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Protein

V-type proton ATPase subunit H

Gene

VMA13

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Vacuolar ATPases regulate the organelle acidity. This subunit is essential for activity, but not assembly, of the enzyme complex.

GO - Molecular functioni

  • proton-transporting ATPase activity, rotational mechanism Source: SGD

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

Enzyme and pathway databases

BioCyciYEAST:G3O-34194-MONOMER.
ReactomeiR-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 H
Short name:
V-ATPase subunit H
Alternative name(s):
V-ATPase 54 kDa subunit
Vacuolar proton pump subunit H
Gene namesi
Name:VMA13
Synonyms:CLS11
Ordered Locus Names:YPR036W
ORF Names:YP3085.02
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR036W.
SGDiS000006240. VMA13.

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478V-type proton ATPase subunit HPRO_0000124202Add
BLAST

Proteomic databases

MaxQBiP41807.
PeptideAtlasiP41807.
PRIDEiP41807.

PTM databases

iPTMnetiP41807.

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 with YND1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
VMA7P391114EBI-20281,EBI-20272

Protein-protein interaction databases

BioGridi36214. 97 interactions.
DIPiDIP-6640N.
IntActiP41807. 20 interactions.
MINTiMINT-656652.

Structurei

Secondary structure

1
478
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2212Combined sources
Helixi27 – 326Combined sources
Helixi38 – 5215Combined sources
Helixi77 – 859Combined sources
Helixi90 – 10516Combined sources
Beta strandi107 – 1104Combined sources
Helixi111 – 1199Combined sources
Helixi123 – 1308Combined sources
Helixi136 – 15015Combined sources
Turni153 – 1553Combined sources
Helixi158 – 1669Combined sources
Helixi168 – 1758Combined sources
Helixi180 – 19415Combined sources
Helixi197 – 2048Combined sources
Helixi207 – 22216Combined sources
Helixi239 – 25315Combined sources
Helixi257 – 2648Combined sources
Helixi268 – 28013Combined sources
Helixi284 – 29613Combined sources
Beta strandi299 – 3024Combined sources
Helixi305 – 31612Combined sources
Helixi318 – 3269Combined sources
Helixi333 – 35119Combined sources
Helixi355 – 36511Combined sources
Helixi372 – 3754Combined sources
Helixi377 – 3837Combined sources
Helixi385 – 3873Combined sources
Helixi390 – 3923Combined sources
Helixi393 – 40715Combined sources
Helixi414 – 43320Combined sources
Helixi435 – 4373Combined sources
Helixi438 – 4447Combined sources
Helixi446 – 4538Combined sources
Helixi459 – 47517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HO8X-ray2.95A1-478[»]
3J9Telectron microscopy6.90P1-478[»]
3J9Uelectron microscopy7.60P1-478[»]
3J9Velectron microscopy8.30P1-478[»]
ProteinModelPortaliP41807.
SMRiP41807. Positions 1-478.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41807.

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase H subunit family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000003289.
HOGENOMiHOG000066030.
InParanoidiP41807.
KOiK02144.
OrthoDBiEOG74XSH8.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
1.25.40.150. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR004908. ATPase_V1-cplx_hsu.
IPR011987. ATPase_V1-cplx_hsu_C.
[Graphical view]
PANTHERiPTHR10698. PTHR10698. 1 hit.
PfamiPF11698. V-ATPase_H_C. 1 hit.
[Graphical view]
PIRSFiPIRSF032184. ATPase_V1_H. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

