VATF_YEAST
ID VATF_YEAST Reviewed; 118 AA.
AC P39111; D6VUF5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=V-type proton ATPase subunit F;
DE Short=V-ATPase subunit F;
DE AltName: Full=V-ATPase 14 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit F;
GN Name=VMA7 {ECO:0000303|PubMed:7929071}; OrderedLocusNames=YGR020C;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=7929071; DOI=10.1016/s0021-9258(19)51061-4;
RA Nelson H., Mandiyan S., Nelson N.;
RT "The Saccharomyces cerevisiae VMA7 gene encodes a 14-kDa subunit of the
RT vacuolar H(+)-ATPase catalytic sector.";
RL J. Biol. Chem. 269:24150-24155(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sigma 1278B;
RX PubMed=7929308; DOI=10.1016/s0021-9258(18)47146-3;
RA Graham L.A., Hill K.J., Stevens T.H.;
RT "VMA7 encodes a novel 14-kDa subunit of the Saccharomyces cerevisiae
RT vacuolar H(+)-ATPase complex.";
RL J. Biol. Chem. 269:25974-25977(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION IN THE V-ATPASE COMPLEX, MASS SPECTROMETRY, AND CLEAVAGE OF
RP INITIATOR METHIONINE.
RX PubMed=18055462; DOI=10.1074/jbc.m707924200;
RA Kitagawa N., Mazon H., Heck A.J.R., Wilkens S.;
RT "Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase
RT determined by mass spectrometry.";
RL J. Biol. Chem. 283:3329-3337(2008).
RN [8] {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 [9] {ECO:0007744|PDB:5D80}
RP X-RAY CRYSTALLOGRAPHY (6.20 ANGSTROMS), AND IDENTIFICATION IN THE V-ATPASE
RP 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:7929071). V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments (PubMed:7929071).
CC {ECO:0000269|PubMed:7929071}.
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:18055462, ECO:0000269|PubMed:25971514,
CC ECO:0000269|PubMed:27295975, ECO:0000269|PubMed:7929071}.
CC -!- INTERACTION:
CC P39111; P41807: VMA13; NbExp=3; IntAct=EBI-20272, EBI-20281;
CC P39111; P32366: VMA6; NbExp=7; IntAct=EBI-20272, EBI-20201;
CC P39111; P32610: VMA8; NbExp=3; IntAct=EBI-20272, EBI-20264;
CC P39111; P32563: VPH1; NbExp=5; IntAct=EBI-20272, EBI-20455;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:7929071};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=13374.1; Mass_error=1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18055462};
CC -!- MISCELLANEOUS: Present with 4050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the V-ATPase F subunit family. {ECO:0000305}.
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DR EMBL; U10073; AAA50753.1; -; Genomic_DNA.
DR EMBL; U12786; AAA53208.1; -; Genomic_DNA.
DR EMBL; Z72805; CAA97003.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08116.1; -; Genomic_DNA.
DR PIR; A55118; A55118.
DR RefSeq; NP_011534.1; NM_001181149.1.
DR PDB; 3J9T; EM; 6.90 A; N=1-118.
DR PDB; 3J9U; EM; 7.60 A; N=1-118.
DR PDB; 3J9V; EM; 8.30 A; N=1-118.
DR PDB; 4IX9; X-ray; 2.33 A; A/B/C/D=1-94.
DR PDB; 4RND; X-ray; 3.18 A; B/D=1-118.
DR PDB; 5D80; X-ray; 6.20 A; O/o=1-118.
DR PDB; 5VOX; EM; 6.80 A; N=1-118.
DR PDB; 5VOY; EM; 7.90 A; N=1-118.
DR PDB; 5VOZ; EM; 7.60 A; N=1-118.
DR PDB; 6O7V; EM; 6.60 A; N=1-118.
DR PDB; 6O7W; EM; 7.00 A; N=1-118.
DR PDB; 6O7X; EM; 8.70 A; N=1-118.
DR PDB; 7FDA; EM; 4.20 A; N=1-118.
DR PDB; 7FDB; EM; 4.80 A; N=1-118.
DR PDB; 7FDC; EM; 6.60 A; N=1-118.
DR PDB; 7FDE; EM; 3.80 A; N=1-118.
DR PDBsum; 3J9T; -.
DR PDBsum; 3J9U; -.
DR PDBsum; 3J9V; -.
DR PDBsum; 4IX9; -.
DR PDBsum; 4RND; -.
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 AlphaFoldDB; P39111; -.
DR SMR; P39111; -.
DR BioGRID; 33262; 62.
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-2077N; -.
DR IntAct; P39111; 22.
DR MINT; P39111; -.
DR STRING; 4932.YGR020C; -.
DR TCDB; 3.A.2.2.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR MaxQB; P39111; -.
DR PaxDb; P39111; -.
DR PRIDE; P39111; -.
DR TopDownProteomics; P39111; -.
DR EnsemblFungi; YGR020C_mRNA; YGR020C; YGR020C.
DR GeneID; 852903; -.
DR KEGG; sce:YGR020C; -.
DR SGD; S000003252; VMA7.
DR VEuPathDB; FungiDB:YGR020C; -.
DR eggNOG; KOG3432; Eukaryota.
DR GeneTree; ENSGT00390000013208; -.
DR HOGENOM; CLU_135754_0_0_1; -.
DR InParanoid; P39111; -.
DR OMA; YTNAFPA; -.
DR BioCyc; YEAST:G3O-30746-MON; -.
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 PRO; PR:P39111; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P39111; protein.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA: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; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0007035; P:vacuolar acidification; TAS:SGD.
DR Gene3D; 3.40.50.10580; -; 1.
DR InterPro; IPR008218; ATPase_V1-cplx_f_g_su.
DR InterPro; IPR005772; ATPase_V1-cplx_fsu_euk.
DR InterPro; IPR036906; ATPase_V1_fsu_sf.
DR Pfam; PF01990; ATP-synt_F; 1.
DR PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR SUPFAM; SSF159468; SSF159468; 1.
DR TIGRFAMs; TIGR01101; V_ATP_synt_F; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18055462"
FT CHAIN 2..118
FT /note="V-type proton ATPase subunit F"
FT /id="PRO_0000144812"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:4RND"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:4IX9"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:4IX9"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:4IX9"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:4IX9"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4IX9"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:4IX9"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:4IX9"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:4IX9"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:4IX9"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:4IX9"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:4IX9"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:4RND"
SQ SEQUENCE 118 AA; 13461 MW; D21EC0980EB99DFF CRC64;
MAEKRTLIAV IADEDTTTGL LLAGIGQITP ETQEKNFFVY QEGKTTKEEI TDKFNHFTEE
RDDIAILLIN QHIAENIRAR VDSFTNAFPA ILEIPSKDHP YDPEKDSVLK RVRKLFGE
