P17255 · VATA_YEAST
- ProteinV-type proton ATPase catalytic subunit A
- GeneVMA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1071 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:18055462, PubMed:2139027).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:18055462, PubMed:2139027).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:18055462, PubMed:2139027).
PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates 'homing', a genetic event that converts a VMA1 allele lacking VDE into one that contains it.
Miscellaneous
Present with 199895 molecules/cell in log phase SD medium.
Catalytic activity
- ATP + 4 H+(in) + H2O = ADP + 5 H+(out) + phosphate
CHEBI:30616 + 4 H+ (in)CHEBI:15378+ CHEBI:15377 = CHEBI:456216 + 5 H+ (out)CHEBI:15378+ CHEBI:43474
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fungal-type vacuole membrane | |
Cellular Component | Golgi membrane | |
Cellular Component | proton-transporting V-type ATPase complex | |
Cellular Component | vacuolar proton-transporting V-type ATPase complex | |
Cellular Component | vacuolar proton-transporting V-type ATPase, V1 domain | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | endonuclease activity | |
Molecular Function | mRNA binding | |
Molecular Function | proton-transporting ATP synthase activity, rotational mechanism | |
Molecular Function | proton-transporting ATPase activity, rotational mechanism | |
Biological Process | endosomal lumen acidification | |
Biological Process | Golgi lumen acidification | |
Biological Process | intein-mediated protein splicing | |
Biological Process | intron homing | |
Biological Process | proton transmembrane transport | |
Biological Process | vacuolar acidification |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameV-type proton ATPase catalytic subunit A
- EC number
- Short namesV-ATPase subunit A
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP17255
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endomembrane system ; Peripheral membrane protein
Vacuole membrane ; Peripheral membrane protein
Note: Membranes of various intracellular acidic compartments.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 284 | Reduces splicing reaction speed. Inhibits splicing; when associated with N-362; S-737 and S-738 in X10SSSVDE. | ||||
Sequence: C → S | ||||||
Mutagenesis | 362 | Inhibits splicing; when associated with S-284; S-737 and S-738 in X10SSSVDE. | ||||
Sequence: H → N | ||||||
Mutagenesis | 737 | Inhibits splicing; when associated with S-284; N-362 and S-738 in X10SSSVDE. | ||||
Sequence: N → S | ||||||
Mutagenesis | 738 | Reduces splicing reaction speed. Inhibits splicing; when associated with S-284; N-362 and S-737 in X10SSSVDE. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 24 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000002458 | 2-283 | V-type proton ATPase catalytic subunit A, 1st part | |||
Sequence: AGAIENARKEIKRISLEDHAESEYGAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMETIYDGIQRPLKAIKEESQSIYIPRGIDTPALDRTIKWQFTPGKFQVGDHISGGDIYGSVFENSLISSHKILLPPRSRGTITWIAPAGEYTLDEKILEVEFDGKKSDFTLYHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKTVISQSLSKYSNSDAIIYVG | ||||||
Modified residue | 131 | Phosphothreonine | ||||
Sequence: T | ||||||
Chain | PRO_0000002459 | 284-737 | Endonuclease PI-SceI | |||
Sequence: CFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSVVQKSQHRAHKSDSSREVPELLKFTCNATHELVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIVELVKEVSKSYPISEGPERANELVESYRKASNKAYFEWTIEARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIEGPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVVSVNAEPAKVDMNGTKHKISYAIYMSGGDVLLNVLSKCAGSKKFRPAPAAAFARECRGFYFELQELKEDDYYGITLSDDSDHQFLLANQVVVHN | ||||||
Chain | PRO_0000002460 | 738-1071 | V-type proton ATPase catalytic subunit A, 2nd part | |||
Sequence: CGERGNEMAEVLMEFPELYTEMSGTKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNYPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLDVATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADSTGDVKHAVSSSKFFEPSRGEKEVHGEFEKLLSTMQERFAESTD | ||||||
Modified residue | 858 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 928 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
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, e, f and VOA1) (PubMed:18055462, PubMed:25971514, PubMed:27295975).
Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase (PubMed:11283612).
Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase (PubMed:11283612).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P17255 | RAV1 P47104 | 3 | EBI-20245, EBI-25471 | |
BINARY | P17255 | VMA6 P32366 | 7 | EBI-20245, EBI-20201 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 494-642 | DOD-type homing endonuclease | ||||
Sequence: LLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGL |
Sequence similarities
Belongs to the ATPase alpha/beta chains family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,071
- Mass (Da)118,637
- Last updated2007-01-23 v3
- Checksum2A4C65D2F59426FD
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 875 | in Ref. 8; AAB63978 | ||||
Sequence: G → D |
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J05409 EMBL· GenBank· DDBJ | AAA34664.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X83276 EMBL· GenBank· DDBJ | CAA58261.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z74233 EMBL· GenBank· DDBJ | CAA98760.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z74233 EMBL· GenBank· DDBJ | CAA98761.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
Z74233 EMBL· GenBank· DDBJ | CAA98762.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X58857 EMBL· GenBank· DDBJ | CAA41657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21609 EMBL· GenBank· DDBJ | AAB63978.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006938 EMBL· GenBank· DDBJ | DAA11677.1 EMBL· GenBank· DDBJ | Genomic DNA |