ATO2_YEAST
ID ATO2_YEAST Reviewed; 282 AA.
AC P32907; D6W1H8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ammonia transport outward protein 2;
GN Name=ATO2; Synonyms=FUN34; OrderedLocusNames=YNR002C; ORFNames=N2029;
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].
RC STRAIN=S288c / GRF88;
RX PubMed=1400451; DOI=10.1016/s0021-9258(19)36622-0;
RA Stettler S., Mariotte S., Riva M., Sentenac A., Thuriaux P.;
RT "An essential and specific subunit of RNA polymerase III (C) is encoded by
RT gene RPC34 in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 267:21390-21395(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=7941739; DOI=10.1002/yea.320100412;
RA Lalo D., Stettler S., Mariotte S., Gendreau E., Thuriaux P.;
RT "Organization of the centromeric region of chromosome XIV in Saccharomyces
RT cerevisiae.";
RL Yeast 10:523-533(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7900425; DOI=10.1002/yea.320101013;
RA Verhasselt P., Aert R., Voet M., Volckaert G.;
RT "Twelve open reading frames revealed in the 23.6 kb segment flanking the
RT centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
RL Yeast 10:1355-1361(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [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 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 [8]
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 [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2; SER-7; SER-21; SER-22; SER-28 AND SER-40, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP 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. Involved in
CC acetate resistance. {ECO:0000269|PubMed:12429834,
CC ECO:0000269|PubMed:17233767}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17395151};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17395151}.
CC Note=Localizes to large detergent resistant patches of the cell
CC membrane (DRM) enriched in ergosterol and sphingolipids.
CC -!- INDUCTION: By external ammonia. {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; X63746; CAA45279.1; -; Genomic_DNA.
DR EMBL; X77395; CAA54571.1; -; Genomic_DNA.
DR EMBL; Z71617; CAA96278.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10544.1; -; Genomic_DNA.
DR PIR; S31258; S31258.
DR RefSeq; NP_014399.3; NM_001183179.3.
DR AlphaFoldDB; P32907; -.
DR SMR; P32907; -.
DR BioGRID; 35828; 43.
DR DIP; DIP-7904N; -.
DR STRING; 4932.YNR002C; -.
DR TCDB; 2.A.96.1.7; the acetate uptake transporter (acetr) family.
DR iPTMnet; P32907; -.
DR PaxDb; P32907; -.
DR PRIDE; P32907; -.
DR EnsemblFungi; YNR002C_mRNA; YNR002C; YNR002C.
DR GeneID; 855736; -.
DR KEGG; sce:YNR002C; -.
DR SGD; S000005285; ATO2.
DR VEuPathDB; FungiDB:YNR002C; -.
DR eggNOG; ENOG502QUJS; Eukaryota.
DR GeneTree; ENSGT00940000176398; -.
DR HOGENOM; CLU_051062_0_0_1; -.
DR InParanoid; P32907; -.
DR OMA; FHIADAY; -.
DR BioCyc; YEAST:G3O-33321-MON; -.
DR PRO; PR:P32907; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P32907; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
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:0015123; F:acetate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IMP:SGD.
DR GO; GO:0072488; P:ammonium transmembrane transport; IMP:SGD.
DR GO; GO:0019740; P:nitrogen utilization; 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 Acetylation; Ammonia transport; Cell membrane; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17761666"
FT CHAIN 2..282
FT /note="Ammonia transport outward protein 2"
FT /id="PRO_0000135701"
FT TOPO_DOM 2..86
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..34
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"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
SQ SEQUENCE 282 AA; 30701 MW; F5E20F9324CE8199 CRC64;
MSDREQSSGN TAFENPKALD SSEGEFISEN NDQSRHSQES ICKIYTAGKN NEYIYIGRQK
FLRDDLFEAF GGTLNPGLAP APVHKFANPA PLGLSGFALT TFVLSMFNAR AQGITIPNVV
VGCAMFYGGL VQLIAGIWEI ALENTFGGTA LCSFGGFWLS FGAIYIPWFG ILDAYKDKES
DLGNALGFYL LGWALFTFGL SVCTMKSTIM FFALFFLLAV TFLLLSIANF TGEVGVTRAG
GVLGVIVAFI AWYNAYAGIA TRQNSYIMVH PFALPSNDKV FF
