VATB_DICDI
ID VATB_DICDI Reviewed; 493 AA.
AC Q76NU1; Q23926; Q54ZN4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=V-type proton ATPase subunit B;
DE Short=V-ATPase subunit B;
DE AltName: Full=Vacuolar proton pump subunit B;
GN Name=vatB; Synonyms=dvacB; ORFNames=DDB_G0277401;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9426215; DOI=10.1016/s0014-5793(97)01425-7;
RA Bracco E., Peracino B., Noegel A.A., Bozzaro S.;
RT "Cloning and transcriptional regulation of the gene encoding the
RT vacuolar/H+ ATPase B subunit of Dictyostelium discoideum.";
RL FEBS Lett. 419:37-40(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP PROTEIN SEQUENCE OF 2-19; 232-241; 292-307; 391-421 AND 433-445, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7593293; DOI=10.1242/jcs.108.10.3331;
RA Adessi C., Chapel A., Vincon M., Rabilloud T., Klein G., Satre M.,
RA Garin J.;
RT "Identification of major proteins associated with Dictyostelium discoideum
RT endocytic vesicles.";
RL J. Cell Sci. 108:3331-3337(1995).
RN [5]
RP PROTEIN SEQUENCE OF 2-13 AND 60-68, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Patel H., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 213-488, AND FUNCTION.
RX PubMed=8899714; DOI=10.1111/j.1365-2958.1996.tb02661.x;
RA Davies L., Farrar N.A., Satre M., Dottin R.P., Gross J.D.;
RT "Vacuolar H(+)-ATPase and weak base action in Dictyostelium.";
RL Mol. Microbiol. 22:119-126(1996).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=8509452; DOI=10.1083/jcb.121.6.1311;
RA Heuser J., Zhu Q., Clarke M.;
RT "Proton pumps populate the contractile vacuoles of Dictyostelium amoebae.";
RL J. Cell Biol. 121:1311-1327(1993).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16445684; DOI=10.1111/j.1600-0854.2005.00356.x;
RA Peracino B., Wagner C., Balest A., Balbo A., Pergolizzi B., Noegel A.A.,
RA Steinert M., Bozzaro S.;
RT "Function and mechanism of action of Dictyostelium Nramp1 (Slc11a1) in
RT bacterial infection.";
RL Traffic 7:22-38(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
CC -!- FUNCTION: Vacuolar ATPase is responsible for acidifying a variety of
CC intracellular compartments in eukaryotic cells. The B subunit is non-
CC catalytic but combines with other subunits to form the catalytic
CC complex. V-ATPase is responsible for energizing electrophoretic
CC K(+)/2H(+) antiport by generating a transmembrane voltage of more than
CC 200 mV (By similarity). {ECO:0000250, ECO:0000269|PubMed:8899714}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (main components: subunits A, B, C, D, E, and F)
CC attached to an integral membrane V0 proton pore complex (main
CC component: the proteolipid protein). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side. Endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Contractile vacuole membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Detected on macropinosomes and
CC phagosomes, on contractile vacuoles, cytoplasmic cisternae and on the
CC tubular extensions linking these vesicles.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during vegetative growth. Down-
CC regulated in starving cells and during development.
CC {ECO:0000269|PubMed:9426215}.
CC -!- INDUCTION: Down-regulated when cells are exposed to an acid
CC environment. Up-regulated when cells are exposed to high pH.
CC {ECO:0000269|PubMed:9426215}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000020; EAL68663.1; -; Genomic_DNA.
DR EMBL; U63317; AAB04559.1; -; mRNA.
DR RefSeq; XP_642608.1; XM_637516.1.
DR AlphaFoldDB; Q76NU1; -.
DR SMR; Q76NU1; -.
DR STRING; 44689.DDB0185207; -.
DR PaxDb; Q76NU1; -.
DR EnsemblProtists; EAL68663; EAL68663; DDB_G0277401.
DR GeneID; 8621025; -.
DR KEGG; ddi:DDB_G0277401; -.
DR dictyBase; DDB_G0277401; vatB.
DR eggNOG; KOG1351; Eukaryota.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; Q76NU1; -.
DR OMA; GFKIKPR; -.
DR PhylomeDB; Q76NU1; -.
DR Reactome; R-DDI-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-DDI-77387; Insulin receptor recycling.
DR Reactome; R-DDI-917977; Transferrin endocytosis and recycling.
DR Reactome; R-DDI-9639288; Amino acids regulate mTORC1.
DR PRO; PR:Q76NU1; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0031164; C:contractile vacuolar membrane; IDA:dictyBase.
DR GO; GO:0030139; C:endocytic vesicle; IDA:dictyBase.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140220; C:pathogen-containing vacuole; HDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0036176; P:response to neutral pH; IMP:dictyBase.
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 Cytoplasmic vesicle; Direct protein sequencing; Endosome;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7593293, ECO:0000269|Ref.5"
FT CHAIN 2..493
FT /note="V-type proton ATPase subunit B"
FT /id="PRO_0000328285"
FT CONFLICT 237
FT /note="F -> S (in Ref. 6; AAB04559)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="G -> R (in Ref. 6; AAB04559)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="Y -> N (in Ref. 6; AAB04559)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="N -> K (in Ref. 6; AAB04559)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="L -> W (in Ref. 6; AAB04559)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="I -> L (in Ref. 6; AAB04559)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="L -> F (in Ref. 6; AAB04559)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="D -> E (in Ref. 6; AAB04559)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="R -> K (in Ref. 6; AAB04559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 54876 MW; 602007FAD488CEB0 CRC64;
MVGFEDHIAA ITRNYQVNPR LDYRTVTAVN GPLVILDNIR GPKFSEIVTL TLGDGTQRKG
QVLEIQGKRA VVQVFEGTIG IDAKHTRCEF SGDILKMPVS EDSLGRIFNG SGKPVDKGPN
VLAEEYLDIQ GQPINPSVRV YPQEMIQTGI SAIDTMNSIA RGQKIPIFSA AGLPHNEIAA
QICRQAGLVK KSGKGVIDDH EDNFAIVFAA MGVNMETASF FKRDFEESGS MDRTALFLNL
ADHPTIERII TPRLALTTAE YLAYQCEKHV LVLLTDMSSY ADALREVSAA REEVPGRRGY
PGYMYTDLST IYERAGRIQG RNGSITQIPI LTMPNDDITH PIPDLTGYIT EGQIFIDRQI
NNRQIYPPIN VLPSLSRLMK SAIGDDMTRG DHSEVSNQMY ANYAIGKDVQ AMKAVVGEEA
LSSEDKLYLE FLERFESSFV GQNHYENRDI FNSLDLGWSL LRTFPSNLLK RITEKTIKQY
YSRSSKGTVD STN
