P31408 · VATB2_BOVIN
- ProteinV-type proton ATPase subunit B, brain isoform
- GeneATP6V1B2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids511 (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:32764564).
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 (PubMed:32764564).
In renal intercalated cells, can partially compensate the lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine under base-line conditions but not in conditions of acid load (By similarity).
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 (PubMed:32764564).
In renal intercalated cells, can partially compensate the lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine under base-line conditions but not in conditions of acid load (By similarity).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | clathrin-coated vesicle membrane | |
Cellular Component | cytosol | |
Cellular Component | melanosome | |
Cellular Component | plasma membrane | |
Cellular Component | synaptic vesicle membrane | |
Cellular Component | vacuolar proton-transporting V-type ATPase, V1 domain | |
Molecular Function | ATP binding | |
Molecular Function | proton-transporting ATPase activity, rotational mechanism | |
Biological Process | ATP metabolic process | |
Biological Process | pH reduction | |
Biological Process | proton transmembrane transport | |
Biological Process | vacuolar acidification |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameV-type proton ATPase subunit B, brain isoform
- Short namesV-ATPase subunit B 2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP31408
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, clathrin-coated vesicle membrane ; Peripheral membrane protein
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Variants
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The viewer provides 35 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000144625 | 1-511 | V-type proton ATPase subunit B, brain isoform | |||
Sequence: MALRAMRGIVNGAAPELPVPTSGPLAGSREQALAVSRNYLSQPRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERNFIAQGPYENRTVYETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH |
Proteomic 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 (PubMed:32764564).
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 (PubMed:32764564).
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 (PubMed:32764564).
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 (PubMed:32764564).
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 (PubMed:32764564).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length511
- Mass (Da)56,577
- Last updated2007-06-26 v3
- ChecksumE8DC915692F25E99
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 24 | in Ref. 1; AAA30400 | ||||
Sequence: Missing | ||||||
Sequence conflict | 83 | in Ref. 2; AAA30391 | ||||
Sequence: S → T | ||||||
Sequence conflict | 161-162 | in Ref. 1; AAA30400 | ||||
Sequence: QC → HF | ||||||
Sequence conflict | 250 | in Ref. 3; CAA41275 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 460 | in Ref. 1; AAA30400 | ||||
Sequence: R → K | ||||||
Sequence conflict | 464 | in Ref. 1; AAA30400 | ||||
Sequence: A → T | ||||||
Sequence conflict | 510-511 | in Ref. 2; AAA30391 | ||||
Sequence: KH → NS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M88690 EMBL· GenBank· DDBJ | AAA30400.1 EMBL· GenBank· DDBJ | mRNA | ||
M83131 EMBL· GenBank· DDBJ | AAA30391.1 EMBL· GenBank· DDBJ | mRNA | ||
X58385 EMBL· GenBank· DDBJ | CAA41275.1 EMBL· GenBank· DDBJ | mRNA | ||
BC123404 EMBL· GenBank· DDBJ | AAI23405.1 EMBL· GenBank· DDBJ | mRNA |