ID A0A2R8MBE4_CALJA Unreviewed; 540 AA.
AC A0A2R8MBE4;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
DE Short=V-ATPase subunit B {ECO:0000256|RuleBase:RU366021};
DE AltName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
GN Name=ATP6V1B2 {ECO:0000313|Ensembl:ENSCJAP00000056835.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000056835.1, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000056835.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000056835.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments and in some cell
CC types, is targeted to the plasma membrane, where it is responsible for
CC acidifying the extracellular environment.
CC {ECO:0000256|RuleBase:RU366021}.
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. The V1 complex consists of three catalytic AB heterodimers
CC that form a heterohexamer, three peripheral stalks each consisting of
CC EG heterodimers, one central rotor including subunits D and F, and the
CC regulatory subunits C and H. The proton translocation complex V0
CC consists of the proton transport subunit a, a ring of proteolipid
CC subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC subunits. {ECO:0000256|RuleBase:RU366021}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000256|ARBA:ARBA00029434}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00029434}. Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane {ECO:0000256|ARBA:ARBA00037827};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037827}. Melanosome
CC {ECO:0000256|ARBA:ARBA00004223}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU366021}.
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DR RefSeq; XP_002756929.2; XM_002756883.4.
DR AlphaFoldDB; A0A2R8MBE4; -.
DR STRING; 9483.ENSCJAP00000056835; -.
DR Ensembl; ENSCJAT00000082871.3; ENSCJAP00000056835.1; ENSCJAG00000014436.5.
DR GeneID; 100405540; -.
DR KEGG; cjc:100405540; -.
DR CTD; 526; -.
DR GeneTree; ENSGT00940000155068; -.
DR InParanoid; A0A2R8MBE4; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 5473721at2759; -.
DR Proteomes; UP000008225; Chromosome 13.
DR Bgee; ENSCJAG00000014436; Expressed in frontal cortex and 6 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl.
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 NCBIfam; TIGR01040; V-ATPase_V1_B; 1.
DR PANTHER; PTHR43389; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR PANTHER; PTHR43389:SF5; V-TYPE PROTON ATPASE SUBUNIT B, BRAIN 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 PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU366021};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU366021};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT DOMAIN 79..145
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 202..428
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 540 AA; 59480 MW; EF1110E15B7A6E8C CRC64;
MGGPGSAGRL GISAHVRRRC WASRDGGDKM ALRAMRGIVN GAAPELPVPA GGPAVGAREQ
ALAVSRNYLS QPRLTYKTVS GVNGPLVILD HVKFPRYAEI VHLTLPDGTK RSGQVLEVSG
SKAVVQVFEG TSGIDAKKTS CEFTGDILRT PVSEDMLGRV FNGSGKPIDR GPVVLAEDFL
DIMGQPINPQ CRIYPEEMIQ TGISAIDGMN SIARGQKIPI FSAAGLPHNE IAAQICRQAG
LVKKSKDVVD YSEENFAIVF AAMGVNMETA RFFKSDFEEN GSMDNVCLFL NLANDPTIER
IITPRLALTT AEFLAYQCEK HVLVILTDMS SYAEALREVS AAREEVPGRR GFPGYMYTDL
ATIYERAGRV EGRNGSITQI PILTMPNDDI THPIPDLTGY ITEGQIYVDR QLHNRQIYPP
INVLPSLSRL MKSAIGEGMT RKDHADVSNQ LYACYAIGKD VQAMKAVVGE EALTSDDLLY
LEFLQKFERN FIAQGPYENR TVYETLDIGW QLLRIFPKEM LKRIPQSTLS EFYPRDSAKH
//
