Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P15313 (VATB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ATP6V1B1
Synonyms:ATP6B1, VATB, VPP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00310

Subunit structure

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.

Subcellular location

Endomembrane system; Peripheral membrane protein. Note: Endomembrane. HAMAP-Rule MF_00310

Tissue specificity

Expressed in the cochlea and endolymphatic sac. Ref.7

Domain

The PDZ-binding motif mediates interactions with SLC9A3R1 and SCL4A7. Ref.6

Involvement in disease

Renal tubular acidosis, distal, with progressive nerve deafness (dRTA-D) [MIM:267300]: An autosomal recessive disease characterized by the association of renal distal tubular acidosis with sensorineural hearing loss. Distal renal tubular acidosis is characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. It is due to functional failure of alpha-intercalated cells of the cortical collecting duct of the distal nephron, where vectorial proton transport is required for urinary acidification.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Sequence caution

The sequence AAA36498.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHydrogen ion transport
Ion transport
Transport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDeafness
Disease mutation
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: InterPro

ATP metabolic process

Inferred from electronic annotation. Source: InterPro

calcium ion homeostasis

Inferred from mutant phenotype PubMed 19478356PubMed 20622307. Source: UniProtKB

cellular iron ion homeostasis

Traceable author statement. Source: Reactome

excretion

Inferred from mutant phenotype PubMed 19478356. Source: UniProtKB

inner ear morphogenesis

Inferred from mutant phenotype PubMed 19639346. Source: UniProtKB

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

interaction with host

Traceable author statement. Source: Reactome

ossification

Inferred from mutant phenotype PubMed 16433694. Source: HGNC

pH reduction

Inferred from mutant phenotype PubMed 19478356PubMed 20622307. Source: UniProtKB

phagosome maturation

Traceable author statement. Source: Reactome

proton transport

Inferred from mutant phenotype Ref.8. Source: HGNC

regulation of pH

Inferred from mutant phenotype Ref.8. Source: HGNC

sensory perception of sound

Inferred from mutant phenotype PubMed 19478356PubMed 20622307. Source: UniProtKB

transferrin transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 16928804. Source: UniProtKB

basolateral plasma membrane

Inferred from sequence or structural similarity PubMed 14585495. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity PubMed 14585495. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

lateral plasma membrane

Inferred from sequence or structural similarity PubMed 14585495. Source: UniProtKB

microvillus

Inferred from sequence or structural similarity PubMed 14585495. Source: UniProtKB

proton-transporting V-type ATPase, V1 domain

Inferred from electronic annotation. Source: InterPro

vacuolar proton-transporting V-type ATPase complex

Inferred from mutant phenotype Ref.8. Source: HGNC

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

hydrogen ion transmembrane transporter activity

Inferred from sequence or structural similarity PubMed 14585495. Source: UniProtKB

hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513V-type proton ATPase subunit B, kidney isoform HAMAP-Rule MF_00310
PRO_0000144624

Regions

Motif510 – 5134PDZ-binding HAMAP-Rule MF_00310

Natural variations

Natural variant301T → I. Ref.3 Ref.8
Corresponds to variant rs17720303 [ dbSNP | Ensembl ].
VAR_021011
Natural variant811L → P in dRTA-D. Ref.7 Ref.8 Ref.9
VAR_007866
Natural variant1231G → V in dRTA-D. Ref.8
VAR_021012
Natural variant1241R → W in dRTA-D. Ref.7
VAR_007867
Natural variant1571R → C in dRTA-D. Ref.8
VAR_021013
Natural variant1611E → K. Ref.8
Corresponds to variant rs114234874 [ dbSNP | Ensembl ].
VAR_021014
Natural variant1741M → R in dRTA-D. Ref.7
VAR_007868
Natural variant2751T → P in dRTA-D. Ref.7 Ref.8
VAR_007869
Natural variant3161G → E in dRTA-D. Ref.7
VAR_007870
Natural variant3461P → R in dRTA-D. Ref.7 Ref.8 Ref.9
VAR_007871
Natural variant3641G → S in dRTA-D. Ref.7
VAR_007872
Natural variant4651R → H in dRTA-D. Ref.9
Corresponds to variant rs142905621 [ dbSNP | Ensembl ].
VAR_021015

Experimental info

Mutagenesis5131L → G: Loss of interactions with SLC9A3R1 and SCL4A7. Ref.6
Sequence conflict4671V → M in AAA36498. Ref.1
Sequence conflict4741G → S in AAA36498. Ref.1
Sequence conflict5031A → R in AAA36498. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15313 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 5399E2849F3B99AA

FASTA51356,833
        10         20         30         40         50         60 
MAMEIDSRPG GLPGSSCNLG AAREHMQAVT RNYITHPRVT YRTVCSVNGP LVVLDRVKFA 

        70         80         90        100        110        120 
QYAEIVHFTL PDGTQRSGQV LEVAGTKAIV QVFEGTSGID ARKTTCEFTG DILRTPVSED 

       130        140        150        160        170        180 
MLGRVFNGSG KPIDKGPVVM AEDFLDINGQ PINPHSRIYP EEMIQTGISP IDVMNSIARG 

       190        200        210        220        230        240 
QKIPIFSAAG LPHNEIAAQI CRQAGLVKKS KAVLDYHDDN FAIVFAAMGV NMETARFFKS 

       250        260        270        280        290        300 
DFEQNGTMGN VCLFLNLAND PTIERIITPR LALTTAEFLA YQCEKHVLVI LTDMSSYAEA 

       310        320        330        340        350        360 
LREVSAAREE VPGRRGFPGY MYTDLATIYE RAGRVEGRGG SITQIPILTM PNDDITHPIP 

