Q9Z1G4 · VPP1_MOUSE
- ProteinV-type proton ATPase 116 kDa subunit a 1
- GeneAtp6v0a1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids839 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Subunit of the V0 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 (By similarity).
V-ATPase is responsible for the acidification of various organelles, such as lysosomes, endosomes, the trans-Golgi network, and secretory granules, including synaptic vesicles. In certain cell types, can be exported to the plasma membrane, where it is involved in the acidification of the extracellular environment (By similarity).
Required for assembly and activity of the vacuolar ATPase (By similarity).
Through its action on compartment acidification, plays an essential role in neuronal development in terms of integrity and connectivity of neurons (PubMed:33833240).
V-ATPase is responsible for the acidification of various organelles, such as lysosomes, endosomes, the trans-Golgi network, and secretory granules, including synaptic vesicles. In certain cell types, can be exported to the plasma membrane, where it is involved in the acidification of the extracellular environment (By similarity).
Required for assembly and activity of the vacuolar ATPase (By similarity).
Through its action on compartment acidification, plays an essential role in neuronal development in terms of integrity and connectivity of neurons (PubMed:33833240).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | clathrin-coated vesicle membrane | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | intracellular organelle | |
Cellular Component | melanosome | |
Cellular Component | nuclear speck | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | synaptic vesicle | |
Cellular Component | synaptic vesicle membrane | |
Cellular Component | vacuolar proton-transporting V-type ATPase complex | |
Cellular Component | vacuolar proton-transporting V-type ATPase, V0 domain | |
Molecular Function | ATPase binding | |
Molecular Function | proton-transporting ATPase activity, rotational mechanism | |
Biological Process | regulation of macroautophagy | |
Biological Process | synaptic vesicle lumen acidification | |
Biological Process | vacuolar acidification |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameV-type proton ATPase 116 kDa subunit a 1
- Short namesV-ATPase 116 kDa subunit a 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9Z1G4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, clathrin-coated vesicle membrane ; Multi-pass membrane protein
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-395 | Cytoplasmic | ||||
Sequence: MGELFRSEEMTLAQLFLQSEAAYCCVSELGELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKFILRKTQQFFDEAELHHQQMADPDLLEESSSLLEPNEMGRGAPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTGDYVHKSVFIIFFQGDQLKNRVKKICEGFRASLYPCPETPQERKEMASGVNTRIDDLQMVLNQTEDHRQRVLQAAAKNIRVWFIKVRKMKAIYHTLNLCNIDVTQKCLIAEVWCPVTDLDSIQFALRRGTEHSGSTVPSILNRMQTNQTPPTYNKTNKFTHGFQNIVDAYGIGTYRE | ||||||
Transmembrane | 396-414 | Helical | ||||
Sequence: INPAPYTVITFPFLFAVMF | ||||||
Topological domain | 415-416 | Vacuolar | ||||
Sequence: GD | ||||||
Transmembrane | 417-433 | Helical | ||||
Sequence: FGHGILMTLFAVWMVLR | ||||||
Topological domain | 434-448 | Cytoplasmic | ||||
Sequence: ESRILSQKHENEMFS | ||||||
Transmembrane | 449-478 | Helical | ||||
Sequence: MVFSGRYIILLMGLFSIYTGLIYNDCFSKS | ||||||
Topological domain | 479-542 | Vacuolar | ||||
Sequence: LNIFGSSWSVRPMFTQGNWTEETLLGSSVLQLNPAIPGVFGGPYPFGIDPIWNIATNKLTFLNS | ||||||
Transmembrane | 543-562 | Helical | ||||
Sequence: FKMKMSVILGIIHMLFGVSL | ||||||
Topological domain | 563-580 | Cytoplasmic | ||||
Sequence: SLFNHIYFKKPLNIYFGF | ||||||
Transmembrane | 581-601 | Helical | ||||
Sequence: IPEIIFMSSLFGYLVILIFYK | ||||||
Topological domain | 602-646 | Vacuolar | ||||
Sequence: WTAYDAHSSRNAPSLLIHFINMFLFSYPESGNAMLYSGQKGIQCF | ||||||
Transmembrane | 647-666 | Helical | ||||
Sequence: LIVVAMLCVPWMLLFKPLIL | ||||||
Topological domain | 667-726 | Cytoplasmic | ||||
Sequence: RHQYLRKKHLGTLNFGGIRVGNGPTEEDAEIIQHDQLSTHSEDAEEFDFGDTMVHQAIHT | ||||||
Transmembrane | 727-751 | Helical | ||||
Sequence: IEYCLGCISNTASYLRLWALSLAHA | ||||||
Topological domain | 752-772 | Vacuolar | ||||
Sequence: QLSEVLWTMVIHIGLHVRSLA | ||||||
Transmembrane | 773-811 | Helical | ||||
Sequence: GGLGLFFIFAAFATLTVAILLIMEGLSAFLHALRLHWVE | ||||||
Topological domain | 812-839 | Cytoplasmic | ||||
Sequence: FQNKFYTGTGFKFLPFSFEHIREGKFDE |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Embryonic lethal. Knockout embryos die at 5 to 6 dpc, before gastrulation.