P41807-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGATKILMDS THFNEIRSII RSRSVAWDAL ARSEELSEID ASTAKALESI
60 70 80 90 100
LVKKNIGDGL SSSNNAHSGF KVNGKTLIPL IHLLSTSDNE DCKKSVQNLI
110 120 130 140 150
AELLSSDKYG DDTVKFFQED PKQLEQLFDV SLKGDFQTVL ISGFNVVSLL
160 170 180 190 200
VQNGLHNVKL VEKLLKNNNL INILQNIEQM DTCYVCIRLL QELAVIPEYR
210 220 230 240 250
DVIWLHEKKF MPTLFKILQR ATDSQLATRI VATNSNHLGI QLQYHSLLLI
260 270 280 290 300
WLLTFNPVFA NELVQKYLSD FLDLLKLVKI TIKEKVSRLC ISIILQCCST
310 320 330 340 350
RVKQHKKVIK QLLLLGNALP TVQSLSERKY SDEELRQDIS NLKEILENEY
360 370 380 390 400
QELTSFDEYV AELDSKLLCW SPPHVDNGFW SDNIDEFKKD NYKIFRQLIE
410 420 430 440 450
LLQAKVRNGD VNAKQEKIII QVALNDITHV VELLPESIDV LDKTGGKADI
460 470
MELLNHSDSR VKYEALKATQ AIIGYTFK
Length:478
Mass (Da):54,416
Last modified:November 1, 1995 - v1
Checksum:i54131FF9C2C87594
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13916 Genomic DNA. Translation: BAA03011.1.
Z68111 Genomic DNA. Translation: CAA92142.1.
Z71255 Genomic DNA. Translation: CAA94986.1.
BK006949 Genomic DNA. Translation: DAA11462.1.
PIRiA47429.
RefSeqiNP_015361.1. NM_001184133.1.

Genome annotation databases

EnsemblFungiiYPR036W; YPR036W; YPR036W.
GeneIDi856148.
KEGGisce:YPR036W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13916 Genomic DNA. Translation: BAA03011.1.
Z68111 Genomic DNA. Translation: CAA92142.1.
Z71255 Genomic DNA. Translation: CAA94986.1.
BK006949 Genomic DNA. Translation: DAA11462.1.
PIRiA47429.
RefSeqiNP_015361.1. NM_001184133.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HO8X-ray2.95A1-478[»]
3J9Telectron microscopy6.90P1-478[»]
3J9Uelectron microscopy7.60P1-478[»]
3J9Velectron microscopy8.30P1-478[»]
ProteinModelPortaliP41807.
SMRiP41807. Positions 1-478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36214. 97 interactions.
DIPiDIP-6640N.
IntActiP41807. 20 interactions.
MINTiMINT-656652.

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

iPTMnetiP41807.

Proteomic databases

MaxQBiP41807.
PeptideAtlasiP41807.
PRIDEiP41807.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR036W; YPR036W; YPR036W.
GeneIDi856148.
KEGGisce:YPR036W.

Organism-specific databases

EuPathDBiFungiDB:YPR036W.
SGDiS000006240. VMA13.

Phylogenomic databases

GeneTreeiENSGT00390000003289.
HOGENOMiHOG000066030.
InParanoidiP41807.
KOiK02144.
OrthoDBiEOG74XSH8.

Enzyme and pathway databases

BioCyciYEAST:G3O-34194-MONOMER.
ReactomeiR-SCE-77387. Insulin receptor recycling.
R-SCE-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

EvolutionaryTraceiP41807.
NextBioi981274.
PROiP41807.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
1.25.40.150. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR004908. ATPase_V1-cplx_hsu.
IPR011987. ATPase_V1-cplx_hsu_C.
[Graphical view]
PANTHERiPTHR10698. PTHR10698. 1 hit.
PfamiPF11698. V-ATPase_H_C. 1 hit.
[Graphical view]
PIRSFiPIRSF032184. ATPase_V1_H. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "VMA13 encodes a 54-kDa vacuolar H(+)-ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae."
    Ho M.N., Hirata R., Umemoto N., Ohya Y., Takatsuki A., Stevens T.H., Anraku Y.
    J. Biol. Chem. 268:18286-18292(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26786 / X2180-1A.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Regulation of yeast ectoapyrase ynd1p activity by activator subunit Vma13p of vacuolar H+-ATPase."
    Zhong X., Malhotra R., Guidotti G.
    J. Biol. Chem. 275:35592-35599(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YND1.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae."
    Sagermann M., Stevens T.H., Matthews B.W.
    Proc. Natl. Acad. Sci. U.S.A. 98:7134-7139(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS).

Entry informationi

Entry nameiVATH_YEAST
AccessioniPrimary (citable) accession number: P41807
Secondary accession number(s): D6W446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 157 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 22500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 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.