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Protein

Ammonium transporter MEP2

Gene

MEP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  • ammonium transmembrane transporter activity Source: SGD

GO - Biological processi

  • ammonium transport Source: SGD
  • nitrogen utilization Source: SGD
  • pseudohyphal growth Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ammonia transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33160-MONOMER.

Protein family/group databases

TCDBi1.A.11.3.2. the ammonia transporter channel (amt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Ammonium transporter MEP2
Gene namesi
Name:MEP2
Synonyms:AMT2
Ordered Locus Names:YNL142W
ORF Names:N1207, N1820
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL142W.
SGDiS000005086. MEP2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3131ExtracellularSequence analysisAdd
BLAST
Transmembranei32 – 5221HelicalSequence analysisAdd
BLAST
Topological domaini53 – 6210CytoplasmicSequence analysis
Transmembranei63 – 8321HelicalSequence analysisAdd
BLAST
Topological domaini84 – 12239ExtracellularSequence analysisAdd
BLAST
Transmembranei123 – 14321HelicalSequence analysisAdd
BLAST
Topological domaini144 – 1529CytoplasmicSequence analysis
Transmembranei153 – 17321HelicalSequence analysisAdd
BLAST
Topological domaini174 – 18714ExtracellularSequence analysisAdd
BLAST
Transmembranei188 – 20821HelicalSequence analysisAdd
BLAST
Topological domaini209 – 23022CytoplasmicSequence analysisAdd
BLAST
Transmembranei231 – 25121HelicalSequence analysisAdd
BLAST
Topological domaini252 – 2576ExtracellularSequence analysis
Transmembranei258 – 27821HelicalSequence analysisAdd
BLAST
Topological domaini279 – 30022CytoplasmicSequence analysisAdd
BLAST
Transmembranei301 – 32121HelicalSequence analysisAdd
BLAST
Topological domaini322 – 34625ExtracellularSequence analysisAdd
BLAST
Transmembranei347 – 36721HelicalSequence analysisAdd
BLAST
Topological domaini368 – 39326CytoplasmicSequence analysisAdd
BLAST
Transmembranei394 – 41421HelicalSequence analysisAdd
BLAST
Topological domaini415 – 49985ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 41N → Q: Molecular weight equal to non-glycosylated form. 1 Publication
Mutagenesisi252 – 2521N → Q: Molecular weight similar to wild-type glycosylated form. 1 Publication
Mutagenesisi368 – 3681N → Q: Molecular weight similar to wild-type glycosylated form. 1 Publication
Mutagenesisi483 – 4831N → Q: Molecular weight similar to wild-type glycosylated form. 1 Publication

Chemistry

ChEMBLiCHEMBL1741183.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Ammonium transporter MEP2PRO_0000139755Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi4 – 41N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

PTM databases

iPTMnetiP41948.

Interactioni

Protein-protein interaction databases

BioGridi35685. 45 interactions.
DIPiDIP-4340N.
IntActiP41948. 1 interaction.
MINTiMINT-568645.

Chemistry

BindingDBiP41948.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 264Combined sources
Helixi29 – 4315Combined sources
Helixi45 – 5511Combined sources
Helixi65 – 8218Combined sources
Helixi84 – 896Combined sources
Beta strandi91 – 10010Combined sources
Helixi105 – 1073Combined sources
Beta strandi111 – 1144Combined sources
Helixi122 – 14221Combined sources
Helixi150 – 16314Combined sources
Helixi165 – 1728Combined sources
Turni178 – 1836Combined sources
Turni190 – 1934Combined sources
Helixi194 – 20714Combined sources
Helixi214 – 2163Combined sources
Helixi228 – 24720Combined sources
Helixi248 – 2503Combined sources
Beta strandi251 – 2544Combined sources
Helixi255 – 28228Combined sources
Helixi291 – 30212Combined sources
Turni303 – 3097Combined sources
Helixi314 – 33017Combined sources
Helixi333 – 3364Combined sources
Helixi342 – 36221Combined sources
Helixi365 – 3684Combined sources
Helixi369 – 3746Combined sources
Helixi382 – 3843Combined sources
Helixi389 – 41527Combined sources
Turni419 – 4213Combined sources
Turni427 – 4293Combined sources
Helixi436 – 4383Combined sources
Beta strandi441 – 4444Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AEXX-ray3.20A/B/C/D/E/F/H/I/J1-499[»]
ProteinModelPortaliP41948.
SMRiP41948. Positions 30-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000064546.
HOGENOMiHOG000017736.
InParanoidiP41948.
KOiK03320.
OMAiFLWMTIV.
OrthoDBiEOG79SF67.

