ID VATA_YEAST Reviewed; 1071 AA. AC P17255; D6VRG7; O74301; Q9Y7W5; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 261. DE RecName: Full=V-type proton ATPase catalytic subunit A {ECO:0000303|PubMed:2139027}; DE Short=V-ATPase subunit A; DE EC=7.1.2.2 {ECO:0000305|PubMed:18055462, ECO:0000305|PubMed:2139027}; DE AltName: Full=Vacuolar proton pump subunit A; DE Contains: DE RecName: Full=Endonuclease PI-SceI; DE EC=3.1.-.-; DE AltName: Full=Sce VMA intein; DE AltName: Full=VMA1-derived endonuclease; DE Short=VDE; GN Name=VMA1 {ECO:0000303|PubMed:2139027}; Synonyms=CLS8, TFP1; GN OrderedLocusNames=YDL185W; ORFNames=D1286; 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 181-196; 815-820; RP 826-836; 862-879; 925-936 AND 1004-1013, FUNCTION, CATALYTIC ACTIVITY, AND RP SUBCELLULAR LOCATION. RC STRAIN=ATCC 26786 / X2180-1A; RX PubMed=2139027; DOI=10.1016/s0021-9258(19)39210-5; RA Hirata R., Ohsumi Y., Nakano A., Kawasaki H., Suzuki K., Anraku Y.; RT "Molecular structure of a gene, VMA1, encoding the catalytic subunit of RT H(+)-translocating adenosine triphosphatase from vacuolar membranes of RT Saccharomyces cerevisiae."; RL J. Biol. Chem. 265:6726-6733(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8533471; DOI=10.1002/yea.320111007; RA Verhasselt P., Voet M., Volckaert G.; RT "New open reading frames, one of which is similar to the nifV gene of RT Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of RT Saccharomyces cerevisiae."; RL Yeast 11:961-966(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34. RC STRAIN=ATCC 208353 / W303-1A; RX PubMed=1656215; DOI=10.1128/mcb.11.10.4876-4884.1991; RA Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.; RT "Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth RT and bud morphogenesis."; RL Mol. Cell. Biol. 11:4876-4884(1991). RN [6] RP PROTEIN SEQUENCE OF 2-10; 52-63; 115-136; 173-178; 181-207; 220-239; RP 264-272; 770-784; 804-814; 826-842; 853-861; 918-937; 940-959; 1004-1014 RP AND 1058-1065, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RA Bienvenut W.V., Peters C.; RL Submitted (OCT-2005) to UniProtKB. RN [7] RP PROTEIN SEQUENCE OF 2-6, CLEAVAGE OF INITIATOR METHIONINE, MUTAGENESIS OF RP CYS-284; HIS-362; ASN-737 AND CYS-738, AND X-RAY CRYSTALLOGRAPHY (2.1 RP ANGSTROMS) OF 274-747. RX PubMed=11884132; DOI=10.1006/jmbi.2001.5357; RA Mizutani R., Nogami S., Kawasaki M., Ohya Y., Anraku Y., Satow Y.; RT "Protein-splicing reaction via a thiazolidine intermediate: crystal RT structure of the VMA1-derived endonuclease bearing the N and C-terminal RT propeptides."; RL J. Mol. Biol. 316:919-929(2002). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-1071. RX PubMed=2905423; DOI=10.1128/mcb.8.8.3094-3103.1988; RA Shih C.K., Wagner R., Feinstein S., Kanik-Ennulat C., Neff N.; RT "A dominant trifluoperazine resistance gene from Saccharomyces cerevisiae RT has homology with F0F1 ATP synthase and confers calcium-sensitive growth."; RL Mol. Cell. Biol. 8:3094-3103(1988). RN [9] RP PROTEIN SPLICING. RX PubMed=2146742; DOI=10.1126/science.2146742; RA Kane P.M., Yamashiro C.T., Wolczyk D.F., Neff N., Goebl M., Stevens T.H.; RT "Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit RT of the vacuolar H(+)-adenosine triphosphatase."; RL Science 250:651-657(1990). RN [10] RP MUTAGENESIS OF CYS-284 AND CYS-738. RX PubMed=1417861; DOI=10.1016/0006-291x(92)92347-z; RA Hirata R., Anraku Y.; RT "Mutations at the putative junction sites of the yeast VMA1 protein, the RT catalytic subunit of the vacuolar membrane H(+)-ATPase, inhibit its RT processing by protein splicing."; RL Biochem. Biophys. Res. Commun. 188:40-47(1992). RN [11] RP SELF-SPLICING MECHANISM. RX PubMed=8508780; DOI=10.1002/j.1460-2075.1993.tb05913.x; RA Cooper A.A., Chen Y.