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 27-MAR-2024, entry version 200. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7TMM; EM; 3.50 A; O=1-392. DR PDB; 7TMR; EM; 3.50 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 PDBsum; 7TMM; -. DR PDBsum; 7TMR; -. DR AlphaFoldDB; P31412; -. DR EMDB; EMD-31541; -. DR SMR; P31412; -. DR BioGRID; 34052; 191. 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; 4932-YKL080W; -. DR PeptideAtlas; P31412; -. DR EnsemblFungi; YKL080W_mRNA; YKL080W; YKL080W. DR GeneID; 853782; -. DR KEGG; sce:YKL080W; -. DR AGR; SGD:S000001563; -. 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; VMIWIHV; -. DR OrthoDB; 166742at2759; -. DR BioCyc; YEAST:G3O-31875-MONOMER; -. 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 BioGRID-ORCS; 853782; 8 hits in 10 CRISPR screens. DR EvolutionaryTrace; P31412; -. DR PRO; PR:P31412; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P31412; Protein. DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD. DR GO; GO:0000139; C:Golgi membrane; NAS: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; NAS:ComplexPortal. DR GO; GO:0061795; P:Golgi lumen acidification; NAS: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 Gene3D; 3.30.70.100; -; 1. DR Gene3D; 1.20.1460.10; subunit c (vma5p) of the yeast v-atpase, domain 2; 1. DR InterPro; IPR004907; ATPase_V1-cplx_csu. DR InterPro; IPR036132; Vac_ATP_synth_c_sf. DR PANTHER; PTHR10137; V-TYPE PROTON ATPASE SUBUNIT C; 1. DR PANTHER; PTHR10137:SF0; V-TYPE PROTON ATPASE SUBUNIT C; 1. DR Pfam; PF03223; V-ATPase_C; 1. DR SUPFAM; SSF118203; Vacuolar ATP synthase subunit C; 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 STRAND 23..25 FT /evidence="ECO:0007829|PDB:7TMM" 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 HELIX 90..93 FT /evidence="ECO:0007829|PDB:7TMM" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:1U7L" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:7TMM" 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 HELIX 219..221 FT /evidence="ECO:0007829|PDB:7TMM" 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 334..336 FT /evidence="ECO:0007829|PDB:7TMM" 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 //