Q91YH6 · VATB1_MOUSE
- ProteinV-type proton ATPase subunit B, kidney isoform
- GeneAtp6v1b1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids513 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Non-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:16174750, PubMed:23028982).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Essential for the proper assembly and activity of V-ATPase (By similarity).
In renal intercalated cells, mediates secretion of protons (H+) into the urine thereby ensuring correct urinary acidification (PubMed:16174750).
Required for optimal olfactory function by mediating the acidification of the nasal olfactory epithelium (PubMed:23028982).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Essential for the proper assembly and activity of V-ATPase (By similarity).
In renal intercalated cells, mediates secretion of protons (H+) into the urine thereby ensuring correct urinary acidification (PubMed:16174750).
Required for optimal olfactory function by mediating the acidification of the nasal olfactory epithelium (PubMed:23028982).
Features
Showing features for binding site.
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameV-type proton ATPase subunit B, kidney isoform
- Short namesV-ATPase subunit B 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ91YH6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice show a higher urinary pH and a more severe metabolic acidosis after oral acid challenge in comparison to wild-type littermates (PubMed:16174750).
Mice show diminished innate avoidance behavior (revealed as a decrease in freezing time and an increase in the number of sniffs in the presence of trimethyl-thiazoline) and diminished innate appetitive behavior (a decrease in time spent investigating the urine of the opposite sex) (PubMed:23028982).
Mice show diminished innate avoidance behavior (revealed as a decrease in freezing time and an increase in the number of sniffs in the presence of trimethyl-thiazoline) and diminished innate appetitive behavior (a decrease in time spent investigating the urine of the opposite sex) (PubMed:23028982).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000453034 | 1-513 | V-type proton ATPase subunit B, kidney isoform | |||
Sequence: MATTVDSRSSGFTGNSCDPGTAQEHVQAVTRNYITHPRVTYRTVCSVNGPLVVLDQVKFAQYAEIVNFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDSQKTTCEFTGDILRTPVSEDMLGRIFNGSGKPIDKGPAVMAEEFLDINGQPINPHDRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKAVLDYHEDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQVYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFITQGPYENRTVFESLDLGWKLLRIFPKEMLKRIPQSMTDEFYSRQGAQQDPASDTAL |
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in the kidney; found in early distal nephron, encompassing thick ascending limbs and distal convoluted tubules and in the alpha-intercalated cells of the cortical collecting ducts (at protein level) (PubMed:14585495, PubMed:29993276).
Expressed in the olfactory epithelium (at protein level) (PubMed:23028982).
Expressed at lower levels in the testis (PubMed:14585495).
Expressed in the olfactory epithelium (at protein level) (PubMed:23028982).
Expressed at lower levels in the testis (PubMed:14585495).
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).
Forms a complex with NHERF1 and SCL4A7 (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).
Forms a complex with NHERF1 and SCL4A7 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MATTVDSRSSGFTGNSCDPGT | ||||||
Motif | 510-513 | PDZ-binding | ||||
Sequence: DTAL |
Domain
The PDZ-binding motif mediates interactions with NHERF1 and SCL4A7.
Sequence similarities
Belongs to the ATPase alpha/beta chains family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length513
- Mass (Da)56,791
- Last updated2001-12-01 v1
- Checksum43EE1D236D4F6406
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RPW7 | A0A0U1RPW7_MOUSE | Atp6v1b1 | 68 | ||
A0A0U1RNU9 | A0A0U1RNU9_MOUSE | Atp6v1b1 | 215 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 7 | in Ref. 4; AAH62202 | ||||
Sequence: Missing | ||||||
Sequence conflict | 73 | in Ref. 2; BAC39470 | ||||
Sequence: G → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF435091 EMBL· GenBank· DDBJ | AAN45856.1 EMBL· GenBank· DDBJ | mRNA | ||
AK052604 EMBL· GenBank· DDBJ | BAC35059.1 EMBL· GenBank· DDBJ | mRNA | ||
AK052707 EMBL· GenBank· DDBJ | BAC35108.1 EMBL· GenBank· DDBJ | mRNA | ||
AK078810 EMBL· GenBank· DDBJ | BAC37404.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168980 EMBL· GenBank· DDBJ | BAE40781.1 EMBL· GenBank· DDBJ | mRNA | ||
AK085549 EMBL· GenBank· DDBJ | BAC39470.1 EMBL· GenBank· DDBJ | mRNA | ||
AC090647 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC017127 EMBL· GenBank· DDBJ | AAH17127.1 EMBL· GenBank· DDBJ | mRNA | ||
BC062202 EMBL· GenBank· DDBJ | AAH62202.1 EMBL· GenBank· DDBJ | mRNA |