ID ADY2_YEAST Reviewed; 283 AA. AC P25613; D6VR19; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 27-MAR-2024, entry version 154. DE RecName: Full=Accumulation of dyads protein 2; DE AltName: Full=Ammonia transport outward protein 1; GN Name=ADY2; Synonyms=ATO1; OrderedLocusNames=YCR010C; ORFNames=YCR10C; 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]. RX PubMed=1626432; DOI=10.1002/yea.320080508; RA Skala J., Purnelle B., Goffeau A.; RT "The complete sequence of a 10.8 kb segment distal of SUF2 on the right arm RT of chromosome III from Saccharomyces cerevisiae reveals seven open reading RT frames including the RVS161, ADP1 and PGK genes."; RL Yeast 8:409-417(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=1574125; DOI=10.1038/357038a0; RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C., RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., RA Richterich P., Roberts A.B., Rodriguez F., Sanz E., RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., RA Sgouros J.G.; RT "The complete DNA sequence of yeast chromosome III."; RL Nature 357:38-46(1992). 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 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 [5] RP FUNCTION. RX PubMed=11470404; DOI=10.1016/s0960-9822(01)00274-3; RA Rabitsch K.P., Toth A., Galova M., Schleiffer A., Schaffner G., Aigner E., RA Rupp C., Penkner A.M., Moreno-Borchart A.C., Primig M., Esposito R.E., RA Klein F., Knop M., Nasmyth K.; RT "A screen for genes required for meiosis and spore formation based on RT whole-genome expression."; RL Curr. Biol. 11:1001-1009(2001). RN [6] RP FUNCTION. RX PubMed=12429834; DOI=10.1091/mbc.e01-12-0149; RA Palkova Z., Devaux F., Icicova M., Minarikova L., Le Crom S., Jacq C.; RT "Ammonia pulses and metabolic oscillations guide yeast colony RT development."; RL Mol. Biol. Cell 13:3901-3914(2002). RN [7] RP FUNCTION. RX PubMed=14968426; DOI=10.1002/yea.1056; RA Paiva S., Devaux F., Barbosa S., Jacq C., Casal M.; RT "Ady2p is essential for the acetate permease activity in the yeast RT Saccharomyces cerevisiae."; RL Yeast 21:201-210(2004). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=16286509; DOI=10.1083/jcb.200507168; RA Taxis C., Keller P., Kavagiou Z., Jensen L.J., Colombelli J., Bork P., RA Stelzer E.H.K., Knop M.; RT "Spore number control and breeding in Saccharomyces cerevisiae: a key role RT for a self-organizing system."; RL J. Cell Biol. 171:627-640(2005). RN [9] RP SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=17395151; DOI=10.1016/j.bbamem.2007.02.011; RA Ricicova M., Kucerova H., Vachova L., Palkova Z.; RT "Association of putative ammonium exporters Ato with detergent-resistant RT compartments of plasma membrane during yeast colony development: pH affects RT Ato1p localisation in patches."; RL Biochim. Biophys. Acta 1768:1170-1178(2007). RN [10] RP FUNCTION. RX PubMed=17233767; DOI=10.1111/j.1567-1364.2006.00191.x; RA Gentsch M., Kuschel M., Schlegel S., Barth G.; RT "Mutations at different sites in members of the Gpr1/Fun34/YaaH protein RT family cause hypersensitivity to acetic acid in Saccharomyces cerevisiae as RT well as in Yarrowia lipolytica."; RL FEMS Yeast Res. 7:380-390(2007). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200; RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; RT "Profiling phosphoproteins of yeast mitochondria reveals a role of RT phosphorylation in assembly of the ATP synthase."; RL Mol. Cell. Proteomics 6:1896-1906(2007). CC -!- FUNCTION: Transporter protein required for ammonia export and acetate CC uptake and resistance. Necessary for up-regulation and down-regulation CC of meiotic plaque (MP) component levels in a dependency on external CC acetate. Has a role in ascus formation. {ECO:0000269|PubMed:11470404, CC ECO:0000269|PubMed:12429834, ECO:0000269|PubMed:14968426, CC ECO:0000269|PubMed:16286509, ECO:0000269|PubMed:17233767}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16286509, CC ECO:0000269|PubMed:17395151}; Multi-pass membrane protein CC {ECO:0000269|PubMed:16286509, ECO:0000269|PubMed:17395151}. Vacuole CC membrane {ECO:0000269|PubMed:16286509}; Multi-pass membrane protein CC {ECO:0000269|PubMed:16286509}. Note=Localizes to large detergent CC resistant patches of the cell membrane (DRM) enriched in ergosterol and CC sphingolipids (PubMed:17395151). CC -!