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Protein

V-type proton ATPase subunit B, kidney isoform

Gene

ATP6V1B1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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
  • calcium ion homeostasis Source: UniProtKB
  • excretion Source: UniProtKB
  • inner ear morphogenesis Source: UniProtKB
  • ossification Source: UniProtKB
  • pH reduction Source: UniProtKB
  • proton transport Source: UniProtKB
  • regulation of pH Source: UniProtKB
  • sensory perception of sound Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit B, kidney isoform
Short name:
V-ATPase subunit B 1
Alternative name(s):
Endomembrane proton pump 58 kDa subunit
Vacuolar proton pump subunit B 1
Gene namesi
Name:ATP6V1B1
Synonyms:ATP6B1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cell membrane

  • Note: Plasma membrane of the renal intercalated cells.

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • lateral plasma membrane Source: UniProtKB
  • microvillus Source: UniProtKB
  • proton-transporting V-type ATPase, V1 domain Source: InterPro
  • vacuolar proton-transporting V-type ATPase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001446231 – 513V-type proton ATPase subunit B, kidney isoformAdd BLAST513

Proteomic databases

PaxDbiP31407.
PeptideAtlasiP31407.
PRIDEiP31407.

Expressioni

Tissue specificityi

Kidney cortex and medulla.

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). Forms a complex with SLC9A3R1 and SCL4A7 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014039.

Structurei

3D structure databases

ProteinModelPortaliP31407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi510 – 513PDZ-bindingBy similarity4

Domaini

The PDZ-binding motif mediates interactions with SLC9A3R1 and SCL4A7.By similarity

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiKOG1351. Eukaryota.
COG1156. LUCA.
HOGENOMiHOG000165320.
HOVERGENiHBG002176.
InParanoidiP31407.
KOiK02147.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch. 1 hit.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
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.

P31407-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAEVDSRPR GLPGGGASLG AAREHVQAVT RNYITHPRIT YRTVCSVNGP
60 70 80 90 100
LVVLDQVKFA QYAEIVNFTL PNGTQRSGQV LEVSGTKAIV QVFEGTSGID
110 120 130 140 150
AQKTTCEFTG DILRTPVSED MLGRVFNGSG KPIDKGPVVM AEDFLDINGQ
160 170 180 190 200
PINPHDRIYP EEMIETGISP IDVMNSIARG QKIPIFSAAG LPHNEIAAQI
210 220 230 240 250
CRQAGLVKKS KAVLDYHDDN FAIVFAAMGV NMETARFFKS DFEQNGTMGN
260 270 280 290 300
VCLFLNLAND PTIERIITPR LALTTAEFLA YQCEKHVLVI LTDMSSYAEA
310 320 330 340 350
LREVSAAREE VPGRRGFPGY MYTDLATIYE RAGRVEGRGG SITQIPILTM
360 370 380 390 400
PNDDITHPIP DLTGFITEGQ IYVDRQLHNR QIYPPINVLP SLSRLMKSAI
410 420 430 440 450
GEGMTRKDHG DVSNQLYACY AIGKDVQAMK AVVGEEALTS EDLLYLEFLQ
460 470 480 490 500
KFEKKFINQG PYEKRSVFES LDLGWKLLRT FPKEMLKRIP QNIIDEFFSR
510
EGAPQDTEAD TAL
Length:513
Mass (Da):56,747
Last modified:July 1, 1993 - v1
Checksum:i4C6DBE4E12570A25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88691 mRNA. Translation: AAA30394.1.
PIRiC44138.
RefSeqiNP_788827.1. NM_176654.2.
UniGeneiBt.4211.

Genome annotation databases

GeneIDi338059.
KEGGibta:338059.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88691 mRNA. Translation: AAA30394.1.
PIRiC44138.
RefSeqiNP_788827.1. NM_176654.2.
UniGeneiBt.4211.

3D structure databases

ProteinModelPortaliP31407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014039.

Proteomic databases

PaxDbiP31407.
PeptideAtlasiP31407.
PRIDEiP31407.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi338059.
KEGGibta:338059.

Organism-specific databases

CTDi525.

Phylogenomic databases

eggNOGiKOG1351. Eukaryota.
COG1156. LUCA.
HOGENOMiHOG000165320.
HOVERGENiHBG002176.
InParanoidiP31407.
KOiK02147.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch. 1 hit.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
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...

Entry informationi

Entry nameiVATB1_BOVIN
AccessioniPrimary (citable) accession number: P31407
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 119 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.