RNK_YEAST
ID RNK_YEAST Reviewed; 85 AA.
AC P0C5R9; D6W4H1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=V-type proton ATPase subunit f {ECO:0000303|PubMed:29526695};
DE Short=V-ATPase subunit f;
GN OrderedLocusNames=YPR170W-B {ECO:0000312|SGD:S000028515};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP GENOME REANNOTATION.
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [4]
RP GENOME REANNOTATION.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [5]
RP IDENTIFICATION IN THE V-ATPASE COMPLEX.
RX PubMed=27776355; DOI=10.1038/nature19828;
RA Mazhab-Jafari M.T., Rohou A., Schmidt C., Bueler S.A., Benlekbir S.,
RA Robinson C.V., Rubinstein J.L.;
RT "Atomic model for the membrane-embedded VO motor of a eukaryotic V-
RT ATPase.";
RL Nature 539:118-122(2016).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=26928762; DOI=10.1038/nmeth.3795;
RA Yofe I., Weill U., Meurer M., Chuartzman S., Zalckvar E., Goldman O.,
RA Ben-Dor S., Schuetze C., Wiedemann N., Knop M., Khmelinskii A.,
RA Schuldiner M.;
RT "One library to make them all: streamlining the creation of yeast libraries
RT via a SWAp-Tag strategy.";
RL Nat. Methods 13:371-378(2016).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29897761; DOI=10.1021/acs.jproteome.8b00032;
RA He C., Jia C., Zhang Y., Xu P.;
RT "Enrichment-based proteogenomics identifies microproteins, missing
RT proteins, and novel smORFs in Saccharomyces cerevisiae.";
RL J. Proteome Res. 17:2335-2344(2018).
RN [8] {ECO:0007744|PDB:6C6L}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND IDENTIFICATION IN
RP THE V-ATPASE COMPLEX.
RX PubMed=29526695; DOI=10.1016/j.molcel.2018.02.006;
RA Roh S.H., Stam N.J., Hryc C.F., Couoh-Cardel S., Pintilie G., Chiu W.,
RA Wilkens S.;
RT "The 3.5-A cryoEM structure of nanodisc-reconstituted yeast vacuolar ATPase
RT V0 proton channel.";
RL Mol. Cell 69:993-1004.e3(2018).
RN [9] {ECO:0007744|PDB:6O7T, ECO:0007744|PDB:6O7U, ECO:0007744|PDB:6O7V, ECO:0007744|PDB:6O7W, ECO:0007744|PDB:6O7X}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS).
RX PubMed=30910982; DOI=10.1073/pnas.1814818116;
RA Vasanthakumar T., Bueler S.A., Wu D., Beilsten-Edmands V., Robinson C.V.,
RA Rubinstein J.L.;
RT "Structural comparison of the vacuolar and Golgi V-ATPases from
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:7272-7277(2019).
RN [10] {ECO:0007744|PDB:6M0R, ECO:0007744|PDB:6M0S}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS) OF 7-75.
RX PubMed=33028525; DOI=10.1126/sciadv.abb9605;
RA Roh S.H., Shekhar M., Pintilie G., Chipot C., Wilkens S., Singharoy A.,
RA Chiu W.;
RT "Cryo-EM and MD infer water-mediated proton transport and autoinhibition
RT mechanisms of Vo complex.";
RL Sci. Adv. 6:0-0(2020).
CC -!- FUNCTION: Accessory component of the V0 complex of vacuolar(H+)-ATPase
CC (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1)
CC that hydrolyzes ATP and a membrane integral complex (V0) that
CC translocates protons (PubMed:29526695). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments
CC (PubMed:29526695). {ECO:0000269|PubMed:29526695}.
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:29526695, ECO:0000269|PubMed:30910982,
CC ECO:0000269|PubMed:33028525}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30910982, ECO:0000305|PubMed:29526695}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:29526695,
CC ECO:0000269|PubMed:30910982}. Vacuole membrane
CC {ECO:0000269|PubMed:26928762, ECO:0000269|PubMed:30910982}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:30910982}.
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DR EMBL; U25840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U25842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006949; DAA11587.1; -; Genomic_DNA.
