VATO_YEAST
ID VATO_YEAST Reviewed; 213 AA.
AC P23968; D3DKX3;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=V-type proton ATPase subunit c'';
DE Short=V-ATPase subunit c'';
DE AltName: Full=V-ATPase 22 kDa proteolipid subunit;
DE AltName: Full=Vacuolar proton pump c'' subunit;
GN Name=VMA16; Synonyms=PPA1; OrderedLocusNames=YHR026W;
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].
RX PubMed=2139779; DOI=10.1016/0006-291x(90)92359-8;
RA Apperson M., Jensen R.E., Suda K., Witte C., Yaffe M.P.;
RT "A yeast protein, homologous to the proteolipid of the chromaffin granule
RT proton-ATPase, is important for cell growth.";
RL Biochem. Biophys. Res. Commun. 168:574-579(1990).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-108.
RX PubMed=9030535; DOI=10.1074/jbc.272.8.4795;
RA Hirata R., Graham L.A., Takatsuki A., Stevens T.H., Anraku Y.;
RT "VMA11 and VMA16 encode second and third proteolipid subunits of the
RT Saccharomyces cerevisiae vacuolar membrane H+-ATPase.";
RL J. Biol. Chem. 272:4795-4803(1997).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [7] {ECO:0007744|PDB:5TJ5}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), AND IDENTIFICATION IN
RP 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 [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 Vo Proton Channel.";
RL Mol. Cell 69:993-1004.e3(2018).
CC -!- FUNCTION: Proton-conducting pore forming of the V0 complex of
CC vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC complex (V0) that translocates protons (PubMed:9030535). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments (PubMed:9030535). {ECO:0000269|PubMed:9030535}.
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) (PubMed:27776355, PubMed:29526695). The decameric c-ring forms
CC the proton-conducting pore, and is composed of eight proteolipid
CC subunits c, one subunit c' and one subunit c'' (PubMed:27776355,
CC PubMed:29526695). {ECO:0000269|PubMed:27776355,
CC ECO:0000269|PubMed:29526695}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:9030535};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; M35294; AAA34892.1; -; Genomic_DNA.
DR EMBL; U10399; AAB68881.1; -; Genomic_DNA.
DR EMBL; AY692797; AAT92816.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06717.1; -; Genomic_DNA.
DR PIR; A34633; A34633.
DR RefSeq; NP_011891.1; NM_001179156.1.
DR PDB; 5TJ5; EM; 3.90 A; B=1-213.
DR PDB; 5VOX; EM; 6.80 A; R=1-213.
DR PDB; 5VOY; EM; 7.90 A; R=1-213.
DR PDB; 5VOZ; EM; 7.60 A; R=1-213.
DR PDB; 6C6L; EM; 3.50 A; C=1-213.
DR PDB; 6M0R; EM; 2.70 A; C=16-213.
DR PDB; 6M0S; EM; 3.60 A; C=16-213.
DR PDB; 6O7T; EM; 3.20 A; c=1-213.
DR PDB; 6O7U; EM; 3.10 A; c=1-213.
DR PDB; 6O7V; EM; 6.60 A; c=1-213.
DR PDB; 6O7W; EM; 7.00 A; c=1-213.
DR PDB; 6O7X; EM; 8.70 A; c=1-213.
DR PDB; 6PE4; EM; 3.10 A; G=1-213.
DR PDB; 6PE5; EM; 3.20 A; G=1-213.
DR PDB; 7FDA; EM; 4.20 A; T=1-213.
DR PDB; 7FDB; EM; 4.80 A; T=1-213.
DR PDB; 7FDC; EM; 6.60 A; T=1-213.
DR PDB; 7TAO; EM; 3.20 A; C=1-213.
DR PDB; 7TAP; EM; 2.80 A; C=1-213.
DR PDB; 7TMR; EM; 3.50 A; c=1-213.
DR PDB; 7TMS; EM; 3.80 A; c=1-213.
DR PDBsum; 5TJ5; -.
DR PDBsum; 5VOX; -.
DR PDBsum; 5VOY; -.
DR PDBsum; 5VOZ; -.
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; P23968; -.
DR SMR; P23968; -.
DR BioGRID; 36457; 64.
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-4054N; -.
DR IntAct; P23968; 9.
DR MINT; P23968; -.
DR STRING; 4932.YHR026W; -.
DR TCDB; 3.A.2.2.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PaxDb; P23968; -.
DR PRIDE; P23968; -.
DR EnsemblFungi; YHR026W_mRNA; YHR026W; YHR026W.
DR GeneID; 856421; -.
DR KEGG; sce:YHR026W; -.
DR SGD; S000001068; VMA16.
DR VEuPathDB; FungiDB:YHR026W; -.
DR eggNOG; KOG0233; Eukaryota.
DR GeneTree; ENSGT00550000075120; -.
DR HOGENOM; CLU_085752_0_1_1; -.
DR OMA; PYAWAST; -.
DR BioCyc; YEAST:G3O-31086-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:P23968; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P23968; protein.
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; IDA:SGD.
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; IDA:MGI.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:UniProtKB.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IDA:MGI.
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:MGI.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..213
FT /note="V-type proton ATPase subunit c''"
FT /id="PRO_0000071780"
FT TOPO_DOM 1..14
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..100
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..183
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT SITE 108
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000269|PubMed:9030535"
FT MUTAGEN 108
FT /note="E->D: Partial inactivation."
FT /evidence="ECO:0000269|PubMed:9030535"
FT MUTAGEN 108
FT /note="E->L,Q,V: Inactivation."
FT /evidence="ECO:0000269|PubMed:9030535"
FT HELIX 17..38
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 56..89
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 97..101
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 102..122
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 136..176
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 180..205
FT /evidence="ECO:0007829|PDB:6M0R"
SQ SEQUENCE 213 AA; 22596 MW; 033FF5A516B97F8B CRC64;
MNKESKDDDM SLGKFSFSHF LYYLVLIVVI VYGLYKLFTG HGSDINFGKF LLRTSPYMWA
NLGIALCVGL SVVGAAWGIF ITGSSMIGAG VRAPRITTKN LISIIFCEVV AIYGLIIAIV
FSSKLTVATA ENMYSKSNLY TGYSLFWAGI TVGASNLICG IAVGITGATA AISDAADSAL
FVKILVIEIF GSILGLLGLI VGLLMAGKAS EFQ
