ID VATB1_BOVIN Reviewed; 513 AA.
AC P31407;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 27-NOV-2024, entry version 153.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 504-513, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=1373501; DOI=10.1073/pnas.89.8.3541;
RA Nelson R.D., Guo X.-L., Masood K., Brown D., Kalkbrenner M., Gluck S.;
RT "Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase
RT 56-kilodalton subunit in renal intercalated cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3541-3545(1992).
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 (By similarity). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments and in
CC some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment (By
CC similarity). Essential for the proper assembly and activity of V-ATPase
CC (By similarity). In renal intercalated cells, mediates secretion of
CC protons (H+) into the urine thereby ensuring correct urinary
CC acidification (By similarity). Required for optimal olfactory function
CC by mediating the acidification of the nasal olfactory epithelium (By
CC similarity). {ECO:0000250|UniProtKB:P15313,
CC ECO:0000250|UniProtKB:P31408, ECO:0000250|UniProtKB:Q91YH6}.
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:P31408}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P15313}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q91YH6}.
CC -!- TISSUE SPECIFICITY: Kidney cortex and medulla.
CC {ECO:0000269|PubMed:1373501}.
CC -!- DOMAIN: The PDZ-binding motif mediates interactions with NHERF1 and
CC SCL4A7. {ECO:0000250|UniProtKB:P15313}.
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; M88691; AAA30394.1; -; mRNA.
DR PIR; C44138; C44138.
DR RefSeq; NP_788827.1; NM_176654.2.
DR AlphaFoldDB; P31407; -.
DR SMR; P31407; -.
DR CORUM; P31407; -.
DR STRING; 9913.ENSBTAP00000014039; -.
DR PaxDb; 9913-ENSBTAP00000014039; -.
DR PeptideAtlas; P31407; -.
DR GeneID; 338059; -.
DR KEGG; bta:338059; -.
DR CTD; 525; -.
DR VEuPathDB; HostDB:ENSBTAG00000010620; -.
DR eggNOG; KOG1351; Eukaryota.
DR InParanoid; P31407; -.
DR OMA; ICELRTP; -.
DR OrthoDB; 5473721at2759; -.
DR Reactome; R-BTA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-BTA-77387; Insulin receptor recycling.
DR Reactome; R-BTA-917977; Transferrin endocytosis and recycling.
DR Reactome; R-BTA-9639288; Amino acids regulate mTORC1.
DR Reactome; R-BTA-983712; Ion channel transport.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000010620; Expressed in adult mammalian kidney and 63 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; ISS:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006885; P:regulation of pH; ISS:UniProtKB.
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 FunFam; 3.40.50.12240:FF:000001; V-type proton ATPase subunit B, brain; 1.
DR Gene3D; 3.40.50.12240; -; 1.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR055190; ATP-synt_VA_C.
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 NCBIfam; TIGR01040; V-ATPase_V1_B; 1.
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 Pfam; PF22919; ATP-synt_VA_C; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..513
FT /note="V-type proton ATPase subunit B, kidney isoform"
FT /id="PRO_0000144623"
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:P31408"
SQ SEQUENCE 513 AA; 56747 MW; 4C6DBE4E12570A25 CRC64;
MAAEVDSRPR GLPGGGASLG AAREHVQAVT RNYITHPRIT YRTVCSVNGP LVVLDQVKFA
QYAEIVNFTL PNGTQRSGQV LEVSGTKAIV QVFEGTSGID AQKTTCEFTG DILRTPVSED
MLGRVFNGSG KPIDKGPVVM AEDFLDINGQ PINPHDRIYP EEMIETGISP IDVMNSIARG
QKIPIFSAAG LPHNEIAAQI CRQAGLVKKS KAVLDYHDDN FAIVFAAMGV NMETARFFKS
DFEQNGTMGN VCLFLNLAND PTIERIITPR LALTTAEFLA YQCEKHVLVI LTDMSSYAEA
LREVSAAREE VPGRRGFPGY MYTDLATIYE RAGRVEGRGG SITQIPILTM PNDDITHPIP
DLTGFITEGQ IYVDRQLHNR QIYPPINVLP SLSRLMKSAI GEGMTRKDHG DVSNQLYACY
AIGKDVQAMK AVVGEEALTS EDLLYLEFLQ KFEKKFINQG PYEKRSVFES LDLGWKLLRT
FPKEMLKRIP QNIIDEFFSR EGAPQDTEAD TAL
//
