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Accumulation of dyads protein 2 (Ammonia transport outward protein 1)

 ADY2_YEAST              Reviewed;         283 AA.
P25613; D6VR19;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
23-MAY-2018, entry version 129.
RecName: Full=Accumulation of dyads protein 2;
AltName: Full=Ammonia transport outward protein 1;
Name=ADY2; Synonyms=ATO1; OrderedLocusNames=YCR010C; ORFNames=YCR10C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1626432; DOI=10.1002/yea.320080508;
Skala J., Purnelle B., Goffeau A.;
"The complete sequence of a 10.8 kb segment distal of SUF2 on the
right arm of chromosome III from Saccharomyces cerevisiae reveals
seven open reading frames including the RVS161, ADP1 and PGK genes.";
Yeast 8:409-417(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1574125; DOI=10.1038/357038a0;
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[5]
FUNCTION.
PubMed=11470404; DOI=10.1016/S0960-9822(01)00274-3;
Rabitsch K.P., Toth A., Galova M., Schleiffer A., Schaffner G.,
Aigner E., Rupp C., Penkner A.M., Moreno-Borchart A.C., Primig M.,
Esposito R.E., Klein F., Knop M., Nasmyth K.;
"A screen for genes required for meiosis and spore formation based on
whole-genome expression.";
Curr. Biol. 11:1001-1009(2001).
[6]
FUNCTION.
PubMed=12429834; DOI=10.1091/mbc.E01-12-0149;
Palkova Z., Devaux F., Icicova M., Minarikova L., Le Crom S., Jacq C.;
"Ammonia pulses and metabolic oscillations guide yeast colony
development.";
Mol. Biol. Cell 13:3901-3914(2002).
[7]
FUNCTION.
PubMed=14968426; DOI=10.1002/yea.1056;
Paiva S., Devaux F., Barbosa S., Jacq C., Casal M.;
"Ady2p is essential for the acetate permease activity in the yeast
Saccharomyces cerevisiae.";
Yeast 21:201-210(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=16286509; DOI=10.1083/jcb.200507168;
Taxis C., Keller P., Kavagiou Z., Jensen L.J., Colombelli J., Bork P.,
Stelzer E.H.K., Knop M.;
"Spore number control and breeding in Saccharomyces cerevisiae: a key
role for a self-organizing system.";
J. Cell Biol. 171:627-640(2005).
[9]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=17395151; DOI=10.1016/j.bbamem.2007.02.011;
Ricicova M., Kucerova H., Vachova L., Palkova Z.;
"Association of putative ammonium exporters Ato with detergent-
resistant compartments of plasma membrane during yeast colony
development: pH affects Ato1p localisation in patches.";
Biochim. Biophys. Acta 1768:1170-1178(2007).
[10]
FUNCTION.
PubMed=17233767; DOI=10.1111/j.1567-1364.2006.00191.x;
Gentsch M., Kuschel M., Schlegel S., Barth G.;
"Mutations at different sites in members of the Gpr1/Fun34/YaaH
protein family cause hypersensitivity to acetic acid in Saccharomyces
cerevisiae as well as in Yarrowia lipolytica.";
FEMS Yeast Res. 7:380-390(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=17761666; DOI=10.1074/mcp.M700098-MCP200;
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
"Profiling phosphoproteins of yeast mitochondria reveals a role of
phosphorylation in assembly of the ATP synthase.";
Mol. Cell. Proteomics 6:1896-1906(2007).
-!- FUNCTION: Transporter protein required for ammonia export and
acetate uptake and resistance. Necessary for up-regulation and
down-regulation of meiotic plaque (MP) component levels in a
dependency on external acetate. Has a role in ascus formation.
{ECO:0000269|PubMed:11470404, ECO:0000269|PubMed:12429834,
ECO:0000269|PubMed:14968426, ECO:0000269|PubMed:16286509,
ECO:0000269|PubMed:17233767}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16286509,
ECO:0000269|PubMed:17395151}; Multi-pass membrane protein
{ECO:0000269|PubMed:16286509, ECO:0000269|PubMed:17395151}.