-J., Lindorfer M.A., Stevens T.H.; RT "Protein splicing of the yeast TFP1 intervening protein sequence: a model RT for self-excision."; RL EMBO J. 12:2575-2583(1993). RN [12] RP FUNCTION OF VDE. RX PubMed=1534148; DOI=10.1038/357301a0; RA Gimble F.S., Thorner J.; RT "Homing of a DNA endonuclease gene by meiotic gene conversion in RT Saccharomyces cerevisiae."; RL Nature 357:301-306(1992). RN [13] RP INTERACTION WITH RAV1 AND RAV2. RX PubMed=11283612; DOI=10.1038/35070067; RA Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.; RT "Skp1 forms multiple protein complexes, including RAVE, a regulator of V- RT ATPase assembly."; RL Nat. Cell Biol. 3:384-391(2001). RN [14] 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 [15] 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 [16] RP REVIEW. RX PubMed=15335920; DOI=10.1016/0960-9822(92)90336-9; RA Grivell L.A.; RT "Homing in on an endosymbiotic endonuclease."; RL Curr. Biol. 2:450-452(1992). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE V-ATPASE COMPLEX, MASS RP SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE. RX PubMed=18055462; DOI=10.1074/jbc.m707924200; RA Kitagawa N., Mazon H., Heck A.J.R., Wilkens S.; RT "Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase RT determined by mass spectrometry."; RL J. Biol. Chem. 283:3329-3337(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131; SER-858 AND SER-928, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [19] 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 [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF PI-SCE I. RX PubMed=9160747; DOI=10.1016/s0092-8674(00)80237-8; RA Duan X., Gimble F.S., Quiocho F.A.; RT "Crystal structure of PI-SceI, a homing endonuclease with protein splicing RT activity."; RL Cell 89:555-564(1997). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PI-SCE I. RX PubMed=10644733; DOI=10.1074/jbc.275.4.2705; RA Hu D., Crist M., Duan X., Quiocho F.A., Gimble F.S.; RT "Probing the structure of the PI-SceI-DNA complex by affinity cleavage and RT affinity photocross-linking."; RL J. Biol. Chem. 275:2705-2712(2000). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 283-741, AND MUTAGENESIS OF RP CYS-284 AND ASN-737. RX PubMed=10828056; DOI=10.1074/jbc.275.22.16408; RA Poland B.W., Xu M.-Q., Quiocho F.A.; RT "Structural insights into the protein splicing mechanism of PI-SceI."; RL J. Biol. Chem. 275:16408-16413(2000). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 284-465. RX PubMed=12235380; DOI=10.1093/nar/gkf523; RA Werner E., Wende W., Pingoud A., Heinemann U.; RT "High resolution crystal structure of domain I of the Saccharomyces RT cerevisiae homing endonuclease PI-SceI."; RL Nucleic Acids Res. 30:3962-3971(2002). RN [25] {ECO:0007744|PDB:3J9T, ECO:0007744|PDB:3J9U, ECO:0007744|PDB:3J9V} RP STRUCTURE BY ELECTRON MICROSCOPY (6.90 ANGSTROMS) OF 2-1071, AND RP IDENTIFICATION IN 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 [26] {ECO:0007744|PDB:5BW9, ECO:0007744|PDB:5D80} RP X-RAY CRYSTALLOGRAPHY (6.20 ANGSTROMS), AND IDENTIFICATION IN THE V-ATPASE RP COMPLEX. RX PubMed=27295975; DOI=10.15252/embj.201593447; RA Oot R.A., Kane P.M., Berry E.A., Wilkens S.; RT "Crystal structure of yeast V1-ATPase in the autoinhibited state."; RL EMBO J. 35:1694-1706(2016). CC -!- FUNCTION: Catalytic subunit of the V1 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:2139027, PubMed:18055462). V-ATPase is CC responsible for acidifying and maintaining the pH of intracellular CC compartments (PubMed:2139027, PubMed:18055462). CC {ECO:0000269|PubMed:18055462, ECO:0000269|PubMed:2139027}. CC -!- FUNCTION: PI-SceI is an endonuclease that can cleave at a site present CC in a VMA1 allele that lacks the derived endonuclease segment of the CC open reading frame; cleavage at this site only occurs during meiosis CC and initiates 'homing', a genetic event that converts a VMA1 allele CC lacking VDE into one that contains it. {ECO:0000269|PubMed:1534148}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; CC Evidence={ECO:0000305|PubMed:18055462, ECO:0000305|PubMed:2139027}; 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:18055462, PubMed:27295975). Interacts CC with RAV1 and RAV2 components of the RAVE complex, which are essential CC for the stability and assembly of V-ATPase (PubMed:11283612). CC {ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:18055462, CC ECO:0000269|PubMed:25971514, ECO:0000269|PubMed:27295975}. CC -!