Family and domain databases

Gene3Di1.10.3430.10. 1 hit.
InterProiIPR029020. Ammonium/urea_transptr.
IPR001905. Ammonium_transpt.
IPR018047. Ammonium_transpt_CS.
IPR024041. NH4_transpt_AmtB-like_dom.
[Graphical view]
PANTHERiPTHR11730. PTHR11730. 1 hit.
PfamiPF00909. Ammonium_transp. 1 hit.
[Graphical view]
SUPFAMiSSF111352. SSF111352. 1 hit.
TIGRFAMsiTIGR00836. amt. 1 hit.
PROSITEiPS01219. AMMONIUM_TRANSP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41948-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYNFTGTPT GEGTGGNSLT TDLNTQFDLA NMGWIGVASA GVWIMVPGIG
60 70 80 90 100
LLYSGLSRKK HALSLLWASM MASAVCIFQW FFWGYSLAFS HNTRGNGFIG
110 120 130 140 150
TLEFFGFRNV LGAPSSVSSL PDILFAVYQG MFAAVTGALM LGGACERARL
160 170 180 190 200
FPMMVFLFLW MTIVYCPIAC WVWNAEGWLV KLGSLDYAGG LCVHLTSGHG
210 220 230 240 250
GLVYALILGK RNDPVTRKGM PKYKPHSVTS VVLGTVFLWF GWMFFNGGSA
260 270 280 290 300
GNATIRAWYS IMSTNLAAAC GGLTWMVIDY FRCGRKWTTV GLCSGIIAGL
310 320 330 340 350
VGITPAAGFV PIWSAVVIGV VTGAGCNLAV DLKSLLRIDD GLDCYSIHGV
360 370 380 390 400
GGCIGSVLTG IFAADYVNAT AGSYISPIDG GWINHHYKQV GYQLAGICAA
410 420 430 440 450
LAWTVTVTSI LLLTMNAIPF LKLRLSADEE ELGTDAAQIG EFTYEESTAY
460 470 480 490
IPEPIRSKTS AQMPPPHENI DDKIVGNTDA EKNSTPSDAS STKNTDHIV
Length:499
Mass (Da):53,401
Last modified:November 1, 1995 - v1
Checksum:i9E81D08018B68D94
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83608 Genomic DNA. Translation: CAA58587.1.
Z46843 Genomic DNA. Translation: CAA86884.1.
Z71418 Genomic DNA. Translation: CAA96025.1.
BK006947 Genomic DNA. Translation: DAA10406.1.
PIRiS51089.
RefSeqiNP_014257.1. NM_001182980.1.

Genome annotation databases

EnsemblFungiiYNL142W; YNL142W; YNL142W.
GeneIDi855580.
KEGGisce:YNL142W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83608 Genomic DNA. Translation: CAA58587.1.
Z46843 Genomic DNA. Translation: CAA86884.1.
Z71418 Genomic DNA. Translation: CAA96025.1.
BK006947 Genomic DNA. Translation: DAA10406.1.
PIRiS51089.
RefSeqiNP_014257.1. NM_001182980.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AEXX-ray3.20A/B/C/D/E/F/H/I/J1-499[»]
ProteinModelPortaliP41948.
SMRiP41948. Positions 30-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35685. 45 interactions.
DIPiDIP-4340N.
IntActiP41948. 1 interaction.
MINTiMINT-568645.

Chemistry

BindingDBiP41948.
ChEMBLiCHEMBL1741183.

Protein family/group databases

TCDBi1.A.11.3.2. the ammonia transporter channel (amt) family.

PTM databases

iPTMnetiP41948.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL142W; YNL142W; YNL142W.
GeneIDi855580.
KEGGisce:YNL142W.

Organism-specific databases

EuPathDBiFungiDB:YNL142W.
SGDiS000005086. MEP2.

Phylogenomic databases

GeneTreeiENSGT00530000064546.
HOGENOMiHOG000017736.
InParanoidiP41948.
KOiK03320.
OMAiFLWMTIV.
OrthoDBiEOG79SF67.

Enzyme and pathway databases

BioCyciYEAST:G3O-33160-MONOMER.

Miscellaneous databases

NextBioi979706.
PROiP41948.

Family and domain databases

Gene3Di1.10.3430.10. 1 hit.
InterProiIPR029020. Ammonium/urea_transptr.
IPR001905. Ammonium_transpt.
IPR018047. Ammonium_transpt_CS.
IPR024041. NH4_transpt_AmtB-like_dom.
[Graphical view]
PANTHERiPTHR11730. PTHR11730. 1 hit.
PfamiPF00909. Ammonium_transp. 1 hit.
[Graphical view]
SUPFAMiSSF111352. SSF111352. 1 hit.
TIGRFAMsiTIGR00836. amt. 1 hit.
PROSITEiPS01219. AMMONIUM_TRANSP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A family of ammonium transporters in Saccharomyces cerevisiae."
    Marini A.-M., Soussi-Boudekou S., Vissers S., Andre B.
    Mol. Cell. Biol. 17:4282-4293(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: Sigma 1278B.
  2. "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."
    Mallet L., Bussereau F., Jacquet M.
    Yeast 11:1195-1209(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    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.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "The MEP2 ammonium permease regulates pseudohyphal differentiation in Saccharomyces cerevisiae."
    Lorenz M.C., Heitman J.
    EMBO J. 17:1236-1247(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: Sigma 1278B.
  6. "In vivo N-glycosylation of the mep2 high-affinity ammonium transporter of Saccharomyces cerevisiae reveals an extracytosolic N-terminus."
    Marini A.-M., Andre B.
    Mol. Microbiol. 38:552-564(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TOPOLOGY, MUTAGENESIS OF ASN-4; ASN-252; ASN-368 AND ASN-483, GLYCOSYLATION AT ASN-4.
    Strain: Sigma 1278B.
  7. "Evidence that fungal MEP proteins mediate diffusion of the uncharged species NH(3) across the cytoplasmic membrane."
    Soupene E., Ramirez R.M., Kustu S.
    Mol. Cell. Biol. 21:5733-5741(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

Entry informationi

Entry nameiMEP2_YEAST
AccessioniPrimary (citable) accession number: P41948
Secondary accession number(s): D6W140
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.