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MEP3_YEAST
ID   MEP3_YEAST              Reviewed;         489 AA.
AC   P53390; D6W4D6; Q6B2F5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Ammonium transporter MEP3;
GN   Name=MEP3; Synonyms=AMT3; OrderedLocusNames=YPR138C; ORFNames=P9659.14;
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], AND 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
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   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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).
CC   -!- FUNCTION: Transporter for ammonium (both charged and uncharged NH3 and
CC       NH4) to use as a nitrogen source. The affinity of MEP2 is about twenty
CC       times higher than that of MEP1. MEP3 has the lowest affinity.
CC       {ECO:0000269|PubMed:11486013, ECO:0000269|PubMed:9234685}.
CC   -!- INTERACTION:
CC       P53390; P40260: MEP1; NbExp=3; IntAct=EBI-10729, EBI-10714;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- MISCELLANEOUS: Present with 3820 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC       family. {ECO:0000305}.
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DR   EMBL; U40829; AAB68278.1; -; Genomic_DNA.
DR   EMBL; AY692775; AAT92794.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11552.1; -; Genomic_DNA.
DR   PIR; S69027; S69027.
DR   RefSeq; NP_015464.1; NM_001184235.1.
DR   AlphaFoldDB; P53390; -.
DR   SMR; P53390; -.
DR   BioGRID; 36307; 47.
DR   DIP; DIP-4909N; -.
DR   IntAct; P53390; 22.
DR   MINT; P53390; -.
DR   STRING; 4932.YPR138C; -.
DR   PaxDb; P53390; -.
DR   PRIDE; P53390; -.
DR   EnsemblFungi; YPR138C_mRNA; YPR138C; YPR138C.
DR   GeneID; 856260; -.
DR   KEGG; sce:YPR138C; -.
DR   SGD; S000006342; MEP3.
DR   VEuPathDB; FungiDB:YPR138C; -.
DR   eggNOG; KOG0682; Eukaryota.
DR   GeneTree; ENSGT00530000064546; -.
DR   HOGENOM; CLU_000445_33_0_1; -.
DR   InParanoid; P53390; -.
DR   OMA; CWVGWGF; -.
DR   BioCyc; YEAST:G3O-34273-MON; -.
DR   PRO; PR:P53390; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P53390; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; -; 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   PANTHER; PTHR43029; PTHR43029; 1.
DR   Pfam; PF00909; Ammonium_transp; 1.
DR   TIGRFAMs; TIGR00836; amt; 1.
DR   PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE   1: Evidence at protein level;
KW   Ammonia transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..489
FT                   /note="Ammonium transporter MEP3"
FT                   /id="PRO_0000139756"
FT   TOPO_DOM        1..17
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..108
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..267
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        311..330
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        352..372
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        394..489
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          448..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        7
FT                   /note="H -> P (in Ref. 4; AAT92794)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   489 AA;  53690 MW;  2309338F36D96258 CRC64;
     MARGDGHLWT ETYDSSTVAF MILGAALVFF MVPGLGFLYS GLARRKSALA LIWVVIMATL
     VGILQWYFWG YSLAFSKTAT NNKFIGNLDS FGFRNVYGKI SDDSTYPELI YAIFQMMFMC
     VALSIIAGAT AERGKLFPHM VFLFVFATLV YCPITYWIWA PGGWAYQWGV LDWAGGGNIE
     ILSAVAGFVY SYFLGRRKEN LLINFRPHNV SMVTLGTSIL WFGWLLFNAA SSLSPNMRSV
     YAFMNTCLSA TTGGMTWCLL DYRSEKKWST VGLCSGIICG LVAATPSSGC ITLYGSLIQG
     IIAGVVCNFA TKIKYYLKVD DSLDLLAEHG IAGVVGLIFN ALFAADWVIG MDGTTKHKGG
     WLTHNWKQMY IQIAYIGASA GYCAVVTAII CFVLGKIPGV HLRVTEEAEA LGLDEDQIGE
     FAYDYVEVRR DYYQWGVDTD ALHTTCNGAN SASETNPTED SQNSSLSSAT VSGQNEKSNN
     PKLHHAKEA
 
 
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