DR RefSeq; NP_001106949.1; NM_001184525.1.
DR PDB; 6C6L; EM; 3.50 A; O=1-85.
DR PDB; 6M0R; EM; 2.70 A; O=7-75.
DR PDB; 6M0S; EM; 3.60 A; O=7-75.
DR PDB; 6O7T; EM; 3.20 A; f=1-85.
DR PDB; 6O7U; EM; 3.10 A; f=1-85.
DR PDB; 6O7V; EM; 6.60 A; f=1-85.
DR PDB; 6O7W; EM; 7.00 A; f=1-85.
DR PDB; 6O7X; EM; 8.70 A; f=1-85.
DR PDB; 6PE4; EM; 3.10 A; F=1-85.
DR PDB; 6PE5; EM; 3.20 A; F=1-85.
DR PDB; 7FDA; EM; 4.20 A; f=1-85.
DR PDB; 7FDB; EM; 4.80 A; f=1-85.
DR PDB; 7FDC; EM; 6.60 A; f=1-85.
DR PDB; 7TAO; EM; 3.20 A; O=1-85.
DR PDB; 7TAP; EM; 2.80 A; O=1-85.
DR PDB; 7TMR; EM; 3.50 A; f=1-85.
DR PDB; 7TMS; EM; 3.80 A; f=1-85.
DR PDBsum; 6C6L; -.
DR PDBsum; 6M0R; -.
DR PDBsum; 6M0S; -.
DR PDBsum; 6O7T; -.
DR PDBsum; 6O7U; -.
DR PDBsum; 6O7V; -.
DR PDBsum; 6O7W; -.
DR PDBsum; 6O7X; -.
DR PDBsum; 6PE4; -.
DR PDBsum; 6PE5; -.
DR PDBsum; 7FDA; -.
DR PDBsum; 7FDB; -.
DR PDBsum; 7FDC; -.
DR PDBsum; 7TAO; -.
DR PDBsum; 7TAP; -.
DR PDBsum; 7TMR; -.
DR PDBsum; 7TMS; -.
DR AlphaFoldDB; P0C5R9; -.
DR SMR; P0C5R9; -.
DR BioGRID; 927818; 4.
DR ComplexPortal; CPX-1192; Vacuolar proton translocating ATPase complex, Golgi variant.
DR ComplexPortal; CPX-1193; Vacuolar proton translocating ATPase complex, vacuole variant.
DR STRING; 4932.YPR170W-B; -.
DR iPTMnet; P0C5R9; -.
DR PaxDb; P0C5R9; -.
DR PRIDE; P0C5R9; -.
DR EnsemblFungi; YPR170W-B_mRNA; YPR170W-B; YPR170W-B.
DR GeneID; 5848745; -.
DR KEGG; sce:YPR170W-B; -.
DR SGD; S000028515; YPR170W-B.
DR VEuPathDB; FungiDB:YPR170W-B; -.
DR eggNOG; ENOG502S504; Eukaryota.
DR GeneTree; ENSGT00940000176787; -.
DR HOGENOM; CLU_115063_1_0_1; -.
DR InParanoid; P0C5R9; -.
DR OMA; AMNAWTC; -.
DR BioCyc; YEAST:G3O-34362-MON; -.
DR PRO; PR:P0C5R9; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P0C5R9; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IC:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IC:UniProtKB.
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; IC:UniProtKB.
DR InterPro; IPR026770; RNase_K.
DR PANTHER; PTHR31733; PTHR31733; 1.
PE 3: Inferred from homology;
KW 3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..85
FT /note="V-type proton ATPase subunit f"
FT /id="PRO_0000309067"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:30910982"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30910982"
FT TOPO_DOM 32..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30910982"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30910982"
FT TOPO_DOM 76..85
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:30910982"
FT HELIX 8..33
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 48..74
FT /evidence="ECO:0007829|PDB:6M0R"
SQ SEQUENCE 85 AA; 9361 MW; 5F3F0188E0381587 CRC64;
MRPVVSTGKA WCCTVLSAFG VVILSVIAHL FNTNHESFVG SINDPEDGPA VAHTVYLAAL
VYLVFFVFCG FQVYLARRKP SIELR