Vacuole membrane {ECO:0000269|PubMed:16286509}; Multi-pass
membrane protein {ECO:0000269|PubMed:16286509}. Note=Localizes to
large detergent resistant patches of the cell membrane (DRM)
enriched in ergosterol and sphingolipids (PubMed:17395151).
-!- INDUCTION: During meiosis and by external ammonia.
{ECO:0000269|PubMed:16286509, ECO:0000269|PubMed:17395151}.
-!- SIMILARITY: Belongs to the acetate uptake transporter (AceTr) (TC
2.A.96) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X59720; CAA42327.1; -; Genomic_DNA.
EMBL; BK006937; DAA07488.1; -; Genomic_DNA.
PIR; S19420; S19420.
RefSeq; NP_009936.1; NM_001178723.1.
ProteinModelPortal; P25613; -.
BioGrid; 30989; 71.
DIP; DIP-7894N; -.
IntAct; P25613; 4.
MINT; P25613; -.
STRING; 4932.YCR010C; -.
TCDB; 2.A.96.1.4; the acetate uptake transporter (acetr) family.
CarbonylDB; P25613; -.
iPTMnet; P25613; -.
PaxDb; P25613; -.
PRIDE; P25613; -.
EnsemblFungi; CAA42327; CAA42327; CAA42327.
EnsemblFungi; YCR010C; YCR010C; YCR010C.
GeneID; 850368; -.
KEGG; sce:YCR010C; -.
EuPathDB; FungiDB:YCR010C; -.
SGD; S000000603; ADY2.
GeneTree; ENSGT00390000006887; -.
HOGENOM; HOG000224167; -.
InParanoid; P25613; -.
KO; K07034; -.
OMA; WKKGNTF; -.
OrthoDB; EOG092C3O7T; -.
BioCyc; YEAST:G3O-29327-MONOMER; -.
PRO; PR:P25613; -.
Proteomes; UP000002311; Chromosome III.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
GO; GO:0015123; F:acetate transmembrane transporter activity; IMP:SGD.
GO; GO:0008519; F:ammonium transmembrane transporter activity; IMP:SGD.
GO; GO:0006846; P:acetate transport; IMP:SGD.
GO; GO:0015696; P:ammonium transport; IMP:SGD.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0019740; P:nitrogen utilization; IMP:SGD.
GO; GO:0006847; P:plasma membrane acetate transport; IBA:GO_Central.
GO; GO:0055085; P:transmembrane transport; IMP:SGD.
InterPro; IPR000791; Grp1/Fun34/SatP.
Pfam; PF01184; Grp1_Fun34_YaaH; 1.
PROSITE; PS01114; GPR1_FUN34_YAAH; 1.
1: Evidence at protein level;
Ammonia transport; Cell membrane; Complete proteome; Ion transport;
Meiosis; Membrane; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Vacuole.
CHAIN 1 283 Accumulation of dyads protein 2.
/FTId=PRO_0000135706.
TOPO_DOM 1 89 Cytoplasmic. {ECO:0000255}.
TRANSMEM 90 110 Helical. {ECO:0000255}.
TOPO_DOM 111 120 Extracellular. {ECO:0000255}.
TRANSMEM 121 141 Helical. {ECO:0000255}.
TOPO_DOM 142 151 Cytoplasmic. {ECO:0000255}.
TRANSMEM 152 172 Helical. {ECO:0000255}.
TOPO_DOM 173 185 Extracellular. {ECO:0000255}.
TRANSMEM 186 206 Helical. {ECO:0000255}.
TOPO_DOM 207 208 Cytoplasmic. {ECO:0000255}.
TRANSMEM 209 229 Helical. {ECO:0000255}.
TOPO_DOM 230 240 Extracellular. {ECO:0000255}.
TRANSMEM 241 261 Helical. {ECO:0000255}.
TOPO_DOM 262 283 Cytoplasmic. {ECO:0000255}.
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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