       370        380        390        400        410        420 
DLTGFITEGQ IYVDRQLHNR QIYPPINVLP SLSRLMKSAI GEGMTRKDHG DVSNQLYACY 

       430        440        450        460        470        480 
AIGKDVQAMK AVVGEEALTS EDLLYLEFLQ KFEKNFINQG PYENRSVFES LDLGWKLLRI 

       490        500        510 
FPKEMLKRIP QAVIDEFYSR EGALQDLAPD TAL 

« Hide

References

« Hide 'large scale' references
[1]"Human endomembrane H+ pump strongly resembles the ATP-synthetase of Archaebacteria."
Suedhof T.C., Fried V.A., Stone D.K., Johnston P.A., Xie X.-S.
Proc. Natl. Acad. Sci. U.S.A. 86:6067-6071(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-30.
Tissue: Kidney.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Lung.
[6]"The COOH termini of NBC3 and the 56-kDa H+-ATPase subunit are PDZ motifs involved in their interaction."
Pushkin A., Abuladze N., Newman D., Muronets V., Sassani P., Tatishchev S., Kurtz I.
Am. J. Physiol. 284:C667-C673(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC9A3R1 AND SLC4A7, DOMAIN, MUTAGENESIS OF LEU-513.
[7]"Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness."
Karet F.E., Finberg K.E., Nelson R.D., Nayir A., Mocan H., Sanjad S.A., Rodriguez-Soriano J., Santos F., Cremers C.W.R.J., Di Pietro A., Hoffbrand B.I., Winiarski J., Bakkaloglu A., Ozen S., Dusunsel R., Goodyer P., Hulton S.A., Wu D.K. expand/collapse author list , Skvorak A.B., Morton C.C., Cunningham M.J., Jha V., Lifton R.P.
Nat. Genet. 21:84-90(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DRTA-D PRO-81; TRP-124; ARG-174; PRO-275; GLU-316; ARG-346 AND SER-364, TISSUE SPECIFICITY.
[8]"Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss."
Stover E.H., Borthwick K.J., Bavalia C., Eady N., Fritz D.M., Rungroj N., Giersch A.B.S., Morton C.C., Axon P.R., Akil I., Al-Sabban E.A., Baguley D.M., Bianca S., Bakkaloglu A., Bircan Z., Chauveau D., Clermont M.-J., Guala A. expand/collapse author list , Hulton S.A., Kroes H., Li Volti G., Mir S., Mocan H., Nayir A., Ozen S., Rodriguez Soriano J., Sanjad S.A., Tasic V., Taylor C.M., Topaloglu R., Smith A.N., Karet F.E.
J. Med. Genet. 39:796-803(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DRTA-D PRO-81; VAL-123; CYS-157; PRO-275 AND ARG-346, VARIANTS ILE-30 AND LYS-161.
[9]"Confirmation of the ATP6B1 gene as responsible for distal renal tubular acidosis."
Ruf R., Rensing C., Topaloglu R., Guay-Woodford L., Klein C., Vollmer M., Otto E., Beekmann F., Haller M., Wiedensohler A., Leumann E., Antignac C., Rizzoni G., Filler G., Brandis M., Weber J.L., Hildebrandt F.
Pediatr. Nephrol. 18:105-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DRTA-D PRO-81; ARG-346 AND HIS-465.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25809 mRNA. Translation: AAA36498.1. Different initiation.
AK291121 mRNA. Translation: BAF83810.1.
AK313194 mRNA. Translation: BAG36011.1.
AK223151 mRNA. Translation: BAD96871.1.
CH471053 Genomic DNA. Translation: EAW99790.1.
BC063411 mRNA. Translation: AAH63411.1.
CCDSCCDS1912.1.
PIRA33281.
RefSeqNP_001683.2. NM_001692.3.
UniGeneHs.64173.

3D structure databases

ProteinModelPortalP15313.
SMRP15313. Positions 41-497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107008. 80 interactions.
IntActP15313. 3 interactions.
MINTMINT-8417607.
STRING9606.ENSP00000234396.

Chemistry

BindingDBP15313.
ChEMBLCHEMBL3217.

Protein family/group databases

TCDB3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteP15313.

Polymorphism databases

DMDM215274116.

Proteomic databases

MaxQBP15313.
PaxDbP15313.
PRIDEP15313.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234396; ENSP00000234396; ENSG00000116039.
ENST00000606226; ENSP00000475397; ENSG00000271809.
GeneID525.
KEGGhsa:525.
UCSCuc002shi.1. human.

Organism-specific databases

CTD525.
GeneCardsGC02P071162.
HGNCHGNC:853. ATP6V1B1.
HPACAB009523.
HPA031847.
MIM192132. gene.
267300. phenotype.
neXtProtNX_P15313.
Orphanet93611. Autosomal recessive distal renal tubular acidosis with deafness.
PharmGKBPA25154.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1156.
HOGENOMHOG000165320.
HOVERGENHBG002176.
InParanoidP15313.
KOK02147.
OMAGIDSQKT.
OrthoDBEOG7NW68Q.
PhylomeDBP15313.
TreeFamTF300313.

Enzyme and pathway databases

BioCycMetaCyc:HS03975-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP15313.
BgeeP15313.
CleanExHS_ATP6V1B1.
GenevestigatorP15313.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00310. ATP_synth_B_arch.
InterProIPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
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]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiATP6V1B1.
GenomeRNAi525.
NextBio2179.
PROP15313.
SOURCESearch...

Entry information

Entry nameVATB1_HUMAN
AccessionPrimary (citable) accession number: P15313
Secondary accession number(s): Q53FY0, Q6P4H6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM