ID   VATG_YEAST              Reviewed;         114 AA.
AC   P48836; D3DKY7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=V-type proton ATPase subunit G;
DE            Short=V-ATPase subunit G;
DE   AltName: Full=V-ATPase 13 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit G;
GN   Name=VMA10 {ECO:0000303|PubMed:7775427}; OrderedLocusNames=YHR039C-A;
GN   ORFNames=YHR039BC, YHR039C-B;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-15; 57-65 AND 71-84,
RP   FUNCTION, IDENTIFICATION IN THE V-ATPASE COMPLEX, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 200060 / W303;
RX   PubMed=7775427; DOI=10.1074/jbc.270.23.13726;
RA   Supekova L., Supek F., Nelson N.;
RT   "The Saccharomyces cerevisiae VMA10 is an intron-containing gene encoding a
RT   novel 13-kDa subunit of vacuolar H(+)-ATPase.";
RL   J. Biol. Chem. 270:13726-13732(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [6] {ECO:0007744|PDB:3J9T, ECO:0007744|PDB:3J9U, ECO:0007744|PDB:3J9V}
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.90 ANGSTROMS), AND IDENTIFICATION IN
RP   THE V-ATPASE COMPLEX.
RX   PubMed=25971514; DOI=10.1038/nature14365;
RA   Zhao J., Benlekbir S., Rubinstein J.L.;
RT   "Electron cryomicroscopy observation of rotational states in a eukaryotic
RT   V-ATPase.";
RL   Nature 521:241-245(2015).
RN   [7] {ECO:0007744|PDB:5BW9, ECO:0007744|PDB:5D80}
RP   X-RAY CRYSTALLOGRAPHY (6.20 ANGSTROMS) OF 2-114, AND IDENTIFICATION IN THE
RP   V-ATPASE COMPLEX.
RX   PubMed=27295975; DOI=10.15252/embj.201593447;
RA   Oot R.A., Kane P.M., Berry E.A., Wilkens S.;
RT   "Crystal structure of yeast V1-ATPase in the autoinhibited state.";
RL   EMBO J. 35:1694-1706(2016).
CC   -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (PubMed:7775427). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments (PubMed:7775427).
CC       {ECO:0000269|PubMed:7775427}.
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). {ECO:0000269|PubMed:25971514, ECO:0000269|PubMed:27295975,
CC       ECO:0000269|PubMed:7775427}.
CC   -!- INTERACTION:
CC       P48836; P22203: VMA4; NbExp=4; IntAct=EBI-20276, EBI-20268;
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:7775427};
CC       Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 2280 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {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; U21240; AAA74570.1; -; mRNA.
DR   EMBL; U00062; AAB68921.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06731.1; -; Genomic_DNA.
DR   PIR; S70777; S70777.
DR   RefSeq; NP_011905.1; NM_001180027.1.
DR   PDB; 2K88; NMR; -; A=2-58.
DR   PDB; 2KWY; NMR; -; A=61-101.
DR   PDB; 3J9T; EM; 6.90 A; H/J/L=1-114.
DR   PDB; 3J9U; EM; 7.60 A; H/J/L=1-114.
DR   PDB; 3J9V; EM; 8.30 A; H/J/L=1-114.
DR   PDB; 4DL0; X-ray; 2.90 A; G/K=1-114.
DR   PDB; 4EFA; X-ray; 2.82 A; G=1-114.
DR   PDB; 5BW9; X-ray; 7.00 A; J/L/N/j/l/n=2-114.
DR   PDB; 5D80; X-ray; 6.20 A; J/L/N/j/l/n=2-114.
DR   PDB; 5VOX; EM; 6.80 A; H/J/L=1-114.
DR   PDB; 5VOY; EM; 7.90 A; H/J/L=1-114.
DR   PDB; 5VOZ; EM; 7.60 A; H/J/L=1-114.
DR   PDB; 6O7V; EM; 6.60 A; H/J/L=1-114.
DR   PDB; 6O7W; EM; 7.00 A; H/J/L=1-114.
DR   PDB; 6O7X; EM; 8.70 A; H/J/L=1-114.
DR   PDB; 7FDA; EM; 4.20 A; H/J/L=2-114.
DR   PDB; 7FDB; EM; 4.80 A; H/J/L=2-114.
DR   PDB; 7FDC; EM; 6.60 A; H/J/L=2-114.
DR   PDB; 7FDE; EM; 3.80 A; H/J/L=2-114.
DR   PDB; 7TMM; EM; 3.50 A; H/J/L=1-114.
DR   PDB; 7TMO; EM; 3.30 A; H/J/L=1-114.
DR   PDB; 7TMP; EM; 3.30 A; H/J/L=1-114.
DR   PDB; 7TMQ; EM; 3.30 A; H/J/L=1-114.
DR   PDB; 7TMR; EM; 3.50 A; H/J/L=1-114.
DR   PDB; 7TMS; EM; 3.80 A; H/J/L=1-114.
DR   PDB; 7TMT; EM; 3.80 A; H/J/L=1-114.
DR   PDBsum; 2K88; -.
DR   PDBsum; 2KWY; -.
DR   PDBsum; 3J9T; -.
DR   PDBsum; 3J9U; -.
DR   PDBsum; 3J9V; -.
DR   PDBsum; 4DL0; -.
DR   PDBsum; 4EFA; -.
DR   PDBsum; 5BW9; -.
DR   PDBsum; 5D80; -.
DR   PDBsum; 5VOX; -.
DR   PDBsum; 5VOY; -.
DR   PDBsum; 5VOZ; -.
DR   PDBsum; 6O7V; -.
DR   PDBsum; 6O7W; -.
DR   PDBsum; 6O7X; -.
DR   PDBsum; 7FDA; -.
DR   PDBsum; 7FDB; -.
DR   PDBsum; 7FDC; -.
DR   PDBsum; 7FDE; -.
DR   PDBsum; 7TMM; -.
DR   PDBsum; 7TMO; -.
DR   PDBsum; 7TMP; -.
DR   PDBsum; 7TMQ; -.
DR   PDBsum; 7TMR; -.
DR   PDBsum; 7TMS; -.
DR   PDBsum; 7TMT; -.
DR   AlphaFoldDB; P48836; -.
DR   BMRB; P48836; -.
DR   EMDB; EMD-0646; -.
DR   EMDB; EMD-0647; -.
DR   EMDB; EMD-0648; -.
DR   EMDB; EMD-25996; -.
DR   EMDB; EMD-25997; -.
DR   EMDB; EMD-25998; -.
DR   EMDB; EMD-25999; -.
DR   EMDB; EMD-26000; -.
DR   EMDB; EMD-26001; -.
DR   EMDB; EMD-26002; -.
DR   EMDB; EMD-31538; -.
DR   EMDB; EMD-31539; -.
DR   EMDB; EMD-31540; -.
DR   EMDB; EMD-31541; -.
DR   EMDB; EMD-8724; -.
DR   EMDB; EMD-8725; -.
DR   EMDB; EMD-8726; -.
DR   SMR; P48836; -.
DR   BioGRID; 36471; 418.
DR   ComplexPortal; CPX-1192; Vacuolar proton translocating ATPase complex, Golgi variant.
DR   ComplexPortal; CPX-1193; Vacuolar proton translocating ATPase complex, vacuole variant.
DR   DIP; DIP-2720N; -.
DR   IntAct; P48836; 9.
DR   MINT; P48836; -.
DR   STRING; 4932.YHR039C-A; -.
DR   TCDB; 3.A.2.2.3; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; P48836; -.
DR   MaxQB; P48836; -.
DR   PaxDb; 4932-YHR039C-A; -.
DR   PeptideAtlas; P48836; -.
DR   TopDownProteomics; P48836; -.
DR   EnsemblFungi; YHR039C-A_mRNA; YHR039C-A; YHR039C-A.
DR   GeneID; 856435; -.
DR   KEGG; sce:YHR039C-A; -.
DR   AGR; SGD:S000002100; -.
DR   SGD; S000002100; VMA10.
DR   VEuPathDB; FungiDB:YHR039C-A; -.
DR   eggNOG; KOG1772; Eukaryota.
DR   HOGENOM; CLU_125101_2_1_1; -.
DR   InParanoid; P48836; -.
DR   OMA; ARKYRQD; -.
DR   OrthoDB; 2730216at2759; -.
DR   BioCyc; YEAST:G3O-31242-MONOMER; -.
DR   Reactome; R-SCE-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-SCE-77387; Insulin receptor recycling.
DR   Reactome; R-SCE-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR   BioGRID-ORCS; 856435; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P48836; -.
DR   PRO; PR:P48836; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P48836; Protein.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; NAS:ComplexPortal.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; TAS:SGD.
DR   GO; GO:0048388; P:endosomal lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0061795; P:Golgi lumen acidification; NAS:ComplexPortal.
DR   GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal.
DR   GO; GO:0007035; P:vacuolar acidification; TAS:SGD.
DR   Gene3D; 1.20.5.620; F1F0 ATP synthase subunit B, membrane domain; 1.
DR   Gene3D; 1.20.5.730; Single helix bin; 1.
DR   InterPro; IPR005124; V-ATPase_G.
DR   NCBIfam; TIGR01147; V_ATP_synt_G; 1.
DR   PANTHER; PTHR12713:SF11; V-TYPE PROTON ATPASE SUBUNIT G; 1.
DR   PANTHER; PTHR12713; VACUOLAR ATP SYNTHASE SUBUNIT G; 1.
DR   Pfam; PF03179; V-ATPase_G; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport; Vacuole.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..114
FT                   /note="V-type proton ATPase subunit G"
FT                   /id="PRO_0000192916"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   HELIX           4..60
FT                   /evidence="ECO:0007829|PDB:4EFA"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:7TMO"
FT   HELIX           70..73
FT                   /evidence="ECO:0007829|PDB:4DL0"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:4EFA"
FT   HELIX           77..89
FT                   /evidence="ECO:0007829|PDB:4EFA"
FT   HELIX           91..102
FT                   /evidence="ECO:0007829|PDB:4EFA"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:7TMP"
SQ   SEQUENCE   114 AA;  12713 MW;  259660D440A933D0 CRC64;
     MSQKNGIATL LQAEKEAHEI VSKARKYRQD KLKQAKTDAA KEIDSYKIQK DKELKEFEQK
     NAGGVGELEK KAEAGVQGEL AEIKKIAEKK KDDVVKILIE TVIKPSAEVH INAL
//