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 22-FEB-2023, entry version 183. 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 NHERF1 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 NHERF1 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 iPTMnet; Q91YH6; -. DR PhosphoSitePlus; Q91YH6; -. DR jPOST; Q91YH6; -. DR MaxQB; Q91YH6; -. DR PaxDb; Q91YH6; -. DR ProteomicsDB; 331224; -. DR Antibodypedia; 4020; 379 antibodies from 30 providers. DR DNASU; 110935; -. DR Ensembl; ENSMUST00000006431.8; ENSMUSP00000006431.7; ENSMUSG00000006269.8. DR GeneID; 110935; -. DR KEGG; mmu:110935; -. DR UCSC; uc009coc.1; mouse. DR AGR; MGI:103285; -. 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; 5473721at2759; -. 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 78 CRISPR screens. DR ChiTaRS; Atp6v1b1; mouse. DR PRO; PR:Q91YH6; -. 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; ISO:MGI. 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:0008021; C:synaptic vesicle; ISO:MGI. 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; ISO:MGI. 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:0097401; P:synaptic vesicle lumen acidification; IDA:SynGO. 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 CDD; cd18112; ATP-synt_V_A-type_beta_C; 1. DR CDD; cd18118; ATP-synt_V_A-type_beta_N; 1. DR CDD; cd01135; V_A-ATPase_B; 1. DR Gene3D; 3.40.50.12240; -; 1. 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; V-TYPE PROTON ATPASE SUBUNIT B; 1. DR PANTHER; PTHR43389:SF1; V-TYPE PROTON ATPASE SUBUNIT B, KIDNEY ISOFORM; 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; P-loop containing nucleoside triphosphate hydrolases; 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 //