VATC_YEAST
ID VATC_YEAST Reviewed; 392 AA.
AC P31412; D6VXK7;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=V-type proton ATPase subunit C {ECO:0000303|PubMed:1730668};
DE Short=V-ATPase subunit C;
DE AltName: Full=V-ATPase 42 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit C;
GN Name=VMA5 {ECO:0000303|PubMed:8416931}; Synonyms=VAT3, VATC;
GN OrderedLocusNames=YKL080W; ORFNames=YKL410;
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], PROTEIN SEQUENCE OF 99-117, AND
RP FUNCTION.
RX PubMed=1730668; DOI=10.1016/s0021-9258(18)48351-2;
RA Beltran C., Kopecky J., Pan Y.-C.E., Nelson H., Nelson N.;
RT "Cloning and mutational analysis of the gene encoding subunit C of yeast
RT vacuolar H(+)-ATPase.";
RL J. Biol. Chem. 267:774-779(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 99-111; 147-156;
RP 242-251 AND 311-318, AND FUNCTION.
RX PubMed=8416931; DOI=10.1016/s0021-9258(18)54138-7;
RA Ho M.N., Hill K.J., Lindorfer M.A., Stevens T.H.;
RT "Isolation of vacuolar membrane H(+)-ATPase-deficient yeast mutants; the
RT VMA5 and VMA4 genes are essential for assembly and activity of the vacuolar
RT H(+)-ATPase.";
RL J. Biol. Chem. 268:221-227(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8203165; DOI=10.1002/yea.320100211;
RA James C.M., Gent M.E., Indge K.J., Oliver S.G.;
RT "Sequence analysis of a 10 kb fragment of yeast chromosome XI identifies
RT the SMY1 locus and reveals sequences related to a pre-mRNA splicing factor
RT and vacuolar ATPase subunit C plus a number of unidentified open reading
RT frames.";
RL Yeast 10:247-255(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 PROTEIN SEQUENCE OF 2-70; 82-98; 126-146; 157-164; 209-215; 242-251;
RP 259-285; 319-328 AND 342-358, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 106-115 AND 358-365, NUCLEOTIDE-BINDING, AND FUNCTION.
RX PubMed=15792803; DOI=10.1016/j.febslet.2005.02.042;
RA Armbruester A., Hohn C., Hermesdorf A., Schumacher K., Boersch M.,
RA Grueber G.;
RT "Evidence for major structural changes in subunit C of the vacuolar ATPase
RT due to nucleotide binding.";
RL FEBS Lett. 579:1961-1967(2005).
RN [8]
RP FUNCTION.
RX PubMed=10781598; DOI=10.1074/jbc.m002305200;
RA Parra K.J., Keenan K.L., Kane P.M.;
RT "The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity
RT of cytosolic V1 complexes.";
RL J. Biol. Chem. 275:21761-21767(2000).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF PHE-255.
RX PubMed=11777935; DOI=10.1074/jbc.m111708200;
RA Curtis K.K., Francis S.A., Oluwatosin Y., Kane P.M.;
RT "Mutational analysis of the subunit C (Vma5p) of the yeast vacuolar H+-
RT ATPase.";
RL J. Biol. Chem. 277:8979-8988(2002).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
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 [12]
RP INTERACTION WITH VMA4.
RX PubMed=15751969; DOI=10.1021/bi048402x;
RA Jones R.P.O., Durose L.J., Findlay J.B.C., Harrison M.A.;
RT "Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G
RT (Vma10p) within the stator structure of the vacuolar H(+)-ATPase.";
RL Biochemistry 44:3933-3941(2005).
RN [13]
RP ERRATUM OF PUBMED:15751969.
RX DOI=10.1021/bi058022r;
RA Jones R.P.O., Durose L.J., Findlay J.B.C., Harrison M.A.;
RL Biochemistry 44:11924-11924(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RX PubMed=15540116; DOI=10.1038/sj.embor.7400294;
RA Drory O., Frolow F., Nelson N.;
RT "Crystal structure of yeast V-ATPase subunit C reveals its stator
RT function.";
RL EMBO Rep. 5:1148-1152(2004).
RN [16] {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).
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:10781598, PubMed:11777935, PubMed:1730668,
CC PubMed:8416931). V-ATPase is responsible for acidifying and maintaining
CC the pH of intracellular compartments (PubMed:8416931). Subunit C is
CC necessary for the assembly of the catalytic sector of the enzyme and is
CC likely to have a specific function in its catalytic activity
CC (PubMed:15792803). Reversibly leaves the enzyme after glucose
CC depletion, causing the catalytic subcomplex V1 to detach from the V0
CC section (PubMed:15792803). {ECO:0000269|PubMed:10781598,
CC ECO:0000269|PubMed:11777935, ECO:0000269|PubMed:15792803,
CC ECO:0000269|PubMed:1730668, ECO:0000269|PubMed:8416931}.
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). Interacts directly with VMA4
CC (PubMed:15751969). {ECO:0000269|PubMed:15751969,
CC ECO:0000269|PubMed:25971514}.
CC -!- INTERACTION:
CC P31412; P32366: VMA6; NbExp=4; IntAct=EBI-20260, EBI-20201;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Peripheral membrane protein {ECO:0000269|PubMed:14562095}; Cytoplasmic
CC side {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 21114 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34440.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M77143; AAA34440.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X75560; CAA53237.1; -; Genomic_DNA.
DR EMBL; Z28080; CAA81917.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09077.1; -; Genomic_DNA.
DR PIR; S37905; S37905.
DR RefSeq; NP_012843.1; NM_001179646.1.
DR PDB; 1U7L; X-ray; 1.75 A; A=1-392.
DR PDB; 3J9T; EM; 6.90 A; O=1-392.
DR PDB; 3J9U; EM; 7.60 A; O=1-392.
DR PDB; 3J9V; EM; 8.30 A; O=1-392.
DR PDB; 4DL0; X-ray; 2.90 A; C/I=158-277.
DR PDB; 4EFA; X-ray; 2.82 A; C=158-277.
DR PDB; 5VOX; EM; 6.80 A; O=1-392.
DR PDB; 5VOY; EM; 7.90 A; O=1-392.
DR PDB; 5VOZ; EM; 7.60 A; O=1-392.
DR PDB; 6O7V; EM; 6.60 A; O=1-392.
DR PDB; 6O7W; EM; 7.00 A; O=1-392.
DR PDB; 6O7X; EM; 8.70 A; O=1-392.
DR PDB; 7FDA; EM; 4.20 A; O=1-392.
DR PDB; 7FDB; EM; 4.80 A; O=1-392.
DR PDB; 7FDC; EM; 6.60 A; O=1-392.
DR PDB; 7FDE; EM; 3.80 A; O=1-392.
DR PDBsum; 1U7L; -.
DR PDBsum; 3J9T; -.
DR PDBsum; 3J9U; -.
DR PDBsum; 3J9V; -.
DR PDBsum; 4DL0; -.
DR PDBsum; 4EFA; -.
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; P31412; -.
DR SMR; P31412; -.
DR BioGRID; 34052; 179.
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-4701N; -.
DR IntAct; P31412; 20.
DR MINT; P31412; -.
DR STRING; 4932.YKL080W; -.
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; P31412; -.
DR MaxQB; P31412; -.
DR PaxDb; P31412; -.
DR PRIDE; P31412; -.
DR EnsemblFungi; YKL080W_mRNA; YKL080W; YKL080W.
DR GeneID; 853782; -.
DR KEGG; sce:YKL080W; -.
DR SGD; S000001563; VMA5.
DR VEuPathDB; FungiDB:YKL080W; -.
DR eggNOG; KOG2909; Eukaryota.
DR GeneTree; ENSGT00390000004263; -.
DR HOGENOM; CLU_017554_3_0_1; -.
DR InParanoid; P31412; -.
DR OMA; GEYWLIS; -.
DR BioCyc; YEAST:G3O-31875-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 EvolutionaryTrace; P31412; -.
DR PRO; PR:P31412; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P31412; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
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 CDD; cd14785; V-ATPase_C; 1.
DR InterPro; IPR004907; ATPase_V1-cplx_csu.
DR InterPro; IPR036132; Vac_ATP_synth_c_sf.
DR PANTHER; PTHR10137; PTHR10137; 1.
DR Pfam; PF03223; V-ATPase_C; 1.
DR SUPFAM; SSF118203; SSF118203; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Reference proteome; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..392
FT /note="V-type proton ATPase subunit C"
FT /id="PRO_0000209358"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 255
FT /note="F->A: Is rapidly degraded and disrupts stable ATPase
FT assembly."
FT /evidence="ECO:0000269|PubMed:11777935"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1U7L"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 61..88
FT /evidence="ECO:0007829|PDB:1U7L"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:1U7L"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 127..165
FT /evidence="ECO:0007829|PDB:1U7L"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1U7L"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1U7L"
FT STRAND 189..199
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1U7L"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:4DL0"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1U7L"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:1U7L"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 264..319
FT /evidence="ECO:0007829|PDB:1U7L"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:1U7L"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:1U7L"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:1U7L"
SQ SEQUENCE 392 AA; 44189 MW; 0CD1B814046C377E CRC64;
MATALYTAND FILISLPQNA QPVTAPGSKT DSWFNETLIG GRAFVSDFKI PEFKIGSLDT
LIVESEELSK VDNQIGASIG KIIEILQGLN ETSTNAYRTL PINNMPVPEY LENFQWQTRK
FKLDKSIKDL ITLISNESSQ LDADVRATYA NYNSAKTNLA AAERKKTGDL SVRSLHDIVK
PEDFVLNSEH LTTVLVAVPK SLKSDFEKSY ETLSKNVVPA SASVIAEDAE YVLFNVHLFK
KNVQEFTTAA REKKFIPREF NYSEELIDQL KKEHDSAASL EQSLRVQLVR LAKTAYVDVF
INWFHIKALR VYVESVLRYG LPPHFNIKII AVPPKNLSKC KSELIDAFGF LGGNAFMKDK
KGKINKQDTS LHQYASLVDT EYEPFVMYII NL
