P31408 · VATB2_BOVIN

  • Protein
    V-type proton ATPase subunit B, brain isoform
  • Gene
    ATP6V1B2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Features

Showing features for binding site.

151150100150200250300350400450500
TypeIDPosition(s)Description
Binding site400ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentapical plasma membrane
Cellular Componentclathrin-coated vesicle membrane
Cellular Componentcytosol
Cellular Componentmelanosome
Cellular Componentplasma membrane
Cellular Componentsynaptic vesicle membrane
Cellular Componentvacuolar proton-transporting V-type ATPase, V1 domain
Molecular FunctionATP binding
Molecular Functionproton-transporting ATPase activity, rotational mechanism
Biological ProcessATP metabolic process
Biological ProcesspH reduction
Biological Processproton transmembrane transport
Biological Processvacuolar acidification

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    V-type proton ATPase subunit B, brain isoform
  • Short names
    V-ATPase subunit B 2
  • Alternative names
    • Endomembrane proton pump 58 kDa subunit
    • Vacuolar proton pump subunit B 2

Gene names

    • Name
      ATP6V1B2
    • Synonyms
      ATP6B2

Organism names

  • Taxonomic identifier
  • Strain
    • Hereford
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P31408
  • Secondary accessions
    • A4FUX5
    • Q28058

Proteomes

Organism-specific databases

Phenotypes & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 35 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001446251-511V-type proton ATPase subunit B, brain isoform

Proteomic databases

Expression

Tissue specificity

Expressed in brain (at protein level) (PubMed:1371275, PubMed:32764564).
Expressed in all tissues tested, but highest in brain and in adrenal medulla (PubMed:1371275, PubMed:32764564).

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 (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

Family & Domains

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    511
  • Mass (Da)
    56,577
  • Last updated
    2007-06-26 v3
  • Checksum
    E8DC915692F25E99
MALRAMRGIVNGAAPELPVPTSGPLAGSREQALAVSRNYLSQPRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERNFIAQGPYENRTVYETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict24in Ref. 1; AAA30400
Sequence conflict83in Ref. 2; AAA30391
Sequence conflict161-162in Ref. 1; AAA30400
Sequence conflict250in Ref. 3; CAA41275
Sequence conflict460in Ref. 1; AAA30400
Sequence conflict464in Ref. 1; AAA30400
Sequence conflict510-511in Ref. 2; AAA30391

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp