P15313 (VATB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ATP6V1B1
Synonyms:	ATP6B1, VATB, VPP3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subunit structure	V-ATPase is an 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.
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	Defects in ATP6V1B1 are the cause of distal renal tubular acidosis with deafness (dRTA-D) [MIM:267300]. Inheritance is autosomal recessive. Patients with recessive dRTA are severely affected, presenting with either acute illness or growth failure at a young age, and bilateral sensorineural deafness. Other features include low serum K+ due to renal potassium wasting, and elevated urinary calcium. If untreated, this acidosis may result in dissolution of bone, leading to osteomalacia and rickets. Renal deposition of calcium salts (nephrocalcinosis) and renal stone formation commonly occur.
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 process	Hydrogen ion transport Ion transport Transport
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Deafness Disease mutation
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro calcium ion homeostasis Inferred from mutant phenotype. Source: UniProtKB cellular iron ion homeostasis Traceable author statement. Source: Reactome excretion Inferred from mutant phenotype. Source: UniProtKB inner ear morphogenesis Inferred from mutant phenotype. Source: UniProtKB insulin receptor signaling pathway Traceable author statement. Source: Reactome ossification Inferred from mutant phenotype. Source: HGNC pH reduction Inferred from mutant phenotype. Source: UniProtKB sensory perception of sound Inferred from mutant phenotype. Source: UniProtKB transferrin transport Traceable author statement. Source: Reactome
Cellular component	apical plasma membrane Inferred from direct assay. Source: UniProtKB basolateral plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB cytosol Traceable author statement. Source: Reactome endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell lateral plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB microvillus Inferred from sequence or structural similarity. 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 function	ATP binding Inferred from electronic annotation. Source: InterPro hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 513	513	V-type proton ATPase subunit B, kidney isoform		PRO_0000144624
Regions
	Motif	510 – 513	4	PDZ-binding
Natural variations
	Natural variant	30	1	T → I. Ref.3 Ref.8 Corresponds to variant rs17720303 [ dbSNP | Ensembl ].		VAR_021011
	Natural variant	81	1	L → P in dRTA-D. Ref.7 Ref.8 Ref.9		VAR_007866
	Natural variant	123	1	G → V in dRTA-D. Ref.8		VAR_021012
	Natural variant	124	1	R → W in dRTA-D. Ref.7		VAR_007867
	Natural variant	157	1	R → C in dRTA-D. Ref.8		VAR_021013
	Natural variant	161	1	E → K. Ref.8		VAR_021014
	Natural variant	174	1	M → R in dRTA-D. Ref.7		VAR_007868
	Natural variant	275	1	T → P in dRTA-D. Ref.7 Ref.8		VAR_007869
	Natural variant	316	1	G → E in dRTA-D. Ref.7		VAR_007870
	Natural variant	346	1	P → R in dRTA-D. Ref.7 Ref.8 Ref.9		VAR_007871
	Natural variant	364	1	G → S in dRTA-D. Ref.7		VAR_007872
	Natural variant	465	1	R → H in dRTA-D. Ref.9		VAR_021015
Experimental info
	Mutagenesis	513	1	L → G: Loss of interactions with SLC9A3R1 and SCL4A7. Ref.6
	Sequence conflict	467	1	V → M in AAA36498. Ref.1
	Sequence conflict	474	1	G → S in AAA36498. Ref.1
	Sequence conflict	503	1	A → R in AAA36498. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P15313 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: 5399E2849F3B99AA	FASTA	513	56,833
	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

References

	« Hide 'large scale' referencesShow '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: 2527371] [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. , 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: 14702039] [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. , 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: 15489334] [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: 12444018] [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. , Skvorak A.B., Morton C.C., Cunningham M.J., Jha V., Lifton R.P. Nat. Genet. 21:84-90(1999) [PubMed: 9916796] [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. , 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: 12414817] [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: 12579397] [Abstract] Cited for: VARIANTS DRTA-D PRO-81; ARG-346 AND HIS-465.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.
IPI	IPI00304911.
PIR	A33281.
RefSeq	NP_001683.2. NM_001692.3.
UniGene	Hs.64173.
3D structure databases
ProteinModelPortal	P15313.
SMR	P15313. Positions 38-499.
ModBase	Search...
Protein-protein interaction databases
IntAct	P15313. 1 interaction.
STRING	P15313.
Protein family/group databases
TCDB	3.A.2.2.4. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.
PTM databases
PhosphoSite	P15313.
Polymorphism databases
DMDM	215274116.
Proteomic databases
PRIDE	P15313.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000234396; ENSP00000234396; ENSG00000116039.
GeneID	525.
KEGG	hsa:525.
Organism-specific databases
CTD	525.
GeneCards	GC02P071162.
H-InvDB	HIX0023969.
HGNC	HGNC:853. ATP6V1B1.
HPA	CAB009523.
MIM	192132. gene. 267300. phenotype.
neXtProt	NX_P15313.
Orphanet	18. Distal renal tubular acidosis.
PharmGKB	PA25154.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12784.
HOGENOM	HBG565875.
HOVERGEN	HBG002176.
InParanoid	P15313.
OMA	GWRERRY.
OrthoDB	EOG4HMJ93.
PhylomeDB	P15313.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	P15313.
Bgee	P15313.
CleanEx	HS_ATP6V1B1.
Genevestigator	P15313.
GermOnline	ENSG00000116039. Homo sapiens.
Family and domain databases
InterPro	IPR020003. ATPase_a/bsu_AS. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR005723. ATPase_V1-cplx_bsu. IPR022879. V-ATPase_su_B/beta. [Graphical view]
KO	K02147.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01040. V-ATPase_V1_B. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

VATB1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.