- INTERACTION: CC P17255; P47104: RAV1; NbExp=2; IntAct=EBI-20245, EBI-25471; CC P17255; P32366: VMA6; NbExp=6; IntAct=EBI-20245, EBI-20201; CC -!- SUBCELLULAR LOCATION: Endomembrane system CC {ECO:0000269|PubMed:14562095}; Peripheral membrane protein CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Vacuole membrane CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:2139027}; Peripheral CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. CC Note=Membranes of various intracellular acidic compartments. CC {ECO:0000269|PubMed:14562095}. CC -!- PTM: This protein undergoes a protein self splicing that involves a CC post-translational excision of the VDE intervening region (intein) CC followed by peptide ligation. CC -!- MASS SPECTROMETRY: Mass=67642.1; Mass_error=28; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:18055462}; CC -!- MISCELLANEOUS: Present with 199895 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Description of Sce VMA in Inbase; CC URL="http://tools.neb.com/inbase/intein.php?name=Sce+VMA"; 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; J05409; AAA34664.1; -; Genomic_DNA. DR EMBL; X83276; CAA58261.1; -; Genomic_DNA. DR EMBL; Z74233; CAA98760.1; -; Genomic_DNA. DR EMBL; Z74233; CAA98761.1; ALT_SEQ; Genomic_DNA. DR EMBL; Z74233; CAA98762.1; -; Genomic_DNA. DR EMBL; X58857; CAA41657.1; -; Genomic_DNA. DR EMBL; M21609; AAB63978.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11677.1; -; Genomic_DNA. DR PIR; A35746; PXBYVA. DR RefSeq; NP_010096.1; NM_001180245.1. DR PDB; 1DFA; X-ray; 2.00 A; A=284-737. DR PDB; 1EF0; X-ray; 2.10 A; A/B=283-741. DR PDB; 1GPP; X-ray; 1.35 A; A=284-466, A=693-736. DR PDB; 1JVA; X-ray; 2.10 A; A/B=274-747. DR PDB; 1LWS; X-ray; 3.50 A; A=284-737. DR PDB; 1LWT; X-ray; 3.20 A; A=284-737. DR PDB; 1UM2; X-ray; 2.90 A; A/B=284-737, C/D=274-747. DR PDB; 1VDE; X-ray; 2.40 A; A/B=284-737. DR PDB; 3J9T; EM; 6.90 A; A/C/E=2-1071. DR PDB; 3J9U; EM; 7.60 A; A/C/E=2-1071. DR PDB; 3J9V; EM; 8.30 A; A/C/E=2-1071. DR PDB; 5BW9; X-ray; 7.00 A; A/B/C/a/b/c=1-1071. DR PDB; 5D80; X-ray; 6.20 A; A/B/C/a/b/c=1-1071. DR PDB; 5VOX; EM; 6.80 A; A/C/E=1-1071. DR PDB; 5VOY; EM; 7.90 A; A/C/E=1-1071. DR PDB; 5VOZ; EM; 7.60 A; A/C/E=1-1071. DR PDB; 7FDA; EM; 4.20 A; A/C/E=1-1071. DR PDB; 7FDB; EM; 4.80 A; A/C/E=1-1071. DR PDB; 7FDC; EM; 6.60 A; A/C/E=1-1071. DR PDB; 7FDE; EM; 3.80 A; A/C/E=1-1071. DR PDB; 7TMM; EM; 3.50 A; A/C/E=1-1071. DR PDB; 7TMO; EM; 3.30 A; A/C/E=1-1071. DR PDB; 7TMP; EM; 3.30 A; A/C/E=1-1071. DR PDB; 7TMQ; EM; 3.30 A; A/C/E=1-1071. DR PDB; 7TMR; EM; 3.50 A; A/C/E=1-1071. DR PDBsum; 1DFA; -. DR PDBsum; 1EF0; -. DR PDBsum; 1GPP; -. DR PDBsum; 1JVA; -. DR PDBsum; 1LWS; -. DR PDBsum; 1LWT; -. DR PDBsum; 1UM2; -. DR PDBsum; 1VDE; -. DR PDBsum; 3J9T; -. DR PDBsum; 3J9U; -. DR PDBsum; 3J9V; -. DR PDBsum; 5BW9; -. DR PDBsum; 5D80; -. DR PDBsum; 5VOX; -. DR PDBsum; 5VOY; -. DR PDBsum; 5VOZ; -. DR PDBsum; 7FDA; -. DR PDBsum; 7FDB; -. DR PDBsum; 7FDC; -. DR PDBsum; 7FDE; -. DR PDBsum; 7TMM; -. DR PDBsum; 7TMO; -. DR PDBsum; 7TMP; -. DR PDBsum; 7TMQ; -. DR PDBsum; 7TMR; -. DR AlphaFoldDB; P17255; -. DR EMDB; EMD-25996; -. DR EMDB; EMD-25997; -. DR EMDB; EMD-25998; -. DR EMDB; EMD-25999; -. DR EMDB; EMD-31538; -. DR EMDB; EMD-31539; -. DR EMDB; EMD-31540; -. DR EMDB; EMD-31541; -. DR EMDB; EMD-8724; -. DR EMDB; EMD-8725; -. DR EMDB; EMD-8726; -. DR SMR; P17255; -. DR BioGRID; 31859; 556. 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-2293N; -. DR IntAct; P17255; 103. DR MINT; P17255; -. DR STRING; 4932.YDL185W; -. DR MEROPS; N09.001; -. DR REBASE; 2615; PI-SceI. 