VATB2_BOVIN
ID VATB2_BOVIN Reviewed; 511 AA.
AC P31408; A4FUX5; Q28058;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=V-type proton ATPase subunit B, brain isoform;
DE Short=V-ATPase subunit B 2;
DE AltName: Full=Endomembrane proton pump 58 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit B 2;
GN Name=ATP6V1B2; Synonyms=ATP6B2;
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].
RC TISSUE=Brain;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-58, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1371275; DOI=10.1016/s0021-9258(19)50581-6;
RA Puopolo K., Kumamoto C., Adachi I., Magner R., Forgac M.;
RT "Differential expression of the 'B' subunit of the vacuolar H(+)-ATPase in
RT bovine tissues.";
RL J. Biol. Chem. 267:3696-3706(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1835703; DOI=10.1016/0014-5793(91)81158-5;
RA Pan Y.X., Xu J., Strasser J.E., Howell M., Dean G.E.;
RT "Structure and expression of subunit A from the bovine chromaffin cell
RT vacuolar ATPase.";
RL FEBS Lett. 293:89-92(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS) IN COMPLEX WITH ADP,
RP FUNCTION, IDENTIFICATION IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32764564; DOI=10.1038/s41467-020-17762-9;
RA Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.;
RT "Cryo-EM structures of intact V-ATPase from bovine brain.";
RL Nat. Commun. 11:3921-3921(2020).
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:32764564). V-ATPase is responsible
CC for acidifying and maintaining the pH of intracellular compartments and
CC in some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment
CC (PubMed:32764564). In renal intercalated cells, can partially
CC compensate the lack of ATP6V1B1 and mediate secretion of protons (H+)
CC into the urine under base-line conditions but not in conditions of acid
CC load (By similarity). {ECO:0000250|UniProtKB:P62814,
CC ECO:0000269|PubMed:32764564}.
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 (PubMed:32764564). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:32764564). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:32764564).
CC {ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P21281}. Melanosome
CC {ECO:0000250|UniProtKB:P21281}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62814}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000269|PubMed:32764564}; Peripheral membrane
CC protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:P62815}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level)
CC (PubMed:1371275, PubMed:32764564). Expressed in all tissues tested, but
CC highest in brain and in adrenal medulla (PubMed:1371275,
CC PubMed:32764564). {ECO:0000269|PubMed:1371275,
CC ECO:0000269|PubMed:32764564}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; M88690; AAA30400.1; -; mRNA.
DR EMBL; M83131; AAA30391.1; -; mRNA.
DR EMBL; X58385; CAA41275.1; -; mRNA.
DR EMBL; BC123404; AAI23405.1; -; mRNA.
DR PIR; S32614; S32614.
DR RefSeq; NP_001001146.1; NM_001001146.1.
DR RefSeq; NP_788844.2; NM_176671.3.
DR PDB; 6XBW; EM; 3.37 A; D/E/F=1-511.
DR PDB; 6XBY; EM; 3.79 A; D/E/F=1-511.
DR PDB; 7KHR; EM; 3.62 A; D/E/F=1-511.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR AlphaFoldDB; P31408; -.
DR SMR; P31408; -.
DR CORUM; P31408; -.
DR STRING; 9913.ENSBTAP00000024812; -.
DR ChEMBL; CHEMBL4798; -.
DR PaxDb; P31408; -.
DR PeptideAtlas; P31408; -.
DR PRIDE; P31408; -.
DR Ensembl; ENSBTAT00000024812; ENSBTAP00000024812; ENSBTAG00000018646.
DR GeneID; 338082; -.
DR KEGG; bta:338082; -.
DR CTD; 526; -.
DR VEuPathDB; HostDB:ENSBTAG00000018646; -.
DR VGNC; VGNC:26318; ATP6V1B2.
DR eggNOG; KOG1351; Eukaryota.
DR GeneTree; ENSGT00940000155068; -.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; P31408; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 541116at2759; -.
DR TreeFam; TF300313; -.
DR Reactome; R-BTA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-BTA-9639288; Amino acids regulate mTORC1.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000018646; Expressed in occipital lobe and 101 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0045851; P:pH reduction; IC:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IC:UniProtKB.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
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 3D-structure; ATP-binding; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Synapse; Transport.
FT CHAIN 1..511
FT /note="V-type proton ATPase subunit B, brain isoform"
FT /id="PRO_0000144625"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:32764564,
FT ECO:0000312|PDB:6XBW, ECO:0007744|PDB:6XBY"
FT CONFLICT 24
FT /note="Missing (in Ref. 1; AAA30400)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="S -> T (in Ref. 2; AAA30391)"
FT /evidence="ECO:0000305"
FT CONFLICT 161..162
FT /note="QC -> HF (in Ref. 1; AAA30400)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="E -> Q (in Ref. 3; CAA41275)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="R -> K (in Ref. 1; AAA30400)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="A -> T (in Ref. 1; AAA30400)"
FT /evidence="ECO:0000305"
FT CONFLICT 510..511
FT /note="KH -> NS (in Ref. 2; AAA30391)"
FT /evidence="ECO:0000305"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 199..204
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 392..399
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 415..438
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 446..461
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 473..482
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 483..486
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 497..503
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 511 AA; 56577 MW; E8DC915692F25E99 CRC64;
MALRAMRGIV NGAAPELPVP TSGPLAGSRE QALAVSRNYL SQPRLTYKTV SGVNGPLVIL
DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE GTSGIDAKKT SCEFTGDILR
TPVSEDMLGR VFNGSGKPID RGPVVLAEDF LDIMGQPINP QCRIYPEEMI QTGISAIDGM
NSIARGQKIP IFSAAGLPHN EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET
ARFFKSDFEE NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM
SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD
ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR LMKSAIGEGM TRKDHADVSN
QLYACYAIGK DVQAMKAVVG EEALTSDDLL YLEFLQKFER NFIAQGPYEN RTVYETLDIG
WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H
