Q9R1Q9 · VAS1_MOUSE
- ProteinV-type proton ATPase subunit S1
- GeneAtp6ap1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids463 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles (PubMed:18713856).
Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity. Involved in membrane trafficking and Ca2+-dependent membrane fusion. May play a role in the assembly of the V-type ATPase complex. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe2+ prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity).
In islets of Langerhans cells, may regulate the acidification of dense-core secretory granules (PubMed:18713856).
Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity. Involved in membrane trafficking and Ca2+-dependent membrane fusion. May play a role in the assembly of the V-type ATPase complex. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe2+ prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity).
In islets of Langerhans cells, may regulate the acidification of dense-core secretory granules (PubMed:18713856).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 225-226 | Cleavage; by furin | ||||
Sequence: RD |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | clathrin-coated vesicle membrane | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | endoplasmic reticulum-Golgi intermediate compartment membrane | |
Cellular Component | endosome membrane | |
Cellular Component | proton-transporting V-type ATPase complex | |
Cellular Component | synaptic vesicle membrane | |
Molecular Function | ATPase activator activity | |
Molecular Function | small GTPase binding | |
Molecular Function | transporter activator activity | |
Biological Process | cellular response to increased oxygen levels | |
Biological Process | endosome to plasma membrane protein transport | |
Biological Process | intracellular iron ion homeostasis | |
Biological Process | osteoclast development | |
Biological Process | regulation of cellular pH | |
Biological Process | synaptic vesicle lumen acidification |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameV-type proton ATPase subunit S1
- Short namesV-ATPase subunit S1
- 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 accessionQ9R1Q9
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass type I membrane protein
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Single-pass type I membrane protein
Cytoplasmic vesicle, clathrin-coated vesicle membrane ; Single-pass type I membrane protein
Note: Not detected in trans-Golgi network.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 33-412 | Lumenal | ||||
Sequence: VATEQQVPLVLWSSDRNLWAPVADTHEGHITSDMQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAISTLTTYLQEKLGASPLHVDLATLKELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLKSEDVPYTAALTAVRPSRVARDITMVAGGLGRQLLQTQVASPAIHPPVSYNDTAPRILFWAQNFSVAYKDEWKDLTSLTFGVENLNLTGSFWNDSFAMLSLTYEPLFGATVTFKFILASRFYPVSARYWFAMERLEIHSNGSVAHFNVSQVTGPSIYSFHCEYVSSVSKKGNLLVTNVPSVWQMTLHNFQIQAFNVTGEQFSYASDCA | ||||||
Transmembrane | 413-433 | Helical | ||||
Sequence: GFFSPGIWMGLLTTLFMLFIF | ||||||
Topological domain | 434-463 | Cytoplasmic | ||||
Sequence: TYGLHMILSLKTMDRFDDHKGPTITLTQIV |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 222-225 | Impairs propeptide cleavage. | ||||
Sequence: RVAR → AVAA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 58 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, propeptide, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-32 | |||||
Sequence: MMAATVVSRIRTGTGRAPVMWLSLSLVAVAAA | ||||||
Propeptide | PRO_0000454042 | 33-225 | ||||
Sequence: VATEQQVPLVLWSSDRNLWAPVADTHEGHITSDMQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAISTLTTYLQEKLGASPLHVDLATLKELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLKSEDVPYTAALTAVRPSRVAR | ||||||
Chain | PRO_0000002544 | 33-463 | V-type proton ATPase subunit S1 | |||
Sequence: VATEQQVPLVLWSSDRNLWAPVADTHEGHITSDMQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAISTLTTYLQEKLGASPLHVDLATLKELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLKSEDVPYTAALTAVRPSRVARDITMVAGGLGRQLLQTQVASPAIHPPVSYNDTAPRILFWAQNFSVAYKDEWKDLTSLTFGVENLNLTGSFWNDSFAMLSLTYEPLFGATVTFKFILASRFYPVSARYWFAMERLEIHSNGSVAHFNVSQVTGPSIYSFHCEYVSSVSKKGNLLVTNVPSVWQMTLHNFQIQAFNVTGEQFSYASDCAGFFSPGIWMGLLTTLFMLFIFTYGLHMILSLKTMDRFDDHKGPTITLTQIV | ||||||
Glycosylation | 164 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 255 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 267 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 290 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 297 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 344 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 351 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 365↔411 | |||||
Sequence: CEYVSSVSKKGNLLVTNVPSVWQMTLHNFQIQAFNVTGEQFSYASDC | ||||||
Glycosylation | 399 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Accessory component of the multisubunit proton-transporting vacuolar (V)-ATPase protein pump. Interacts (via N-terminus) with ATP6AP2 (via N-terminus). Interacts with RNASEK (By similarity).
Interacts with TMEM106B (via C-terminus) (By similarity).
Interacts with TMEM106B (via C-terminus) (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length463
- Mass (Da)51,008
- Last updated2000-05-01 v1
- ChecksumAE28D99718BA0AC0
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB031290 EMBL· GenBank· DDBJ | BAA83498.1 EMBL· GenBank· DDBJ | mRNA | ||
BC048241 EMBL· GenBank· DDBJ | AAH48241.1 EMBL· GenBank· DDBJ | mRNA |