ID   VATB_SCHPO              Reviewed;         503 AA.
AC   P31411;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=V-type proton ATPase subunit B {ECO:0000303|PubMed:1441756};
DE            Short=V-ATPase subunit B;
DE   AltName: Full=V-ATPase 57 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit B;
GN   Name=vma2 {ECO:0000312|PomBase:SPAC637.05c};
GN   ORFNames=SPAC637.05c {ECO:0000312|PomBase:SPAC637.05c};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=1441756; DOI=10.1002/yea.320080913;
RA   Ghislain M., Bowman E.J.;
RT   "Sequence of the genes encoding subunits A and B of the vacuolar H(+)-
RT   ATPase of Schizosaccharomyces pombe.";
RL   Yeast 8:791-799(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   INTERACTION WITH RAV1.
RX   PubMed=18441123; DOI=10.1128/ec.00037-08;
RA   Dawson K., Toone W.M., Jones N., Wilkinson C.R.;
RT   "Loss of regulators of vacuolar ATPase function and ceramide synthesis
RT   results in multidrug sensitivity in Schizosaccharomyces pombe.";
RL   Eukaryot. Cell 7:926-937(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491; SER-492; SER-502 AND
RP   SER-503, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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 (By
CC       similarity). {ECO:0000250|UniProtKB:P16140}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (components A to H) attached to an integral
CC       membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC       VOA1) (By similarity). Interacts with rav1 (PubMed:18441123).
CC       {ECO:0000250|UniProtKB:P16140, ECO:0000269|PubMed:18441123}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P16140};
CC       Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}.
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; X69638; CAA49339.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA22584.1; -; Genomic_DNA.
DR   PIR; S25335; S25335.
DR   PIR; T38997; T38997.
DR   RefSeq; NP_594623.1; NM_001020051.2.
DR   AlphaFoldDB; P31411; -.
DR   SMR; P31411; -.
DR   BioGRID; 279830; 8.
DR   STRING; 284812.P31411; -.
DR   iPTMnet; P31411; -.
DR   MaxQB; P31411; -.
DR   PaxDb; 4896-SPAC637-05c-1; -.
DR   EnsemblFungi; SPAC637.05c.1; SPAC637.05c.1:pep; SPAC637.05c.
DR   GeneID; 2543408; -.
DR   KEGG; spo:SPAC637.05c; -.
DR   PomBase; SPAC637.05c; vma2.
DR   VEuPathDB; FungiDB:SPAC637.05c; -.
DR   eggNOG; KOG1351; Eukaryota.
DR   HOGENOM; CLU_022916_3_0_1; -.
DR   InParanoid; P31411; -.
DR   OMA; GFKIKPR; -.
DR   PhylomeDB; P31411; -.
DR   Reactome; R-SPO-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-SPO-77387; Insulin receptor recycling.
DR   Reactome; R-SPO-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-SPO-9639288; Amino acids regulate mTORC1.
DR   PRO; PR:P31411; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISO:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IC:PomBase.
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:1902600; P:proton transmembrane transport; ISO:PomBase.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
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:SF4; V-TYPE PROTON ATPASE SUBUNIT B; 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   1: Evidence at protein level;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transport; Vacuole.
FT   CHAIN           1..503
FT                   /note="V-type proton ATPase subunit B"
FT                   /id="PRO_0000144647"
FT   BINDING         378
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21281"
FT   MOD_RES         491
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         492
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         502
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   503 AA;  55841 MW;  BC1C15C7E915920F CRC64;
     MASLFDINAA AAVKDYSIKP RLSYNTVNSI TGPLVILDNI RRPQYNEIVN LNLPDGSVRS
     GQVLEVAGHK AIVQVFEGTS GVDVRKTTID FTGHSMRIPV SEDMLGRVFN GSGLPIDKGP
     NLLAEDYLDI NGSPINPYAR IYPEEMIQTG ISSIDGLNSI ARGQKIPIFS AAGLPHNEIA
     AQICRQAGLV KRPTKDVHDG HEDNFSIVFA AMGVNLETAR FFQRDFEENG SFERVTLFLN
     LANDPTIERI ITPRLALSAS EFLAYQTEKH VLTILTDMTS YADALREVSA AREEVPGRRG
     YPGYMYTDLS TIYERAGRVE GRNGSITQIP ILTMPNDDIT HPIPDLTGYI TEGQIFVDRQ
     LHNNAIYPPI NVLPSLSRLM KSAIGEGMTR NDHGDVSNQL YAMYAIGRDA ASMKSVVGEE
     ALSQEDRLAL EFLGKFEKTF ISQGAYENRT IFETLDLAWS LLRIFPREML TRIPKKILDQ
     YYSRSSAYTE SSKDVIDNTP ESS
//