- INDUCTION: During meiosis and by external ammonia. CC {ECO:0000269|PubMed:16286509, ECO:0000269|PubMed:17395151}. CC -!- SIMILARITY: Belongs to the acetate uptake transporter (AceTr) CC (TC 2.A.96) family. {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; X59720; CAA42327.1; -; Genomic_DNA. DR EMBL; BK006937; DAA07488.1; -; Genomic_DNA. DR PIR; S19420; S19420. DR RefSeq; NP_009936.1; NM_001178723.1. DR AlphaFoldDB; P25613; -. DR SMR; P25613; -. DR BioGRID; 30989; 84. DR DIP; DIP-7894N; -. DR IntAct; P25613; 4. DR MINT; P25613; -. DR STRING; 4932.YCR010C; -. DR TCDB; 2.A.96.1.4; the acetate uptake transporter (acetr) family. DR CarbonylDB; P25613; -. DR iPTMnet; P25613; -. DR PaxDb; 4932-YCR010C; -. DR PeptideAtlas; P25613; -. DR EnsemblFungi; YCR010C_mRNA; YCR010C; YCR010C. DR GeneID; 850368; -. DR KEGG; sce:YCR010C; -. DR AGR; SGD:S000000603; -. DR SGD; S000000603; ADY2. DR VEuPathDB; FungiDB:YCR010C; -. DR eggNOG; ENOG502QUJS; Eukaryota. DR GeneTree; ENSGT00940000176398; -. DR HOGENOM; CLU_051062_0_0_1; -. DR InParanoid; P25613; -. DR OMA; WKKGNTF; -. DR OrthoDB; 2033997at2759; -. DR BioCyc; YEAST:G3O-29327-MONOMER; -. DR BioGRID-ORCS; 850368; 10 hits in 10 CRISPR screens. DR PRO; PR:P25613; -. DR Proteomes; UP000002311; Chromosome III. DR RNAct; P25613; Protein. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005886; C:plasma membrane; IDA:SGD. DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015123; F:acetate transmembrane transporter activity; IMP:SGD. DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IMP:SGD. DR GO; GO:0006846; P:acetate transport; IMP:SGD. DR GO; GO:0072488; P:ammonium transmembrane transport; IMP:SGD. DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW. DR GO; GO:0019740; P:nitrogen utilization; IMP:SGD. DR GO; GO:0055085; P:transmembrane transport; IMP:SGD. DR InterPro; IPR000791; Gpr1/Fun34/SatP-like. DR InterPro; IPR047622; GPR1_FUN34_YAAH. DR NCBIfam; NF038013; AceTr_1; 1. DR PANTHER; PTHR31123; ACCUMULATION OF DYADS PROTEIN 2-RELATED; 1. DR PANTHER; PTHR31123:SF1; ACCUMULATION OF DYADS PROTEIN 2-RELATED; 1. DR Pfam; PF01184; Gpr1_Fun34_YaaH; 1. DR PROSITE; PS01114; GPR1_FUN34_YAAH; 1. PE 1: Evidence at protein level; KW Ammonia transport; Cell membrane; Ion transport; Meiosis; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole. FT CHAIN 1..283 FT /note="Accumulation of dyads protein 2" FT /id="PRO_0000135706" FT TOPO_DOM 1..89 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 90..110 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 111..120 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 121..141 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 142..151 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 152..172 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 173..185 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 186..206 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 207..208 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 209..229 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 230..240 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 241..261 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 262..283 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 1..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 283 AA; 30726 MW; 36DE421B09D8BB40 CRC64; MSDKEQTSGN TDLENAPAGY YSSHDNDVNG VAEDERPSHD SLGKIYTGGD NNEYIYIGRQ KFLKSDLYQA FGGTLNPGLA PAPVHKFANP APLGLSAFAL TTFVLSMFNA RAQGITVPNV VVGCAMFYGG LVQLIAGIWE IALENTFGGT ALCSYGGFWL SFAAIYIPWF GILEAYEDNE SDLNNALGFY LLGWAIFTFG LTVCTMKSTV MFFLLFFLLA LTFLLLSIGH FANRLGVTRA GGVLGVVVAF IAWYNAYAGV ATKQNSYVLA RPFPLPSTER VIF //