VATL1_YEAST
ID VATL1_YEAST Reviewed; 160 AA.
AC P25515; D3DLM1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=V-type proton ATPase subunit c {ECO:0000303|PubMed:1825730};
DE Short=V-ATPase subunit c;
DE AltName: Full=Guanine nucleotide exchange factor 2;
DE AltName: Full=V-ATPase 16 kDa proteolipid subunit 1;
DE AltName: Full=Vacuolar proton pump c subunit;
GN Name=VMA3; Synonyms=CLS7, CUP5, GEF2; OrderedLocusNames=YEL027W;
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].
RX PubMed=2540044; DOI=10.1016/0014-5793(89)81259-1;
RA Nelson H., Nelson N.;
RT "The progenitor of ATP synthases was closely related to the current
RT vacuolar H+-ATPase.";
RL FEBS Lett. 247:147-153(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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, AND MUTAGENESIS OF GLU-137.
RX PubMed=1825730; DOI=10.1073/pnas.88.5.1938;
RA Moumi T., Beltran C., Nelson H., Nelson N.;
RT "Mutational analysis of yeast vacuolar H(+)-ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1938-1942(1991).
RN [6]
RP SUBCELLULAR LOCATION.
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 [7]
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 [8]
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 [9] {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 [10] {ECO:0007744|PDB:5TJ5}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 9-158, AND
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 [11] {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:1825730). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments (PubMed:1825730). {ECO:0000269|PubMed:1825730}.
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:25971514, PubMed:27776355, PubMed:29526695). The
CC decameric c-ring forms the proton-conducting pore, and is composed of
CC eight proteolipid subunits c, one subunit c' and one subunit c''
CC (PubMed:25971514, PubMed:27776355, PubMed:29526695).
CC {ECO:0000269|PubMed:25971514, 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 -!- MISCELLANEOUS: Present with 8450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; X15155; CAA33249.1; -; mRNA.
DR EMBL; U18530; AAB64504.1; -; Genomic_DNA.
DR EMBL; AY558342; AAS56668.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07625.1; -; Genomic_DNA.
DR PIR; S22257; PXBYL6.
DR RefSeq; NP_010887.3; NM_001178842.3.
DR PDB; 3J9T; EM; 6.90 A; R/S/T/U/V/W/X/Y/Z/a=1-160.
DR PDB; 3J9U; EM; 7.60 A; R/S/T/U/V/W/X/Y/Z/a=1-160.
DR PDB; 3J9V; EM; 8.30 A; R/S/T/U/V/W/X/Y/Z/a=1-160.
DR PDB; 5TJ5; EM; 3.90 A; E/F/G/H/I/J/M/N=9-158.
DR PDB; 5VOX; EM; 6.80 A; T/U/V/W/X/Y/Z/a=1-160.
DR PDB; 5VOY; EM; 7.90 A; T/U/V/W/X/Y/Z/a=1-160.
DR PDB; 5VOZ; EM; 7.60 A; T/U/V/W/X/Y/Z/a=1-160.
DR PDB; 6C6L; EM; 3.50 A; E/F/G/H/I/J/K/L=1-160.
DR PDB; 6M0R; EM; 2.70 A; E/F/G/H/I/J/K/L=1-159.
DR PDB; 6M0S; EM; 3.60 A; E/F/G/H/I/J/K/L=1-159.
DR PDB; 6O7T; EM; 3.20 A; g/h/i/j/k/l/m/n=1-160.
DR PDB; 6O7U; EM; 3.10 A; g/h/i/j/k/l/m/n=1-160.
DR PDB; 6O7V; EM; 6.60 A; g/h/i/j/k/l/m/n=1-160.
DR PDB; 6O7W; EM; 7.00 A; g/h/i/j/k/l/m/n=1-160.
DR PDB; 6O7X; EM; 8.70 A; g/h/i/j/k/l/m/n=1-160.
DR PDB; 6PE4; EM; 3.10 A; I/J/K/L/M/N/O/P=1-160.
DR PDB; 6PE5; EM; 3.20 A; I/J/K/L/M/N/O/P=1-160.
DR PDB; 7FDA; EM; 4.20 A; V/W/X/Y/Z/a/b/c=1-160.
DR PDB; 7FDB; EM; 4.80 A; V/W/X/Y/Z/a/b/c=1-160.
DR PDB; 7FDC; EM; 6.60 A; V/W/X/Y/Z/a/b/c=1-160.
DR PDB; 7TAO; EM; 3.20 A; E/F/G/H/I/J/K/L=1-160.
DR PDB; 7TAP; EM; 2.80 A; E/F/G/H/I/J/K/L=1-160.
DR PDB; 7TMR; EM; 3.50 A; g/h/i/j/k/l/m/n=1-160.
DR PDB; 7TMS; EM; 3.80 A; g/h/i/j/k/l/m/n=1-160.
DR PDBsum; 3J9T; -.
DR PDBsum; 3J9U; -.
DR PDBsum; 3J9V; -.
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; P25515; -.
DR SMR; P25515; -.
DR BioGRID; 36702; 392.
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-8123N; -.
DR IntAct; P25515; 12.
DR MINT; P25515; -.
DR STRING; 4932.YEL027W; -.
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; P25515; -.
DR PaxDb; P25515; -.
DR PRIDE; P25515; -.
DR TopDownProteomics; P25515; -.
DR EnsemblFungi; YEL027W_mRNA; YEL027W; YEL027W.
DR GeneID; 856686; -.
DR KEGG; sce:YEL027W; -.
DR SGD; S000000753; VMA3.
DR VEuPathDB; FungiDB:YEL027W; -.
DR eggNOG; KOG0232; Eukaryota.
DR GeneTree; ENSGT00550000074873; -.
DR HOGENOM; CLU_085752_1_2_1; -.
DR InParanoid; P25515; -.
DR OMA; NFIQLGA; -.
DR BioCyc; YEAST:G3O-30150-MON; -.
DR Reactome; R-SCE-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
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:P25515; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P25515; 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; IPI:ComplexPortal.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:UniProtKB.
DR GO; GO:0015078; F:proton transmembrane transporter activity; TAS:SGD.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IC:UniProtKB.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0048388; P:endosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC:ComplexPortal.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR GO; GO:0007033; P:vacuole organization; 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; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
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..160
FT /note="V-type proton ATPase subunit c"
FT /id="PRO_0000071762"
FT TOPO_DOM 1..8
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..90
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..160
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT SITE 137
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000269|PubMed:1825730"
FT MUTAGEN 137
FT /note="E->D: Partial inactivation."
FT /evidence="ECO:0000269|PubMed:1825730"
FT MUTAGEN 137
FT /note="E->Q,V,K: Inactivation."
FT /evidence="ECO:0000269|PubMed:1825730"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 10..43
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6C6L"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 55..75
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 84..119
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 129..153
FT /evidence="ECO:0007829|PDB:6M0R"
SQ SEQUENCE 160 AA; 16351 MW; FB8A142FFA1FA964 CRC64;
MTELCPVYAP FFGAIGCASA IIFTSLGAAY GTAKSGVGIC ATCVLRPDLL FKNIVPVIMA
GIIAIYGLVV SVLVCYSLGQ KQALYTGFIQ LGAGLSVGLS GLAAGFAIGI VGDAGVRGSS
QQPRLFVGMI LILIFAEVLG LYGLIVALLL NSRATQDVVC
