VATB1_MOUSE
ID VATB1_MOUSE Reviewed; 513 AA.
AC Q91YH6; Q6P6I3; Q8C3L6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=V-type proton ATPase subunit B, kidney isoform;
DE Short=V-ATPase subunit B 1;
DE AltName: Full=Endomembrane proton pump 58 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit B 1;
GN Name=Atp6v1b1; Synonyms=Atp6b1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=14585495; DOI=10.1016/s0378-1119(03)00790-x;
RA Finberg K.E., Wagner C.A., Stehberger P.A., Geibel J.P., Lifton R.P.;
RT "Molecular cloning and characterization of Atp6v1b1, the murine vacuolar H+
RT -ATPase B1-subunit.";
RL Gene 318:25-34(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16174750; DOI=10.1073/pnas.0506769102;
RA Finberg K.E., Wagner C.A., Bailey M.A., Paunescu T.G., Breton S., Brown D.,
RA Giebisch G., Geibel J.P., Lifton R.P.;
RT "The B1-subunit of the H(+) ATPase is required for maximal urinary
RT acidification.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13616-13621(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23028982; DOI=10.1371/journal.pone.0045395;
RA Paunescu T.G., Rodriguez S., Benz E., McKee M., Tyszkowski R., Albers M.W.,
RA Brown D.;
RT "Loss of the V-ATPase B1 subunit isoform expressed in non-neuronal cells of
RT the mouse olfactory epithelium impairs olfactory function.";
RL PLoS ONE 7:e45395-e45395(2012).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29993276; DOI=10.1152/ajprenal.00539.2017;
RA Frische S., Chambrey R., Trepiccione F., Zamani R., Marcussen N.,
RA Alexander R.T., Skjoedt K., Svenningsen P., Dimke H.;
RT "H+-ATPase B1 subunit localizes to thick ascending limb and distal
RT convoluted tubule of rodent and human kidney.";
RL Am. J. Physiol. 315:F429-F444(2018).
CC -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC that translocates protons (PubMed:16174750, PubMed:23028982). V-ATPase
CC is responsible for acidifying and maintaining the pH of intracellular
CC compartments and in some cell types, is targeted to the plasma
CC membrane, where it is responsible for acidifying the extracellular
CC environment (By similarity). Essential for the proper assembly and
CC activity of V-ATPase (By similarity). In renal intercalated cells,
CC mediates secretion of protons (H+) into the urine thereby ensuring
CC correct urinary acidification (PubMed:16174750). Required for optimal
CC olfactory function by mediating the acidification of the nasal
CC olfactory epithelium (PubMed:23028982). {ECO:0000250|UniProtKB:P15313,
CC ECO:0000269|PubMed:16174750, ECO:0000269|PubMed:23028982}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex (By similarity). The V1 complex consists of three catalytic
CC AB heterodimers that form a heterohexamer, three peripheral stalks each
CC consisting of EG heterodimers, one central rotor including subunits D
CC and F, and the regulatory subunits C and H (By similarity). The proton
CC translocation complex V0 consists of the proton transport subunit a, a
CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC similarity). Forms a complex with SLC9A3R1 and SCL4A7 (By similarity).
CC {ECO:0000250|UniProtKB:P15313, ECO:0000250|UniProtKB:P21281}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:23028982, ECO:0000269|PubMed:29993276}. Basolateral
CC cell membrane {ECO:0000269|PubMed:23028982}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the kidney; found in early
CC distal nephron, encompassing thick ascending limbs and distal
CC convoluted tubules and in the alpha-intercalated cells of the cortical
CC collecting ducts (at protein level) (PubMed:14585495, PubMed:29993276).
CC Expressed in the olfactory epithelium (at protein level)
CC (PubMed:23028982). Expressed at lower levels in the testis
CC (PubMed:14585495). {ECO:0000269|PubMed:14585495,
CC ECO:0000269|PubMed:23028982, ECO:0000269|PubMed:29993276}.
CC -!- DOMAIN: The PDZ-binding motif mediates interactions with SLC9A3R1 and
CC SCL4A7. {ECO:0000250|UniProtKB:P15313}.
CC -!- DISRUPTION PHENOTYPE: Mice show a higher urinary pH and a more severe
CC metabolic acidosis after oral acid challenge in comparison to wild-type
CC littermates (PubMed:16174750). Mice show diminished innate avoidance
CC behavior (revealed as a decrease in freezing time and an increase in
CC the number of sniffs in the presence of trimethyl-thiazoline) and
CC diminished innate appetitive behavior (a decrease in time spent
CC investigating the urine of the opposite sex) (PubMed:23028982).
CC {ECO:0000269|PubMed:16174750, ECO:0000269|PubMed:23028982}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AF435091; AAN45856.1; -; mRNA.
DR EMBL; AK052604; BAC35059.1; -; mRNA.
DR EMBL; AK052707; BAC35108.1; -; mRNA.