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; P17255; -. DR MaxQB; P17255; -. DR PaxDb; 4932-YDL185W; -. DR PeptideAtlas; P17255; -. DR EnsemblFungi; YDL185W_mRNA; YDL185W; YDL185W. DR GeneID; 851342; -. DR KEGG; sce:YDL185W; -. DR AGR; SGD:S000002344; -. DR SGD; S000002344; VMA1. DR VEuPathDB; FungiDB:YDL185W; -. DR eggNOG; KOG1352; Eukaryota. DR GeneTree; ENSGT00550000074787; -. DR HOGENOM; CLU_008162_0_1_1; -. DR InParanoid; P17255; -. DR OMA; CFAKGTE; -. DR OrthoDB; 5473187at2759; -. DR BioCyc; YEAST:G3O-29571-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; 851342; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P17255; -. DR PRO; PR:P17255; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P17255; Protein. DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:UniProtKB. 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:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003729; F:mRNA binding; HDA:SGD. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IDA:SGD. DR GO; GO:0048388; P:endosomal lumen acidification; NAS:ComplexPortal. DR GO; GO:0061795; P:Golgi lumen acidification; NAS:ComplexPortal. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW. DR GO; GO:0019538; P:protein metabolic process; IDA:SGD. DR GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal. DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD. DR CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1. DR CDD; cd18119; ATP-synt_V_A-type_alpha_N; 1. DR CDD; cd00081; Hint; 1. DR CDD; cd01134; V_A-ATPase_A; 1. DR Gene3D; 2.40.30.20; -; 1. DR Gene3D; 2.40.50.100; -; 1. DR Gene3D; 3.10.28.10; Homing endonucleases; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR031686; ATP-synth_a_Xtn. DR InterPro; IPR023366; ATP_synth_asu-like_sf. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N. DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR024034; ATPase_F1/V1_b/a_C. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR036844; Hint_dom_sf. DR InterPro; IPR007868; Hom_end_hint. DR InterPro; IPR007869; Homing_endonuc_PI-Sce. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022878; V-ATPase_asu. DR PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1. DR PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1. DR Pfam; PF00006; ATP-synt_ab; 2. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR Pfam; PF16886; ATP-synt_ab_Xtn; 1. DR Pfam; PF05204; Hom_end; 2. DR Pfam; PF05203; Hom_end_hint; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1. DR SUPFAM; SSF55608; Homing endonucleases; 2. DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. DR UCD-2DPAGE; P17255; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Autocatalytic cleavage; KW Direct protein sequencing; DNA-binding; Endonuclease; KW Hydrogen ion transport; Hydrolase; Intron homing; Ion transport; Membrane; KW Nuclease; Nucleotide-binding; Phosphoprotein; Protein splicing; KW Reference proteome; Translocase; Transport; Vacuole. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:11884132, FT ECO:0000269|PubMed:18055462, ECO:0000269|Ref.6, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..283 FT /note="V-type proton ATPase catalytic subunit A, 1st part" FT /id="PRO_0000002458" FT CHAIN 284..737 FT /note="Endonuclease PI-SceI" FT /id="PRO_0000002459" FT CHAIN 738..1071 FT /note="V-type proton ATPase catalytic subunit A, 2nd part" FT /id="PRO_0000002460" FT DOMAIN 494..642 FT /note="DOD-type homing endonuclease" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273" FT BINDING 257..264 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P38606" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22814378" FT MOD_RES 131 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 858 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 928 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MUTAGEN 284 FT /note="C->S: Reduces splicing reaction speed. Inhibits FT splicing; when associated