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 194 | |||||
Sequence: L → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 44 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000119212 | 1-839 | V-type proton ATPase 116 kDa subunit a 1 | |||
Sequence: MGELFRSEEMTLAQLFLQSEAAYCCVSELGELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKFILRKTQQFFDEAELHHQQMADPDLLEESSSLLEPNEMGRGAPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTGDYVHKSVFIIFFQGDQLKNRVKKICEGFRASLYPCPETPQERKEMASGVNTRIDDLQMVLNQTEDHRQRVLQAAAKNIRVWFIKVRKMKAIYHTLNLCNIDVTQKCLIAEVWCPVTDLDSIQFALRRGTEHSGSTVPSILNRMQTNQTPPTYNKTNKFTHGFQNIVDAYGIGTYREINPAPYTVITFPFLFAVMFGDFGHGILMTLFAVWMVLRESRILSQKHENEMFSMVFSGRYIILLMGLFSIYTGLIYNDCFSKSLNIFGSSWSVRPMFTQGNWTEETLLGSSVLQLNPAIPGVFGGPYPFGIDPIWNIATNKLTFLNSFKMKMSVILGIIHMLFGVSLSLFNHIYFKKPLNIYFGFIPEIIFMSSLFGYLVILIFYKWTAYDAHSSRNAPSLLIHFINMFLFSYPESGNAMLYSGQKGIQCFLIVVAMLCVPWMLLFKPLILRHQYLRKKHLGTLNFGGIRVGNGPTEEDAEIIQHDQLSTHSEDAEEFDFGDTMVHQAIHTIEYCLGCISNTASYLRLWALSLAHAQLSEVLWTMVIHIGLHVRSLAGGLGLFFIFAAFATLTVAILLIMEGLSAFLHALRLHWVEFQNKFYTGTGFKFLPFSFEHIREGKFDE | ||||||
Modified residue | 257 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 367 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 371 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Predominantly expressed in neurons in the cortex and in the dentate gyrus, CA1 and CA3 regions of the hippocampus (at protein level) (PubMed:33833240).
Expressed at lower levels in astrocytes, oligodendrocytes and microglia (at protein level) (PubMed:33833240).
In the cerebellum, present in Purkinje and granule cells (at protein level) (PubMed:33833240).
Expressed at lower levels in astrocytes, oligodendrocytes and microglia (at protein level) (PubMed:33833240).
In the cerebellum, present in Purkinje and granule cells (at protein level) (PubMed:33833240).
Gene expression databases
Interaction
Subunit
V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex (By similarity).
The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (By similarity).
The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By similarity).
Interacts with SPAAR (PubMed:28024296).
The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (By similarity).
The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By similarity).
Interacts with SPAAR (PubMed:28024296).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Z1G4 | Psen1 P49769 | 2 | EBI-771149, EBI-990067 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9Z1G4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameA1-II
- Length839
- Mass (Da)96,467
- Last updated2011-07-27 v3
- ChecksumE102667721450C06
Q9Z1G4-2
- NameA1-I
Q9Z1G4-3
- NameA1-III
- Differences from canonical
- 142-148: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A2A599 | A2A599_MOUSE | Atp6v0a1 | 79 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 36 | in Ref. 1; AAC83083 | ||||
Sequence: Q → N | ||||||
Sequence conflict | 88-92 | in Ref. 1; AAC83083 | ||||
Sequence: VPFPR → APLPW | ||||||
Sequence conflict | 112 | in Ref. 1; AAC83083 | ||||
Sequence: N → D | ||||||
Alternative sequence | VSP_000342 | 142-148 | in isoform A1-I and isoform A1-III | |||
Sequence: Missing | ||||||
Sequence conflict | 190 | in Ref. 1; AAC83083 | ||||
Sequence: F → S | ||||||
Sequence conflict | 262 | in Ref. 1; AAC83083 | ||||
Sequence: K → T | ||||||
Sequence conflict | 337 | in Ref. 1; AAC83083 | ||||
Sequence: L → P | ||||||
Sequence conflict | 357 | in Ref. 1; AAC83083 | ||||
Sequence: S → F | ||||||
Sequence conflict | 415 | in Ref. 1; AAC83083 | ||||
Sequence: G → R | ||||||
Sequence conflict | 518 | in Ref. 1; AAC83083 | ||||
Sequence: F → L | ||||||
Sequence conflict | 683 | in Ref. 1; AAC83083 | ||||
Sequence: G → W | ||||||
Alternative sequence | VSP_000343 | 712 | in isoform A1-I | |||
Sequence: E → EPTEDEV | ||||||
Sequence conflict | 803 | in Ref. 1; AAC83083 | ||||
Sequence: H → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U13836 EMBL· GenBank· DDBJ | AAC83083.1 EMBL· GenBank· DDBJ | mRNA | ||
AF218249 EMBL· GenBank· DDBJ | AAF59918.1 EMBL· GenBank· DDBJ | mRNA | ||
AF218250 EMBL· GenBank· DDBJ | AAF59919.1 EMBL· GenBank· DDBJ | mRNA | ||
AF218251 EMBL· GenBank· DDBJ | AAF59920.1 EMBL· GenBank· DDBJ | mRNA | ||
AB022321 EMBL· GenBank· DDBJ | BAA93005.1 EMBL· GenBank· DDBJ | mRNA | ||
AL591425 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466677 EMBL· GenBank· DDBJ | EDL03866.1 EMBL· GenBank· DDBJ | Genomic DNA |