VATA_YEAST
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 03-AUG-2022, entry version 252.
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";
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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 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 AlphaFoldDB; P17255; -.
DR SMR; P17255; -.
DR BioGRID; 31859; 524.
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 UCD-2DPAGE; P17255; -.
DR MaxQB; P17255; -.
DR PaxDb; P17255; -.
DR PRIDE; P17255; -.
DR EnsemblFungi; YDL185W_mRNA; YDL185W; YDL185W.
DR GeneID; 851342; -.
DR KEGG; sce:YDL185W; -.
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 BioCyc; YEAST:G3O-29571-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; P17255; -.
DR PRO; PR:P17255; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P17255; protein.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:UniProtKB.
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: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; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC: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 Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.10.28.10; -; 2.
DR Gene3D; 3.40.50.300; -; 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; PTHR43607; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
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; SSF50615; SSF50615; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF55608; SSF55608; 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.
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 X10SSS VDE."
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 X10SSS VDE."
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 X10SSS VDE."
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 X10SSS VDE."
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 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"
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