DR EMBL; AK078810; BAC37404.1; -; mRNA.
DR EMBL; AK168980; BAE40781.1; -; mRNA.
DR EMBL; AK085549; BAC39470.1; -; mRNA.
DR EMBL; AC090647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017127; AAH17127.1; -; mRNA.
DR EMBL; BC062202; AAH62202.1; -; mRNA.
DR CCDS; CCDS20283.1; -.
DR RefSeq; NP_598918.1; NM_134157.2.
DR AlphaFoldDB; Q91YH6; -.
DR SMR; Q91YH6; -.
DR IntAct; Q91YH6; 2.
DR MINT; Q91YH6; -.
DR STRING; 10090.ENSMUSP00000006431; -.
DR TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSitePlus; Q91YH6; -.
DR jPOST; Q91YH6; -.
DR MaxQB; Q91YH6; -.
DR PaxDb; Q91YH6; -.
DR PRIDE; Q91YH6; -.
DR ProteomicsDB; 331224; -.
DR Antibodypedia; 4020; 380 antibodies from 30 providers.
DR DNASU; 110935; -.
DR Ensembl; ENSMUST00000006431; ENSMUSP00000006431; ENSMUSG00000006269.
DR GeneID; 110935; -.
DR KEGG; mmu:110935; -.
DR UCSC; uc009coc.1; mouse.
DR CTD; 525; -.
DR MGI; MGI:103285; Atp6v1b1.
DR VEuPathDB; HostDB:ENSMUSG00000006269; -.
DR eggNOG; KOG1351; Eukaryota.
DR GeneTree; ENSGT00940000161413; -.
DR HOGENOM; CLU_022916_0_0_1; -.
DR InParanoid; Q91YH6; -.
DR OMA; AVLDYHE; -.
DR OrthoDB; 541116at2759; -.
DR PhylomeDB; Q91YH6; -.
DR TreeFam; TF300313; -.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-77387; Insulin receptor recycling.
DR Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR Reactome; R-MMU-983712; Ion channel transport.
DR BioGRID-ORCS; 110935; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Atp6v1b1; mouse.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91YH6; protein.
DR Bgee; ENSMUSG00000006269; Expressed in vibrissa unit and 128 other tissues.
DR ExpressionAtlas; Q91YH6; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; ISS:UniProtKB.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0046034; P:ATP metabolic process; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
DR GO; GO:0055064; P:chloride ion homeostasis; IMP:MGI.
DR GO; GO:0042048; P:olfactory behavior; IMP:MGI.
DR GO; GO:0001503; P:ossification; ISS:UniProtKB.
DR GO; GO:0045851; P:pH reduction; ISO:MGI.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:MGI.
DR GO; GO:0006693; P:prostaglandin metabolic process; IMP:MGI.
DR GO; GO:1902600; P:proton transmembrane transport; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006885; P:regulation of pH; IMP:UniProtKB.
DR GO; GO:0035812; P:renal sodium excretion; IMP:MGI.
DR GO; GO:0003096; P:renal sodium ion transport; IMP:MGI.
DR GO; GO:0097254; P:renal tubular secretion; ISO:MGI.
DR GO; GO:0003091; P:renal water homeostasis; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; ISS:UniProtKB.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR PANTHER; PTHR43389; PTHR43389; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Hydrogen ion transport; Ion transport;
KW Membrane; Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1..513
FT /note="V-type proton ATPase subunit B, kidney isoform"
FT /id="PRO_0000453034"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 510..513
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:P15313"
FT BINDING 394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P21281"
FT CONFLICT 7
FT /note="Missing (in Ref. 4; AAH62202)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="G -> V (in Ref. 2; BAC39470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 56791 MW; 43EE1D236D4F6406 CRC64;
MATTVDSRSS GFTGNSCDPG TAQEHVQAVT RNYITHPRVT YRTVCSVNGP LVVLDQVKFA
QYAEIVNFTL PDGTQRSGQV LEVAGTKAIV QVFEGTSGID SQKTTCEFTG DILRTPVSED
MLGRIFNGSG KPIDKGPAVM AEEFLDINGQ PINPHDRIYP EEMIQTGISP IDVMNSIARG
QKIPIFSAAG LPHNEIAAQI CRQAGLVKKS KAVLDYHEDN FAIVFAAMGV NMETARFFKS
DFEQNGTMGN VCLFLNLAND PTIERIITPR LALTTAEFLA YQCEKHVLVI LTDMSSYAEA
LREVSAAREE VPGRRGFPGY MYTDLATIYE RAGRVEGRGG SITQIPILTM PNDDITHPIP
DLTGFITEGQ IYVDRQLHNR QVYPPINVLP SLSRLMKSAI GEGMTRKDHG DVSNQLYACY
AIGKDVQAMK AVVGEEALTS EDLLYLEFLQ KFEKNFITQG PYENRTVFES LDLGWKLLRI
FPKEMLKRIP QSMTDEFYSR QGAQQDPASD TAL
