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ADY2_YEAST
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   03-AUG-2022, entry version 148.
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) (TC
CC       2.A.96) family. {ECO:0000305}.
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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; 72.
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; P25613; -.
DR   PRIDE; P25613; -.
DR   EnsemblFungi; YCR010C_mRNA; YCR010C; YCR010C.
DR   GeneID; 850368; -.
DR   KEGG; sce:YCR010C; -.
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   BioCyc; YEAST:G3O-29327-MON; -.
DR   PRO; PR:P25613; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25613; protein.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0019740; P:nitrogen utilization; IMP:SGD.
DR   GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR   InterPro; IPR000791; Gpr1/Fun34/SatP.
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
 
 
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