AMF1_YEAST
ID AMF1_YEAST Reviewed; 515 AA.
AC Q08902; D6W371;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Low affinity ammonium transporter {ECO:0000303|PubMed:24707045};
DE AltName: Full=Ammonium facilitator 1 {ECO:0000303|PubMed:24707045};
GN Name=AMF1 {ECO:0000303|PubMed:24707045}; OrderedLocusNames=YOR378W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
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 [3]
RP INDUCTION BY NEOCARZINOSTATIN.
RX PubMed=11562456; DOI=10.1073/pnas.191340698;
RA Schaus S.E., Cavalieri D., Myers A.G.;
RT "Gene transcription analysis of Saccharomyces cerevisiae exposed to
RT neocarzinostatin protein-chromophore complex reveals evidence of DNA
RT damage, a potential mechanism of resistance, and consequences of prolonged
RT exposure.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11075-11080(2001).
RN [4]
RP INDUCTION.
RX PubMed=16278933; DOI=10.1002/yea.1302;
RA de Lichtenberg U., Wernersson R., Jensen T.S., Nielsen H.B., Fausboell A.,
RA Schmidt P., Hansen F.B., Knudsen S., Brunak S.;
RT "New weakly expressed cell cycle-regulated genes in yeast.";
RL Yeast 22:1191-1201(2005).
RN [5]
RP IDENTIFICATION.
RX PubMed=16630275; DOI=10.1111/j.1567-1364.2006.00058.x;
RA Gbelska Y., Krijger J.J., Breunig K.D.;
RT "Evolution of gene families: the multidrug resistance transporter genes in
RT five related yeast species.";
RL FEMS Yeast Res. 6:345-355(2006).
RN [6]
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 [7]
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=19414602; DOI=10.1128/mcb.01646-08;
RA Kaya A., Karakaya H.C., Fomenko D.E., Gladyshev V.N., Koc A.;
RT "Identification of a novel system for boron transport: Atr1 is a main boron
RT exporter in yeast.";
RL Mol. Cell. Biol. 29:3665-3674(2009).
RN [8]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION.
RX PubMed=24707045; DOI=10.1073/pnas.1312801111;
RA Chiasson D.M., Loughlin P.C., Mazurkiewicz D., Mohammadidehcheshmeh M.,
RA Fedorova E.E., Okamoto M., McLean E., Glass A.D., Smith S.E., Bisseling T.,
RA Tyerman S.D., Day D.A., Kaiser B.N.;
RT "Soybean SAT1 (Symbiotic Ammonium Transporter 1) encodes a bHLH
RT transcription factor involved in nodule growth and NH4+ transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4814-4819(2014).
CC -!- FUNCTION: Low affinity ammonium transporter of the plasma membrane
CC (PubMed:24707045). May be involved in drug resistance through pumping
CC them out of the cell (By similarity). {ECO:0000250|UniProtKB:P13090,
CC ECO:0000269|PubMed:24707045}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24707045};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced by neocarzinostatin (PubMed:11562456).
CC Expression is induced during G2 phase of cell cycle (PubMed:16278933).
CC Expression is slightly up-regulated upon exposure to boric acid
CC (PubMed:19414602). The AMF1 promoter contains 8 predicted enhancer box
CC (E-box) transcription factor binding domains (PubMed:24707045).
CC {ECO:0000269|PubMed:11562456, ECO:0000269|PubMed:16278933,
CC ECO:0000269|PubMed:19414602, ECO:0000269|PubMed:24707045}.
CC -!- DISRUPTION PHENOTYPE: Does not affect boron tolerance
CC (PubMed:19414602). Impairs methylammonium (MA) transport and toxicity
CC (PubMed:24707045). {ECO:0000269|PubMed:19414602,
CC ECO:0000269|PubMed:24707045}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; Z75286; CAA99709.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11137.1; -; Genomic_DNA.
DR PIR; S67290; S67290.
DR RefSeq; NP_015023.1; NM_001183798.1.
DR AlphaFoldDB; Q08902; -.
DR SMR; Q08902; -.
DR BioGRID; 34760; 24.
DR DIP; DIP-4051N; -.
DR IntAct; Q08902; 1.
DR STRING; 4932.YOR378W; -.
DR TCDB; 2.A.1.3.52; the major facilitator superfamily (mfs).
DR PaxDb; Q08902; -.
DR PRIDE; Q08902; -.
DR EnsemblFungi; YOR378W_mRNA; YOR378W; YOR378W.
DR GeneID; 854560; -.
DR KEGG; sce:YOR378W; -.
DR SGD; S000005905; AMF1.
DR VEuPathDB; FungiDB:YOR378W; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_27_4_1; -.
DR InParanoid; Q08902; -.
DR OMA; CAGQFLV; -.
DR BioCyc; YEAST:G3O-33842-MON; -.
DR PRO; PR:Q08902; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08902; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:SGD.
DR GO; GO:0072488; P:ammonium transmembrane transport; IGI:SGD.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Ammonia transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..515
FT /note="Low affinity ammonium transporter"
FT /id="PRO_0000244476"
FT TOPO_DOM 1..78
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..346
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..403
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..479
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 515 AA; 56110 MW; 2A74E99CDCC433C2 CRC64;
MSTSSSVTQK NLDTNAEALK KEDKVLSEFD IQDERPKSLL WESAFVGVLC SAQLMTQAGL
GQSLAPLHII GNSFGTTNAG QLSWFASAYS LTVGTFILIA GRLGDIFGHK KFFVLGFFWY
ALWSLLAGFS VYSNQIFFDC CRAFQGMGPA FLLPNAIAIL GRTYKPGRRK NMVFSLFGAS
APGGFFLGAV FSSMLGQLAW WPWAYWIMGI ACFVLAVAGY FVIPHTPMPS RDASSFKLLE
RIDFAGSVTG VVGLILFNFA WNQGPVVGWQ TPYTYALLIV GTFFLVIFAY IESRAAFPLL
PFAALSSDTA FVLSCIAAGW ASFGIWIFYT WQFMEDSRGQ TPLLSSAQFS PVAISGFCAA
VTTGFLLSHT PPSTVMLFAM TAFTVGTILI ATAPVHQTYW AQTFVSIIVM PWGMDMSFPA
ATIMLSDSMP HEHQGLAASL VNTVVNYSIS IGLGIAGTIE SRVNDGGAKP LKGYRCSWYM
GIGLSGLGIF VAATYAWSTF MKSKKRISEK QHFIE
