VATB2_RAT
ID VATB2_RAT Reviewed; 511 AA.
AC P62815; O09045; P50517;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
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, Vat2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Westberg M.S., Lundberg L.G.;
RT "Antisense technology and bone resorption.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP PROTEIN SEQUENCE OF 189-208; 387-400 AND 461-471, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4] {ECO:0007744|PDB:6VQ6, ECO:0007744|PDB:6VQ7, ECO:0007744|PDB:6VQ8, ECO:0007744|PDB:6VQ9, ECO:0007744|PDB:6VQA, ECO:0007744|PDB:6VQB}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 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=32165585; DOI=10.1126/science.aaz2924;
RA Abbas Y.M., Wu D., Bueler S.A., Robinson C.V., Rubinstein J.L.;
RT "Structure of V-ATPase from the mammalian brain.";
RL Science 367:1240-1246(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:32165585). 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:32165585). 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:32165585}.
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:32165585). 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:32165585). 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:32165585).
CC {ECO:0000269|PubMed:32165585}.
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, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; Peripheral
CC membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000269|PubMed:32165585}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32165585}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; Y12635; CAA73183.1; -; mRNA.
DR EMBL; BC085714; AAH85714.1; -; mRNA.
DR RefSeq; NP_476561.1; NM_057213.2.
DR PDB; 6VQ6; EM; 3.90 A; D/E/F=1-511.
DR PDB; 6VQ7; EM; 4.00 A; D/E/F=1-511.
DR PDB; 6VQ8; EM; 3.90 A; D/E/F=1-511.
DR PDB; 6VQ9; EM; 3.60 A; D/E/F=1-511.
DR PDB; 6VQA; EM; 3.70 A; D/E/F=1-511.
DR PDB; 6VQB; EM; 3.60 A; D/E/F=1-511.
DR PDBsum; 6VQ6; -.
DR PDBsum; 6VQ7; -.
DR PDBsum; 6VQ8; -.
DR PDBsum; 6VQ9; -.
DR PDBsum; 6VQA; -.
DR PDBsum; 6VQB; -.
DR AlphaFoldDB; P62815; -.
DR SMR; P62815; -.
DR BioGRID; 250775; 4.
DR IntAct; P62815; 7.
DR MINT; P62815; -.
DR STRING; 10116.ENSRNOP00000015931; -.
DR iPTMnet; P62815; -.
DR PhosphoSitePlus; P62815; -.
DR World-2DPAGE; 0004:P62815; -.
DR jPOST; P62815; -.
DR PaxDb; P62815; -.
DR PRIDE; P62815; -.
DR Ensembl; ENSRNOT00000015931; ENSRNOP00000015931; ENSRNOG00000011891.
DR GeneID; 117596; -.
DR KEGG; rno:117596; -.
DR UCSC; RGD:620284; rat.
DR CTD; 526; -.
DR RGD; 620284; Atp6v1b2.
DR eggNOG; KOG1351; Eukaryota.
DR GeneTree; ENSGT00940000155068; -.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; P62815; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 541116at2759; -.
DR PhylomeDB; P62815; -.
DR TreeFam; TF300313; -.
DR Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-RNO-77387; Insulin receptor recycling.
DR Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR Reactome; R-RNO-983712; Ion channel transport.
DR PRO; PR:P62815; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000011891; Expressed in brain and 20 other tissues.
DR Genevisible; P62815; RN.
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:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
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:0030641; P:regulation of cellular pH; TAS:RGD.
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_0000144629"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:32165585,
FT ECO:0000312|PDB:6VQ6, ECO:0000312|PDB:6VQ9,
FT ECO:0007744|PDB:6VQ7, ECO:0007744|PDB:6VQ8,
FT ECO:0007744|PDB:6VQA, ECO:0007744|PDB:6VQB"
SQ SEQUENCE 511 AA; 56551 MW; E116BF9A36EEF36B CRC64;
MALRAMRGIV NGAAPELPVP TGGPMAGARE 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 YLEFLQKFEK NFITQGPYEN RTVYETLDIG
WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H
