined sources3
Helixi264 – 319Combined sources56
Beta strandi325 – 332Combined sources8
Helixi337 – 348Combined sources12
Helixi349 – 352Combined sources4
Beta strandi384 – 392Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U7LX-ray1.75A1-392[»]
3J9Telectron microscopy6.90O1-392[»]
3J9Uelectron microscopy7.60O1-392[»]
3J9Velectron microscopy8.30O1-392[»]
4DL0X-ray2.90C/I158-277[»]
4EFAX-ray2.82C158-277[»]
ProteinModelPortaliP31412.
SMRiP31412.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31412.

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase C subunit family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000004263.
HOGENOMiHOG000207528.
InParanoidiP31412.
KOiK02148.
OMAiTARENKF.
OrthoDBiEOG092C36IX.

Family and domain databases

CDDicd14785. V-ATPase_C. 1 hit.
InterProiIPR004907. ATPase_V1-cplx_csu.
[Graphical view]
PANTHERiPTHR10137. PTHR10137. 1 hit.
PfamiPF03223. V-ATPase_C. 1 hit.
[Graphical view]
SUPFAMiSSF118203. SSF118203. 1 hit.

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 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.
PIRiS37905.
RefSeqiNP_012843.1. NM_001179646.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U7LX-ray1.75A1-392[»]
3J9Telectron microscopy6.90O1-392[»]
3J9Uelectron microscopy7.60O1-392[»]
3J9Velectron microscopy8.30O1-392[»]
4DL0X-ray2.90C/I158-277[»]
4EFAX-ray2.82C158-277[»]
ProteinModelPortaliP31412.
SMRiP31412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34052. 79 interactors.
DIPiDIP-4701N.
IntActiP31412. 16 interactors.
MINTiMINT-496270.

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.

PTM databases

iPTMnetiP31412.

Proteomic databases

MaxQBiP31412.
PRIDEiP31412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YKL080W.
SGDiS000001563. VMA5.

Phylogenomic databases

GeneTreeiENSGT00390000004263.
HOGENOMiHOG000207528.
InParanoidiP31412.
KOiK02148.
OMAiTARENKF.
OrthoDBiEOG092C36IX.

Enzyme and pathway databases

BioCyciYEAST:G3O-31875-MONOMER.
ReactomeiR-SCE-1222556. ROS, RNS production in response to bacteria.
R-SCE-77387. Insulin receptor recycling.
R-SCE-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

EvolutionaryTraceiP31412.
PROiP31412.

Family and domain databases

CDDicd14785. V-ATPase_C. 1 hit.
InterProiIPR004907. ATPase_V1-cplx_csu.
[Graphical view]
PANTHERiPTHR10137. PTHR10137. 1 hit.
PfamiPF03223. V-ATPase_C. 1 hit.
[Graphical view]
SUPFAMiSSF118203. SSF118203. 1 hit.
ProtoNetiSearch...

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 30, 2016
This is version 150 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

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.