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Ammonium transporter MEP2

 MEP2_YEAST              Reviewed;         499 AA.
P41948; D6W140;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
28-FEB-2018, entry version 138.
RecName: Full=Ammonium transporter MEP2;
Name=MEP2; Synonyms=AMT2; OrderedLocusNames=YNL142W;
ORFNames=N1207, N1820;
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], AND FUNCTION.
STRAIN=Sigma 1278B;
PubMed=9234685; DOI=10.1128/MCB.17.8.4282;
Marini A.-M., Soussi-Boudekou S., Vissers S., Andre B.;
"A family of ammonium transporters in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 17:4282-4293(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8619318; DOI=10.1002/yea.320111210;
Mallet L., Bussereau F., Jacquet M.;
"A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
deaminase gene and 14 new open reading frames.";
Yeast 11:1195-1209(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
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).
[5]
FUNCTION.
STRAIN=Sigma 1278B;
PubMed=9482721; DOI=10.1093/emboj/17.5.1236;
Lorenz M.C., Heitman J.;
"The MEP2 ammonium permease regulates pseudohyphal differentiation in
Saccharomyces cerevisiae.";
EMBO J. 17:1236-1247(1998).
[6]
FUNCTION, TOPOLOGY, MUTAGENESIS OF ASN-4; ASN-252; ASN-368 AND
ASN-483, AND GLYCOSYLATION AT ASN-4.
STRAIN=Sigma 1278B;
PubMed=11069679; DOI=10.1046/j.1365-2958.2000.02151.x;
Marini A.-M., Andre B.;
"In vivo N-glycosylation of the mep2 high-affinity ammonium
transporter of Saccharomyces cerevisiae reveals an extracytosolic N-
terminus.";
Mol. Microbiol. 38:552-564(2000).
[7]
FUNCTION.
PubMed=11486013; DOI=10.1128/MCB.21.17.5733-5741.2001;
Soupene E., Ramirez R.M., Kustu S.;
"Evidence that fungal MEP proteins mediate diffusion of the uncharged
species NH(3) across the cytoplasmic membrane.";
Mol. Cell. Biol. 21:5733-5741(2001).
[8]
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).
-!- FUNCTION: Transporter for ammonium (both charged and uncharged NH3
and NH4) to use as a nitrogen source. The affinity of MEP2 is
about twenty times higher than that of MEP1. MEP3 has the lowest
affinity. Under ammonium limitation acts as an ammonium sensor,
generating a signal that leads to pseudohyphal growth.
{ECO:0000269|PubMed:11069679, ECO:0000269|PubMed:11486013,
ECO:0000269|PubMed:9234685, ECO:0000269|PubMed:9482721}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- SIMILARITY: Belongs to the ammonia transporter channel (TC
1.A.11.2) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X83608; CAA58587.1; -; Genomic_DNA.
EMBL; Z46843; CAA86884.1; -; Genomic_DNA.
EMBL; Z71418; CAA96025.1; -; Genomic_DNA.
EMBL; BK006947; DAA10406.1; -; Genomic_DNA.
PIR; S51089; S51089.
RefSeq; NP_014257.1; NM_001182980.1.
PDB; 5AEX; X-ray; 3.20 A; A/B/C/D/E/F/H/I/J=1-499.
PDBsum; 5AEX; -.
ProteinModelPortal; P41948; -.
SMR; P41948; -.
BioGrid; 35685; 101.
DIP; DIP-4340N; -.
IntAct; P41948; 1.
STRING; 4932.YNL142W; -.
BindingDB; P41948; -.
ChEMBL; CHEMBL1741183; -.
TCDB; 1.A.11.3.2; the ammonium transporter channel (amt) family.
iPTMnet; P41948; -.
PaxDb; P41948; -.
PRIDE; P41948; -.
EnsemblFungi; YNL142W; YNL142W; YNL142W.
GeneID; 855580; -.
KEGG; sce:YNL142W; -.
EuPathDB; FungiDB:YNL142W; -.
SGD; S000005086; MEP2.
GeneTree; ENSGT00530000064546; -.
HOGENOM; HOG000017736; -.
InParanoid; P41948; -.
KO; K03320; -.
OMA; AHMVWFW; -.
OrthoDB; EOG092C1Z22; -.
BioCyc; YEAST:G3O-33160-MONOMER; -.
PRO; PR:P41948; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:SGD.
GO; GO:0015696; P:ammonium transport; IMP:SGD.
GO; GO:0019740; P:nitrogen utilization; IMP:SGD.
GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
Gene3D; 1.10.3430.10; -; 1.
InterPro; IPR029020; Ammonium/urea_transptr.
InterPro; IPR001905; Ammonium_transpt.
InterPro; IPR018047; Ammonium_transpt_CS.
InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
Pfam; PF00909; Ammonium_transp; 1.
TIGRFAMs; TIGR00836; amt; 1.
PROSITE; PS01219; AMMONIUM_TRANSP; 1.
1: Evidence at protein level;
3D-structure; Ammonia transport; Complete proteome; Glycoprotein;
Membrane; Reference proteome; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 499 Ammonium transporter MEP2.
/FTId=PRO_0000139755.
TOPO_DOM 1 31 Extracellular. {ECO:0000255}.
TRANSMEM 32 52 Helical. {ECO:0000255}.
TOPO_DOM 53 62 Cytoplasmic. {ECO:0000255}.
TRANSMEM 63 83 Helical. {ECO:0000255}.
