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Protein

V-type proton ATPase subunit B, brain isoform

Gene

Atp6v1b2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • ATP metabolic process Source: InterPro
  • regulation of cellular pH Source: RGD
  • vacuolar acidification Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-77387. Insulin receptor recycling.
R-RNO-917977. Transferrin endocytosis and recycling.
R-RNO-983712. Ion channel transport.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit B, brain isoform
Short name:
V-ATPase subunit B 2
Alternative name(s):
Endomembrane proton pump 58 kDa subunit
Vacuolar proton pump subunit B 2
Gene namesi
Name:Atp6v1b2
Synonyms:Atp6b2, Vat2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi620284. Atp6v1b2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 511511V-type proton ATPase subunit B, brain isoformPRO_0000144629Add
BLAST

Proteomic databases

PaxDbiP62815.
PRIDEiP62815.

2D gel databases

World-2DPAGE0004:P62815.

PTM databases

iPTMnetiP62815.
PhosphoSiteiP62815.

Expressioni

Gene expression databases

GenevisibleiP62815. RN.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein).

Protein-protein interaction databases

BioGridi250775. 1 interaction.
IntActiP62815. 2 interactions.
STRINGi10116.ENSRNOP00000015931.

Structurei

3D structure databases

ProteinModelPortaliP62815.
SMRiP62815. Positions 49-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiKOG1351. Eukaryota.
COG1156. LUCA.
GeneTreeiENSGT00550000074724.
HOGENOMiHOG000165320.
HOVERGENiHBG002176.
InParanoidiP62815.
KOiK02147.
OMAiWRERRYL.
OrthoDBiEOG7NW68Q.
PhylomeDBiP62815.
TreeFamiTF300313.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR005723. ATPase_V1-cplx_bsu.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039114. V-ATPsynth_beta/V-ATPase_B. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62815-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRAMRGIV NGAAPELPVP TGGPMAGARE QALAVSRNYL SQPRLTYKTV
60 70 80 90 100
SGVNGPLVIL DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE
110 120 130 140 150
GTSGIDAKKT SCEFTGDILR TPVSEDMLGR VFNGSGKPID RGPVVLAEDF
160 170 180 190 200
LDIMGQPINP QCRIYPEEMI QTGISAIDGM NSIARGQKIP IFSAAGLPHN
210 220 230 240 250
EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET ARFFKSDFEE
260 270 280 290 300
NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM
310 320 330 340 350
SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ
360 370 380 390 400
IPILTMPNDD ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR
410 420 430 440 450
LMKSAIGEGM TRKDHADVSN QLYACYAIGK DVQAMKAVVG EEALTSDDLL
460 470 480 490 500
YLEFLQKFEK NFITQGPYEN RTVYETLDIG WQLLRIFPKE MLKRIPQSTL
510
SEFYPRDSAK H
Length:511
Mass (Da):56,551
Last modified:August 16, 2004 - v1
Checksum:iE116BF9A36EEF36B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12635 mRNA. Translation: CAA73183.1.
BC085714 mRNA. Translation: AAH85714.1.
RefSeqiNP_476561.1. NM_057213.2.
UniGeneiRn.8109.

Genome annotation databases

EnsembliENSRNOT00000015931; ENSRNOP00000015931; ENSRNOG00000011891.
GeneIDi117596.
KEGGirno:117596.
UCSCiRGD:620284. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12635 mRNA. Translation: CAA73183.1.
BC085714 mRNA. Translation: AAH85714.1.
RefSeqiNP_476561.1. NM_057213.2.
UniGeneiRn.8109.

3D structure databases

ProteinModelPortaliP62815.
SMRiP62815. Positions 49-504.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250775. 1 interaction.
IntActiP62815. 2 interactions.
STRINGi10116.ENSRNOP00000015931.

PTM databases

iPTMnetiP62815.
PhosphoSiteiP62815.

2D gel databases

World-2DPAGE0004:P62815.

Proteomic databases

PaxDbiP62815.
PRIDEiP62815.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015931; ENSRNOP00000015931; ENSRNOG00000011891.
GeneIDi117596.
KEGGirno:117596.
UCSCiRGD:620284. rat.

Organism-specific databases

CTDi526.
RGDi620284. Atp6v1b2.

Phylogenomic databases

eggNOGiKOG1351. Eukaryota.
COG1156. LUCA.
GeneTreeiENSGT00550000074724.
HOGENOMiHOG000165320.
HOVERGENiHBG002176.
InParanoidiP62815.
KOiK02147.
OMAiWRERRYL.
OrthoDBiEOG7NW68Q.
PhylomeDBiP62815.
TreeFamiTF300313.

Enzyme and pathway databases

ReactomeiR-RNO-77387. Insulin receptor recycling.
R-RNO-917977. Transferrin endocytosis and recycling.
R-RNO-983712. Ion channel transport.

Miscellaneous databases

NextBioi620435.
PROiP62815.

Gene expression databases

GenevisibleiP62815. RN.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR005723. ATPase_V1-cplx_bsu.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039114. V-ATPsynth_beta/V-ATPase_B. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Antisense technology and bone resorption."
    Westberg M.S., Lundberg L.G.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 189-208; 387-400 AND 461-471, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.

Entry informationi

Entry nameiVATB2_RAT
AccessioniPrimary (citable) accession number: P62815
Secondary accession number(s): O09045, P50517
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: May 11, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.