with N-362; S-737 and S-738 in FT X10SSSVDE." FT /evidence="ECO:0000269|PubMed:10828056, FT ECO:0000269|PubMed:11884132, ECO:0000269|PubMed:1417861" FT MUTAGEN 362 FT /note="H->N: Inhibits splicing; when associated with S-284; FT S-737 and S-738 in X10SSSVDE." FT /evidence="ECO:0000269|PubMed:11884132" FT MUTAGEN 737 FT /note="N->S: Inhibits splicing; when associated with S-284; FT N-362 and S-738 in X10SSSVDE." FT /evidence="ECO:0000269|PubMed:10828056, FT ECO:0000269|PubMed:11884132" FT MUTAGEN 738 FT /note="C->S: Reduces splicing reaction speed. Inhibits FT splicing; when associated with S-284; N-362 and S-737 in FT X10SSSVDE." FT /evidence="ECO:0000269|PubMed:11884132, FT ECO:0000269|PubMed:1417861" FT CONFLICT 875 FT /note="G -> D (in Ref. 8; AAB63978)" FT /evidence="ECO:0000305" FT STRAND 26..32 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:7TMO" FT TURN 53..56 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 57..63 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 69..75 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 85..92 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:7TMP" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 113..120 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:7TMQ" FT STRAND 140..144 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 158..162 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 181..186 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 206..210 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 214..220 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 239..243 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:7TMP" FT HELIX 263..273 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 277..282 FT /evidence="ECO:0007829|PDB:7TMR" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 290..293 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 298..300 FT /evidence="ECO:0007829|PDB:1GPP" FT HELIX 301..303 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 309..312 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 315..322 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 325..335 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:1EF0" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:1EF0" FT STRAND 355..359 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 363..369 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 372..379 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 382..396 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 398..400 FT /evidence="ECO:0007829|PDB:1VDE" FT STRAND 402..414 FT /evidence="ECO:0007829|PDB:1GPP" FT HELIX 415..417 FT /evidence="ECO:0007829|PDB:1GPP" FT HELIX 420..431 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 434..443 FT /evidence="ECO:0007829|PDB:1GPP" FT HELIX 444..449 FT /evidence="ECO:0007829|PDB:1GPP" FT HELIX 452..457 FT /evidence="ECO:0007829|PDB:1GPP" FT STRAND 459..462 FT /evidence="ECO:0007829|PDB:1GPP" FT TURN 471..474 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 479..481 FT /evidence="ECO:0007829|PDB:1VDE" FT STRAND 485..487 FT /evidence="ECO:0007829|PDB:1DFA" FT HELIX 488..501 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 506..514 FT /evidence="ECO:0007829|PDB:1EF0" FT HELIX 516..528 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 531..533 FT /evidence="ECO:0007829|PDB:1LWT" FT STRAND 534..537 FT /evidence="ECO:0007829|PDB:1EF0" FT STRAND 538..540 FT /evidence="ECO:0007829|PDB:1UM2" FT TURN 541..543 FT /evidence="ECO:0007829|PDB:1EF0" FT STRAND 544..548 FT /evidence="ECO:0007829|PDB:1EF0" FT TURN 556..559 FT /evidence="ECO:0007829|PDB:1LWT" FT HELIX 570..575 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 579..584 FT /evidence="ECO:0007829|PDB:1DFA" FT HELIX 588..591 FT /evidence="ECO:0007829|PDB:1DFA" FT HELIX 595..609 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 610..613 FT /evidence="ECO:0007829|PDB:1EF0" FT STRAND 619..625 FT /evidence="ECO:0007829|PDB:1DFA" FT HELIX 627..639 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 643..650 FT /evidence="ECO:0007829|PDB:1DFA" FT HELIX 654..656 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 657..659 FT /evidence="ECO:0007829|PDB:1EF0" FT STRAND 661..669 FT /evidence="ECO:0007829|PDB:1DFA" FT HELIX 672..678 FT /evidence="ECO:0007829|PDB:1DFA" FT TURN 684..686 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 692..694 FT /evidence="ECO:0007829|PDB:1LWT" FT STRAND 700..702 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 704..714 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 721..723 FT /evidence="ECO:0007829|PDB:1EF0" FT STRAND 725..729 FT /evidence="ECO:0007829|PDB:1DFA" FT STRAND 733..736 FT /evidence="ECO:0007829|PDB:1DFA" FT HELIX 742..751 FT /evidence="ECO:0007829|PDB:7TMO" FT TURN 752..754 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 755..757 FT /evidence="ECO:0007829|PDB:7TMP" FT HELIX 759..761 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 766..769 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 770..775 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 777..779 FT /evidence="ECO:0007829|PDB:7TMR" FT HELIX 783..800 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 804..810 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 812..826 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 832..834 FT /evidence="ECO:0007829|PDB:7TMM" FT HELIX 839..848 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 856..859 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 862..865 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 874..876 FT /evidence="ECO:0007829|PDB:7TMP" FT HELIX 881..889 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 891..893 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 898..901 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 902..904 FT /evidence="ECO:0007829|PDB:7TMO" FT TURN 911..913 FT /evidence="ECO:0007829|PDB:7TMO" FT TURN 917..922 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 923..929 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 933..957 FT /evidence="ECO:0007829|PDB:7TMO" FT STRAND 959..961 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 964..979 FT /evidence="ECO:0007829|PDB:7TMO" FT TURN 988..990 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 995..1018 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 1022..1028 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 1030..1037 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 1038..1041 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 1044..1046 FT /evidence="ECO:0007829|PDB:7TMO" FT HELIX 1048..1069 FT /evidence="ECO:0007829|PDB:7TMO" SQ SEQUENCE 1071 AA; 118637 MW; 2A4C65D2F59426FD CRC64; MAGAIENARK EIKRISLEDH AESEYGAIYS VSGPVVIAEN MIGCAMYELV KVGHDNLVGE VIRIDGDKAT IQVYEETAGL TVGDPVLRTG KPLSVELGPG LMETIYDGIQ RPLKAIKEES QSIYIPRGID TPALDRTIKW QFTPGKFQVG DHISGGDIYG SVFENSLISS HKILLPPRSR GTITWIAPAG EYTLDEKILE VEFDGKKSDF TLYHTWPVRV PRPVTEKLSA DYPLLTGQRV LDALFPCVQG GTTCIPGAFG CGKTVISQSL SKYSNSDAII YVGCFAKGTN VLMADGSIEC IENIEVGNKV MGKDGRPREV IKLPRGRETM YSVVQKSQHR AHKSDSSREV PELLKFTCNA THELVVRTPR SVRRLSRTIK GVEYFEVITF EMGQKKAPDG RIVELVKEVS KSYPISEGPE RANELVESYR KASNKAYFEW TIEARDLSLL GSHVRKATYQ TYAPILYEND HFFDYMQKSK FHLTIEGPKV LAYLLGLWIG DGLSDRATFS VDSRDTSLME RVTEYAEKLN LCAEYKDRKE PQVAKTVNLY SKVVRGNGIR NNLNTENPLW DAIVGLGFLK DGVKNIPSFL STDNIGTRET FLAGLIDSDG YVTDEHGIKA TIKTIHTSVR DGLVSLARSL GLVVSVNAEP AKVDMNGTKH KISYAIYMSG GDVLLNVLSK CAGSKKFRPA PAAAFARECR GFYFELQELK EDDYYGITLS DDSDHQFLLA NQVVVHNCGE RGNEMAEVLM EFPELYTEMS GTKEPIMKRT TLVANTSNMP VAAREASIYT GITLAEYFRD QGKNVSMIAD SSSRWAEALR EISGRLGEMP ADQGFPAYLG AKLASFYERA GKAVALGSPD RTGSVSIVAA VSPAGGDFSD PVTTATLGIT QVFWGLDKKL AQRKHFPSIN TSVSYSKYTN VLNKFYDSNY PEFPVLRDRM KEILSNAEEL EQVVQLVGKS ALSDSDKITL DVATLIKEDF LQQNGYSTYD AFCPIWKTFD MMRAFISYHD EAQKAVANGA NWSKLADSTG DVKHAVSSSK FFEPSRGEKE VHGEFEKLLS TMQERFAEST D //