TOPO_DOM 84 122 Extracellular. {ECO:0000255}.
TRANSMEM 123 143 Helical. {ECO:0000255}.
TOPO_DOM 144 152 Cytoplasmic. {ECO:0000255}.
TRANSMEM 153 173 Helical. {ECO:0000255}.
TOPO_DOM 174 187 Extracellular. {ECO:0000255}.
TRANSMEM 188 208 Helical. {ECO:0000255}.
TOPO_DOM 209 230 Cytoplasmic. {ECO:0000255}.
TRANSMEM 231 251 Helical. {ECO:0000255}.
TOPO_DOM 252 257 Extracellular. {ECO:0000255}.
TRANSMEM 258 278 Helical. {ECO:0000255}.
TOPO_DOM 279 300 Cytoplasmic. {ECO:0000255}.
TRANSMEM 301 321 Helical. {ECO:0000255}.
TOPO_DOM 322 346 Extracellular. {ECO:0000255}.
TRANSMEM 347 367 Helical. {ECO:0000255}.
TOPO_DOM 368 393 Cytoplasmic. {ECO:0000255}.
TRANSMEM 394 414 Helical. {ECO:0000255}.
TOPO_DOM 415 499 Extracellular. {ECO:0000255}.
CARBOHYD 4 4 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11069679}.
MUTAGEN 4 4 N->Q: Molecular weight equal to non-
glycosylated form.
{ECO:0000269|PubMed:11069679}.
MUTAGEN 252 252 N->Q: Molecular weight similar to wild-
type glycosylated form.
{ECO:0000269|PubMed:11069679}.
MUTAGEN 368 368 N->Q: Molecular weight similar to wild-
type glycosylated form.
{ECO:0000269|PubMed:11069679}.
MUTAGEN 483 483 N->Q: Molecular weight similar to wild-
type glycosylated form.
{ECO:0000269|PubMed:11069679}.
HELIX 23 26 {ECO:0000244|PDB:5AEX}.
HELIX 29 43 {ECO:0000244|PDB:5AEX}.
HELIX 45 55 {ECO:0000244|PDB:5AEX}.
HELIX 65 82 {ECO:0000244|PDB:5AEX}.
HELIX 84 89 {ECO:0000244|PDB:5AEX}.
STRAND 91 100 {ECO:0000244|PDB:5AEX}.
HELIX 105 107 {ECO:0000244|PDB:5AEX}.
STRAND 111 114 {ECO:0000244|PDB:5AEX}.
HELIX 122 142 {ECO:0000244|PDB:5AEX}.
HELIX 150 163 {ECO:0000244|PDB:5AEX}.
HELIX 165 172 {ECO:0000244|PDB:5AEX}.
TURN 178 183 {ECO:0000244|PDB:5AEX}.
TURN 190 193 {ECO:0000244|PDB:5AEX}.
HELIX 194 207 {ECO:0000244|PDB:5AEX}.
HELIX 214 216 {ECO:0000244|PDB:5AEX}.
HELIX 228 247 {ECO:0000244|PDB:5AEX}.
HELIX 248 250 {ECO:0000244|PDB:5AEX}.
STRAND 251 254 {ECO:0000244|PDB:5AEX}.
HELIX 255 282 {ECO:0000244|PDB:5AEX}.
HELIX 291 302 {ECO:0000244|PDB:5AEX}.
TURN 303 309 {ECO:0000244|PDB:5AEX}.
HELIX 314 330 {ECO:0000244|PDB:5AEX}.
HELIX 333 336 {ECO:0000244|PDB:5AEX}.
HELIX 342 362 {ECO:0000244|PDB:5AEX}.
HELIX 365 368 {ECO:0000244|PDB:5AEX}.
HELIX 369 374 {ECO:0000244|PDB:5AEX}.
HELIX 382 384 {ECO:0000244|PDB:5AEX}.
HELIX 389 415 {ECO:0000244|PDB:5AEX}.
TURN 419 421 {ECO:0000244|PDB:5AEX}.
TURN 427 429 {ECO:0000244|PDB:5AEX}.
HELIX 436 438 {ECO:0000244|PDB:5AEX}.
STRAND 441 444 {ECO:0000244|PDB:5AEX}.
SEQUENCE 499 AA; 53401 MW; 9E81D08018B68D94 CRC64;
MSYNFTGTPT GEGTGGNSLT TDLNTQFDLA NMGWIGVASA GVWIMVPGIG LLYSGLSRKK
HALSLLWASM MASAVCIFQW FFWGYSLAFS HNTRGNGFIG TLEFFGFRNV LGAPSSVSSL
PDILFAVYQG MFAAVTGALM LGGACERARL FPMMVFLFLW MTIVYCPIAC WVWNAEGWLV
KLGSLDYAGG LCVHLTSGHG GLVYALILGK RNDPVTRKGM PKYKPHSVTS VVLGTVFLWF
GWMFFNGGSA GNATIRAWYS IMSTNLAAAC GGLTWMVIDY FRCGRKWTTV GLCSGIIAGL
VGITPAAGFV PIWSAVVIGV VTGAGCNLAV DLKSLLRIDD GLDCYSIHGV GGCIGSVLTG
IFAADYVNAT AGSYISPIDG GWINHHYKQV GYQLAGICAA LAWTVTVTSI LLLTMNAIPF
LKLRLSADEE ELGTDAAQIG EFTYEESTAY IPEPIRSKTS AQMPPPHENI DDKIVGNTDA
EKNSTPSDAS STKNTDHIV


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