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

V-type proton ATPase subunit H

Gene

VMA13

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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.

Miscellaneous

Present with 22500 molecules/cell in log phase SD medium.1 Publication

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

Keywordsi

Biological processHydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-34194-MONOMER
ReactomeiR-SCE-1222556 ROS, RNS production in phagocytes
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 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001242021 – 478V-type proton ATPase subunit HAdd BLAST478

Proteomic databases

MaxQBiP41807
PaxDbiP41807
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

Show more details

Protein-protein interaction databases

BioGridi36214, 422 interactors
DIPiDIP-6640N
IntActiP41807, 23 interactors
MINTiP41807
STRINGi4932.YPR036W

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 22Combined sources12
Helixi27 – 32Combined sources6
Helixi38 – 52Combined sources15
Helixi77 – 85Combined sources9
Helixi90 – 105Combined sources16
Beta strandi107 – 110Combined sources4
Helixi111 – 119Combined sources9
Helixi123 – 130Combined sources8
Helixi136 – 150Combined sources15
Turni153 – 155Combined sources3
Helixi158 – 166Combined sources9
Helixi168 – 175Combined sources8
Helixi180 – 194Combined sources15
Helixi197 – 204Combined sources8
Helixi207 – 222Combined sources16
Helixi239 – 253Combined sources15
Helixi257 – 264Combined sources8
Helixi268 – 280Combined sources13
Helixi284 – 296Combined sources13
Beta strandi299 – 302Combined sources4
Helixi305 – 316Combined sources12
Helixi318 – 326Combined sources9
Helixi333 – 351Combined sources19
Helixi355 – 365Combined sources11
Helixi372 – 375Combined sources4
Helixi377 – 383Combined sources7
Helixi385 – 387Combined sources3
Helixi390 – 392Combined sources3
Helixi393 – 407Combined sources15
Helixi414 – 433Combined sources20
Helixi435 – 437Combined sources3
Helixi438 – 444Combined sources7
Helixi446 – 453Combined sources8
Helixi459 – 475Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HO8X-ray2.95A1-478[»]
3J9Telectron microscopy6.90P1-478[»]
3J9Uelectron microscopy7.60P1-478[»]
3J9Velectron microscopy8.30P1-478[»]
5BW9X-ray7.00H/h1-478[»]
5D80X-ray6.20H/h1-478[»]
5VOXelectron microscopy6.80P1-478[»]
5VOYelectron microscopy7.90P1-478[»]
5VOZelectron microscopy7.60P1-478[»]
ProteinModelPortaliP41807
SMRiP41807
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41807

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase H subunit family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000003289
HOGENOMiHOG000066030
InParanoidiP41807
KOiK02144
OMAiDSKLLCW
OrthoDBiEOG092C3N1W

Family and domain databases

Gene3Di1.25.10.10, 1 hit
1.25.40.150, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR004908 ATPase_V1-cplx_hsu
IPR011987 ATPase_V1-cplx_hsu_C
IPR038497 ATPase_V1-cplx_hsu_C_sf
PANTHERiPTHR10698 PTHR10698, 1 hit
PfamiView protein in Pfam
PF11698 V-ATPase_H_C, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiVATH_YEAST
AccessioniPrimary (citable) accession number: P41807
Secondary accession number(s): D6W446
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 175 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health