ID   MEP1_YEAST              Reviewed;         492 AA.
AC   P40260; D6VUQ2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Ammonium transporter MEP1;
GN   Name=MEP1; Synonyms=AMT1; OrderedLocusNames=YGR121C; ORFNames=G6331;
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=Sigma 1278B;
RX   PubMed=8062822; DOI=10.1002/j.1460-2075.1994.tb06651.x;
RA   Marini A.-M., Vissers S., Urrestarazu A., Andre B.;
RT   "Cloning and expression of the MEP1 gene encoding an ammonium transporter
RT   in Saccharomyces cerevisiae.";
RL   EMBO J. 13:3456-3463(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9046098;
RX   DOI=10.1002/(sici)1097-0061(199702)13:2<171::aid-yea57>3.0.co;2-v;
RA   van Dyck L., Tettelin H., Purnelle B., Goffeau A.;
RT   "An 18.3 kb DNA fragment from yeast chromosome VII carries four unknown
RT   open reading frames, the gene for an Asn synthase, remnants of Ty and three
RT   tRNA genes.";
RL   Yeast 13:171-176(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [5]
RP   FUNCTION.
RC   STRAIN=Sigma 1278B;
RX   PubMed=9234685; DOI=10.1128/mcb.17.8.4282;
RA   Marini A.-M., Soussi-Boudekou S., Vissers S., Andre B.;
RT   "A family of ammonium transporters in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 17:4282-4293(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=11486013; DOI=10.1128/mcb.21.17.5733-5741.2001;
RA   Soupene E., Ramirez R.M., Kustu S.;
RT   "Evidence that fungal MEP proteins mediate diffusion of the uncharged
RT   species NH(3) across the cytoplasmic membrane.";
RL   Mol. Cell. Biol. 21:5733-5741(2001).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442 AND SER-445, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Transporter for ammonium (both charged and uncharged NH3 and
CC       NH4) to use as a nitrogen source. Can also transport methylamine. The
CC       affinity of MEP1 is about twenty times lower than that of MEP2. MEP3
CC       has the lowest affinity. {ECO:0000269|PubMed:11486013,
CC       ECO:0000269|PubMed:9234685}.
CC   -!- INTERACTION:
CC       P40260; P53390: MEP3; NbExp=3; IntAct=EBI-10714, EBI-10729;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC       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; X77608; CAA54699.1; -; Genomic_DNA.
DR   EMBL; X83099; CAA58156.1; -; Genomic_DNA.
DR   EMBL; Z72906; CAA97132.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08213.1; -; Genomic_DNA.
DR   PIR; S46225; S46225.
DR   RefSeq; NP_011636.3; NM_001181250.3.
DR   AlphaFoldDB; P40260; -.
DR   SMR; P40260; -.
DR   BioGRID; 33367; 132.
DR   DIP; DIP-5530N; -.
DR   IntAct; P40260; 14.
DR   MINT; P40260; -.
DR   STRING; 4932.YGR121C; -.
DR   TCDB; 1.A.11.3.1; the ammonium transporter channel (amt) family.
DR   iPTMnet; P40260; -.
DR   PaxDb; 4932-YGR121C; -.
DR   PeptideAtlas; P40260; -.
DR   EnsemblFungi; YGR121C_mRNA; YGR121C; YGR121C.
DR   GeneID; 853019; -.
DR   KEGG; sce:YGR121C; -.
DR   AGR; SGD:S000003353; -.
DR   SGD; S000003353; MEP1.
DR   VEuPathDB; FungiDB:YGR121C; -.
DR   eggNOG; KOG0682; Eukaryota.
DR   GeneTree; ENSGT00530000064546; -.
DR   HOGENOM; CLU_000445_33_0_1; -.
DR   InParanoid; P40260; -.
DR   OMA; ERIKFHS; -.
DR   OrthoDB; 1109542at2759; -.
DR   BioCyc; YEAST:G3O-30828-MONOMER; -.
DR   BioGRID-ORCS; 853019; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40260; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P40260; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
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; IMP:SGD.
DR   GO; GO:0019740; P:nitrogen utilization; IMP:SGD.
DR   Gene3D; 1.10.3430.10; Ammonium transporter AmtB like domains; 1.
DR   InterPro; IPR029020; Ammonium/urea_transptr.
DR   InterPro; IPR001905; Ammonium_transpt.
DR   InterPro; IPR018047; Ammonium_transpt_CS.
DR   InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR   NCBIfam; TIGR00836; amt; 1.
DR   PANTHER; PTHR43029:SF4; AMMONIUM TRANSPORTER MEP1-RELATED; 1.
DR   PANTHER; PTHR43029; AMMONIUM TRANSPORTER MEP2; 1.
DR   Pfam; PF00909; Ammonium_transp; 1.
DR   SUPFAM; SSF111352; Ammonium transporter; 1.
DR   PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE   1: Evidence at protein level;
KW   Ammonia transport; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..492
FT                   /note="Ammonium transporter MEP1"
FT                   /id="PRO_0000139754"
FT   TOPO_DOM        1..18
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..109
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..174
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        312..331
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        353..373
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..492
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          455..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         442
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   492 AA;  54202 MW;  CC7DF0EB838D0B77 CRC64;
     MESRTTGPLT TETYDGPTVA FMILGAALVF FMVPGLGFLY SGLARRKSAL ALIWVVLMAT
     LVGILQWYFW GYSLAFSKSA PNNKFIGNLD SFGFRNVYGK KFDEDAYPEL AYATFQMMFS
     CVNLSIIAGA TAERGRLLPH MVFLFILATI GYCPVTYWIW SPGGWAYQWG VLDWAGGGNI
     EILSAVSGFV YSWFLGKRNE KLLINFRPHN VSLVTLGTSI LWFGWLLFNS ASSLSPNLRS
     VYAFMNTCLS AITGGMTWCL LDYRSEKKWS TVGLCSGIIS GLVAATPSSG CITLYGSLIQ
     GIVAGVVCNF ATKLKYYAKV DDAMDILAEH GVAGVIGLIF NALFGADWVI GMDGTTEHEG
     GWVTHNYKQM YKQIAYIAAS IGYTAAVTAI ICFVLGYIPG MRLRISEEAE EAGMDEDQIG
     EFAYDYVEVR RDYYLWGVDE DSQRSDVNHR VNNAHLAAER SSSGTNSSSD GNGEMIQSEK
     ILPIHQEDPA NR
//